|
Name |
Accession |
Description |
Interval |
E-value |
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
9-536 |
0e+00 |
|
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: 896.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 9 NIVYGGPVTERQAQDSRSLGQYILDKYKSFGDRTVLVDAVNGVEYSASFMHKSIVRLAYILQKLGVKQNDVVGLSSENSV 88
Cdd:cd17642 1 IIVGPGPFYPLEDGTAGEQLHKAMKRYASVPGTIAFTDAHTGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 89 NFALAMFAGLAVGATVAPLNVTYSDREVDHAINLSKPKIIFASKITIDRVAKVASKNKFVKGIIALSGtskkfknIYDLK 168
Cdd:cd17642 81 QFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFCSKKGLQKVLNVQKKLKIIKTIIILDS-------KEDYK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 169 ELMEDEKFKTQP--------DFTSPAANKDEDVSLIVCSSGTTGLPKGVQLTQMNLLATLDSQIQPTVI--PMEEVTLLT 238
Cdd:cd17642 154 GYQCLYTFITQNlppgfneyDFKPPSFDRDEQVALIMNSSGSTGLPKGVQLTHKNIVARFSHARDPIFGnqIIPDTAILT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 239 VIPWFHAFGCLTLITTACVGARLVYLPKFEEKLFLSAIEKYRVMMAFMVPPLMVFLAKHPIVDKYDLSSLMVLLCGAAPL 318
Cdd:cd17642 234 VIPFHHGFGMFTTLGYLICGFRVVLMYKFEEELFLRSLQDYKVQSALLVPTLFAFFAKSTLVDKYDLSNLHEIASGGAPL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 319 SRETEDQIKERIGVPFIRQGYGLSESTLSVLVQNDEFCKPGSVGVLKVGIYAKVIDPDTGKLLGANERGELCFKGDGIMK 398
Cdd:cd17642 314 SKEVGEAVAKRFKLPGIRQGYGLTETTSAILITPEGDDKPGAVGKVVPFFYAKVVDLDTGKTLGPNERGELCVKGPMIMK 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 399 GYIGDTKSTQTAI-KDGWLHTGDIGYYDDDFEFFIVDRIKELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGE 477
Cdd:cd17642 394 GYVNNPEATKALIdKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGE 473
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 21355181 478 LPLAFVVKQANVQLTENEVIQFVNDNASPAKRLRGGVIFVDEIPKNPSGKILRRILREM 536
Cdd:cd17642 474 LPAAVVVLEAGKTMTEKEVMDYVASQVSTAKRLRGGVKFVDEVPKGLTGKIDRRKIREI 532
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
43-529 |
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: 554.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 43 VLVDAVNGVEYSASFMHKSIVRLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREVDHAINL 122
Cdd:cd05911 1 AQIDADTGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 123 SKPKIIFASKITIDRVAKVASKNKFVKGIIALSGTSKKFKNIYDLKELMEDEKFKTQPDftsPAANKDEDVSLIVCSSGT 202
Cdd:cd05911 81 SKPKVIFTDPDGLEKVKEAAKELGPKDKIIVLDDKPDGVLSIEDLLSPTLGEEDEDLPP---PLKDGKDDTAAILYSSGT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 203 TGLPKGVQLTQMNLLATLDSQIQPTVIPME-EVTLLTVIPWFHAFGCLTLITTACVGARLVYLPKFEEKLFLSAIEKYRV 281
Cdd:cd05911 158 TGLPKGVCLSHRNLIANLSQVQTFLYGNDGsNDVILGFLPLYHIYGLFTTLASLLNGATVIIMPKFDSELFLDLIEKYKI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 282 MMAFMVPPLMVFLAKHPIVDKYDLSSLMVLLCGAAPLSRETEDQIKERIGVPFIRQGYGLSESTLSVLVQNDEFCKPGSV 361
Cdd:cd05911 238 TFLYLVPPIAAALAKSPLLDKYDLSSLRVILSGGAPLSKELQELLAKRFPNATIKQGYGMTETGGILTVNPDGDDKPGSV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 362 GVLKVGIYAKVIDPDTGKLLGANERGELCFKGDGIMKGYIGDTKSTQTAI-KDGWLHTGDIGYYDDDFEFFIVDRIKELI 440
Cdd:cd05911 318 GRLLPNVEAKIVDDDGKDSLGPNEPGEICVRGPQVMKGYYNNPEATKETFdEDGWLHTGDIGYFDEDGYLYIVDRKKELI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 441 KYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGELPLAFVVKQANVQLTENEVIQFVNDNASPAKRLRGGVIFVDEI 520
Cdd:cd05911 398 KYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGEKLTEKEVKDYVAKKVASYKQLRGGVVFVDEI 477
|
....*....
gi 21355181 521 PKNPSGKIL 529
Cdd:cd05911 478 PKSASGKIL 486
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
26-533 |
2.76e-172 |
|
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: 496.76 E-value: 2.76e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 26 SLGQYILDKYKSFGDRTVLVDAVNGVEYSASFMHKSIVRLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVA 105
Cdd:cd05904 6 PLDSVSFLFASAHPSRPALIDAATGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 106 PLNVTYSDREVDHAINLSKPKIIFAskiTIDRVAKVASknkFVKGIIALSgtSKKFKNIYdlkelMEDEKFKTQPDFTSP 185
Cdd:cd05904 86 TANPLSTPAEIAKQVKDSGAKLAFT---TAELAEKLAS---LALPVVLLD--SAEFDSLS-----FSDLLFEADEAEPPV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 186 AANKDEDVSLIVCSSGTTGLPKGVQLTQMNLLATLDSQ--IQPTVIPMEEVTLLtVIPWFHAFGcLTLITTA--CVGARL 261
Cdd:cd05904 153 VVIKQDDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQFvaGEGSNSDSEDVFLC-VLPMFHIYG-LSSFALGllRLGATV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 262 VYLPKFEEKLFLSAIEKYRVMMAFMVPPLMVFLAKHPIVDKYDLSSLMVLLCGAAPLSRETEDQIKERIGVPFIRQGYGL 341
Cdd:cd05904 231 VVMPRFDLEELLAAIERYKVTHLPVVPPIVLALVKSPIVDKYDLSSLRQIMSGAAPLGKELIEAFRAKFPNVDLGQGYGM 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 342 SEST---LSVLVQNDEFCKPGSVGVLKVGIYAKVIDPDTGKLLGANERGELCFKGDGIMKGYIGDTKSTQTAI-KDGWLH 417
Cdd:cd05904 311 TESTgvvAMCFAPEKDRAKYGSVGRLVPNVEAKIVDPETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATIdKEGWLH 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 418 TGDIGYYDDDFEFFIVDRIKELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGELPLAFVVKQANVQLTENEVI 497
Cdd:cd05904 391 TGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKPGSSLTEDEIM 470
|
490 500 510
....*....|....*....|....*....|....*.
gi 21355181 498 QFVNDNASPAKRLRgGVIFVDEIPKNPSGKILRRIL 533
Cdd:cd05904 471 DFVAKQVAPYKKVR-KVAFVDAIPKSPSGKILRKEL 505
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
26-537 |
1.23e-148 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 437.49 E-value: 1.23e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 26 SLGQYILDKYKSFGDRTVLVDAVNGVEYSASFMHKSIVRLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVA 105
Cdd:PLN02246 24 PLHDYCFERLSEFSDRPCLIDGATGRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 106 PLNVTYSDREVDHAINLSKPKIIFASKITIDRVAKVASKNKFVkgIIALSGTSKKFKNIYDLKELMEDE--KFKTQPDft 183
Cdd:PLN02246 104 TANPFYTPAEIAKQAKASGAKLIITQSCYVDKLKGLAEDDGVT--VVTIDDPPEGCLHFSELTQADENElpEVEISPD-- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 184 spaankdeDVSLIVCSSGTTGLPKGVQLTQMNLLATLDSQI---QPTVIPMEEVTLLTVIPWFHAFgCLTLITTAC--VG 258
Cdd:PLN02246 180 --------DVVALPYSSGTTGLPKGVMLTHKGLVTSVAQQVdgeNPNLYFHSDDVILCVLPMFHIY-SLNSVLLCGlrVG 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 259 ARLVYLPKFEEKLFLSAIEKYRVMMAFMVPPLMVFLAKHPIVDKYDLSSLMVLLCGAAPLSRETEDQIKERIGVPFIRQG 338
Cdd:PLN02246 251 AAILIMPKFEIGALLELIQRHKVTIAPFVPPIVLAIAKSPVVEKYDLSSIRMVLSGAAPLGKELEDAFRAKLPNAVLGQG 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 339 YGLSESTlSVLVQNDEFCK------PGSVGVLKVGIYAKVIDPDTGKLLGANERGELCFKGDGIMKGYIGDTKSTQTAI- 411
Cdd:PLN02246 331 YGMTEAG-PVLAMCLAFAKepfpvkSGSCGTVVRNAELKIVDPETGASLPRNQPGEICIRGPQIMKGYLNDPEATANTId 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 412 KDGWLHTGDIGYYDDDFEFFIVDRIKELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGELPLAFVVKQANVQL 491
Cdd:PLN02246 410 KDGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVVRSNGSEI 489
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 21355181 492 TENEVIQFVNDNASPAKRLRgGVIFVDEIPKNPSGKILRRILREML 537
Cdd:PLN02246 490 TEDEIKQFVAKQVVFYKRIH-KVFFVDSIPKAPSGKILRKDLRAKL 534
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
27-540 |
6.74e-137 |
|
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: 404.19 E-value: 6.74e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 27 LGQYILDKYKSFGDRTVLVDAvnGVEYSASFMHKSIVRLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAP 106
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFG--GRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 107 LNVTYSDREVDHAINLSKPKIIFaskitidrvakvasknkfvkgiialsgtskkfkniydlkelmedekfktqpdftspa 186
Cdd:COG0318 79 LNPRLTAEELAYILEDSGARALV--------------------------------------------------------- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 187 ankdedVSLIVCSSGTTGLPKGVQLTQMNLLATLDSQIQptVIPM-EEVTLLTVIPWFHAFG-CLTLITTACVGARLVYL 264
Cdd:COG0318 102 ------TALILYTSGTTGRPKGVMLTHRNLLANAAAIAA--ALGLtPGDVVLVALPLFHVFGlTVGLLAPLLAGATLVLL 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 265 PKFEEKLFLSAIEKYRVMMAFMVPPLMVFLAKHPIVDKYDLSSLMVLLCGAAPLSRETEDQIKERIGVPFIrQGYGLSES 344
Cdd:COG0318 174 PRFDPERVLELIERERVTVLFGVPTMLARLLRHPEFARYDLSSLRLVVSGGAPLPPELLERFEERFGVRIV-EGYGLTET 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 345 TLSVLV--QNDEFCKPGSVGVLKVGIYAKVIDPDtGKLLGANERGELCFKGDGIMKGYIGDTKSTQTAIKDGWLHTGDIG 422
Cdd:COG0318 253 SPVVTVnpEDPGERRPGSVGRPLPGVEVRIVDED-GRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAFRDGWLRTGDLG 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 423 YYDDDFEFFIVDRIKELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGELPLAFVVKQANVQLTENEVIQFVND 502
Cdd:COG0318 332 RLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPGAELDAEELRAFLRE 411
|
490 500 510
....*....|....*....|....*....|....*...
gi 21355181 503 NASPAKRLRgGVIFVDEIPKNPSGKILRRILREMLKKQ 540
Cdd:COG0318 412 RLARYKVPR-RVEFVDELPRTASGKIDRRALRERYAAG 448
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
62-534 |
4.41e-115 |
|
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: 349.17 E-value: 4.41e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 62 IVRLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREVDHAINLSKPKIIfaskitidrvakv 141
Cdd:cd05936 34 AEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYTPRELEHILNDSGAKAL------------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 142 asknkfvkgIIALSgtskkFKniydlkelmedEKFKTQPDFTSPAANKDEDVSLIVCSSGTTGLPKGVQLTQMNLLATLd 221
Cdd:cd05936 101 ---------IVAVS-----FT-----------DLLAAGAPLGERVALTPEDVAVLQYTSGTTGVPKGAMLTHRNLVANA- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 222 SQIQ---PTVIPMEEVtLLTVIPWFHAFGCLT-LITTACVGARLVYLPKFEEKLFLSAIEKYRVMMAFMVPPLMVFLAKH 297
Cdd:cd05936 155 LQIKawlEDLLEGDDV-VLAALPLFHVFGLTVaLLLPLALGATIVLIPRFRPIGVLKEIRKHRVTIFPGVPTMYIALLNA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 298 PIVDKYDLSSLMVLLCGAAPLSRETEDQIKERIGVPfIRQGYGLSEsTLSVLVQN--DEFCKPGSVGVLKVGIYAKVIDP 375
Cdd:cd05936 234 PEFKKRDFSSLRLCISGGAPLPVEVAERFEELTGVP-IVEGYGLTE-TSPVVAVNplDGPRKPGSIGIPLPGTEVKIVDD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 376 DtGKLLGANERGELCFKGDGIMKGYIGDTKSTQTAIKDGWLHTGDIGYYDDDFEFFIVDRIKELIKYKGYQVPPAEIEAL 455
Cdd:cd05936 312 D-GEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFVDGWLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEV 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21355181 456 LLTNDKIKDAAVIGKPDEEAGELPLAFVVKQANVQLTENEVIQFVNDNASPAKRLRgGVIFVDEIPKNPSGKILRRILR 534
Cdd:cd05936 391 LYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEGASLTEEEIIAFCREQLAGYKVPR-QVEFRDELPKSAVGKILRRELR 468
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
36-541 |
8.38e-114 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 347.56 E-value: 8.38e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 36 KSFGDRTVLVDAVNGVEYsASFmHKSIVRLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDRE 115
Cdd:PRK06187 17 RKHPDKEAVYFDGRRTTY-AEL-DERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPINIRLKPEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 116 VDHAINLSKPKIIFASKITIDRVAKVASKNKFVKGIIALSGTSKKFKNIY--DLKELMEDekfktQPDfTSPAANKDE-D 192
Cdd:PRK06187 95 IAYILNDAEDRVVLVDSEFVPLLAAILPQLPTVRTVIVEGDGPAAPLAPEvgEYEELLAA-----ASD-TFDFPDIDEnD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 193 VSLIVCSSGTTGLPKGVQLTQMNLLA-TLDSQIQPTVIPmEEVTLLtVIPWFHAFGcLTLITTAC-VGARLVYLPKFEEK 270
Cdd:PRK06187 169 AAAMLYTSGTTGHPKGVVLSHRNLFLhSLAVCAWLKLSR-DDVYLV-IVPMFHVHA-WGLPYLALmAGAKQVIPRRFDPE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 271 LFLSAIEKYRVMMAFMVPPLMVFLAKHPIVDKYDLSSLMVLLCGAAPLSRETEDQIKERIGVPFIrQGYGLSES--TLSV 348
Cdd:PRK06187 246 NLLDLIETERVTFFFAVPTIWQMLLKAPRAYFVDFSSLRLVIYGGAALPPALLREFKEKFGIDLV-QGYGMTETspVVSV 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 349 LVQNDE----FCKPGSVGVLKVGIYAKVIDPDtGKLLGAN--ERGELCFKGDGIMKGYIGDTKSTQTAIKDGWLHTGDIG 422
Cdd:PRK06187 325 LPPEDQlpgqWTKRRSAGRPLPGVEARIVDDD-GDELPPDggEVGEIIVRGPWLMQGYWNRPEATAETIDGGWLHTGDVG 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 423 YYDDDFEFFIVDRIKELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGELPLAFVVKQANVQLTENEVIQFVND 502
Cdd:PRK06187 404 YIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVLKPGATLDAKELRAFLRG 483
|
490 500 510
....*....|....*....|....*....|....*....
gi 21355181 503 NASPAKRLRgGVIFVDEIPKNPSGKILRRILREMLKKQK 541
Cdd:PRK06187 484 RLAKFKLPK-RIAFVDELPRTSVGKILKRVLREQYAEGK 521
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
192-529 |
3.16e-105 |
|
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: 318.85 E-value: 3.16e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 192 DVSLIVCSSGTTGLPKGVQLTQMNLLATLDSQIQPTVIPMEEVTLLTViPWFHAFGCLTLITTACVGARLVYLPKFEEKL 271
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTL-PLFHIGGLFGLLGALLAGGTVVLLPKFDPEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 272 FLSAIEKYRVMMAFMVPPLMVFLAKHPIVDKYDLSSLMVLLCGAAPLSRETEDQIKERIGVPFIrQGYGLSESTLSVLVQ 351
Cdd:cd04433 80 ALELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGAPLPPELLERFEEAPGIKLV-NGYGLTETGGTVATG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 352 N--DEFCKPGSVGVLKVGIYAKVIDPDTGkLLGANERGELCFKGDGIMKGYIGDTKSTQTAIKDGWLHTGDIGYYDDDFE 429
Cdd:cd04433 159 PpdDDARKPGSVGRPVPGVEVRIVDPDGG-ELPPGEIGELVVRGPSVMKGYWNNPEATAAVDEDGWYRTGDLGRLDEDGY 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 430 FFIVDRIKELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGELPLAFVVKQANVQLTENEVIQFVNDNASPAKR 509
Cdd:cd04433 238 LYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLDAEELRAHVRERLAPYKV 317
|
330 340
....*....|....*....|
gi 21355181 510 LRgGVIFVDEIPKNPSGKIL 529
Cdd:cd04433 318 PR-RVVFVDALPRTASGKID 336
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
23-542 |
5.35e-104 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 323.08 E-value: 5.35e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 23 DSRSLGQYILDKYKSFGDRTVLVDAVNGVEYSASFMHKSIVRLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGA 102
Cdd:PLN02330 26 DKLTLPDFVLQDAELYADKVAFVEAVTGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 103 TVAPLNVTYSDREVDHAINLSKPKIIFASKITIDRVAKVASKnkfvkgIIALSGTskKFKNIYDLKELMEdekfktQPDF 182
Cdd:PLN02330 106 VFSGANPTALESEIKKQAEAAGAKLIVTNDTNYGKVKGLGLP------VIVLGEE--KIEGAVNWKELLE------AADR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 183 TSPAANKDEDVSLIVC----SSGTTGLPKGVQLTQMNLLATLDSQ---IQPTVIpmEEVTLLTVIPWFHAFGcltlITTA 255
Cdd:PLN02330 172 AGDTSDNEEILQTDLCalpfSSGTTGISKGVMLTHRNLVANLCSSlfsVGPEMI--GQVVTLGLIPFFHIYG----ITGI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 256 CVG-----ARLVYLPKFEEKLFLSAIEKYRVMMAFMVPPLMVFLAKHPIVDKYDLSSLMV--LLCGAAPLSRETEDQIKE 328
Cdd:PLN02330 246 CCAtlrnkGKVVVMSRFELRTFLNALITQEVSFAPIVPPIILNLVKNPIVEEFDLSKLKLqaIMTAAAPLAPELLTAFEA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 329 RIGVPFIRQGYGLSESTLSVLVQNDE-----FCKPGSVGVLKVGIYAKVIDPDTGKLLGANERGELCFKGDGIMKGYIGD 403
Cdd:PLN02330 326 KFPGVQVQEAYGLTEHSCITLTHGDPekghgIAKKNSVGFILPNLEVKFIDPDTGRSLPKNTPGELCVRSQCVMQGYYNN 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 404 TKSTQTAI-KDGWLHTGDIGYYDDDFEFFIVDRIKELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGELPLAF 482
Cdd:PLN02330 406 KEETDRTIdEDGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAAC 485
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21355181 483 VVKQANVQLTENEVIQFVNDNASPAKRLRgGVIFVDEIPKNPSGKILRRILRE-MLKKQKS 542
Cdd:PLN02330 486 VVINPKAKESEEDILNFVAANVAHYKKVR-VVQFVDSIPKSLSGKIMRRLLKEkMLSINKA 545
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
39-530 |
1.70e-101 |
|
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: 313.01 E-value: 1.70e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 39 GDRTVLVDAvnGVEYSASFMHKSIVRLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREVDH 118
Cdd:cd17631 9 PDRTALVFG--GRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEVAY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 119 AINLSKPKIIFaskitidrvakvasknkfvkgiialsgtskkfkniydlkelmedekfktqpdftspaankdEDVSLIVC 198
Cdd:cd17631 87 ILADSGAKVLF-------------------------------------------------------------DDLALLMY 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 199 SSGTTGLPKGVQLTQMNLLATLDSQIQPTVIPMEEVTLLtVIPWFH--AFGCLTLITTAcVGARLVYLPKFEEKLFLSAI 276
Cdd:cd17631 106 TSGTTGRPKGAMLTHRNLLWNAVNALAALDLGPDDVLLV-VAPLFHigGLGVFTLPTLL-RGGTVVILRKFDPETVLDLI 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 277 EKYRVMMAFMVPPLMVFLAKHPIVDKYDLSSLMVLLCGAAPLSRETEDQIKERiGVPFIrQGYGLSEST--LSVLVQNDE 354
Cdd:cd17631 184 ERHRVTSFFLVPTMIQALLQHPRFATTDLSSLRAVIYGGAPMPERLLRALQAR-GVKFV-QGYGMTETSpgVTFLSPEDH 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 355 FCKPGSVGVLKVGIYAKVIDPDtGKLLGANERGELCFKGDGIMKGYIGDTKSTQTAIKDGWLHTGDIGYYDDDFEFFIVD 434
Cdd:cd17631 262 RRKLGSAGRPVFFVEVRIVDPD-GREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFRDGWFHTGDLGRLDEDGYLYIVD 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 435 RIKELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGELPLAFVVKQANVQLTENEVIQFVNDNASPAKRLRgGV 514
Cdd:cd17631 341 RKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPGAELDEDELIAHCRERLARYKIPK-SV 419
|
490
....*....|....*.
gi 21355181 515 IFVDEIPKNPSGKILR 530
Cdd:cd17631 420 EFVDALPRNATGKILK 435
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
40-537 |
3.18e-100 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 313.70 E-value: 3.18e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 40 DRTVLVDAVNGVEYSASFMHKSIVRLAY-ILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREVDH 118
Cdd:PLN02574 54 GDTALIDSSTGFSISYSELQPLVKSMAAgLYHVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKK 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 119 AINLSKPKIIFASkitIDRVAKVASKNKFVKGIIALSGTSKKFKNIYDLKELMedekfKTQPDFTSPAANKDEDVSLIVC 198
Cdd:PLN02574 134 RVVDCSVGLAFTS---PENVEKLSPLGVPVIGVPENYDFDSKRIEFPKFYELI-----KEDFDFVPKPVIKQDDVAAIMY 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 199 SSGTTGLPKGVQLTQMNLLATLD-------SQIQptvIPMEEVTLLTVIPWFHAFGcLTLITTACV--GARLVYLPKFEE 269
Cdd:PLN02574 206 SSGTTGASKGVVLTHRNLIAMVElfvrfeaSQYE---YPGSDNVYLAALPMFHIYG-LSLFVVGLLslGSTIVVMRRFDA 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 270 KLFLSAIEKYRVMMAFMVPPLMVFLAKHP-IVDKYDLSSLMVLLCGAAPLSRET-EDQIKERIGVPFIrQGYGLSESTL- 346
Cdd:PLN02574 282 SDMVKVIDRFKVTHFPVVPPILMALTKKAkGVCGEVLKSLKQVSCGAAPLSGKFiQDFVQTLPHVDFI-QGYGMTESTAv 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 347 -SVLVQNDEFCKPGSVGVLKVGIYAKVIDPDTGKLLGANERGELCFKGDGIMKGYIGDTKSTQ-TAIKDGWLHTGDIGYY 424
Cdd:PLN02574 361 gTRGFNTEKLSKYSSVGLLAPNMQAKVVDWSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQsTIDKDGWLRTGDIAYF 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 425 DDDFEFFIVDRIKELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGELPLAFVVKQANVQLTENEVIQFVNDNA 504
Cdd:PLN02574 441 DEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQGSTLSQEAVINYVAKQV 520
|
490 500 510
....*....|....*....|....*....|...
