|
Name |
Accession |
Description |
Interval |
E-value |
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
55-530 |
0e+00 |
|
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: 525.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 55 AQISITEDIVLTREDLHMNAMRVASYMRNMGLGQTDIVGVMGRHTTHQSAVAYACFFNGTPLHALHNAYEEACIAKLFGI 134
Cdd:cd05911 1 AQIDADTGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 135 TKPRLIFCDGDEYEKVKSATKDL--QVTIVTMRNHPRGSVRIQDVLTTPVMQN--FQPLRLKDGIDHTLAILSSSGTSGF 210
Cdd:cd05911 81 SKPKVIFTDPDGLEKVKEAAKELgpKDKIIVLDDKPDGVLSIEDLLSPTLGEEdeDLPPPLKDGKDDTAAILYSSGTTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 211 PKAVTISNSHKIIVDYMAIN-------NSNIQYTSSTLDWCSGLSMAITSGVFSTTSIIADCdFDPGLFCRAIGKYRISM 283
Cdd:cd05911 161 PKGVCLSHRNLIANLSQVQTflygndgSNDVILGFLPLYHIYGLFTTLASLLNGATVIIMPK-FDSELFLDLIEKYKITF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 284 VLLSSSYLAIFANCPEFESADLSSLNYVIFGGSSCSLEVQRKVRSRLSHDCLNFCYGLTELNSAGSVNLNFDEKPNSVGR 363
Cdd:cd05911 240 LYLVPPIAAALAKSPLLDKYDLSSLRVILSGGAPLSKELQELLAKRFPNATIKQGYGMTETGGILTVNPDGDDKPGSVGR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 364 AIRGIKIKVIDEQG-EAQEPNVVGEICFHNSQKWAGYYKNPDETRQIQDSENWIHTGDLGYVDKDGYLFVIDRLKDMLKY 442
Cdd:cd05911 320 LLPNVEAKIVDDDGkDSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGWLHTGDIGYFDEDGYLYIVDRKKELIKY 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 443 QNIMYYPSEIENVIAEMPNVLEACVFGIWDPVNGDEAAASLVKKPGTQLEAQDVVEYVRKRItAKFKQLNGGALIVDQIV 522
Cdd:cd05911 400 KGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGEKLTEKEVKDYVAKKV-ASYKQLRGGVVFVDEIP 478
|
....*...
gi 281365686 523 RSGNRKTN 530
Cdd:cd05911 479 KSASGKIL 486
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
59-540 |
3.31e-86 |
|
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: 273.99 E-value: 3.31e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 59 ITEDIVLTREDLHMNAMRVASYMRNMGLGQTDIVGVMGRHTTHQSAVAYACFFNGTPLHALHNAYEEACIAKLFGITKPR 138
Cdd:COG0318 19 VFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAEELAYILEDSGAR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 139 LIFcdgdeyekvksatkdlqvtivtmrnhprgsvriqdvlttpvmqnfqplrlkdgidhTLAILSSSGTSGFPKAVTIS- 217
Cdd:COG0318 99 ALV--------------------------------------------------------TALILYTSGTTGRPKGVMLTh 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 218 ----NSHKIIVDYMAINNSNIQYTSSTLDWCSGLSMAITSGVFS-TTSIIADcDFDPGLFCRAIGKYRISMVLLSSSYLA 292
Cdd:COG0318 123 rnllANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAgATLVLLP-RFDPERVLELIERERVTVLFGVPTMLA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 293 IFANCPEFESADLSSLNYVIFGGSSCSLEVQRKVRSRLSHDCLNfCYGLTELNSAGSVNL--NFDEKPNSVGRAIRGIKI 370
Cdd:COG0318 202 RLLRHPEFARYDLSSLRLVVSGGAPLPPELLERFEERFGVRIVE-GYGLTETSPVVTVNPedPGERRPGSVGRPLPGVEV 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 371 KVIDEQGEAQEPNVVGEICFHNSQKWAGYYKNPDETRQ-IQDseNWIHTGDLGYVDKDGYLFVIDRLKDMLKY--QNImy 447
Cdd:COG0318 281 RIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEaFRD--GWLRTGDLGRLDEDGYLYIVGRKKDMIISggENV-- 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 448 YPSEIENVIAEMPNVLEACVFGIWDPVNGDEAAASLVKKPGTQLEAQDVVEYVRKRItAKFK---QLnggaLIVDQIVRS 524
Cdd:COG0318 357 YPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPGAELDAEELRAFLRERL-ARYKvprRV----EFVDELPRT 431
|
490
....*....|....*.
gi 281365686 525 GNRKTNRSAVKEHFLK 540
Cdd:COG0318 432 ASGKIDRRALRERYAA 447
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
197-509 |
9.34e-76 |
|
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: 242.96 E-value: 9.34e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 197 HTLAILSSSGTSGFPKAVTISN-----SHKIIVDYMAINNSNIQYTSSTLDWCSGLS---MAITSGvfsTTSIIADcDFD 268
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHrnllaAAAALAASGGLTEGDVFLSTLPLFHIGGLFgllGALLAG---GTVVLLP-KFD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 269 PGLFCRAIGKYRISMVLLSSSYLAIFANCPEFESADLSSLNYVIFGGSSCSLEVQRKVRSRLSHDCLNfCYGLTELNSAG 348
Cdd:cd04433 77 PEAALELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGAPLPPELLERFEEAPGIKLVN-GYGLTETGGTV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 349 SVNL--NFDEKPNSVGRAIRGIKIKVIDEQGEAQEPNVVGEICFHNSQKWAGYYKNPDETRQIqDSENWIHTGDLGYVDK 426
Cdd:cd04433 156 ATGPpdDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAV-DEDGWYRTGDLGRLDE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 427 DGYLFVIDRLKDMLKYQNIMYYPSEIENVIAEMPNVLEACVFGIWDPVNGDEAAASLVKKPGTQLEAQDVVEYVRKRItA 506
Cdd:cd04433 235 DGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLDAEELRAHVRERL-A 313
|
...
gi 281365686 507 KFK 509
Cdd:cd04433 314 PYK 316
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
66-536 |
4.90e-72 |
|
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: 239.35 E-value: 4.90e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 66 TREDLHMNAMRVASYMRNMGLGQTDIVGVMGRHTTHQSAVAYACFFNGTPLHALHNAYEEACIAKLFGITKPRLIFCDGD 145
Cdd:cd17642 46 SYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFCSKK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 146 EYEKVKSATKDLQV--TIVTM--RNHPRGSVRIQDVLTTPVMQNFQPLRLK----DGIDHTLAILSSSGTSGFPKAVTIS 217
Cdd:cd17642 126 GLQKVLNVQKKLKIikTIIILdsKEDYKGYQCLYTFITQNLPPGFNEYDFKppsfDRDEQVALIMNSSGSTGLPKGVQLT 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 218 nsHKIIV-------DYMAINNSNIQYTSST-LDWCSGLSMAITSGVFST-TSIIADCDFDPGLFCRAIGKYRISMVLLSS 288
Cdd:cd17642 206 --HKNIVarfsharDPIFGNQIIPDTAILTvIPFHHGFGMFTTLGYLICgFRVVLMYKFEEELFLRSLQDYKVQSALLVP 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 289 SYLAIFANCPEFESADLSSLNYVIFGGSSCSLEVQRKVRSRLSHDCLNFCYGLTELNSAGSVNLNFDEKPNSVGRAIRGI 368
Cdd:cd17642 284 TLFAFFAKSTLVDKYDLSNLHEIASGGAPLSKEVGEAVAKRFKLPGIRQGYGLTETTSAILITPEGDDKPGAVGKVVPFF 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 369 KIKVID-EQGEAQEPNVVGEICFHNSQKWAGYYKNPDETRQIQDSENWIHTGDLGYVDKDGYLFVIDRLKDMLKYQNIMY 447
Cdd:cd17642 364 YAKVVDlDTGKTLGPNERGELCVKGPMIMKGYVNNPEATKALIDKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQV 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 448 YPSEIENVIAEMPNVLEACVFGIWDPVNGDEAAASLVKKPGTQLEAQDVVEYVRKRITAKfKQLNGGALIVDQIVRSGNR 527
Cdd:cd17642 444 PPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVVLEAGKTMTEKEVMDYVASQVSTA-KRLRGGVKFVDEVPKGLTG 522
|
....*....
gi 281365686 528 KTNRSAVKE 536
Cdd:cd17642 523 KIDRRKIRE 531
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
65-511 |
1.83e-67 |
|
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: 226.35 E-value: 1.83e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 65 LTREDLHMNAMRVASYMRNMGLGQTDIVGVMGrhtthQSAVAYACFFNG--------TPLHALHNAYEeacIAKLFGITK 136
Cdd:cd05904 33 LTYAELERRVRRLAAGLAKRGGRKGDVVLLLS-----PNSIEFPVAFLAvlslgavvTTANPLSTPAE---IAKQVKDSG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 137 PRLIFCDGDEYEKVKSatkdLQVTIVTMRNHPRGSVRIQDVLTTpvmQNF-QPLRLKDGIDHTLAILSSSGTSGFPKAVT 215
Cdd:cd05904 105 AKLAFTTAELAEKLAS----LALPVVLLDSAEFDSLSFSDLLFE---ADEaEPPVVVIKQDDVAALLYSSGTTGRSKGVM 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 216 ISnsHKIIVD----YMAINNSNIQYTSSTLdwCS-------GLSMAITSGVFSTTSIIADCDFDPGLFCRAIGKYRISMV 284
Cdd:cd05904 178 LT--HRNLIAmvaqFVAGEGSNSDSEDVFL--CVlpmfhiyGLSSFALGLLRLGATVVVMPRFDLEELLAAIERYKVTHL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 285 LLSSSYLAIFANCPEFESADLSSLNYVIFGGSSCSLEVQRKVRSRLSHDCLNFCYGLTELNSAGSVNLNFDE---KPNSV 361
Cdd:cd05904 254 PVVPPIVLALVKSPIVDKYDLSSLRQIMSGAAPLGKELIEAFRAKFPNVDLGQGYGMTESTGVVAMCFAPEKdraKYGSV 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 362 GRAIRGIKIKVID-EQGEAQEPNVVGEICFHNSQKWAGYYKNPDETRQIQDSENWIHTGDLGYVDKDGYLFVIDRLKDML 440
Cdd:cd05904 334 GRLVPNVEAKIVDpETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDKEGWLHTGDLCYIDEDGYLFIVDRLKELI 413
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 281365686 441 KYQNIMYYPSEIENVIAEMPNVLEACVFGIWDPVNGDEAAASLVKKPGTQLEAQDVVEYVRKRItAKFKQL 511
Cdd:cd05904 414 KYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKPGSSLTEDEIMDFVAKQV-APYKKV 483
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
195-528 |
1.21e-61 |
|
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: 209.00 E-value: 1.21e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 195 IDHTLAILSSSGTSGFPKAVTIS------NSHKIIVDYmAINNSNIQYTSSTLDWCSGLSMAITSGVFSTTSIIADCDFD 268
Cdd:cd17631 97 FDDLALLMYTSGTTGRPKGAMLThrnllwNAVNALAAL-DLGPDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVILRKFD 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 269 PGLFCRAIGKYRISMVLLSSSYLAIFANCPEFESADLSSLNYVIFGGSSCSLEVQRKVRSRlshdclNF----CYGLTEL 344
Cdd:cd17631 176 PETVLDLIERHRVTSFFLVPTMIQALLQHPRFATTDLSSLRAVIYGGAPMPERLLRALQAR------GVkfvqGYGMTET 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 345 NSAGSVNLNFD--EKPNSVGRAIRGIKIKVIDEQGEAQEPNVVGEICFHNSQKWAGYYKNPDETRQ-IQDseNWIHTGDL 421
Cdd:cd17631 250 SPGVTFLSPEDhrRKLGSAGRPVFFVEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAaFRD--GWFHTGDL 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 422 GYVDKDGYLFVIDRLKDMLKY--QNImyYPSEIENVIAEMPNVLEACVFGIWDPVNGDEAAASLVKKPGTQLEAQDVVEY 499
Cdd:cd17631 328 GRLDEDGYLYIVDRKKDMIISggENV--YPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPGAELDEDELIAH 405
|
330 340 350
....*....|....*....|....*....|..
gi 281365686 500 VRKRItAKFK---QLnggaLIVDQIVRSGNRK 528
Cdd:cd17631 406 CRERL-ARYKipkSV----EFVDALPRNATGK 432
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
57-443 |
2.25e-61 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 207.94 E-value: 2.25e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 57 ISITEDIVLTREDLHMNAMRVASYMRNMGLGQTDIVGVMGRHTTHQSAVAYACFFNGTPLHALHNAYEEACIAKLFGITK 136
Cdd:pfam00501 14 LEVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDSG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 137 PRLIFCDGD-EYEKVKSATKDLQVTIVTMRNHPRGSVRIQDVLTTPVMQNFQPLRLKD-GIDHTLAILSSSGTSGFPKAV 214
Cdd:pfam00501 94 AKVLITDDAlKLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVPPPPPPPpDPDDLAYIIYTSGTTGKPKGV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 215 TIS---------NSHKIIVDYMAINNSNIQYTSSTLDWCSGLSMAITSGVFS-TTSIIAD--CDFDPGLFCRAIGKYRIS 282
Cdd:pfam00501 174 MLThrnlvanvlSIKRVRPRGFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAgATVVLPPgfPALDPAALLELIERYKVT 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 283 MVLLSSSYLAIFANCPEFESADLSSLNYVIFGGSSCSLEVQRKVRSRLSHDCLNfCYGLTELNSAGSVNLNFDEK---PN 359
Cdd:pfam00501 254 VLYGVPTLLNMLLEAGAPKRALLSSLRLVLSGGAPLPPELARRFRELFGGALVN-GYGLTETTGVVTTPLPLDEDlrsLG 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 360 SVGRAIRGIKIKVIDEQ-GEAQEPNVVGEICFHNSQKWAGYYKNPDETRQIQDSENWIHTGDLGYVDKDGYLFVIDRLKD 438
Cdd:pfam00501 333 SVGRPLPGTEVKIVDDEtGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDEDGWYRTGDLGRRDEDGYLEIVGRKKD 412
|
....*
gi 281365686 439 MLKYQ 443
Cdd:pfam00501 413 QIKLG 417
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
65-509 |
2.32e-54 |
|
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341259 [Multi-domain] Cd Length: 468 Bit Score: 190.47 E-value: 2.32e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 65 LTREDLHMNAMRVASYMRNMGLGQTDIVGVMGRHTTHQSAVAYACFFNG---TPLHALHNAYEeacIAKLFGITKPRLIF 141
Cdd:cd05936 25 LTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGavvVPLNPLYTPRE---LEHILNDSGAKALI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 142 CDGDEYEKVKSATKDLQVTIVTmrnhprgsvriqdvlttpvmqnfqplrlkdgIDHTLAILSSSGTSGFPKAVTISnsHK 221
Cdd:cd05936 102 VAVSFTDLLAAGAPLGERVALT-------------------------------PEDVAVLQYTSGTTGVPKGAMLT--HR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 222 IIVdymainnSNIQytsSTLDWCS-------------------GLSMAITSGVFSTTSIIADCDFDPGLFCRAIGKYRIS 282
Cdd:cd05936 149 NLV-------ANAL---QIKAWLEdllegddvvlaalplfhvfGLTVALLLPLALGATIVLIPRFRPIGVLKEIRKHRVT 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 283 -MVLLSSSYLAIFANcPEFESADLSSLNYVIFGGSSCSLEVQRKVRSRLSHDCLNfCYGLTELNSAGSVN-LNFDEKPNS 360
Cdd:cd05936 219 iFPGVPTMYIALLNA-PEFKKRDFSSLRLCISGGAPLPVEVAERFEELTGVPIVE-GYGLTETSPVVAVNpLDGPRKPGS 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 361 VGRAIRGIKIKVIDEQGEAQEPNVVGEICFHNSQKWAGYYKNPDETRQ-IQDSenWIHTGDLGYVDKDGYLFVIDRLKDM 439
Cdd:cd05936 297 IGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEaFVDG--WLRTGDIGYMDEDGYFFIVDRKKDM 374
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281365686 440 L--KYQNImyYPSEIENVIAEMPNVLEACVFGIWDPVNGDEAAASLVKKPGTQLEAQDVVEYVRKRItAKFK 509
Cdd:cd05936 375 IivGGFNV--YPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEGASLTEEEIIAFCREQL-AGYK 443
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
37-509 |
3.48e-53 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 188.47 E-value: 3.48e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 37 LSIGEIIFGDMVNNPKliAQISITEDIVLTREDLHMNAMRVASYMRNMGLGQTDIVGVMGRHTTHqsavAYACFFnGTP- 115
Cdd:PRK06187 6 LTIGRILRHGARKHPD--KEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHE----YLEAYF-AVPk 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 116 ----LHALHNAYEEACIAKLFGITKPRLIFCDGD---EYEKVKSATKDLQvTIVTMRNHPRGSVRIQDVLTTPVMQNFQP 188
Cdd:PRK06187 79 igavLHPINIRLKPEEIAYILNDAEDRVVLVDSEfvpLLAAILPQLPTVR-TVIVEGDGPAAPLAPEVGEYEELLAAASD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 189 LRLKDGID-HTLA-ILSSSGTSGFPKAVTISN----SHKIIV-DYMAINNSNI------QYTSSTLDWCSglsMAITSGV 255
Cdd:PRK06187 158 TFDFPDIDeNDAAaMLYTSGTTGHPKGVVLSHrnlfLHSLAVcAWLKLSRDDVylvivpMFHVHAWGLPY---LALMAGA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 256 fstTSIIADcDFDPGLFCRAIGKYRISMVLLSSSYLAIFANCPEFESADLSSLNYVIFGGSSCSLEVQRKVRSRlsHDCl 335
Cdd:PRK06187 235 ---KQVIPR-RFDPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYFVDFSSLRLVIYGGAALPPALLREFKEK--FGI- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 336 NFC--YGLTELNSAGSVN------LNFDEKPNSVGRAIRGIKIKVIDEQGEAQEPNV--VGEICFHNSQKWAGYYKNPDE 405
Cdd:PRK06187 308 DLVqgYGMTETSPVVSVLppedqlPGQWTKRRSAGRPLPGVEARIVDDDGDELPPDGgeVGEIIVRGPWLMQGYWNRPEA 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 406 TRQIQDSEnWIHTGDLGYVDKDGYLFVIDRLKDMLKY--QNImyYPSEIENVIAEMPNVLEACVFGIWDPVNGDEAAASL 483
Cdd:PRK06187 388 TAETIDGG-WLHTGDVGYIDEDGYLYITDRIKDVIISggENI--YPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVV 464
|
490 500
....*....|....*....|....*.
gi 281365686 484 VKKPGTQLEAQDVVEYVRKRItAKFK 509
Cdd:PRK06187 465 VLKPGATLDAKELRAFLRGRL-AKFK 489
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
64-504 |
1.69e-52 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 187.11 E-value: 1.69e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 64 VLTREDLHMNAMRVASYMRNMGLGQTDIVGVMGRHTTHQSAVAYACFFNGTPLHALHNAYEEACIAKLFGITKPRLIFCD 143
Cdd:PLN02246 50 VYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAKLIITQ 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 144 GDEYEKVKSATKDLQVTIVTMRNHPRGSVRIQDvLTTPVMQNFQPLRLKDgiDHTLAILSSSGTSGFPKAVTISnsHKII 223
Cdd:PLN02246 130 SCYVDKLKGLAEDDGVTVVTIDDPPEGCLHFSE-LTQADENELPEVEISP--DDVVALPYSSGTTGLPKGVMLT--HKGL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 224 VDYMAI----NNSNIQYTSSTLDWCS-------GLSMAITSGVFSTTSIIADCDFDPGLFCRAIGKYRISMVLLSSSYLA 292
Cdd:PLN02246 205 VTSVAQqvdgENPNLYFHSDDVILCVlpmfhiySLNSVLLCGLRVGAAILIMPKFEIGALLELIQRHKVTIAPFVPPIVL 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 293 IFANCPEFESADLSSLNYVIFGGSSCSLEVQRKVRSRLSHDCLNFCYGLTELNSAGSVNLNF-----DEKPNSVGRAIRG 367
Cdd:PLN02246 285 AIAKSPVVEKYDLSSIRMVLSGAAPLGKELEDAFRAKLPNAVLGQGYGMTEAGPVLAMCLAFakepfPVKSGSCGTVVRN 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 368 IKIKVID-EQGEAQEPNVVGEICFHNSQKWAGYYKNPDETRQIQDSENWIHTGDLGYVDKDGYLFVIDRLKDMLKYQNIM 446
Cdd:PLN02246 365 AELKIVDpETGASLPRNQPGEICIRGPQIMKGYLNDPEATANTIDKDGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQ 444
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 281365686 447 YYPSEIENVIAEMPNVLEACVFGIWDPVNGDEAAASLVKKPGTQLEAQDVVEYVRKRI 504
Cdd:PLN02246 445 VAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVVRSNGSEITEDEIKQFVAKQV 502
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
205-509 |
5.04e-52 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 180.94 E-value: 5.04e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 205 SGTSGFPKAVTISNsHKIIvdymaiNNSNI-----QYTSST-------LDWCSGLSMAITSGV-FSTTSIIADCDFDPGL 271
Cdd:cd05917 11 SGTTGSPKGATLTH-HNIV------NNGYFigerlGLTEQDrlcipvpLFHCFGSVLGVLACLtHGATMVFPSPSFDPLA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 272 FCRAIGKYRISMVL-LSSSYLAIFaNCPEFESADLSSLNYVIFGGSSCSLEVQRKVRSRLSHDCLNFCYGLTE---LNSA 347
Cdd:cd05917 84 VLEAIEKEKCTALHgVPTMFIAEL-EHPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEVMNMKDVTIAYGMTEtspVSTQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 348 GSVNLNFDEKPNSVGRAIRGIKIKVIDEQGEAQEP-NVVGEICFHNSQKWAGYYKNPDETRQIQDSENWIHTGDLGYVDK 426
Cdd:cd05917 163 TRTDDSIEKRVNTVGRIMPHTEAKIVDPEGGIVPPvGVPGELCIRGYSVMKGYWNDPEKTAEAIDGDGWLHTGDLAVMDE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 427 DGYLFVIDRLKDMLKY--QNImyYPSEIENVIAEMPNVLEACVFGIWDPVNGDEAAASLVKKPGTQLEAQDVVEYVRKRI 504
Cdd:cd05917 243 DGYCRIVGRIKDMIIRggENI--YPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLKEGAELTEEDIKAYCKGKI 320
|
....*
gi 281365686 505 tAKFK 509
Cdd:cd05917 321 -AHYK 324
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
46-510 |
1.21e-51 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 184.34 E-value: 1.21e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 46 DMVNNPKLIAQIS---------ITEDIVLTREDLHMNAMRVASYMRNMGLGQTDIVGVMGRHTTHQSAVAYACFFNGTPL 116
Cdd:PRK07656 3 EWMTLPELLARAArrfgdkeayVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 117 HALHNAYEEACIAKLFGITKPRLIFCDGD---EYEKVKSATKDLQVTIV----TMRNHPRGSVRIQDVLTTPvMQNFQPL 189
Cdd:PRK07656 83 VPLNTRYTADEAAYILARGDAKALFVLGLflgVDYSATTRLPALEHVVIceteEDDPHTEKMKTFTDFLAAG-DPAERAP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 190 RLKDgiDHTLAILSSSGTSGFPKAVTISnsHKiivdymainnsniQYTSSTLDWCSGLSmaITSG-----------VFST 258
Cdd:PRK07656 162 EVDP--DDVADILFTSGTTGRPKGAMLT--HR-------------QLLSNAADWAEYLG--LTEGdrylaanpffhVFGY 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 259 TSIIADC-----------DFDPGLFCRAIGKYRISMV---------LLSSsylaifancPEFESADLSSLNYVIFGGSSC 318
Cdd:PRK07656 223 KAGVNAPlmrgatilplpVFDPDEVFRLIETERITVLpgpptmynsLLQH---------PDRSAEDLSSLRLAVTGAASM 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 319 SLEVQRKVRSRLSHDCLNFCYGLTElnSAGSVNLN-----FDEKPNSVGRAIRGIKIKVIDEQGEAQEPNVVGEIC---F 390
Cdd:PRK07656 294 PVALLERFESELGVDIVLTGYGLSE--ASGVTTFNrldddRKTVAGTIGTAIAGVENKIVNELGEEVPVGEVGELLvrgP 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 391 HNSQkwaGYYKNPDETRQIQDSENWIHTGDLGYVDKDGYLFVIDRLKDMLKYQNIMYYPSEIENVIAEMPNVLEACVFGI 470
Cdd:PRK07656 372 NVMK---GYYDDPEATAAAIDADGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGV 448
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 281365686 471 WDPVNGDEAAASLVKKPGTQLEAQDVVEYVRKRItAKFKQ 510
Cdd:PRK07656 449 PDERLGEVGKAYVVLKPGAELTEEELIAYCREHL-AKYKV 487
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
61-509 |
1.17e-48 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 176.28 E-value: 1.17e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 61 EDIVLTREDLHMNAMRVASYMRNMGLGQTDIVGVMGRHTTHQSAVAYACFFNG---TPLHALHNAYEeacIAKLFGITKP 137
Cdd:PRK08316 33 GDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGavhVPVNFMLTGEE---LAYILDHSGA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 138 RLIFCDGDEYEKVKSATKDLQVT------IVTMRNHPRGSVRIQDVLTTPvmQNFQPLRLKDGIDhtLA-ILSSSGTSGF 210
Cdd:PRK08316 110 RAFLVDPALAPTAEAALALLPVDtlilslVLGGREAPGGWLDFADWAEAG--SVAEPDVELADDD--LAqILYTSGTESL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 211 PKAVTISnsHKIIVDymainnsniQYTSS--TLDWCSG------------------LSMAITSGvfsTTSIIADCDfDPG 270
Cdd:PRK08316 186 PKGAMLT--HRALIA---------EYVSCivAGDMSADdiplhalplyhcaqldvfLGPYLYVG---ATNVILDAP-DPE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 271 LFCRAIGKYRISMVLLSSSYLAIFANCPEFESADLSSLNYVIFGGSSCSLEVQRKVRSRLSHDCLNFCYGLTELNSAGSV 350
Cdd:PRK08316 251 LILRTIEAERITSFFAPPTVWISLLRHPDFDTRDLSSLRKGYYGASIMPVEVLKELRERLPGLRFYNCYGQTEIAPLATV 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 351 nLNFDE---KPNSVGRAIRGIKIKVIDEQGEAQEPNVVGEICFHNSQKWAGYYKNPDETRQ-IQDSenWIHTGDLGYVDK 426
Cdd:PRK08316 331 -LGPEEhlrRPGSAGRPVLNVETRVVDDDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEaFRGG--WFHSGDLGVMDE 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 427 DGYLFVIDRLKDMLKYQNIMYYPSEIENVIAEMPNVLEACVFGIWDPVNGDEAAASLVKKPGTQLEAQDVVEYVRKRItA 506
Cdd:PRK08316 408 EGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAGATVTEDELIAHCRARL-A 486
|
...
gi 281365686 507 KFK 509
Cdd:PRK08316 487 GFK 489
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
205-509 |
1.59e-48 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 176.54 E-value: 1.59e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 205 SGTSGFPKAVTISnsHKIIVdymaiNN-----SNIQYTSST-------LDWCSGLSM----AITSGvfSTTSIIADcDFD 268
Cdd:PRK08315 208 SGTTGFPKGATLT--HRNIL-----NNgyfigEAMKLTEEDrlcipvpLYHCFGMVLgnlaCVTHG--ATMVYPGE-GFD 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 269 PGLFCRAIGKYRIS-------MvllsssYLAIFaNCPEFESADLSSLNYVIFGGSSCSLEVQRKVRSRLSHDCLNFCYGL 341
Cdd:PRK08315 278 PLATLAAVEEERCTalygvptM------FIAEL-DHPDFARFDLSSLRTGIMAGSPCPIEVMKRVIDKMHMSEVTIAYGM 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 342 TE---LNSAGSVNLNFDEKPNSVGRAIRGIKIKVID-EQGEAQEPNVVGEIC---FHNSQkwaGYYKNPDETRQIQDSEN 414
Cdd:PRK08315 351 TEtspVSTQTRTDDPLEKRVTTVGRALPHLEVKIVDpETGETVPRGEQGELCtrgYSVMK---GYWNDPEKTAEAIDADG 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 415 WIHTGDLGYVDKDGYLFVIDRLKDMLKY--QNImyYPSEIENVIAEMPNVLEACVFGIWDPVNGDEAAASLVKKPGTQLE 492
Cdd:PRK08315 428 WMHTGDLAVMDEEGYVNIVGRIKDMIIRggENI--YPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRPGATLT 505
|
330
....*....|....*..
gi 281365686 493 AQDVVEYVRKRItAKFK 509
Cdd:PRK08315 506 EEDVRDFCRGKI-AHYK 521
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
196-509 |
1.05e-44 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 166.10 E-value: 1.05e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 196 DHTLAILSSSGTSGFPKAVTIS-----NSHKIIVDYMAINNSNIQYTSSTLDWCSGLSMAITSGVFSTTSIIADCD-FDP 269
Cdd:PRK12583 201 DDPINIQYTSGTTGFPKGATLShhnilNNGYFVAESLGLTEHDRLCVPVPLYHCFGMVLANLGCMTVGACLVYPNEaFDP 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 270 GLFCRAIGKYRISMVL-LSSSYLAIFANcPEFESADLSSLNYVIFGGSSCSLEVQRKVRSRLSHDCLNFCYGLTE---LN 345
Cdd:PRK12583 281 LATLQAVEEERCTALYgVPTMFIAELDH-PQRGNFDLSSLRTGIMAGAPCPIEVMRRVMDEMHMAEVQIAYGMTEtspVS 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 346 SAGSVNLNFDEKPNSVGRAIRGIKIKVIDEQGEAQEPNVVGEICFHNSQKWAGYYKNPDETRQIQDSENWIHTGDLGYVD 425
Cdd:PRK12583 360 LQTTAADDLERRVETVGRTQPHLEVKVVDPDGATVPRGEIGELCTRGYSVMKGYWNNPEATAESIDEDGWMHTGDLATMD 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 426 KDGYLFVIDRLKDMLKY--QNImyYPSEIENVIAEMPNVLEACVFGIWDPVNGDEAAASLVKKPGTQLEAQDVVEYVRKR 503
Cdd:PRK12583 440 EQGYVRIVGRSKDMIIRggENI--YPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRLHPGHAASEEELREFCKAR 517
|
....*.
gi 281365686 504 ItAKFK 509
Cdd:PRK12583 518 I-AHFK 522
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
49-509 |
2.26e-43 |
|
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: 160.94 E-value: 2.26e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 49 NNPKLIAqisITEDIVLTREDLHMNAMRVASYMRNMGLGQTDIVGV-MGRhtTHQSAVA-YACFFNGTPLHALHNAYEEA 126
Cdd:cd05926 2 DAPALVV---PGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIaLPN--GLEFVVAfLAAARAGAVVAPLNPAYKKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 127 CIAKLFGITKPRLIFCDGDE-YEKVKSA------TKDLQVTIVTMRNHPRGSvriQDVLTTPVMQNFQPLRLKDGIDHTL 199
Cdd:cd05926 77 EFEFYLADLGSKLVLTPKGElGPASRAAsklglaILELALDVGVLIRAPSAE---SLSNLLADKKNAKSEGVPLPDDLAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 200 aILSSSGTSGFPKAV-----TISNSHKIIVDYMAINNSNIQYTSSTLDWCSGLSMAITSGVFSTTSIIADCDFDPGLFCR 274
Cdd:cd05926 154 -ILHTSGTTGRPKGVplthrNLAASATNITNTYKLTPDDRTLVVMPLFHVHGLVASLLSTLAAGGSVVLPPRFSASTFWP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 275 AIGKYR---------ISMVLLSSSylaifancPEFESADLSSLNYVIFGGSSCSLEVQRKVRSRLSHDCLNfCYGLTELN 345
Cdd:cd05926 233 DVRDYNatwytavptIHQILLNRP--------EPNPESPPPKLRFIRSCSASLPPAVLEALEATFGAPVLE-AYGMTEAA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 346 SAGSVNlNFDE---KPNSVGRAIrGIKIKVIDEQGEAQEPNVVGEICFHNSQKWAGYYKNPDETRQIQDSENWIHTGDLG 422
Cdd:cd05926 304 HQMTSN-PLPPgprKPGSVGKPV-GVEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGWFRTGDLG 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 423 YVDKDGYLFVIDRLKDMLKY--QNIMyyPSEIENVIAEMPNVLEACVFGIWDPVNGDEAAASLVKKPGTQLEAQDVVEYV 500
Cdd:cd05926 382 YLDADGYLFLTGRIKELINRggEKIS--PLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGASVTEEELRAFC 459
|
....*....
gi 281365686 501 RKRItAKFK 509
Cdd:cd05926 460 RKHL-AAFK 467
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
186-538 |
1.50e-42 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 159.38 E-value: 1.50e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 186 FQPLRLKDGIDHT--LAILSSSGTSGFPKAVTISnsHKIIVDyMAinnsNIQYTssTLDW--------CSGLSMA----I 251
Cdd:PRK06188 156 FGPAPLVAAALPPdiAGLAYTGGTTGKPKGVMGT--HRSIAT-MA----QIQLA--EWEWpadprflmCTPLSHAggafF 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 252 TSGVFSTTSIIADCDFDPGLFCRAIGKYRISMVLLSSSYLAIFANCPEFESADLSSLNYVIFGGSSCSlevqrKVRSRLS 331
Cdd:PRK06188 227 LPTLLRGGTVIVLAKFDPAEVLRAIEEQRITATFLVPTMIYALLDHPDLRTRDLSSLETVYYGASPMS-----PVRLAEA 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 332 HDCLN--FC--YGLTELNSAGSVNLNFDEKPN------SVGRAIRGIKIKVIDEQGEAQEPNVVGEICFHNSQKWAGYYK 401
Cdd:PRK06188 302 IERFGpiFAqyYGQTEAPMVITYLRKRDHDPDdpkrltSCGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWN 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 402 NPDETRQIQdSENWIHTGDLGYVDKDGYLFVIDRLKDMLKYQNIMYYPSEIENVIAEMPNVLEACVFGIWDPVNGDEAAA 481
Cdd:PRK06188 382 RPEETAEAF-RDGWLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTA 460
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 482 SLVKKPGTQLEAQDVVEYVRKR---ITAKfKQLNggalIVDQIVRSGNRKTNRSAVKEHF 538
Cdd:PRK06188 461 VVVLRPGAAVDAAELQAHVKERkgsVHAP-KQVD----FVDSLPLTALGKPDKKALRARY 515
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
59-536 |
1.79e-41 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 155.79 E-value: 1.79e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 59 ITEDIVLTREDLHMNAMRVASYMRN-MGLGQTDIVGVMGrhtthQSAVAYacffngtpLHALHNAYEEACIAKLFGI--T 135
Cdd:PRK06839 22 ITEEEEMTYKQLHEYVSKVAAYLIYeLNVKKGERIAILS-----QNSLEY--------IVLLFAIAKVECIAVPLNIrlT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 136 KPRLIFCDGDEYEKVKSATKDLQVTIVTMRNhpRGSVRIQDVLTTPV-MQNFQPLRLKD-GIDHTLAILSSSGTSGFPKA 213
Cdd:PRK06839 89 ENELIFQLKDSGTTVLFVEKTFQNMALSMQK--VSYVQRVISITSLKeIEDRKIDNFVEkNESASFIICYTSGTTGKPKG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 214 VTISNSHKIivdYMAINNS-NIQYTSStlDWC---------SGLSMAITSGVFSTTSIIADCDFDPGLFCRAIGKYRISM 283
Cdd:PRK06839 167 AVLTQENMF---WNALNNTfAIDLTMH--DRSivllplfhiGGIGLFAFPTLFAGGVIIVPRKFEPTKALSMIEKHKVTV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 284 VLLSSSYLAIFANCPEFESADLSSLNYVIFGGSSCSLEVQRKVRSRlshdCLNFC--YGLTElnSAGSVNL----NFDEK 357
Cdd:PRK06839 242 VMGVPTIHQALINCSKFETTNLQSVRWFYNGGAPCPEELMREFIDR----GFLFGqgFGMTE--TSPTVFMlseeDARRK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 358 PNSVGRAIRGIKIKVIDEQGEAQEPNVVGEICFHNSQKWAGYYKNPDETRQ-IQDSenWIHTGDLGYVDKDGYLFVIDRL 436
Cdd:PRK06839 316 VGSIGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEEtIQDG--WLCTGDLARVDEDGFVYIVGRK 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 437 KDMLKY--QNImyYPSEIENVIAEMPNVLEACVFGIWDPVNGDEAAASLVKKPGTQLEAQDVVEYVRKRItAKFKqLNGG 514
Cdd:PRK06839 394 KEMIISggENI--YPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVLIEKDVIEHCRLFL-AKYK-IPKE 469
|
490 500
....*....|....*....|..