gi 21355181 505 SPAKRLRgGVIFVDEIPKNPSGKILRRILREML 537
Cdd:PLN02574 521 APYKKVR-KVVFVQSIPKSPAGKILRRELKRSL 552
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
64-443 |
2.71e-94 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 293.83 E-value: 2.71e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 64 RLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREVDHAINLSKPKIIFASKI-TIDRVAKVA 142
Cdd:pfam00501 33 RLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDSGAKVLITDDAlKLEELLEAL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 143 SKNKFVKGIIALSGTSkkfkniYDLKELMEDEKFKTQPDFTSPAANKDEDVSLIVCSSGTTGLPKGVQLTQMNLLATLDS 222
Cdd:pfam00501 113 GKLEVVKLVLVLDRDP------VLKEEPLPEEAKPADVPPPPPPPPDPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLS 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 223 Q--IQPTVIPMEEV-TLLTVIPWFHAFGCLT-LITTACVGARLVYLPKFEE---KLFLSAIEKYRVMMAFMVPPLMVFLA 295
Cdd:pfam00501 187 IkrVRPRGFGLGPDdRVLSTLPLFHDFGLSLgLLGPLLAGATVVLPPGFPAldpAALLELIERYKVTVLYGVPTLLNMLL 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 296 KHPIVDKYDLSSLMVLLCGAAPLSRETEDQIKERIGVPFIrQGYGLSESTLSVLV---QNDEFCKPGSVGVLKVGIYAKV 372
Cdd:pfam00501 267 EAGAPKRALLSSLRLVLSGGAPLPPELARRFRELFGGALV-NGYGLTETTGVVTTplpLDEDLRSLGSVGRPLPGTEVKI 345
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21355181 373 IDPDTGKLLGANERGELCFKGDGIMKGYIGDTKSTQTAIK-DGWLHTGDIGYYDDDFEFFIVDRIKELIKYK 443
Cdd:pfam00501 346 VDDETGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDeDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
36-536 |
2.76e-93 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 294.12 E-value: 2.76e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 36 KSFGDRTVLVDAVNGVEYSAsfMHKSIVRLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDRE 115
Cdd:PRK07656 16 RRFGDKEAYVFGDQRLTYAE--LNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 116 VDHAINLSKPKIIFASKITIDRVAKVASKNKFVKGIIALSGTSKKfkniydlkelMEDEKFKTQPDFTSPAAN------- 188
Cdd:PRK07656 94 AAYILARGDAKALFVLGLFLGVDYSATTRLPALEHVVICETEEDD----------PHTEKMKTFTDFLAAGDPaerapev 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 189 KDEDVSLIVCSSGTTGLPKGVQLTQMNLLATLDS-----QIQptvipmEEVTLLTVIPWFHAFgCLTLITTACV--GARL 261
Cdd:PRK07656 164 DPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADwaeylGLT------EGDRYLAANPFFHVF-GYKAGVNAPLmrGATI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 262 VYLPKFEEKLFLSAIEKYRVMMAFMVPPLMVFLAKHPIVDKYDLSSLMVLLCGAAPLSRETEDQIKERIGVPFIRQGYGL 341
Cdd:PRK07656 237 LPLPVFDPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSAEDLSSLRLAVTGAASMPVALLERFESELGVDIVLTGYGL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 342 SES----TLSVLvqNDEF-CKPGSVGVLKVGIYAKVIDPDtGKLLGANERGELCFKGDGIMKGYIGDTKSTQTAIK-DGW 415
Cdd:PRK07656 317 SEAsgvtTFNRL--DDDRkTVAGTIGTAIAGVENKIVNEL-GEEVPVGEVGELLVRGPNVMKGYYDDPEATAAAIDaDGW 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 416 LHTGDIGYYDDDFEFFIVDRIKELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGELPLAFVVKQANVQLTENE 495
Cdd:PRK07656 394 LHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVLKPGAELTEEE 473
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 21355181 496 VIQFVNDNASPAKRLRgGVIFVDEIPKNPSGKILRRILREM 536
Cdd:PRK07656 474 LIAYCREHLAKYKVPR-SIEFLDELPKNATGKVLKRALREK 513
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
64-533 |
4.13e-88 |
|
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: 278.21 E-value: 4.13e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 64 RLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREVDHAINlskpkiifaskitiDRVAKVAs 143
Cdd:cd05935 13 KLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILN--------------DSGAKVA- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 144 knkfvkgiIALSgtskkfkniydlkELmedekfktqpdftspaankdEDVSLIVCSSGTTGLPKGVQLTQMNLLATLDSQ 223
Cdd:cd05935 78 --------VVGS-------------EL--------------------DDLALIPYTSGTTGLPKGCMHTHFSAAANALQS 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 224 IQPTVIPMEEVTLLTvIPWFHAFGCLTLITTAC-VGARLVYLPKFEEKLFLSAIEKYRVMMAFMVPPLMVFLAKHPIVDK 302
Cdd:cd05935 117 AVWTGLTPSDVILAC-LPLFHVTGFVGSLNTAVyVGGTYVLMARWDRETALELIEKYKVTFWTNIPTMLVDLLATPEFKT 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 303 YDLSSLMVLLCGAAPLSRETEDQIKERIGVPFIrQGYGLSESTLSVLVQNDEFCKPGSVGVLKVGIYAKVIDPDTGKLLG 382
Cdd:cd05935 196 RDLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFV-EGYGLTETMSQTHTNPPLRPKLQCLGIP*FGVDARVIDIETGRELP 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 383 ANERGELCFKGDGIMKGYIGDTKSTQTA-IKDG---WLHTGDIGYYDDDFEFFIVDRIKELIKYKGYQVPPAEIEALLLT 458
Cdd:cd05935 275 PNEVGEIVVRGPQIFKGYWNRPEETEESfIEIKgrrFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYK 354
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21355181 459 NDKIKDAAVIGKPDEEAGELPLAFVV--KQANVQLTENEVIQFVNDNASPAKRLRgGVIFVDEIPKNPSGKILRRIL 533
Cdd:cd05935 355 HPAI*EVCVISVPDERVGEEVKAFIVlrPEYRGKVTEEDIIEWAREQMAAYKYPR-EVEFVDELPRSASGKILWRLL 430
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
62-535 |
4.62e-82 |
|
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: 264.56 E-value: 4.62e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 62 IVRLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREVDHAINLSKPKIIFASKITIDRVAKV 141
Cdd:cd05926 24 VDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVLTPKGELGPASRA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 142 ASKnkFVKGIIALSGTSKKFKNIYDLKELMEDEKFKTQPdfTSPAANKDEDVSLIVCSSGTTGLPKGVQLTQMNLLATLd 221
Cdd:cd05926 104 ASK--LGLAILELALDVGVLIRAPSAESLSNLLADKKNA--KSEGVPLPDDLALILHTSGTTGRPKGVPLTHRNLAASA- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 222 SQIQPTVIPMEEVTLLTVIPWFHAFGCL-TLITTACVGARLVYLPKFEEKLFLSAIEKYRVMMAFMVPPLMVFLAKHPIV 300
Cdd:cd05926 179 TNITNTYKLTPDDRTLVVMPLFHVHGLVaSLLSTLAAGGSVVLPPRFSASTFWPDVRDYNATWYTAVPTIHQILLNRPEP 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 301 DKYD-LSSLMVLLCGAAPLSRETEDQIKERIGVPFIrQGYGLSEST-------LSVLVQndefcKPGSVGvLKVGIYAKV 372
Cdd:cd05926 259 NPESpPPKLRFIRSCSASLPPAVLEALEATFGAPVL-EAYGMTEAAhqmtsnpLPPGPR-----KPGSVG-KPVGVEVRI 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 373 IDPDtGKLLGANERGELCFKGDGIMKGYIGDTKSTQT-AIKDGWLHTGDIGYYDDDFEFFIVDRIKELIKYKGYQVPPAE 451
Cdd:cd05926 332 LDED-GEILPPGVVGEICLRGPNVTRGYLNNPEANAEaAFKDGWFRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLE 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 452 IEALLLTNDKIKDAAVIGKPDEEAGELPLAFVVKQANVQLTENEVIQFVNDN-AS---PAKrlrggVIFVDEIPKNPSGK 527
Cdd:cd05926 411 VDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGASVTEEELRAFCRKHlAAfkvPKK-----VYFVDELPKTATGK 485
|
....*...
gi 21355181 528 ILRRILRE 535
Cdd:cd05926 486 IQRRKVAE 493
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
30-540 |
4.40e-80 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 261.20 E-value: 4.40e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 30 YILDKY-KSFGDRTVLV-DAVNGVEYSASF--MHKSIVRLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVA 105
Cdd:COG0365 13 NCLDRHaEGRGDKVALIwEGEDGEERTLTYaeLRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 106 PLNVTYSDREVDHAINLSKPKIIFASKITI---------DRVAKVASKNKFVKGIIALSGTSKK--FKNIYDLKELMEDe 174
Cdd:COG0365 93 PVFPGFGAEALADRIEDAEAKVLITADGGLrggkvidlkEKVDEALEELPSLEHVIVVGRTGADvpMEGDLDWDELLAA- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 175 kfktQPDFTSPAANKDEDVSLIVCSSGTTGLPKGVQLTQMNLLATLDS------QIQPtvipmEEVtLLTVIPWFHAFGc 248
Cdd:COG0365 172 ----ASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATtakyvlDLKP-----GDV-FWCTADIGWATG- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 249 LTLITTA--CVGARLVYlpkFEEKL-------FLSAIEKYRVMMAFMVPPLMVFLAKHPI--VDKYDLSSLMVLLCGAAP 317
Cdd:COG0365 241 HSYIVYGplLNGATVVL---YEGRPdfpdpgrLWELIEKYGVTVFFTAPTAIRALMKAGDepLKKYDLSSLRLLGSAGEP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 318 LSRETEDQIKERIGVPfIRQGYGLSEsTLSVLVQNDEF--CKPGSVGVLKVGIYAKVIDPDtGKLLGANERGELCFKGD- 394
Cdd:COG0365 318 LNPEVWEWWYEAVGVP-IVDGWGQTE-TGGIFISNLPGlpVKPGSMGKPVPGYDVAVVDED-GNPVPPGEEGELVIKGPw 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 395 -GIMKGYIGD---TKSTQTAIKDGWLHTGDIGYYDDDFEFFIVDRIKELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGK 470
Cdd:COG0365 395 pGMFRGYWNDperYRETYFGRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVGV 474
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21355181 471 PDEEAGELPLAFVVKQANVQLTE---NEVIQFVNDNASPAKRLRgGVIFVDEIPKNPSGKILRRILREMLKKQ 540
Cdd:COG0365 475 PDEIRGQVVKAFVVLKPGVEPSDelaKELQAHVREELGPYAYPR-EIEFVDELPKTRSGKIMRRLLRKIAEGR 546
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
21-541 |
2.55e-77 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 254.19 E-value: 2.55e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 21 AQDSRSLGQYILDKYKSFGDRTVLvdAVNGVEYSASFMHKSIVRLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAV 100
Cdd:PRK06710 20 SYDIQPLHKYVEQMASRYPEKKAL--HFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 101 GATVAPLNVTYSDREVDHAINLSKPKIIFASKITIDRVAKVASKNK--------------FVKGIIALSGTSKKFKNIYD 166
Cdd:PRK06710 98 GGIVVQTNPLYTERELEYQLHDSGAKVILCLDLVFPRVTNVQSATKiehvivtriadflpFPKNLLYPFVQKKQSNLVVK 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 167 LKEL----MEDEKFKTQPDFTSPAANKDEDVSLIVCSSGTTGLPKGVQLTQMNLLATLDSQIQ--PTVIPMEEVtLLTVI 240
Cdd:PRK06710 178 VSESetihLWNSVEKEVNTGVEVPCDPENDLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQwlYNCKEGEEV-VLGVL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 241 PWFHAFGCLTLITTACV-GARLVYLPKFEEKLFLSAIEKYRVMMAFMVPPLMVFLAKHPIVDKYDLSSLMVLLCGAAPLS 319
Cdd:PRK06710 257 PFFHVYGMTAVMNLSIMqGYKMVLIPKFDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLLKEYDISSIRACISGSAPLP 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 320 RETEDQIkERIGVPFIRQGYGLSESTlSVLVQNDEFCK--PGSVGVLKVGIYAKVIDPDTGKLLGANERGELCFKGDGIM 397
Cdd:PRK06710 337 VEVQEKF-ETVTGGKLVEGYGLTESS-PVTHSNFLWEKrvPGSIGVPWPDTEAMIMSLETGEALPPGEIGEIVVKGPQIM 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 398 KGYIGDTKSTQTAIKDGWLHTGDIGYYDDDFEFFIVDRIKELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGE 477
Cdd:PRK06710 415 KGYWNKPEETAAVLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGE 494
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21355181 478 LPLAFVVKQANVQLTENEVIQFVNDNASpAKRLRGGVIFVDEIPKNPSGKILRRILREMLKKQK 541
Cdd:PRK06710 495 TVKAFVVLKEGTECSEEELNQFARKYLA-AYKVPKVYEFRDELPKTTVGKILRRVLIEEEKRKN 557
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
50-541 |
6.55e-73 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 241.79 E-value: 6.55e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 50 GVEYSASFMHKSIVRLA-YILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREVDHAINLSKPKII 128
Cdd:PRK08314 33 GRAISYRELLEEAERLAgYLQQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHYVTDSGARVA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 129 FASKITIDRVAKVASKNKFVKGIIALSGTSKKFKNIYDLKELMEDEKFKTQPDFTSPAANKD---------------EDV 193
Cdd:PRK08314 113 IVGSELAPKVAPAVGNLRLRHVIVAQYSDYLPAEPEIAVPAWLRAEPPLQALAPGGVVAWKEalaaglappphtagpDDL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 194 SLIVCSSGTTGLPKGVQLTQMNLLATLDSQIQPTVIPMEEVTLlTVIPWFHAFGCLTLITTAC-VGARLVYLPKFEEKLF 272
Cdd:PRK08314 193 AVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVL-AVLPLFHVTGMVHSMNAPIyAGATVVLMPRWDREAA 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 273 LSAIEKYRVMMAFMVPPLMV-FLAKhPIVDKYDLSSLMVLLCGAAPLSRETEDQIKERIGVPFIrQGYGLSESTLSVLVQ 351
Cdd:PRK08314 272 ARLIERYRVTHWTNIPTMVVdFLAS-PGLAERDLSSLRYIGGGGAAMPEAVAERLKELTGLDYV-EGYGLTETMAQTHSN 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 352 NDEFCKPGSVGVLKVGIYAKVIDPDTGKLLGANERGELCFKGDGIMKGYIGDTKSTQTA-IK-DG--WLHTGDIGYYDDD 427
Cdd:PRK08314 350 PPDRPKLQCLGIPTFGVDARVIDPETLEELPPGEVGEIVVHGPQVFKGYWNRPEATAEAfIEiDGkrFFRTGDLGRMDEE 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 428 FEFFIVDRIKELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGELPLAFVVKQANVQ--LTENEVIQFVNDNAS 505
Cdd:PRK08314 430 GYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPDPRRGETVKAVVVLRPEARgkTTEEEIIAWAREHMA 509
|
490 500 510
....*....|....*....|....*....|....*...
gi 21355181 506 PAKRLRgGVIFVDEIPKNPSGKILRRIL--REMLKKQK 541
Cdd:PRK08314 510 AYKYPR-IVEFVDSLPKSGSGKILWRQLqeQEKARAAK 546
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
50-534 |
2.52e-72 |
|
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: 236.80 E-value: 2.52e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 50 GVEYSASFMHKSIVRLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREVDHAINLSKPKIIF 129
Cdd:cd05934 1 GRRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 130 ASKITIdrvakvasknkfvkgiialsgtskkfknIYdlkelmedekfktqpdftspaankdedvslivcSSGTTGLPKGV 209
Cdd:cd05934 81 VDPASI----------------------------LY---------------------------------TSGTTGPPKGV 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 210 QLTQMNLLATLDSQIQPTVIPMEEVtLLTVIPWFHAFG-CLTLITTACVGARLVYLPKFEEKLFLSAIEKYRVMMAFMVP 288
Cdd:cd05934 100 VITHANLTFAGYYSARRFGLGEDDV-YLTVLPLFHINAqAVSVLAALSVGATLVLLPRFSASRFWSDVRRYGATVTNYLG 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 289 PLMVFLAKHPIVDkyDLSSLMVLLCGAAPLSRETEDQIKERIGVPfIRQGYGLSESTLSVLVQNDEFCKPGSVGVLKVGI 368
Cdd:cd05934 179 AMLSYLLAQPPSP--DDRAHRLRAAYGAPNPPELHEEFEERFGVR-LLEGYGMTETIVGVIGPRDEPRRPGSIGRPAPGY 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 369 YAKVIDPDtGKLLGANERGELCFK---GDGIMKGYIGDTKSTQTAIKDGWLHTGDIGYYDDDFEFFIVDRIKELIKYKGY 445
Cdd:cd05934 256 EVRIVDDD-GQELPAGEPGELVIRglrGWGFFKGYYNMPEATAEAMRNGWFHTGDLGYRDADGFFYFVDRKKDMIRRRGE 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 446 QVPPAEIEALLLTNDKIKDAAVIGKPDEEAGELPLAFVVKQANVQLTENEVIQFVNDNASPAKRLRgGVIFVDEIPKNPS 525
Cdd:cd05934 335 NISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLDPEELFAFCEGQLAYFKVPR-YIRFVDDLPKTPT 413
|
....*....
gi 21355181 526 GKILRRILR 534
Cdd:cd05934 414 EKVAKAQLR 422
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
58-538 |
2.66e-72 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 238.99 E-value: 2.66e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 58 MHKSIVRLA-YILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREVDHAINLSKPKIIFASKiTID 136
Cdd:PRK06839 33 LHEYVSKVAaYLIYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTTVLFVEK-TFQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 137 RVAKVASKNKFVKGIIALSgtskkfkniyDLKELMEDEKfktqpdftSPAANKDEDVSLIVC-SSGTTGLPKGVQLTQMN 215
Cdd:PRK06839 112 NMALSMQKVSYVQRVISIT----------SLKEIEDRKI--------DNFVEKNESASFIICyTSGTTGKPKGAVLTQEN 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 216 L-------LATLDsqiqptvIPMEEVTLlTVIPWFHAFGC-LTLITTACVGARLVYLPKFEEKLFLSAIEKYRVMMAFMV 287
Cdd:PRK06839 174 MfwnalnnTFAID-------LTMHDRSI-VLLPLFHIGGIgLFAFPTLFAGGVIIVPRKFEPTKALSMIEKHKVTVVMGV 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 288 PPLMVFLAKHPIVDKYDLSSLMVLLCGAAPLSRETEDQIKERiGVPFiRQGYGLSES--TLSVLVQNDEFCKPGSVGVLK 365
Cdd:PRK06839 246 PTIHQALINCSKFETTNLQSVRWFYNGGAPCPEELMREFIDR-GFLF-GQGFGMTETspTVFMLSEEDARRKVGSIGKPV 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 366 VGIYAKVIDPDTGKLlGANERGELCFKGDGIMKGYIGDTKSTQTAIKDGWLHTGDIGYYDDDFEFFIVDRIKELIKYKGY 445
Cdd:PRK06839 324 LFCDYELIDENKNKV-EVGEVGELLIRGPNVMKEYWNRPDATEETIQDGWLCTGDLARVDEDGFVYIVGRKKEMIISGGE 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 446 QVPPAEIEALLLTNDKIKDAAVIGKPDEEAGELPLAFVVKQANVQLTENEVIQFVNDNASPAKRLRgGVIFVDEIPKNPS 525
Cdd:PRK06839 403 NIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVLIEKDVIEHCRLFLAKYKIPK-EIVFLKELPKNAT 481
|
490
....*....|...
gi 21355181 526 GKILRRILREMLK 538
Cdd:PRK06839 482 GKIQKAQLVNQLK 494
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
38-535 |
4.07e-70 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 234.06 E-value: 4.07e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 38 FGDRTVLVDavNGVEYSASFMHKSIVRLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREVD 117
Cdd:PRK08316 24 YPDKTALVF--GDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 118 HAINLSKPKIIFASKITIDRVAKVASKNKFVKGIIALSGTSKKfkniYDLKELMEDEKFKTQPDFTSPAANKDEDVSLIV 197
Cdd:PRK08316 102 YILDHSGARAFLVDPALAPTAEAALALLPVDTLILSLVLGGRE----APGGWLDFADWAEAGSVAEPDVELADDDLAQIL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 198 CSSGTTGLPKGVQLTQMNLLA-----TLDSQIQPTVIPmeevtlLTVIPWFH-----AFgcltLITTACVGARLVYLPKF 267
Cdd:PRK08316 178 YTSGTESLPKGAMLTHRALIAeyvscIVAGDMSADDIP------LHALPLYHcaqldVF----LGPYLYVGATNVILDAP 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 268 EEKLFLSAIEKYRVMMAFMVPPLMVFLAKHPIVDKYDLSSLMVLLCGAAPLSRETEDQIKERIgvPFIR--QGYGLSE-- 343
Cdd:PRK08316 248 DPELILRTIEAERITSFFAPPTVWISLLRHPDFDTRDLSSLRKGYYGASIMPVEVLKELRERL--PGLRfyNCYGQTEia 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 344 STLSVLVQNDEFCKPGSVG--VLKVgiYAKVIDPDtGKLLGANERGELCFKGDGIMKGYIGDTKSTQTAIKDGWLHTGDI 421
Cdd:PRK08316 326 PLATVLGPEEHLRRPGSAGrpVLNV--ETRVVDDD-GNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEAFRGGWFHSGDL 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 422 GYYDDDFEFFIVDRIKELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGELPLAFVVKQANVQLTENEVIQFVN 501
Cdd:PRK08316 403 GVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAGATVTEDELIAHCR 482
|
490 500 510
....*....|....*....|....*....|....
gi 21355181 502 DNASPAKRLRgGVIFVDEIPKNPSGKILRRILRE 535
Cdd:PRK08316 483 ARLAGFKVPK-RVIFVDELPRNPSGKILKRELRE 515
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
28-535 |
5.54e-67 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 225.64 E-value: 5.54e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 28 GQYILDKYKSFGDRTVLVDavNGVEYSASFMHKSIVRLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPL 107
Cdd:PRK06188 15 GHLLVSALKRYPDRPALVL--GDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 108 NVTYSdrEVDHAINLSKPKIifaSKITIDRVAkvasknkFVKGIIALSGTSKKFKNIYDLKELMEDEKFKTQPDFTSPA- 186
Cdd:PRK06188 93 HPLGS--LDDHAYVLEDAGI---STLIVDPAP-------FVERALALLARVPSLKHVLTLGPVPDGVDLLAAAAKFGPAp 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 187 ---ANKDEDVSLIVCSSGTTGLPKGVQLTQMNLLATLDSQIQPTVIPmEEVTLLTVIPWFHAFGcLTLITTACVGARLVY 263
Cdd:PRK06188 161 lvaAALPPDIAGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWP-ADPRFLMCTPLSHAGG-AFFLPTLLRGGTVIV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 264 LPKFEEKLFLSAIEKYRVMMAFMVPPLMVFLAKHPIVDKYDLSSLMVLLCGAAPLSRETEDQIKERIGvPFIRQGYGLSE 343
Cdd:PRK06188 239 LAKFDPAEVLRAIEEQRITATFLVPTMIYALLDHPDLRTRDLSSLETVYYGASPMSPVRLAEAIERFG-PIFAQYYGQTE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 344 --STLSVLVQNDEFCKP----GSVGVLKVGIYAKVIDPDtGKLLGANERGELCFKGDGIMKGYIGDTKSTQTAIKDGWLH 417
Cdd:PRK06188 318 apMVITYLRKRDHDPDDpkrlTSCGRPTPGLRVALLDED-GREVAQGEVGEICVRGPLVMDGYWNRPEETAEAFRDGWLH 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 418 TGDIGYYDDDFEFFIVDRIKELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGELPLAFVVKQANVQLTENEVI 497
Cdd:PRK06188 397 TGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRPGAAVDAAELQ 476
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 21355181 498 QFVNDNASPA---KRlrggVIFVDEIPKNPSGKILRRILRE 535
Cdd:PRK06188 477 AHVKERKGSVhapKQ----VDFVDSLPLTALGKPDKKALRA 513
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
38-535 |
2.32e-66 |
|
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: 223.66 E-value: 2.32e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 38 FGDRTVLVDAVNG--VEYSASFMHKSIVRLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDRE 115
Cdd:cd12119 9 HGDREIVSRTHEGevHRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 116 VDHAINLSKPKIIFASKITIDRVAKVASKNKFVKGIIALS----GTSKKFKNIYDLKELMEDEKFKTQ-PDFtspaankD 190
Cdd:cd12119 89 IAYIINHAEDRVVFVDRDFLPLLEAIAPRLPTVEHVVVMTddaaMPEPAGVGVLAYEELLAAESPEYDwPDF-------D 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 191 EDVSLIVC-SSGTTGLPKGVQLTQ-MNLLATLdSQIQPTVIPMEEV-TLLTVIPWFHAFGCLTLITTACVGARLVYL-PK 266
Cdd:cd12119 162 ENTAAAICyTSGTTGNPKGVVYSHrSLVLHAM-AALLTDGLGLSESdVVLPVVPMFHVNAWGLPYAAAMVGAKLVLPgPY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 267 FEEKLFLSAIEKYRVMMAFMVPPLMVFLAKHPIVDKYDLSSLMVLLCG--AAP--LSRETEDqikerIGVPFIrQGYGLS 342
Cdd:cd12119 241 LDPASLAELIEREGVTFAAGVPTVWQGLLDHLEANGRDLSSLRRVVIGgsAVPrsLIEAFEE-----RGVRVI-HAWGMT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 343 E-STLSVLVQ----------NDEFCKPGSVGVLKVGIYAKVIDPDTGKL-LGANERGELCFKGDGIMKGYIGDTKSTQTA 410
Cdd:cd12119 315 EtSPLGTVARppsehsnlseDEQLALRAKQGRPVPGVELRIVDDDGRELpWDGKAVGELQVRGPWVTKSYYKNDEESEAL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 411 IKDGWLHTGDIGYYDDDFEFFIVDRIKELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGELPLAFVVKQANVQ 490
Cdd:cd12119 395 TEDGWLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLKEGAT 474
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 21355181 491 LTENEVIQFVNDNAspAK-RLRGGVIFVDEIPKNPSGKILRRILRE 535
Cdd:cd12119 475 VTAEELLEFLADKV--AKwWLPDDVVFVDEIPKTSTGKIDKKALRE 518
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
17-475 |
2.60e-66 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 225.75 E-value: 2.60e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 17 TERQAQDSRSLGQYILDKYKSFGDRTVLVDAVNG--VEYSASFMHKSIVRLAYILQKLGVKQNDVVGLSSENSVNFALAM 94
Cdd:COG1022 3 EFSDVPPADTLPDLLRRRAARFPDRVALREKEDGiwQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIAD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 95 FAGLAVGATVAPLNVTYSDREVDHAINLSKPKIIFASKITI-DRVAKVASKNKFVKGIIALSG-TSKKFKNIYDLKELME 172
Cdd:COG1022 83 LAILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVEDQEQlDKLLEVRDELPSLRHIVVLDPrGLRDDPRLLSLDELLA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 173 D-EKFKTQPDFTS-PAANKDEDVSLIVCSSGTTGLPKGVQLTQMNLLATLDSQIQPTVIPMEEVTLLtVIPWFHAFG-CL 249
Cdd:COG1022 163 LgREVADPAELEArRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLS-FLPLAHVFErTV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 250 TLITTACvGARLVYLP---------------------------------KFEE------KLFLSAIE---KYRVMMAFMV 287
Cdd:COG1022 242 SYYALAA-GATVAFAEspdtlaedlrevkptfmlavprvwekvyagiqaKAEEagglkrKLFRWALAvgrRYARARLAGK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 288 PPLMVFLAKHPIVDKYDLSSLM--------VLLCGAAPLSRETEdqikeR----IGVPfIRQGYGLSESTLSVLVQNDEF 355
Cdd:COG1022 321 SPSLLLRLKHALADKLVFSKLRealggrlrFAVSGGAALGPELA-----RffraLGIP-VLEGYGLTETSPVITVNRPGD 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 356 CKPGSVGVLKVGIYAKvIDPDtgkllganerGELCFKGDGIMKGYIGDTKSTQTAI-KDGWLHTGDIGYYDDDFEFFIVD 434
Cdd:COG1022 395 NRIGTVGPPLPGVEVK-IAED----------GEILVRGPNVMKGYYKNPEATAEAFdADGWLHTGDIGELDEDGFLRITG 463
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 21355181 435 RIKELI-----KYkgyqVPPAEIEALLLTNDKIKDAAVIGK----------PDEEA 475
Cdd:COG1022 464 RKKDLIvtsggKN----VAPQPIENALKASPLIEQAVVVGDgrpflaalivPDFEA 515
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
58-535 |
3.75e-64 |
|
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: 214.90 E-value: 3.75e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 58 MHKSIVRLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNvtysdrevdhainlskpkiifaSKITIdr 137
Cdd:cd05912 7 LFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLN----------------------TRLTP-- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 138 vakvasknkfvkgiialsgtskkfkniYDLKELMEDEKFKTqpdftspaankdEDVSLIVCSSGTTGLPKGVQLTQMNLL 217
Cdd:cd05912 63 ---------------------------NELAFQLKDSDVKL------------DDIATIMYTSGTTGKPKGVQQTFGNHW 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 218 ATLDSQiQPTVIPMEEVTLLTVIPWFHAFGCLTLITTACVGARLVYLPKFEEKLFLSAIEKYRVMMAFMVPPLMVFLAKh 297
Cdd:cd05912 104 WSAIGS-ALNLGLTEDDNWLCALPLFHISGLSILMRSVIYGMTVYLVDKFDAEQVLHLINSGKVTIISVVPTMLQRLLE- 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 298 pIVDKYDLSSLMVLLCGAAPLSRETEDQIKERiGVPFIrQGYGLSESTLSVLVQNDEFC--KPGSVGVLKVGIYAKVIDP 375
Cdd:cd05912 182 -ILGEGYPNNLRCILLGGGPAPKPLLEQCKEK-GIPVY-QSYGMTETCSQIVTLSPEDAlnKIGSAGKPLFPVELKIEDD 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 376 DTGKllgaNERGELCFKGDGIMKGYIGDTKSTQTAIKDGWLHTGDIGYYDDDFEFFIVDRIKELIKYKGYQVPPAEIEAL 455
Cdd:cd05912 259 GQPP----YEVGEILLKGPNVTKGYLNRPDATEESFENGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEV 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 456 LLTNDKIKDAAVIGKPDEEAGELPLAFVVKQANVqlTENEVIQFVNDNASPAKRLRgGVIFVDEIPKNPSGKILRRILRE 535
Cdd:cd05912 335 LLSHPAIKEAGVVGIPDDKWGQVPVAFVVSERPI--SEEELIAYCSEKLAKYKVPK-KIYFVDELPRTASGKLLRHELKQ 411
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
68-535 |
6.62e-64 |
|
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: 215.23 E-value: 6.62e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 68 ILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREVDHAINLSKPKIIfaskitIDRvakvasknkf 147
Cdd:cd05941 28 LLALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITDSEPSLV------LDP---------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 148 vkgiialsgtskkfkniydlkelmedekfktqpdftspaankdedvSLIVCSSGTTGLPKGVQLTQMNLLATLDSQIQP- 226
Cdd:cd05941 92 ----------------------------------------------ALILYTSGTTGRPKGVVLTHANLAANVRALVDAw 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 227 --TvipmEEVTLLTVIPWFHAFGC-LTLITTACVGARLVYLPKFEEKLFLSAIEKYRVMMAFMVPPLMVFLAKHP----- 298
Cdd:cd05941 126 rwT----EDDVLLHVLPLHHVHGLvNALLCPLFAGASVEFLPKFDPKEVAISRLMPSITVFMGVPTIYTRLLQYYeahft 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 299 ---IVDKYDLSSLMVLLCGAAPLSRETEDQIKERIGVPFIRQgYGLSES--TLSVLVQNDEfcKPGSVGVLKVGIYAKVI 373
Cdd:cd05941 202 dpqFARAAAAERLRLMVSGSAALPVPTLEEWEAITGHTLLER-YGMTEIgmALSNPLDGER--RPGTVGMPLPGVQARIV 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 374 DPDTGKLLGANERGELCFKGDGIMKGYIGDTKSTQTAIK-DGWLHTGDIGYYDDDFEFFIVDRIK-ELIKYKGYQVPPAE 451
Cdd:cd05941 279 DEETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTdDGWFKTGDLGVVDEDGYYWILGRSSvDIIKSGGYKVSALE 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 452 IEALLLTNDKIKDAAVIGKPDEEAGELPLAFVVKQANV-QLTENEVIQFVNDNASPAKRLRgGVIFVDEIPKNPSGKILR 530
Cdd:cd05941 359 IERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGAaALSLEELKEWAKQRLAPYKRPR-RLILVDELPRNAMGKVNK 437
|
....*
gi 21355181 531 RILRE 535
Cdd:cd05941 438 KELRK 442
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
27-536 |
1.58e-63 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 217.33 E-value: 1.58e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 27 LGQYILDKYKS----FGDRTVLVDAVNGVEYSASFMHKSIVRLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGA 102
Cdd:PRK12583 16 LTQTIGDAFDAtvarFPDREALVVRHQALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 103 TVAPLNVTYSDREVDHAINLSKPKIIF---ASKiTIDRVAKVAS----------------KNKFVKGIIALSGTSKK-FK 162
Cdd:PRK12583 96 ILVNINPAYRASELEYALGQSGVRWVIcadAFK-TSDYHAMLQEllpglaegqpgalaceRLPELRGVVSLAPAPPPgFL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 163 NIYDLkeLMEDEKFKTQPDFTSPAANKDEDVSLIVCSSGTTGLPKGVQLTQMNLLAtlDSQIQPTVIPMEEVTLLTV-IP 241
Cdd:PRK12583 175 AWHEL--QARGETVSREALAERQASLDRDDPINIQYTSGTTGFPKGATLSHHNILN--NGYFVAESLGLTEHDRLCVpVP 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 242 WFHAFGCLtLITTAC--VGARLVYlPK--FEEKLFLSAIEKYRVMMAFMVPPLMVFLAKHPIVDKYDLSSLMVLLCGAAP 317
Cdd:PRK12583 251 LYHCFGMV-LANLGCmtVGACLVY-PNeaFDPLATLQAVEEERCTALYGVPTMFIAELDHPQRGNFDLSSLRTGIMAGAP 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 318 LSRETEDQIKERIGVPFIRQGYGLSES---TLSVLVQNDEFCKPGSVGVLKVGIYAKVIDPDtGKLLGANERGELCFKGD 394
Cdd:PRK12583 329 CPIEVMRRVMDEMHMAEVQIAYGMTETspvSLQTTAADDLERRVETVGRTQPHLEVKVVDPD-GATVPRGEIGELCTRGY 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 395 GIMKGYIGDTKSTQTAI-KDGWLHTGDIGYYDDDFEFFIVDRIKELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDE 473
Cdd:PRK12583 408 SVMKGYWNNPEATAESIdEDGWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDE 487
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21355181 474 EAGELPLAFVVKQANVQLTENEVIQFVNDNASPAKRLRgGVIFVDEIPKNPSGKILRRILREM 536
Cdd:PRK12583 488 KYGEEIVAWVRLHPGHAASEEELREFCKARIAHFKVPR-YFRFVDEFPMTVTGKVQKFRMREI 549
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
24-534 |
6.66e-63 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 214.55 E-value: 6.66e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 24 SRSLGQYILDKYKSFGDRTVLV-DAVNGV--EYSASFMHKSIVRLAYILQKLGVKQNDVVGLSSENSVNFALAMFaGLA- 99
Cdd:PRK08008 6 GQHLRQMWDDLADVYGHKTALIfESSGGVvrRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWF-GLAk 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 100 VGATVAPLNVTYSDREVDHAINLSKPKIIFASKI---TIDRVAKVASKNkfVKGIIALSGTSKKFKNIYDLKELMEDEKf 176
Cdd:PRK08008 85 IGAIMVPINARLLREESAWILQNSQASLLVTSAQfypMYRQIQQEDATP--LRHICLTRVALPADDGVSSFTQLKAQQP- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 177 kTQPDFTSPAANkdEDVSLIVCSSGTTGLPKGVQLTQMNLL-ATLDSQIQPTVipMEEVTLLTVIPWFHA-FGCLTLITT 254
Cdd:PRK08008 162 -ATLCYAPPLST--DDTAEILFTSGTTSRPKGVVITHYNLRfAGYYSAWQCAL--RDDDVYLTVMPAFHIdCQCTAAMAA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 255 ACVGARLVYLPKFEEKLFLSAIEKYRVM----MAFMVPPLMVFLAKhPIVDKYDLSSLMVLLcgaaPLSRETEDQIKERI 330
Cdd:PRK08008 237 FSAGATFVLLEKYSARAFWGQVCKYRATitecIPMMIRTLMVQPPS-ANDRQHCLREVMFYL----NLSDQEKDAFEERF 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 331 GVPFIrQGYGLSESTLSVLvqNDefcKPG------SVGVLKVGIYAKVIDpDTGKLLGANERGELCFKG---DGIMKGYI 401
Cdd:PRK08008 312 GVRLL-TSYGMTETIVGII--GD---RPGdkrrwpSIGRPGFCYEAEIRD-DHNRPLPAGEIGEICIKGvpgKTIFKEYY 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 402 GDTKSTQTAIK-DGWLHTGDIGYYDDDFEFFIVDRIKELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGELPL 480
Cdd:PRK08008 385 LDPKATAKVLEaDGWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIK 464
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 21355181 481 AFVVKQANVQLTENEVIQFVNDNASPAKrLRGGVIFVDEIPKNPSGKILRRILR 534
Cdd:PRK08008 465 AFVVLNEGETLSEEEFFAFCEQNMAKFK-VPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
65-536 |
1.91e-62 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 214.02 E-value: 1.91e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 65 LAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREVDHAINLSKPKIIFASKITIDRVAKVASK 144
Cdd:PRK07788 87 LARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQLAEVAAREGVKALVYDDEFTDLLSALPPD 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 145 NKFVKGIIAL-SGTSKKFKNIYDLKELMEDEKFKTQPDFTSPAankdedvSLIVCSSGTTGLPKGVQLTQMNLLATLDSQ 223
Cdd:PRK07788 167 LGRLRAWGGNpDDDEPSGSTDETLDDLIAGSSTAPLPKPPKPG-------GIVILTSGTTGTPKGAPRPEPSPLAPLAGL 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 224 IQPTVIPMEEVTLLTViPWFHA--FGCLTLITTacVGARLVYLPKFEEKLFLSAIEKYRVMMAFMVPplmVFLakHPIVD 301
Cdd:PRK07788 240 LSRVPFRAGETTLLPA-PMFHAtgWAHLTLAMA--LGSTVVLRRRFDPEATLEDIAKHKATALVVVP---VML--SRILD 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 302 -------KYDLSSLMVLLCGAAPLSRETEDQIKERIGvPFIRQGYGLSESTLSVLVQNDEFCK-PGSVGVLKVGIYAKVI 373
Cdd:PRK07788 312 lgpevlaKYDTSSLKIIFVSGSALSPELATRALEAFG-PVLYNLYGSTEVAFATIATPEDLAEaPGTVGRPPKGVTVKIL 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 374 DPDtGKLLGANERGELcFKGDGI-MKGYIgDTKSTQtaIKDGWLHTGDIGYYDDDFEFFIVDRIKELIKYKGYQVPPAEI 452
Cdd:PRK07788 391 DEN-GNEVPRGVVGRI-FVGNGFpFEGYT-DGRDKQ--IIDGLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEV 465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 453 EALLLTNDKIKDAAVIGKPDEEAGELPLAFVVKQANVQLTENEVIQFVNDNASPAKRLRgGVIFVDEIPKNPSGKILRRI 532
Cdd:PRK07788 466 EDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKAPGAALDEDAIKDYVRDNLARYKVPR-DVVFLDELPRNPTGKVLKRE 544
|
....
gi 21355181 533 LREM 536
Cdd:PRK07788 545 LREM 548
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
38-540 |
2.33e-62 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 214.48 E-value: 2.33e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 38 FGDRTVLvdAVNGVEYSASFMHKSIVRLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREVD 117
Cdd:PRK05605 45 FGDRPAL--DFFGATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVEHNPLYTAHELE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 118 HAINLSKPKIIFASKITIDRVAKVASKNKfVKGIIALSGTS--------------KKFK-----------NIYDLKELME 172
Cdd:PRK05605 123 HPFEDHGARVAIVWDKVAPTVERLRRTTP-LETIVSVNMIAampllqrlalrlpiPALRkaraaltgpapGTVPWETLVD 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 173 DEKFKTQPDFTSPAANKDeDVSLIVCSSGTTGLPKGVQLTQMNLLATLdsqIQ-----PTVIPMEEvTLLTVIPWFHAFG 247
Cdd:PRK05605 202 AAIGGDGSDVSHPRPTPD-DVALILYTSGTTGKPKGAQLTHRNLFANA---AQgkawvPGLGDGPE-RVLAALPMFHAYG 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 248 cLTLITTACV--GARLVYLPKFEEKLFLSAIEKYRVMMAFMVPPLMVFLAKHPIVDKYDLSSLMVLLCGAAPLSRETEDQ 325
Cdd:PRK05605 277 -LTLCLTLAVsiGGELVLLPAPDIDLILDAMKKHPPTWLPGVPPLYEKIAEAAEERGVDLSGVRNAFSGAMALPVSTVEL 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 326 IKERIGvPFIRQGYGLSEsTLSVLVQN--DEFCKPGSVGVLKVGIYAKVIDPDT-GKLLGANERGELCFKGDGIMKGYIG 402
Cdd:PRK05605 356 WEKLTG-GLLVEGYGLTE-TSPIIVGNpmSDDRRPGYVGVPFPDTEVRIVDPEDpDETMPDGEEGELLVRGPQVFKGYWN 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 403 DTKSTQTAIKDGWLHTGDIGYYDDDFEFFIVDRIKELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGELPLAF 482
Cdd:PRK05605 434 RPEETAKSFLDGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAA 513
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 21355181 483 VVKQANVQLTENEVIQFVNDNASPAKRLRgGVIFVDEIPKNPSGKILRRILREMLKKQ 540
Cdd:PRK05605 514 VVLEPGAALDPEGLRAYCREHLTRYKVPR-RFYHVDELPRDQLGKVRRREVREELLEK 570
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
58-538 |
2.41e-62 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 215.59 E-value: 2.41e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 58 MHKSIVRLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGaTVAPLNVTYSDREVDHAINLSKPKIIFA----SKI 133
Cdd:PRK07529 64 LLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGEAAG-IANPINPLLEPEQIAELLRAAGAKVLVTlgpfPGT 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 134 TI-DRVAKVASKNKFVKGIIALSG-----TSKKFK----------NIYDLKELMedekfKTQPD---FTSPAANKDeDVS 194
Cdd:PRK07529 143 DIwQKVAEVLAALPELRTVVEVDLarylpGPKRLAvplirrkahaRILDFDAEL-----ARQPGdrlFSGRPIGPD-DVA 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 195 LIVCSSGTTGLPKGVQLTQMNL-----LATLDSQIQPtvipmeEVTLLTVIPWFHAFGCL-TLITTACVGARLVYLPK-- 266
Cdd:PRK07529 217 AYFHTGGTTGMPKLAQHTHGNEvanawLGALLLGLGP------GDTVFCGLPLFHVNALLvTGLAPLARGAHVVLATPqg 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 267 ------FEEklFLSAIEKYRVMMAFMVPPLMVFLAKHPiVDKYDLSSLMVLLCGAAPLSRETEDQIKERIGVPfIRQGYG 340
Cdd:PRK07529 291 yrgpgvIAN--FWKIVERYRINFLSGVPTVYAALLQVP-VDGHDISSLRYALCGAAPLPVEVFRRFEAATGVR-IVEGYG 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 341 LSESTLSVLVqN--DEFCKPGSVGVLKVGIYAKVI--DPDTGKL--LGANERGELCFKGDGIMKGYIGDTKSTQTAIKDG 414
Cdd:PRK07529 367 LTEATCVSSV-NppDGERRIGSVGLRLPYQRVRVVilDDAGRYLrdCAVDEVGVLCIAGPNVFSGYLEAAHNKGLWLEDG 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 415 WLHTGDIGYYDDDFEFFIVDRIKELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGELPLAFVVKQANVQLTEN 494
Cdd:PRK07529 446 WLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGELPVAYVQLKPGASATEA 525
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 21355181 495 EVIQFVNDN-----ASPaKRlrggVIFVDEIPKNPSGKIL---------RRILREMLK 538
Cdd:PRK07529 526 ELLAFARDHiaeraAVP-KH----VRILDALPKTAVGKIFkpalrrdaiRRVLRAALR 578
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
191-534 |
6.03e-61 |
|
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: 204.43 E-value: 6.03e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 191 EDVSLIVCSSGTTGLPKGVQLTQMNLLATlDSQIQPTVIPMEEVTLLTVIPWFHAFGCLtLITTACV--GARLVYL-PKF 267
Cdd:cd05917 2 DDVINIQFTSGTTGSPKGATLTHHNIVNN-GYFIGERLGLTEQDRLCIPVPLFHCFGSV-LGVLACLthGATMVFPsPSF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 268 EEKLFLSAIEKYRVMMAFMVPPLMVFLAKHPIVDKYDLSSLMVLLCGAAPLSRETEDQIKERIGVPFIRQGYGLSE---- 343
Cdd:cd05917 80 DPLAVLEAIEKEKCTALHGVPTMFIAELEHPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEVMNMKDVTIAYGMTEtspv 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 344 STLSVLvqNDEF-CKPGSVGVLKVGIYAKVIDPDTGKLLGANERGELCFKGDGIMKGYIGDTKSTQTAI-KDGWLHTGDI 421
Cdd:cd05917 160 STQTRT--DDSIeKRVNTVGRIMPHTEAKIVDPEGGIVPPVGVPGELCIRGYSVMKGYWNDPEKTAEAIdGDGWLHTGDL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 422 GYYDDDFEFFIVDRIKELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGELPLAFVVKQANVQLTENEVIQFVN 501
Cdd:cd05917 238 AVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLKEGAELTEEDIKAYCK 317
|
330 340 350
....*....|....*....|....*....|...