gi 281365686 515 ALIVDQIVRSGNRKTNRSAVKE 536
Cdd:PRK06839 470 IVFLKELPKNATGKIQKAQLVN 491
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
61-506 |
6.55e-40 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 152.57 E-value: 6.55e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 61 EDIVLTREDLHMNAMRVASYMRNMGLGQTDIVGV-MGRhtTHQSAVAY-ACFFNG---TPLHALHNAyeEAcIAKLFGIT 135
Cdd:COG0365 36 EERTLTYAELRREVNRFANALRALGVKKGDRVAIyLPN--IPEAVIAMlACARIGavhSPVFPGFGA--EA-LADRIEDA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 136 KPRLIFCDgDEY-------------EKVKSATKDLQVTIVTMRN----HPRGSVRIQDVLTTPVmQNFQPLRLKDgiDHT 198
Cdd:COG0365 111 EAKVLITA-DGGlrggkvidlkekvDEALEELPSLEHVIVVGRTgadvPMEGDLDWDELLAAAS-AEFEPEPTDA--DDP 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 199 LAILSSSGTSGFPKAVTISNShkiivDYMAINNSNIQYTsstLD-------WCS---GLSMAITSGVFS-----TTSIIA 263
Cdd:COG0365 187 LFILYTSGTTGKPKGVVHTHG-----GYLVHAATTAKYV---LDlkpgdvfWCTadiGWATGHSYIVYGpllngATVVLY 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 264 D--CDF-DPGLFCRAIGKYRISMVLLSSSYLAIFAN-CPEF-ESADLSSLNYVIFGGSSCSLEVQRKVRSRLSHDCLNFc 338
Cdd:COG0365 259 EgrPDFpDPGRLWELIEKYGVTVFFTAPTAIRALMKaGDEPlKKYDLSSLRLLGSAGEPLNPEVWEWWYEAVGVPIVDG- 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 339 YGLTELNSA-GSVNLNFDEKPNSVGRAIRGIKIKVIDEQGEAQEPNVVGEICFHNSqkW----AGYYKNPDETRQI--QD 411
Cdd:COG0365 338 WGQTETGGIfISNLPGLPVKPGSMGKPVPGYDVAVVDEDGNPVPPGEEGELVIKGP--WpgmfRGYWNDPERYRETyfGR 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 412 SENWIHTGDLGYVDKDGYLFVIDRLKDMLKY--QNImyYPSEIENVIAEMPNVLEACVFGIWDPVNGDEAAASLVKKPGT 489
Cdd:COG0365 416 FPGWYRTGDGARRDEDGYFWILGRSDDVINVsgHRI--GTAEIESALVSHPAVAEAAVVGVPDEIRGQVVKAFVVLKPGV 493
|
490 500
....*....|....*....|
gi 281365686 490 QLE---AQDVVEYVRKRITA 506
Cdd:COG0365 494 EPSdelAKELQAHVREELGP 513
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
201-509 |
1.01e-39 |
|
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: 147.26 E-value: 1.01e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 201 ILSSSGTSGFPKAVTISnsHKIIVDYMAINNSNIQYTSSTLDWCS-------GLSMAITSGVFSTTSIIADCDFDPGLFC 273
Cdd:cd17638 5 IMFTSGTTGRSKGVMCA--HRQTLRAAAAWADCADLTEDDRYLIInpffhtfGYKAGIVACLLTGATVVPVAVFDVDAIL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 274 RAIGKYRISMVLLSSS-YLAIFANcPEFESADLSSLNYVIFGGSSCSLEVQRKVRSRLSHDCLNFCYGLTElnsAGSVNL 352
Cdd:cd17638 83 EAIERERITVLPGPPTlFQSLLDH-PGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFETVLTAYGLTE---AGVATM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 353 -----NFDEKPNSVGRAIRGIKIKVIDEqgeaqepnvvGEICFHNSQKWAGYYKNPDETRQIQDSENWIHTGDLGYVDKD 427
Cdd:cd17638 159 crpgdDAETVATTCGRACPGFEVRIADD----------GEVLVRGYNVMQGYLDDPEATAEAIDADGWLHTGDVGELDER 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 428 GYLFVIDRLKDMLKYQNIMYYPSEIENVIAEMPNVLEACVFGIWDPVNGDEAAASLVKKPGTQLEAQDVVEYVRKRItAK 507
Cdd:cd17638 229 GYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGVTLTEEDVIAWCRERL-AN 307
|
..
gi 281365686 508 FK 509
Cdd:cd17638 308 YK 309
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
199-531 |
1.96e-39 |
|
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: 148.78 E-value: 1.96e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 199 LAILS-SSGTSGFPKAV----------TISNSHKIIVDYMAINNSNIQYTSSTldwcsGLSMAITSGVFSTTSIIADCDF 267
Cdd:cd05935 86 LALIPyTSGTTGLPKGCmhthfsaaanALQSAVWTGLTPSDVILACLPLFHVT-----GFVGSLNTAVYVGGTYVLMARW 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 268 DPGLFCRAIGKYRISMVLLSSSYLAIFANCPEFESADLSSLNYVIFGGSSCSLEVQRKVRSRLSHDcLNFCYGLTELNSA 347
Cdd:cd05935 161 DRETALELIEKYKVTFWTNIPTMLVDLLATPEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTGLR-FVEGYGLTETMSQ 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 348 GSVNLNFDEKPNSVGRAIRGIKIKVID-EQGEAQEPNVVGEICFHNSQKWAGYYKNPDETRQ--IQDS-ENWIHTGDLGY 423
Cdd:cd05935 240 THTNPPLRPKLQCLGIP*FGVDARVIDiETGRELPPNEVGEIVVRGPQIFKGYWNRPEETEEsfIEIKgRRFFRTGDLGY 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 424 VDKDGYLFVIDRLKDMLKYQNIMYYPSEIENVIAEMPNVLEACVFGIWDPVNGDEAAASLVKKPGTQLEA--QDVVEYVR 501
Cdd:cd05935 320 MDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEYRGKVteEDIIEWAR 399
|
330 340 350
....*....|....*....|....*....|
gi 281365686 502 KRITAkFKQLNgGALIVDQIVRSGNRKTNR 531
Cdd:cd05935 400 EQMAA-YKYPR-EVEFVDELPRSASGKILW 427
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
59-509 |
1.32e-37 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 145.23 E-value: 1.32e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 59 ITEDIVLTREDLHMNAMRVASYMRNMGLGQTDIVGVMGRHTTHQSAVAYACFFNG---TPLHaLHNAYEEacIAKLFGIT 135
Cdd:PRK12406 6 ISGDRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGayaVPVN-WHFKPEE--IAYILEDS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 136 KPRLIFCDGDEYEKVKSAT-KDLQVTIVTMRNHPRGSVRIQDVLTTPV---------MQNFQPlrlKDG--IDHTLAILS 203
Cdd:PRK12406 83 GARVLIAHADLLHGLASALpAGVTVLSVPTPPEIAAAYRISPALLTPPagaidwegwLAQQEP---YDGppVPQPQSMIY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 204 SSGTSGFPKAVTISN---SHKIIVDYMAINNSNIQYTSSTLdwCSGL-------SMAITSGVFSTTsIIADCDFDPGLFC 273
Cdd:PRK12406 160 TSGTTGHPKGVRRAAptpEQAAAAEQMRALIYGLKPGIRAL--LTGPlyhsapnAYGLRAGRLGGV-LVLQPRFDPEELL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 274 RAIGKYRIS-MVLLSSSYLAIFANCPEFESA-DLSSLNYVIFGGSSCSLEVQRKVRSRLSHDCLNFcYGLTElnsAGSVN 351
Cdd:PRK12406 237 QLIERHRIThMHMVPTMFIRLLKLPEEVRAKyDVSSLRHVIHAAAPCPADVKRAMIEWWGPVIYEY-YGSTE---SGAVT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 352 LNFDE----KPNSVGRAIRGIKIKVIDEQGEAQEPNVVGEICFHNsqkwAGY----YKNPDETRQIQDSENWIHTGDLGY 423
Cdd:PRK12406 313 FATSEdalsHPGTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRI----AGNpdftYHNKPEKRAEIDRGGFITSGDVGY 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 424 VDKDGYLFVIDRLKDMLKYQNIMYYPSEIENVIAEMPNVLEACVFGIWDPVNGDEAAASLVKKPGTQLEAQDVVEYVRKR 503
Cdd:PRK12406 389 LDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPGATLDEADIRAQLKAR 468
|
....*.
gi 281365686 504 ItAKFK 509
Cdd:PRK12406 469 L-AGYK 473
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
59-509 |
1.52e-37 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 145.84 E-value: 1.52e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 59 ITEDIVLTREDLHMNAMRVASYMRNMGLGQTDIVGVMGRHttHQSAV--AYACFFNGTPLHALHNAYEEACIAKLFGITK 136
Cdd:PRK07788 69 IDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARN--HRGFVlaLYAAGKVGARIILLNTGFSGPQLAEVAAREG 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 137 PRLIFCDgDEYEKVKSATKDLQVTIVTMRNHPRGsVRIQDVlTTPVMQNF------QPLRL---KDGIdhtlaILSSSGT 207
Cdd:PRK07788 147 VKALVYD-DEFTDLLSALPPDLGRLRAWGGNPDD-DEPSGS-TDETLDDLiagsstAPLPKppkPGGI-----VILTSGT 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 208 SGFPKAVTISN-----SHKIIVDYMAIN-NSNIQYTSS---TLDW-CSGLSMAITSgvfsttSIIADCDFDPGLFCRAIG 277
Cdd:PRK07788 219 TGTPKGAPRPEpsplaPLAGLLSRVPFRaGETTLLPAPmfhATGWaHLTLAMALGS------TVVLRRRFDPEATLEDIA 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 278 KYRISMVLLSSSYLA-IFANCPEFESA-DLSSLNYVIFGGSSCSLEVQRKVRSRLSHDCLNFcYGLTELNSAGSVNL-NF 354
Cdd:PRK07788 293 KHKATALVVVPVMLSrILDLGPEVLAKyDTSSLKIIFVSGSALSPELATRALEAFGPVLYNL-YGSTEVAFATIATPeDL 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 355 DEKPNSVGRAIRGIKIKVIDEQGEAQEPNVVGEICFHNSQKWAGYYKNPDetRQIQDSenWIHTGDLGYVDKDGYLFVID 434
Cdd:PRK07788 372 AEAPGTVGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFPFEGYTDGRD--KQIIDG--LLSSGDVGYFDEDGLLFVDG 447
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281365686 435 RLKDMLKY--QNImyYPSEIENVIAEMPNVLEACVFGIWDPVNGDEAAASLVKKPGTQLEAQDVVEYVRKRItAKFK 509
Cdd:PRK07788 448 RDDDMIVSggENV--FPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKAPGAALDEDAIKDYVRDNL-ARYK 521
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
54-509 |
1.57e-37 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 145.05 E-value: 1.57e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 54 IAQISITEDIVLTREDLHMNAMRVASYMRNMGLGQTDIVGVMGRHTTHQSAVAYACFFNGTPLHAL--HNAYEEA----- 126
Cdd:PRK08276 1 PAVIMAPSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPInwHLTAAEIayivd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 127 -CIAKLFgITKPRLIfcdgdeyEKVKSATKDLqvtivtmrnhPRG-SVRIQDVLTTPVMQNFQPLRLK----DGIDHTL- 199
Cdd:PRK08276 81 dSGAKVL-IVSAALA-------DTAAELAAEL----------PAGvPLLLVVAGPVPGFRSYEEALAAqpdtPIADETAg 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 200 -AILSSSGTSGFPKAVTISNSHK-----------IIVDYMAINNSNIQ------YTSSTLDWCSglsMAITSGVfstTSI 261
Cdd:PRK08276 143 aDMLYSSGTTGRPKGIKRPLPGLdpdeapgmmlaLLGFGMYGGPDSVYlspaplYHTAPLRFGM---SALALGG---TVV 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 262 IADcDFDPGLFCRAIGKYRIS---MV------LLsssylaifaNCPEF--ESADLSSLNYVIFGGSSCSLEVQRKVRSRL 330
Cdd:PRK08276 217 VME-KFDAEEALALIERYRVThsqLVptmfvrML---------KLPEEvrARYDVSSLRVAIHAAAPCPVEVKRAMIDWW 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 331 ShDCLNFCYGLTELNsaGSVNLNFDE---KPNSVGRAIRGiKIKVIDEQGEAQEPNVVGEICFHNSQKWAGYYKNPDETR 407
Cdd:PRK08276 287 G-PIIHEYYASSEGG--GVTVITSEDwlaHPGSVGKAVLG-EVRILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTA 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 408 QIQDSENWIHTGDLGYVDKDGYLFVIDRLKDMLKYQ--NImyYPSEIENVIAEMPNVLEACVFGIWDPVNGDEAAASLVK 485
Cdd:PRK08276 363 AARNPHGWVTVGDVGYLDEDGYLYLTDRKSDMIISGgvNI--YPQEIENLLVTHPKVADVAVFGVPDEEMGERVKAVVQP 440
|
490 500
....*....|....*....|....*..
gi 281365686 486 KPGTQL---EAQDVVEYVRKRItAKFK 509
Cdd:PRK08276 441 ADGADAgdaLAAELIAWLRGRL-AHYK 466
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
64-509 |
1.98e-37 |
|
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: 143.29 E-value: 1.98e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 64 VLTREDLHMNAMRVASYMRNMGLGQTDIVGVM--GRHtthQSAVAY-ACFFNGTPLHALHNAYEEACIAKLFGITKPRLI 140
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQlpNWW---EFAVLYlACLRIGAVTNPILPFFREHELAFILRRAKAKVF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 141 FcdgdeyekvksatkdlqvtivtmrnhprgsvriqdvlttpVMQNFQPLRLKDGIDHTLAILSSSGTSGFPKAV-----T 215
Cdd:cd05903 78 V----------------------------------------VPERFRQFDPAAMPDAVALLLFTSGTTGEPKGVmhshnT 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 216 ISNSHKIIVDYMAINNSNIQYTSSTLDWCSGLSMAITSGVFSTTSIIADCDFDPGLFCRAIGKYRISMVLLSSSYLAIFA 295
Cdd:cd05903 118 LSASIRQYAERLGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQDIWDPDKALALMREHGVTFMMGATPFLTDLL 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 296 NCPEFESADLSSLNYVIFGGSScsleVQRKVRSRLShDCLNF----CYGLTELNSA-GSVNLNFDEKP-NSVGRAIRGIK 369
Cdd:cd05903 198 NAVEEAGEPLSRLRTFVCGGAT----VPRSLARRAA-ELLGAkvcsAYGSTECPGAvTSITPAPEDRRlYTDGRPLPGVE 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 370 IKVIDEQGEAQEPNVVGEICFHNSQKWAGYYKNPDETRQiQDSENWIHTGDLGYVDKDGYLFVIDRLKDMLKY--QNIMy 447
Cdd:cd05903 273 IKVVDDTGATLAPGVEGELLSRGPSVFLGYLDRPDLTAD-AAPEGWFRTGDLARLDEDGYLRITGRSKDIIIRggENIP- 350
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281365686 448 yPSEIENVIAEMPNVLEACVFGIWDPVNGDEAAASLVKKPGTQLEAQDVVEYVRKRITAKFK 509
Cdd:cd05903 351 -VLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGALLTFDELVAYLDRQGVAKQY 411
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
296-510 |
2.04e-37 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 145.40 E-value: 2.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 296 NCPEFESADLSSLNYVIFGGsscsLEVQRKVRSR---LSHDCLNFCYGLTELNSAGSVN-LNFDEKPNSVGRAIRGIKIK 371
Cdd:PRK08751 319 NTPGFDQIDFSSLKMTLGGG----MAVQRSVAERwkqVTGLTLVEAYGLTETSPAACINpLTLKEYNGSIGLPIPSTDAC 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 372 VIDEQGEAQEPNVVGEICFHNSQKWAGYYKNPDETRQIQDSENWIHTGDLGYVDKDGYLFVIDRLKDMLKYQNIMYYPSE 451
Cdd:PRK08751 395 IKDDAGTVLAIGEIGELCIKGPQVMKGYWKRPEETAKVMDADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNE 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 281365686 452 IENVIAEMPNVLEACVFGIWDPVNGDEAAASLVKKpGTQLEAQDVVEYVRKRITAkFKQ 510
Cdd:PRK08751 475 IEDVIAMMPGVLEVAAVGVPDEKSGEIVKVVIVKK-DPALTAEDVKAHARANLTG-YKQ 531
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
65-506 |
3.98e-37 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 144.79 E-value: 3.98e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 65 LTREDLHMNAMRVASYMRNMGLGQTDIVGVMGRHTTHQSAVAYACFFNGTPLHALHNAYEEACIAKLFGITKPRLIFCDG 144
Cdd:PRK06710 50 ITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILCLD 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 145 DEYEKV---KSATKdLQVTIVTmrnhprgsvRIQDVLTTP-------VMQNFQPLRLKDGIDHT---------------- 198
Cdd:PRK06710 130 LVFPRVtnvQSATK-IEHVIVT---------RIADFLPFPknllypfVQKKQSNLVVKVSESETihlwnsvekevntgve 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 199 --------LAILS-SSGTSGFPKAVTISnsHKIIVD---------YMAINNSNIQYTSSTLDWCSGLSMAITSGVFSTTS 260
Cdd:PRK06710 200 vpcdpendLALLQyTGGTTGFPKGVMLT--HKNLVSntlmgvqwlYNCKEGEEVVLGVLPFFHVYGMTAVMNLSIMQGYK 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 261 IIADCDFDPGLFCRAIGKYRISMVLLSSSYLAIFANCPEFESADLSSLNYVIFGGSSCSLEVQRKVRsRLSHDCLNFCYG 340
Cdd:PRK06710 278 MVLIPKFDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLLKEYDISSIRACISGSAPLPVEVQEKFE-TVTGGKLVEGYG 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 341 LTELNSAGSVNLNFDEK-PNSVGRAIRGIKIKVID-EQGEAQEPNVVGEICFHNSQKWAGYYKNPDETRQI-QDSenWIH 417
Cdd:PRK06710 357 LTESSPVTHSNFLWEKRvPGSIGVPWPDTEAMIMSlETGEALPPGEIGEIVVKGPQIMKGYWNKPEETAAVlQDG--WLH 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 418 TGDLGYVDKDGYLFVIDRLKDMLKYQNIMYYPSEIENVIAEMPNVLEACVFGIWDPVNGDEAAASLVKKPGTQLEAQDVV 497
Cdd:PRK06710 435 TGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVLKEGTECSEEELN 514
|
....*....
gi 281365686 498 EYVRKRITA 506
Cdd:PRK06710 515 QFARKYLAA 523
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
196-469 |
1.55e-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: 141.19 E-value: 1.55e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 196 DHTLAILSSSGTSGFPKAVTISNSH-----KIIVDYMAINNSNIQYT----SSTLDWCSGLSMAITSGV-----FSTTSI 261
Cdd:cd05907 87 DDLATIIYTSGTTGRPKGVMLSHRNilsnaLALAERLPATEGDRHLSflplAHVFERRAGLYVPLLAGAriyfaSSAETL 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 262 IADC-DFDPGLFCRAIGKYR-----ISMVLLSSSYLAIFAncpefeSADLSSLNYVIFGGSSCSLEVQRKVRsrlsHDCL 335
Cdd:cd05907 167 LDDLsEVRPTVFLAVPRVWEkvyaaIKVKAVPGLKRKLFD------LAVGGRLRFAASGGAPLPAELLHFFR----ALGI 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 336 NFC--YGLTELNSAGSVNLNFDEKPNSVGRAIRGIKIKvIDEQGEAQepnVVGEICFHnsqkwaGYYKNPDETRQIQDSE 413
Cdd:cd05907 237 PVYegYGLTETSAVVTLNPPGDNRIGTVGKPLPGVEVR-IADDGEIL---VRGPNVML------GYYKNPEATAEALDAD 306
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 281365686 414 NWIHTGDLGYVDKDGYLFVIDRLKDMLKY---QNImyYPSEIENVIAEMPNVLEACVFG 469
Cdd:cd05907 307 GWLHTGDLGEIDEDGFLHITGRKKDLIITsggKNI--SPEPIENALKASPLISQAVVIG 363
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
198-509 |
2.19e-36 |
|
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: 140.12 E-value: 2.19e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 198 TLAILSSSGTSGFPKAVTISNSH-----KIIVDYMAINNSNIQYTSSTLDWCSGLSMAITSGVFSTTSIIADCDFDPGLF 272
Cdd:cd05934 83 PASILYTSGTTGPPKGVVITHANltfagYYSARRFGLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLLPRFSASRF 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 273 CRAIGKYRISMVLLSSSYLAIFANCPEFESaDLSSLNYVIFGGSSCSLEVQRkVRSRLSHDCLNfCYGLTElNSAGSVN- 351
Cdd:cd05934 163 WSDVRRYGATVTNYLGAMLSYLLAQPPSPD-DRAHRLRAAYGAPNPPELHEE-FEERFGVRLLE-GYGMTE-TIVGVIGp 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 352 LNFDEKPNSVGRAIRGIKIKVIDEQGEAQEPNVVGEICFHNSQKWA---GYYKNPDETRQIQdSENWIHTGDLGYVDKDG 428
Cdd:cd05934 239 RDEPRRPGSIGRPAPGYEVRIVDDDGQELPAGEPGELVIRGLRGWGffkGYYNMPEATAEAM-RNGWFHTGDLGYRDADG 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 429 YLFVIDRLKDMLKY--QNIMyyPSEIENVIAEMPNVLEACVFGIWDPVNGDEAAASLVKKPGTQLEAQDVVEYVRKRItA 506
Cdd:cd05934 318 FFYFVDRKKDMIRRrgENIS--SAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLDPEELFAFCEGQL-A 394
|
...
gi 281365686 507 KFK 509
Cdd:cd05934 395 YFK 397
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
193-506 |
5.36e-36 |
|
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: 139.49 E-value: 5.36e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 193 DGIDHTLAILSSSGTSGFPKAVTisNSHKII-----VDYMAIN----NSNIQYTSSTLDWCSGLSMAITSGVFSTTSIIA 263
Cdd:cd05971 85 DGSDDPALIIYTSGTTGPPKGAL--HAHRVLlghlpGVQFPFNlfprDGDLYWTPADWAWIGGLLDVLLPSLYFGVPVLA 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 264 --DCDFDPGLFCRAIGKYRISMVLLSSSYLAIFANCPEFESADLSSLNYVIFGGSSCSLEVQRKVRSRLSHDCLNFcYGL 341
Cdd:cd05971 163 hrMTKFDPKAALDLMSRYGVTTAFLPPTALKMMRQQGEQLKHAQVKLRAIATGGESLGEELLGWAREQFGVEVNEF-YGQ 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 342 TELNSAGSVNLN-FDEKPNSVGRAIRGIKIKVIDEQGEAQEPNVVGEIC--FHNSQKWAGYYKNPDETRQiQDSENWIHT 418
Cdd:cd05971 242 TECNLVIGNCSAlFPIKPGSMGKPIPGHRVAIVDDNGTPLPPGEVGEIAveLPDPVAFLGYWNNPSATEK-KMAGDWLLT 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 419 GDLGYVDKDGYLFVIDRLKDMLKYQNIMYYPSEIENVIAEMPNVLEACVFGIWDPVNGDEAAASLVKKPG---TQLEAQD 495
Cdd:cd05971 321 GDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGetpSDALARE 400
|
330
....*....|.
gi 281365686 496 VVEYVRKRITA 506
Cdd:cd05971 401 IQELVKTRLAA 411
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
138-506 |
1.44e-35 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 140.10 E-value: 1.44e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 138 RLIFCDGDEYEKVKSATKDLQV--TIVTM------------------RNHPRGSVRIQDVLT--TPVMQNFQPLRLKDGI 195
Cdd:PRK08314 110 RVAIVGSELAPKVAPAVGNLRLrhVIVAQysdylpaepeiavpawlrAEPPLQALAPGGVVAwkEALAAGLAPPPHTAGP 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 196 DhTLAILS-SSGTSGFPKAVTisNSHKIIvdyMAINNSNIQYTSSTLD--------------WCSGLSMAITSGvfSTTS 260
Cdd:PRK08314 190 D-DLAVLPyTSGTTGVPKGCM--HTHRTV---MANAVGSVLWSNSTPEsvvlavlplfhvtgMVHSMNAPIYAG--ATVV 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 261 IIADCDFDpgLFCRAIGKYRIS-------MV--LLSSsylaifancPEFESADLSSLNYVIFGGSSCSLEVQRKVRSRLS 331
Cdd:PRK08314 262 LMPRWDRE--AAARLIERYRVThwtniptMVvdFLAS---------PGLAERDLSSLRYIGGGGAAMPEAVAERLKELTG 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 332 hdcLNFC--YGLTELNSAGSVNLNFDEKPNSVGRAIRGIKIKVID-EQGEAQEPNVVGEICFHNSQKWAGYYKNPDETRQ 408
Cdd:PRK08314 331 ---LDYVegYGLTETMAQTHSNPPDRPKLQCLGIPTFGVDARVIDpETLEELPPGEVGEIVVHGPQVFKGYWNRPEATAE 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 409 --IQ-DSENWIHTGDLGYVDKDGYLFVIDRLKDMLKYQNIMYYPSEIENVIAEMPNVLEACVFGIWDPVNGDEAAASLVK 485
Cdd:PRK08314 408 afIEiDGKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPDPRRGETVKAVVVL 487
|
410 420
....*....|....*....|...
gi 281365686 486 KPGTQ--LEAQDVVEYVRKRITA 506
Cdd:PRK08314 488 RPEARgkTTEEEIIAWAREHMAA 510
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
35-538 |
2.16e-35 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 139.59 E-value: 2.16e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 35 PNLSIGEIIFGDMvNNPKLIAQISITEDIVLTREDLHMNAMRVASYMRN-MGLGQTDIVGVMGRHTTHQSAVAYACFFNG 113
Cdd:PLN02574 38 PNLDAVSFIFSHH-NHNGDTALIDSSTGFSISYSELQPLVKSMAAGLYHvMGVRQGDVVLLLLPNSVYFPVIFLAVLSLG 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 114 TPLHALHNAYEEACIAKLFGITKPRLIFCDGDEYEKVKSatkdLQVTIVTM-RNHPRGSVRIQ------------DVLTT 180
Cdd:PLN02574 117 GIVTTMNPSSSLGEIKKRVVDCSVGLAFTSPENVEKLSP----LGVPVIGVpENYDFDSKRIEfpkfyelikedfDFVPK 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 181 PVMqnfqplrlkdGIDHTLAILSSSGTSGFPKAVTISNSHKIIV----------DYMAINNSNIQYTSSTLDWCSGLSMA 250
Cdd:PLN02574 193 PVI----------KQDDVAAIMYSSGTTGASKGVVLTHRNLIAMvelfvrfeasQYEYPGSDNVYLAALPMFHIYGLSLF 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 251 ITSGVFSTTSIIADCDFDPGLFCRAIGKYRIS--------MVLLSSSYLAIFANCpefesadLSSLNYVIFGGSSCSLEV 322
Cdd:PLN02574 263 VVGLLSLGSTIVVMRRFDASDMVKVIDRFKVThfpvvppiLMALTKKAKGVCGEV-------LKSLKQVSCGAAPLSGKF 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 323 QRKVRSRLSHDCLNFCYGLTELNSAGSVNLNFDE--KPNSVGRAIRGIKIKVID-EQGEAQEPNVVGEICFHNSQKWAGY 399
Cdd:PLN02574 336 IQDFVQTLPHVDFIQGYGMTESTAVGTRGFNTEKlsKYSSVGLLAPNMQAKVVDwSTGCLLPPGNCGELWIQGPGVMKGY 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 400 YKNPDETRQIQDSENWIHTGDLGYVDKDGYLFVIDRLKDMLKYQNIMYYPSEIENVIAEMPNVLEACVFGIWDPVNGDEA 479
Cdd:PLN02574 416 LNNPKATQSTIDKDGWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIP 495
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 281365686 480 AASLVKKPGTQLEAQDVVEYVRKRItAKFKQLNgGALIVDQIVRSGNRKTNRSAVKEHF 538
Cdd:PLN02574 496 VAFVVRRQGSTLSQEAVINYVAKQV-APYKKVR-KVVFVQSIPKSPAGKILRRELKRSL 552
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
196-506 |
5.38e-35 |
|
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.
Pssm-ID: 341276 [Multi-domain] Cd Length: 428 Bit Score: 136.31 E-value: 5.38e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 196 DHTLAILSSSGTSGFPKAVTISNS----HKI-IVDYMAINNSNIQYTSSTLDWCSGLSMAITS--GVFSTTSIIADCDFD 268
Cdd:cd05972 81 EDPALIYFTSGTTGLPKGVLHTHSyplgHIPtAAYWLGLRPDDIHWNIADPGWAKGAWSSFFGpwLLGATVFVYEGPRFD 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 269 PGLFCRAIGKYRISMVLLSSSYLAIFANcPEFESADLSSLNYVIFGGSSCSLEVQRKVRSRLSHDCLNFcYGLTELNSAG 348
Cdd:cd05972 161 AERILELLERYGVTSFCGPPTAYRMLIK-QDLSSYKFSHLRLVVSAGEPLNPEVIEWWRAATGLPIRDG-YGQTETGLTV 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 349 SVNLNFDEKPNSVGRAIRGIKIKVIDEQGEAQEPNVVGEICFHNS--QKWAGYYKNPDETRQiQDSENWIHTGDLGYVDK 426
Cdd:cd05972 239 GNFPDMPVKPGSMGRPTPGYDVAIIDDDGRELPPGEEGDIAIKLPppGLFLGYVGDPEKTEA-SIRGDYYLTGDRAYRDE 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 427 DGYLFVIDRLKDMLKYQNIMYYPSEIENVIAEMPNVLEACVFGIWDPVNGDEAAASLVKKPG---TQLEAQDVVEYVRKR 503
Cdd:cd05972 318 DGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGyepSEELAEELQGHVKKV 397
|
...
gi 281365686 504 ITA 506
Cdd:cd05972 398 LAP 400
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
269-506 |
1.27e-33 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 134.51 E-value: 1.27e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 269 PGlFCRAIGKYRIS-MVLLSSSYLAIfANCPEFESADLSSLNYVIFGGSSCSLEVQRKVRSRLSHDCLNfCYGLTELNSA 347
Cdd:PRK05677 290 PA-MVKELGKWKFSgFVGLNTLFVAL-CNNEAFRKLDFSALKLTLSGGMALQLATAERWKEVTGCAICE-GYGMTETSPV 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 348 GSVNLNFDEKPNSVGRAIRGIKIKVIDEQGEAQEPNVVGEICFHNSQKWAGYYKNPDETRQIQDSENWIHTGDLGYVDKD 427
Cdd:PRK05677 367 VSVNPSQAIQVGTIGIPVPSTLCKVIDDDGNELPLGEVGELCVKGPQVMKGYWQRPEATDEILDSDGWLKTGDIALIQED 446
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281365686 428 GYLFVIDRLKDMLKYQNIMYYPSEIENVIAEMPNVLEACVFGIWDPVNGDEAAASLVKKPGTQLEAQDVVEYVRKRITA 506
Cdd:PRK05677 447 GYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIKVFVVVKPGETLTKEQVMEHMRANLTG 525
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
69-509 |
2.22e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 133.09 E-value: 2.22e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 69 DLHMNAMRVASYMRNMGLGQTDIVGVMGRHTTHQSAVAYACFFNGT---PLHALHNAYEEACIAklfGITKPRLIFCDgD 145
Cdd:PRK06145 32 EFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAvflPINYRLAADEVAYIL---GDAGAKLLLVD-E 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 146 EYEkvksATKDLQVTIVTMRNHPRGSVRI--QDVLTTPVMQNFQPlrlkdgiDHTLAILSSSGTSGFPKAVTIS--NSHK 221
Cdd:PRK06145 108 EFD----AIVALETPKIVIDAAAQADSRRlaQGGLEIPPQAAVAP-------TDLVRLMYTSGTTDRPKGVMHSygNLHW 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 222 IIVDYMA---INNSNIQYTSSTLDWCSGLSMAITSGVFSTTSIIADCDFDPGLFCRAIGKYRISMVLLSSSYLAIFANCP 298
Cdd:PRK06145 177 KSIDHVIalgLTASERLLVVGPLYHVGAFDLPGIAVLWVGGTLRIHREFDPEAVLAAIERHRLTCAWMAPVMLSRVLTVP 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 299 EFESADLSSLNYVIFGGSSCSLEVQRKVRSRLSHDCLNFCYGLTELNSAGSVNLNFDE--KPNSVGRAIRGIKIKVIDEQ 376
Cdd:PRK06145 257 DRDRFDLDSLAWCIGGGEKTPESRIRDFTRVFTRARYIDAYGLTETCSGDTLMEAGREieKIGSTGRALAHVEIRIADGA 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 377 GEAQEPNVVGEICFHNSQKWAGYYKNPDET-RQIQDseNWIHTGDLGYVDKDGYLFVIDRLKDML--KYQNIMyyPSEIE 453
Cdd:PRK06145 337 GRWLPPNMKGEICMRGPKVTKGYWKDPEKTaEAFYG--DWFRSGDVGYLDEEGFLYLTDRKKDMIisGGENIA--SSEVE 412
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 281365686 454 NVIAEMPNVLEACVFGIWDPVNGDEAAASLVKKPGTQLEAQDVVEYVRKRItAKFK 509
Cdd:PRK06145 413 RVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPGATLTLEALDRHCRQRL-ASFK 467
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
14-539 |
1.18e-32 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 131.64 E-value: 1.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 14 MCTYDDKlKIWSGREAPSLFSPNLSIGEIIFGDMVNNPKLIAQISITEDIVLTREDLHMNAMRVASYMRNMGLGQTDIVG 93
Cdd:PLN02330 6 QKQEDNE-HIFRSRYPSVPVPDKLTLPDFVLQDAELYADKVAFVEAVTGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 94 VMGRHTTHQSAVAYACFFNGTPLHALHNAYEEACIAKLFGITKPRLIFCDGDEYEKVKSatkdLQVTIVTMrnhprGSVR 173
Cdd:PLN02330 85 VVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTNDTNYGKVKG----LGLPVIVL-----GEEK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 174 IQDVLttpvmqNFQPL-----RLKDGIDHTL-------AILSSSGTSGFPKAVTISnsHKIIVDYMAinNSNIQYTSSTL 241
Cdd:PLN02330 156 IEGAV------NWKELleaadRAGDTSDNEEilqtdlcALPFSSGTTGISKGVMLT--HRNLVANLC--SSLFSVGPEMI 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 242 DWCSGLSM-------AITSGVFSTT----SIIADCDFDPGLFCRAIGKYRISMVLLSSSYLAIFANCPEFESADLSSLNY 310
Cdd:PLN02330 226 GQVVTLGLipffhiyGITGICCATLrnkgKVVVMSRFELRTFLNALITQEVSFAPIVPPIILNLVKNPIVEEFDLSKLKL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 311 --VIFGGSSCSLEVQRKVRSRLSHDCLNFCYGLTELNSAGSVNLNFDE-----KPNSVGRAIRGIKIKVID-EQGEAQEP 382
Cdd:PLN02330 306 qaIMTAAAPLAPELLTAFEAKFPGVQVQEAYGLTEHSCITLTHGDPEKghgiaKKNSVGFILPNLEVKFIDpDTGRSLPK 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 383 NVVGEICFHNSQKWAGYYKNPDETRQIQDSENWIHTGDLGYVDKDGYLFVIDRLKDMLKYQNIMYYPSEIENVIAEMPNV 462
Cdd:PLN02330 386 NTPGELCVRSQCVMQGYYNNKEETDRTIDEDGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSV 465
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281365686 463 LEACVFGIWDPVNGDEAAASLVKKPGTQLEAQDVVEYVRKRItAKFKQLNgGALIVDQIVRSGNRKTNRSAVKEHFL 539
Cdd:PLN02330 466 EDAAVVPLPDEEAGEIPAACVVINPKAKESEEDILNFVAANV-AHYKKVR-VVQFVDSIPKSLSGKIMRRLLKEKML 540
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
199-509 |
1.59e-32 |
|
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: 127.39 E-value: 1.59e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 199 LAILSSSGTSGFPKAVTISNSHKIIVDY-----MAINNSNIQYTSSTLDWCSGLSMAITSGVFSTTSIIADcDFDPGLFC 273
Cdd:cd17637 3 FVIIHTAAVAGRPRGAVLSHGNLIAANLqlihaMGLTEADVYLNMLPLFHIAGLNLALATFHAGGANVVME-KFDPAEAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 274 RAIGKYRISMVLLSSSYLAIFANCPEFESADLSSLNYViFGgsscsLEVQRKVRSRLSHDCLNF--CYGLTElnSAGSVN 351
Cdd:cd17637 82 ELIEEEKVTLMGSFPPILSNLLDAAEKSGVDLSSLRHV-LG-----LDAPETIQRFEETTGATFwsLYGQTE--TSGLVT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 352 LN-FDEKPNSVGRAIRGIKIKVIDEQGEAQEPNVVGEICFHNSQKWAGYYKNPDETRQIQDsENWIHTGDLGYVDKDGYL 430
Cdd:cd17637 154 LSpYRERPGSAGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTFR-NGWHHTGDLGRFDEDGYL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 431 FVIDRL--KDMLKY--QNImyYPSEIENVIAEMPNVLEACVFGIWDPVNGDEAAASLVKKPGTQLEAQDVVEYVRKRItA 506
Cdd:cd17637 233 WYAGRKpeKELIKPggENV--YPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKPGATLTADELIEFVGSRI-A 309
|
...