gi 21355181 502 DNASPAKRLRgGVIFVDEIPKNPSGKILRRILR 534
Cdd:cd05917 318 GKIAHYKVPR-YVFFVDEFPLTVSGKIQKFKLR 349
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
25-540 |
3.92e-60 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 208.13 E-value: 3.92e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 25 RSLGQYILDKYKSFGDRTVLVDAVNGVEYSASFMHKSIVRLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATV 104
Cdd:PRK08315 16 QTIGQLLDRTAARYPDREALVYRDQGLRWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAIL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 105 APLNVTYSDREVDHAINLSKPKIIFASK------------------ITIDRVAKVASKNKFVKGIIALSGtsKKFKNIYD 166
Cdd:PRK08315 96 VTINPAYRLSELEYALNQSGCKALIAADgfkdsdyvamlyelapelATCEPGQLQSARLPELRRVIFLGD--EKHPGMLN 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 167 LKELMEDEKFKTQPDFTSPAANKD-EDVSLIVCSSGTTGLPKGVQLTQMNLLA-----------TLDSQIqptVIPmeev 234
Cdd:PRK08315 174 FDELLALGRAVDDAELAARQATLDpDDPINIQYTSGTTGFPKGATLTHRNILNngyfigeamklTEEDRL---CIP---- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 235 tlltvIPWFHAFGCLtLITTACV--GARLVY-LPKFEEKLFLSAIEKYRVMMAFMVPplMVFLAK--HPIVDKYDLSSLM 309
Cdd:PRK08315 247 -----VPLYHCFGMV-LGNLACVthGATMVYpGEGFDPLATLAAVEEERCTALYGVP--TMFIAEldHPDFARFDLSSLR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 310 VLLCGAAPLSRETEDQIKERIGVPFIRQGYGLSEsTLSVLVQ---NDEFCKP-GSVGVLKVGIYAKVIDPDTGKLLGANE 385
Cdd:PRK08315 319 TGIMAGSPCPIEVMKRVIDKMHMSEVTIAYGMTE-TSPVSTQtrtDDPLEKRvTTVGRALPHLEVKIVDPETGETVPRGE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 386 RGELCFKGDGIMKGYIGDTKSTQTAI-KDGWLHTGDIGYYDDDFEFFIVDRIKELIKYKGYQVPPAEIEALLLTNDKIKD 464
Cdd:PRK08315 398 QGELCTRGYSVMKGYWNDPEKTAEAIdADGWMHTGDLAVMDEEGYVNIVGRIKDMIIRGGENIYPREIEEFLYTHPKIQD 477
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21355181 465 AAVIGKPDEEAGELPLAFVVKQANVQLTENEVIQFVNDNASPAKRLRgGVIFVDEIPKNPSGKILRRILREMLKKQ 540
Cdd:PRK08315 478 VQVVGVPDEKYGEEVCAWIILRPGATLTEEDVRDFCRGKIAHYKIPR-YIRFVDEFPMTVTGKIQKFKMREMMIEE 552
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
40-540 |
7.40e-60 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 205.58 E-value: 7.40e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 40 DRTVLVDAvngvEYSASFM--HKSIVRLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREVD 117
Cdd:PRK03640 17 DRTAIEFE----EKKVTFMelHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 118 HAINLSKPKIIFASKITIDRVAKVASKnkfvkgiialsgtskkfkniyDLKELMEDEKFKTQPDFTSPaankDEDVSLIV 197
Cdd:PRK03640 93 WQLDDAEVKCLITDDDFEAKLIPGISV---------------------KFAELMNGPKEEAEIQEEFD----LDEVATIM 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 198 CSSGTTGLPKGVQLTQMNLLATLDSqiqpTVIPM---EEVTLLTVIPWFHAFGCLTLITTACVGARLVYLPKFEEKLFLS 274
Cdd:PRK03640 148 YTSGTTGKPKGVIQTYGNHWWSAVG----SALNLgltEDDCWLAAVPIFHISGLSILMRSVIYGMRVVLVEKFDAEKINK 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 275 AIEKYRVMMAFMVPpLMV--FLAKHPiVDKYDlSSLMVLLCGAAPLSRETEDQIKERiGVPFIrQGYGLSE--STLSVLV 350
Cdd:PRK03640 224 LLQTGGVTIISVVS-TMLqrLLERLG-EGTYP-SSFRCMLLGGGPAPKPLLEQCKEK-GIPVY-QSYGMTEtaSQIVTLS 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 351 QNDEFCKPGSVGvlKVGIYAKVIDPDTGKLLGANERGELCFKGDGIMKGYIGDTKSTQTAIKDGWLHTGDIGYYDDDFEF 430
Cdd:PRK03640 299 PEDALTKLGSAG--KPLFPCELKIEKDGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQDGWFKTGDIGYLDEEGFL 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 431 FIVDRIKELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGELPLAFVVKqaNVQLTENEVIQFVNDN-AS---P 506
Cdd:PRK03640 377 YVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVK--SGEVTEEELRHFCEEKlAKykvP 454
|
490 500 510
....*....|....*....|....*....|....
gi 21355181 507 AKrlrggVIFVDEIPKNPSGKILRRILREMLKKQ 540
Cdd:PRK03640 455 KR-----FYFVEELPRNASGKLLRHELKQLVEEM 483
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
62-528 |
8.04e-60 |
|
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: 205.64 E-value: 8.04e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 62 IVRLAYILQKlGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREVDHAINLSKPKIIFASKITIDrvakv 141
Cdd:cd05909 17 AIALARKLAK-MTKEGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVLTSKQFIE----- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 142 asKNKFVKGIIALSGtskkFKNIY--DLK-ELMEDEKFKT--QPDFTSP--------AANKDEDVSLIVCSSGTTGLPKG 208
Cdd:cd05909 91 --KLKLHHLFDVEYD----ARIVYleDLRaKISKADKCKAflAGKFPPKwllrifgvAPVQPDDPAVILFTSGSEGLPKG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 209 VQLTQMNLLATLDsQIQPTVIPMEEVTLLTVIPWFHAFG-CLTLITTACVGARLVYLPK-FEEKLFLSAIEKYRVMMAFM 286
Cdd:cd05909 165 VVLSHKNLLANVE-QITAIFDPNPEDVVFGALPFFHSFGlTGCLWLPLLSGIKVVFHPNpLDYKKIPELIYDKKATILLG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 287 VPPLMVFLAKHpiVDKYDLSSLMVLLCGAAPLSRETEDQIKERIGVPfIRQGYGLSEST--LSVLVQNDEFcKPGSVGVL 364
Cdd:cd05909 244 TPTFLRGYARA--AHPEDFSSLRLVVAGAEKLKDTLRQEFQEKFGIR-ILEGYGTTECSpvISVNTPQSPN-KEGTVGRP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 365 KVGIYAKVIDPDTGKLLGANERGELCFKGDGIMKGYIGDTKSTQTAIKDGWLHTGDIGYYDDDFEFFIVDRIKELIKYKG 444
Cdd:cd05909 320 LPGMEVKIVSVETHEEVPIGEGGLLLVRGPNVMLGYLNEPELTSFAFGDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 445 YQVPPAEIEALLLTNDKIK-DAAVIGKPDEEAGELPLAFVVKQAnvqLTENEVIQFVNDNASPAKRLRGGVIFVDEIPKN 523
Cdd:cd05909 400 EMVSLEAIEDILSEILPEDnEVAVVSVPDGRKGEKIVLLTTTTD---TDPSSLNDILKNAGISNLAKPSYIHQVEEIPLL 476
|
....*
gi 21355181 524 PSGKI 528
Cdd:cd05909 477 GTGKP 481
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
26-539 |
4.66e-59 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 204.98 E-value: 4.66e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 26 SLGQYILDKYKSFGDRTVLVDAvNGVEYSASFMHKSIVRLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVA 105
Cdd:PRK06087 24 SLADYWQQTARAMPDKIAVVDN-HGASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 106 PLNVTYSDREVDHAINLSKPKIIFA----SKIT-IDRVAKVASKNKFVKGIIALSGTSKKFKNIyDLKELMEDekfkTQP 180
Cdd:PRK06087 103 PLLPSWREAELVWVLNKCQAKMFFAptlfKQTRpVDLILPLQNQLPQLQQIVGVDKLAPATSSL-SLSQIIAD----YEP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 181 DFTSPAANKDeDVSLIVCSSGTTGLPKGVQLTQMNLLATLDSQIQPTVIPMEEVTLLTViPWFHAFGCL-TLITTACVGA 259
Cdd:PRK06087 178 LTTAITTHGD-ELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPA-PLGHATGFLhGVTAPFLIGA 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 260 RLVYLPKFEEKLFLSAIEKYRVMMAFMVPPLMVFLAKHPIVDKYDLSSLMVLLCGAAPLSRETEDQIKERiGVPFIrQGY 339
Cdd:PRK06087 256 RSVLLDIFTPDACLALLEQQRCTCMLGATPFIYDLLNLLEKQPADLSALRFFLCGGTTIPKKVARECQQR-GIKLL-SVY 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 340 GLSESTLSVLVQNDEfCKP---GSVGVLKVGIYAKVIDPDTgKLLGANERGELCFKGDGIMKGYIGDTKSTQTAI-KDGW 415
Cdd:PRK06087 334 GSTESSPHAVVNLDD-PLSrfmHTDGYAAAGVEIKVVDEAR-KTLPPGCEGEEASRGPNVFMGYLDEPELTARALdEEGW 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 416 LHTGDIGYYDDDFEFFIVDRIKELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGELPLAFVVKQANVQ-LTEN 494
Cdd:PRK06087 412 YYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVVLKAPHHsLTLE 491
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 21355181 495 EVIQFVNDNASPAKRLRGGVIFVDEIPKNPSGKILRRILREMLKK 539
Cdd:PRK06087 492 EVVAFFSRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRKDIMR 536
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
64-541 |
2.37e-58 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 203.73 E-value: 2.37e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 64 RLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREVDHAINLSKPKIIfaskITIDRVAKVAS 143
Cdd:PRK06178 70 RFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVL----LALDQLAPVVE 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 144 KNK--------FVKGIIA-------------LSGTSKKFKNIYDLKELMEDEKFKTQ---PDFTSPAAnkdedvslIVCS 199
Cdd:PRK06178 146 QVRaetslrhvIVTSLADvlpaeptlplpdsLRAPRLAAAGAIDLLPALRACTAPVPlppPALDALAA--------LNYT 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 200 SGTTGLPKGVQLTQMNLLATLDSQIQPTVIPMEEVTLLTVIPWFHAFG-CLTLITTACVGARLVYLPKFEEKLFLSAIEK 278
Cdd:PRK06178 218 GGTTGMPKGCEHTQRDMVYTAAAAYAVAVVGGEDSVFLSFLPEFWIAGeNFGLLFPLFSGATLVLLARWDAVAFMAAVER 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 279 YRVMMAFMVPPLMVFLAKHPIVDKYDLSSLMVLLCGA--APLSRETEDQIKERIGVPFIRQGYGLSES----TLSVLVQN 352
Cdd:PRK06178 298 YRVTRTVMLVDNAVELMDHPRFAEYDLSSLRQVRVVSfvKKLNPDYRQRWRALTGSVLAEAAWGMTEThtcdTFTAGFQD 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 353 DEF---CKPGSVGVLKVGIYAKVIDPDTGKLLGANERGELCFKGDGIMKGYIGDTKSTQTAIKDGWLHTGDIGYYDDDFE 429
Cdd:PRK06178 378 DDFdllSQPVFVGLPVPGTEFKICDFETGELLPLGAEGEIVVRTPSLLKGYWNKPEATAEALRDGWLHTGDIGKIDEQGF 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 430 FFIVDRIKELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGELPLAFVVKQANVQLTENEVIQFVNDNASPAK- 508
Cdd:PRK06178 458 LHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPGADLTAAALQAWCRENMAVYKv 537
|
490 500 510
....*....|....*....|....*....|....
gi 21355181 509 -RLRggviFVDEIPKNPSGKILRRILREMLKKQK 541
Cdd:PRK06178 538 pEIR----IVDALPMTATGKVRKQDLQALAEELK 567
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
190-534 |
2.76e-58 |
|
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: 199.87 E-value: 2.76e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 190 DEDVSLIVCSSGTTGLPKGVQLTQMNLLATLDSQIQPTVIPMEEVTLLTVIP------WFHAFGCLTLITTacvgaRLVY 263
Cdd:cd05972 80 AEDPALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGLRPDDIHWNIADPgwakgaWSSFFGPWLLGAT-----VFVY 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 264 -LPKFEEKLFLSAIEKYRVMmAFMVPPLMVFLAKHPIVDKYDLSSLMVLLCGAAPLSRETEDQIKERIGVPfIRQGYGLS 342
Cdd:cd05972 155 eGPRFDAERILELLERYGVT-SFCGPPTAYRMLIKQDLSSYKFSHLRLVVSAGEPLNPEVIEWWRAATGLP-IRDGYGQT 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 343 ESTLSVLVQNDEFCKPGSVGVLKVGIYAKVIDpDTGKLLGANERGELCFKGD--GIMKGYIGDTKSTQTAIKDGWLHTGD 420
Cdd:cd05972 233 ETGLTVGNFPDMPVKPGSMGRPTPGYDVAIID-DDGRELPPGEEGDIAIKLPppGLFLGYVGDPEKTEASIRGDYYLTGD 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 421 IGYYDDDFEFFIVDRIKELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGELPLAFVVKQANVQLTE---NEVI 497
Cdd:cd05972 312 RAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYEPSEelaEELQ 391
|
330 340 350
....*....|....*....|....*....|....*...
gi 21355181 498 QFVNDNASPAKRLRggVI-FVDEIPKNPSGKILRRILR 534
Cdd:cd05972 392 GHVKKVLAPYKYPR--EIeFVEELPKTISGKIRRVELR 427
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
62-535 |
1.01e-56 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 198.00 E-value: 1.01e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 62 IVRLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREVDHAINLSKPKIIFASKITIDRVAKV 141
Cdd:PRK12406 21 AARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAHADLLHGLASA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 142 ASKNKFV------------KGIIALSGTSKKFKniYDLKELMEDEKFKTQPDFTSPAankdedvSLIVcSSGTTGLPKGV 209
Cdd:PRK12406 101 LPAGVTVlsvptppeiaaaYRISPALLTPPAGA--IDWEGWLAQQEPYDGPPVPQPQ-------SMIY-TSGTTGHPKGV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 210 Q---------LTQMNLLATLDSQIQPTVipmeevTLLTViPWFH----AFGcltlITTACVGARLVYLPKFEEKLFLSAI 276
Cdd:PRK12406 171 RraaptpeqaAAAEQMRALIYGLKPGIR------ALLTG-PLYHsapnAYG----LRAGRLGGVLVLQPRFDPEELLQLI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 277 EKYRVMMAFMVPPLMVFLAKHP--IVDKYDLSSLMVLLCGAAPLSRETEDQIKERIGvPFIRQGYGLSESTLSVLVQNDE 354
Cdd:PRK12406 240 ERHRITHMHMVPTMFIRLLKLPeeVRAKYDVSSLRHVIHAAAPCPADVKRAMIEWWG-PVIYEYYGSTESGAVTFATSED 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 355 -FCKPGSVGVLKVGIYAKVIDPDtGKLLGANERGELCFKGDGIMK-GYIGDTKSTQTAIKDGWLHTGDIGYYDDDFEFFI 432
Cdd:PRK12406 319 aLSHPGTVGKAAPGAELRFVDED-GRPLPQGEIGEIYSRIAGNPDfTYHNKPEKRAEIDRGGFITSGDVGYLDADGYLFL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 433 VDRIKELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGELPLAFVVKQANVQLTENEViqfvndNASPAKRLRG 512
Cdd:PRK12406 398 CDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPGATLDEADI------RAQLKARLAG 471
|
490 500
....*....|....*....|....*...
gi 21355181 513 -----GVIFVDEIPKNPSGKILRRILRE 535
Cdd:PRK12406 472 ykvpkHIEIMAELPREDSGKIFKRRLRD 499
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
38-535 |
1.61e-56 |
|
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: 196.75 E-value: 1.61e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 38 FGDRTVLVDAvnGVEYSASFMHKSIVRLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREVD 117
Cdd:cd12118 17 YPDRTSIVYG--DRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 118 HAINLSKPKIIFAskitiDRVakvasknkfvkgiialsgtskkfkniYDLKELMEDEKfktqPDFTS-PAANKDEDVSLI 196
Cdd:cd12118 95 FILRHSEAKVLFV-----DRE--------------------------FEYEDLLAEGD----PDFEWiPPADEWDPIALN 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 197 VcSSGTTGLPKGVQLTQMN-LLATLDSQIQpTVIPMEEVTLLTViPWFHAFG-CLTLITTAcVGARLVYLPKFEEKLFLS 274
Cdd:cd12118 140 Y-TSGTTGRPKGVVYHHRGaYLNALANILE-WEMKQHPVYLWTL-PMFHCNGwCFPWTVAA-VGGTNVCLRKVDAKAIYD 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 275 AIEKYRVMMAFMVPPLMVFLAKHPIVDKYDLS-SLMVLLCGAAPLSRETEDqiKERIGvpF-IRQGYGLSESTLSVLV-- 350
Cdd:cd12118 216 LIEKHKVTHFCGAPTVLNMLANAPPSDARPLPhRVHVMTAGAPPPAAVLAK--MEELG--FdVTHVYGLTETYGPATVca 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 351 ---------QNDEFCKPGSVGVLKVGIYA-KVIDPDTGKLLGAN--ERGELCFKGDGIMKGYIGDTKSTQTAIKDGWLHT 418
Cdd:cd12118 292 wkpewdelpTEERARLKARQGVRYVGLEEvDVLDPETMKPVPRDgkTIGEIVFRGNIVMKGYLKNPEATAEAFRGGWFHS 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 419 GDIGYYDDDFEFFIVDRIKELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGELPLAFVVKQANVQLTENEVIQ 498
Cdd:cd12118 372 GDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVELKEGAKVTEEEIIA 451
|
490 500 510
....*....|....*....|....*....|....*..
gi 21355181 499 FVNDNaSPAKRLRGGVIFvDEIPKNPSGKILRRILRE 535
Cdd:cd12118 452 FCREH-LAGFMVPKTVVF-GELPKTSTGKIQKFVLRD 486
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
192-530 |
1.73e-56 |
|
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: 192.33 E-value: 1.73e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 192 DVSLIVCSSGTTGLPKGV---QLTQMNLLATLDSQIQPTvipmEEVTLLTVIPWFHAFG----CLTLITTacvGARLVYL 264
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVmcaHRQTLRAAAAWADCADLT----EDDRYLIINPFFHTFGykagIVACLLT---GATVVPV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 265 PKFEEKLFLSAIEKYRVMMAFMVPPLMVFLAKHPIVDKYDLSSLMVLLCGAAPLSRETEDQIKERIGVPFIRQGYGLSES 344
Cdd:cd17638 74 AVFDVDAILEAIERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFETVLTAYGLTEA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 345 TLSVLvqndefCKPGSVGVLKVGIYAKVIDpdtGKLLGANERGELCFKGDGIMKGYIGDTKSTQTAI-KDGWLHTGDIGY 423
Cdd:cd17638 154 GVATM------CRPGDDAETVATTCGRACP---GFEVRIADDGEVLVRGYNVMQGYLDDPEATAEAIdADGWLHTGDVGE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 424 YDDDFEFFIVDRIKELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGELPLAFVVKQANVQLTENEVIQFVNDN 503
Cdd:cd17638 225 LDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGVTLTEEDVIAWCRER 304
|
330 340
....*....|....*....|....*..
gi 21355181 504 ASPAKRLRgGVIFVDEIPKNPSGKILR 530
Cdd:cd17638 305 LANYKVPR-FVRFLDELPRNASGKVMK 330
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
27-540 |
4.11e-56 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 196.80 E-value: 4.11e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 27 LGQYILDKYKSFGDRTVLVDAVNGVEYSAsfMHKSIVRLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAP 106
Cdd:PRK07470 9 LAHFLRQAARRFPDRIALVWGDRSWTWRE--IDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 107 LNVTYSDREVDHAINLSKPKIIFASKITIDRVAKVASKNKFVKGIIALSGTSkkFKNIYD--LKELMEDEkfktqpdfTS 184
Cdd:PRK07470 87 TNFRQTPDEVAYLAEASGARAMICHADFPEHAAAVRAASPDLTHVVAIGGAR--AGLDYEalVARHLGAR--------VA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 185 PAANKDEDVSLIVCSSGTTGLPKGVQLT--QM-----NLLATLdsqiqptvIP--MEEVTLLTVIPWFHAFGCLTLITTA 255
Cdd:PRK07470 157 NAAVDHDDPCWFFFTSGTTGRPKAAVLThgQMafvitNHLADL--------MPgtTEQDASLVVAPLSHGAGIHQLCQVA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 256 cVGARLVYLP--KFEEKLFLSAIEKYRVMMAFMVPPLMVFLAKHPIVDKYDLSSLMVLLCGAAPLSRETEDQIKERIGvP 333
Cdd:PRK07470 229 -RGAATVLLPseRFDPAEVWALVERHRVTNLFTVPTILKMLVEHPAVDRYDHSSLRYVIYAGAPMYRADQKRALAKLG-K 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 334 FIRQGYGLSEST--LSVL------VQNDEFCKPGSVGVLKVGIYAKVIDpDTGKLLGANERGELCFKGDGIMKGYIGDTK 405
Cdd:PRK07470 307 VLVQYFGLGEVTgnITVLppalhdAEDGPDARIGTCGFERTGMEVQIQD-DEGRELPPGETGEICVIGPAVFAGYYNNPE 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 406 STQTAIKDGWLHTGDIGYYDDDFEFFIVDRIKELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGELPLAFVVK 485
Cdd:PRK07470 386 ANAKAFRDGWFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVA 465
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 21355181 486 QANVQLTENEVIQFVnDNASPAKRLRGGVIFVDEIPKNPSGKILRRILREMLKKQ 540
Cdd:PRK07470 466 RDGAPVDEAELLAWL-DGKVARYKLPKRFFFWDALPKSGYGKITKKMVREELEER 519
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
66-543 |
5.65e-56 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 197.20 E-value: 5.65e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 66 AYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREVDHAINLSKPKII-----FASkiTIDRVAK 140
Cdd:PRK08974 63 AYLQNGLGLKKGDRVALMMPNLLQYPIALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAKAIvivsnFAH--TLEKVVF 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 141 vaskNKFVKGII------ALS---GTSKKFKNIYdLKELMEdeKFKTqPDFTS---------------PAANKDeDVSLI 196
Cdd:PRK08974 141 ----KTPVKHVIltrmgdQLStakGTLVNFVVKY-IKRLVP--KYHL-PDAISfrsalhkgrrmqyvkPELVPE-DLAFL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 197 VCSSGTTGLPKGVQLTQMNLLATL---DSQIQPTVIPMEEVtLLTVIPWFHAFG----CLTLITtacVGAR--LVYLPKf 267
Cdd:PRK08974 212 QYTGGTTGVAKGAMLTHRNMLANLeqaKAAYGPLLHPGKEL-VVTALPLYHIFAltvnCLLFIE---LGGQnlLITNPR- 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 268 EEKLFLSAIEKYRVMMAFMVPPLMVFLAKHPIVDKYDLSSLMVLLCGAAPLSRETEDQIKERIGVpFIRQGYGLSEStlS 347
Cdd:PRK08974 287 DIPGFVKELKKYPFTAITGVNTLFNALLNNEEFQELDFSSLKLSVGGGMAVQQAVAERWVKLTGQ-YLLEGYGLTEC--S 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 348 VLVQndefCKP-------GSVGVLKVGIYAKVIDpDTGKLLGANERGELCFKGDGIMKGYIGDTKSTQTAIKDGWLHTGD 420
Cdd:PRK08974 364 PLVS----VNPydldyysGSIGLPVPSTEIKLVD-DDGNEVPPGEPGELWVKGPQVMLGYWQRPEATDEVIKDGWLATGD 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 421 IGYYDDDFEFFIVDRIKELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGELPLAFVVKQANvQLTENEVIQFV 500
Cdd:PRK08974 439 IAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAVKIFVVKKDP-SLTEEELITHC 517
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 21355181 501 NDNASPAK--RLrggVIFVDEIPKNPSGKILRRILREMLKKQKSK 543
Cdd:PRK08974 518 RRHLTGYKvpKL---VEFRDELPKSNVGKILRRELRDEARAKVDN 559
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
40-537 |
6.16e-56 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 195.49 E-value: 6.16e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 40 DRTVLVdaVNGVEYSASFMHKSIVRLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREVDHA 119
Cdd:PRK06145 17 DRAALV--YRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 120 INLSKPKIIFASKITIDRVAKVASKnkFVKGIIALSGTSKKfkniydlkelmedekfkTQPDFTSP--AANKDEDVSLIV 197
Cdd:PRK06145 95 LGDAGAKLLLVDEEFDAIVALETPK--IVIDAAAQADSRRL-----------------AQGGLEIPpqAAVAPTDLVRLM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 198 CSSGTTGLPKGVQLTQMNLLATLDSQIQPTVIPMEEvTLLTVIPWFHAFGC-LTLITTACVGARLVYLPKFEEKLFLSAI 276
Cdd:PRK06145 156 YTSGTTDRPKGVMHSYGNLHWKSIDHVIALGLTASE-RLLVVGPLYHVGAFdLPGIAVLWVGGTLRIHREFDPEAVLAAI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 277 EKYRVMMAFMVPPLMVFLAKHPIVDKYDLSSLMVLLCGAaplSRETEDQIKErIGVPFIR----QGYGLSESTL--SVLV 350
Cdd:PRK06145 235 ERHRLTCAWMAPVMLSRVLTVPDRDRFDLDSLAWCIGGG---EKTPESRIRD-FTRVFTRaryiDAYGLTETCSgdTLME 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 351 QNDEFCKPGSVGVLKVGIYAKVIDpDTGKLLGANERGELCFKGDGIMKGYIGDTKSTQTAIKDGWLHTGDIGYYDDDFEF 430
Cdd:PRK06145 311 AGREIEKIGSTGRALAHVEIRIAD-GAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGDWFRSGDVGYLDEEGFL 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 431 FIVDRIKELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGELPLAFVVKQANVQLTENEVIQFVNDNASPAKRL 510
Cdd:PRK06145 390 YLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPGATLTLEALDRHCRQRLASFKVP 469
|
490 500
....*....|....*....|....*..
gi 21355181 511 RgGVIFVDEIPKNPSGKILRRILREML 537
Cdd:PRK06145 470 R-QLKVRDELPRNPSGKVLKRVLRDEL 495
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
38-535 |
8.71e-56 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 195.09 E-value: 8.71e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 38 FGDRT-VLVDAVNGVEYSASFMHKSIVRLAYILQKLGVKQNDVVGLSSENSVNfALAMF-AGLAVGATVAPLNVTYSDRE 115
Cdd:PRK07514 13 FADRDaPFIETPDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPE-ALALYlATLRAGAVFLPLNTAYTLAE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 116 VDHAINLSKPKIIFASKITIDRVAKVASKnkfvKGIIAL-------SGTskkfkniydLKELMEDEKfktqPDFTsPAAN 188
Cdd:PRK07514 92 LDYFIGDAEPALVVCDPANFAWLSKIAAA----AGAPHVetldadgTGS---------LLEAAAAAP----DDFE-TVPR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 189 KDEDVSLIVCSSGTTGLPKGVQLTQMNLLA---TLDSQIQPTvipmEEVTLLTVIPWFHAFGCLTLITTACV-GARLVYL 264
Cdd:PRK07514 154 GADDLAAILYTSGTTGRSKGAMLSHGNLLSnalTLVDYWRFT----PDDVLIHALPIFHTHGLFVATNVALLaGASMIFL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 265 PKFEEKLFLSAIEKYRVMMAfmVPPLMVFLAKHPIVDKyDLSSLMVL-LCGAAPLSRETEDQIKERIGVPfIRQGYGLSE 343
Cdd:PRK07514 230 PKFDPDAVLALMPRATVMMG--VPTFYTRLLQEPRLTR-EAAAHMRLfISGSAPLLAETHREFQERTGHA-ILERYGMTE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 344 StlSVLVQN--DEFCKPGSVGVLKVGIYAKVIDPDTGKLLGANERGELCFKGDGIMKGYI---GDTKSTQTAikDGWLHT 418
Cdd:PRK07514 306 T--NMNTSNpyDGERRAGTVGFPLPGVSLRVTDPETGAELPPGEIGMIEVKGPNVFKGYWrmpEKTAEEFRA--DGFFIT 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 419 GDIGYYDDDFEFFIVDRIKELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGELPLAFVVKQANVQLTENEVIQ 498
Cdd:PRK07514 382 GDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKPGAALDEAAILA 461
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 21355181 499 FVND---NASPAKRlrggVIFVDEIPKNPSGKILRRILRE 535
Cdd:PRK07514 462 ALKGrlaRFKQPKR----VFFVDELPRNTMGKVQKNLLRE 497
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
66-543 |
1.08e-54 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 193.44 E-value: 1.08e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 66 AYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREVDHAINLSKPK--IIFAS----------KI 133
Cdd:PRK05677 64 AWLQQHTDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVNTNPLYTAREMEHQFNDSGAKalVCLANmahlaekvlpKT 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 134 TIDRV--AKVASKNKFVKGIIaLSGTSKKFKNIYDLKELMEDEKFKT-------QPdfTSPAANKDEDVSLIVCSSGTTG 204
Cdd:PRK05677 144 GVKHVivTEVADMLPPLKRLL-INAVVKHVKKMVPAYHLPQAVKFNDalakgagQP--VTEANPQADDVAVLQYTGGTTG 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 205 LPKGVQLTQMNLLATLdSQIQPTV-IPMEE--VTLLTVIPWFH----AFGCLTLITTacvGARLVYLPKFEE-KLFLSAI 276
Cdd:PRK05677 221 VAKGAMLTHRNLVANM-LQCRALMgSNLNEgcEILIAPLPLYHiyafTFHCMAMMLI---GNHNILISNPRDlPAMVKEL 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 277 EKYRVMMAFMVPPLMVFLAKHPIVDKYDLSSLMVLLCGAAPLSRETEDQIKERIGVPfIRQGYGLSESTLSVLVQNDEFC 356
Cdd:PRK05677 297 GKWKFSGFVGLNTLFVALCNNEAFRKLDFSALKLTLSGGMALQLATAERWKEVTGCA-ICEGYGMTETSPVVSVNPSQAI 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 357 KPGSVGVLKVGIYAKVIDPDtGKLLGANERGELCFKGDGIMKGYIGDTKSTQTAI-KDGWLHTGDIGYYDDDFEFFIVDR 435
Cdd:PRK05677 376 QVGTIGIPVPSTLCKVIDDD-GNELPLGEVGELCVKGPQVMKGYWQRPEATDEILdSDGWLKTGDIALIQEDGYMRIVDR 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 436 IKELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGELPLAFVVKQANVQLTENEVIQFVNDNASPAKRLRgGVI 515
Cdd:PRK05677 455 KKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIKVFVVVKPGETLTKEQVMEHMRANLTGYKVPK-AVE 533
|
490 500
....*....|....*....|....*....
gi 21355181 516 FVDEIPKNPSGKILRRILR-EMLKKQKSK 543
Cdd:PRK05677 534 FRDELPTTNVGKILRRELRdEELKKAGLK 562
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
64-535 |
1.09e-54 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 192.04 E-value: 1.09e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 64 RLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREVDHAINLSKPKIIFASKITIDRVAKVAS 143
Cdd:PRK08276 23 RLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVLIVSAALADTAAELAA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 144 KNKF-VKGIIALSGTSKKFKniyDLKELMEDekfktQPDfTSPAankdeDVSL---IVCSSGTTGLPKGV--QLTQMNLL 217
Cdd:PRK08276 103 ELPAgVPLLLVVAGPVPGFR---SYEEALAA-----QPD-TPIA-----DETAgadMLYSSGTTGRPKGIkrPLPGLDPD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 218 ATLDSQIQPTVIPM----EEVTLLTViPWFHAFGCLTLITTACVGARLVYLPKFEEKLFLSAIEKYRVMMAFMVPPLMVF 293
Cdd:PRK08276 169 EAPGMMLALLGFGMyggpDSVYLSPA-PLYHTAPLRFGMSALALGGTVVVMEKFDAEEALALIERYRVTHSQLVPTMFVR 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 294 LAKHP--IVDKYDLSSLMVLLCGAAPLSRETEDQIKERIGvPFIRQGYGLSESTLSVLVQNDEFC-KPGSVGVLKVGIyA 370
Cdd:PRK08276 248 MLKLPeeVRARYDVSSLRVAIHAAAPCPVEVKRAMIDWWG-PIIHEYYASSEGGGVTVITSEDWLaHPGSVGKAVLGE-V 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 371 KVIDPDtGKLLGANERGELCFKGDGIMKGYIGDTKSTQTA-IKDGWLHTGDIGYYDDDFEFFIVDRIKELIKYKGYQVPP 449
Cdd:PRK08276 326 RILDED-GNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAArNPHGWVTVGDVGYLDEDGYLYLTDRKSDMIISGGVNIYP 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 450 AEIEALLLTNDKIKDAAVIGKPDEEAGELPLAfVVK-----QANVQLTEnEVIQFVNDNASPAKRLRgGVIFVDEIPKNP 524
Cdd:PRK08276 405 QEIENLLVTHPKVADVAVFGVPDEEMGERVKA-VVQpadgaDAGDALAA-ELIAWLRGRLAHYKCPR-SIDFEDELPRTP 481
|
490
....*....|.
gi 21355181 525 SGKILRRILRE 535
Cdd:PRK08276 482 TGKLYKRRLRD 492
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
64-535 |
5.17e-54 |
|
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: 188.74 E-value: 5.17e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 64 RLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREVDHAINLSKPKIIFaskitidrvakvas 143
Cdd:cd05903 13 RLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFV-------------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 144 knkfvkgiialsgTSKKFKNiydlkelmedekfktqpdfTSPAANKDeDVSLIVCSSGTTGLPKGVQLTQMNLLATLDSQ 223
Cdd:cd05903 79 -------------VPERFRQ-------------------FDPAAMPD-AVALLLFTSGTTGEPKGVMHSHNTLSASIRQY 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 224 IQPTVIPmEEVTLLTVIPWFHAFGCLTLITTACV-GARLVYLPKFEEKLFLSAIEKYRVMMAFMVPPLMVFLAKHPIVDK 302
Cdd:cd05903 126 AERLGLG-PGDVFLVASPMAHQTGFVYGFTLPLLlGAPVVLQDIWDPDKALALMREHGVTFMMGATPFLTDLLNAVEEAG 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 303 YDLSSLMVLLCGAAPLSRETEDQIKERIGVpFIRQGYGLSE--STLSVLVQNDEFCKPGSVGVLKVGIYAKVIDpDTGKL 380
Cdd:cd05903 205 EPLSRLRTFVCGGATVPRSLARRAAELLGA-KVCSAYGSTEcpGAVTSITPAPEDRRLYTDGRPLPGVEIKVVD-DTGAT 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 381 LGANERGELCFKGDGIMKGYIGDTKSTQTAIKDGWLHTGDIGYYDDDFEFFIVDRIKELIKYKGYQVPPAEIEALLLTND 460
Cdd:cd05903 283 LAPGVEGELLSRGPSVFLGYLDRPDLTADAAPEGWFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHP 362
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21355181 461 KIKDAAVIGKPDEEAGELPLAFVVKQANVQLTENEVIQFVnDNASPAK-RLRGGVIFVDEIPKNPSGKILRRILRE 535
Cdd:cd05903 363 GVIEAAVVALPDERLGERACAVVVTKSGALLTFDELVAYL-DRQGVAKqYWPERLVHVDDLPRTPSGKVQKFRLRE 437
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
64-535 |
3.12e-53 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 188.36 E-value: 3.12e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 64 RLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREVDHAINLSKPKIIFASKITIDRVAKVAS 143
Cdd:PRK13391 36 RLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAAYIVDDSGARALITSAAKLDVARALLK 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 144 KNKFVKGIIAL--SGTSKKFkniYDLKELMEDekfktQPDftSPAANKDEDVSLIVcSSGTTGLPKGV--QL------TQ 213
Cdd:PRK13391 116 QCPGVRHRLVLdgDGELEGF---VGYAEAVAG-----LPA--TPIADESLGTDMLY-SSGTTGRPKGIkrPLpeqppdTP 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 214 MNLLATLdsqiQPTVIPMEEVTLLTVIPWFHAFGCLTLITTACVGARLVYLPKFEEKLFLSAIEKYRVMMAFMVPPLMVF 293
Cdd:PRK13391 185 LPLTAFL----QRLWGFRSDMVYLSPAPLYHSAPQRAVMLVIRLGGTVIVMEHFDAEQYLALIEEYGVTHTQLVPTMFSR 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 294 LAKHP--IVDKYDLSSLMVLLCGAAPLSRETEDQIKERIGvPFIRQGYGLSESTLSVLVQNDEF-CKPGSVGVLKVGIYa 370
Cdd:PRK13391 261 MLKLPeeVRDKYDLSSLEVAIHAAAPCPPQVKEQMIDWWG-PIIHEYYAATEGLGFTACDSEEWlAHPGTVGRAMFGDL- 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 371 kVIDPDTGKLLGANERGELCFKGdGIMKGYIGDTKSTQTAIKD--GWLHTGDIGYYDDDFEFFIVDRIKELIKYKGYQVP 448
Cdd:PRK13391 339 -HILDDDGAELPPGEPGTIWFEG-GRPFEYLNDPAKTAEARHPdgTWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIY 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 449 PAEIEALLLTNDKIKDAAVIGKPDEEAGELPLAFVVK----QANVQLTEnEVIQFVNDNASPAKRLRgGVIFVDEIPKNP 524
Cdd:PRK13391 417 PQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPvdgvDPGPALAA-ELIAFCRQRLSRQKCPR-SIDFEDELPRLP 494
|
490
....*....|.
gi 21355181 525 SGKILRRILRE 535
Cdd:PRK13391 495 TGKLYKRLLRD 505
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
31-535 |
3.38e-53 |
|
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: 188.86 E-value: 3.38e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 31 ILDKY-KSFGDRTVLV---DAVNGVEYSASFMHKSIVRLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAP 106
Cdd:cd05970 22 VVDAMaKEYPDKLALVwcdDAGEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 107 LNVTYSDREVDHAINLSKPKIIFA--SKITIDRVAKVA----SKNKFVK-GIIALSGtskkfknIYDLKELMEDekfkTQ 179
Cdd:cd05970 102 ATHQLTAKDIVYRIESADIKMIVAiaEDNIPEEIEKAApecpSKPKLVWvGDPVPEG-------WIDFRKLIKN----AS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 180 PDFTSPAAN---KDEDVSLIVCSSGTTGLPKGVQ----------LTQMNLLATLDSQIQPTVIPmeevTLLTVIPWFHAF 246
Cdd:cd05970 171 PDFERPTANsypCGEDILLVYFSSGTTGMPKMVEhdftyplghiVTAKYWQNVREGGLHLTVAD----TGWGKAVWGKIY 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 247 GcltliTTACVGARLVY-LPKFEEKLFLSAIEKYRVMmAFMVPPLMV-FLAKHPIvDKYDLSSLMVLLCGAAPLSRETED 324
Cdd:cd05970 247 G-----QWIAGAAVFVYdYDKFDPKALLEKLSKYGVT-TFCAPPTIYrFLIREDL-SRYDLSSLRYCTTAGEALNPEVFN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 325 QIKERIGVPfIRQGYGLSESTLSVLVQNDEFCKPGSVGVLKVGIYAKVIDPDtGKLLGANERGELCFKGD-----GIMKG 399
Cdd:cd05970 320 TFKEKTGIK-LMEGFGQTETTLTIATFPWMEPKPGSMGKPAPGYEIDLIDRE-GRSCEAGEEGEIVIRTSkgkpvGLFGG 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 400 YIGDTKSTQTAIKDGWLHTGDIGYYDDDFEFFIVDRIKELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGELP 479
Cdd:cd05970 398 YYKDAEKTAEVWHDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVV 477
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 21355181 480 LAFVVKQANVQLTE---NEVIQFVNDNASPAKRLRgGVIFVDEIPKNPSGKILRRILRE 535
Cdd:cd05970 478 KATIVLAKGYEPSEelkKELQDHVKKVTAPYKYPR-IVEFVDELPKTISGKIRRVEIRE 535
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
25-534 |
7.70e-53 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 188.31 E-value: 7.70e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 25 RSLGQYILDKYKSFGDRTVLVdavngveysasFMHKSI---------VRLAYILQKLGVKQNDVVGLSSENSVNFALAMF 95
Cdd:PRK07059 23 PSLADLLEESFRQYADRPAFI-----------CMGKAItygeldelsRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 96 AGLAVGATVAPLNVTYSDREVDHAINLSKPKII-----FASkiTIDRV-AKVASKNKFV---------KGII-------- 152
Cdd:PRK07059 92 AVLRAGYVVVNVNPLYTPRELEHQLKDSGAEAIvvlenFAT--TVQQVlAKTAVKHVVVasmgdllgfKGHIvnfvvrrv 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 153 -------ALSGtSKKFKNIydlkeLMEDEKFKTQPDFTSPaankdEDVSLIVCSSGTTGLPKGVQLTQMNLLAT---LDS 222
Cdd:PRK07059 170 kkmvpawSLPG-HVRFNDA-----LAEGARQTFKPVKLGP-----DDVAFLQYTGGTTGVSKGATLLHRNIVANvlqMEA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 223 QIQPTVI---PMEEVTLLTVIPWFHAFGcLT---LITTACvGARLVYLPKFEE-KLFLSAIEKYRVMMAFMVPPLMVFLA 295
Cdd:PRK07059 239 WLQPAFEkkpRPDQLNFVCALPLYHIFA-LTvcgLLGMRT-GGRNILIPNPRDiPGFIKELKKYQVHIFPAVNTLYNALL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 296 KHPIVDKYDLSSLMVLLCGAAPLSRETEDQIKERIGVPfIRQGYGLSEsTLSVLVQN----DEFCkpGSVGVLKVGIYAK 371
Cdd:PRK07059 317 NNPDFDKLDFSKLIVANGGGMAVQRPVAERWLEMTGCP-ITEGYGLSE-TSPVATCNpvdaTEFS--GTIGLPLPSTEVS 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 372 VIDpDTGKLLGANERGELCFKGDGIMKGYIGDTKSTQTAI-KDGWLHTGDIGYYDDDFEFFIVDRIKELIKYKGYQVPPA 450
Cdd:PRK07059 393 IRD-DDGNDLPLGEPGEICIRGPQVMAGYWNRPDETAKVMtADGFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPN 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 451 EIEALLLTNDKIKDAAVIGKPDEEAGELPLAFVVKQaNVQLTENEVIQFVNDNASPAKRLRgGVIFVDEIPKNPSGKILR 530
Cdd:PRK07059 472 EIEEVVASHPGVLEVAAVGVPDEHSGEAVKLFVVKK-DPALTEEDVKAFCKERLTNYKRPK-FVEFRTELPKTNVGKILR 549
|
....
gi 21355181 531 RILR 534
Cdd:PRK07059 550 RELR 553
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
30-534 |
1.26e-52 |
|
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: 186.81 E-value: 1.26e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 30 YILDKYKSFGDRTVLVDAVNGVEYSAsfMHKSIVRLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNV 109
Cdd:cd05959 9 VDLNLNEGRGDKTAFIDDAGSLTYAE--LEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 110 TYSDREVDHAINLSKPKIIFASKITIDRVAKVASKNKFVKGIIALSGTSKKFKNIYDLKELMEDEkfktQPDFTsPAANK 189
Cdd:cd05959 87 LLTPDDYAYYLEDSRARVVVVSGELAPVLAAALTKSEHTLVVLIVSGGAGPEAGALLLAELVAAE----AEQLK-PAATH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 190 DEDVSLIVCSSGTTGLPKGVQLTQMNLLATLDSQIQPTVIPMEEVTLLTVIPWFHAFGCLTLITTA-CVGARLVYLPKF- 267
Cdd:cd05959 162 ADDPAFWLYSSGSTGRPKGVVHLHADIYWTAELYARNVLGIREDDVCFSAAKLFFAYGLGNSLTFPlSVGATTVLMPERp 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 268 EEKLFLSAIEKYRVMMAFMVPPLMVFLAKHPIVDKYDLSSLMVLLCGAAPLSRETEDQIKERIGVPfIRQGYGLSEsTLS 347
Cdd:cd05959 242 TPAAVFKRIRRYRPTVFFGVPTLYAAMLAAPNLPSRDLSSLRLCVSAGEALPAEVGERWKARFGLD-ILDGIGSTE-MLH 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 348 VLVQN-DEFCKPGSVGVLKVGIYAKVIDPDtGKLLGANERGELCFKGDGIMKGYIGDTKSTQTAIKDGWLHTGDIGYYDD 426
Cdd:cd05959 320 IFLSNrPGRVRYGTTGKPVPGYEVELRDED-GGDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQGEWTRTGDKYVRDD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 427 DFEFFIVDRIKELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGELPLAFVVKQANVQLTEN---EVIQFVNDN 503
Cdd:cd05959 399 DGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPGYEDSEAleeELKEFVKDR 478
|
490 500 510
....*....|....*....|....*....|.
gi 21355181 504 ASPAKRLRgGVIFVDEIPKNPSGKILRRILR 534
Cdd:cd05959 479 LAPYKYPR-WIVFVDELPKTATGKIQRFKLR 508
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
51-469 |
7.17e-52 |
|
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: 183.18 E-value: 7.17e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 51 VEYSASFMHKSIVRLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREVDHAINLSKPKIIFA 130
Cdd:cd05907 4 QPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 131 SKitidrvakvasknkfvkgiialsgtskkfkniydlkelmedekfktqPDftspaankdeDVSLIVCSSGTTGLPKGVQ 210
Cdd:cd05907 84 ED-----------------------------------------------PD----------DLATIIYTSGTTGRPKGVM 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 211 LTQMNLLATLDSQIQpTVIPMEEVTLLTVIPWFHAFGCLTLITTACV-GARLVYLPkfEEKLFLSAIEKYR--VMMAfmV 287
Cdd:cd05907 107 LSHRNILSNALALAE-RLPATEGDRHLSFLPLAHVFERRAGLYVPLLaGARIYFAS--SAETLLDDLSEVRptVFLA--V 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 288 PPLM------VFLAKHP-----IVDKYDLSSLMVLLCGAAPLSRETeDQIKERIGVPfIRQGYGLSESTLSVLVQNDEFC 356
Cdd:cd05907 182 PRVWekvyaaIKVKAVPglkrkLFDLAVGGRLRFAASGGAPLPAEL-LHFFRALGIP-VYEGYGLTETSAVVTLNPPGDN 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 357 KPGSVGVLKVGIYAKvIDPDtgkllganerGELCFKGDGIMKGYIGDT-KSTQTAIKDGWLHTGDIGYYDDDFEFFIVDR 435
Cdd:cd05907 260 RIGTVGKPLPGVEVR-IADD----------GEILVRGPNVMLGYYKNPeATAEALDADGWLHTGDLGEIDEDGFLHITGR 328
|
410 420 430
....*....|....*....|....*....|....*
gi 21355181 436 IKELIKY-KGYQVPPAEIEALLLTNDKIKDAAVIG 469
Cdd:cd05907 329 KKDLIITsGGKNISPEPIENALKASPLISQAVVIG 363
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
58-535 |
7.29e-52 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 185.37 E-value: 7.29e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 58 MHKSIVRLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREVDHAINLSKPKIIFASKITIDR 137
Cdd:PRK07786 48 LDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAHVVVTEAALAPV 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 138 VAKVASKNKFVKGIIALSGTSKKfkNIYDLKELMEDekfkTQPDFtSPAANKDEDVSLIVCSSGTTGLPKGVQLTQMNLL 217
Cdd:PRK07786 128 ATAVRDIVPLLSTVVVAGGSSDD--SVLGYEDLLAE----AGPAH-APVDIPNDSPALIMYTSGTTGRPKGAVLTHANLT 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 218 ATLDSQIQPTVIPME-EVTLLTViPWFHAFGCLTLITTACVGARLVYLP--KFEEKLFLSAIEKYRVMMAFMVPPLMVFL 294
Cdd:PRK07786 201 GQAMTCLRTNGADINsDVGFVGV-PLFHIAGIGSMLPGLLLGAPTVIYPlgAFDPGQLLDVLEAEKVTGIFLVPAQWQAV 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 295 AKHPIVDKYDLSsLMVLLCGAAPLSRETEDQIKERIGVPFIRQGYGLSEST--LSVLVQNDEFCKPGSVGVLKVGIYAKV 372
Cdd:PRK07786 280 CAEQQARPRDLA-LRVLSWGAAPASDTLLRQMAATFPEAQILAAFGQTEMSpvTCMLLGEDAIRKLGSVGKVIPTVAARV 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 373 IDPDTGKLlGANERGELCFKGDGIMKGYIGDTKSTQTAIKDGWLHTGDIGYYDDDFEFFIVDRIKELIKYKGYQVPPAEI 452
Cdd:PRK07786 359 VDENMNDV-PVGEVGEIVYRAPTLMSGYWNNPEATAEAFAGGWFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEV 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 453 EALLLTNDKIKDAAVIGKPDEEAGELPLAFV-VKQANVQLTENEVIQFVNDNASPAKRLRGGVIfVDEIPKNPSGKILRR 531
Cdd:PRK07786 438 ENVLASHPDIVEVAVIGRADEKWGEVPVAVAaVRNDDAALTLEDLAEFLTDRLARYKHPKALEI-VDALPRNPAGKVLKT 516
|
....