gi 281365686 507 KFK 509
Cdd:cd17637 310 RYK 312
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
200-536 |
1.60e-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: 129.72 E-value: 1.60e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 200 AILSSSGTSGFPKAVTISnsHKIIvdymainNSNIQYTSSTLDWCS--------------GLSMAITSGVFSTTSIIADC 265
Cdd:cd05941 93 LILYTSGTTGRPKGVVLT--HANL-------AANVRALVDAWRWTEddvllhvlplhhvhGLVNALLCPLFAGASVEFLP 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 266 DFDPGLFCRAIGKYRISMVL--------LSSSYLAIFANCPEFESADLSSLNYVIFGGSSCSLEVQRKVRSRLSHDCLNF 337
Cdd:cd05941 164 KFDPKEVAISRLMPSITVFMgvptiytrLLQYYEAHFTDPQFARAAAAERLRLMVSGSAALPVPTLEEWEAITGHTLLER 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 338 cYGLTELNSAGSVNLNFDEKPNSVGRAIRGIKIKVIDEQ-GEAQEPNVVGEICFHNSQKWAGYYKNPDETRQIQDSENWI 416
Cdd:cd05941 244 -YGMTEIGMALSNPLDGERRPGTVGMPLPGVQARIVDEEtGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGWF 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 417 HTGDLGYVDKDGYLFVIDRLKDML-KYQNIMYYPSEIENVIAEMPNVLEACVFGIWDPVNGDEAAASLVKKPG-TQLEAQ 494
Cdd:cd05941 323 KTGDLGVVDEDGYYWILGRSSVDIiKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGaAALSLE 402
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 281365686 495 DVVEYVRKRItAKFKQlNGGALIVDQIVRSGNRKTNRSAVKE 536
Cdd:cd05941 403 ELKEWAKQRL-APYKR-PRRLILVDELPRNAMGKVNKKELRK 442
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
269-505 |
6.01e-32 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 129.76 E-value: 6.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 269 PGlFCRAIGKYRISMV-LLSSSYLAIFaNCPEFESADLSSLNYVIFGGsscsLEVQRKVRSRLSHdcLNFC-----YGLT 342
Cdd:PRK07059 291 PG-FIKELKKYQVHIFpAVNTLYNALL-NNPDFDKLDFSKLIVANGGG----MAVQRPVAERWLE--MTGCpitegYGLS 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 343 ELNSAGSVN-LNFDEKPNSVGRAIRGIKIKVIDEQGEAQEPNVVGEICFHNSQKWAGYYKNPDETRQIQDSENWIHTGDL 421
Cdd:PRK07059 363 ETSPVATCNpVDATEFSGTIGLPLPSTEVSIRDDDGNDLPLGEPGEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDV 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 422 GYVDKDGYLFVIDRLKDMLKYQNIMYYPSEIENVIAEMPNVLEACVFGIWDPVNGDEAAASLVKK-PGtqLEAQDVVEYV 500
Cdd:PRK07059 443 GVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGEAVKLFVVKKdPA--LTEEDVKAFC 520
|
....*
gi 281365686 501 RKRIT 505
Cdd:PRK07059 521 KERLT 525
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
69-536 |
1.41e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 128.24 E-value: 1.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 69 DLHMNAMRVAsyMRNMGLGQTDIVGVMGRHTTHQSAVAYACF----------FNGTPlhalhnayEEacIAKLFGITKPR 138
Cdd:PRK07470 39 DARVDALAAA--LAARGVRKGDRILVHSRNCNQMFESMFAAFrlgavwvptnFRQTP--------DE--VAYLAEASGAR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 139 LIFCDGD--EY-EKVKSATKDLQVTIVTmrNHPRGSVRIQDVLTTPVMQNFQPLRLKDgiDHTLAILSSSGTSGFPKAVT 215
Cdd:PRK07470 107 AMICHADfpEHaAAVRAASPDLTHVVAI--GGARAGLDYEALVARHLGARVANAAVDH--DDPCWFFFTSGTTGRPKAAV 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 216 ISNSHkiivdyMA--INNSNIQYTSSTLDWCSGLSMAITS---GVF--------STTSIIADCDFDPGLFCRAIGKYRIS 282
Cdd:PRK07470 183 LTHGQ------MAfvITNHLADLMPGTTEQDASLVVAPLShgaGIHqlcqvargAATVLLPSERFDPAEVWALVERHRVT 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 283 MVLLSSSYLAIFANCPEFESADLSSLNYVIFGGSSCSLEVQRKVRSRLSHDCLNFcYGLTELNSAGSV---NLNF-DEKP 358
Cdd:PRK07470 257 NLFTVPTILKMLVEHPAVDRYDHSSLRYVIYAGAPMYRADQKRALAKLGKVLVQY-FGLGEVTGNITVlppALHDaEDGP 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 359 N----SVGRAIRGIKIKVIDEQGEAQEPNVVGEICFHNSQKWAGYYKNPDETRQ-IQDSenWIHTGDLGYVDKDGYLFVI 433
Cdd:PRK07470 336 DarigTCGFERTGMEVQIQDDEGRELPPGETGEICVIGPAVFAGYYNNPEANAKaFRDG--WFRTGDLGHLDARGFLYIT 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 434 DRLKDMlkY----QNImyYPSEIENVIAEMPNVLEACVFGIWDPVNGDEAAASLVKKPGTQLEAQDVVEYVRKRItAKFK 509
Cdd:PRK07470 414 GRASDM--YisggSNV--YPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVARDGAPVDEAELLAWLDGKV-ARYK 488
|
490 500
....*....|....*....|....*..
gi 281365686 510 qLNGGALIVDQIVRSGNRKTNRSAVKE 536
Cdd:PRK07470 489 -LPKRFFFWDALPKSGYGKITKKMVRE 514
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
200-536 |
2.37e-31 |
|
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: 126.72 E-value: 2.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 200 AILSSSGTSGFPKAVTISNSHKIIVD---YMAINNSNIQYTSSTLdwCSG-LSMAITSGVFST------TSIIADcDFDP 269
Cdd:cd05929 129 KMLYSGGTTGRPKGIKRGLPGGPPDNdtlMAAALGFGPGADSVYL--SPApLYHAAPFRWSMTalfmggTLVLME-KFDP 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 270 GLFCRAIGKYRISMVLLSSSYLAIFANCPEFESA--DLSSLNYVIFGGSSCSLEVQRKVRSRLSHDCLNFcYGLTELNsa 347
Cdd:cd05929 206 EEFLRLIERYRVTFAQFVPTMFVRLLKLPEAVRNayDLSSLKRVIHAAAPCPPWVKEQWIDWGGPIIWEY-YGGTEGQ-- 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 348 GSVNLNFDE---KPNSVGRAIRGiKIKVIDEQGEAQEPNVVGEICFHNSQKWAgYYKNPDETRQIQDSENWIHTGDLGYV 424
Cdd:cd05929 283 GLTIINGEEwltHPGSVGRAVLG-KVHILDEDGNEVPPGEIGEVYFANGPGFE-YTNDPEKTAAARNEGGWSTLGDVGYL 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 425 DKDGYLFVIDRLKDMLKYQNIMYYPSEIENVIAEMPNVLEACVFGIWDPVNGDEAAASLVKKPGT---QLEAQDVVEYVR 501
Cdd:cd05929 361 DEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVQPAPGAdagTALAEELIAFLR 440
|
330 340 350
....*....|....*....|....*....|....*
gi 281365686 502 KRITAkFKQLNGGAlIVDQIVRSGNRKTNRSAVKE 536
Cdd:cd05929 441 DRLSR-YKCPRSIE-FVAELPRDDTGKLYRRLLRD 473
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
76-536 |
2.77e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 126.85 E-value: 2.77e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 76 RVASYMRNMGLGQTDIVGVMGRHTTHQSAVAYACFFNG---TPLHALHNAYEeacIAKLFGITKPRLIFCDgDEYEKVKS 152
Cdd:PRK09088 34 RLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGaiyVPLNWRLSASE---LDALLQDAEPRLLLGD-DAVAAGRT 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 153 ATKDLQVTIvtmrnhprGSVRIQDVLTTPVMQNfqplrlkdgiDHTLAILSSSGTSGFPKAVTISNSHkiiVDYMAINNS 232
Cdd:PRK09088 110 DVEDLAAFI--------ASADALEPADTPSIPP----------ERVSLILFTSGTSGQPKGVMLSERN---LQQTAHNFG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 233 ---NIQYTSSTLdwCS-------GLSMAITSGVFSTTSIIADCDFDPGlfcRAIGkyRISMVLLSSSY-------LAIFA 295
Cdd:PRK09088 169 vlgRVDAHSSFL--CDapmfhiiGLITSVRPVLAVGGSILVSNGFEPK---RTLG--RLGDPALGITHyfcvpqmAQAFR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 296 NCPEFESADLSSLNYVIFGGSSCSLEvqrKVRSRLSHDCLNFC-YGLTELNSAGSVNLN---FDEKPNSVGRAIRGIKIK 371
Cdd:PRK09088 242 AQPGFDAAALRHLTALFTGGAPHAAE---DILGWLDDGIPMVDgFGMSEAGTVFGMSVDcdvIRAKAGAAGIPTPTVQTR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 372 VIDEQGEAQEPNVVGEICFHNSQKWAGYYKNPDETRQIQDSENWIHTGDLGYVDKDGYLFVIDRLKDMLKYQNIMYYPSE 451
Cdd:PRK09088 319 VVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFTGDGWFRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 452 IENVIAEMPNVLEACVFGIWDPVNGDEAAASLVKKPGTQLEAQDVVEYVRKRItAKFKqLNGGALIVDQIVRSGNRKTNR 531
Cdd:PRK09088 399 IEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADGAPLDLERIRSHLSTRL-AKYK-VPKHLRLVDALPRTASGKLQK 476
|
....*
gi 281365686 532 SAVKE 536
Cdd:PRK09088 477 ARLRD 481
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
73-535 |
5.60e-31 |
|
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: 125.63 E-value: 5.60e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 73 NAMRVASYMRNMGLGQTD--IVGVMGRHTTHQS--AVAYACFFNGTPLHALHNAYEEACIAKLFGITKPRLIFCD---GD 145
Cdd:cd05922 2 GVSAAASALLEAGGVRGErvVLILPNRFTYIELsfAVAYAGGRLGLVFVPLNPTLKESVLRYLVADAGGRIVLADagaAD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 146 EYEKVKSATKDLQVTI----VTMRNHPRGSVRIQDvlttpvmqnfqplrlkdgiDHTLAILSSSGTSGFPKAVTISNSH- 220
Cdd:cd05922 82 RLRDALPASPDPGTVLdadgIRAARASAPAHEVSH-------------------EDLALLLYTSGSTGSPKLVRLSHQNl 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 221 ----KIIVDYMAINNSNIQYTSSTLDWCSGLSMAITSGVFSTTSIIADcDFDPGL-FCRAIGKYRISMVLLSSSYLAIFA 295
Cdd:cd05922 143 lanaRSIAEYLGITADDRALTVLPLSYDYGLSVLNTHLLRGATLVLTN-DGVLDDaFWEDLREHGATGLAGVPSTYAMLT 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 296 NCpEFESADLSSLNYVIFGGSSCSLEVQRKVRSRLSHDCLNFCYGLTELnSAGSVNL---NFDEKPNSVGRAIRGIKIKV 372
Cdd:cd05922 222 RL-GFDPAKLPSLRYLTQAGGRLPQETIARLRELLPGAQVYVMYGQTEA-TRRMTYLppeRILEKPGSIGLAIPGGEFEI 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 373 IDEQGEAQEPNVVGEICFHNSQKWAGYYKNPDETRQIQDSENWIHTGDLGYVDKDGYLFVIDRLKDMLKYQNIMYYPSEI 452
Cdd:cd05922 300 LDDDGTPTPPGEPGEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEI 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 453 ENVIAEMPNVLEACVFGIWDPVnGDEAAASLVKKPGtqLEAQDVVEYVRKRITAkfkQLNGGAL-IVDQIVRSGNRKTNR 531
Cdd:cd05922 380 EAAARSIGLIIEAAAVGLPDPL-GEKLALFVTAPDK--IDPKDVLRSLAERLPP---YKVPATVrVVDELPLTASGKVDY 453
|
....
gi 281365686 532 SAVK 535
Cdd:cd05922 454 AALR 457
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
185-509 |
2.50e-30 |
|
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.
Pssm-ID: 341238 [Multi-domain] Cd Length: 411 Bit Score: 122.84 E-value: 2.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 185 NFQPLRLKDGIDHTLAILSSSGTSGFPKAVTIS-NSHKiivdYMAINNS-NIQYTSSTlDW--------CSGLSMAITSG 254
Cdd:cd05912 66 AFQLKDSDVKLDDIATIMYTSGTTGKPKGVQQTfGNHW----WSAIGSAlNLGLTEDD-NWlcalplfhISGLSILMRSV 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 255 VFSTTSIIADcDFDPGLFCRAIGKYRISMVLLSSSYLA-IFANCPEFESadlSSLNYVIFGGSSCSLEVQRKVRSRlshd 333
Cdd:cd05912 141 IYGMTVYLVD-KFDAEQVLHLINSGKVTIISVVPTMLQrLLEILGEGYP---NNLRCILLGGGPAPKPLLEQCKEK---- 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 334 clNF----CYGLTELNSAgSVNLNFDE---KPNSVGRAIRGIKIKVIDEQgeaQEPNVVGEICFHNSQKWAGYYKNPDET 406
Cdd:cd05912 213 --GIpvyqSYGMTETCSQ-IVTLSPEDalnKIGSAGKPLFPVELKIEDDG---QPPYEVGEILLKGPNVTKGYLNRPDAT 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 407 RQ-IQDseNWIHTGDLGYVDKDGYLFVIDRLKDMLKY--QNImyYPSEIENVIAEMPNVLEACVFGIWDPVNGDEAAASL 483
Cdd:cd05912 287 EEsFEN--GWFKTGDIGYLDEEGFLYVLDRRSDLIISggENI--YPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFV 362
|
330 340
....*....|....*....|....*..
gi 281365686 484 V-KKPGTQLEAQDvveYVRKRItAKFK 509
Cdd:cd05912 363 VsERPISEEELIA---YCSEKL-AKYK 385
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
64-509 |
3.00e-30 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 124.03 E-value: 3.00e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 64 VLTREDLHMNAMRVASYMRNMGLGQTDIVGVMGRHTTHQSAVAYACFFNG---TPLHALHNAYEEACIAKLFGitkPRLI 140
Cdd:PRK13391 24 VVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGlyyTCVNSHLTPAEAAYIVDDSG---ARAL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 141 FCDGDEYEKVKSATKDL-QVTIVTMRNHPRGSVRIQDVltTPVMQNFQPLRLKDGIDHTlAILSSSGTSGFPKAVTISNS 219
Cdd:PRK13391 101 ITSAAKLDVARALLKQCpGVRHRLVLDGDGELEGFVGY--AEAVAGLPATPIADESLGT-DMLYSSGTTGRPKGIKRPLP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 220 HKIIVD---YMAINNSNIQYTSSTLDWC---------SGLSMAITSgvFSTTSIIADcDFDPGLFCRAIGKYRISMVLLS 287
Cdd:PRK13391 178 EQPPDTplpLTAFLQRLWGFRSDMVYLSpaplyhsapQRAVMLVIR--LGGTVIVME-HFDAEQYLALIEEYGVTHTQLV 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 288 SSYLAIFANCPE--FESADLSSLNYVIFGGSSCSLEVQRKVRSRLS---HDClnfcYGLTELNSAGSVNL-NFDEKPNSV 361
Cdd:PRK13391 255 PTMFSRMLKLPEevRDKYDLSSLEVAIHAAAPCPPQVKEQMIDWWGpiiHEY----YAATEGLGFTACDSeEWLAHPGTV 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 362 GRAIRGiKIKVIDEQGEAQEPNVVGEICFHNSQKWAgYYKNPDETRQIQDSE-NWIHTGDLGYVDKDGYLFVIDRLKDML 440
Cdd:PRK13391 331 GRAMFG-DLHILDDDGAELPPGEPGTIWFEGGRPFE-YLNDPAKTAEARHPDgTWSTVGDIGYVDEDGYLYLTDRAAFMI 408
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281365686 441 KYQNIMYYPSEIENVIAEMPNVLEACVFGIWDPVNGDEAAASLVKKPGTQLE---AQDVVEYVRKRItAKFK 509
Cdd:PRK13391 409 ISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPVDGVDPGpalAAELIAFCRQRL-SRQK 479
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
59-533 |
1.02e-29 |
|
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: 121.48 E-value: 1.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 59 ITEDIVLTREDLHMNAMRVASYMRNMGLGQTDIVGVMgRHTTHQSAVAY-------ACFfngTPLHAlhnAYEEACIAKL 131
Cdd:cd05930 7 VDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVL-LERSLEMVVAIlavlkagAAY---VPLDP---SYPAERLAYI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 132 FGITKPRLifcdgdeyekvksatkdlqvtivtmrnhprgsvriqdVLTTPvmqnfqplrlkdgiDHTLAILSSSGTSGFP 211
Cdd:cd05930 80 LEDSGAKL-------------------------------------VLTDP--------------DDLAYVIYTSGSTGKP 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 212 KAVTISnsHKIIVDYMAINNSNI---------QYTSSTLDwcsgLS-----MAITSGVfstTSIIAD--CDFDPGLFCRA 275
Cdd:cd05930 109 KGVMVE--HRGLVNLLLWMQEAYpltpgdrvlQFTSFSFD----VSvweifGALLAGA---TLVVLPeeVRKDPEALADL 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 276 IGKYRISMVLLSSSYLAIFANCPEFesADLSSLNYVIFGGSSCSLEVQRKVRSRLSHDCLNFCYGLTElNSAGSV----- 350
Cdd:cd05930 180 LAEEGITVLHLTPSLLRLLLQELEL--AALPSLRLVLVGGEALPPDLVRRWRELLPGARLVNLYGPTE-ATVDATyyrvp 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 351 NLNFDEKPNSVGRAIRGIKIKVIDEQGEAQEPNVVGEICFHNSQKWAGYYKNPDETRQ--IQDSEN-WI---HTGDLGYV 424
Cdd:cd05930 257 PDDEEDGRVPIGRPIPNTRVYVLDENLRPVPPGVPGELYIGGAGLARGYLNRPELTAErfVPNPFGpGErmyRTGDLVRW 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 425 DKDGYLFVIDRLKDMLKyqnIMYY---PSEIENVIAEMPNVLEACVFGIWDPVNGDEAAASLVKKPGTQLEAQDVVEYVR 501
Cdd:cd05930 337 LPDGNLEFLGRIDDQVK---IRGYrieLGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEGGELDEEELRAHLA 413
|
490 500 510
....*....|....*....|....*....|....*..
gi 281365686 502 KR-----ITAKFKQLnggalivDQIVRSGNRKTNRSA 533
Cdd:cd05930 414 ERlpdymVPSAFVVL-------DALPLTPNGKVDRKA 443
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
198-504 |
4.63e-29 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 121.02 E-value: 4.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 198 TLAILSSSGTSGFPKAVTISNSHKII-----VDYMAINNSNIQYTSSTLDWCSGLSMAITSGVFSTTSIIADcDFDPGLF 272
Cdd:PRK06155 182 TAAILYTSGTTGPSKGVCCPHAQFYWwgrnsAEDLEIGADDVLYTTLPLFHTNALNAFFQALLAGATYVLEP-RFSASGF 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 273 CRAIGKYRISMVLLSSSYLAIFANCPEFESADLSSLNYVIFGGSSCSLevQRKVRSRLSHDCLNfCYGLTELNSAGSVNL 352
Cdd:PRK06155 261 WPAVRRHGATVTYLLGAMVSILLSQPARESDRAHRVRVALGPGVPAAL--HAAFRERFGVDLLD-GYGSTETNFVIAVTH 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 353 NfDEKPNSVGRAIRGIKIKVIDEQGEAQEPNVVGEICFHNSQKWA---GYYKNPDETrqIQDSEN-WIHTGDLGYVDKDG 428
Cdd:PRK06155 338 G-SQRPGSMGRLAPGFEARVVDEHDQELPDGEPGELLLRADEPFAfatGYFGMPEKT--VEAWRNlWFHTGDRVVRDADG 414
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281365686 429 YLFVIDRLKDMLKY--QNIMYYpsEIENVIAEMPNVLEACVFGIWDPVNGDEAAASLVKKPGTQLEAQDVVEYVRKRI 504
Cdd:PRK06155 415 WFRFVDRIKDAIRRrgENISSF--EVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDGTALEPVALVRHCEPRL 490
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
204-509 |
5.23e-29 |
|
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: 117.12 E-value: 5.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 204 SSGTSGFPKAVTISN-----SHKIIVDYMAINNSNIQYTSSTLDWcSGLSMAITSGVFSTTSIIADCDFDPGLFCRAIGK 278
Cdd:cd17633 8 TSGTTGLPKAYYRSErswieSFVCNEDLFNISGEDAILAPGPLSH-SLFLYGAISALYLGGTFIGQRKFNPKSWIRKINQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 279 YRISMVLLSSSYLAIFANCPEFESADLSslnyvIF-GGSSCSLEVQRKVRSRLSHDCLNFCYGLTELNSagsVNLNFDE- 356
Cdd:cd17633 87 YNATVIYLVPTMLQALARTLEPESKIKS-----IFsSGQKLFESTKKKLKNIFPKANLIEFYGTSELSF---ITYNFNQe 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 357 --KPNSVGRAIRGIKIKVideqgEAQEPNVVGEICFHNSQKWAGYYK----NPDEtrqiqdsenWIHTGDLGYVDKDGYL 430
Cdd:cd17633 159 srPPNSVGRPFPNVEIEI-----RNADGGEIGKIFVKSEMVFSGYVRggfsNPDG---------WMSVGDIGYVDEEGYL 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281365686 431 FVIDRLKDMLKYQNIMYYPSEIENVIAEMPNVLEACVFGIWDPVNGdEAAASLVKkpGTQLEAQDVVEYVRKRItAKFK 509
Cdd:cd17633 225 YLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFG-EIAVALYS--GDKLTYKQLKRFLKQKL-SRYE 299
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
74-540 |
7.49e-29 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 120.24 E-value: 7.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 74 AMRVASYMRNMGLGQTDIVGVMGRHTTHQSAVAYACFFNGTPLHALHNAYEEACIAKLFGITKPRLIFCDgdEYEKvKSA 153
Cdd:PRK06087 59 ASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFAP--TLFK-QTR 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 154 TKDLQVTIVTMRNHPRGSVRIQDV---LTTP----VMQNFQPLRLKDGI--DHTLAILSSSGTSGFPKAVTISN-----S 219
Cdd:PRK06087 136 PVDLILPLQNQLPQLQQIVGVDKLapaTSSLslsqIIADYEPLTTAITThgDELAAVLFTSGTEGLPKGVMLTHnnilaS 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 220 HKIIVDYMAINNSNIQYTSSTLDWCSGLSMAITSGVFSTTSIIADCDFDPGLFCRAIGKYRISMVLLSSSYLAIFANCPE 299
Cdd:PRK06087 216 ERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVLLDIFTPDACLALLEQQRCTCMLGATPFIYDLLNLLE 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 300 FESADLSSLNYVIFGGSScslevqrkVRSRLSHDCLNF------CYGLTELNSAGSVNLnfdEKP-----NSVGRAIRGI 368
Cdd:PRK06087 296 KQPADLSALRFFLCGGTT--------IPKKVARECQQRgikllsVYGSTESSPHAVVNL---DDPlsrfmHTDGYAAAGV 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 369 KIKVIDEQGEAQEPNVVGEICFHNSQKWAGYYKNPDETRQIQDSENWIHTGDLGYVDKDGYLFVIDRLKDMLKY--QNIM 446
Cdd:PRK06087 365 EIKVVDEARKTLPPGCEGEEASRGPNVFMGYLDEPELTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRggENIS 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 447 yyPSEIENVIAEMPNVLEACVFGIWDPVNGDEAAASLVKKPGTQ-LEAQDVVEYVRKRITAKFKQLNGGALIvDQIVRSG 525
Cdd:PRK06087 445 --SREVEDILLQHPKIHDACVVAMPDERLGERSCAYVVLKAPHHsLTLEEVVAFFSRKRVAKYKYPEHIVVI-DKLPRTA 521
|
490
....*....|....*
gi 281365686 526 NRKTNRSAVKEHFLK 540
Cdd:PRK06087 522 SGKIQKFLLRKDIMR 536
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
200-521 |
7.67e-29 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.
Pssm-ID: 341284 [Multi-domain] Cd Length: 518 Bit Score: 120.04 E-value: 7.67e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 200 AILSSSGTSGFPKAVTISnsH-KIIVDYMAINNSNIQYTSStldwcSGLSMAITS-------GV-FSTTSIIADC----- 265
Cdd:cd12119 167 AICYTSGTTGNPKGVVYS--HrSLVLHAMAALLTDGLGLSE-----SDVVLPVVPmfhvnawGLpYAAAMVGAKLvlpgp 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 266 DFDPGLFCRAIGKYRISMVLLSSSYLAIFANCPEFESADLSSLNYVIFGGSSCSLEVQRKVRSRLshdcLNFC--YGLTE 343
Cdd:cd12119 240 YLDPASLAELIEREGVTFAAGVPTVWQGLLDHLEANGRDLSSLRRVVIGGSAVPRSLIEAFEERG----VRVIhaWGMTE 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 344 LNSAGSV--------NLNFDEKPN---SVGRAIRGIKIKVIDEQGEAQE--PNVVGEICFhnSQKW--AGYYKNPDETRQ 408
Cdd:cd12119 316 TSPLGTVarppsehsNLSEDEQLAlraKQGRPVPGVELRIVDDDGRELPwdGKAVGELQV--RGPWvtKSYYKNDEESEA 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 409 IqDSENWIHTGDLGYVDKDGYLFVIDRLKDMLKYQNIMYYPSEIENVIAEMPNVLEACVFGIWDPVNGDEAAASLVKKPG 488
Cdd:cd12119 394 L-TEDGWLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLKEG 472
|
330 340 350
....*....|....*....|....*....|...
gi 281365686 489 TQLEAQDVVEYVRKRItAKFkQLNGGALIVDQI 521
Cdd:cd12119 473 ATVTAEELLEFLADKV-AKW-WLPDDVVFVDEI 503
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
339-469 |
7.89e-29 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 120.59 E-value: 7.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 339 YGLTELNSAGSVNLNFDEKPNSVGRAIRGIKIKvIDEQGE--AQEPNVvgeicFhnsqkwAGYYKNPDETRQIQDSENWI 416
Cdd:COG1022 378 YGLTETSPVITVNRPGDNRIGTVGPPLPGVEVK-IAEDGEilVRGPNV-----M------KGYYKNPEATAEAFDADGWL 445
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 281365686 417 HTGDLGYVDKDGYLFVIDRLKDML-----KYqnimYYPSEIENVIAEMPNVLEACVFG 469
Cdd:COG1022 446 HTGDIGELDEDGFLRITGRKKDLIvtsggKN----VAPQPIENALKASPLIEQAVVVG 499
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
59-509 |
1.07e-28 |
|
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: 119.33 E-value: 1.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 59 ITEDIVLTREDLHMNAMRVASYMRNMGLGQTDIVGVMGRHTthqsAVAYACFFnGTP-----LHALHNAYEEACIAKLFG 133
Cdd:cd12118 24 VYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNT----PAMYELHF-GVPmagavLNALNTRLDAEEIAFILR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 134 ITKPRLIFCDGD-EYEKVKSATKDlqvtivtmrnhprgsvriqdvlttpvmqNFQPLRLKDGIDhTLAILSSSGTSGFPK 212
Cdd:cd12118 99 HSEAKVLFVDREfEYEDLLAEGDP----------------------------DFEWIPPADEWD-PIALNYTSGTTGRPK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 213 AVTISnsHKIIvdY-MAInnSNIQYTSS--------TLD------WCSGLSMAITSGvfstTSIIADcDFDPGLFCRAIG 277
Cdd:cd12118 150 GVVYH--HRGA--YlNAL--ANILEWEMkqhpvylwTLPmfhcngWCFPWTVAAVGG----TNVCLR-KVDAKAIYDLIE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 278 KYRISMVLLSSSYLAIFANCPEFESADLSSLNYVIFGGSSCSLEVQRKVRSrlshdcLNFC----YGLTELNSAGSVNL- 352
Cdd:cd12118 219 KHKVTHFCGAPTVLNMLANAPPSDARPLPHRVHVMTAGAPPPAAVLAKMEE------LGFDvthvYGLTETYGPATVCAw 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 353 --NFDEKP---NSVGRAIRGIK------IKVIDEQGEAQEP---NVVGEICFHNSQKWAGYYKNPDETRQ-IQDSenWIH 417
Cdd:cd12118 293 kpEWDELPteeRARLKARQGVRyvgleeVDVLDPETMKPVPrdgKTIGEIVFRGNIVMKGYLKNPEATAEaFRGG--WFH 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 418 TGDLGYVDKDGYLFVIDRLKDML--KYQNImyypS--EIENVIAEMPNVLEACVFGIWDPVNGDEAAASLVKKPGTQLEA 493
Cdd:cd12118 371 SGDLAVIHPDGYIEIKDRSKDIIisGGENI----SsvEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVELKEGAKVTE 446
|
490
....*....|....*.
gi 281365686 494 QDVVEYVRKRItAKFK 509
Cdd:cd12118 447 EEIIAFCREHL-AGFM 461
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
296-505 |
1.76e-28 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 119.39 E-value: 1.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 296 NCPEFESADLSSLNYVIFGGSScsleVQRKVRSR---LSHDCLNFCYGLTE---LNSAGSVNLnfDEKPNSVGRAIRGIK 369
Cdd:PRK08974 315 NNEEFQELDFSSLKLSVGGGMA----VQQAVAERwvkLTGQYLLEGYGLTEcspLVSVNPYDL--DYYSGSIGLPVPSTE 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 370 IKVIDEQGEAQEPNVVGEICFHNSQKWAGYYKNPDETRQIQdSENWIHTGDLGYVDKDGYLFVIDRLKDMLKYQNIMYYP 449
Cdd:PRK08974 389 IKLVDDDGNEVPPGEPGELWVKGPQVMLGYWQRPEATDEVI-KDGWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYP 467
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 281365686 450 SEIENVIAEMPNVLEACVFGIWDPVNGDEAAASLVKKPGTqLEAQDVVEYVRKRIT 505
Cdd:PRK08974 468 NEIEDVVMLHPKVLEVAAVGVPSEVSGEAVKIFVVKKDPS-LTEEELITHCRRHLT 522
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
198-485 |
4.26e-28 |
|
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: 115.05 E-value: 4.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 198 TLAILSSSGTSGFPKAVTISN------SHKIIVDYMAINNSNIQYTSSTLDWCSGLSMAITSgVFSTTSIIADCDF-DPG 270
Cdd:cd17635 3 PLAVIFTSGTTGEPKAVLLANktffavPDILQKEGLNWVVGDVTYLPLPATHIGGLWWILTC-LIHGGLCVTGGENtTYK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 271 LFCRAIGKYRISMVLLSSSYLAIFANCPEFESADLSSLNYVIFGGSscsLEVQRKVRSRLSHDCLNFC--YGLTELNSAG 348
Cdd:cd17635 82 SLFKILTTNAVTTTCLVPTLLSKLVSELKSANATVPSLRLIGYGGS---RAIAADVRFIEATGLTNTAqvYGLSETGTAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 349 SVNLNFDEKP-NSVGRAIRGIKIKVIDEQGEAQEPNVVGEICFHNSQKWAGYYKNPDETRQIQdSENWIHTGDLGYVDKD 427
Cdd:cd17635 159 CLPTDDDSIEiNAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLGERRED 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 281365686 428 GYLFVIDRLKDMLKYQNIMYYPSEIENVIAEMPNVLEACVFGIWDPVNGDEAAASLVK 485
Cdd:cd17635 238 GFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVA 295
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
339-509 |
5.31e-28 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 116.99 E-value: 5.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 339 YGLTELNSAgSVNLNFD---EKPNSVGRAIRGIKIKvIDEQGEAQEPNVVGEICFHNSQKWAGYYKNPDETRQ-IQDseN 414
Cdd:PRK03640 285 YGMTETASQ-IVTLSPEdalTKLGSAGKPLFPCELK-IEKDGVVVPPFEEGEIVVKGPNVTKGYLNREDATREtFQD--G 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 415 WIHTGDLGYVDKDGYLFVIDRLKDMLKY--QNImyYPSEIENVIAEMPNVLEACVFGIWDPVNGDEAAASLVKkpGTQLE 492
Cdd:PRK03640 361 WFKTGDIGYLDEEGFLYVLDRRSDLIISggENI--YPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVK--SGEVT 436
|
170
....*....|....*..
gi 281365686 493 AQDVVEYVRKRItAKFK 509
Cdd:PRK03640 437 EEELRHFCEEKL-AKYK 452
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
202-509 |
8.60e-28 |
|
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.
Pssm-ID: 341269 [Multi-domain] Cd Length: 508 Bit Score: 116.70 E-value: 8.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 202 LSSSGTSGFPKAVTISNSHKIIV------DYMAINNSNIQYTSSTLDWCSGLSMAIT--SGVFSTTSIIADcDFDPGLFC 273
Cdd:cd05959 169 LYSSGSTGRPKGVVHLHADIYWTaelyarNVLGIREDDVCFSAAKLFFAYGLGNSLTfpLSVGATTVLMPE-RPTPAAVF 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 274 RAIGKYRISMVLLSSSYLAIFANCPEFESADLSSLNYVIFGGSSCSLEVQRKVRSRLSHDCLNfCYGLTEL------NSA 347
Cdd:cd05959 248 KRIRRYRPTVFFGVPTLYAAMLAAPNLPSRDLSSLRLCVSAGEALPAEVGERWKARFGLDILD-GIGSTEMlhiflsNRP 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 348 GSVnlnfdeKPNSVGRAIRGIKIKVIDEQGEAQEPNVVGEICFHNSQKWAGYYKNPDETRQIQDSEnWIHTGDLGYVDKD 427
Cdd:cd05959 327 GRV------RYGTTGKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQGE-WTRTGDKYVRDDD 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 428 GYLFVIDRLKDMLKYQNIMYYPSEIENVIAEMPNVLEACVFGIWDPVNGDEAAASLVKKPGTQ---LEAQDVVEYVRKRI 504
Cdd:cd05959 400 GFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPGYEdseALEEELKEFVKDRL 479
|
....*
gi 281365686 505 tAKFK 509
Cdd:cd05959 480 -APYK 483
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
201-488 |
1.08e-27 |
|
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: 115.68 E-value: 1.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 201 ILSSSGTSGFPKAVTisNSHKIIVDYMAINNSNIQYTSSTLDWCSGLSMAITSGVF--------STTSIIADCDFDPGLF 272
Cdd:cd05969 94 LHYTSGTTGTPKGVL--HVHDAMIFYYFTGKYVLDLHPDDIYWCTADPGWVTGTVYgiwapwlnGVTNVVYEGRFDAESW 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 273 CRAIGKYRIS----------MVLLSSSYLAifancpefESADLSSLNYVIFGGSSCSLEVQR---KVRSRLSHDClnfcY 339
Cdd:cd05969 172 YGIIERVKVTvwytaptairMLMKEGDELA--------RKYDLSSLRFIHSVGEPLNPEAIRwgmEVFGVPIHDT----W 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 340 GLTELNSAGSVN-LNFDEKPNSVGRAIRGIKIKVIDEQGEAQEPNVVGEIC------------FHNSQKWAGYYKNpdet 406
Cdd:cd05969 240 WQTETGSIMIANyPCMPIKPGSMGKPLPGVKAAVVDENGNELPPGTKGILAlkpgwpsmfrgiWNDEERYKNSFID---- 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 407 rqiqdseNWIHTGDLGYVDKDGYLFVIDRLKDMLKYQNIMYYPSEIENVIAEMPNVLEACVFGIWDPVNGDEAAASLVKK 486
Cdd:cd05969 316 -------GWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLK 388
|
..
gi 281365686 487 PG 488
Cdd:cd05969 389 EG 390
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
360-509 |
2.01e-27 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 115.94 E-value: 2.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 360 SVGRAIRGIKIKVIDEQGEAQEPNVVGEICFHN---SQKWAGYYKNPDETRQIQDSENWIHTGDLGYVDKDGYLFVIDRL 436
Cdd:PRK08008 341 SIGRPGFCYEAEIRDDHNRPLPAGEIGEICIKGvpgKTIFKEYYLDPKATAKVLEADGWLHTGDTGYVDEEGFFYFVDRR 420
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 281365686 437 KDMLKY--QNIMyyPSEIENVIAEMPNVLEACVFGIWDPVNgDEAA-ASLVKKPGTQLEAQDVVEYVRKRItAKFK 509
Cdd:PRK08008 421 CNMIKRggENVS--CVELENIIATHPKIQDIVVVGIKDSIR-DEAIkAFVVLNEGETLSEEEFFAFCEQNM-AKFK 492
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
65-481 |
6.24e-27 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 114.69 E-value: 6.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 65 LTREDLHMNAMRVASYMRNMGLGQTD-IVGVMGRHttHQSAVAY-ACFFNG---TPLHALHN-AYEEACIAKLFGI---- 134
Cdd:cd05906 40 QSYQDLLEDARRLAAGLRQLGLRPGDsVILQFDDN--EDFIPAFwACVLAGfvpAPLTVPPTyDEPNARLRKLRHIwqll 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 135 ------TKPRLIfcdgDEYEKVK--SATKDLQVTIvtmrnhprgsvrIQDVLTTPVMQNFQPLRLKDgidhTLAILSSSG 206
Cdd:cd05906 118 gspvvlTDAELV----AEFAGLEtlSGLPGIRVLS------------IEELLDTAADHDLPQSRPDD----LALLMLTSG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 207 TSGFPKAVTISnsHKIIVDYMAINNSNIQYTSS--TLDW-----CSGLSMaitSGVFSttsIIADCD----------FDP 269
Cdd:cd05906 178 STGFPKAVPLT--HRNILARSAGKIQHNGLTPQdvFLNWvpldhVGGLVE---LHLRA---VYLGCQqvhvpteeilADP 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 270 GLFCRAIGKYRISMVLLSSSYLAIFAN-CPEFE--SADLSSLNYVIFGGSSCSLEVQRKVRSRLSH-----DCLNFCYGL 341
Cdd:cd05906 250 LRWLDLIDRYRVTITWAPNFAFALLNDlLEEIEdgTWDLSSLRYLVNAGEAVVAKTIRRLLRLLEPyglppDAIRPAFGM 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 342 TElNSAGSVNLNFDEKPN--------SVGRAIRGIKIKVIDEQGEAQEPNVVGEICFHNSQKWAGYYKNPDETRQIQDSE 413
Cdd:cd05906 330 TE-TCSGVIYSRSFPTYDhsqalefvSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTED 408
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 414 NWIHTGDLGYVDkDGYLFVIDRLKDMLKYQNIMYYPSEIENVIAEMPNVLE--ACVFGIWDPVNGDEAAA 481
Cdd:cd05906 409 GWFRTGDLGFLD-NGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPsfTAAFAVRDPGAETEELA 477
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
200-509 |
6.49e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 114.75 E-value: 6.49e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 200 AILSSSGTSGFPKAVTISNSHKIivdYMAINNSNIQYTSSTLD---------WCSGLSMAITSGVFSTTSIIADCDFDPG 270
Cdd:PRK06178 213 ALNYTGGTTGMPKGCEHTQRDMV---YTAAAAYAVAVVGGEDSvflsflpefWIAGENFGLLFPLFSGATLVLLARWDAV 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 271 LFCRAIGKYRI-SMVLLSSSYLAIFaNCPEFESADLSSLNYVifGGSSCSLEVQRKVRSR---LSHDCL-NFCYGLTELN 345
Cdd:PRK06178 290 AFMAAVERYRVtRTVMLVDNAVELM-DHPRFAEYDLSSLRQV--RVVSFVKKLNPDYRQRwraLTGSVLaEAAWGMTETH 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 346 SAGSVNLNFDE-------KPNSVGRAIRGIKIKVID-EQGEAQEPNVVGEICFHNSQKWAGYYKNPDETRQ-IQDSenWI 416
Cdd:PRK06178 367 TCDTFTAGFQDddfdllsQPVFVGLPVPGTEFKICDfETGELLPLGAEGEIVVRTPSLLKGYWNKPEATAEaLRDG--WL 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 417 HTGDLGYVDKDGYLFVIDRLKDMLKYQNIMYYPSEIENVIAEMPNVLEACVFGIWDPVNGDEAAASLVKKPGTQLEAQDV 496
Cdd:PRK06178 445 HTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPGADLTAAAL 524
|
330
....*....|...