gi 21355181 532 ILRE 535
Cdd:PRK07786 517 ELRE 520
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
69-535 |
1.45e-51 |
|
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: 182.96 E-value: 1.45e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 69 LQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREVDHAINLSKPKIIFASKITIDRVAKVASKNKFV 148
Cdd:cd05929 14 QRRLLLLDVYSIALNRNARAAAAEGVWIADGVYIYLINSILTVFAAAAAWKCGACPAYKSSRAPRAEACAIIEIKAAALV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 149 KGIIALSGTSKKFkniydlkelmedekfktqPDFTSPAANKDE----DVS---LIVCSSGTTGLPKGVQLTQMNLLATLD 221
Cdd:cd05929 94 CGLFTGGGALDGL------------------EDYEAAEGGSPEtpieDEAagwKMLYSGGTTGRPKGIKRGLPGGPPDND 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 222 SQIQPTVI--PMEEVTLLTVIPWFHAFGCLTLITTACVGARLVYLPKFEEKLFLSAIEKYRVMMAFMVPPLMVFLAKHP- 298
Cdd:cd05929 156 TLMAAALGfgPGADSVYLSPAPLYHAAPFRWSMTALFMGGTLVLMEKFDPEEFLRLIERYRVTFAQFVPTMFVRLLKLPe 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 299 -IVDKYDLSSLMVLLCGAAPLSreteDQIKERI---GVPFIRQGYGLSESTLSVLVQNDEFCK-PGSVGVLKVGIyAKVI 373
Cdd:cd05929 236 aVRNAYDLSSLKRVIHAAAPCP----PWVKEQWidwGGPIIWEYYGGTEGQGLTIINGEEWLThPGSVGRAVLGK-VHIL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 374 DPDtGKLLGANERGELCFKGdGIMKGYIGDTKSTQTAI-KDGWLHTGDIGYYDDDFEFFIVDRIKELIKYKGYQVPPAEI 452
Cdd:cd05929 311 DED-GNEVPPGEIGEVYFAN-GPGFEYTNDPEKTAAARnEGGWSTLGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEI 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 453 EALLLTNDKIKDAAVIGKPDEEAGELPLAFV----VKQANVQLTEnEVIQFVNDNASPAKRLRgGVIFVDEIPKNPSGKI 528
Cdd:cd05929 389 ENALIAHPKVLDAAVVGVPDEELGQRVHAVVqpapGADAGTALAE-ELIAFLRDRLSRYKCPR-SIEFVAELPRDDTGKL 466
|
....*..
gi 21355181 529 LRRILRE 535
Cdd:cd05929 467 YRRLLRD 473
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
58-530 |
2.76e-49 |
|
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 162605 [Multi-domain] Cd Length: 436 Bit Score: 176.10 E-value: 2.76e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 58 MHKSIVRLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREVDHAINLSKPKIIFASkitidr 137
Cdd:TIGR01923 5 LDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTD------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 138 vakvASKNKFVKGIIALSGTSKKFKniydlkelmEDEKFKTQPdftspaanKDEDVSLIVCSSGTTGLPKGVQLTQMNLL 217
Cdd:TIGR01923 79 ----SLLEEKDFQADSLDRIEAAGR---------YETSLSASF--------NMDQIATLMFTSGTTGKPKAVPHTFRNHY 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 218 ATLDSQIQpTVIPMEEVTLLTVIPWFHAFGCLTLITTACVGARLVYLPKFEEklFLSAIEKYRVMMAFMVPPLMVFLAK- 296
Cdd:TIGR01923 138 ASAVGSKE-NLGFTEDDNWLLSLPLYHISGLSILFRWLIEGATLRIVDKFNQ--LLEMIANERVTHISLVPTQLNRLLDe 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 297 --HPivdkydlSSLMVLLCGAAPLSRETEDQIKERiGVPfIRQGYGLSESTLSVLVQNDEFCK-PGSVGVLKVGIYAKVI 373
Cdd:TIGR01923 215 ggHN-------ENLRKILLGGSAIPAPLIEEAQQY-GLP-IYLSYGMTETCSQVTTATPEMLHaRPDVGRPLAGREIKIK 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 374 DPDTGkllganERGELCFKGDGIMKGYIGDTKSTQTAIKDGWLHTGDIGYYDDDFEFFIVDRIKELIKYKGYQVPPAEIE 453
Cdd:TIGR01923 286 VDNKE------GHGEIMVKGANLMKGYLYQGELTPAFEQQGWFNTGDIGELDGEGFLYVLGRRDDLIISGGENIYPEEIE 359
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21355181 454 ALLLTNDKIKDAAVIGKPDEEAGELPLAFVVkqANVQLTENEVIQFVNDNASPAKRLRgGVIFVDEIPKNPSGKILR 530
Cdd:TIGR01923 360 TVLYQHPGIQEAVVVPKPDAEWGQVPVAYIV--SESDISQAKLIAYLTEKLAKYKVPI-AFEKLDELPYNASGKILR 433
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
40-537 |
5.79e-49 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 176.54 E-value: 5.79e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 40 DRTVLVDAVNGVEYSASFMHKSIVRLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREVDHA 119
Cdd:PRK09088 10 QRLAAVDLALGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDAL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 120 INLSKPKIIFASKITIDRVAKVASKNKFVKGIIALsgtskkfkniydlkelmedekfktQPDFTSPAanKDEDVSLIVCS 199
Cdd:PRK09088 90 LQDAEPRLLLGDDAVAAGRTDVEDLAAFIASADAL------------------------EPADTPSI--PPERVSLILFT 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 200 SGTTGLPKGVQLTQMNLLATLDSQIQPTVIPMEEVTLLTViPWFHAFGCLTLI-TTACVGARLVYLPKFEEKLFLS---- 274
Cdd:PRK09088 144 SGTSGQPKGVMLSERNLQQTAHNFGVLGRVDAHSSFLCDA-PMFHIIGLITSVrPVLAVGGSILVSNGFEPKRTLGrlgd 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 275 ---AIEKYrvmmaFMVPPLMVFLAKHPIVDKYDLSSLMVLLCGAAP-LSRETEDQIKEriGVPFIrQGYGLSE--STLSV 348
Cdd:PRK09088 223 palGITHY-----FCVPQMAQAFRAQPGFDAAALRHLTALFTGGAPhAAEDILGWLDD--GIPMV-DGFGMSEagTVFGM 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 349 LVQNDEF-CKPGSVGVLKVGIYAKVIDpDTGKLLGANERGELCFKGDGIMKGYIGDTKSTQTAI-KDGWLHTGDIGYYDD 426
Cdd:PRK09088 295 SVDCDVIrAKAGAAGIPTPTVQTRVVD-DQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFtGDGWFRTGDIARRDA 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 427 DFEFFIVDRIKELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGELPLAFVVKQANVQLTENEVIQFVNDNASP 506
Cdd:PRK09088 374 DGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADGAPLDLERIRSHLSTRLAK 453
|
490 500 510
....*....|....*....|....*....|.
gi 21355181 507 AKrLRGGVIFVDEIPKNPSGKILRRILREML 537
Cdd:PRK09088 454 YK-VPKHLRLVDALPRTASGKLQKARLRDAL 483
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
25-538 |
6.60e-49 |
|
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: 177.26 E-value: 6.60e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 25 RSLGQYILDKYKSFGDRTVLVDAvngvEYSASF--MHKSIVRLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGA 102
Cdd:COG1021 25 ETLGDLLRRRAERHPDRIAVVDG----ERRLSYaeLDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 103 tvAPLNVTYSDR--EVDHAINLSKPKIIfaskITIDRVAK---------VASKNKFVKGIIALsGTSKKFkniYDLKELM 171
Cdd:COG1021 101 --IPVFALPAHRraEISHFAEQSEAVAY----IIPDRHRGfdyralareLQAEVPSLRHVLVV-GDAGEF---TSLDALL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 172 EDEKFKTQPDftsPAAnkdEDVSLIVCSSGTTGLPKGV---------QLTQMNLLATLDSQiqpTVipmeevtLLTVIPW 242
Cdd:COG1021 171 AAPADLSEPR---PDP---DDVAFFQLSGGTTGLPKLIprthddylySVRASAEICGLDAD---TV-------YLAALPA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 243 FHAF--GCLTLITTACVGARLVYLPKFEEKLFLSAIEKYRVMMAFMVPPLMVFLAKHPIVDKYDLSSLMVLLCGAAPLSR 320
Cdd:COG1021 235 AHNFplSSPGVLGVLYAGGTVVLAPDPSPDTAFPLIERERVTVTALVPPLALLWLDAAERSRYDLSSLRVLQVGGAKLSP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 321 ETEDQIKERIGVpFIRQGYGLSESTLSV--------LVQN---------DEFckpgsvgvlkvgiyaKVIDPDtGKLLGA 383
Cdd:COG1021 315 ELARRVRPALGC-TLQQVFGMAEGLVNYtrlddpeeVILTtqgrpispdDEV---------------RIVDED-GNPVPP 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 384 NERGELCFKGDGIMKGYIGDTKSTQTAI-KDGWLHTGDIGYYDDDFEFFIVDRIKELIKYKGYQVPPAEIEALLLTNDKI 462
Cdd:COG1021 378 GEVGELLTRGPYTIRGYYRAPEHNARAFtPDGFYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAV 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 463 KDAAVIGKPDEEAGELPLAFVVKQaNVQLTENEVIQFVndnaspakRLRG--------GVIFVDEIPKNPSGKILRRILR 534
Cdd:COG1021 458 HDAAVVAMPDEYLGERSCAFVVPR-GEPLTLAELRRFL--------RERGlaafklpdRLEFVDALPLTAVGKIDKKALR 528
|
....
gi 21355181 535 EMLK 538
Cdd:COG1021 529 AALA 532
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
66-535 |
8.92e-49 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 177.38 E-value: 8.92e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 66 AYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREVDHAINLSKPKII-----FASKITiDRVAK 140
Cdd:PRK08751 65 AYLLGELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVLvvidnFGTTVQ-QVIAD 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 141 VASKNKFVKGIIALSGTSKK----FKNIYdLKELMEDEKFKTQPDF----------TSPAANKD-EDVSLIVCSSGTTGL 205
Cdd:PRK08751 144 TPVKQVITTGLGDMLGFPKAalvnFVVKY-VKKLVPEYRINGAIRFrealalgrkhSMPTLQIEpDDIAFLQYTGGTTGV 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 206 PKGVQLTQMNLLATLD--SQIQPTVIPMEE--VTLLTVIPWFHAF-------------GCLTLITTacvgarlvylPKfE 268
Cdd:PRK08751 223 AKGAMLTHRNLVANMQqaHQWLAGTGKLEEgcEVVITALPLYHIFaltanglvfmkigGCNHLISN----------PR-D 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 269 EKLFLSAIEKYRVMMAFMVPPLMVFLAKHPIVDKYDLSSLMVLLCGAAPLSRETEDQIKERIGVPFIrQGYGLSESTLSV 348
Cdd:PRK08751 292 MPGFVKELKKTRFTAFTGVNTLFNGLLNTPGFDQIDFSSLKMTLGGGMAVQRSVAERWKQVTGLTLV-EAYGLTETSPAA 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 349 LVQN---DEFckPGSVGvLKVGIYAKVIDPDTGKLLGANERGELCFKGDGIMKGYIGDTKSTQTAIK-DGWLHTGDIGYY 424
Cdd:PRK08751 371 CINPltlKEY--NGSIG-LPIPSTDACIKDDAGTVLAIGEIGELCIKGPQVMKGYWKRPEETAKVMDaDGWLHTGDIARM 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 425 DDDFEFFIVDRIKELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGELPLAFVVKQaNVQLTENEVIQFVNDNA 504
Cdd:PRK08751 448 DEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEIVKVVIVKK-DPALTAEDVKAHARANL 526
|
490 500 510
....*....|....*....|....*....|.
gi 21355181 505 SPAKRLRgGVIFVDEIPKNPSGKILRRILRE 535
Cdd:PRK08751 527 TGYKQPR-IIEFRKELPKTNVGKILRRELRD 556
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
17-532 |
1.18e-48 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 181.66 E-value: 1.18e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 17 TERQAQDSRSLGQYILDKYKSFGDRTVLVDAVnGVEYSASFMHKSIVRLAYILQKLGVKQnDVVGLSSENSVNFALAMFA 96
Cdd:PRK08633 607 WKSRKEALPPLAEAWIDTAKRNWSRLAVADST-GGELSYGKALTGALALARLLKRELKDE-ENVGILLPPSVAGALANLA 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 97 GLAVGATVAPLNVTYSDREVDHAINLSKPKIIFASKITIDRVAKvasknkfvKGIIALSGTSKKFKNIYDLKELMED-EK 175
Cdd:PRK08633 685 LLLAGKVPVNLNYTASEAALKSAIEQAQIKTVITSRKFLEKLKN--------KGFDLELPENVKVIYLEDLKAKISKvDK 756
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 176 FKT------QPDFTSPAAN----KDEDVSLIVCSSGTTGLPKGVQLTQMNLLATLDsQIQPTVIPMEEVTLLTVIPWFHA 245
Cdd:PRK08633 757 LTAllaarlLPARLLKRLYgptfKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIE-QISDVFNLRNDDVILSSLPFFHS 835
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 246 FGCL-TLITTACVGARLVYLPK-FEEKLFLSAIEKYRVMMAFMVPPLMVFLAKHPIVDKYDLSSLMVLLCGAAPLSRETE 323
Cdd:PRK08633 836 FGLTvTLWLPLLEGIKVVYHPDpTDALGIAKLVAKHRATILLGTPTFLRLYLRNKKLHPLMFASLRLVVAGAEKLKPEVA 915
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 324 DQIKERIGVPfIRQGYGLSEST--LSVLVQNDE--------FCKPGSVGVLKVGIYAKVIDPDTGKLLGANERGELCFKG 393
Cdd:PRK08633 916 DAFEEKFGIR-ILEGYGATETSpvASVNLPDVLaadfkrqtGSKEGSVGMPLPGVAVRIVDPETFEELPPGEDGLILIGG 994
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 394 DGIMKGYIGDTKSTQTAIKD----GWLHTGDIGYYDDDFEFFIVDRIKELIKYKGYQVPPAEIEALLLT--NDKIKDAAV 467
Cdd:PRK08633 995 PQVMKGYLGDPEKTAEVIKDidgiGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAKalGGEEVVFAV 1074
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21355181 468 IGKPDEEAGElplAFVVKQANVQLTENEVIQFVNDNASPAKRLRGGVIFVDEIPKNPSGKI-LRRI 532
Cdd:PRK08633 1075 TAVPDEKKGE---KLVVLHTCGAEDVEELKRAIKESGLPNLWKPSRYFKVEALPLLGSGKLdLKGL 1137
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
191-534 |
2.68e-48 |
|
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: 173.43 E-value: 2.68e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 191 EDVSLIVCSSGTTGLPKGVQLTQMNLLATLDSQIQPTVIPMEEVTLLTVIPWFHAFGC-LTLITTACVGARLVYLPKFEE 269
Cdd:cd05958 97 DDICILAFTSGTTGAPKATMHFHRDPLASADRYAVNVLRLREDDRFVGSPPLAFTFGLgGVLLFPFGVGASGVLLEEATP 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 270 KLFLSAIEKYRVMMAFMVPPLMVFLAKHPIVDKYDLSSLMVLLCGAAPLSRETEDQIKERIGVPFIrQGYGLSEStLSVL 349
Cdd:cd05958 177 DLLLSAIARYKPTVLFTAPTAYRAMLAHPDAAGPDLSSLRKCVSAGEALPAALHRAWKEATGIPII-DGIGSTEM-FHIF 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 350 VQNDE-FCKPGSVGVLKVGIYAKVIDpDTGKLLGANERGELCFKGDGIMKgYIGDtKSTQTAIKDGWLHTGDIGYYDDDF 428
Cdd:cd05958 255 ISARPgDARPGATGKPVPGYEAKVVD-DEGNPVPDGTIGRLAVRGPTGCR-YLAD-KRQRTYVQGGWNITGDTYSRDPDG 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 429 EFFIVDRIKELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGELPLAFVVKQANVQLTE---NEVIQFVNDNAS 505
Cdd:cd05958 332 YFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIPGPvlaRELQDHAKAHIA 411
|
330 340
....*....|....*....|....*....
gi 21355181 506 PAKRLRgGVIFVDEIPKNPSGKILRRILR 534
Cdd:cd05958 412 PYKYPR-AIEFVTELPRTATGKLQRFALR 439
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
192-534 |
3.21e-48 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 171.12 E-value: 3.21e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 192 DVSLIVCSSGTTGLPKGVQLTQMNLLA-----TLDSQIQPTVipmeevTLLTVIPWFHAFGCL-TLITTACVGARLV--- 262
Cdd:cd05944 3 DVAAYFHTGGTTGTPKLAQHTHSNEVYnawmlALNSLFDPDD------VLLCGLPLFHVNGSVvTLLTPLASGAHVVlag 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 263 ---YLPKFEEKLFLSAIEKYRVMMAFMVPPLMVFLAKHPIvdKYDLSSLMVLLCGAAPLSRETEDQIKERIGVPFIrQGY 339
Cdd:cd05944 77 pagYRNPGLFDNFWKLVERYRITSLSTVPTVYAALLQVPV--NADISSLRFAMSGAAPLPVELRARFEDATGLPVV-EGY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 340 GLSEST-LSVLVQNDEFCKPGSVGV----LKVGIyaKVIDPDTGKLL--GANERGELCFKGDGIMKGYIGDTKSTQTAIK 412
Cdd:cd05944 154 GLTEATcLVAVNPPDGPKRPGSVGLrlpyARVRI--KVLDGVGRLLRdcAPDEVGEICVAGPGVFGGYLYTEGNKNAFVA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 413 DGWLHTGDIGYYDDDFEFFIVDRIKELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGELPLAFVVKQANVQLT 492
Cdd:cd05944 232 DGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPGAVVE 311
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 21355181 493 ENEVIQFVNDNASPAKRLRGGVIFVDEIPKNPSGKILRRILR 534
Cdd:cd05944 312 EEELLAWARDHVPERAAVPKHIEVLEELPVTAVGKVFKPALR 353
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
64-534 |
5.56e-48 |
|
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: 172.69 E-value: 5.56e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 64 RLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREVDHAINLSKPKIIFASKitidrvakvas 143
Cdd:cd05969 12 RFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTE----------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 144 knkfvkgiialsgtskkfkniydlkELMEdekfKTQPdftspaankdEDVSLIVCSSGTTGLPKGVQLTQMNLLATLDSQ 223
Cdd:cd05969 81 -------------------------ELYE----RTDP----------EDPTLLHYTSGTTGTPKGVLHVHDAMIFYYFTG 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 224 IQPTVIPMEEVTLLTVIPWFHAFGCLTLITTACVGARLV-YLPKFEEKLFLSAIEKYRVMMAFMVPPLMVFLAKHPI--V 300
Cdd:cd05969 122 KYVLDLHPDDIYWCTADPGWVTGTVYGIWAPWLNGVTNVvYEGRFDAESWYGIIERVKVTVWYTAPTAIRMLMKEGDelA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 301 DKYDLSSLMVLLCGAAPLSRETEDQIKERIGVPfIRQGYGLSEsTLSVLVQN--DEFCKPGSVGVLKVGIYAKVIDPDtG 378
Cdd:cd05969 202 RKYDLSSLRFIHSVGEPLNPEAIRWGMEVFGVP-IHDTWWQTE-TGSIMIANypCMPIKPGSMGKPLPGVKAAVVDEN-G 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 379 KLLGANERGELCFKGD--GIMKGYIGDTKSTQTAIKDGWLHTGDIGYYDDDFEFFIVDRIKELIKYKGYQVPPAEIEALL 456
Cdd:cd05969 279 NELPPGTKGILALKPGwpSMFRGIWNDEERYKNSFIDGWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESAL 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 457 LTNDKIKDAAVIGKPDEEAGELPLAFVVKQANVQLTE---NEVIQFVNDN--ASPAKRlrgGVIFVDEIPKNPSGKILRR 531
Cdd:cd05969 359 MEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPSDelkEEIINFVRQKlgAHVAPR---EIEFVDNLPKTRSGKIMRR 435
|
...
gi 21355181 532 ILR 534
Cdd:cd05969 436 VLK 438
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
53-536 |
4.24e-47 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 172.70 E-value: 4.24e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 53 YSASFMhksivrlAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREVDHAINLSKPKIIFASK 132
Cdd:PRK12492 58 HSAAFA-------AYLQQHTDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVNTNPLYTAREMRHQFKDSGARALVYLN 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 133 ITIDRVAKV-------------------ASKNKFVKGIIalsgtsKKFKNIYDLKELMEDEKFKT-----QPDFTSPAAN 188
Cdd:PRK12492 131 MFGKLVQEVlpdtgieylieakmgdllpAAKGWLVNTVV------DKVKKMVPAYHLPQAVPFKQalrqgRGLSLKPVPV 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 189 KDEDVSLIVCSSGTTGLPKGVQLTQMNLLATL----------DSQIQPTVIPMEEVtLLTVIPWFH--AF--GCLTLITT 254
Cdd:PRK12492 205 GLDDIAVLQYTGGTTGLAKGAMLTHGNLVANMlqvraclsqlGPDGQPLMKEGQEV-MIAPLPLYHiyAFtaNCMCMMVS 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 255 ACVGArLVYLPKfEEKLFLSAIEKYRVMMAFMVPPLMVFLAKHPIVDKYDLSSLMVLLCGAAPLSRETEDQIKERIGVPf 334
Cdd:PRK12492 284 GNHNV-LITNPR-DIPGFIKELGKWRFSALLGLNTLFVALMDHPGFKDLDFSALKLTNSGGTALVKATAERWEQLTGCT- 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 335 IRQGYGLSEsTLSVLVQN--DEFCKPGSVGVLKVGIYAKVIDpDTGKLLGANERGELCFKGDGIMKGYIGDTKSTQTAI- 411
Cdd:PRK12492 361 IVEGYGLTE-TSPVASTNpyGELARLGTVGIPVPGTALKVID-DDGNELPLGERGELCIKGPQVMKGYWQQPEATAEALd 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 412 KDGWLHTGDIGYYDDDFEFFIVDRIKELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGELPLAFVVKQANvQL 491
Cdd:PRK12492 439 AEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVKLFVVARDP-GL 517
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 21355181 492 TENEVIQFVNDNASPAKRLRgGVIFVDEIPKNPSGKILRRILREM 536
Cdd:PRK12492 518 SVEELKAYCKENFTGYKVPK-HIVLRDSLPMTPVGKILRRELRDI 561
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
50-530 |
8.27e-47 |
|
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: 169.93 E-value: 8.27e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 50 GVEYSASFMHKSIVRLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREVDHAINLSKPKIIF 129
Cdd:cd05914 5 GEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 130 ASKitidrvakvasknkfvkgiialsgtskkfkniydlkelmedekfktqpdftspaankDEDVSLIVCSSGTTGLPKGV 209
Cdd:cd05914 85 VSD---------------------------------------------------------EDDVALINYTSGTTGNSKGV 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 210 QLTQMNLLATLDSQIQpTVIPMEEVTLLTVIPWFHAFGCL-TLITTACVGARLVYLPKFEEKLFLsAIEKYRVMMAFMVP 288
Cdd:cd05914 108 MLTYRNIVSNVDGVKE-VVLLGKGDKILSILPLHHIYPLTfTLLLPLLNGAHVVFLDKIPSAKII-ALAFAQVTPTLGVP 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 289 -PLMVF-LAKHPIVDKYDLSSLMVLL-----------------------------CGAAPLSRETEDQIKErIGVPFIrQ 337
Cdd:cd05914 186 vPLVIEkIFKMDIIPKLTLKKFKFKLakkinnrkirklafkkvheafggnikefvIGGAKINPDVEEFLRT-IGFPYT-I 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 338 GYGLSESTLSVLVQNDEFCKPGSVGVLKVGIYAKVIDPDTgkllgANERGELCFKGDGIMKGYIGDTKSTQTAI-KDGWL 416
Cdd:cd05914 264 GYGMTETAPIISYSPPNRIRLGSAGKVIDGVEVRIDSPDP-----ATGEGEIIVRGPNVMKGYYKNPEATAEAFdKDGWF 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 417 HTGDIGYYDDDFEFFIVDRIKELI-KYKGYQVPPAEIEALL------------LTNDKIKDAAVIGKPDEEAGELplafv 483
Cdd:cd05914 339 HTGDLGKIDAEGYLYIRGRKKEMIvLSSGKNIYPEEIEAKInnmpfvleslvvVQEKKLVALAYIDPDFLDVKAL----- 413
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 21355181 484 vKQANVQLT-ENEVIQFVNDNASPAKRLRGGVIFVDEIPKNPSGKILR 530
Cdd:cd05914 414 -KQRNIIDAiKWEVRDKVNQKVPNYKKISKVKIVKEEFEKTPKGKIKR 460
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
40-533 |
2.19e-45 |
|
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: 166.53 E-value: 2.19e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 40 DRTVLVDAVNGVEYSASFMHKSIVRLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREVDHA 119
Cdd:cd05923 16 DACAIADPARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 120 INLSKpkiIFASKITIDRVAKVASKNKFVKgIIALSgtskkfkniyDLKELMEDEKFKTQPDFTSPaanKDEDVSLIVCS 199
Cdd:cd05923 96 IERGE---MTAAVIAVDAQVMDAIFQSGVR-VLALS----------DLVGLGEPESAGPLIEDPPR---EPEQPAFVFYT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 200 SGTTGLPKGVQLTQmnllatldSQIQPTVIPMEEVT---------LLTVIPWFHAFGCLTLITTACVGARLVYLPK-FEE 269
Cdd:cd05923 159 SGTTGLPKGAVIPQ--------RAAESRVLFMSTQAglrhgrhnvVLGLMPLYHVIGFFAVLVAALALDGTYVVVEeFDP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 270 KLFLSAIEKYRVMMAFMVPPLMVFLAKHPIVDKYDLSSLMVLLCGAAPLSRETEDQIKERIGVPFIRQgYGLSESTLSVL 349
Cdd:cd05923 231 ADALKLIEQERVTSLFATPTHLDALAAAAEFAGLKLSSLRHVTFAGATMPDAVLERVNQHLPGEKVNI-YGTTEAMNSLY 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 350 VQNdefCKPGSVgvLKVGIYAKV----IDPDTGKLLGANERGELCFK--GDGIMKGYIGDTKSTQTAIKDGWLHTGDIGY 423
Cdd:cd05923 310 MRD---ARTGTE--MRPGFFSEVrivrIGGSPDEALANGEEGELIVAaaADAAFTGYLNQPEATAKKLQDGWYRTGDVGY 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 424 YDDDFEFFIVDRIKELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGELPLAFVVKQANvQLTENEVIQFVNDN 503
Cdd:cd05923 385 VDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREG-TLSADELDQFCRAS 463
|
490 500 510
....*....|....*....|....*....|.
gi 21355181 504 A-SPAKRLRGGViFVDEIPKNPSGKILRRIL 533
Cdd:cd05923 464 ElADFKRPRRYF-FLDELPKNAMNKVLRRQL 493
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
40-540 |
3.15e-45 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 167.15 E-value: 3.15e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 40 DRTVLVDAVNGVEYSASFMHKSIV----RLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDRE 115
Cdd:PRK13295 39 DKTAVTAVRLGTGAPRRFTYRELAalvdRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 116 VDHAINLSKPKIIFASKI--TIDRVAKVAsknkfvkgiiALSGTSKKFKNIY--------DLKELMEDEKFKTQPD---- 181
Cdd:PRK13295 119 LSFMLKHAESKVLVVPKTfrGFDHAAMAR----------RLRPELPALRHVVvvggdgadSFEALLITPAWEQEPDapai 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 182 FTSPAANKDeDVSLIVCSSGTTGLPKGVqltqMNLLATLDSQIQPTVIPM----EEVTLLTViPWFHAFGCLT-LITTAC 256
Cdd:PRK13295 189 LARLRPGPD-DVTQLIYTSGTTGEPKGV----MHTANTLMANIVPYAERLglgaDDVILMAS-PMAHQTGFMYgLMMPVM 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 257 VGARLVYLPKFEEKLFLSAIEKYRVMMAFMVPPLMVFLAKHPIVDKYDLSSLMVLLCGAAPLSRETEDQIKERIGVPfIR 336
Cdd:PRK13295 263 LGATAVLQDIWDPARAAELIRTEGVTFTMASTPFLTDLTRAVKESGRPVSSLRTFLCAGAPIPGALVERARAALGAK-IV 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 337 QGYGLSES---TLSVLVQNDEFCKpGSVGVLKVGIYAKVIDPDtGKLLGANERGELCFKGDGIMKGYIGDTKSTQTAiKD 413
Cdd:PRK13295 342 SAWGMTENgavTLTKLDDPDERAS-TTDGCPLPGVEVRVVDAD-GAPLPAGQIGRLQVRGCSNFGGYLKRPQLNGTD-AD 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 414 GWLHTGDIGYYDDDFEFFIVDRIKELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGELPLAFVVKQANVQLTE 493
Cdd:PRK13295 419 GWFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPRPGQSLDF 498
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 21355181 494 NEVIQFVnDNASPAK-----RLrggvIFVDEIPKNPSGKILRRILREMLKKQ 540
Cdd:PRK13295 499 EEMVEFL-KAQKVAKqyipeRL----VVRDALPRTPSGKIQKFRLREMLRGE 545
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
64-534 |
1.47e-44 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 163.77 E-value: 1.47e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 64 RLAYILQKLGVKQNDVVGLSSENSVNFALAMF----AGLAVGATVAPLNVTYSDREVDHAINLSKPKIIFASKITIDRVA 139
Cdd:cd05922 5 AAASALLEAGGVRGERVVLILPNRFTYIELSFavayAGGRLGLVFVPLNPTLKESVLRYLVADAGGRIVLADAGAADRLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 140 KVAsknkfvkgiIALSGTSKkfknIYDLKELMEDEkfktqpDFTSPAANKDEDVSLIVCSSGTTGLPKGVQLTQMNLLAT 219
Cdd:cd05922 85 DAL---------PASPDPGT----VLDADGIRAAR------ASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLAN 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 220 LDSQIQPTVIPMEEVtLLTVIPWFHAFGCLTLITTACVGARLVYLPKFE-EKLFLSAIEKYRVMMAFMVPPLMVFLAKhP 298
Cdd:cd05922 146 ARSIAEYLGITADDR-ALTVLPLSYDYGLSVLNTHLLRGATLVLTNDGVlDDAFWEDLREHGATGLAGVPSTYAMLTR-L 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 299 IVDKYDLSSLMVLLCGAAPLSRETEDQIKERIGVPFIRQGYGLSEST--LSVLVQNDEFCKPGSVGVLKVGIYAKVIDPD 376
Cdd:cd05922 224 GFDPAKLPSLRYLTQAGGRLPQETIARLRELLPGAQVYVMYGQTEATrrMTYLPPERILEKPGSIGLAIPGGEFEILDDD 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 377 tGKLLGANERGELCFKGDGIMKGY----IGDTKSTQTAikdGWLHTGDIGYYDDDFEFFIVDRIKELIKYKGYQVPPAEI 452
Cdd:cd05922 304 -GTPTPPGEPGEIVHRGPNVMKGYwndpPYRRKEGRGG---GVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEI 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 453 EALLLTNDKIKDAAVIGKPDeEAGELPLAFVVkqANVQLTENEVIQFVNDNASPAKrLRGGVIFVDEIPKNPSGKILRRI 532
Cdd:cd05922 380 EAAARSIGLIIEAAAVGLPD-PLGEKLALFVT--APDKIDPKDVLRSLAERLPPYK-VPATVRVVDELPLTASGKVDYAA 455
|
..
gi 21355181 533 LR 534
Cdd:cd05922 456 LR 457
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
192-530 |
1.59e-43 |
|
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: 157.43 E-value: 1.59e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 192 DVSLIVCSSGTTGLPKGVQLTQMNLLATlDSQIQPTVIPMEEVTLLTVIPWFHAFGCLTLITTACVGARLVYLPKFEEKL 271
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLIAA-NLQLIHAMGLTEADVYLNMLPLFHIAGLNLALATFHAGGANVVMEKFDPAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 272 FLSAIEKYRVMMAFMVPPLMVFLAKHPIVDKYDLSSLMVLLCGAAPlsrETEDQIKERIGVPFIrQGYGLSE-STLSVLV 350
Cdd:cd17637 80 ALELIEEEKVTLMGSFPPILSNLLDAAEKSGVDLSSLRHVLGLDAP---ETIQRFEETTGATFW-SLYGQTEtSGLVTLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 351 QNDEfcKPGSVGvlKVGIYAKV-IDPDTGKLLGANERGELCFKGDGIMKGYIGDTKSTQTAIKDGWLHTGDIGYYDDDFE 429
Cdd:cd17637 156 PYRE--RPGSAG--RPGPLVRVrIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTFRNGWHHTGDLGRFDEDGY 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 430 FFIVDRI--KELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGELPLAFVVKQANVQLTENEVIQFVNDNASPA 507
Cdd:cd17637 232 LWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKPGATLTADELIEFVGSRIARY 311
|
330 340
....*....|....*....|...
gi 21355181 508 KRLRgGVIFVDEIPKNPSGKILR 530
Cdd:cd17637 312 KKPR-YVVFVEALPKTADGSIDR 333
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
180-534 |
2.44e-43 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 160.54 E-value: 2.44e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 180 PDFTSPAankdedvsLIVCSSGTTGLPKGVQLTQMNLLATLDS-----QIQPtvipmeEVTLLTVIPWFHAFG-CLTLIT 253
Cdd:PRK07787 125 PDPDAPA--------LIVYTSGTTGPPKGVVLSRRAIAADLDAlaeawQWTA------DDVLVHGLPLFHVHGlVLGVLG 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 254 TACVGARLVYLPKFEEKLFLSAIEKyRVMMAFMVPPLMVFLAKHPIVDKYdLSSLMVLLCGAAPLSRETEDQIKERIGVP 333
Cdd:PRK07787 191 PLRIGNRFVHTGRPTPEAYAQALSE-GGTLYFGVPTVWSRIAADPEAARA-LRGARLLVSGSAALPVPVFDRLAALTGHR 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 334 FIRQgYGLSES--TLSVLVQNDEfcKPGSVGVLKVGIYAKVIDpDTGKLLGAN--ERGELCFKGDGIMKGYIGDTKSTQT 409
Cdd:PRK07787 269 PVER-YGMTETliTLSTRADGER--RPGWVGLPLAGVETRLVD-EDGGPVPHDgeTVGELQVRGPTLFDGYLNRPDATAA 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 410 AI-KDGWLHTGDIGYYDDDFEFFIVDRIK-ELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGELPLAFVVKQA 487
Cdd:PRK07787 345 AFtADGWFRTGDVAVVDPDGMHRIVGREStDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVGAD 424
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 21355181 488 NVqlTENEVIQFVNDNASPAKRLRgGVIFVDEIPKNPSGKILRRILR 534
Cdd:PRK07787 425 DV--AADELIDFVAQQLSVHKRPR-EVRFVDALPRNAMGKVLKKQLL 468
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
23-535 |
3.19e-43 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 161.46 E-value: 3.19e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 23 DSRSLGQYILDKYKSFGDRTVLVDavNGVEYSASFMHKSIVRLAYILQKLGVKQNDVVGLSSENSVNFaLAMFAGLA-VG 101
Cdd:PRK06155 19 SERTLPAMLARQAERYPDRPLLVF--GGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEF-LDVFLGCAwLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 102 ATVAPLNVTYSDREVDHAINLSKPKIIFASKITIDRVAKVASKNKFVKGIIALSGTSkkfkniydlkELMEDEKFKTQP- 180
Cdd:PRK06155 96 AIAVPINTALRGPQLEHILRNSGARLLVVEAALLAALEAADPGDLPLPAVWLLDAPA----------SVSVPAGWSTAPl 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 181 ---DFTSPAAN-KDEDVSLIVCSSGTTGLPKGVQLTQMNL-----LATLDSQIQPtvipmEEVtLLTVIPWFHAFGCLTL 251
Cdd:PRK06155 166 pplDAPAPAAAvQPGDTAAILYTSGTTGPSKGVCCPHAQFywwgrNSAEDLEIGA-----DDV-LYTTLPLFHTNALNAF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 252 ITTACVGARLVYLPKFEEKLFLSAIEKYRVMMAFMVPPLMVFLAKHPIVDKYDLSSLMVLLCGAAPLsrETEDQIKERIG 331
Cdd:PRK06155 240 FQALLAGATYVLEPRFSASGFWPAVRRHGATVTYLLGAMVSILLSQPARESDRAHRVRVALGPGVPA--ALHAAFRERFG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 332 VPfIRQGYGLSESTLSVLVQNDEfCKPGSVGVLKVGIYAKVIDPDtGKLLGANERGELCFKGD---GIMKGYIGDTKSTQ 408
Cdd:PRK06155 318 VD-LLDGYGSTETNFVIAVTHGS-QRPGSMGRLAPGFEARVVDEH-DQELPDGEPGELLLRADepfAFATGYFGMPEKTV 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 409 TAIKDGWLHTGDIGYYDDDFEFFIVDRIKELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGELPLAFVVKQAN 488
Cdd:PRK06155 395 EAWRNLWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDG 474
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 21355181 489 VQLTENEVIQFVNDN----ASPakRLrggVIFVDEIPKNPSGKILRRILRE 535
Cdd:PRK06155 475 TALEPVALVRHCEPRlayfAVP--RY---VEFVAALPKTENGKVQKFVLRE 520
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
64-531 |
8.05e-43 |
|
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: 158.46 E-value: 8.05e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 64 RLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREVDHAINLSKPKIIFaskitidrvakvas 143
Cdd:cd05930 24 RLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYILEDSGAKLVL-------------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 144 knkfvkgiialsgtskkfkniydlkelmedekfkTQPDftspaankdeDVSLIVCSSGTTGLPKGVQLTQMNLLATLDSQ 223
Cdd:cd05930 90 ----------------------------------TDPD----------DLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWM 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 224 IQPTVIPMEEVTLLTVIPWFHAFGCLTLiTTACVGARLVYLPKFEEKL---FLSAIEKYRVMMAFMVPPLMVFLAKHPIV 300
Cdd:cd05930 126 QEAYPLTPGDRVLQFTSFSFDVSVWEIF-GALLAGATLVVLPEEVRKDpeaLADLLAEEGITVLHLTPSLLRLLLQELEL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 301 DkyDLSSLMVLLCGAAPLSRETEDQIKERIGVPFIRQGYGLSESTLSVLVQNdefCKPGSVGVLKVGI-------YAKVI 373
Cdd:cd05930 205 A--ALPSLRLVLVGGEALPPDLVRRWRELLPGARLVNLYGPTEATVDATYYR---VPPDDEEDGRVPIgrpipntRVYVL 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 374 DPDtGKLLGANERGELCFKGDGIMKGYIGDTKSTQTAI------KDGWLH-TGDIGYYDDD--FEFFivDRIKELIKYKG 444
Cdd:cd05930 280 DEN-LRPVPPGVPGELYIGGAGLARGYLNRPELTAERFvpnpfgPGERMYrTGDLVRWLPDgnLEFL--GRIDDQVKIRG 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 445 YQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGELPLAFVVKQANVQLTENEVIQFVNDNAS----PAKrlrggVIFVDEI 520
Cdd:cd05930 357 YRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEGGELDEEELRAHLAERLPdymvPSA-----FVVLDAL 431
|
490
....*....|.
gi 21355181 521 PKNPSGKILRR 531
Cdd:cd05930 432 PLTPNGKVDRK 442
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
39-544 |
4.09e-42 |
|
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: 159.79 E-value: 4.09e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 39 GDRTVL--VDAVNGVEYSASF--MHKSIVRLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDR 114
Cdd:cd05967 65 GDQIALiyDSPVTGTERTYTYaeLLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGFAAK 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 115 EVDHAINLSKPKIIFASKITIdRVAKVASKNKFVKGIIALSGTSKKFKNIYDlKELMEDEKFKTQPDF-----------T 183
Cdd:cd05967 145 ELASRIDDAKPKLIVTASCGI-EPGKVVPYKPLLDKALELSGHKPHHVLVLN-RPQVPADLTKPGRDLdwsellakaepV 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 184 SPAANKDEDVSLIVCSSGTTGLPKGVQLTQMNLLATLDSQIQpTV--IPMEEVtlltvipWF----------HAFGCLTL 251
Cdd:cd05967 223 DCVPVAATDPLYILYTSGTTGKPKGVVRDNGGHAVALNWSMR-NIygIKPGDV-------WWaasdvgwvvgHSYIVYGP 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 252 IttaCVGARLVYlpkFEEK--------LFLSAIEKYRVMMAFMVPPLMVFLAKHP----IVDKYDLSSLMVLLCGAAPLS 319
Cdd:cd05967 295 L---LHGATTVL---YEGKpvgtpdpgAFWRVIEKYQVNALFTAPTAIRAIRKEDpdgkYIKKYDLSSLRTLFLAGERLD 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 320 RETEDQIKERIGVPFIRQgYGLSES----TLSVLVQNDEFCKPGSVGVLKVGIYAKVIDpDTGKLLGANERGELCFKGD- 394
Cdd:cd05967 369 PPTLEWAENTLGVPVIDH-WWQTETgwpiTANPVGLEPLPIKAGSPGKPVPGYQVQVLD-EDGEPVGPNELGNIVIKLPl 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 395 --GIMKGYIGDT---KSTQTAIKDGWLHTGDIGYYDDDFEFFIVDRIKELIKYKGYQVPPAEIEALLLTNDKIKDAAVIG 469
Cdd:cd05967 447 ppGCLLTLWKNDerfKKLYLSKFPGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVG 526
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21355181 470 KPDEEAGELPLAFVVKQANVQLT----ENEVIQFVNDNASPAKRLRgGVIFVDEIPKNPSGKILRRILREMLKKQKSKL 544
Cdd:cd05967 527 VRDELKGQVPLGLVVLKEGVKITaeelEKELVALVREQIGPVAAFR-LVIFVKRLPKTRSGKILRRTLRKIADGEDYTI 604
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
40-535 |
4.31e-42 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 158.38 E-value: 4.31e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 40 DRTVLVDAVNGVEYSAsfMHKSIVRLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREVDHA 119
Cdd:PRK13382 58 DRPGLIDELGTLTWRE--LDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPALAEV 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 120 INLSKPKIIFASKITIDRVAKVASKNKFVKGIIALSGTSKKFkniydLKELMEDEKFKTQPdftsPAANKDEDVslIVCS 199
Cdd:PRK13382 136 VTREGVDTVIYDEEFSATVDRALADCPQATRIVAWTDEDHDL-----TVEVLIAAHAGQRP----EPTGRKGRV--ILLT 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 200 SGTTGLPKGVQLTQMNLLATLDSQIQPTVIPMEEVTLLtVIPWFHAFGCLTLITTACVGARLVYLPKFEEKLFLSAIEKY 279
Cdd:PRK13382 205 SGTTGTPKGARRSGPGGIGTLKAILDRTPWRAEEPTVI-VAPMFHAWGFSQLVLAASLACTIVTRRRFDPEATLDLIDRH 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 280 RVMMAFMVPPLMVFLAKHP--IVDKYDLSSLMVLLCGAAPLSRETEDQIKERIGvPFIRQGYGLSESTLSVLVQNDEFCK 357
Cdd:PRK13382 284 RATGLAVVPVMFDRIMDLPaeVRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFG-DVIYNNYNATEAGMIATATPADLRA 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 358 -PGSVGVLKVGIYAKVIDPDtGKLLGANERGELCFKGDGIMKGYigdTKSTQTAIKDGWLHTGDIGYYDDDFEFFIVDRI 436
Cdd:PRK13382 363 aPDTAGRPAEGTEIRILDQD-FREVPTGEVGTIFVRNDTQFDGY---TSGSTKDFHDGFMASGDVGYLDENGRLFVVGRD 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 437 KELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGELPLAFVVKQANVQLTENEVIQFVNDNASPAKRLRGGVIf 516
Cdd:PRK13382 439 DEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPGASATPETLKQHVRDNLANYKVPRDIVV- 517
|
490
....*....|....*....
gi 21355181 517 VDEIPKNPSGKILRRILRE 535
Cdd:PRK13382 518 LDELPRGATGKILRRELQA 536
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
40-534 |
1.77e-41 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 155.94 E-value: 1.77e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 40 DRTVLVDAVNGVEYSASFMHKSIVRLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREVDHA 119
Cdd:PRK13390 12 DRPAVIVAETGEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 120 INLSKPKIIFASKiTIDRVAKVASKNKFVKgiIALSGTSKKFKNiydlkelmedekFKTQPDFTSPAANKDEDVSLIVCS 199
Cdd:PRK13390 92 VGDSGARVLVASA-ALDGLAAKVGADLPLR--LSFGGEIDGFGS------------FEAALAGAGPRLTEQPCGAVMLYS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 200 SGTTGLPKGVQ--LTQMNLlatlDSQIQPTV--------IPMEEVtLLTVIPWFHAFGCLTLITTACVGARLVYLPKFEE 269
Cdd:PRK13390 157 SGTTGFPKGIQpdLPGRDV----DAPGDPIVaiarafydISESDI-YYSSAPIYHAAPLRWCSMVHALGGTVVLAKRFDA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 270 KLFLSAIEKYRVMMAFMVPPLMVFLAK--HPIVDKYDLSSLMVLLCGAAPLSRETEDQIKERIGvPFIRQGYGLSES-TL 346
Cdd:PRK13390 232 QATLGHVERYRITVTQMVPTMFVRLLKldADVRTRYDVSSLRAVIHAAAPCPVDVKHAMIDWLG-PIVYEYYSSTEAhGM 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 347 SVLVQNDEFCKPGSVGVLKVGIYAkvIDPDTGKLLGANERGELCFKGDGIMKGYIGDTKSTQTAIKDG---WLHTGDIGY 423
Cdd:PRK13390 311 TFIDSPDWLAHPGSVGRSVLGDLH--ICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAAAQHPAhpfWTTVGDLGS 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 424 YDDDFEFFIVDRIKELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGELPLAFVVKQANVQLTEN---EVIQFV 500
Cdd:PRK13390 389 VDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLVEGIRGSDElarELIDYT 468
|
490 500 510
....*....|....*....|....*....|....
gi 21355181 501 NDNASPAKRLRgGVIFVDEIPKNPSGKILRRILR 534
Cdd:PRK13390 469 RSRIAHYKAPR-SVEFVDELPRTPTGKLVKGLLR 501
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
64-536 |
8.89e-40 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 151.82 E-value: 8.89e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 64 RLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREVDHAINLSKPK--IIFASKITIDRVAKV 141
Cdd:PRK06164 47 RLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRARwlVVWPGFKGIDFAAIL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 142 ASKNKFV----KGIIALSGTSKkfkNIYDLKELMEDEKFKTQPDFTSPAANKDEDV----SLIVCSSGTTGLPKGVQLTQ 213
Cdd:PRK06164 127 AAVPPDAlpplRAIAVVDDAAD---ATPAPAPGARVQLFALPDPAPPAAAGERAADpdagALLFTTSGTTSGPKLVLHRQ 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 214 MNLLATLDSQIQPTVIPMEEVTLLtVIPWFHAFGCLTLITTACVGARLVYLPKFEEKLFLSAIEKYRVMMAFMVPPLMVF 293
Cdd:PRK06164 204 ATLLRHARAIARAYGYDPGAVLLA-ALPFCGVFGFSTLLGALAGGAPLVCEPVFDAARTARALRRHRVTHTFGNDEMLRR 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 294 LAKHPIVDKyDLSSLMVLLCGA-APLSRETEDQIKERiGVPfIRQGYGLSEstLSVLVQNDEFCKPGSVGVLKVGIYA-- 370
Cdd:PRK06164 283 ILDTAGERA-DFPSARLFGFASfAPALGELAALARAR-GVP-LTGLYGSSE--VQALVALQPATDPVSVRIEGGGRPAsp 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 371 ----KVIDPDTGKLLGANERGELCFKGDGIMKGYIGDTKSTQTAIK-DGWLHTGDIGYYDDDFEFFIVDRIKELIKYKGY 445
Cdd:PRK06164 358 earvRARDPQDGALLPDGESGEIEIRAPSLMRGYLDNPDATARALTdDGYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGF 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 446 QVPPAEIEALLLTNDKIKDAAVIGKpDEEAGELPLAFVVKQANVQLTENEVIQFVNDNASPAKrLRGGVIFVDEIPKNPS 525
Cdd:PRK06164 438 LVNPAEIEHALEALPGVAAAQVVGA-TRDGKTVPVAFVIPTDGASPDEAGLMAACREALAGFK-VPARVQVVEAFPVTES 515
|
490
....*....|....