gi 281365686 497 VEYVRKRItAKFK 509
Cdd:PRK06178 525 QAWCRENM-AVYK 536
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
201-509 |
6.92e-27 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 113.95 E-value: 6.92e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 201 ILSSSGTSGFPKAV-------TISNSHKIIV----DYMAINNSNIQYTSST------LDWCSGLSmaitsgVFSTTSIIA 263
Cdd:PRK13390 153 MLYSSGTTGFPKGIqpdlpgrDVDAPGDPIVaiarAFYDISESDIYYSSAPiyhaapLRWCSMVH------ALGGTVVLA 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 264 DcDFDPGLFCRAIGKYRISMV-LLSSSYLAIFANCPEFESA-DLSSLNYVIFGGSSCSLEVQRKVRSRLSHDCLNFcYGL 341
Cdd:PRK13390 227 K-RFDAQATLGHVERYRITVTqMVPTMFVRLLKLDADVRTRyDVSSLRAVIHAAAPCPVDVKHAMIDWLGPIVYEY-YSS 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 342 TELNSAGSVNL-NFDEKPNSVGRAIRGiKIKVIDEQGEAQEPNVVGEICFHNSQKWAGYYKNPDETRQIQDSEN--WIHT 418
Cdd:PRK13390 305 TEAHGMTFIDSpDWLAHPGSVGRSVLG-DLHICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAAAQHPAHpfWTTV 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 419 GDLGYVDKDGYLFVIDRLKDMLKYQNIMYYPSEIENVIAEMPNVLEACVFGIWDPVNGDE--AAASLVK--KPGTQLeAQ 494
Cdd:PRK13390 384 GDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQvkAVIQLVEgiRGSDEL-AR 462
|
330
....*....|....*
gi 281365686 495 DVVEYVRKRItAKFK 509
Cdd:PRK13390 463 ELIDYTRSRI-AHYK 476
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
58-468 |
1.49e-26 |
|
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: 112.54 E-value: 1.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 58 SITEDIVLTREDLHMNAMRVASYMRNMGLGQTDIVGVMGRHTTHQSAVAYACFFNG---TPLHALHNAYEeacIAKLFGI 134
Cdd:cd05914 1 LYYGGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGaiaVPILAEFTADE---VHHILNH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 135 TKPRLIFCDGDEyekvksatkDLQVTIVT--MRNHPRGSVRIQDVLTTPVMQNFQPLRLKDGiDHTLAILSSSGTsgFPK 212
Cdd:cd05914 78 SEAKAIFVSDED---------DVALINYTsgTTGNSKGVMLTYRNIVSNVDGVKEVVLLGKG-DKILSILPLHHI--YPL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 213 AVTI-----SNSHKIIVDYMainnsniqyTSSTLDWCSGLSMAITSGVFSTTSI--IADCDFDPGLfCRAIGKYRISMVL 285
Cdd:cd05914 146 TFTLllpllNGAHVVFLDKI---------PSAKIIALAFAQVTPTLGVPVPLVIekIFKMDIIPKL-TLKKFKFKLAKKI 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 286 LSSSYL-AIFANCPE-FESAdlssLNYVIFGGSSCSLEVQRKVRSrlshdcLNFC----YGLTELNSAGSVNLNFDEKPN 359
Cdd:cd05914 216 NNRKIRkLAFKKVHEaFGGN----IKEFVIGGAKINPDVEEFLRT------IGFPytigYGMTETAPIISYSPPNRIRLG 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 360 SVGRAIRGIKIKVIDEQGEAQEpnvvGEICFHNSQKWAGYYKNPDETRQIQDSENWIHTGDLGYVDKDGYLFVIDRLKDM 439
Cdd:cd05914 286 SAGKVIDGVEVRIDSPDPATGE----GEIIVRGPNVMKGYYKNPEATAEAFDKDGWFHTGDLGKIDAEGYLYIRGRKKEM 361
|
410 420 430
....*....|....*....|....*....|..
gi 281365686 440 L---KYQNImyYPSEIENVIAEMPNVLEACVF 468
Cdd:cd05914 362 IvlsSGKNI--YPEEIEAKINNMPFVLESLVV 391
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
268-492 |
1.54e-26 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 113.38 E-value: 1.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 268 DPGLFCRAIGKYRISMVL-LSSSYLAIFANcPEFESADLSSLNYVIFGGSSCSLEVQRKVRSrlshdcLNFC-----YGL 341
Cdd:PRK12492 295 DIPGFIKELGKWRFSALLgLNTLFVALMDH-PGFKDLDFSALKLTNSGGTALVKATAERWEQ------LTGCtivegYGL 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 342 TELNSAGSVNlNFDEKPN--SVGRAIRGIKIKVIDEQGEAQEPNVVGEICFHNSQKWAGYYKNPDETRQIQDSENWIHTG 419
Cdd:PRK12492 368 TETSPVASTN-PYGELARlgTVGIPVPGTALKVIDDDGNELPLGERGELCIKGPQVMKGYWQQPEATAEALDAEGWFKTG 446
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281365686 420 DLGYVDKDGYLFVIDRLKDMLKYQNIMYYPSEIENVIAEMPNVLEACVFGIWDPVNGdEAAASLV--KKPGTQLE 492
Cdd:PRK12492 447 DIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSG-EAVKLFVvaRDPGLSVE 520
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
195-504 |
4.84e-26 |
|
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: 109.49 E-value: 4.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 195 IDHTLAILSSSGTSGFPKAVTISNSHKIivdYMA-INNSNIQYTSSTLDWCS-----------GLSMAITSG---VFSTT 259
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEV---YNAwMLALNSLFDPDDVLLCGlplfhvngsvvTLLTPLASGahvVLAGP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 260 SIIADcdfdPGL---FCRAIGKYRISMVLLSSSYLAIFANCPEfeSADLSSLNYVIFGGSSCSLEVQRKVRSRLShdcLN 336
Cdd:cd05944 78 AGYRN----PGLfdnFWKLVERYRITSLSTVPTVYAALLQVPV--NADISSLRFAMSGAAPLPVELRARFEDATG---LP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 337 FC--YGLTELNSAGSVNL-NFDEKPNSVGRAI--RGIKIKVIDEQGEAQE---PNVVGEICFHNSQKWAGYYkNPDETRQ 408
Cdd:cd05944 149 VVegYGLTEATCLVAVNPpDGPKRPGSVGLRLpyARVRIKVLDGVGRLLRdcaPDEVGEICVAGPGVFGGYL-YTEGNKN 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 409 IQDSENWIHTGDLGYVDKDGYLFVIDRLKDMLKY--QNImyYPSEIENVIAEMPNVLEACVFGIWDPVNGDEAAASLVKK 486
Cdd:cd05944 228 AFVADGWLNTGDLGRLDADGYLFITGRAKDLIIRggHNI--DPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLK 305
|
330
....*....|....*...
gi 281365686 487 PGTQLEAQDVVEYVRKRI 504
Cdd:cd05944 306 PGAVVEEEELLAWARDHV 323
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
201-531 |
4.68e-25 |
|
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: 108.37 E-value: 4.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 201 ILSSSGTSGFPKAVTISNSHKII-VDYMAinnSNIQYTSSTLDWCSGLsMAI--TSGVFST--------TSIIADCDFDP 269
Cdd:cd05923 155 VFYTSGTTGLPKGAVIPQRAAESrVLFMS---TQAGLRHGRHNVVLGL-MPLyhVIGFFAVlvaalaldGTYVVVEEFDP 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 270 GLFCRAIGKYRISMVLLSSSYLAIFANCPEFESADLSSLNYVIFGGSSCSLEVQRKVRSRLSHDCLNFcYGLTE-LNSAg 348
Cdd:cd05923 231 ADALKLIEQERVTSLFATPTHLDALAAAAEFAGLKLSSLRHVTFAGATMPDAVLERVNQHLPGEKVNI-YGTTEaMNSL- 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 349 svnLNFDEKPNSVGRAIRGIKIKVIDEQGEAQEPNVVGE-----ICFHNSQKWAGYYKNPDETRQiQDSENWIHTGDLGY 423
Cdd:cd05923 309 ---YMRDARTGTEMRPGFFSEVRIVRIGGSPDEALANGEegeliVAAAADAAFTGYLNQPEATAK-KLQDGWYRTGDVGY 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 424 VDKDGYLFVIDRLKDMLKY--QNImyYPSEIENVIAEMPNVLEACVFGIWDPVNGDEAAASLVKKPGTqLEAQDVVEYVR 501
Cdd:cd05923 385 VDPSGDVRILGRVDDMIISggENI--HPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREGT-LSADELDQFCR 461
|
330 340 350
....*....|....*....|....*....|
gi 281365686 502 KRITAKFKQLNGGAlIVDQIVRSGNRKTNR 531
Cdd:cd05923 462 ASELADFKRPRRYF-FLDELPKNAMNKVLR 490
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
196-537 |
4.91e-25 |
|
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.
Pssm-ID: 341274 [Multi-domain] Cd Length: 537 Bit Score: 108.74 E-value: 4.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 196 DHTLAILSSSGTSGFPKAVTISNSHKI--IVDYMAINN---SNIQYTSSTLDWCS-------GLSMAiTSGVFsttsiIA 263
Cdd:cd05970 185 EDILLVYFSSGTTGMPKMVEHDFTYPLghIVTAKYWQNvreGGLHLTVADTGWGKavwgkiyGQWIA-GAAVF-----VY 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 264 DCD-FDPGLFCRAIGKYRISmVLLSSSYLAIFANCPEFESADLSSLNYVIFGGSSCSLEVQRKVRSRLSHDcLNFCYGLT 342
Cdd:cd05970 259 DYDkFDPKALLEKLSKYGVT-TFCAPPTIYRFLIREDLSRYDLSSLRYCTTAGEALNPEVFNTFKEKTGIK-LMEGFGQT 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 343 ELNSAGSVNLNFDEKPNSVGRAIRGIKIKVIDEQGEAQEPNVVGEICFHNSQK-----WAGYYKNPDETRQIQdSENWIH 417
Cdd:cd05970 337 ETTLTIATFPWMEPKPGSMGKPAPGYEIDLIDREGRSCEAGEEGEIVIRTSKGkpvglFGGYYKDAEKTAEVW-HDGYYH 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 418 TGDLGYVDKDGYLFVIDRLKDMLKYQNIMYYPSEIENVIAEMPNVLEACVFGIWDPVNGDEAAASLV----KKPGTQL-- 491
Cdd:cd05970 416 TGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIVlakgYEPSEELkk 495
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 281365686 492 EAQDVVeyvrKRITAKFKQLNgGALIVDQIVRSGNRKTNRSAVKEH 537
Cdd:cd05970 496 ELQDHV----KKVTAPYKYPR-IVEFVDELPKTISGKIRRVEIRER 536
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
65-534 |
5.64e-25 |
|
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: 107.72 E-value: 5.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 65 LTREDLHMNAMRVASYMRNMGLGQTDIVGVMGRHTTHQSAVAYACFFNGTPLHALHNAYEEACIAKLFGITKPRLIFCDG 144
Cdd:cd05945 17 LTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERIREILDAAKPALLIADG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 145 DEYekvksatkdlqvtivtmrnhprgsvriqdvlttpvmqnfqplrlkdgidhtLAILSSSGTSGFPKAVTISnsHKIIV 224
Cdd:cd05945 97 DDN---------------------------------------------------AYIIFTSGSTGRPKGVQIS--HDNLV 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 225 DYMAINNSNIQYTS--------------STLDWCSGLsmaiTSGVfSTTSIIADCDFDPGLFCRAIGKYRISMVLLSSSY 290
Cdd:cd05945 124 SFTNWMLSDFPLGPgdvflnqapfsfdlSVMDLYPAL----ASGA-TLVPVPRDATADPKQLFRFLAEHGITVWVSTPSF 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 291 LAIFANCPEFESADLSSLNYVIFGGSSCSLEVQRKVRSRLShDC--LNfCYGLTELNSAGSVN-----LNFDEKPNSVGR 363
Cdd:cd05945 199 AAMCLLSPTFTPESLPSLRHFLFCGEVLPHKTARALQQRFP-DAriYN-TYGPTEATVAVTYIevtpeVLDGYDRLPIGY 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 364 AIRGIKIKVIDEQGEAQEPNVVGEICFHNSQKWAGYYKNPDETRQI---QDSENWIHTGDLGYVDKDGYLFVIDRLKDML 440
Cdd:cd05945 277 AKPGAKLVILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAffpDEGQRAYRTGDLVRLEADGLLFYRGRLDFQV 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 441 KYQNIMYYPSEIENVIAEMPNVLEACVFGIWDPVNGDEAAASLVKKPGTqlEAQDVVE---YVRKR-----ITAKFkqln 512
Cdd:cd05945 357 KLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPGA--EAGLTKAikaELAERlppymIPRRF---- 430
|
490 500
....*....|....*....|..
gi 281365686 513 ggaLIVDQIVRSGNRKTNRSAV 534
Cdd:cd05945 431 ---VYLDELPLNANGKIDRKAL 449
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
311-535 |
7.76e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 107.56 E-value: 7.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 311 VIFGGSSCSLEVQRKVRSRLSHDCLNFCYGLTELN-SAGSVNLNFDEKPNSVGRAIRGIKIKVIDEQGEAQEPNVVGEIC 389
Cdd:PRK07638 258 IISSGAKWEAEAKEKIKNIFPYAKLYEFYGASELSfVTALVDEESERRPNSVGRPFHNVQVRICNEAGEEVQKGEIGTVY 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 390 FHNSQKWAGYYKNPDETRQIQDSEnWIHTGDLGYVDKDGYLFVIDRLKDMLKYQNIMYYPSEIENVIAEMPNVLEACVFG 469
Cdd:PRK07638 338 VKSPQFFMGYIIGGVLARELNADG-WMTVRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIG 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 281365686 470 IWDPVNGDEAAAsLVKKPGTqleAQDVVEYVRKRITAkFKqLNGGALIVDQIVRSGNRKTNRSAVK 535
Cdd:PRK07638 417 VPDSYWGEKPVA-IIKGSAT---KQQLKSFCLQRLSS-FK-IPKEWHFVDEIPYTNSGKIARMEAK 476
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
196-535 |
2.79e-24 |
|
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.
Pssm-ID: 341271 [Multi-domain] Cd Length: 617 Bit Score: 107.02 E-value: 2.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 196 DHTLAILSSSGTSGFPKAVTISNS-HKIIVDYMAINNSNIQ-----YTSSTLDWCSGLSMaITSG--VFSTTSII----A 263
Cdd:cd05967 230 TDPLYILYTSGTTGKPKGVVRDNGgHAVALNWSMRNIYGIKpgdvwWAASDVGWVVGHSY-IVYGplLHGATTVLyegkP 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 264 DCDFDPGLFCRAIGKYRISMvlLSSSYLAIFA------NCPEFESADLSSLNYVIFGGSSCSLEVQRKVRSRLSHDCLNF 337
Cdd:cd05967 309 VGTPDPGAFWRVIEKYQVNA--LFTAPTAIRAirkedpDGKYIKKYDLSSLRTLFLAGERLDPPTLEWAENTLGVPVIDH 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 338 cYGLTELNSAGSVNL----NFDEKPNSVGRAIRGIKIKVIDEQGEAQEPNVVGEICFH---NSQKWAGYYKNPDETRQ-- 408
Cdd:cd05967 387 -WWQTETGWPITANPvglePLPIKAGSPGKPVPGYQVQVLDEDGEPVGPNELGNIVIKlplPPGCLLTLWKNDERFKKly 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 409 IQDSENWIHTGDLGYVDKDGYLFVIDRLKDMLKYQNIMYYPSEIENVIAEMPNVLEACVFGIWDPVNGDEAAASLVKKPG 488
Cdd:cd05967 466 LSKFPGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELKGQVPLGLVVLKEG 545
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 281365686 489 TQLEAQDV----VEYVRKRI--TAKFKQlnggALIVDQI--VRSGnrKTNRSAVK 535
Cdd:cd05967 546 VKITAEELekelVALVREQIgpVAAFRL----VIFVKRLpkTRSG--KILRRTLR 594
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
65-509 |
6.48e-24 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 105.23 E-value: 6.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 65 LTREDLHMNAMRVASYMRNMGLGQTDIVGVMGRHttHQSAVAYACFFN--GTPLHALHNAYEEACIAKLFGITKPRLIFC 142
Cdd:PRK13382 69 LTWRELDERSDALAAALQALPIGEPRVVGIMCRN--HRGFVEALLAANriGADILLLNTSFAGPALAEVVTREGVDTVIY 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 143 DGDEYEKVKSATKDL--QVTIVTMRNHPrGSVRIQDVLTTPVMQNFQPLRLKDGIdhtlaILSSSGTSGFPKAVTISNSH 220
Cdd:PRK13382 147 DEEFSATVDRALADCpqATRIVAWTDED-HDLTVEVLIAAHAGQRPEPTGRKGRV-----ILLTSGTTGTPKGARRSGPG 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 221 -----KIIVDYMAINNSNIQYTSSTLDWCSGLSMAITSGVFSTTsIIADCDFDPGLFCRAIGKYRISMVLLSSSYLAIFA 295
Cdd:PRK13382 221 gigtlKAILDRTPWRAEEPTVIVAPMFHAWGFSQLVLAASLACT-IVTRRRFDPEATLDLIDRHRATGLAVVPVMFDRIM 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 296 NCPE--FESADLSSLNYVIFGGSSCSLEVQRKVRSRLShDCLNFCYGLTELNSAGSVN-LNFDEKPNSVGRAIRGIKIKV 372
Cdd:PRK13382 300 DLPAevRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFG-DVIYNNYNATEAGMIATATpADLRAAPDTAGRPAEGTEIRI 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 373 IDEQGEAQEPNVVGEICFHNSQKWAGYykNPDETRQIQDSenWIHTGDLGYVDKDGYLFVIDRLKDMLKYQNIMYYPSEI 452
Cdd:PRK13382 379 LDQDFREVPTGEVGTIFVRNDTQFDGY--TSGSTKDFHDG--FMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEV 454
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 281365686 453 ENVIAEMPNVLEACVFGIWDPVNGDEAAASLVKKPGTQLEAQDVVEYVRKRItAKFK 509
Cdd:PRK13382 455 EKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPGASATPETLKQHVRDNL-ANYK 510
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
196-538 |
1.21e-23 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 104.47 E-value: 1.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 196 DHTLAILSSSGTSGFPKAVTISNSH------KIIVDYMAINNSNIQYTSSTLDWCSGLSMAITSGVFSTTSIIADCD-FD 268
Cdd:PRK07786 174 DSPALIMYTSGTTGRPKGAVLTHANltgqamTCLRTNGADINSDVGFVGVPLFHIAGIGSMLPGLLLGAPTVIYPLGaFD 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 269 PGLFCRAIGKYRISMV-LLSSSYLAIFANcPEFESADLSsLNYVIFGGSSCSLEVQRKVRSRLSHDCLNFCYGLTELNSA 347
Cdd:PRK07786 254 PGQLLDVLEAEKVTGIfLVPAQWQAVCAE-QQARPRDLA-LRVLSWGAAPASDTLLRQMAATFPEAQILAAFGQTEMSPV 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 348 GSVNLNFD--EKPNSVGRAIRGIKIKVIDEQGEAQEPNVVGEICFHNSQKWAGYYKNPDETRQIQDSeNWIHTGDLGYVD 425
Cdd:PRK07786 332 TCMLLGEDaiRKLGSVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFAG-GWFHSGDLVRQD 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 426 KDGYLFVIDRLKDMLKY--QNImyYPSEIENVIAEMPNVLEACVFGIWDPVNGD-EAAASLVKKPGTQLEAQDVVEYVRK 502
Cdd:PRK07786 411 EEGYVWVVDRKKDMIISggENI--YCAEVENVLASHPDIVEVAVIGRADEKWGEvPVAVAAVRNDDAALTLEDLAEFLTD 488
|
330 340 350
....*....|....*....|....*....|....*.
gi 281365686 503 RItAKFKQLNgGALIVDQIVRSGNRKTNRSAVKEHF 538
Cdd:PRK07786 489 RL-ARYKHPK-ALEIVDALPRNPAGKVLKTELRERY 522
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
65-506 |
1.26e-23 |
|
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: 103.37 E-value: 1.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 65 LTREDLHMNAMRVASYMRNMGLGQTDIV-GVMGRhTTHQSAVAYACFFNGTPLHALHNAYEEACIAKLFGITKPRLIFCD 143
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVaGLLPR-TPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 144 GDEYEKVKSATkdlqvtivtmrnhprgsvriqdvlttpvmqnfqplrlkdgidhtLAILSSSGTSGFPKAV-----TISN 218
Cdd:cd05973 80 AANRHKLDSDP--------------------------------------------FVMMFTSGTTGLPKGVpvplrALAA 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 219 SHKIIVDYMAINNSNIQYTSSTLDWCSGLSMAITSGV-FSTTSIIADCDFDPGLFCRAIGKYRISMVLLS-SSYLAIFAN 296
Cdd:cd05973 116 FGAYLRDAVDLRPEDSFWNAADPGWAYGLYYAITGPLaLGHPTILLEGGFSVESTWRVIERLGVTNLAGSpTAYRLLMAA 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 297 CPEFESADLSSLNYVIFGGSSCSLEVQRKVRSRLS---HDClnfcYGLTELnsaGSV--NLNFDEKP---NSVGRAIRGI 368
Cdd:cd05973 196 GAEVPARPKGRLRRVSSAGEPLTPEVIRWFDAALGvpiHDH----YGQTEL---GMVlaNHHALEHPvhaGSAGRAMPGW 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 369 KIKVIDEQGEAQEPNVVGEICF--HNSQ-KW-AGYYKNPDETRqiqdSENWIHTGDLGYVDKDGYLFVIDRLKDMLKYQN 444
Cdd:cd05973 269 RVAVLDDDGDELGPGEPGRLAIdiANSPlMWfRGYQLPDTPAI----DGGYYLTGDTVEFDPDGSFSFIGRADDVITMSG 344
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281365686 445 IMYYPSEIENVIAEMPNVLEACVFGIWDPVNGDEAAASLVKKPGTQLE---AQDVVEYVRKRITA 506
Cdd:cd05973 345 YRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHEGTpalADELQLHVKKRLSA 409
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
254-509 |
1.53e-23 |
|
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: 104.07 E-value: 1.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 254 GVFST--TSIIADcDFDPGLFCRAIGKYRISMVLLSSSYLAIFANCPEFESADLSSLNYVIFGGSSCSLEVQRKVRSRLs 331
Cdd:COG1021 247 GVLYAggTVVLAP-DPSPDTAFPLIERERVTVTALVPPLALLWLDAAERSRYDLSSLRVLQVGGAKLSPELARRVRPAL- 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 332 hDC-LNFCYGLTElnsaGSVNLNFDEKP-----NSVGRAIR-GIKIKVIDEQGEAQEPNVVGEICFHNSQKWAGYYKNPD 404
Cdd:COG1021 325 -GCtLQQVFGMAE----GLVNYTRLDDPeevilTTQGRPISpDDEVRIVDEDGNPVPPGEVGELLTRGPYTIRGYYRAPE 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 405 ETRQIQDSENWIHTGDLGYVDKDGYLFVIDRLKDMLKY--QNImyYPSEIENVIAEMPNVLEACVFGIWDPVNGDEAAAS 482
Cdd:COG1021 400 HNARAFTPDGFYRTGDLVRRTPDGYLVVEGRAKDQINRggEKI--AAEEVENLLLAHPAVHDAAVVAMPDEYLGERSCAF 477
|
250 260
....*....|....*....|....*..
gi 281365686 483 LVKKpGTQLEAQDVVEYVRKRITAKFK 509
Cdd:COG1021 478 VVPR-GEPLTLAELRRFLRERGLAAFK 503
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
199-509 |
5.46e-23 |
|
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.
Pssm-ID: 341251 [Multi-domain] Cd Length: 530 Bit Score: 102.54 E-value: 5.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 199 LAILSSSGTSGFPKAVTISNS---HKIIVD---YMAINNSNIQYTSSTLDWcsglSMAITSGVFSTTsIIADC------- 265
Cdd:cd05928 177 MAIYFTSGTTGSPKMAEHSHSslgLGLKVNgryWLDLTASDIMWNTSDTGW----IKSAWSSLFEPW-IQGACvfvhhlp 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 266 DFDPGLFCRAIGKYRI-SMVLLSSSYLAIFANcpEFESADLSSLNYVIFGGSSCSLEVQRKVRSRLSHDcLNFCYGLTEL 344
Cdd:cd05928 252 RFDPLVILKTLSSYPItTFCGAPTVYRMLVQQ--DLSSYKFPSLQHCVTGGEPLNPEVLEKWKAQTGLD-IYEGYGQTET 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 345 NSAGSVNLNFDEKPNSVGRAIRGIKIKVIDEQGEAQEPNVVGEI----------CFHNsqkwaGYYKNPDETRQIQDSEN 414
Cdd:cd05928 329 GLICANFKGMKIKPGSMGKASPPYDVQIIDDNGNVLPPGTEGDIgirvkpirpfGLFS-----GYVDNPEKTAATIRGDF 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 415 WIhTGDLGYVDKDGYLFVIDRLKDMLKYQNIMYYPSEIENVIAEMPNVLEACVFGIWDPVNGDEAAASLVKKPGTQ---- 490
Cdd:cd05928 404 YL-TGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLAPQFLshdp 482
|
330 340
....*....|....*....|...
gi 281365686 491 ----LEAQDVVeyvrKRITAKFK 509
Cdd:cd05928 483 eqltKELQQHV----KSVTAPYK 501
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
339-469 |
5.71e-23 |
|
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: 102.50 E-value: 5.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 339 YGLTELNSAGSVNLNFDEKPNSVGRAIRGIKIKvIDEqgeaqepnvVGEICFHNSQKWAGYYKNPDETRQIQDSENWIHT 418
Cdd:cd17641 355 YGQTELAGAYTVHRDGDVDPDTVGVPFPGTEVR-IDE---------VGEILVRSPGVFVGYYKNPEATAEDFDEDGWLHT 424
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 281365686 419 GDLGYVDKDGYLFVIDRLKDMLKYQN-IMYYPSEIENVIAEMPNVLEACVFG 469
Cdd:cd17641 425 GDAGYFKENGHLVVIDRAKDVGTTSDgTRFSPQFIENKLKFSPYIAEAVVLG 476
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
49-506 |
5.73e-23 |
|
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: 102.66 E-value: 5.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 49 NNPKLIAQISITEDIVLTR----EDLHMNAMRVASYMRNMGLGQTDIVGVMGRHTTHQSAVAYACFFNGTPLHALHNAYE 124
Cdd:cd17634 65 ENGDRTAIIYEGDDTSQSRtisyRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFA 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 125 EACIAKLFGITKPR-LIFCDGD-------EYEKVKSATKDLQVTIV-TMRNHPRGSVRIQ---------DVLTTPVMQNF 186
Cdd:cd17634 145 PEAVAGRIIDSSSRlLITADGGvragrsvPLKKNVDDALNPNVTSVeHVIVLKRTGSDIDwqegrdlwwRDLIAKASPEH 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 187 QPLRLkDGIDhTLAILSSSGTSGFPK---------AVTISNSHKIIVDYMAinnSNIQYTSSTLDWCSGLSMAITSGVF- 256
Cdd:cd17634 225 QPEAM-NAED-PLFILYTSGTTGKPKgvlhttggyLVYAATTMKYVFDYGP---GDIYWCTADVGWVTGHSYLLYGPLAc 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 257 STTSIIADCDFD---PGLFCRAIGKYRISMVLLSSSylAIFANCPE----FESADLSSLNYVIFGGSSCSLEVQR---KV 326
Cdd:cd17634 300 GATTLLYEGVPNwptPARMWQVVDKHGVNILYTAPT--AIRALMAAgddaIEGTDRSSLRILGSVGEPINPEAYEwywKK 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 327 RSRLSHDCLNFCYGlTELNSAGSVNLNFDE--KPNSVGRAIRGIKIKVIDEQGEAQEPNVVGEICFHNSqkWAG----YY 400
Cdd:cd17634 378 IGKEKCPVVDTWWQ-TETGGFMITPLPGAIelKAGSATRPVFGVQPAVVDNEGHPQPGGTEGNLVITDP--WPGqtrtLF 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 401 KNPDETRQIQDS--ENWIHTGDLGYVDKDGYLFVIDRLKDMLKYQNIMYYPSEIENVIAEMPNVLEACVFGIWDPVNGDE 478
Cdd:cd17634 455 GDHERFEQTYFStfKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQA 534
|
490 500 510
....*....|....*....|....*....|.
gi 281365686 479 AAASLVKKPGTQLE---AQDVVEYVRKRITA 506
Cdd:cd17634 535 PYAYVVLNHGVEPSpelYAELRNWVRKEIGP 565
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
76-467 |
1.39e-22 |
|
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: 100.03 E-value: 1.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 76 RVASYMRNM-GLGQTDIVGVMGRHTTHQSAVAYACFFNG---TPLHAlhnAYEEACIAKLFGITKPRLIFCDGDEyekvk 151
Cdd:TIGR01733 11 RLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGaayVPLDP---AYPAERLAFILEDAGARLLLTDSAL----- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 152 sATKDLQVTIVTMRNHPRGSVRIQDVLTTPvmqnfqPLRLKDGIDHTLAILSSSGTSGFPKAVTISnsHKIIVDYMAINN 231
Cdd:TIGR01733 83 -ASRLAGLVLPVILLDPLELAALDDAPAPP------PPDAPSGPDDLAYVIYTSGSTGRPKGVVVT--HRSLVNLLAWLA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 232 SNI---------QYTS-----STLDWCsglsMAITSGvfSTTSIIADCD--FDPGLFCRAIGKYRISMVLLSSSYLAIFA 295
Cdd:TIGR01733 154 RRYgldpddrvlQFASlsfdaSVEEIF----GALLAG--ATLVVPPEDEerDDAALLAALIAEHPVTVLNLTPSLLALLA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 296 NCPEFesaDLSSLNYVIFGGSSCSLEVQRKVRSRLSHDCLNFCYGLTELNSAGSVNL-----NFDEKPNSVGRAIRGIKI 370
Cdd:TIGR01733 228 AALPP---ALASLRLVILGGEALTPALVDRWRARGPGARLINLYGPTETTVWSTATLvdpddAPRESPVPIGRPLANTRL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 371 KVIDEQGEAQEPNVVGEICFHNSQKWAGYYKNPDETRQ--------IQDSENWIHTGDLGYVDKDGYLFVIDRLKDMLKy 442
Cdd:TIGR01733 305 YVLDDDLRPVPVGVVGELYIGGPGVARGYLNRPELTAErfvpdpfaGGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVK- 383
|
410 420
....*....|....*....|....*...
gi 281365686 443 qnIMYY---PSEIENVIAEMPNVLEACV 467
Cdd:TIGR01733 384 --IRGYrieLGEIEAALLRHPGVREAVV 409
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
339-509 |
2.29e-22 |
|
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: 98.14 E-value: 2.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 339 YGLTELnsAGSVNLNF--DEKPNSVGRAIRGIKIKVIDEQGEAQEPNVVGEICFHNSQKWAGYYKNPDETRQIQDSeNWI 416
Cdd:cd17636 143 YGQTEV--MGLATFAAlgGGAIGGAGRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRTRG-GWH 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 417 HTGDLGYVDKDGYLFVIDRLKDMLKY--QNImyYPSEIENVIAEMPNVLEACVFGIWDPVNGDEAAASLVKKPGTQLEAQ 494
Cdd:cd17636 220 HTNDLGRREPDGSLSFVGPKTRMIKSgaENI--YPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPGASVTEA 297
|
170
....*....|....*
gi 281365686 495 DVVEYVRKRItAKFK 509
Cdd:cd17636 298 ELIEHCRARI-ASYK 311
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
339-510 |
3.30e-22 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 99.95 E-value: 3.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 339 YGLTELNSAGSVNLNFDEKPNSVGRAIRGIKIKVID-EQGEAQEPNVVGEICFHNSQKWAGYYKNPDETRQIQDSENWIH 417
Cdd:PRK07514 301 YGMTETNMNTSNPYDGERRAGTVGFPLPGVSLRVTDpETGAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGFFI 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 418 TGDLGYVDKDGYLFVIDRLKDML---KYqNImyYPSEIENVIAEMPNVLEACVFGIWDPVNGDEAAASLVKKPGTQLEAQ 494
Cdd:PRK07514 381 TGDLGKIDERGYVHIVGRGKDLIisgGY-NV--YPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKPGAALDEA 457
|
170
....*....|....*.
gi 281365686 495 DVVEYVRKRItAKFKQ 510
Cdd:PRK07514 458 AILAALKGRL-ARFKQ 472
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
60-539 |
4.08e-22 |
|
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: 100.01 E-value: 4.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 60 TEDIVLTREDLHMNAMRVASYMRnmGLGQT-DIVGVMGRHTTHQSAVAYACFFNG---TPLHALHNAYEEACIAKLFGIT 135
Cdd:cd05931 20 GREETLTYAELDRRARAIAARLQ--AVGKPgDRVLLLAPPGLDFVAAFLGCLYAGaiaVPLPPPTPGRHAERLAAILADA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 136 KPRLIFCDGDEYEKVKSatkdlqvTIVTMRNHPRGSVRIQDVLTTPVMQNFQPLRLKDGidhTLAILS-SSGTSGFPKAV 214
Cdd:cd05931 98 GPRVVLTTAAALAAVRA-------FAASRPAAGTPRLLVVDLLPDTSAADWPPPSPDPD---DIAYLQyTSGSTGTPKGV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 215 TIS------NSHKIIVDYMainnsnIQYTSSTLDWCS-----GLSMAITSGVFS--TTSIIADCDF--DPGLFCRAIGKY 279
Cdd:cd05931 168 VVThrnllaNVRQIRRAYG------LDPGDVVVSWLPlyhdmGLIGGLLTPLYSggPSVLMSPAAFlrRPLRWLRLISRY 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 280 RismvllsssylAIFANCPEF--------------ESADLSSLNYVIFGGsscslE-VQRKVRSR---------LSHDCL 335
Cdd:cd05931 242 R-----------ATISAAPNFaydlcvrrvrdedlEGLDLSSWRVALNGA-----EpVRPATLRRfaeafapfgFRPEAF 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 336 NFCYGLTE---------------------LNSAGSVNLNFDEKPN-----SVGRAIRGIKIKVIDEQGEAQ-EPNVVGEI 388
Cdd:cd05931 306 RPSYGLAEatlfvsggppgtgpvvlrvdrDALAGRAVAVAADDPAarelvSCGRPLPDQEVRIVDPETGRElPDGEVGEI 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 389 CFHNSQKWAGYYKNPDETRQI------QDSENWIHTGDLGYVdKDGYLFVIDRLKDMLkyqnIM----YYPSEIENVIAE 458
Cdd:cd05931 386 WVRGPSVASGYWGRPEATAETfgalaaTDEGGWLRTGDLGFL-HDGELYITGRLKDLI----IVrgrnHYPQDIEATAEE 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 459 MPNVLE---ACVFGIWDPVNGDEAAASLVKKPGTQLEAQDVVEYVRKRITAKFKqlnggaLIVDQIV--------R--SG 525
Cdd:cd05931 461 AHPALRpgcVAAFSVPDDGEERLVVVAEVERGADPADLAAIAAAIRAAVAREHG------VAPADVVlvrpgsipRtsSG 534
|
570
....*....|....
gi 281365686 526 nrKTNRSAVKEHFL 539
Cdd:cd05931 535 --KIQRRACRAAYL 546
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
65-507 |
6.21e-22 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 99.36 E-value: 6.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 65 LTREDLHMNAMRVASYMRNMGLGQTDIVGVMGRHTTHQSAVAYACFFNGTPLHALHNAYEEACI--------AKLFGItk 136
Cdd:PRK13295 56 FTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERELsfmlkhaeSKVLVV-- 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 137 PRLIfcDGDEYE----KVKSATKDLQVTIVTMRNhprGSVRIQDVLTTPVMQNFQPL-----RLKDGIDHTLAILSSSGT 207
Cdd:PRK13295 134 PKTF--RGFDHAamarRLRPELPALRHVVVVGGD---GADSFEALLITPAWEQEPDApailaRLRPGPDDVTQLIYTSGT 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 208 SGFPKAV------TISNSHKIiVDYMAINNSNIQYTSSTL----DWCSGLSMAITSGvfsTTSIIADCdFDPGLFCRAIG 277
Cdd:PRK13295 209 TGEPKGVmhtantLMANIVPY-AERLGLGADDVILMASPMahqtGFMYGLMMPVMLG---ATAVLQDI-WDPARAAELIR 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 278 KYRISMVLLSSSYLAIFANCPEFESADLSSLNYVIFGGSSCSLEVQRKVRSRLShdcLNFC--YGLTElNSAGSVNL--N 353
Cdd:PRK13295 284 TEGVTFTMASTPFLTDLTRAVKESGRPVSSLRTFLCAGAPIPGALVERARAALG---AKIVsaWGMTE-NGAVTLTKldD 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 354 FDEKP-NSVGRAIRGIKIKVIDEQGEAQEPNVVGEI----CFHnsqkWAGYYKNPDETRQiqDSENWIHTGDLGYVDKDG 428
Cdd:PRK13295 360 PDERAsTTDGCPLPGVEVRVVDADGAPLPAGQIGRLqvrgCSN----FGGYLKRPQLNGT--DADGWFDTGDLARIDADG 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 429 YLFVIDRLKDMLKY--QNImyyP-SEIENVIAEMPNVLEACVFGIWDPVNGDEAAASLVKKPGTQLEAQDVVEYVRKRIT 505
Cdd:PRK13295 434 YIRISGRSKDVIIRggENI---PvVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPRPGQSLDFEEMVEFLKAQKV 510
|
..
gi 281365686 506 AK 507
Cdd:PRK13295 511 AK 512
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
59-509 |
6.26e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 99.43 E-value: 6.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 59 ITEDIVLTREDLHMNAMRVASYMRNMGLGQTDIVGVMGRHTTHQSAVAYACFFNGTPLHALHNAYEEACIAKLFGITKPR 138
Cdd:PRK06164 30 IDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRAR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 139 LI-----FCDGDEYEKV----KSATKDLQVTIVTMRNH-----PRGSVRIQdVLTTPVMQNFQPLRLKDGIDHTLAIL-S 203
Cdd:PRK06164 110 WLvvwpgFKGIDFAAILaavpPDALPPLRAIAVVDDAAdatpaPAPGARVQ-LFALPDPAPPAAAGERAADPDAGALLfT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 204 SSGTSGFPKAVT------ISNSHKIIVDYMAINNSNIqytsstldwcsgLSMAITSGVFSTTSIIADCD----------F 267
Cdd:PRK06164 189 TSGTTSGPKLVLhrqatlLRHARAIARAYGYDPGAVL------------LAALPFCGVFGFSTLLGALAggaplvcepvF 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 268 DPGLFCRAIGKYRISMVLLSSSYLA-IFANCPEfeSADLSSLNYVIFGG-SSCSLEVQRKVRSRLShdCLNFCYGLTE-- 343
Cdd:PRK06164 257 DAARTARALRRHRVTHTFGNDEMLRrILDTAGE--RADFPSARLFGFASfAPALGELAALARARGV--PLTGLYGSSEvq 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 344 -LNSAGSVNLNFDEKPNSVGRAIRG-IKIKVIDEQ-GEAQEPNVVGEICFHNSQKWAGYYKNPDETRQIQDSENWIHTGD 420
Cdd:PRK06164 333 aLVALQPATDPVSVRIEGGGRPASPeARVRARDPQdGALLPDGESGEIEIRAPSLMRGYLDNPDATARALTDDGYFRTGD 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 421 LGYVDKDGYLFVIDRLKDMLKYQNIMYYPSEIENVIAEMPNVLEACVFGIwdPVNGD-EAAASLVKKPGTQLEAQDVVEY 499
Cdd:PRK06164 413 LGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGA--TRDGKtVPVAFVIPTDGASPDEAGLMAA 490
|
490
....*....|
gi 281365686 500 VRKRItAKFK 509
Cdd:PRK06164 491 CREAL-AGFK 499
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
268-504 |
1.15e-21 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 98.87 E-value: 1.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 268 DPGLFCR---AIGKYRISMVLLSSSYLAIFANCPeFESADLSSLNYVIFGGSSCSLEVQRKVRSRLSHDCLNfCYGLTEL 344
Cdd:PRK07529 293 GPGVIANfwkIVERYRINFLSGVPTVYAALLQVP-VDGHDISSLRYALCGAAPLPVEVFRRFEAATGVRIVE-GYGLTEA 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 345 NSAGSVN-LNFDEKPNSVGraIR----GIKIKVIDEQGEAQ---EPNVVGEICFHNSQKWAGYYkNPDETRQIQDSENWI 416
Cdd:PRK07529 371 TCVSSVNpPDGERRIGSVG--LRlpyqRVRVVILDDAGRYLrdcAVDEVGVLCIAGPNVFSGYL-EAAHNKGLWLEDGWL 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 417 HTGDLGYVDKDGYLFVIDRLKDMLKY--QNImyYPSEIENVIAEMPNVLEACVFGIWDPVNGDEAAASLVKKPGTQLEAQ 494
Cdd:PRK07529 448 NTGDLGRIDADGYFWLTGRAKDLIIRggHNI--DPAAIEEALLRHPAVALAAAVGRPDAHAGELPVAYVQLKPGASATEA 525
|
250
....*....|
gi 281365686 495 DVVEYVRKRI 504
Cdd:PRK07529 526 ELLAFARDHI 535
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
61-533 |
1.77e-21 |
|
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: 97.66 E-value: 1.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 61 EDIVLTREDLHMNAMRVASYMRNMGLGQTDIVGVMGRHTTHQSAV---------AYACffngtplhaLHNAYEEACIAKL 131
Cdd:cd12117 19 GDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVAllavlkagaAYVP---------LDPELPAERLAFM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 132 FGITKPRLIFCDGdeyekvksatkdlqvtivTMRNHPRGSVRIQDVLTTPVMQNFQPLRLKDGIDHTLAILSSSGTSGFP 211
Cdd:cd12117 90 LADAGAKVLLTDR------------------SLAGRAGGLEVAVVIDEALDAGPAGNPAVPVSPDDLAYVMYTSGSTGRP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 212 KAVTISnsHKIIV------DYMAIN-------NSNIQYTSSTLD-WCSGLSMAitsgvfstTSIIADCDF--DPGLFCRA 275
Cdd:cd12117 152 KGVAVT--HRGVVrlvkntNYVTLGpddrvlqTSPLAFDASTFEiWGALLNGA--------RLVLAPKGTllDPDALGAL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 276 IGKYRISMVLLSSsylAIFANCPEFESADLSSLNYVIFGGSSCSLEVQRKVRSRLSHDCLNFCYGLTElnsagsvNLNF- 354
Cdd:cd12117 222 IAEEGVTVLWLTA---ALFNQLADEDPECFAGLRELLTGGEVVSPPHVRRVLAACPGLRLVNGYGPTE-------NTTFt 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 355 --------DEKPNSV--GRAIRGIKIKVIDEQGEAQEPNVVGEICFHNSQKWAGYYKNPDETRQ--IQDS----ENWIHT 418
Cdd:cd12117 292 tshvvtelDEVAGSIpiGRPIANTRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAErfVADPfgpgERLYRT 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 419 GDLGYVDKDGYLFVIDRLKDMLKYQNIMYYPSEIENVIAEMPNVLEACVfGIWDPVNGDEA-AASLVkkPGTQLEAQDVV 497
Cdd:cd12117 372 GDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVV-VVREDAGGDKRlVAYVV--AEGALDAAELR 448
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 281365686 498 EYVRKR-----ITAKFKQLnggalivDQIVRSGNRKTNRSA 533
Cdd:cd12117 449 AFLRERlpaymVPAAFVVL-------DELPLTANGKVDRRA 482
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
339-506 |
3.25e-21 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 97.38 E-value: 3.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 339 YGLTELNSAGSVN-LNFDEKPNSVGRAIRGIKIKVIDEQ--GEAQEPNVVGEICFHNSQKWAGYYKNPDETRQIQdSENW 415
Cdd:PRK05605 368 YGLTETSPIIVGNpMSDDRRPGYVGVPFPDTEVRIVDPEdpDETMPDGEEGELLVRGPQVFKGYWNRPEETAKSF-LDGW 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 416 IHTGDLGYVDKDGYLFVIDRLKDMLKYQNIMYYPSEIENVIAEMPNVLEACVFGIWDPVNGDEAAASLVKKPGTQLEAQD 495
Cdd:PRK05605 447 FRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEPGAALDPEG 526
|
170
....*....|.
gi 281365686 496 VVEYVRKRITA 506
Cdd:PRK05605 527 LRAYCREHLTR 537
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
204-506 |
8.19e-21 |
|
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: 95.22 E-value: 8.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 204 SSGTSGFPKAVTisNSHK--------IIVDYMAINNSNIQYTSSTLDWCSGLSMAITSGVFS-TTSIIADCDFDPGLFCR 274
Cdd:cd05919 99 SSGTTGPPKGVM--HAHRdpllfadaMAREALGLTPGDRVFSSAKMFFGYGLGNSLWFPLAVgASAVLNPGWPTAERVLA 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 275 AIGKYRISmVLLSSSylAIFANC---PEFESADLSSLNYVIFGGSSCSLEVQRKVRSRLSHDCLNfCYGLTEL------N 345
Cdd:cd05919 177 TLARFRPT-VLYGVP--TFYANLldsCAGSPDALRSLRLCVSAGEALPRGLGERWMEHFGGPILD-GIGATEVghiflsN 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 346 SAGSVnlnfdeKPNSVGRAIRGIKIKVIDEQGEAQEPNVVGEICFHNSQKWAGYYKNPDETRQIQDSEnWIHTGDLGYVD 425
Cdd:cd05919 253 RPGAW------RLGSTGRPVPGYEIRLVDEEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATFNGG-WYRTGDKFCRD 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 426 KDGYLFVIDRLKDMLKYQNIMYYPSEIENVIAEMPNVLEACVFGIWDPVNGDEAAASLVKKPG---TQLEAQDVVEYVRK 502
Cdd:cd05919 326 ADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPaapQESLARDIHRHLLE 405
|
....
gi 281365686 503 RITA 506
Cdd:cd05919 406 RLSA 409
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
308-469 |
2.47e-20 |
|
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: 94.20 E-value: 2.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 308 LNYVIFGGSSCSLEVQRKVRsrlshdclNFC------YGLTELNSAGSVNLNFDEKPNSVGRAIRGIKIKVID--EQG-E 378
Cdd:cd17639 252 LRYMLSGGAPLSADTQEFLN--------IVLcpviqgYGLTETCAGGTVQDPGDLETGRVGPPLPCCEIKLVDweEGGyS 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 379 AQEPNVVGEICFHNSQKWAGYYKNPDETRQIQDSENWIHTGDLGYVDKDGYLFVIDRLKDMLKYQNIMYYPSE-IENVIA 457
Cdd:cd17639 324 TDKPPPRGEILIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQNGEYIALEkLESIYR 403
|
170
....*....|..
gi 281365686 458 EMPNVLEACVFG 469
Cdd:cd17639 404 SNPLVNNICVYA 415
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
204-523 |
3.96e-20 |
|
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: 93.55 E-value: 3.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 204 SSGTSGFPKAvtISNSHKIIvDYMAINNSNI-QYTSSTLDWCsGLSMA----ITS-GVFST-----TSIIADcDFDPGLF 272
Cdd:cd05920 147 SGGTTGTPKL--IPRTHNDY-AYNVRASAEVcGLDQDTVYLA-VLPAAhnfpLACpGVLGTllaggRVVLAP-DPSPDAA 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 273 CRAIGKYRISMVLLSSSYLAIFANCPEFESADLSSLNYVIFGGSSCSLEVQRKVRSRLshDC-LNFCYGLTElnsaGSVN 351
Cdd:cd05920 222 FPLIEREGVTVTALVPALVSLWLDAAASRRADLSSLRLLQVGGARLSPALARRVPPVL--GCtLQQVFGMAE----GLLN 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 352 LN-FDEKP----NSVGRAI-RGIKIKVIDEQGEAQEPNVVGEICFHNSQKWAGYYKNPDETRQIQDSENWIHTGDLGYVD 425
Cdd:cd05920 296 YTrLDDPDeviiHTQGRPMsPDDEIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRT 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 426 KDGYLFVIDRLKDMLKYQNIMYYPSEIENVIAEMPNVLEACVFGIWDPVNGDEAAASLVKKPgTQLEAQDVVEYVRKRIT 505
Cdd:cd05920 376 PDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVLRD-PPPSAAQLRRFLRERGL 454
|
330
....*....|....*...
gi 281365686 506 AKFKqlnggalIVDQIVR 523
Cdd:cd05920 455 AAYK-------LPDRIEF 465
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
196-436 |
4.74e-20 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 94.61 E-value: 4.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 196 DHTLAILSSSGTSGFPKAVTISNsHKIIVDYMAI-------NNSNI----------QYTSST-LDWCSGLSMAitsgvfs 257
Cdd:PRK08633 782 DDTATIIFSSGSEGEPKGVMLSH-HNILSNIEQIsdvfnlrNDDVIlsslpffhsfGLTVTLwLPLLEGIKVV------- 853
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 258 ttsiiadCDFDPgLFCRAIGK----YRISMVLLSSSYLAIFANCPEFESADLSSLNYVIFGGSSCSLEVQRKVRSRLSHD 333
Cdd:PRK08633 854 -------YHPDP-TDALGIAKlvakHRATILLGTPTFLRLYLRNKKLHPLMFASLRLVVAGAEKLKPEVADAFEEKFGIR 925
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 334 CLNfCYGLTELNSAGSVNL-NFDE---------KPNSVGRAIRGIKIKVID-EQGEAQEPNVVGEICFHNSQKWAGYYKN 402
Cdd:PRK08633 926 ILE-GYGATETSPVASVNLpDVLAadfkrqtgsKEGSVGMPLPGVAVRIVDpETFEELPPGEDGLILIGGPQVMKGYLGD 1004
|
250 260 270
....*....|....*....|....*....|....*..
gi 281365686 403 PDETRQI---QDSENWIHTGDLGYVDKDGYLFVIDRL 436
Cdd:PRK08633 1005 PEKTAEVikdIDGIGWYVTGDKGHLDEDGFLTITDRY 1041
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
196-497 |
5.45e-20 |
|
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: 93.16 E-value: 5.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 196 DHTLAILSSSGTSGFPKAVTISNsHKIIVDYMAINNsniqYTSSTLDW--CSGL----SMAITSGVFST--TSIIADCDF 267
Cdd:cd05909 147 DDPAVILFTSGSEGLPKGVVLSH-KNLLANVEQITA----IFDPNPEDvvFGALpffhSFGLTGCLWLPllSGIKVVFHP 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 268 DPgLFCRAIG----KYRISMVLLSSSYLAIFANcpEFESADLSSLNYVIFGGSSCSLEVQRKVRSRLsHDCLNFCYGLTE 343
Cdd:cd05909 222 NP-LDYKKIPeliyDKKATILLGTPTFLRGYAR--AAHPEDFSSLRLVVAGAEKLKDTLRQEFQEKF-GIRILEGYGTTE 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 344 LNSAGSVNL-NFDEKPNSVGRAIRGIKIKVIDEQGEAQEP-NVVGEICFHNSQKWAGYYKNPDETrQIQDSENWIHTGDL 421
Cdd:cd05909 298 CSPVISVNTpQSPNKEGTVGRPLPGMEVKIVSVETHEEVPiGEGGLLLVRGPNVMLGYLNEPELT-SFAFGDGWYDTGDI 376
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281365686 422 GYVDKDGYLFVIDRLKDMLKYQNIMYYPSEIENVIAE-MPNVLEACVFGIWDPVNGDEAAASLVKKPGTQLEAQDVV 497
Cdd:cd05909 377 GKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEiLPEDNEVAVVSVPDGRKGEKIVLLTTTTDTDPSSLNDIL 453
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
311-469 |
8.59e-20 |
|
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: 92.66 E-value: 8.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 311 VIFGGSSCSLEVQRKVRSRLshdCLNFC--YGLTELNSAGSVNLNFDEKPNSVGRAIRGIKIKVID--EQG-EAQEPNVV 385
Cdd:cd05927 279 MLTGSAPLSPEVLEFLRVAL---GCPVLegYGQTECTAGATLTLPGDTSVGHVGGPLPCAEVKLVDvpEMNyDAKDPNPR 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 386 GEICFHNSQKWAGYYKNPDETRQIQDSENWIHTGDLGYVDKDGYLFVIDRLKDMLKYQNIMYY-PSEIENVIAEMPNVLE 464
Cdd:cd05927 356 GEVCIRGPNVFSGYYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIFKLSQGEYVaPEKIENIYARSPFVAQ 435
|
....*
gi 281365686 465 ACVFG 469
Cdd:cd05927 436 IFVYG 440
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
159-463 |
2.15e-19 |
|
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: 91.40 E-value: 2.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 159 VTIVTMRNHPRGSVRIQDVLTTPVMQNFQPLrLKDGIDHTLAILSSSGTSGFPKAVTISNsHKIIVDYMAINNS-NIQYT 237
Cdd:cd05908 70 VSIGSNEEHKLKLNKVWNTLKNPYLITEEEV-LCELADELAFIQFSSGSTGDPKGVMLTH-ENLVHNMFAILNStEWKTK 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 238 SSTLDWcsglsMAITSGV----FSTTSIIADCD----------FDPGLFCRAIGKYRISMVL---LSSSYLAIFANCPEF 300
Cdd:cd05908 148 DRILSW-----MPLTHDMgliaFHLAPLIAGMNqylmptrlfiRRPILWLKKASEHKATIVSspnFGYKYFLKTLKPEKA 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 301 ESADLSSLNYVIFGGSSCSLEVQRKVRSRLS-----HDCLNFCYGLTElNSAGS----VNLNF----------------- 354
Cdd:cd05908 223 NDWDLSSIRMILNGAEPIDYELCHEFLDHMSkyglkRNAILPVYGLAE-ASVGAslpkAQSPFktitlgrrhvthgepep 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 355 ---DEKPN-----SVGRAIRGIKIKVIDEQGEAQEPNVVGEICFHNSQKWAGYYKNPDETRQIQDSENWIHTGDLGYVdK 426
Cdd:cd05908 302 evdKKDSEcltfvEVGKPIDETDIRICDEDNKILPDGYIGHIQIRGKNVTPGYYNNPEATAKVFTDDGWLKTGDLGFI-R 380
|
330 340 350
....*....|....*....|....*....|....*..
gi 281365686 427 DGYLFVIDRLKDMLKYQNIMYYPSEIENVIAEMPNVL 463
Cdd:cd05908 381 NGRLVITGREKDIIFVNGQNVYPHDIERIAEELEGVE 417
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
339-538 |
5.66e-19 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 89.95 E-value: 5.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 339 YGLTE----LNSAGSVNLNFDEKPN-SVGRAIR--GIKIKVIDEQGEAQEPNVVGEICFHNSQKWAGYYKNPDETRQiQD 411
Cdd:PRK05852 327 FGMTEathqVTTTQIEGIGQTENPVvSTGLVGRstGAQIRIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDPTITAA-NF 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 412 SENWIHTGDLGYVDKDGYLFVIDRLKDMLKYQNIMYYPSEIENVIAEMPNVLEACVFGIWDPVNGDEAAASLVKKPGTQL 491
Cdd:PRK05852 406 TDGWLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIVPRESAPP 485
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 281365686 492 EAQDVVEYVRKR-----ITAKFKqlnggalIVDQIVRSGNRKTNRSAVKEHF 538
Cdd:PRK05852 486 TAEELVQFCRERlaafeIPASFQ-------EASGLPHTAKGSLDRRAVAEQF 530
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
59-510 |
7.41e-19 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 89.67 E-value: 7.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 59 ITEDIVLTREDLHMNAMRVASYMRNMGLGQTDIVGVMGRHTTHQSAVAYACFFNGTPLHALHNAYEEACIAKLFGITKPR 138
Cdd:PRK13383 55 IDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAALRAHHIS 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 139 LIFCDgDEYEKVKSATKDLQVTIvtmrnHPrGSVRIQDVLTTPVMQnfQPLRLkdgidhtlaILSSSGTSGFPKAVTISN 218
Cdd:PRK13383 135 TVVAD-NEFAERIAGADDAVAVI-----DP-ATAGAEESGGRPAVA--APGRI---------VLLTSGTTGKPKGVPRAP 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 219 --SHKIIVDYMAINNSNIQyTSSTLDWCSGLSMAITSGVFSTT-----SIIADCDFDPGLFCRAIGKYRISMVLLSSSYL 291
Cdd:PRK13383 197 qlRSAVGVWVTILDRTRLR-TGSRISVAMPMFHGLGLGMLMLTialggTVLTHRHFDAEAALAQASLHRADAFTAVPVVL 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 292 AIFANCPEFESA--DLSSLNYVIFGGSSCSLEVQRKVRSRLShDCLNFCYGLTELN-SAGSVNLNFDEKPNSVGRAIRGI 368
Cdd:PRK13383 276 ARILELPPRVRArnPLPQLRVVMSSGDRLDPTLGQRFMDTYG-DILYNGYGSTEVGiGALATPADLRDAPETVGKPVAGC 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 369 KIKVIDEQGEAQEPNVVGEICFHNSQKWAGYykNPDETRQIQDSenWIHTGDLGYVDKDGYLFVIDRLKDMLKYQNIMYY 448
Cdd:PRK13383 355 PVRILDRNNRPVGPRVTGRIFVGGELAGTRY--TDGGGKAVVDG--MTSTGDMGYLDNAGRLFIVGREDDMIISGGENVY 430
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281365686 449 PSEIENVIAEMPNVLEACVFGIWDPVNGDEAAASLVKKPGTQLEAQDVVEYVRKRITaKFKQ 510
Cdd:PRK13383 431 PRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPGSGVDAAQLRDYLKDRVS-RFEQ 491
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
188-506 |
8.06e-19 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 89.57 E-value: 8.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 188 PLRLKDGidhtlAILS-SSGTSGFPKAVtisnshkiivdyMAINNSNIQYTSST---LD-------WCS-------GLSM 249
Cdd:PRK04319 201 WTDREDG-----AILHyTSGSTGKPKGV------------LHVHNAMLQHYQTGkyvLDlheddvyWCTadpgwvtGTSY 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 250 AI----TSGVfstTSIIADCDFDPGLFCRAIGKYRIS----------MVLLSSSYLAifancpefESADLSSLNYVIFGG 315
Cdd:PRK04319 264 GIfapwLNGA---TNVIDGGRFSPERWYRILEDYKVTvwytaptairMLMGAGDDLV--------KKYDLSSLRHILSVG 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 316 SSCSLEVQR---KVRSRLSHDClnfcYGLTELNSAGSVNL-NFDEKPNSVGRAIRGIKIKVIDEQGEAQEPNVVGEIC-- 389
Cdd:PRK04319 333 EPLNPEVVRwgmKVFGLPIHDN----WWMTETGGIMIANYpAMDIKPGSMGKPLPGIEAAIVDDQGNELPPNRMGNLAik 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 390 ----------FHNSQKWAGYYKNpdetrqiqdseNWIHTGDLGYVDKDGYLFVIDRLKDMLKYQNIMYYPSEIENVIAEM 459
Cdd:PRK04319 409 kgwpsmmrgiWNNPEKYESYFAG-----------DWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEH 477
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 281365686 460 PNVLEACVFGIWDPVNGDEAAASLVKKPGTQL-EA--QDVVEYVRKRITA 506
Cdd:PRK04319 478 PAVAEAGVIGKPDPVRGEIIKAFVALRPGYEPsEElkEEIRGFVKKGLGA 527
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
338-469 |
8.90e-19 |
|
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: 89.72 E-value: 8.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 338 CYGLTELNSAGSVNLNFDEKPNSVGRAIRGIKIKVIDEQGEAQepnvvGEICFHNSQKWAGYYKNPDETRQIQDSENWIH 417
Cdd:cd05933 350 LYGMSETSGPHTISNPQAYRLLSCGKALPGCKTKIHNPDADGI-----GEICFWGRHVFMGYLNMEDKTEEAIDEDGWLH 424
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 281365686 418 TGDLGYVDKDGYLFVIDRLKDMLKY---QNIMYYPSEiENVIAEMPNVLEACVFG 469
Cdd:cd05933 425 SGDLGKLDEDGFLYITGRIKELIITaggENVPPVPIE-DAVKKELPIISNAMLIG 478
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
62-504 |
1.69e-18 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.
Pssm-ID: 213283 [Multi-domain] Cd Length: 509 Bit Score: 88.64 E-value: 1.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 62 DIVLTREDLHMNAMRVASYMRNMGLGQTDIVGVMGRHTTHQSAVAYACFFNGTPLHALHNAYEEACIAKLFGITKPRLIF 141
Cdd:cd05915 22 VHRTTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVLL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 142 CDgDEYEKVKSATKDLQVTIVTMRNHPRGSVRIQDVLTTPvMQNFQPLRLKDGIDhTLAILSSSGTSGFPKAVTIS---- 217
Cdd:cd05915 102 FD-PNLLPLVEAIRGELKTVQHFVVMDEKAPEGYLAYEEA-LGEEADPVRVPERA-ACGMAYTTGTTGLPKGVVYShral 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 218 --NSHKI-IVDYMAINNSNIQYTSSTLDWCSGLSMAITSGVFSTTSI-IADCDFDPGLFcRAIGKYRISMVLLSSSYLAI 293
Cdd:cd05915 179 vlHSLAAsLVDGTALSEKDVVLPVVPMFHVNAWCLPYAATLVGAKQVlPGPRLDPASLV-ELFDGEGVTFTAGVPTVWLA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 294 FANCPEFESADLSSLNYVIFGGSSCSlEVQRKVRsRLSHDCLNFCYGLTELNSAGSVNL------NFDEKPNSVGRAIRG 367
Cdd:cd05915 258 LADYLESTGHRLKTLRRLVVGGSAAP-RSLIARF-ERMGVEVRQGYGLTETSPVVVQNFvkshleSLSEEEKLTLKAKTG 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 368 IK-----IKVIDEQGEA--QEPNVVGEICFHNSQKWAGYYKNPDETRQIQDSENWIHTGDLGYVDKDGYLFVIDRLKDML 440
Cdd:cd05915 336 LPiplvrLRVADEEGRPvpKDGKALGEVQLKGPWITGGYYGNEEATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLI 415
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 281365686 441 KYQNIMYYPSEIENVIAEMPNVLEACVFGIWDPVNGdEAAASLVKKPGTQLEAQDVVEYVRKRI 504
Cdd:cd05915 416 KSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQ-ERPLAVVVPRGEKPTPEELNEHLLKAG 478
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
196-503 |
2.10e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 88.20 E-value: 2.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 196 DHTLAILSSSGTSGFPKAVTISNsHKI------IVDYMAINNSNIQYTSSTL--------DW----CSGLSMAITSGvFS 257
Cdd:PRK07867 152 DDLFMLIFTSGTSGDPKAVRCTH-RKVasagvmLAQRFGLGPDDVCYVSMPLfhsnavmaGWavalAAGASIALRRK-FS 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 258 TTSIIADCdfdpglfcRAIGKYRISMVLLSSSYlaIFANCPEFESADlSSLNyVIFGGSSCSLEVQRKVRsRLshDC-LN 336
Cdd:PRK07867 230 ASGFLPDV--------RRYGATYANYVGKPLSY--VLATPERPDDAD-NPLR-IVYGNEGAPGDIARFAR-RF--GCvVV 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 337 FCYGLTELnsAGSVNLNFDEKPNSVGRAIRGIKI-----------KVIDEQGEAQEPNVVGEICFHNSQKW-AGYYKNPD 404
Cdd:PRK07867 295 DGFGSTEG--GVAITRTPDTPPGALGPLPPGVAIvdpdtgtecppAEDADGRLLNADEAIGELVNTAGPGGfEGYYNDPE 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 405 -ETRQIQDSenWIHTGDLGYVDKDGYLFVIDRLKDMLKY--QNIMYYPseIENVIAEMPNVLEACVFGIWDPVNGDEAAA 481
Cdd:PRK07867 373 aDAERMRGG--VYWSGDLAYRDADGYAYFAGRLGDWMRVdgENLGTAP--IERILLRYPDATEVAVYAVPDPVVGDQVMA 448
|
330 340
....*....|....*....|..
gi 281365686 482 SLVKKPGTQLEAQDVVEYVRKR 503
Cdd:PRK07867 449 ALVLAPGAKFDPDAFAEFLAAQ 470
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
205-538 |
2.19e-18 |
|
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: 86.23 E-value: 2.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 205 SGTSGFPKAVTISnSHKIIVDYMAINnSNIQYTSSTLDWCS-------GLSMAITSGVFSTTSIIADCDFDPGLFCRAIG 277
Cdd:cd17630 9 SGSTGTPKAVVHT-AANLLASAAGLH-SRLGFGGGDSWLLSlplyhvgGLAILVRSLLAGAELVLLERNQALAEDLAPPG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 278 KYRISMV------LLSSSylaifancpeFESADLSSLNYVIFGGSSCSLEV-----QRKVRSRLShdclnfcYGLTELNS 346
Cdd:cd17630 87 VTHVSLVptqlqrLLDSG----------QGPAALKSLRAVLLGGAPIPPELleraaDRGIPLYTT-------YGMTETAS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 347 ---AGSVNlnfDEKPNSVGRAIRGIKIKVIDEqgeaqepnvvGEICFHNSQKWAGYYKNPdeTRQIQDSENWIHTGDLGY 423
Cdd:cd17630 150 qvaTKRPD---GFGRGGVGVLLPGRELRIVED----------GEIWVGGASLAMGYLRGQ--LVPEFNEDGWFTTKDLGE 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 424 VDKDGYLFVIDRLKDMLKY--QNIMyyPSEIENVIAEMPNVLEACVFGIWDPVNGDEAAASLVkkPGTQLEAQDVVEYVR 501
Cdd:cd17630 215 LHADGRLTVLGRADNMIISggENIQ--PEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIV--GRGPADPAELRAWLK 290
|
330 340 350
....*....|....*....|....*....|....*..
gi 281365686 502 KRItAKFKQLNgGALIVDQIVRSGNRKTNRSAVKEHF 538
Cdd:cd17630 291 DKL-ARFKLPK-RIYPVPELPRTGGGKVDRRALRAWL 325
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
335-469 |
3.96e-18 |
|
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: 87.52 E-value: 3.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 335 LNFC--YGLTElNSAGS-VNLNFDEKPNSVGRAIRGIKIKvIDEQGEAQepnvvgeicFHNSQKWAGYYKNPDETRQIQD 411
Cdd:cd05932 300 LNILeaYGMTE-NFAYShLNYPGRDKIGTVGNAGPGVEVR-ISEDGEIL---------VRSPALMMGYYKDPEATAEAFT 368
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 281365686 412 SENWIHTGDLGYVDKDGYLFVIDRLKDMLKYQNIMYY-PSEIENVIAEMPNVLEACVFG 469
Cdd:cd05932 369 ADGFLRTGDKGELDADGNLTITGRVKDIFKTSKGKYVaPAPIENKLAEHDRVEMVCVIG 427
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
199-507 |
1.19e-17 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 86.20 E-value: 1.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 199 LAILS-SSGTSGFPKAVTISnsHKIIVDYMAINNSNIQY---TSSTLDW--CS-------GLSMAITSG---VFSTTSii 262
Cdd:PRK07768 154 LALMQlTSGSTGSPKAVQIT--HGNLYANAEAMFVAAEFdveTDVMVSWlpLFhdmgmvgFLTVPMYFGaelVKVTPM-- 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 263 adcDF--DPGLFCRAIGKYRISMVLLSSSYLAIFA----NCPEFESADLSSLNYVIFGGSSCSLEVQRK-----VRSRLS 331
Cdd:PRK07768 230 ---DFlrDPLLWAELISKYRGTMTAAPNFAYALLArrlrRQAKPGAFDLSSLRFALNGAEPIDPADVEDlldagARFGLR 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 332 HDCLNFCYGLTELNSAGSVN-----LNFDE----------------KPN-----SVGRAIRGIKIKVIDEQGEAQEPNVV 385
Cdd:PRK07768 307 PEAILPAYGMAEATLAVSFSpcgagLVVDEvdadllaalrravpatKGNtrrlaTLGPPLPGLEVRVVDEDGQVLPPRGV 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 386 GEICFHnSQKWAGYYKNPDETRQIQDSENWIHTGDLGYVDKDGYLFVIDRLKDMLkyqnIM----YYPSEIENVIAEMPN 461
Cdd:PRK07768 387 GVIELR-GESVTPGYLTMDGFIPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVI----IMagrnIYPTDIERAAARVEG 461
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 281365686 462 VLEACVFGI-WDPVNGDEAAASLVKKPGTQLEAQdvVEYVRKRITAK 507
Cdd:PRK07768 462 VRPGNAVAVrLDAGHSREGFAVAVESNAFEDPAE--VRRIRHQVAHE 506
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
65-539 |
1.53e-17 |
|
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: 86.00 E-value: 1.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 65 LTREDLHMNAMRVASYMRNMGLGQTDIVGVMGRHTTHQSAVAYACFFNGTPLHALHNAY-EEACIAKLFGITKPRLIFCD 143
Cdd:cd05968 92 LTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFgKEAAATRLQDAEAKALITAD 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 144 G-----------DEYEKvkSATKDLQVTIVTMRNH---PRGSVRIQDVLTTPVMQNFQPLRLKDGIDHTLAILSSSGTSG 209
Cdd:cd05968 172 GftrrgrevnlkEEADK--ACAQCPTVEKVVVVRHlgnDFTPAKGRDLSYDEEKETAGDGAERTESEDPLMIIYTSGTTG 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 210 FPKAVTisNSH-----KIIVDY---MAINNSNIQYTSSTLDWCSGLSMAITSGVFSTTSIIADC--DFD-PGLFCRAIGK 278
Cdd:cd05968 250 KPKGTV--HVHagfplKAAQDMyfqFDLKPGDLLTWFTDLGWMMGPWLIFGGLILGATMVLYDGapDHPkADRLWRMVED 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 279 YRISMVLLSSSYLAIFANCPE--FESADLSSLNYVIFGGSSCSLEVQRK-VRSRLSHDC--LNFCYGlTELnSAGSVNLN 353
Cdd:cd05968 328 HEITHLGLSPTLIRALKPRGDapVNAHDLSSLRVLGSTGEPWNPEPWNWlFETVGKGRNpiINYSGG-TEI-SGGILGNV 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 354 FDE--KPNSVGRAIRGIKIKVIDEQGEAQEPNVvGEICFhnSQKWAGYYKN--PDETRQI----QDSEN-WIHtGDLGYV 424
Cdd:cd05968 406 LIKpiKPSSFNGPVPGMKADVLDESGKPARPEV-GELVL--LAPWPGMTRGfwRDEDRYLetywSRFDNvWVH-GDFAYY 481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 425 DKDGYLFVIDRLKDMLKYQNIMYYPSEIENVIAEMPNVLEACVFGIWDPVNGDEAAASLVKKPG---TQLEAQDVVEYVR 501
Cdd:cd05968 482 DEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVLKPGvtpTEALAEELMERVA 561
|
490 500 510
....*....|....*....|....*....|....*...
gi 281365686 502 KRITAKFKQLNggALIVDQIVRSGNRKTNRSAVKEHFL 539
Cdd:cd05968 562 DELGKPLSPER--ILFVKDLPKTRNAKVMRRVIRAAYL 597
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
66-542 |
3.47e-17 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 84.42 E-value: 3.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 66 TREDLHMNAMRVASYMRNMGLGQTDIVGVMGRHTTHQSAVAYACFFNGTPLHALHNAYEEACIAKLFGITKPRLIFCDGD 145
Cdd:PRK06018 41 TYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVITDLT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 146 ---EYEKVKSATKDLQVTIV-----TM-RNHPRGSVRIQDVLTtpvmQNFQPLRLKDGIDHTLAILS-SSGTSGFPKAVT 215
Cdd:PRK06018 121 fvpILEKIADKLPSVERYVVltdaaHMpQTTLKNAVAYEEWIA----EADGDFAWKTFDENTAAGMCyTSGTTGDPKGVL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 216 ISNSHKIIVDYMAINNSNIQYTSSTL-----------DWcsGLSMaitSGVFSTTSIIAdcdfdPGLFCRAIGKYRismv 284
Cdd:PRK06018 197 YSHRSNVLHALMANNGDALGTSAADTmlpvvplfhanSW--GIAF---SAPSMGTKLVM-----PGAKLDGASVYE---- 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 285 LLSSSYLAIFANCP----------EFESADLSSLNYVIFGGSSCSLEVqrkVRSRLSHDC-LNFCYGLTELNSAGSV--- 350
Cdd:PRK06018 263 LLDTEKVTFTAGVPtvwlmllqymEKEGLKLPHLKMVVCGGSAMPRSM---IKAFEDMGVeVRHAWGMTEMSPLGTLaal 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 351 -----NLNFDEKPNSV---GRAIRGIKIKVIDEQGEAQ--EPNVVGEICFHNSQKWAGYYKNPDEtrqIQDSENWIHTGD 420
Cdd:PRK06018 340 kppfsKLPGDARLDVLqkqGYPPFGVEMKITDDAGKELpwDGKTFGRLKVRGPAVAAAYYRVDGE---ILDDDGFFDTGD 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 421 LGYVDKDGYLFVIDRLKDMLKYQNIMYYPSEIENVIAEMPNVLEACVFGIWDPVNGDEAAASLVKKPGTQLEAQDVVEYV 500
Cdd:PRK06018 417 VATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQLKPGETATREEILKYM 496
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 281365686 501 RKRItAKFkQLNGGALIVDQIVRSGNRKTNRSAVKEHFlKNY 542
Cdd:PRK06018 497 DGKI-AKW-WMPDDVAFVDAIPHTATGKILKTALREQF-KDY 535
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
197-543 |
1.09e-16 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 83.25 E-value: 1.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 197 HTLAILSSSGTSGFPKAVTISN-SHKIIVDY----MAINNSNIQYTS-STLDWCSGLSMAITSGVFSTTSIIADCDFDPG 270
Cdd:PTZ00237 255 HPLYILYTSGTTGNSKAVVRSNgPHLVGLKYywrsIIEKDIPTVVFShSSIGWVSFHGFLYGSLSLGNTFVMFEGGIIKN 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 271 L-----FCRAIGKYRISMVLLSSS---YLaiFANCPEFESA----DLSSLNYVIFGGSSCSLEVQRKVRSRLSHDCLNFc 338
Cdd:PTZ00237 335 KhieddLWNTIEKHKVTHTLTLPKtirYL--IKTDPEATIIrskyDLSNLKEIWCGGEVIEESIPEYIENKLKIKSSRG- 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 339 YGLTELNSAGSVNLNFDEKP-NSVGRAIRGIKIKVIDEQGEAQEPNVVGEICFHNSQK---WAGYYKNPDETRQI-QDSE 413
Cdd:PTZ00237 412 YGQTEIGITYLYCYGHINIPyNATGVPSIFIKPSILSEDGKELNVNEIGEVAFKLPMPpsfATTFYKNDEKFKQLfSKFP 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 414 NWIHTGDLGYVDKDGYLFVIDRLKDMLKYQNIMYYPSEIENVIAEMPNVLEACVFGIWDPVNGDEAAASLVKKPGTQLEA 493
Cdd:PTZ00237 492 GYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPIGLLVLKQDQSNQS 571
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 281365686 494 QDV------VEYVRKRITAKFKQLNgGALIVDQIVRSGNRKTNRSAVKEhFLKNYN 543
Cdd:PTZ00237 572 IDLnklkneINNIITQDIESLAVLR-KIIIVNQLPKTKTGKIPRQIISK-FLNDSN 625
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
196-534 |
4.29e-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: 80.85 E-value: 4.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 196 DHTLAILSSSGTSGFPKAVTISnsHKIIVDYMAINN--SNIQYTSSTLDWcSGLSM-AITSGVFSTTS-------IIADC 265
Cdd:cd17651 136 DDLAYVIYTSGSTGRPKGVVMP--HRSLANLVAWQAraSSLGPGARTLQF-AGLGFdVSVQEIFSTLCagatlvlPPEEV 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 266 DFDPGLFCRAIGKYRISMVLLSSSYLAIFANCPEFESADLSSLNYVIFGGSSCSLEVQ-RKVRSRLSHDCLNFCYGLTE- 343
Cdd:cd17651 213 RTDPPALAAWLDEQRISRVFLPTVALRALAEHGRPLGVRLAALRYLLTGGEQLVLTEDlREFCAGLPGLRLHNHYGPTEt 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 344 -LNSAGSVNLNFDEKP--NSVGRAIRGIKIKVIDEQGEAQEPNVVGEICFHNSQKWAGYYKNPDETRqiqdsENWI---- 416
Cdd:cd17651 293 hVVTALSLPGDPAAWPapPPIGRPIDNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTA-----ERFVpdpf 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 417 -------HTGDLGYVDKDGYLFVIDRLKDMLKYQNIMYYPSEIENVIAEMPNVLEACVFGIWDPVNGDEAAASLVKKPGT 489
Cdd:cd17651 368 vpgarmyRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPEA 447
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 281365686 490 QLEAQDVVEYVRKRITAKFkqLNGGALIVDQIVRSGNRKTNRSAV 534
Cdd:cd17651 448 PVDAAELRAALATHLPEYM--VPSAFVLLDALPLTPNGKLDRRAL 490
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
199-530 |
5.81e-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: 341248 [Multi-domain] Cd Length: 364 Bit Score: 79.35 E-value: 5.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 199 LAILSSSGTSGFPKAVTISN-------------------SHKIIVDYMAINNSNIQYTSSTLDWCSGLSMAITSGVFSTT 259
Cdd:cd05924 6 LYILYTGGTTGMPKGVMWRQedifrmlmggadfgtgeftPSEDAHKAAAAAAGTVMFPAPPLMHGTGSWTAFGGLLGGQT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 260 SIIADCDFDPGLFCRAIGKYRI-SMVLLSSSYLAifancP---EFESA---DLSSLNYVIFGGSSCSLEVQRKVRSRLSH 332
Cdd:cd05924 86 VVLPDDRFDPEEVWRTIEKHKVtSMTIVGDAMAR-----PlidALRDAgpyDLSSLFAISSGGALLSPEVKQGLLELVPN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 333 DCLNFCYGLTELNSAGSVNLnfDEKPNSVG-RAIRGIKIKVIDEQGEAQEP--NVVGEICfHNSQKWAGYYKNPDETRQI 409
Cdd:cd05924 161 ITLVDAFGSSETGFTGSGHS--AGSGPETGpFTRANPDTVVLDDDGRVVPPgsGGVGWIA-RRGHIPLGYYGDEAKTAET 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 410 ---QDSENWIHTGDLGYVDKDGYLFVIDRLKDMLKYQNIMYYPSEIENVIAEMPNVLEACVFGIWDPVNGDEAAASLVKK 486
Cdd:cd05924 238 fpeVDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQEVVAVVQLR 317
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 281365686 487 PGTQLEAQDVVEYVRKRItAKFKqLNGGALIVDQIVRSGNRKTN 530
Cdd:cd05924 318 EGAGVDLEELREHCRTRI-ARYK-LPKQVVFVDEIERSPAGKAD 359
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
194-499 |
7.40e-16 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 80.46 E-value: 7.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 194 GIDHTLAILSSSGTSGFPKAVTISNSHKIIVDYMAINNSNIqyTSSTLDWCS-----------GLSMAITSGV------- 255
Cdd:PRK13388 148 DAMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGRALTERFGL--TRDDVCYVSmplfhsnavmaGWAPAVASGAavalpak 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 256 FSTTSIIADCDFDPGLFCRAIGKyRISMVLLSssylaifancPEF-ESADlSSLNyVIFG---GSSCSLEVQRKVRSRLS 331
Cdd:PRK13388 226 FSASGFLDDVRRYGATYFNYVGK-PLAYILAT----------PERpDDAD-NPLR-VAFGneaSPRDIAEFSRRFGCQVE 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 332 HDclnfcYGLTElnSAGSVNLNFDEKPNSVGRAIRGIKI-----------KVIDEQGEAQEPN-VVGEIC-FHNSQKWAG 398
Cdd:PRK13388 293 DG-----YGSSE--GAVIVVREPGTPPGSIGRGAPGVAIynpetltecavARFDAHGALLNADeAIGELVnTAGAGFFEG 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 399 YYKNPDETRQ-IQDSENWihTGDLGYVDKDGYLFVIDRLKDMLKY--QNIMYYPseIENVIAEMPNVLEACVFGIWDPVN 475
Cdd:PRK13388 366 YYNNPEATAErMRHGMYW--SGDLAYRDADGWIYFAGRTADWMRVdgENLSAAP--IERILLRHPAINRVAVYAVPDERV 441
|
330 340
....*....|....*....|....
gi 281365686 476 GDEAAASLVKKPGTQLEAQDVVEY 499
Cdd:PRK13388 442 GDQVMAALVLRDGATFDPDAFAAF 465
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
339-506 |
8.53e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 80.03 E-value: 8.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 339 YGLTELNSAGSVNLNFDEKPNSVGRAIRGIKIKVIDEQGE--AQEPNVVGEICFHNSQKWAGYYKNPDETRQIQDSENWI 416
Cdd:PRK07787 273 YGMTETLITLSTRADGERRPGWVGLPLAGVETRLVDEDGGpvPHDGETVGELQVRGPTLFDGYLNRPDATAAAFTADGWF 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 417 HTGDLGYVDKDGYLFVIDRLK-DMLKYQNIMYYPSEIENVIAEMPNVLEACVFGIWDPVNGDEAAASLVkkPGTQLEAQD 495
Cdd:PRK07787 353 RTGDVAVVDPDGMHRIVGREStDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVV--GADDVAADE 430
|
170
....*....|.
gi 281365686 496 VVEYVRKRITA 506
Cdd:PRK07787 431 LIDFVAQQLSV 441
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
194-534 |
9.16e-16 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 80.05 E-value: 9.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 194 GIDHTLAILSSSGTSGFPKAVTISNShkiivDYMAINNSNIQYTSSTLDWCSGLSmaiTSGVFSTTSI-----IADCDFD 268
Cdd:PRK05857 167 GSEDPLAMIFTSGTTGEPKAVLLANR-----TFFAVPDILQKEGLNWVTWVVGET---TYSPLPATHIgglwwILTCLMH 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 269 PGLfCRAIGKYRIS-MVLLSSSYLAIFANCP----------EFESADLSSLNYVIFGGSSCSLEVQRKVRS---RLSHdc 334
Cdd:PRK05857 239 GGL-CVTGGENTTSlLEILTTNAVATTCLVPtllsklvselKSANATVPSLRLVGYGGSRAIAADVRFIEAtgvRTAQ-- 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 335 lnfCYGLTElNSAGSVNLNFDE------KPNSVGRAIRGIKIKVIDEQG------EAQEPNVVGEICFHNSQKWAGYYKN 402
Cdd:PRK05857 316 ---VYGLSE-TGCTALCLPTDDgsivkiEAGAVGRPYPGVDVYLAATDGigptapGAGPSASFGTLWIKSPANMLGYWNN 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 403 PDETRQIQdSENWIHTGDLGYVDKDGYLFVIDRLKDMLKYQNIMYYPSEIENVIAEMPNVLEACVFGIWDPVNGdeAAAS 482
Cdd:PRK05857 392 PERTAEVL-IDGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFG--ALVG 468
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 281365686 483 LVKKPGTQLEAQDVVEyVRKRITAKFKQLNGGA------LIVDQIVRSGNRKTNRSAV 534
Cdd:PRK05857 469 LAVVASAELDESAARA-LKHTIAARFRRESEPMarpstiVIVTDIPRTQSGKVMRASL 525
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
205-467 |
1.27e-15 |
|
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: 80.29 E-value: 1.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 205 SGTSGFPKAVTISnsHKIIVDYMAINNSNI---------QYTS-----STLDWCsglsMAITSGVfstTSIIADCD--FD 268
Cdd:COG1020 626 SGSTGRPKGVMVE--HRALVNLLAWMQRRYglgpgdrvlQFASlsfdaSVWEIF----GALLSGA---TLVLAPPEarRD 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 269 PGLFCRAIGKYRISMVLLSSSYLAIFAncpEFESADLSSLNYVIFGGSSCSLEVQRKVRSRLSH-DCLNfCYGLTElnsa 347
Cdd:COG1020 697 PAALAELLARHRVTVLNLTPSLLRALL---DAAPEALPSLRLVLVGGEALPPELVRRWRARLPGaRLVN-LYGPTE---- 768
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 348 GSVN--------LNFDEKPNSVGRAIRGIKIKVIDEQGEAQEPNVVGEICFhnsqkwA------GYYKNPDETRQ----- 408
Cdd:COG1020 769 TTVDstyyevtpPDADGGSVPIGRPIANTRVYVLDAHLQPVPVGVPGELYI------GgaglarGYLNRPELTAErfvad 842
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 281365686 409 --IQDSENWIHTGDLGYVDKDGYLFVIDRLKDMLKyqnIMYY---PSEIENVIAEMPNVLEACV 467
Cdd:COG1020 843 pfGFPGARLYRTGDLARWLPDGNLEFLGRADDQVK---IRGFrieLGEIEAALLQHPGVREAVV 903
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
171-468 |
4.65e-15 |
|
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: 77.35 E-value: 4.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 171 SVRIQDVLTTPVMQnfqpLRLKDGIDHTLA-ILSSSGTSGFPKAVTISnsHKIIVDYMAINNSNI---------QYTSST 240
Cdd:cd17653 83 SARIQAILRTSGAT----LLLTTDSPDDLAyIIFTSGSTGIPKGVMVP--HRGVLNYVSQPPARLdvgpgsrvaQVLSIA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 241 LDWCSGLsmaitsgVFST-----TSIIADCDFDpglFCRAIGKYRISMvlLSSSYLAIFancpefESADLSSLNYVIFGG 315
Cdd:cd17653 157 FDACIGE-------IFSTlcnggTLVLADPSDP---FAHVARTVDALM--STPSILSTL------SPQDFPNLKTIFLGG 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 316 SSCSlevQRKVRSRLSHDCLNFCYGLTELNSAGSVNLNFDEKPNSVGRAIRGIKIKVIDEQGEAQEPNVVGEICFHNSQK 395
Cdd:cd17653 219 EAVP---PSLLDRWSPGRRLYNAYGPTECTISSTMTELLPGQPVTIGKPIPNSTCYILDADLQPVPEGVVGEICISGVQV 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 396 WAGYYKNPDET----RQIQDSENWIH--TGDLGYVDKDGYLFVIDRLKDMLKYQNIMYYPSEIENVI-AEMPNVLEACVF 468
Cdd:cd17653 296 ARGYLGNPALTaskfVPDPFWPGSRMyrTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEVVlQSQPEVTQAAAI 375
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
339-467 |
7.79e-15 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 77.32 E-value: 7.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 339 YGLTELNSAGSVNLNFDEKPNSVGRAIRGIKIKV--IDEQGEAQEPNVVGEICFHNSQKWAGYYKNPDETRQIQDSENWI 416
Cdd:PTZ00216 459 WGLTETVCCGGIQRTGDLEPNAVGQLLKGVEMKLldTEEYKHTDTPEPRGEILLRGPFLFKGYYKQEELTREVLDEDGWF 538
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 281365686 417 HTGDLGYVDKDGYLFVIDRLKDMLKYQNIMYYPSE-IENVIAE----MPNVLeaCV 467
Cdd:PTZ00216 539 HTGDVGSIAANGTLRIIGRVKALAKNCLGEYIALEaLEALYGQnelvVPNGV--CV 592
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
43-533 |
7.85e-15 |
|
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: 76.70 E-value: 7.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 43 IFGDMVN-NPKLIAQISitEDIVLTREDLHMNAMRVASYMRNMGLGQTDIVGVmgrhtthqsavayaCFFNGTPLhalhn 121
Cdd:cd17644 5 LFEEQVErTPDAVAVVF--EDQQLTYEELNTKANQLAHYLQSLGVKSESLVGI--------------CVERSLEM----- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 122 ayeeacIAKLFGITKPrlifcdGDEYekvksatkdlqvtIVTMRNHPRGSVR--IQD----VLTTpvmqnfQPlrlkdgi 195
Cdd:cd17644 64 ------IIGLLAILKA------GGAY-------------VPLDPNYPQERLTyiLEDaqisVLLT------QP------- 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 196 dHTLA-ILSSSGTSGFPKAVTISN------SHKIIVDYMAINNSNI-QYTSSTLD---------WCSGLSMAI-TSGVFS 257
Cdd:cd17644 106 -ENLAyVIYTSGSTGKPKGVMIEHqslvnlSHGLIKEYGITSSDRVlQFASIAFDvaaeeiyvtLLSGATLVLrPEEMRS 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 258 TTSIIADCdfdpglfcraIGKYRISMVLLSSSYLAIFANCPEFESADL-SSLNYVIFGGSSCSLEVQRKVRSRLSHD--C 334
Cdd:cd17644 185 SLEDFVQY----------IQQWQLTVLSLPPAYWHLLVLELLLSTIDLpSSLRLVIVGGEAVQPELVRQWQKNVGNFiqL 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 335 LNfCYGLTELNSAGSV-NLNFDEKPNS----VGRAIRGIKIKVIDEQGEAQEPNVVGEICFHNSQKWAGYYKNPDETRQ- 408
Cdd:cd17644 255 IN-VYGPTEATIAATVcRLTQLTERNItsvpIGRPIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEk 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 409 -IQDS------ENWIHTGDLGYVDKDGYLFVIDRLKDMLKYQNIMYYPSEIENVIAEMPNVLEACVFGIWDPVNGDEAAA 481
Cdd:cd17644 334 fISHPfnssesERLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVA 413
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 281365686 482 SLVKKPGTQLEAQDVVEYVRKR-----ITAKFKQLNGGALivdqivrSGNRKTNRSA 533
Cdd:cd17644 414 YIVPHYEESPSTVELRQFLKAKlpdymIPSAFVVLEELPL-------TPNGKIDRRA 463
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
451-528 |
1.00e-14 |
|
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: 69.11 E-value: 1.00e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281365686 451 EIENVIAEMPNVLEACVFGIWDPVNGDEAAASLVKKPGTQLEAQDVVEYVRKRItAKFKQLNgGALIVDQIVRSGNRK 528
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVELLEEELVAHVREEL-GPYAVPK-EVVFVDELPKTRSGK 76
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
339-469 |
1.07e-14 |
|
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341295 [Multi-domain] Cd Length: 468 Bit Score: 76.63 E-value: 1.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 339 YGLTELNSAGSVNLNFDEKPNSVGRAIRGIKIKVIDEQG-EAQEPNVVGEICFHNSQKWAGYYKNPDETRQIQDSENWIH 417
Cdd:cd17640 244 YGLTETSPVVSARRLKCNVRGSVGRPLPGTEIKIVDPEGnVVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGWFN 323
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 281365686 418 TGDLGYVDKDGYLFVIDRLKD---MLKYQNIMyyPSEIENVIAEMPNVLEACVFG 469
Cdd:cd17640 324 TGDLGWLTCGGELVLTGRAKDtivLSNGENVE--PQPIEEALMRSPFIEQIMVVG 376
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
51-536 |
1.12e-14 |
|
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: 76.60 E-value: 1.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 51 PKLIAQISitEDIVLTREDLHMNAMRVASYMRNMGLGQTDIVGVMGRHTthqsavayacffngtplhalhnayEEACIAk 130
Cdd:cd17655 11 PDHTAVVF--EDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERS------------------------LEMIVG- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 131 LFGITKPrlifcdGDEY---------EKVKSATKDLQVTIVTMRNH-PRGSVRIQDVLttpvMQNFQPLRLKDGID---- 196
Cdd:cd17655 64 ILGILKA------GGAYlpidpdypeERIQYILEDSGADILLTQSHlQPPIAFIGLID----LLDEDTIYHEESENlepv 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 197 ---HTLA-ILSSSGTSGFPKAVTIsnSHKIIVDYM-AINNSNIQYTSSTLDWCSGLS---------MAITSGvfSTTSII 262
Cdd:cd17655 134 sksDDLAyVIYTSGSTGKPKGVMI--EHRGVVNLVeWANKVIYQGEHLRVALFASISfdasvteifASLLSG--NTLYIV 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 263 ADCDFDPG-LFCRAIGKYRISMVLLSSSYLAIFANCPEFESadlSSLNYVIFGGSSCSLEVQRKVRSRLSHDCLNF-CYG 340
Cdd:cd17655 210 RKETVLDGqALTQYIRQNRITIIDLTPAHLKLLDAADDSEG---LSLKHLIVGGEALSTELAKKIIELFGTNPTITnAYG 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 341 LTELN---SAGSVNLNFDEKPN-SVGRAIRGIKIKVIDEQGEAQEPNVVGEICFHNSQKWAGYYKNPDETRQ--IQD--- 411
Cdd:cd17655 287 PTETTvdaSIYQYEPETDQQVSvPIGKPLGNTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEkfVDDpfv 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 412 -SENWIHTGDLGYVDKDGYLFVIDRLKDMLKYQNIMYYPSEIENVIAEMPNVLEACVFGIWDPVNGDEAAASLVKK---P 487
Cdd:cd17655 367 pGERMYRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEkelP 446
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 281365686 488 GTQLE---AQDVVEYVrkrITAKFKQLnggalivDQIVRSGNRKTNRSAVKE 536
Cdd:cd17655 447 VAQLReflARELPDYM---IPSYFIKL-------DEIPLTPNGKVDRKALPE 488
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
59-509 |
1.25e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 76.52 E-value: 1.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 59 ITEDIVLTREDLHMNAMRVASYMRNMGLGQTDIVGVMGRHTTHQSAVAYACFFNGTPLHALHNAYEEACIAKLFGITKPR 138
Cdd:PRK08162 38 IHGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAASIAFMLRHGEAK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 139 LIFCDGDEYEKVKSATKDLQVTIVTM---------RNHPRGSVRIQDVLTT--PvmqNFQPLRLKDGIDhTLAILSSSGT 207
Cdd:PRK08162 118 VLIVDTEFAEVAREALALLPGPKPLVidvddpeypGGRFIGALDYEAFLASgdP---DFAWTLPADEWD-AIALNYTSGT 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 208 SGFPKAVTisnSHKIIVDYMAInnSNIQYTS--------STL------DWCSGLSMAITSGVfsttsIIADCDFDPGLFC 273
Cdd:PRK08162 194 TGNPKGVV---YHHRGAYLNAL--SNILAWGmpkhpvylWTLpmfhcnGWCFPWTVAARAGT-----NVCLRKVDPKLIF 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 274 RAIGKYRISMVLLSSSYLAIFANCPEFESADLSSLNYVIFGGSSCSLEVQRKVRS---RLSHdclnfCYGLTELNSAGSV 350
Cdd:PRK08162 264 DLIREHGVTHYCGAPIVLSALINAPAEWRAGIDHPVHAMVAGAAPPAAVIAKMEEigfDLTH-----VYGLTETYGPATV 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 351 N--------LNFDEKPNSVGRaiRGIK------IKVIDEQGEAQEPN---VVGEICFHNSQKWAGYYKNPDETRQIQDSe 413
Cdd:PRK08162 339 CawqpewdaLPLDERAQLKAR--QGVRyplqegVTVLDPDTMQPVPAdgeTIGEIMFRGNIVMKGYLKNPKATEEAFAG- 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 414 NWIHTGDLGYVDKDGYLFVIDRLKDMLKY--QNImyypS--EIENVIAEMPNVLEACVFGIWDPVNGDEAAASLVKKPGT 489
Cdd:PRK08162 416 GWFHTGDLAVLHPDGYIKIKDRSKDIIISggENI----SsiEVEDVLYRHPAVLVAAVVAKPDPKWGEVPCAFVELKDGA 491
|
490 500
....*....|....*....|
gi 281365686 490 QLEAQDVVEYVRKRItAKFK 509
Cdd:PRK08162 492 SATEEEIIAHCREHL-AGFK 510
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
328-484 |
1.29e-14 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 76.68 E-value: 1.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 328 SRLSHDCLNF---C--------YGLTELNSAGSVNLNFDEKPNSVGRAIRGIKIKVID----EQGEAQEPNVVGEICFHN 392
Cdd:PLN02736 386 SPLSPDVMEFlriCfggrvlegYGMTETSCVISGMDEGDNLSGHVGSPNPACEVKLVDvpemNYTSEDQPYPRGEICVRG 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 393 SQKWAGYYKNPDETRQIQDSENWIHTGDLGYVDKDGYLFVIDRLKDMLKYQNIMYY-PSEIENVIAEMPNVLEACVFgiw 471
Cdd:PLN02736 466 PIIFKGYYKDEVQTREVIDEDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLAQGEYIaPEKIENVYAKCKFVAQCFVY--- 542
|
170
....*....|...
gi 281365686 472 dpvnGDEAAASLV 484
Cdd:PLN02736 543 ----GDSLNSSLV 551
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
201-472 |
1.62e-14 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 76.38 E-value: 1.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 201 ILSSSGTSGFPKAVTISNSHKI--------IVDYmaiNNSNIQYTSSTLDWCSGLSMAITSGVFSTTSIIADcDFDPGLF 272
Cdd:PLN02860 177 ICFTSGTTGRPKGVTISHSALIvqslakiaIVGY---GEDDVYLHTAPLCHIGGLSSALAMLMVGACHVLLP-KFDAKAA 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 273 CRAIGKYRISMVLLSSSYLA--IFANCPEFESADLSSLNYVIFGGSSCSLEVQRKVRSRLSHDCLNFCYGLTE------- 343
Cdd:PLN02860 253 LQAIKQHNVTSMITVPAMMAdlISLTRKSMTWKVFPSVRKILNGGGSLSSRLLPDAKKLFPNAKLFSAYGMTEacssltf 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 344 -------LNSAGSVNLNFDEKPNS---------VGRAIRGIKIKVideqgEAQEPNVVGEICFHNSQKWAGYYKNPDETR 407
Cdd:PLN02860 333 mtlhdptLESPKQTLQTVNQTKSSsvhqpqgvcVGKPAPHVELKI-----GLDESSRVGRILTRGPHVMLGYWGQNSETA 407
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281365686 408 QIQDSENWIHTGDLGYVDKDGYLFVIDRLKDMLKY--QNImyYPSEIENVIAEMPNVLEACVFGIWD 472
Cdd:PLN02860 408 SVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTggENV--YPEEVEAVLSQHPGVASVVVVGVPD 472
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
204-506 |
1.71e-14 |
|
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 75.85 E-value: 1.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 204 SSGTSGFPKAVTISNsHKII-----VDYMAIN-NSNIQYTSSTLDWCSGLSMAITSGVFSTTSIIADCDFDPGLFCRAIG 277
Cdd:cd05940 89 TSGTTGLPKAAIISH-RRAWrggafFAGSGGAlPSDVLYTCLPLYHSTALIVGWSACLASGATLVIRKKFSASNFWDDIR 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 278 KYRISMVLLSSSYLAIFANCPEFESADLSSLNYVIfgGSSCSLEVQRKVRSRLS-HDCLNFcYGLTELNSAgsvNLNFDE 356
Cdd:cd05940 168 KYQATIFQYIGELCRYLLNQPPKPTERKHKVRMIF--GNGLRPDIWEEFKERFGvPRIAEF-YAATEGNSG---FINFFG 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 357 KPNSVGRA----IRGIKIKVIDEQGEAQEP-------------NVVGEICFHNSQKWA--GYYKNPDETRQI-----QDS 412
Cdd:cd05940 242 KPGAIGRNpsllRKVAPLALVKYDLESGEPirdaegrcikvprGEPGLLISRINPLEPfdGYTDPAATEKKIlrdvfKKG 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 413 ENWIHTGDLGYVDKDGYLFVIDRLKDMLKYQNIMYYPSEIENVIAEMPNVLEACVFGIWDP-VNGDEAAASLVKKPGTQL 491
Cdd:cd05940 322 DAWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQVPgTDGRAGMAAIVLQPNEEF 401
|
330
....*....|....*
gi 281365686 492 EAQDVVEYVRKRITA 506
Cdd:cd05940 402 DLSALAAHLEKNLPG 416
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
269-535 |
1.71e-14 |
|
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.
Pssm-ID: 341268 [Multi-domain] Cd Length: 439 Bit Score: 75.59 E-value: 1.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 269 PGLFCRAIGKYRIS-MVLLSSSYLAIFANcPEFESADLSSLNYVIFGGSSCSLEVQRKVRSRLSHDCLNfCYGLTELNSA 347
Cdd:cd05958 176 PDLLLSAIARYKPTvLFTAPTAYRAMLAH-PDAAGPDLSSLRKCVSAGEALPAALHRAWKEATGIPIID-GIGSTEMFHI 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 348 GSVNLNFDEKPNSVGRAIRGIKIKVIDEQGEAQEPNVVGEICFhnsQKWAGYYKNPDETRQIQDSENWIHTGDLGYVDKD 427
Cdd:cd05958 254 FISARPGDARPGATGKPVPGYEAKVVDDEGNPVPDGTIGRLAV---RGPTGCRYLADKRQRTYVQGGWNITGDTYSRDPD 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 428 GYLFVIDRLKDMLKYQNIMYYPSEIENVIAEMPNVLEACVFGIWDPVNGDEAAASLVKKPG---TQLEAQDVVEYVrKRI 504
Cdd:cd05958 331 GYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGvipGPVLARELQDHA-KAH 409
|
250 260 270
....*....|....*....|....*....|.
gi 281365686 505 TAKFKQLNgGALIVDQIVRSGNRKTNRSAVK 535
Cdd:cd05958 410 IAPYKYPR-AIEFVTELPRTATGKLQRFALR 439
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
268-509 |
2.18e-14 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 75.80 E-value: 2.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 268 DPG-LFC-RAIGKYRISMVLLSSSYLAIF--ANCPEFESADLSSLNYVIFGGSSCSLEVQRKVRSRLShdC-LNFCYGLT 342
Cdd:PRK10946 258 DPSaTLCfPLIEKHQVNVTALVPPAVSLWlqAIAEGGSRAQLASLKLLQVGGARLSETLARRIPAELG--CqLQQVFGMA 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 343 ElnsaGSVNLN-FDEKP----NSVGRAIRGI-KIKVIDEQGEAQEPNVVGEICFHNSQKWAGYYKNPDETRQIQDSENWI 416
Cdd:PRK10946 336 E----GLVNYTrLDDSDerifTTQGRPMSPDdEVWVADADGNPLPQGEVGRLMTRGPYTFRGYYKSPQHNASAFDANGFY 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 417 HTGDLGYVDKDGYLFVIDRLKDMLKYQNIMYYPSEIENVIAEMPNVLEACVFGIWDPVNGDEAAASLV-KKPgtqLEAQD 495
Cdd:PRK10946 412 CSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAFLVvKEP---LKAVQ 488
|
250
....*....|....
gi 281365686 496 VVEYVRKRITAKFK 509
Cdd:PRK10946 489 LRRFLREQGIAEFK 502
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
196-533 |
5.37e-14 |
|
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: 74.28 E-value: 5.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 196 DHTLAILSSSGTSGFPKAVtisnshkiivdymAINNSNiqyTSSTLDWCSG-LSMAITSGVFSTTSIIADCD-FDpgLFC 273
Cdd:cd12115 105 DDLAYVIYTSGSTGRPKGV-------------AIEHRN---AAAFLQWAAAaFSAEELAGVLASTSICFDLSvFE--LFG 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 274 R-AIGkyriSMVLLSSSYLAIFANcPEFESADL------------------SSLNYVIFGGSSCSLEVQRKVRSRLSHDC 334
Cdd:cd12115 167 PlATG----GKVVLADNVLALPDL-PAAAEVTLintvpsaaaellrhdalpASVRVVNLAGEPLPRDLVQRLYARLQVER 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 335 LNFCYGLTELN--SAGSVNLNFDEKPNSVGRAIRGIKIKVIDEQGEAQEPNVVGEICFHNSQKWAGYYKNPDETRQ---- 408
Cdd:cd12115 242 VVNLYGPSEDTtySTVAPVPPGASGEVSIGRPLANTQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAErflp 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 409 --IQDSENWIHTGDLGYVDKDGYLFVIDRLKDMLKYQNIMYYPSEIENVIAEMPNVLEACVFGIWDPVNGDEAAASLVKK 486
Cdd:cd12115 322 dpFGPGARLYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAE 401
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 281365686 487 PGTQLEAQDVVEYVRKRITAKFkqLNGGALIVDQIVRSGNRKTNRSA 533
Cdd:cd12115 402 PGAAGLVEDLRRHLGTRLPAYM--VPSRFVRLDALPLTPNGKIDRSA 446
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
59-534 |
7.96e-14 |
|
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: 73.66 E-value: 7.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 59 ITEDIVLTREDLHMNAMRVASYMRNMGLGQTDIVGVMgrhtTHQSAvayacffngtplhalhnayeeACIAKLFGITKPR 138
Cdd:cd17656 8 VFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIM----MERSA---------------------EMIVGILGILKAG 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 139 LIFCDGD-EY--EKVKSATKDLQVTIVTMRNHprgsvriqdvLTTPVMQNFQPLRLKDGI---------------DHTLA 200
Cdd:cd17656 63 GAFVPIDpEYpeERRIYIMLDSGVRVVLTQRH----------LKSKLSFNKSTILLEDPSisqedtsnidyinnsDDLLY 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 201 ILSSSGTSGFPKAV-----TISNSHKIIVDYMAINNSN--IQYTSSTLD---------WCSGLSMAITSgvfsttsiiAD 264
Cdd:cd17656 133 IIYTSGTTGKPKGVqlehkNMVNLLHFEREKTNINFSDkvLQFATCSFDvcyqeifstLLSGGTLYIIR---------EE 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 265 CDFD-PGLFcRAIGKYRISMVLLSSSYLAIFANCPEFESADLSSLNYVIFGGSSCSL--EVQRKVRSRLSHdcLNFCYGL 341
Cdd:cd17656 204 TKRDvEQLF-DLVKRHNIEVVFLPVAFLKFIFSEREFINRFPTCVKHIITAGEQLVItnEFKEMLHEHNVH--LHNHYGP 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 342 TELNSAGSVNLNF-DEKPN--SVGRAIRGIKIKVIDEQGEAQEPNVVGEICFHNSQKWAGYYKNPDETRQ------IQDS 412
Cdd:cd17656 281 SETHVVTTYTINPeAEIPElpPIGKPISNTWIYILDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEkffpdpFDPN 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 413 ENWIHTGDLGYVDKDGYLFVIDRLKDMLKYQNIMYYPSEIENVIAEMPNVLEACVFGIWDPVNGDEAAA---SLVKKPGT 489
Cdd:cd17656 361 ERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAyfvMEQELNIS 440
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 281365686 490 QLE---AQDVVEYVrkrITAKFKQLnggalivDQIVRSGNRKTNRSAV 534
Cdd:cd17656 441 QLReylAKQLPEYM---IPSFFVPL-------DQLPLTPNGKVDRKAL 478
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
402-535 |
8.96e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 73.15 E-value: 8.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 402 NPDETrQIQDSENWIHTGDLGYVDKDGYLFVIDRLKDMLKYQNIMYYPSEIENVIAEMPNVLEACVFGIWDPVNGDEAAA 481
Cdd:PRK08308 280 APEEI-VVKMGDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKA 358
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 281365686 482 SLVKKpgTQLEAQDVVEYVRKRITAkfKQLNGGALIVDQIVRSGNRKTNRSAVK 535
Cdd:PRK08308 359 KVISH--EEIDPVQLREWCIQHLAP--YQVPHEIESVTEIPKNANGKVSRKLLE 408
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
189-538 |
1.04e-13 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 72.77 E-value: 1.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 189 LRLKDGIDHTLA-ILSSSGTSGFPKAVTISNSHKIivdymAINNSNIQYTSSTLDW--------CSGLSMAITSGVFSTT 259
Cdd:PRK07824 27 LRVGEPIDDDVAlVVATSGTTGTPKGAMLTAAALT-----ASADATHDRLGGPGQWllalpahhIAGLQVLVRSVIAGSE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 260 SIIADCD--FDPGLFCRAIGKYR-----ISMVllsSSYLAIFANCPEfESADLSSLNYVIFGGSSCSLEVQRK------- 325
Cdd:PRK07824 102 PVELDVSagFDPTALPRAVAELGggrryTSLV---PMQLAKALDDPA-ATAALAELDAVLVGGGPAPAPVLDAaaaagin 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 326 -VRSrlshdclnfcYGLTElNSAGSVnlnFDekpnsvGRAIRGIKIKVIDEQGEAQEPNVvgeicfhnsqkwAGYYKNPD 404
Cdd:PRK07824 178 vVRT----------YGMSE-TSGGCV---YD------GVPLDGVRVRVEDGRIALGGPTL------------AKGYRNPV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 405 ETRQIQDsENWIHTGDLGYVDkDGYLFVIDRLKDMLKYQNIMYYPSEIENVIAEMPNVLEACVFGIWDPVNGDEAAASLV 484
Cdd:PRK07824 226 DPDPFAE-PGWFRTDDLGALD-DGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAVV 303
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 281365686 485 KKPGTQLEAQDVVEYVRKRI--TAKFKQLNggalIVDQIVRSGNRKTNRSAVKEHF 538
Cdd:PRK07824 304 GDGGPAPTLEALRAHVARTLdrTAAPRELH----VVDELPRRGIGKVDRRALVRRF 355
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
357-504 |
1.06e-13 |
|
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: 73.75 E-value: 1.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 357 KPNSVGRAIRGIKIKVIDEQGEAQEPNVVGEICFhnSQKWAGY----YKNPDETRQI--QDSENWIHTGDLGYVDKDGYL 430
Cdd:cd05966 408 KPGSATRPFFGIEPAILDEEGNEVEGEVEGYLVI--KRPWPGMartiYGDHERYEDTyfSKFPGYYFTGDGARRDEDGYY 485
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 431 FVIDRLKDMLkyqNIMYY---PSEIENVIAEMPNVLEACVFGIWDPVNGDEAAASLVKKPGTQLE---AQDVVEYVRKRI 504
Cdd:cd05966 486 WITGRVDDVI---NVSGHrlgTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGEEPSdelRKELRKHVRKEI 562
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
196-503 |
1.16e-13 |
|
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: 73.06 E-value: 1.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 196 DHTLAILSSSGTSGFPKAVT-----ISNSHKIIVDYMAINNSN--IQYTS-----STLDWCsglsMAITSGvfsTTSIIA 263
Cdd:cd17652 93 DNLAYVIYTSGSTGRPKGVVvthrgLANLAAAQIAAFDVGPGSrvLQFASpsfdaSVWELL----MALLAG---ATLVLA 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 264 DC-DFDPGL-FCRAIGKYRISMVLLSSSYLAIFancpefESADLSSLNYVIFGGSSCSLE-VQRKVRSRlshDCLNfCYG 340
Cdd:cd17652 166 PAeELLPGEpLADLLREHRITHVTLPPAALAAL------PPDDLPDLRTLVVAGEACPAElVDRWAPGR---RMIN-AYG 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 341 LTELN-SAGSVNLNFDEKPNSVGRAIRGIKIKVIDEQGEAQEPNVVGEICFHNSQKWAGYYKNPDET--RQIQD-----S 412
Cdd:cd17652 236 PTETTvCATMAGPLPGGGVPPIGRPVPGTRVYVLDARLRPVPPGVPGELYIAGAGLARGYLNRPGLTaeRFVADpfgapG 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 413 ENWIHTGDLGYVDKDGYLFVIDRLKDMLKYQNIMYYPSEIENVIAEMPNVLEACVfGIWDPVNGDEA-AASLVKKPGTQL 491
Cdd:cd17652 316 SRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVV-VVRDDRPGDKRlVAYVVPAPGAAP 394
|
330
....*....|..
gi 281365686 492 EAQDVVEYVRKR 503
Cdd:cd17652 395 TAAELRAHLAER 406
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
360-533 |
1.36e-13 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 74.05 E-value: 1.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 360 SVGRAIRGIKIKVIDEQ-GEAQEPNVVGEIcfhnsqkWA-------GYYKNPDETRQI---QDSENWIHTGDLGYVdKDG 428
Cdd:PRK05691 371 SCGRSQPGHAVLIVDPQsLEVLGDNRVGEI-------WAsgpsiahGYWRNPEASAKTfveHDGRTWLRTGDLGFL-RDG 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 429 YLFVIDRLKDML--KYQNImyYPSEIENVIAEMPNVL---EACVFGIWDpvNGDEA---AASLVKKPGTQLEAQDVVEYV 500
Cdd:PRK05691 443 ELFVTGRLKDMLivRGHNL--YPQDIEKTVEREVEVVrkgRVAAFAVNH--QGEEGigiAAEISRSVQKILPPQALIKSI 518
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 281365686 501 RKRITAKFKQ-------LNGGALivdqiVRSGNRKTNRSA 533
Cdd:PRK05691 519 RQAVAEACQEapsvvllLNPGAL-----PKTSSGKLQRSA 553
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
308-469 |
1.45e-13 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 73.31 E-value: 1.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 308 LNYVIFGGSSCSLEVQRKVRSrlshDCLNFC---YGLTElnSAGSVNLNFDEKPNSVGR-----AIRGIKIKVIDEQGea 379
Cdd:PLN02430 385 LRLLISGGAPLSTEIEEFLRV----TSCAFVvqgYGLTE--TLGPTTLGFPDEMCMLGTvgapaVYNELRLEEVPEMG-- 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 380 QEP---NVVGEICFHNSQKWAGYYKNPDETRQIQdSENWIHTGDLGYVDKDGYLFVIDRLKDMLKYQNIMYYPSE-IENV 455
Cdd:PLN02430 457 YDPlgePPRGEICVRGKCLFSGYYKNPELTEEVM-KDGWFHTGDIGEILPNGVLKIIDRKKNLIKLSQGEYVALEyLENV 535
|
170
....*....|....
gi 281365686 456 IAEMPNVLEACVFG 469
Cdd:PLN02430 536 YGQNPIVEDIWVYG 549
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
76-502 |
2.21e-13 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 72.74 E-value: 2.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 76 RVASYMRNMGLGQTDIVGVMGRHTTHQSAVAYACFFNGTPLHALHNAYEEACIAKLFGITKPRLIFCDgDEYEKVKSATK 155
Cdd:PLN03102 51 RLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFVD-RSFEPLAREVL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 156 DLQVTIVTMRNHPRGSVRIQDVLTTP---------VMQNFQP--------LRLKDGIDhTLAILSSSGTSGFPKAVTISN 218
Cdd:PLN03102 130 HLLSSEDSNLNLPVIFIHEIDFPKRPsseeldyecLIQRGEPtpslvarmFRIQDEHD-PISLNYTSGTTADPKGVVISH 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 219 SHKiivdYMAINNSNIQYTSSTLD---W------CSGLSMAITSGVFSTTSIIADCDFDPGLFcRAIGKYRISMVLLSSS 289
Cdd:PLN03102 209 RGA----YLSTLSAIIGWEMGTCPvylWtlpmfhCNGWTFTWGTAARGGTSVCMRHVTAPEIY-KNIEMHNVTHMCCVPT 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 290 YLAIFANCPEFESADLSSLNYVIFGGSSCSLEVQRKVRsRLSHDCLNfCYGLTElnSAGSVNlnFDEKPNSVGRAIRGIK 369
Cdd:PLN03102 284 VFNILLKGNSLDLSPRSGPVHVLTGGSPPPAALVKKVQ-RLGFQVMH-AYGLTE--ATGPVL--FCEWQDEWNRLPENQQ 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 370 IKVIDEQG--------------EAQEP-----NVVGEICFHNSQKWAGYYKNPDETRQiQDSENWIHTGDLGYVDKDGYL 430
Cdd:PLN03102 358 MELKARQGvsilgladvdvknkETQESvprdgKTMGEIVIKGSSIMKGYLKNPKATSE-AFKHGWLNTGDVGVIHPDGHV 436
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281365686 431 FVIDRLKDMLKYQNIMYYPSEIENVIAEMPNVLEACVFGIWDPVNGDEAAASLVKKPGTQLEAQDVVEYVRK 502
Cdd:PLN03102 437 EIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGETTKEDRVDKLVTR 508
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
362-543 |
2.36e-13 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 72.73 E-value: 2.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 362 GRAIRGIKIKVIDEQGEAQEPNVVGEICFHNSQKWAGYYKNPDETRQIqDSENWIHTGDLGYVdKDGYLFVIDRLKDM-- 439
Cdd:PRK09192 388 GKALPGHEIEIRNEAGMPLPERVVGHICVRGPSLMSGYFRDEESQDVL-AADGWLDTGDLGYL-LDGYLYITGRAKDLii 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 440 LKYQNImyYPSEIENVIAEMPNVL--EACVFGIWDPvnGDEAAASLVKKPGTQLEAQdvvEYVRKRITAKFKQLNGGALI 517
Cdd:PRK09192 466 INGRNI--WPQDIEWIAEQEPELRsgDAAAFSIAQE--NGEKIVLLVQCRISDEERR---GQLIHALAALVRSEFGVEAA 538
|
170 180 190
....*....|....*....|....*....|.
gi 281365686 518 VD-----QIVRSGNRKTNRSAVKEHFLKNYN 543
Cdd:PRK09192 539 VElvpphSLPRTSSGKLSRAKAKKRYLSGAF 569
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
59-533 |
3.06e-13 |
|
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: 71.92 E-value: 3.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 59 ITEDIVLTREDLHMNAMRVASYMRNMGLGQTDIVGVMGRHTTHQSAVAYACFFNGTPLHALHNAYEEACIAKLFGITKPR 138
Cdd:cd17646 18 VDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRLAYMLADAGPA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 139 LIFCDGDEyekVKSATKDLQVTIVTMRNHPRGSVRIQDVLTTPvmqnfqplrlkdgiDHTLAILSSSGTSGFPKAVTISn 218
Cdd:cd17646 98 VVLTTADL---AARLPAGGDVALLGDEALAAPPATPPLVPPRP--------------DNLAYVIYTSGSTGRPKGVMVT- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 219 sHKIIVDYMAINNSNI---------QYTSSTLD---WcsGLSMAITSGvfsTTSIIADCDF--DPGLFCRAIGKYRISMV 284
Cdd:cd17646 160 -HAGIVNRLLWMQDEYplgpgdrvlQKTPLSFDvsvW--ELFWPLVAG---ARLVVARPGGhrDPAYLAALIREHGVTTC 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 285 LLSSSYLAIFANCPEFESADlsSLNYVIFGGSSCSLEVQRKVRSRLSHDCLNFcYGLTELN---SAGSVNLNFDEKPNSV 361
Cdd:cd17646 234 HFVPSMLRVFLAEPAAGSCA--SLRRVFCSGEALPPELAARFLALPGAELHNL-YGPTEAAidvTHWPVRGPAETPSVPI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 362 GRAIRGIKIKVIDEQGEAQEPNVVGEICFHNSQKWAGYYKNPDET--RQIQD----SENWIHTGDLGYVDKDGYLFVIDR 435
Cdd:cd17646 311 GRPVPNTRLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTaeRFVPDpfgpGSRMYRTGDLARWRPDGALEFLGR 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 436 LKDMLKYQNIMYYPSEIENVIAEMPNVLEACVFGIWDPVNGDEAAASLVKKPGTQLEAQDVV-EYVRKR-----ITAKFK 509
Cdd:cd17646 391 SDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAAGAAGPDTAALrAHLAERlpeymVPAAFV 470
|
490 500
....*....|....*....|....
gi 281365686 510 QLnggalivDQIVRSGNRKTNRSA 533
Cdd:cd17646 471 VL-------DALPLTANGKLDRAA 487
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
65-427 |
3.42e-13 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 72.00 E-value: 3.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 65 LTREDLHMNAMRVASYMRNMGLGQTDIVGVMGRHTTHQSAVAYACFFNGTPLHALHNAY-----EEACIAKLFGITKPRL 139
Cdd:PRK12582 81 VTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAGVPAAPVSPAYslmshDHAKLKHLFDLVKPRV 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 140 IFC-DGDEYEKVKSATKDLQVTIVTMRNHP--RGSVRIQDVLTTPVMQNFQPLRLKDGIDHTLAILSSSGTSGFPKAVTi 216
Cdd:PRK12582 161 VFAqSGAPFARALAALDLLDVTVVHVTGPGegIASIAFADLAATPPTAAVAAAIAAITPDTVAKYLFTSGSTGMPKAVI- 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 217 sNSHKIivdyMAinnSNIQYTSST------------LDW-----CSG----LSMAITSGvfsTTSIIADCDFDPGLFCRA 275
Cdd:PRK12582 240 -NTQRM----MC---ANIAMQEQLrprepdppppvsLDWmpwnhTMGgnanFNGLLWGG---GTLYIDDGKPLPGMFEET 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 276 IGKYR-ISMVLLSSSYLAIFANCPEFESAD------LSSLNYVIFGGSSCSLEVQRK-----VRSRLSHDCLNFCYGLTE 343
Cdd:PRK12582 309 IRNLReISPTVYGNVPAGYAMLAEAMEKDDalrrsfFKNLRLMAYGGATLSDDLYERmqalaVRTTGHRIPFYTGYGATE 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 344 lnSAG-SVNLNFD-EKPNSVGRAIRGIKIKVIdEQGEAQEPNVVGEICFhnsqkwAGYYKNPDETRQIQDSENWIHTGDL 421
Cdd:PRK12582 389 --TAPtTTGTHWDtERVGLIGLPLPGVELKLA-PVGDKYEVRVKGPNVT------PGYHKDPELTAAAFDEEGFYRLGDA 459
|
....*..
gi 281365686 422 G-YVDKD 427
Cdd:PRK12582 460 ArFVDPD 466
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
305-542 |
5.47e-13 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 71.28 E-value: 5.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 305 LSSLNYVIFGGSSCSLEVQRKVRSRLSHDCLNfCYGLTELNSAGSV--------NLNFDEKPNSV---GRAIRGIKIKVI 373
Cdd:PRK07008 292 FSTLRRTVIGGSACPPAMIRTFEDEYGVEVIH-AWGMTEMSPLGTLcklkwkhsQLPLDEQRKLLekqGRVIYGVDMKIV 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 374 DEQGEAQEPNVVGEICFHNSQKW--AGYYKNpdETRQIQDSenWIHTGDLGYVDKDGYLFVIDRLKDMLKYQNIMYYPSE 451
Cdd:PRK07008 371 GDDGRELPWDGKAFGDLQVRGPWviDRYFRG--DASPLVDG--WFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSID 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 452 IENVIAEMPNVLEACVFGIWDPVNGDEAAASLVKKPGTQLEAQDVVEYVRKRiTAKFkQLNGGALIVDQIVRSGNRKTNR 531
Cdd:PRK07008 447 IENVAVAHPAVAEAACIACAHPKWDERPLLVVVKRPGAEVTREELLAFYEGK-VAKW-WIPDDVVFVDAIPHTATGKLQK 524
|
250
....*....|.
gi 281365686 532 SAVKEHFlKNY 542
Cdd:PRK07008 525 LKLREQF-RDY 534
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
382-541 |
6.67e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 71.13 E-value: 6.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 382 PNVVGEICFHNSQKWAGYYKNPDETR-----QIQD-SEN-----WIHTGDLGYVDkDGYLFVIDRLKDMLkyqnIMY--- 447
Cdd:PRK05850 394 AGTVGEIWVHGDNVAAGYWQKPEETErtfgaTLVDpSPGtpegpWLRTGDLGFIS-EGELFIVGRIKDLL----IVDgrn 468
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 448 -YPSEIENVIAEmpnVLEACVFGIWDPVNGDE---AAASLVKKPGTQLEAQDVVEYVRKRITAKFKQLNGgaLIVDQIV- 522
Cdd:PRK05850 469 hYPDDIEATIQE---ITGGRVAAISVPDDGTEklvAIIELKKRGDSDEEAMDRLRTVKREVTSAISKSHG--LSVADLVl 543
|
170 180
....*....|....*....|....*...
gi 281365686 523 ---------RSGnrKTNRSAVKEHFLKN 541
Cdd:PRK05850 544 vapgsipitTSG--KIRRAACVEQYRQD 569
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
201-504 |
8.62e-13 |
|
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: 70.51 E-value: 8.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 201 ILSSSGTSGFPKAVTISnsHKIIVD--------YMAINNSN---IQYTSSTLD-WCSGLSMAITSGvfSTTSIIADCD-F 267
Cdd:cd17648 99 AIYTSGTTGKPKGVLVE--HGSVVNlrtslserYFGRDNGDeavLFFSNYVFDfFVEQMTLALLNG--QKLVVPPDEMrF 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 268 DPGLFCRAIGKYRISMVLLSSSYLAifancpEFESADLSSLNYVIFGGSSCSLEVQRKVRSRLSHDCLNfCYGLTELnSA 347
Cdd:cd17648 175 DPDRFYAYINREKVTYLSGTPSVLQ------QYDLARLPHLKRVDAAGEEFTAPVFEKLRSRFAGLIIN-AYGPTET-TV 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 348 GSVNLNF---DEKPNSVGRAIRGIKIKVIDEQGEAQEPNVVGEICFHNSQKWAGYYKNPDETRQ------------IQDS 412
Cdd:cd17648 247 TNHKRFFpgdQRFDKSLGRPVRNTKCYVLNDAMKRVPVGAVGELYLGGDGVARGYLNRPELTAErflpnpfqteqeRARG 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 413 EN--WIHTGDLGYVDKDGYLFVIDRLKDMLKYQNIMYYPSEIENVIAEMPNVLEACVFGIWDPVNGDEAAAS-----LVK 485
Cdd:cd17648 327 RNarLYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAKEDASQAQSRIQKylvgyYLP 406
|
330
....*....|....*....
gi 281365686 486 KPGTqLEAQDVVEYVRKRI 504
Cdd:cd17648 407 EPGH-VPESDLLSFLRAKL 424
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
62-537 |
1.67e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 69.91 E-value: 1.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 62 DIVLTREDLHMNAMRVASYMRNMGLGQTDIVGVMGRHTTHQSAVAYACF------FNgtplhaLHNAYEEACIAKLFGIT 135
Cdd:PRK07798 26 DRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFkaravpVN------VNYRYVEDELRYLLDDS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 136 KPRLIFCD---GDEYEKVKSATKDLQVTIV----TMRNHPRGSVRIQDVLTTPvmqnfQPLRlkDGIDHT---LAILSSS 205
Cdd:PRK07798 100 DAVALVYErefAPRVAEVLPRLPKLRTLVVvedgSGNDLLPGAVDYEDALAAG-----SPER--DFGERSpddLYLLYTG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 206 GTSGFPKAV---------------------TISNSHKIiVDYMAINNSNIQYTSSTLDWCSGLS---MAITSGvfSTTSI 261
Cdd:PRK07798 173 GTTGMPKGVmwrqedifrvllggrdfatgePIEDEEEL-AKRAAAGPGMRRFPAPPLMHGAGQWaafAALFSG--QTVVL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 262 IADCDFDPGLFCRAIGKYRISMVLLSSSYLA--IFANCPEFESADLSSLNYVIFGGSSCSLEVQRKVRSRLSHDCLNFCY 339
Cdd:PRK07798 250 LPDVRFDADEVWRTIEREKVNVITIVGDAMArpLLDALEARGPYDLSSLFAIASGGALFSPSVKEALLELLPNVVLTDSI 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 340 GLTELNSAGSVNLNFDEKPNSVGRAIRGIKIKVIDEQGEAQEP--NVVGEIcfhnsqkwA-------GYYKNPDETRQI- 409
Cdd:PRK07798 330 GSSETGFGGSGTVAKGAVHTGGPRFTIGPRTVVLDEDGNPVEPgsGEIGWI--------ArrghiplGYYKDPEKTAETf 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 410 --QDSENWIHTGDLGYVDKDGYLFVIDRlkDML-------KYqnimyYPSEIENVIAEMPNVLEACVFGIWDPVNGDEAA 480
Cdd:PRK07798 402 ptIDGVRYAIPGDRARVEADGTITLLGR--GSVcintggeKV-----FPEEVEEALKAHPDVADALVVGVPDERWGQEVV 474
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 481 ASLVKKPGTQLEAQDVVEYVRKRItAKFK---QLnggaLIVDQIVRSGNRKTNRSAVKEH 537
Cdd:PRK07798 475 AVVQLREGARPDLAELRAHCRSSL-AGYKvprAI----WFVDEVQRSPAGKADYRWAKEQ 529
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
267-511 |
2.67e-12 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 68.75 E-value: 2.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 267 FDPGLFCRAIGKYRISMVLLSSSYLAIFANcpefesADLSS----LNYVIFGGSSCSLEVQRKVRsRLSHDCLNFCYGLT 342
Cdd:cd05974 163 FDAKRVLAALVRYGVTTLCAPPTVWRMLIQ------QDLASfdvkLREVVGAGEPLNPEVIEQVR-RAWGLTIRDGYGQT 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 343 EL-----NSAGSVnlnfdEKPNSVGRAIRGIKIKVIDEQG-EAQEpnvvGEICF-----HNSQKWAGYYKNPDETRQIQD 411
Cdd:cd05974 236 ETtalvgNSPGQP-----VKAGSMGRPLPGYRVALLDPDGaPATE----GEVALdlgdtRPVGLMKGYAGDPDKTAHAMR 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 412 SENWiHTGDLGYVDKDGYLFVIDRLKDMLKYQNIMYYPSEIENVIAEMPNVLEACVFGIWDPVNGDEAAASLVKKPGTQL 491
Cdd:cd05974 307 GGYY-RTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGYEP 385
|
250 260
....*....|....*....|...
gi 281365686 492 E---AQDVVEYVRKRItAKFKQL 511
Cdd:cd05974 386 SpetALEIFRFSRERL-APYKRI 407
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
307-504 |
3.83e-12 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 68.66 E-value: 3.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 307 SLNYVIFGGSSCSLEVQRKVRSRLSHDCLNfCYGLTELNSAGSV-----------NLNFDEkpnSVGRAIRGIKIKVIDE 375
Cdd:PRK05620 299 SLQEIYVGGSAVPPILIKAWEERYGVDVVH-VWGMTETSPVGTVarppsgvsgeaRWAYRV---SQGRFPASLEYRIVND 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 376 qGEAQEPN--VVGEICFHNSQKWAGYYKNPDET----------RQIQD------SENWIHTGDLGYVDKDGYLFVIDRLK 437
Cdd:PRK05620 375 -GQVMESTdrNEGEIQVRGNWVTASYYHSPTEEgggaastfrgEDVEDandrftADGWLRTGDVGSVTRDGFLTIHDRAR 453
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 438 DMLKYQNIMYYPSEIENVIAEMPNVLEACVFGIWDPVNGDEAAASLVKKPG---TQLEAQDVVEYVRKRI 504
Cdd:PRK05620 454 DVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLAVTVLAPGiepTRETAERLRDQLRDRL 523
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
201-467 |
4.33e-12 |
|
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: 68.26 E-value: 4.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 201 ILSSSGTSGFPKAVTISNSHKIIVDYM--------AINNSNIQYTSSTLDWCSG-LSMAITSGvfsTTSIIA--DCDFDP 269
Cdd:cd17650 98 VIYTSGTTGKPKGVMVEHRNVAHAAHAwrreyeldSFPVRLLQMASFSFDVFAGdFARSLLNG---GTLVICpdEVKLDP 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 270 GLFCRAIGKYRIS-MVLLSSSYLAIFANCpEFESADLSSLNYVIFGGSSCSLEVQRKVRSRL-SHDCLNFCYGLTELNSA 347
Cdd:cd17650 175 AALYDLILKSRITlMESTPALIRPVMAYV-YRNGLDLSAMRLLIVGSDGCKAQDFKTLAARFgQGMRIINSYGVTEATID 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 348 GSV-NLNFDEKPNS----VGRAIRGIKIKVIDEQGEAQEPNVVGEICFHNSQKWAGYYKNPDETRQ------IQDSENWI 416
Cdd:cd17650 254 STYyEEGRDPLGDSanvpIGRPLPNTAMYVLDERLQPQPVGVAGELYIGGAGVARGYLNRPELTAErfvenpFAPGERMY 333
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 281365686 417 HTGDLGYVDKDGYLFVIDRLKDMLKYQNIMYYPSEIENVIAEMPNVLEACV 467
Cdd:cd17650 334 RTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVV 384
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
196-511 |
5.13e-12 |
|
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: 67.87 E-value: 5.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 196 DHTLAILSSSGTSGFPKAVTISNSHKiivdymainNSNIQYTSSTLDWCSG-------LSMAITSGVFSTTSIIADCDF- 267
Cdd:cd05910 85 DEPAAILFTSGSTGTPKGVVYRHGTF---------AAQIDALRQLYGIRPGevdlatfPLFALFGPALGLTSVIPDMDPt 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 268 -----DPGLFCRAIGKYRISMVLLSSSYLAIFANCPEFESADLSSLNYVIFGGSSCSLEVQRKVRSRLSHDCLNFC-YGL 341
Cdd:cd05910 156 rparaDPQKLVGAIRQYGVSIVFGSPALLERVARYCAQHGITLPSLRRVLSAGAPVPIALAARLRKMLSDEAEILTpYGA 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 342 TE---LNSAGSVNLNFDEKPNS-------VGRAIRGIKIKVID-------EQGEAQE--PNVVGEICFHNSQKWAGYYKN 402
Cdd:cd05910 236 TEalpVSSIGSRELLATTTAATsggagtcVGRPIPGVRVRIIEiddepiaEWDDTLElpRGEIGEITVTGPTVTPTYVNR 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 403 PDETR--QIQDSEN--WIHTGDLGYVDKDGYLFVIDRLKDMLKYQNIMYYPSEIENVIAEMPNVLEACVFGiwdpvngde 478
Cdd:cd05910 316 PVATAlaKIDDNSEgfWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVG--------- 386
|
330 340 350
....*....|....*....|....*....|....*...
gi 281365686 479 aaaslVKKPGTQL-----EAQDVVEYVRKRITAKFKQL 511
Cdd:cd05910 387 -----VGKPGCQLpvlcvEPLPGTITPRARLEQELRAL 419
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
186-462 |
1.28e-11 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 66.85 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 186 FQPLRLKDgiDHTLAILSSSGTSGFPKAVTISnsHKIIVdymainnSNIQYTSSTLDWCSG-LSMAiTSGVFS------- 257
Cdd:PRK09274 166 FPMADLAP--DDMAAILFTSGSTGTPKGVVYT--HGMFE-------AQIEALREDYGIEPGeIDLP-TFPLFAlfgpalg 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 258 TTSIIADCDF------DPGLFCRAIGKYRISMVLLSSSYLAIFANCPEFESADLSSLNYVIFGGSSCSLEVQRKVRSRLS 331
Cdd:PRK09274 234 MTSVIPDMDPtrpatvDPAKLFAAIERYGVTNLFGSPALLERLGRYGEANGIKLPSLRRVISAGAPVPIAVIERFRAMLP 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 332 HDCLNFC-YGLTE---LNSAGSVNLNFDEKPNS-------VGRAIRGIKIKVID---------EQGEAQEPNVVGEICF- 390
Cdd:PRK09274 314 PDAEILTpYGATEalpISSIESREILFATRAATdngagicVGRPVDGVEVRIIAisdapipewDDALRLATGEIGEIVVa 393
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281365686 391 --HNSQkwaGYYKNPDETRQ--IQDSEN--WIHTGDLGYVDKDGYLFVIDRLKDMLKYQNIMYYPSEIENVIAEMPNV 462
Cdd:PRK09274 394 gpMVTR---SYYNRPEATRLakIPDGQGdvWHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGV 468
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
201-467 |
1.43e-11 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 67.67 E-value: 1.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 201 ILSSSGTSGFPKAVTISnsHKIIVDYMAI---------NNSNIQYTSSTLDWC-SGLSMAITSGvfSTTSIIADCDFDPG 270
Cdd:PRK12316 4699 VIYTSGSTGRPKGVAVS--HGSLVNHLHAtgeryeltpDDRVLQFMSFSFDGShEGLYHPLING--ASVVIRDDSLWDPE 4774
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 271 LFCRAIGKYRISMVLLSSSYLAIFANCPEfESADLSSLNYVIFGGSSCSLEVQRKVRSRLSHDCLNFCYGLTE------- 343
Cdd:PRK12316 4775 RLYAEIHEHRVTVLVFPPVYLQQLAEHAE-RDGEPPSLRVYCFGGEAVAQASYDLAWRALKPVYLFNGYGPTEttvtvll 4853
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 344 LNSAGSVNLNFDEKPnsVGRAIRGIKIKVIDEQGEAQEPNVVGEICFHNSQKWAGYYKNPDET--RQIQD-----SENWI 416
Cdd:PRK12316 4854 WKARDGDACGAAYMP--IGTPLGNRSGYVLDGQLNPLPVGVAGELYLGGEGVARGYLERPALTaeRFVPDpfgapGGRLY 4931
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 281365686 417 HTGDLGYVDKDGYLFVIDRLKDMLKYQNIMYYPSEIENVIAEMPNVLEACV 467
Cdd:PRK12316 4932 RTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVV 4982
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
305-545 |
1.46e-11 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 66.56 E-value: 1.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 305 LSSLNYVIFGGS---SCSLEVQRKVRSRLShdclnFCYGLTElnSAGSVNL----NFDEKPNSVGRAIRGIKIKVideqg 377
Cdd:PRK07445 229 LAQFRTILLGGApawPSLLEQARQLQLRLA-----PTYGMTE--TASQIATlkpdDFLAGNNSSGQVLPHAQITI----- 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 378 eaqEPNVVGEICFHNSQKWAGYYknPdetrQIQDSENWIHTGDLGYVDKDGYLFVIDRLKDMLKY--QNImyYPSEIENV 455
Cdd:PRK07445 297 ---PANQTGNITIQAQSLALGYY--P----QILDSQGIFETDDLGYLDAQGYLHILGRNSQKIITggENV--YPAEVEAA 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 456 IAEMPNVLEACVFGIWDPVNGDEAAASLVKKPGtqleaQDVVEYVRKRIT---AKFKQ----LNggaliVDQIVRSGNRK 528
Cdd:PRK07445 366 ILATGLVQDVCVLGLPDPHWGEVVTAIYVPKDP-----SISLEELKTAIKdqlSPFKQpkhwIP-----VPQLPRNPQGK 435
|
250
....*....|....*..
gi 281365686 529 TNRSAVKEHFLKNYNNN 545
Cdd:PRK07445 436 INRQQLQQIAVQRLGLP 452
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
64-535 |
2.19e-11 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 66.59 E-value: 2.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 64 VLTREDLHMNAMRVASYMRNMGLGQTDIVGVMGRHTTHQSAVAYAC-------FFNGTPLHALHNAYEEACIAKLFGITK 136
Cdd:PRK06060 30 VVTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLAClargvmaFLANPELHRDDHALAARNTEPALVVTS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 137 PRLifCDgdeyekvksatkdlqvtivtmRNHPRGSVRIQDVLTTPVM---QNFQPLrlkdGIDHTLAILSSSGTSGFPKA 213
Cdd:PRK06060 110 DAL--RD---------------------RFQPSRVAEAAELMSEAARvapGGYEPM----GGDALAYATYTSGTTGPPKA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 214 VTISNSHKI-IVDYMAINN-----SNIQYTSSTLDWCSGLSMAI-------TSGVFSTTSIIADcdfdpglfcraigkyr 280
Cdd:PRK06060 163 AIHRHADPLtFVDAMCRKAlrltpEDTGLCSARMYFAYGLGNSVwfplatgGSAVINSAPVTPE---------------- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 281 iSMVLLSSSYL-AIFANCPEFESADLSSLNYVIFGGSSCSLEVQRKVRSRLSHDCLNFCYGLTELNSAGS-------VNL 352
Cdd:PRK06060 227 -AAAILSARFGpSVLYGVPNFFARVIDSCSPDSFRSLRCVVSAGEALELGLAERLMEFFGGIPILDGIGStevgqtfVSN 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 353 NFDE-KPNSVGRAIRGIKIKVIDEQGEAQEPNVVGEICFHNSQKWAGYYKNPDEtrqIQDSENWIHTGDLGYVDKDGYLF 431
Cdd:PRK06060 306 RVDEwRLGTLGRVLPPYEIRVVAPDGTTAGPGVEGDLWVRGPAIAKGYWNRPDS---PVANEGWLDTRDRVCIDSDGWVT 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 432 VIDRLKDMLKYQNIMYYPSEIENVIAEMPNVLEACVFGIWDPVNGDEAAASLVKKPGTQLEaQDVVEYVRKRITAK---F 508
Cdd:PRK06060 383 YRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSGATID-GSVMRDLHRGLLNRlsaF 461
|
490 500
....*....|....*....|....*..
gi 281365686 509 KQLNGGAlIVDQIVRSGNRKTNRSAVK 535
Cdd:PRK06060 462 KVPHRFA-VVDRLPRTPNGKLVRGALR 487
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
198-506 |
3.07e-11 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 66.02 E-value: 3.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 198 TLAILSSSGTSGFPKAVTISNSHKIIvdyMAINNSNIQYTSS------TL------DWCSGLSMAITSGvfstTSIIADC 265
Cdd:PLN02479 197 SIALGYTSGTTASPKGVVLHHRGAYL---MALSNALIWGMNEgavylwTLpmfhcnGWCFTWTLAALCG----TNICLRQ 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 266 DFDPGLFcRAIGKYRISMVLLSSSYLAIFANCPEFESA-DLSSLNYVIFGGSSCSLEVQRKVRS---RLSHdclnfCYGL 341
Cdd:PLN02479 270 VTAKAIY-SAIANYGVTHFCAAPVVLNTIVNAPKSETIlPLPRVVHVMTAGAAPPPSVLFAMSEkgfRVTH-----TYGL 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 342 TELNSAGSV---NLNFDEKP---NSVGRAIRGIK------IKVIDEQGEAQEP---NVVGEICFHNSQKWAGYYKNPDET 406
Cdd:PLN02479 344 SETYGPSTVcawKPEWDSLPpeeQARLNARQGVRyiglegLDVVDTKTMKPVPadgKTMGEIVMRGNMVMKGYLKNPKAN 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 407 RQiQDSENWIHTGDLGYVDKDGYLFVIDRLKDMLKY--QNIMYYpsEIENVIAEMPNVLEACVFGIWDPVNGDEAAASLV 484
Cdd:PLN02479 424 EE-AFANGWFHSGDLGVKHPDGYIEIKDRSKDIIISggENISSL--EVENVVYTHPAVLEASVVARPDERWGESPCAFVT 500
|
330 340
....*....|....*....|....*..
gi 281365686 485 KKPGTQLE-----AQDVVEYVRKRITA 506
Cdd:PLN02479 501 LKPGVDKSdeaalAEDIMKFCRERLPA 527
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
59-534 |
4.80e-11 |
|
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: 64.98 E-value: 4.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 59 ITEDIVLTREDLHMNAMRVASYMRNMGLGQTDIVGVMGRHTTHQSAVAYACFFNGT---PLHAlhnAYEEACIAKLFGIT 135
Cdd:cd12114 7 ICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAayvPVDI---DQPAARREAILADA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 136 KPRLIFCDGdEYEKVKSATKDLQVTIvtmrnhprgsvriQDVLTTPVMQNFQPLRLKDgidhtLA-ILSSSGTSGFPKAV 214
Cdd:cd12114 84 GARLVLTDG-PDAQLDVAVFDVLILD-------------LDALAAPAPPPPVDVAPDD-----LAyVIFTSGSTGTPKGV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 215 TISNSHKI-----IVDYMAINNSNIQYTSSTLDWcsGLSMAITSGVFST--TSIIADC--DFDPGLFCRAIGKYRISMVL 285
Cdd:cd12114 145 MISHRAALntildINRRFAVGPDDRVLALSSLSF--DLSVYDIFGALSAgaTLVLPDEarRRDPAHWAELIERHGVTLWN 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 286 LSSSYLAIFANCPEFESADLSSLNYVIFGGSSCSLEVQRKVRSRLSHDCLNFCYGLTElnsaGSVNLNF------DEKPN 359
Cdd:cd12114 223 SVPALLEMLLDVLEAAQALLPSLRLVLLSGDWIPLDLPARLRALAPDARLISLGGATE----ASIWSIYhpidevPPDWR 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 360 SV--GRAIRGIKIKVIDEQGEAQEPNVVGEIcfhnsqkWA-------GYYKNPDETRQ----IQDSENWIHTGDLGYVDK 426
Cdd:cd12114 299 SIpyGRPLANQRYRVLDPRGRDCPDWVPGEL-------WIggrgvalGYLGDPELTAArfvtHPDGERLYRTGDLGRYRP 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 427 DGYLFVIDRLKDMLKYQNIMYYPSEIENVIAEMPNVLEACVFGIWDPVNGDEAAASLVKKPGTQLEAQDVVEYVRK---- 502
Cdd:cd12114 372 DGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDPGGKRLAAFVVPDNDGTPIAPDALRAFLAQtlpa 451
|
490 500 510
....*....|....*....|....*....|...
gi 281365686 503 -RITAKFKQLnggalivDQIVRSGNRKTNRSAV 534
Cdd:cd12114 452 yMIPSRVIAL-------EALPLTANGKVDRAAL 477
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
61-539 |
5.40e-11 |
|
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.
Pssm-ID: 341231 [Multi-domain] Cd Length: 571 Bit Score: 65.06 E-value: 5.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 61 EDIVLTREDLHMNAMRVASYMRN-MGLGQTDIVGVMGRHTTHQSAVAYACFFNG---TPLHALHNAYEeacIAKLFGITK 136
Cdd:cd05905 11 EATTLTWGKLLSRAEKIAAVLQKkVGLKPGDRVALMYPDPLDFVAAFYGCLYAGvvpIPIEPPDISQQ---LGFLLGTCK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 137 PRLIFcdgdeyeKVKSATKDLQVTIVTMRNH-----PRGSVRIQDVLTTPvMQNFQPLRLKDGI----DHTLAILS-SSG 206
Cdd:cd05905 88 VRVAL-------TVEACLKGLPKKLLKSKTAaeiakKKGWPKILDFVKIP-KSKRSKLKKWGPHpptrDGDTAYIEySFS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 207 TSGFPKAVTISnsHKIIVDYMAINNSNIQYTSST-----LDWCSGLS--MAITSGVFS--TTSIIADCDF--DPGLFCRA 275
Cdd:cd05905 160 SDGSLSGVAVS--HSSLLAHCRALKEACELYESRplvtvLDFKSGLGlwHGCLLSVYSghHTILIPPELMktNPLLWLQT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 276 IGKYRISMVLLSSS----YLAIFANCPEFESA---DLSSLN--YVIFGG----SSCSLEVQRKVRSRLSHDCLNFCYGlT 342
Cdd:cd05905 238 LSQYKVRDAYVKLRtlhwCLKDLSSTLASLKNrdvNLSSLRmcMVPCENrpriSSCDSFLKLFQTLGLSPRAVSTEFG-T 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 343 ELNSA-----------------------GSVNLNFDEKPNS-----VGRAIRGIKIKVIDEQGEAQ-EPNVVGEICFHNS 393
Cdd:cd05905 317 RVNPFicwqgtsgpepsrvyldmralrhGVVRLDERDKPNSlplqdSGKVLPGAQVAIVNPETKGLcKDGEIGEIWVNSP 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 394 QKWAGYYKNPDETRQIQDSEN------------WIHTGDLGYV----------DKDGYLFVIDRLKDMLKYQNIMYYPSE 451
Cdd:cd05905 397 ANASGYFLLDGETNDTFKVFPstrlstgitnnsYARTGLLGFLrptkctdlnvEEHDLLFVVGSIDETLEVRGLRHHPSD 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 452 IEN-VIAEMPNVLEACVFgiwdpvngdEAAASLV----KKPGTQLEAQDVVEYVRKRITAKFKQLNGGALIVD--QIVRS 524
Cdd:cd05905 477 IEAtVMRVHPYRGRCAVF---------SITGLVVvvaeQPPGSEEEALDLVPLVLNAILEEHQVIVDCVALVPpgSLPKN 547
|
570
....*....|....*
gi 281365686 525 GNRKTNRSAVKEHFL 539
Cdd:cd05905 548 PLGEKQRMEIRQAFL 562
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
201-534 |
1.16e-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: 63.73 E-value: 1.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 201 ILSSSGTSGFPKAVTISnsHKIIVDY---------MAINNSNIQYTSSTLDwCSGLSMAITSGVFSTTSII-ADCDFDPG 270
Cdd:cd17645 109 VIYTSGSTGLPKGVMIE--HHNLVNLcewhrpyfgVTPADKSLVYASFSFD-ASAWEIFPHLTAGAALHVVpSERRLDLD 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 271 LFCRAIGKYRISMVLLSSSYlaifanCPEFESADLSSLNYVIFGGSscslevQRKVRSRLSHDCLNfCYGLTELN-SAGS 349
Cdd:cd17645 186 ALNDYFNQEGITISFLPTGA------AEQFMQLDNQSLRVLLTGGD------KLKKIERKGYKLVN-NYGPTENTvVATS 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 350 VNLNFDEKPNSVGRAIRGIKIKVIDEQGEAQEPNVVGEICFHNSQKWAGYYKNPDETRQ--IQD----SENWIHTGDLGY 423
Cdd:cd17645 253 FEIDKPYANIPIGKPIDNTRVYILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEkfIVHpfvpGERMYRTGDLAK 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 424 VDKDGYLFVIDRLKDMLKYQNIMYYPSEIENVIAEMPNVLEACVFGIWDPvNGDEAAASLVKKPgTQLEAQDVVEYVRKR 503
Cdd:cd17645 333 FLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDA-DGRKYLVAYVTAP-EEIPHEELREWLKND 410
|
330 340 350
....*....|....*....|....*....|....*.
gi 281365686 504 -----ITAKFKQLNGGALIVdqivrsgNRKTNRSAV 534
Cdd:cd17645 411 lpdymIPTYFVHLKALPLTA-------NGKVDRKAL 439
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
305-458 |
2.18e-10 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 63.30 E-value: 2.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 305 LSSLNYVIFGGSSCSLEVQRKVRSRLSHDCLNFCYGLTELNSAGSVN-LNFDEKPNSVGRAIRGIKIKVIDEQGEAQEPN 383
Cdd:PRK06334 298 LPSLRFVVIGGDAFKDSLYQEALKTFPHIQLRQGYGTTECSPVITINtVNSPKHESCVGMPIRGMDVLIVSEETKVPVSS 377
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281365686 384 -VVGEICFHNSQKWAGYYKNpDETRQI--QDSENWIHTGDLGYVDKDGYLFVIDRLKDMLKYQNIMYYPSEIENVIAE 458
Cdd:PRK06334 378 gETGLVLTRGTSLFSGYLGE-DFGQGFveLGGETWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILME 454
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
196-467 |
3.44e-10 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 63.44 E-value: 3.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 196 DHTLAILSSSGTSGFPKAVtiSNSHKIIVDYM---------AINNSNIQYTSSTLD---W------CSGLSMAITSgvfs 257
Cdd:PRK12316 655 ENLAYVIYTSGSTGKPKGA--GNRHRALSNRLcwmqqayglGVGDTVLQKTPFSFDvsvWeffwplMSGARLVVAA---- 728
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 258 ttsiiADCDFDPGLFCRAIGKYRISMVLLSSSYLAIFAncPEFESADLSSLNYVIFGGSSCSLEVQRKVRSRLSHDCLNF 337
Cdd:PRK12316 729 -----PGDHRDPAKLVELINREGVDTLHFVPSMLQAFL--QDEDVASCTSLRRIVCSGEALPADAQEQVFAKLPQAGLYN 801
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 338 CYGLTELNSAGSVNLNFDEKPNSV--GRAIRGIKIKVIDEQGEAQEPNVVGEICFHNSQKWAGYYKNPDETRQ------I 409
Cdd:PRK12316 802 LYGPTEAAIDVTHWTCVEEGGDSVpiGRPIANLACYILDANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAErfvpspF 881
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 281365686 410 QDSENWIHTGDLGYVDKDGYLFVIDRLKDMLKYQNIMYYPSEIENVIAEMPNVLEACV 467
Cdd:PRK12316 882 VAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAV 939
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
339-469 |
3.71e-10 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 62.73 E-value: 3.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 339 YGLTElNSAGSVNLNFDE--KPNSVGRAIRGIKIK---VIDEQGEAQEPNVVGEICFHNSQKWAGYYKNPDETRQIQdSE 413
Cdd:PLN02614 418 YGLTE-SCAGTFVSLPDEldMLGTVGPPVPNVDIRlesVPEMEYDALASTPRGEICIRGKTLFSGYYKREDLTKEVL-ID 495
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 281365686 414 NWIHTGDLGYVDKDGYLFVIDRLKDMLKYQNIMYYPSE-IENVIAEMPNVLEACVFG 469
Cdd:PLN02614 496 GWLHTGDVGEWQPNGSMKIIDRKKNIFKLSQGEYVAVEnIENIYGEVQAVDSVWVYG 552
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
339-469 |
8.74e-10 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 61.40 E-value: 8.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 339 YGLTElNSAGSVNLNFDEKP--NSVGRAIRGIKIKV--IDEQGEAQEPNVV-GEICFHNSQKWAGYYKNPDETRQIQdSE 413
Cdd:PLN02861 415 YGLTE-SCGGCFTSIANVFSmvGTVGVPMTTIEARLesVPEMGYDALSDVPrGEICLRGNTLFSGYHKRQDLTEEVL-ID 492
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 281365686 414 NWIHTGDLGYVDKDGYLFVIDRLKDMLKYQNIMYYPSE-IENVIAEMPNVLEACVFG 469
Cdd:PLN02861 493 GWFHTGDIGEWQPNGAMKIIDRKKNIFKLSQGEYVAVEnLENTYSRCPLIASIWVYG 549
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
304-534 |
9.00e-10 |
|
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: 60.78 E-value: 9.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 304 DLSSLNYVIFGGSSCSLEVQRKVRSRLSHDC--LNFCYGLTELnsagSVNLNF--------DEKPNSV-GRAIRGIKIKV 372
Cdd:cd17643 208 DPLALRYVIFGGEALEAAMLRPWAGRFGLDRpqLVNMYGITET----TVHVTFrpldaadlPAAAASPiGRPLPGLRVYV 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 373 IDEQGEAQEPNVVGEICFHNSQKWAGYYKNPDET--RQIQD-----SENWIHTGDLGYVDKDGYLFVIDRLKDMLKYQNI 445
Cdd:cd17643 284 LDADGRPVPPGVVGELYVSGAGVARGYLGRPELTaeRFVANpfggpGSRMYRTGDLARRLPDGELEYLGRADEQVKIRGF 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 446 MYYPSEIENVIAEMPNVLEACVFGIWDPVNGDEAAASLVKKPGTQLEAQDVVEYVRKR-----ITAKFkqlnggaLIVDQ 520
Cdd:cd17643 364 RIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVADDGAAADIAELRALLKELlpdymVPARY-------VPLDA 436
|
250
....*....|....
gi 281365686 521 IVRSGNRKTNRSAV 534
Cdd:cd17643 437 LPLTVNGKLDRAAL 450
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
360-541 |
2.35e-09 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 59.75 E-value: 2.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 360 SVGRAIRGIKIKVIDEQGEAQEPN-VVGEICFHNSQKWAGYYKNPDETRQI------------------QDSENWIHTGD 420
Cdd:PRK12476 403 SCGQVARSQWAVIVDPDTGAELPDgEVGEIWLHGDNIGRGYWGRPEETERTfgaklqsrlaegshadgaADDGTWLRTGD 482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 421 LGyVDKDGYLFVIDRLKDMLKYQNIMYYPSEIENVIAEM-PNVLEACVFGIWDPVNGDEAAASLVKK-PGT-QLEAQDVV 497
Cdd:PRK12476 483 LG-VYLDGELYITGRIADLIVIDGRNHYPQDIEATVAEAsPMVRRGYVTAFTVPAEDNERLVIVAERaAGTsRADPAPAI 561
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 281365686 498 EYVRKRIT-------AKFKQLNGGAlivdqIVRSGNRKTNRSAVKEHFLKN 541
Cdd:PRK12476 562 DAIRAAVSrrhglavADVRLVPAGA-----IPRTTSGKLARRACRAQYLDG 607
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
198-534 |
2.53e-09 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 60.36 E-value: 2.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 198 TLA-ILSSSGTSGFPKAVtiSNSHKIIVDY---------MAINNSNIQYTSSTLD-WCSGLSMAITSGvfstTSIIA--D 264
Cdd:PRK12316 2147 NLAyVIYTSGSTGLPKGV--AVSHGALVAHcqaageryeLSPADCELQFMSFSFDgAHEQWFHPLLNG----ARVLIrdD 2220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 265 CDFDPGLFCRAIGKYRISMVLLSSSYLAIFANCPEFESADLSsLNYVIFGGSSCSLEVQRKVRSRLSHDCLNFCYGLTEl 344
Cdd:PRK12316 2221 ELWDPEQLYDEMERHGVTILDFPPVYLQQLAEHAERDGRPPA-VRVYCFGGEAVPAASLRLAWEALRPVYLFNGYGPTE- 2298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 345 nsAGSVNLNFDEKPNS--------VGRAIRGIKIKVIDEQGEAQEPNVVGEICFHNSQKWAGYYKNPDET--RQIQD--- 411
Cdd:PRK12316 2299 --AVVTPLLWKCRPQDpcgaayvpIGRALGNRRAYILDADLNLLAPGMAGELYLGGEGLARGYLNRPGLTaeRFVPDpfs 2376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 412 --SENWIHTGDLGYVDKDGYLFVIDRLKDMLKYQNIMYYPSEIENVIAEMPNVLEACVFGIwDPVNGDEAAASLVKKPGT 489
Cdd:PRK12316 2377 asGERLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQ-DGASGKQLVAYVVPDDAA 2455
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 281365686 490 QLEAQDVVEYVRKRITAKFkqLNGGALIVDQIVRSGNRKTNRSAV 534
Cdd:PRK12316 2456 EDLLAELRAWLAARLPAYM--VPAHWVVLERLPLNPNGKLDRKAL 2498
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
204-525 |
4.29e-09 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 58.84 E-value: 4.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 204 SSGTSGFPKAVTISNsHKIIvdYMA-------INNSNIQYTSSTLDWCSGLSMAITSGVFSTTSIIADCDFDPGLF---C 273
Cdd:cd05938 152 TSGTTGLPKAARISH-LRVL--QCSgflslcgVTADDVIYITLPLYHSSGFLLGIGGCIELGATCVLKPKFSASQFwddC 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 274 RaigKYRISMVLLSSSYLAIFANCPEFESADLSSLNYVIfgGSSCSLEVQRKVRSRLSHDCLNFCYGLTElnsaGSVN-L 352
Cdd:cd05938 229 R---KHNVTVIQYIGELLRYLCNQPQSPNDRDHKVRLAI--GNGLRADVWREFLRRFGPIRIREFYGSTE----GNIGfF 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 353 NFDEKPNSVGRAIRGIK-------IK--------VIDEQG-----EAQEPNV-VGEICFHNSqkWAGYYKNPDETRQ--- 408
Cdd:cd05938 300 NYTGKIGAVGRVSYLYKllfpfelIKfdvekeepVRDAQGfcipvAKGEPGLlVAKITQQSP--FLGYAGDKEQTEKkll 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 409 ---IQDSENWIHTGDLGYVDKDGYLFVIDRLKDMLKYQNIMYYPSEIENVIAEMPNVLEACVFGIwdPVNGDE---AAAS 482
Cdd:cd05938 378 rdvFKKGDVYFNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVYGV--TVPGHEgriGMAA 455
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 483 LVKKPGTQLEAQDVVEYVRK-----------------RITAKFKQLNGgalivdQIVRSG 525
Cdd:cd05938 456 VKLKPGHEFDGKKLYQHVREylpayarprflriqdslEITGTFKQQKV------RLVEEG 509
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
187-533 |
7.69e-09 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 58.52 E-value: 7.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 187 QPLRLkDGIDHTLAILSSSGTSGFPKAVTISnsHKIIVD--------Y-MAINNSNIQYTSSTLD---WCSGLSMAITSg 254
Cdd:PRK10252 590 APLQL-SQPHHTAYIIFTSGSTGRPKGVMVG--QTAIVNrllwmqnhYpLTADDVVLQKTPCSFDvsvWEFFWPFIAGA- 665
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 255 vfstTSIIA--DCDFDPGLFCRAIGKYRISMVLLSSSYLAIFANCPEFESAD--LSSLNYVIfggssCSLEV----QRKV 326
Cdd:PRK10252 666 ----KLVMAepEAHRDPLAMQQFFAEYGVTTTHFVPSMLAAFVASLTPEGARqsCASLRQVF-----CSGEAlpadLCRE 736
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 327 RSRLSHDCLNFCYGLTELN-------SAGSVNLNFDEKPNSVGRAIRGIKIKVIDEQGEAQEPNVVGEICFHNSQKWAGY 399
Cdd:PRK10252 737 WQQLTGAPLHNLYGPTEAAvdvswypAFGEELAAVRGSSVPIGYPVWNTGLRILDARMRPVPPGVAGDLYLTGIQLAQGY 816
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 400 YKNPDET--RQIQD----SENWIHTGDLGYVDKDGYLFVIDRLKDMLKYQNIMYYPSEIENVIAEMPNVLE----ACVFG 469
Cdd:PRK10252 817 LGRPDLTasRFIADpfapGERMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQavthACVIN 896
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 281365686 470 IWDPVNGDEA--AASLVKKPGTQLEAQDVVEYVRKRITAK-----FKQLnggalivDQIVRSGNRKTNRSA 533
Cdd:PRK10252 897 QAAATGGDARqlVGYLVSQSGLPLDTSALQAQLRERLPPHmvpvvLLQL-------DQLPLSANGKLDRKA 960
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
307-443 |
9.21e-09 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 58.20 E-value: 9.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 307 SLNYVIFGGSSCSLEVQRKVrsrlshdclNFC--------YGLTElNSAGSVNLNFDEkpNSVGRA---IRGIKIKVID- 374
Cdd:PLN02387 421 RIRFMLSGGAPLSGDTQRFI---------NIClgapigqgYGLTE-TCAGATFSEWDD--TSVGRVgppLPCCYVKLVSw 488
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 281365686 375 EQG---EAQEPNVVGEICFHNSQKWAGYYKNPDETRQI-QDSEN---WIHTGDLGYVDKDGYLFVIDRLKDMLKYQ 443
Cdd:PLN02387 489 EEGgylISDKPMPRGEIVIGGPSVTLGYFKNQEKTDEVyKVDERgmrWFYTGDIGQFHPDGCLEIIDRKKDIVKLQ 564
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
69-223 |
1.06e-08 |
|
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: 57.83 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 69 DLHMNAMRVASYMRNMGLGQTDIVGVMGRHTTHQSAVAYACFFNGTPLHALHNAY-----EEACIAKLFGITKPRLIFC- 142
Cdd:cd05921 30 EALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSPAYslmsqDLAKLKHLFELLKPGLVFAq 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 143 DGDEYEKVKSATKDLQVTIVTMRNHP--RGSVRIQDVLTTPVMQNFQPLRLKDGIDHTLAILSSSGTSGFPKAVTisNSH 220
Cdd:cd05921 110 DAAPFARALAAIFPLGTPLVVSRNAVagRGAISFAELAATPPTAAVDAAFAAVGPDTVAKFLFTSGSTGLPKAVI--NTQ 187
|
...
gi 281365686 221 KII 223
Cdd:cd05921 188 RML 190
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
339-503 |
1.19e-08 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 57.58 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 339 YGLTELNsagsVNL-NFDEKPNSVGR--------------------AIRG-----IKIKViDEQGEAqepnvVGEIcfHN 392
Cdd:PRK08279 345 YAASEGN----VGFiNVFNFDGTVGRvplwlahpyaivkydvdtgePVRDadgrcIKVKP-GEVGLL-----IGRI--TD 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 393 SQKWAGYyKNPDETRQ------IQDSENWIHTGDLGYVDKDGYLFVIDRLKDML--KYQNIMyyPSEIENVIAEMPNVLE 464
Cdd:PRK08279 413 RGPFDGY-TDPEASEKkilrdvFKKGDAWFNTGDLMRDDGFGHAQFVDRLGDTFrwKGENVA--TTEVENALSGFPGVEE 489
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 281365686 465 ACVFGIWDP-VNGDEAAASLVKKPGTQLEAQDVVEYVRKR 503
Cdd:PRK08279 490 AVVYGVEVPgTDGRAGMAAIVLADGAEFDLAALAAHLYER 529
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
65-484 |
1.66e-08 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 57.66 E-value: 1.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 65 LTREDLHMNAMRVASYMRNMGLGQTDIVGVMGRHTTHQSAVAYACFFNGTPLHALHNAYEEACIAKLFGITKPRLIFCDg 144
Cdd:PRK12316 3083 LSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLSQ- 3161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 145 deyEKVKSATKDLQVTIVTMRNHPRGSVRIQDVLTTPvmqnfqplrlkdgiDHTLAILSSSGTSGFPKAVTI-----SNS 219
Cdd:PRK12316 3162 ---SHLRLPLAQGVQVLDLDRGDENYAEANPAIRTMP--------------ENLAYVIYTSGSTGKPKGVGIrhsalSNH 3224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 220 HKIIVDYMAI--NNSNIQYTSSTLD-WCSGLSMAITSGVFSTTSIIADCDfDPGLFCRAIGKYRISMVLLSSSYLAIFAN 296
Cdd:PRK12316 3225 LCWMQQAYGLgvGDRVLQFTTFSFDvFVEELFWPLMSGARVVLAGPEDWR-DPALLVELINSEGVDVLHAYPSMLQAFLE 3303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 297 cpEFESADLSSLNYVIFGGSSCSLEVQRKVRSRLShdcLNFCYGLTELNSAGSVNLNFDEKPNS--VGRAIRGIKIKVID 374
Cdd:PRK12316 3304 --EEDAHRCTSLKRIVCGGEALPADLQQQVFAGLP---LYNLYGPTEATITVTHWQCVEEGKDAvpIGRPIANRACYILD 3378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 375 EQGEAQEPNVVGEICFHNSQKWAGYYKNPDETRQ------IQDSENWIHTGDLGYVDKDGYLFVIDRLKDMLKYQNIMYY 448
Cdd:PRK12316 3379 GSLEPVPVGALGELYLGGEGLARGYHNRPGLTAErfvpdpFVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIE 3458
|
410 420 430
....*....|....*....|....*....|....*.
gi 281365686 449 PSEIENVIAEMPNVLEACVFGiwdpVNGDEAAASLV 484
Cdd:PRK12316 3459 LGEIEARLLEHPWVREAVVLA----VDGRQLVAYVV 3490
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
375-536 |
1.94e-08 |
|
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: 56.67 E-value: 1.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 375 EQGEAqepnvVGEICFHNSQKWAGYYKNPDET--RQIQD----SENWIHTGDLGYVDKDGYLFVIDRLKDMLKYQNIMYY 448
Cdd:cd05937 298 EPGEM-----LGRVPFKNREAFQGYLHNEDATesKLVRDvfrkGDIYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVS 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 449 PSEIENVIAEMPNVLEACVFGIWDPVNGDEAAASLVKkpgTQLEAQDVVEYVRKRITA-KFKQLNGGAL-----IVDQIV 522
Cdd:cd05937 373 TTEVADVLGAHPDIAEANVYGVKVPGHDGRAGCAAIT---LEESSAVPTEFTKSLLASlARKNLPSYAVplflrLTEEVA 449
|
170
....*....|....
gi 281365686 523 RSGNRKTNRSAVKE 536
Cdd:cd05937 450 TTDNHKQQKGVLRD 463
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
198-493 |
3.06e-08 |
|
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: 56.22 E-value: 3.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 198 TLA-ILSSSGTSGFPKAVTISN---SH--KIIVDYMAINNSN--IQYTSSTLDWCS-GLSMAITSGvfsTTSIIADCD-- 266
Cdd:cd17649 95 QLAyVIYTSGSTGTPKGVAVSHgplAAhcQATAERYGLTPGDreLQFASFNFDGAHeQLLPPLICG---ACVVLRPDElw 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 267 FDPGLFCRAIGKYRISMVLLSSSYLAIFANcpEFE---SADLSSLNYVIFGGSSCSLEVQRkvRSRLSHDCLNFCYGLTE 343
Cdd:cd17649 172 ASADELAEMVRELGVTVLDLPPAYLQQLAE--EADrtgDGRPPSLRLYIFGGEALSPELLR--RWLKAPVRLFNAYGPTE 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 344 ---LNSAGSVNLNFDEKPNSV--GRAIRGIKIKVIDEQGEAQEPNVVGEIcFHNSQKWA-GYYKNPDET--RQIQD---- 411
Cdd:cd17649 248 atvTPLVWKCEAGAARAGASMpiGRPLGGRSAYILDADLNPVPVGVTGEL-YIGGEGLArGYLGRPELTaeRFVPDpfga 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 412 -SENWIHTGDLGYVDKDGYLFVIDRLKDMLKYQNIMYYPSEIENVIAEMPNVLEACVFGIwDPVNGDEAAASLVKKPGTQ 490
Cdd:cd17649 327 pGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVAL-DGAGGKQLVAYVVLRAAAA 405
|
...
gi 281365686 491 LEA 493
Cdd:cd17649 406 QPE 408
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
268-484 |
6.09e-08 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 55.94 E-value: 6.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 268 DPGLFCRAIGKYRISMVLLSSSYLAIFANCPEfeSADLSSLNYVIFGGSSCSLEVQRKVRSRLSHDCLNFCYGLTELnsa 347
Cdd:PRK05691 1352 DPQRIAELVQQYGVTTLHFVPPLLQLFIDEPL--AAACTSLRRLFSGGEALPAELRNRVLQRLPQVQLHNRYGPTET--- 1426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 348 gSVNLNF------DEKPNSVGRAIRGIKIKVIDEQGEAQEPNVVGEICFHNSQKWAGYYKNPDETRQI-------QDSEN 414
Cdd:PRK05691 1427 -AINVTHwqcqaeDGERSPIGRPLGNVLCRVLDAELNLLPPGVAGELCIGGAGLARGYLGRPALTAERfvpdplgEDGAR 1505
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 415 WIHTGDLGYVDKDGYLFVIDRLKDMLKYQNIMYYPSEIENVIAEMPNVLEACVFgiwdpVNGDEAAASLV 484
Cdd:PRK05691 1506 LYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVL-----VREGAAGAQLV 1570
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
128-478 |
1.36e-07 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 54.13 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 128 IAKLFGITKPRLIFCDGDEyekvksATKDLQVTIVTMRNhprgsvrIQDVLTTPVMQNF-QPLRLKDgidhTLAILSSSG 206
Cdd:PRK04813 91 IEMIIEVAKPSLIIATEEL------PLEILGIPVITLDE-------LKDIFATGNPYDFdHAVKGDD----NYYIIFTSG 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 207 TSGFPKAVTIS-NSHKIIVDYMaINNSNIQYTSSTL-------DwcsgLS-MAI----TSG---VFSTTSIIADcdfdPG 270
Cdd:PRK04813 154 TTGKPKGVQIShDNLVSFTNWM-LEDFALPEGPQFLnqapysfD----LSvMDLyptlASGgtlVALPKDMTAN----FK 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 271 LFCRAIGKYRIS----------MVLLSssylaifancPEFESADLSSLNYVIFGGSSCSLEVQRKVRSRLSHDCLNFCYG 340
Cdd:PRK04813 225 QLFETLPQLPINvwvstpsfadMCLLD----------PSFNEEHLPNLTHFLFCGEELPHKTAKKLLERFPSATIYNTYG 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 341 LTELNSA-GSVNLNfDE-----KPNSVGRAIRGIKIKVIDEQGEAQEPNVVGEICFHNSQKWAGYYKNPDETRQI---QD 411
Cdd:PRK04813 295 PTEATVAvTSIEIT-DEmldqyKRLPIGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAfftFD 373
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281365686 412 SENWIHTGDLGYVDkDGYLFVIDRLKDMLKYQNIMYYPSEIENVIAEMPNVLEACVFgiwdPVNGDE 478
Cdd:PRK04813 374 GQPAYHTGDAGYLE-DGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVV----PYNKDH 435
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
342-453 |
2.70e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 53.19 E-value: 2.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 342 TELNSAGSVNLNfDEKPNSV-----GRAIRGIKIKVID-EQGEAQEPNVVGEICFHNSQKWAGYYKNPDETRQI------ 409
Cdd:PRK07769 370 DELNAGRFVEVP-ADAPNAVaqvsaGKVGVSEWAVIVDpETASELPDGQIGEIWLHGNNIGTGYWGKPEETAATfqnilk 448
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 281365686 410 -----------QDSENWIHTGDLG-YVdkDGYLFVIDRLKDMLKYQNIMYYPSEIE 453
Cdd:PRK07769 449 srlseshaegaPDDALWVRTGDYGvYF--DGELYITGRVKDLVIIDGRNHYPQDLE 502
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
236-467 |
2.71e-07 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 53.23 E-value: 2.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 236 YTSSTLDWCSGLSMaitsgvfSTTSIIADCDFDPGLfcraIGKY--RISMVllsssylaifancpefesaDLSSLNYVIF 313
Cdd:PRK05851 230 FSASPFRWLSWLSD-------SRATLTAAPNFAYNL----IGKYarRVSDV-------------------DLGALRVALN 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 314 GGSSCSLE-VQRKVR--SRLSHD--CLNFCYGLTELNSAGSV-----NLNFDE----------KPNSVGRAIRGIKIKVi 373
Cdd:PRK05851 280 GGEPVDCDgFERFATamAPFGFDagAAAPSYGLAESTCAVTVpvpgiGLRVDEvttddgsgarRHAVLGNPIPGMEVRI- 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 374 dEQGEAQEPNV---VGEICFHNSQKWAGYYKNPDetrqiQDSENWIHTGDLGYVdKDGYLFVIDRLKDMLKY--QNImyY 448
Cdd:PRK05851 359 -SPGDGAAGVAgreIGEIEIRGASMMSGYLGQAP-----IDPDDWFPTGDLGYL-VDGGLVVCGRAKELITVagRNI--F 429
|
250
....*....|....*....
gi 281365686 449 PSEIENVIAEMPNVLEACV 467
Cdd:PRK05851 430 PTEIERVAAQVRGVREGAV 448
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
196-441 |
3.63e-07 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 53.18 E-value: 3.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 196 DHTLAILSSSGTSGFPKAVTISN-----------SHKIIVDY---------------------------MAIN--NSNIQ 235
Cdd:PTZ00342 304 DFITSIVYTSGTSGKPKGVMLSNknlyntvvplcKHSIFKKYnpkthlsylpishiyerviaylsfmlgGTINiwSKDIN 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 236 YTSSTLDWCSGLSMAITSGVFST--TSIIADCDFDPgLFCRAIGKYRISmvLLSSSYLAIFANCPEfESADLSS------ 307
Cdd:PTZ00342 384 YFSKDIYNSKGNILAGVPKVFNRiyTNIMTEINNLP-PLKRFLVKKILS--LRKSNNNGGFSKFLE-GITHISSkikdkv 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 308 ---LNYVIFGGSSCSLEVQRKVRSRLShdcLNFC--YGLTELNSAGSVNLNFDEKPNSVGRAIR-GIKIKVID-EQGEAQ 380
Cdd:PTZ00342 460 npnLEVILNGGGKLSPKIAEELSVLLN---VNYYqgYGLTETTGPIFVQHADDNNTESIGGPISpNTKYKVRTwETYKAT 536
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 281365686 381 EPNVVGEICFHNSQKWAGYYKNPDETRQIQDSENWIHTGDLGYVDKDGYLFVIDRLKDMLK 441
Cdd:PTZ00342 537 DTLPKGELLIKSDSIFSGYFLEKEQTKNAFTEDGYFKTGDIVQINKNGSLTFLDRSKGLVK 597
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
196-467 |
5.10e-07 |
|
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: 52.09 E-value: 5.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 196 DHTLA-ILSSSGTSGFPKAVTIsnSHKIIVdymainnSNIQYTSSTLDWCSG-----------------LSMAITSG--- 254
Cdd:cd17654 117 DECLAyVIHTSGTTGTPKIVAV--PHKCIL-------PNIQHFRSLFNITSEdilfltspltfdpsvveIFLSLSSGatl 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 255 VFSTTSI-IADCDFDPGLFCRaigkYRISMVLLSSSYLAIF--ANCPEFESADLSSLNYVIFGG----SSCSLEVQRKVR 327
Cdd:cd17654 188 LIVPTSVkVLPSKLADILFKR----HRITVLQATPTLFRRFgsQSIKSTVLSATSSLRVLALGGepfpSLVILSSWRGKG 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 328 SRLsHDCLNfcYGLTELNSAGSVN-LNFDEKPNSVGRAIRGIKIKVIDEQGEAQEPNVVGEicfhnsQKWAGYYKNPDET 406
Cdd:cd17654 264 NRT-RIFNI--YGITEVSCWALAYkVPEEDSPVQLGSPLLGTVIEVRDQNGSEGTGQVFLG------GLNRVCILDDEVT 334
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 281365686 407 RQIQDsenWIHTGDLGYVdKDGYLFVIDRLKDMLKYQNIMYYPSEIENVIAEMPNVLEACV 467
Cdd:cd17654 335 VPKGT---MRATGDFVTV-KDGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGVESCAV 391
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
307-510 |
1.15e-06 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 51.03 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 307 SLNYVIFGGSSCSLE-----VQRKVRSrlshdclnFC-YGLTELNSAGSVNLNfDEKPNsVGRAIRGIKIKVIDeqgeaq 380
Cdd:PRK09029 241 SLKAVLLGGAAIPVElteqaEQQGIRC--------WCgYGLTEMASTVCAKRA-DGLAG-VGSPLPGREVKLVD------ 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 381 epnvvGEIcfhnsqkW-------AGYYKNpdetRQIQ---DSENWIHTGDLGYVDkDGYLFVIDRLKDMLKY--QNImyY 448
Cdd:PRK09029 305 -----GEI-------WlrgaslaLGYWRQ----GQLVplvNDEGWFATRDRGEWQ-NGELTILGRLDNLFFSggEGI--Q 365
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281365686 449 PSEIENVIAEMPNVLEACVFGIWDPVNGDEAAASLVKKPGTQLEAqdVVEYVRKRItAKFKQ 510
Cdd:PRK09029 366 PEEIERVINQHPLVQQVFVVPVADAEFGQRPVAVVESDSEAAVVN--LAEWLQDKL-ARFQQ 424
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
357-504 |
1.57e-06 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 50.91 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 357 KPNSVGRAIRGIKIKVIDEQGEAQEPNVVGEICFHNSqkWAGY----YKNPDETRQIQDSE--NWIHTGDLGYVDKDGYL 430
Cdd:PRK00174 422 KPGSATRPLPGIQPAVVDEEGNPLEGGEGGNLVIKDP--WPGMmrtiYGDHERFVKTYFSTfkGMYFTGDGARRDEDGYY 499
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 431 FVIDRLKDMLkyqNImyypS-------EIENVIAEMPNVLEACVFGIWDPVNGDEAAASLVKKPGTQLE---AQDVVEYV 500
Cdd:PRK00174 500 WITGRVDDVL---NV----SghrlgtaEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLKGGEEPSdelRKELRNWV 572
|
....
gi 281365686 501 RKRI 504
Cdd:PRK00174 573 RKEI 576
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
167-536 |
2.36e-06 |
|
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: 50.23 E-value: 2.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 167 HPRGsvRIQDVLT---TPVMqnfqplrLKDGIDHTLAILSSSGTSGFPKAVTISnsHKIIV-------DYMAINNSN--I 234
Cdd:cd05918 83 HPLQ--RLQEILQdtgAKVV-------LTSSPSDAAYVIFTSGSTGKPKGVVIE--HRALStsalahgRALGLTSESrvL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 235 QYTSSTLD---------WCSGLSMAITSGvfsttsiiADCDFDpglFCRAIGKYRISMVLLSSSYLAIFAncPEfesaDL 305
Cdd:cd05918 152 QFASYTFDvsileifttLAAGGCLCIPSE--------EDRLND---LAGFINRLRVTWAFLTPSVARLLD--PE----DV 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 306 SSLNYVIFGGsscslE-VQRKVRSRLSHDC--LNfCYGLTE--LNSAGSVNLNfDEKPNSVGRAIRGIkIKVIDEQGEAQ 380
Cdd:cd05918 215 PSLRTLVLGG-----EaLTQSDVDTWADRVrlIN-AYGPAEctIAATVSPVVP-STDPRNIGRPLGAT-CWVVDPDNHDR 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 381 E--PNVVGEICFHNSQKWAGYYKNPDETRQ--IQDSENWIH-----------TGDLGYVDKDGYLFVIDRLKDMLKYQNI 445
Cdd:cd05918 287 LvpIGAVGELLIEGPILARGYLNDPEKTAAafIEDPAWLKQegsgrgrrlyrTGDLVRYNPDGSLEYVGRKDTQVKIRGQ 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 446 MYYPSEIENVIAE-MPNVLEACVFGIWDPvnGDEAAASLV------KKPGTQLEAQDVVEYVRKRITAKFKQLNGGA--- 515
Cdd:cd05918 367 RVELGEIEHHLRQsLPGAKEVVVEVVKPK--DGSSSPQLVafvvldGSSSGSGDGDSLFLEPSDEFRALVAELRSKLrqr 444
|
410 420 430
....*....|....*....|....*....|.
gi 281365686 516 ----------LIVDQIVRSGNRKTNRSAVKE 536
Cdd:cd05918 445 lpsymvpsvfLPLSHLPLTASGKIDRRALRE 475
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
74-243 |
8.25e-06 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 48.72 E-value: 8.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 74 AMRVASYMRNMGLGQTDIVGVMGRHTTHQSAVAYACFFNGTPLHALHNAYeeACI----AKL---FGITKPRLIFC-DGD 145
Cdd:PRK08180 79 VRAIAQALLDRGLSAERPLMILSGNSIEHALLALAAMYAGVPYAPVSPAY--SLVsqdfGKLrhvLELLTPGLVFAdDGA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 146 EYEKVKSATKDLQVTIVTMRNHP--RGSVRIQDVLTTP----VMQNFQPLrlkdGIDHTLAILSSSGTSGFPKAVTisNS 219
Cdd:PRK08180 157 AFARALAAVVPADVEVVAVRGAVpgRAATPFAALLATPptaaVDAAHAAV----GPDTIAKFLFTSGSTGLPKAVI--NT 230
|
170 180
....*....|....*....|....
gi 281365686 220 HKIIVdymainnSNIQYTSSTLDW 243
Cdd:PRK08180 231 HRMLC-------ANQQMLAQTFPF 247
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
196-467 |
8.90e-06 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 48.81 E-value: 8.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 196 DHTLAILSSSGTSGFPKAVTISnsHKIIVDYMAINNSNIQYTSSTLDWC-----------SGLSMAITSGVfsttsiiad 264
Cdd:PRK06814 793 DDPAVILFTSGSEGTPKGVVLS--HRNLLANRAQVAARIDFSPEDKVFNalpvfhsfgltGGLVLPLLSGV--------- 861
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 265 cdfdPGLFCRAIGKYRI---------SMVLLSSS-YLAIFANcpefeSA---DLSSLNYViFGGSSCSLEVQRKVRS-RL 330
Cdd:PRK06814 862 ----KVFLYPSPLHYRIipeliydtnATILFGTDtFLNGYAR-----YAhpyDFRSLRYV-FAGAEKVKEETRQTWMeKF 931
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 331 SHDCLNfCYGLTELNSAGSVNLNFDEKPNSVGRAIRGIKIKV-----IDEQGE--AQEPNVVgeicfhnsqkwAGYYKnP 403
Cdd:PRK06814 932 GIRILE-GYGVTETAPVIALNTPMHNKAGTVGRLLPGIEYRLepvpgIDEGGRlfVRGPNVM-----------LGYLR-A 998
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 281365686 404 DETRQIQD-SENWIHTGDLGYVDKDGYLFVIDRLKDMLKYQNIMYYPSEIENVIAEM-PNVLEACV 467
Cdd:PRK06814 999 ENPGVLEPpADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELwPDALHAAV 1064
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
357-495 |
2.87e-05 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 46.87 E-value: 2.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 357 KPNSVGRAIRGIKIKVIDEQ-GEAQEPNVVGEI---------C----------FHNSqkwagYYKNPDetRQIQDSENWi 416
Cdd:PRK10524 409 RLGSPGVPMYGYNVKLLNEVtGEPCGPNEKGVLviegplppgCmqtvwgdddrFVKT-----YWSLFG--RQVYSTFDW- 480
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281365686 417 htgdlGYVDKDGYLFVIDRLKDMLKYQNIMYYPSEIENVIAEMPNVLEACVFGIWDPVNGDEAAASLVKKPGTQLEAQD 495
Cdd:PRK10524 481 -----GIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPKDSDSLADRE 554
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
356-506 |
5.70e-05 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 46.04 E-value: 5.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 356 EKPNSVGRAIRGIKIKVIDEQGEAQEPNVVGEICFHNSqkWAGYYKN------PDETRQIQDSENWIHTGDLGYVDKDGY 429
Cdd:PLN02654 451 QKPGSATFPFFGVQPVIVDEKGKEIEGECSGYLCVKKS--WPGAFRTlygdheRYETTYFKPFAGYYFSGDGCSRDKDGY 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 430 LFVIDRLKDMLKYQNIMYYPSEIENVIAEMPNVLEACVFGIWDPVNGD--EAAASLVKK-PGTQLEAQDVVEYVRKRITA 506
Cdd:PLN02654 529 YWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEVKGQgiYAFVTLVEGvPYSEELRKSLILTVRNQIGA 608
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
339-426 |
2.34e-04 |
|
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: 43.98 E-value: 2.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365686 339 YGLTElnsAGSVNLNfdekpnsvGRAIRG--IKIKVID--EQG--EAQEPNVVGEICFHNSQKWAGYYKNPDETRQIQDS 412
Cdd:cd17632 394 YGSTE---AGAVILD--------GVIVRPpvLDYKLVDvpELGyfRTDRPHPRGELLVKTDTLFPGYYKRPEVTAEVFDE 462
|
90 100
....*....|....*....|...
gi 281365686 413 ENWIHTGD---------LGYVDK 426
Cdd:cd17632 463 DGFYRTGDvmaelgpdrLVYVDR 485
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| |