gi 21355181 526 G---KILRRILREM 536
Cdd:PRK06164 516 AngaKIQKHRLREM 529
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
59-534 |
1.29e-39 |
|
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: 149.50 E-value: 1.29e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 59 HKSiVRLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREVDHAINLSKPKIIfaskitidrv 138
Cdd:cd05971 14 TAS-NRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASAL---------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 139 akvasknkfvkgiialsgtskkfknIYDLKElmedekfktqpdftspaankdeDVSLIVCSSGTTGLPKGVQLTQMNLLA 218
Cdd:cd05971 83 -------------------------VTDGSD----------------------DPALIIYTSGTTGPPKGALHAHRVLLG 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 219 TLDS-QIQPTVIPMEEVTLLTVIPWfhafgcltlittACVGARL-VYLP--------------KFEEKLFLSAIEKYRVM 282
Cdd:cd05971 116 HLPGvQFPFNLFPRDGDLYWTPADW------------AWIGGLLdVLLPslyfgvpvlahrmtKFDPKAALDLMSRYGVT 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 283 MAFMVPPLMVFLAKHPIVDKYDLSSLMVLLCGAAPLSRETEDQIKERIGVPfIRQGYGLSESTLSVLVQNDEF-CKPGSV 361
Cdd:cd05971 184 TAFLPPTALKMMRQQGEQLKHAQVKLRAIATGGESLGEELLGWAREQFGVE-VNEFYGQTECNLVIGNCSALFpIKPGSM 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 362 GVLKVGIYAKVIDpDTGKLLGANERGELCFKGDG--IMKGYIGDTKSTQTAIKDGWLHTGDIGYYDDDFEFFIVDRIKEL 439
Cdd:cd05971 263 GKPIPGHRVAIVD-DNGTPLPPGEVGEIAVELPDpvAFLGYWNNPSATEKKMAGDWLLTGDLGRKDSDGYFWYVGRDDDV 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 440 IKYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGELPLAFVVKQANVQLTE---NEVIQFVNDNASPAKRLRgGVIF 516
Cdd:cd05971 342 ITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGETPSDalaREIQELVKTRLAAHEYPR-EIEF 420
|
490
....*....|....*...
gi 21355181 517 VDEIPKNPSGKILRRILR 534
Cdd:cd05971 421 VNELPRTATGKIRRRELR 438
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
199-530 |
5.66e-39 |
|
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: 144.86 E-value: 5.66e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 199 SSGTTGLPKGVQLTQMNLLATLDSQIQPTVIPMEEvTLLTVIPWFHAFGCLTLITTACVGARLVYLPKFEEKLFLSAIEK 278
Cdd:cd17633 8 TSGTTGLPKAYYRSERSWIESFVCNEDLFNISGED-AILAPGPLSHSLFLYGAISALYLGGTFIGQRKFNPKSWIRKINQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 279 YRVMMAFMVPPLMVFLAKHPIVDkydlSSLMVLLCGAAPLSRETEDQIKERIGVPFIRQGYGLSESTLSVLVQNDEFCKP 358
Cdd:cd17633 87 YNATVIYLVPTMLQALARTLEPE----SKIKSIFSSGQKLFESTKKKLKNIFPKANLIEFYGTSELSFITYNFNQESRPP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 359 GSVGVLKVGIYAKVIDPDTGKLlganerGELCFKGDGIMKGYIGDTKSTqtaiKDGWLHTGDIGYYDDDFEFFIVDRIKE 438
Cdd:cd17633 163 NSVGRPFPNVEIEIRNADGGEI------GKIFVKSEMVFSGYVRGGFSN----PDGWMSVGDIGYVDEEGYLYLVGRESD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 439 LIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGELPLAFVVKQanvQLTENEVIQFVNDNASPAKRLRgGVIFVD 518
Cdd:cd17633 233 MIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYSGD---KLTYKQLKRFLKQKLSRYEIPK-KIIFVD 308
|
330
....*....|..
gi 21355181 519 EIPKNPSGKILR 530
Cdd:cd17633 309 SLPYTSSGKIAR 320
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
75-542 |
1.25e-38 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 147.62 E-value: 1.25e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 75 KQNDVVGLSSENSVNFaLAMFAGLA-VGATVAPLNVTYSDREVDHAINLSKPKIIFASKITIDRvakvasknkfvkgiia 153
Cdd:PRK07638 48 SKNKTIAILLENRIEF-LQLFAGAAmAGWTCVPLDIKWKQDELKERLAISNADMIVTERYKLND---------------- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 154 LSGTSKKFKNIYDLKELMEDEKfktqPDFtSPAANKDEDVSLIVCSSGTTGLPKGVQLTQMNLLATLDSQIQPTVIPMEE 233
Cdd:PRK07638 111 LPDEEGRVIEIDEWKRMIEKYL----PTY-APIENVQNAPFYMGFTSGSTGKPKAFLRAQQSWLHSFDCNVHDFHMKRED 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 234 VTLltvIP--WFHAFGCLTLITTACVGARLVYLPKFEEKLFLSAIEKYRVMMAFMVPPLMVFLAKhpiVDKYDLSSLMVL 311
Cdd:PRK07638 186 SVL---IAgtLVHSLFLYGAISTLYVGQTVHLMRKFIPNQVLDKLETENISVMYTVPTMLESLYK---ENRVIENKMKII 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 312 LCGAApLSRETEDQIKERIgvPFIR--QGYGLSE-STLSVLVQNDEFCKPGSVGVLKVGIYAKVIDPDtGKLLGANERGE 388
Cdd:PRK07638 260 SSGAK-WEAEAKEKIKNIF--PYAKlyEFYGASElSFVTALVDEESERRPNSVGRPFHNVQVRICNEA-GEEVQKGEIGT 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 389 LCFKGDGIMKGYIGDTKSTQTAIKDGWLHTGDIGYYDDDFEFFIVDRIKELIKYKGYQVPPAEIEALLLTNDKIKDAAVI 468
Cdd:PRK07638 336 VYVKSPQFFMGYIIGGVLARELNADGWMTVRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVI 415
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21355181 469 GKPDEEAGELPLAFVVKQANVQltenEVIQFVNDNASPAKRLRGGViFVDEIPKNPSGKILRRILREMLKKQKS 542
Cdd:PRK07638 416 GVPDSYWGEKPVAIIKGSATKQ----QLKSFCLQRLSSFKIPKEWH-FVDEIPYTNSGKIARMEAKSWIENQEK 484
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
59-535 |
1.49e-38 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 148.50 E-value: 1.49e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 59 HKSIVR----LAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREvdhaiNLSKPKIIFASKIT 134
Cdd:PRK05852 46 YRDLARlvddLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAE-----QRVRSQAAGARVVL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 135 IDRVAKVASKNKFVKGI-IALSGTSKKFKNIYDLkELMEDEKFKTQPDFTSPAANKDEDvSLIVCSSGTTGLPKGVQLTQ 213
Cdd:PRK05852 121 IDADGPHDRAEPTTRWWpLTVNVGGDSGPSGGTL-SVHLDAATEPTPATSTPEGLRPDD-AMIMFTGGTTGLPKMVPWTH 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 214 MNLLATLDSQIQPTVIPMEEVTLlTVIPWFHAFGCLTLITTACVGARLVYLP---KFEEKLFLSAIEKYRVMMAFMVPPL 290
Cdd:PRK05852 199 ANIASSVRAIITGYRLSPRDATV-AVMPLYHGHGLIAALLATLASGGAVLLPargRFSAHTFWDDIKAVGATWYTAVPTI 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 291 MVFLAKHPIVDKYDL--SSLMVLLCGAAPLSRETEDQIKERIGVPFIrQGYGLSESTLSVLVQN--------DEFCKPGS 360
Cdd:PRK05852 278 HQILLERAATEPSGRkpAALRFIRSCSAPLTAETAQALQTEFAAPVV-CAFGMTEATHQVTTTQiegigqteNPVVSTGL 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 361 VGvLKVGIYAKVIDPDtGKLLGANERGELCFKGDGIMKGYIGDTKSTQTAIKDGWLHTGDIGYYDDDFEFFIVDRIKELI 440
Cdd:PRK05852 357 VG-RSTGAQIRIVGSD-GLPLPAGAVGEVWLRGTTVVRGYLGDPTITAANFTDGWLRTGDLGSLSAAGDLSIRGRIKELI 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 441 KYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGELPLAFVVKQANVQLTENEVIQFVNDNASPAK---RLRggviFV 517
Cdd:PRK05852 435 NRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIVPRESAPPTAEELVQFCRERLAAFEipaSFQ----EA 510
|
490
....*....|....*...
gi 21355181 518 DEIPKNPSGKILRRILRE 535
Cdd:PRK05852 511 SGLPHTAKGSLDRRAVAE 528
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
192-537 |
7.47e-38 |
|
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: 142.08 E-value: 7.47e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 192 DVSLIVCSSGTTGLPKGVQLTQMNLLATLDSQIQPTVIPMEEVTLLTViPWFHAFGCLTLITTACVGARLVYLPKfeEKL 271
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSL-PLYHVGGLAILVRSLLAGAELVLLER--NQA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 272 FLSAIEKYRVMMAFMVPP-LMVFLAKHPIVDkyDLSSLMVLLCGAAPLSRETEDQIKERiGVPfIRQGYGLSE--STLSV 348
Cdd:cd17630 78 LAEDLAPPGVTHVSLVPTqLQRLLDSGQGPA--ALKSLRAVLLGGAPIPPELLERAADR-GIP-LYTTYGMTEtaSQVAT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 349 LVQNDEfcKPGSVGVLKVGIYAKVIDpdtgkllganeRGELCFKGDGIMKGYIgDTKSTQTAIKDGWLHTGDIGYYDDDF 428
Cdd:cd17630 154 KRPDGF--GRGGVGVLLPGRELRIVE-----------DGEIWVGGASLAMGYL-RGQLVPEFNEDGWFTTKDLGELHADG 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 429 EFFIVDRIKELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGELPLAFVVkqANVQLTENEVIQFVNDNASPAK 508
Cdd:cd17630 220 RLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIV--GRGPADPAELRAWLKDKLARFK 297
|
330 340
....*....|....*....|....*....
gi 21355181 509 RLRgGVIFVDEIPKNPSGKILRRILREML 537
Cdd:cd17630 298 LPK-RIYPVPELPRTGGGKVDRRALRAWL 325
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
64-535 |
5.62e-37 |
|
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: 143.76 E-value: 5.62e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 64 RLAYIL-QKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREVDHAINLSKPKIIFASKITIDRVAKVA 142
Cdd:cd05928 53 KAANVLsGACGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSDELAPEVDSVA 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 143 SKNKFVKGIIALSGTSKKfkNIYDLKELMedekfKTQPDFTSPAANKDEDVSLIVCSSGTTGLPKGVQLTQMNLL--ATL 220
Cdd:cd05928 133 SECPSLKTKLLVSEKSRD--GWLNFKELL-----NEASTEHHCVETGSQEPMAIYFTSGTTGSPKMAEHSHSSLGlgLKV 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 221 DSQIQPTVIPMEEVTLLTVIPWFHAFGCLTL---ITTACVGARLvyLPKFEEKLFLSAIEKYRVMmAFMVPPLMVFLAKH 297
Cdd:cd05928 206 NGRYWLDLTASDIMWNTSDTGWIKSAWSSLFepwIQGACVFVHH--LPRFDPLVILKTLSSYPIT-TFCGAPTVYRMLVQ 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 298 PIVDKYDLSSLMVLLCGAAPLSRETEDQIKERIGVPfIRQGYGLSESTLSVLVQNDEFCKPGSVGVLKVGIYAKVIDpDT 377
Cdd:cd05928 283 QDLSSYKFPSLQHCVTGGEPLNPEVLEKWKAQTGLD-IYEGYGQTETGLICANFKGMKIKPGSMGKASPPYDVQIID-DN 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 378 GKLLGANERGELCF-----KGDGIMKGYIGDTKSTQTAIKDGWLHTGDIGYYDDDFEFFIVDRIKELIKYKGYQVPPAEI 452
Cdd:cd05928 361 GNVLPPGTEGDIGIrvkpiRPFGLFSGYVDNPEKTAATIRGDFYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEV 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 453 EALLLTNDKIKDAAVIGKPDEEAGELPLAFVVKQANV------QLTEnEVIQFVNDNASPAKRLRgGVIFVDEIPKNPSG 526
Cdd:cd05928 441 ESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLAPQFlshdpeQLTK-ELQQHVKSVTAPYKYPR-KVEFVQELPKTVTG 518
|
....*....
gi 21355181 527 KILRRILRE 535
Cdd:cd05928 519 KIQRNELRD 527
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
62-495 |
8.73e-37 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 143.79 E-value: 8.73e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 62 IVRLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREVDHAINLSKPKII--------FASKI 133
Cdd:PLN02860 42 VLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWSFEEAKSAMLLVRPVMLvtdetcssWYEEL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 134 TIDRVAKVasknkfvKGIIALSGTSKKFKNiyDLKELMEDEKFKtQPDFTSPAAN---KDEDVSLIVCSSGTTGLPKGVQ 210
Cdd:PLN02860 122 QNDRLPSL-------MWQVFLESPSSSVFI--FLNSFLTTEMLK-QRALGTTELDyawAPDDAVLICFTSGTTGRPKGVT 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 211 LTQMNLLATLDSQIQPTVIPMEEVTLLTViPWFHAFGCLTLITTACVGARLVYLPKFEEKLFLSAIEKYRVMMAFMVPPL 290
Cdd:PLN02860 192 ISHSALIVQSLAKIAIVGYGEDDVYLHTA-PLCHIGGLSSALAMLMVGACHVLLPKFDAKAALQAIKQHNVTSMITVPAM 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 291 M---VFLAKHPIVDKyDLSSLMVLLCGAAPLSRETEDQIKERIGVPFIRQGYGLSE--STLSVLVQNDEFCKPGSVGVLK 365
Cdd:PLN02860 271 MadlISLTRKSMTWK-VFPSVRKILNGGGSLSSRLLPDAKKLFPNAKLFSAYGMTEacSSLTFMTLHDPTLESPKQTLQT 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 366 VG-IYAKVIDPDTG--------------KLLGANERGELCFKGDGIMKGYIGDTKSTQTAI-KDGWLHTGDIGYYDDDFE 429
Cdd:PLN02860 350 VNqTKSSSVHQPQGvcvgkpaphvelkiGLDESSRVGRILTRGPHVMLGYWGQNSETASVLsNDGWLDTGDIGWIDKAGN 429
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21355181 430 FFIVDRIKELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGELPLAFVVKQANVQLTENE 495
Cdd:PLN02860 430 LWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEMVVACVRLRDGWIWSDNE 495
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
64-538 |
1.97e-36 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 142.85 E-value: 1.97e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 64 RLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREVDHAINLSKPKIIFASKITIDRVAKV-- 141
Cdd:PLN03102 51 RLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFVDRSFEPLAREVlh 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 142 ------ASKNKFVKGIIALSGTSKKFKNIYDLKELMEdekfKTQPDFTSPAA-----NKDEDVSLIVcSSGTTGLPKGVQ 210
Cdd:PLN03102 131 llssedSNLNLPVIFIHEIDFPKRPSSEELDYECLIQ----RGEPTPSLVARmfriqDEHDPISLNY-TSGTTADPKGVV 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 211 LT-QMNLLATLDSQI--QPTVIPMeevtLLTVIPWFHAFGCLTLITTACVGARLVYLPKFEEKLFLSAIEKYRVMMAFMV 287
Cdd:PLN03102 206 IShRGAYLSTLSAIIgwEMGTCPV----YLWTLPMFHCNGWTFTWGTAARGGTSVCMRHVTAPEIYKNIEMHNVTHMCCV 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 288 PPLMVFLAKHPIVDKYDLSSLMVLLCGAAPLSRETEDQIkERIGVPfIRQGYGLSESTLSVLV--QNDEFCK-------- 357
Cdd:PLN03102 282 PTVFNILLKGNSLDLSPRSGPVHVLTGGSPPPAALVKKV-QRLGFQ-VMHAYGLTEATGPVLFceWQDEWNRlpenqqme 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 358 -PGSVGVLKVGIYAkvIDPDTGKLLGANER-----GELCFKGDGIMKGYIGDTKSTQTAIKDGWLHTGDIGYYDDDFEFF 431
Cdd:PLN03102 360 lKARQGVSILGLAD--VDVKNKETQESVPRdgktmGEIVIKGSSIMKGYLKNPKATSEAFKHGWLNTGDVGVIHPDGHVE 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 432 IVDRIKELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGELPLAFVV----------KQANVQLTENEVIQFVN 501
Cdd:PLN03102 438 IKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVlekgettkedRVDKLVTRERDLIEYCR 517
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 21355181 502 DN----ASPAKrlrggVIFVDEIPKNPSGKILRRILREMLK 538
Cdd:PLN03102 518 ENlphfMCPRK-----VVFLQELPKNGNGKILKPKLRDIAK 553
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
58-534 |
1.08e-35 |
|
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: 138.36 E-value: 1.08e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 58 MHKSIVRLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREVDHAINLSKPKIIFASkitidr 137
Cdd:cd05919 16 LHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVVTS------ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 138 vakvasknkfvkgiialsgtskkfkniydlkelmedekfktqpdftspaankDEDVSLIVCSSGTTGLPKGVQLTQMNLL 217
Cdd:cd05919 90 ----------------------------------------------------ADDIAYLLYSSGTTGPPKGVMHAHRDPL 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 218 ATLDSQIQPTVIPMEEVTLLTVIPWFHAFGC-LTLITTACVGARLVYLPKF-EEKLFLSAIEKYRVMMAFMVPPLMVFLA 295
Cdd:cd05919 118 LFADAMAREALGLTPGDRVFSSAKMFFGYGLgNSLWFPLAVGASAVLNPGWpTAERVLATLARFRPTVLYGVPTFYANLL 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 296 KHPIVDKYDLSSLMVLLCGAAPLSRETEDQIKERIGVPfIRQGYGLSEsTLSVLVQN--DEFcKPGSVGVLKVGIYAKVI 373
Cdd:cd05919 198 DSCAGSPDALRSLRLCVSAGEALPRGLGERWMEHFGGP-ILDGIGATE-VGHIFLSNrpGAW-RLGSTGRPVPGYEIRLV 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 374 DPDtGKLLGANERGELCFKGDGIMKGYIGDTKSTQTAIKDGWLHTGDIGYYDDDFEFFIVDRIKELIKYKGYQVPPAEIE 453
Cdd:cd05919 275 DEE-GHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVE 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 454 ALLLTNDKIKDAAVIGKPDEEAGELPLAFVV---KQANVQLTENEVIQFVNDNASPAKRLRgGVIFVDEIPKNPSGKILR 530
Cdd:cd05919 354 SLIIQHPAVAEAAVVAVPESTGLSRLTAFVVlksPAAPQESLARDIHRHLLERLSAHKVPR-RIAFVDELPRTATGKLQR 432
|
....
gi 21355181 531 RILR 534
Cdd:cd05919 433 FKLR 436
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
191-535 |
4.83e-35 |
|
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: 136.54 E-value: 4.83e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 191 EDVSLIVCSSGTTGLPKGVQLTQMNLLATLDSQIQPTVIPMEEVTLLTVIP-WF-HAFGCLTLITTACVGARLVYLPKFE 268
Cdd:cd05974 85 DDPMLLYFTSGTTSKPKLVEHTHRSYPVGHLSTMYWIGLKPGDVHWNISSPgWAkHAWSCFFAPWNAGATVFLFNYARFD 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 269 EKLFLSAIEKYRVMmAFMVPPLMvflakHPIVDKYDLSSLMVLL---CGAA-PLSRETEDQIKERIGVPfIRQGYGLSES 344
Cdd:cd05974 165 AKRVLAALVRYGVT-TLCAPPTV-----WRMLIQQDLASFDVKLrevVGAGePLNPEVIEQVRRAWGLT-IRDGYGQTET 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 345 TLSVLVQNDEFCKPGSVGVLKVGIYAKVIDPDTGkllgANERGELCFK-GD----GIMKGYIGDTKSTQTAIKDGWLHTG 419
Cdd:cd05974 238 TALVGNSPGQPVKAGSMGRPLPGYRVALLDPDGA----PATEGEVALDlGDtrpvGLMKGYAGDPDKTAHAMRGGYYRTG 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 420 DIGYYDDDFEFFIVDRIKELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGELPLAFVVKQANVQ---LTENEV 496
Cdd:cd05974 314 DIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGYEpspETALEI 393
|
330 340 350
....*....|....*....|....*....|....*....
gi 21355181 497 IQFVNDNASPAKRLRGgvIFVDEIPKNPSGKILRRILRE 535
Cdd:cd05974 394 FRFSRERLAPYKRIRR--LEFAELPKTISGKIRRVELRR 430
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
59-537 |
1.02e-34 |
|
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: 137.37 E-value: 1.02e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 59 HKSIVRLAYILQKLGvKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLnvtYSDREVDHAINL------SKPKIIFASK 132
Cdd:cd05931 31 DRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPL---PPPTPGRHAERLaailadAGPRVVLTTA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 133 ITIDRVAKVASKNKfVKGIIALSGTskkfkniydlkELMEDEkfkTQPDFTSPAANKDeDVSLIVCSSGTTGLPKGVQLT 212
Cdd:cd05931 107 AALAAVRAFAASRP-AAGTPRLLVV-----------DLLPDT---SAADWPPPSPDPD-DIAYLQYTSGSTGTPKGVVVT 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 213 QMNLLATLdSQIQPTVIPMEEVTLLTVIPWFHAFG-CLTLITTACVGARLVYLP--KFEEK--LFLSAIEKYRVmmAFMV 287
Cdd:cd05931 171 HRNLLANV-RQIRRAYGLDPGDVVVSWLPLYHDMGlIGGLLTPLYSGGPSVLMSpaAFLRRplRWLRLISRYRA--TISA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 288 PPLMVF-LAKHPIVDK----YDLSSLMVLLCGAAPLSRETEDQIKERIGvPF------IRQGYGLSESTLSV-------- 348
Cdd:cd05931 248 APNFAYdLCVRRVRDEdlegLDLSSWRVALNGAEPVRPATLRRFAEAFA-PFgfrpeaFRPSYGLAEATLFVsggppgtg 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 349 ----LVQNDEFCKPG--------------SVGVLKVGIYAKVIDPDTGKLLGANERGELCFKGDGIMKGYIGDTKSTQTA 410
Cdd:cd05931 327 pvvlRVDRDALAGRAvavaaddpaarelvSCGRPLPDQEVRIVDPETGRELPDGEVGEIWVRGPSVASGYWGRPEATAET 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 411 IK-------DGWLHTGDIGYYDDDfEFFIVDRIKELIKYKGYQVPPAEIEA-LLLTNDKIK--DAAVIGKPDEEAGELpl 480
Cdd:cd05931 407 FGalaatdeGGWLRTGDLGFLHDG-ELYITGRLKDLIIVRGRNHYPQDIEAtAEEAHPALRpgCVAAFSVPDDGEERL-- 483
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 481 afvvkqanVQLTENEVIQFVNDNASPAKRLRGGV-----IFVDE--------IPKNPSGKILRRILREML 537
Cdd:cd05931 484 --------VVVAEVERGADPADLAAIAAAIRAAVarehgVAPADvvlvrpgsIPRTSSGKIQRRACRAAY 545
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
64-467 |
2.64e-34 |
|
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: 133.93 E-value: 2.64e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 64 RLA-YILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTY-SDReVDHAINLSKPKIIFASKITIDRVAKV 141
Cdd:TIGR01733 11 RLArHLRAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYpAER-LAFILEDAGARLLLTDSALASRLAGL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 142 asknkfVKGIIALSGTskkfkniydLKELMEDEkfktQPDFTSPAANKDEDVSLIVCSSGTTGLPKGVQLTQMNLLATLD 221
Cdd:TIGR01733 90 ------VLPVILLDPL---------ELAALDDA----PAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 222 SQIQPTVIPMEEVTLLtvipwFHAFG----CLTLITTACVGARLVYLP----KFEEKLFLSAIEKYRVMMAFMVPPLMVF 293
Cdd:TIGR01733 151 WLARRYGLDPDDRVLQ-----FASLSfdasVEEIFGALLAGATLVVPPedeeRDDAALLAALIAEHPVTVLNLTPSLLAL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 294 LAKHpivDKYDLSSLMVLLCGAAPLSRETEDQIKERIGVPFIRQGYGLSESTLSVLVQndEFCKPGSVGVLKVGI----- 368
Cdd:TIGR01733 226 LAAA---LPPALASLRLVILGGEALTPALVDRWRARGPGARLINLYGPTETTVWSTAT--LVDPDDAPRESPVPIgrpla 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 369 --YAKVIDPDtGKLLGANERGELCFKGDGIMKGYIGDtkSTQTA---IKDG--------WLHTGDIGYYDDDFEFFIVDR 435
Cdd:TIGR01733 301 ntRLYVLDDD-LRPVPVGVVGELYIGGPGVARGYLNR--PELTAerfVPDPfaggdgarLYRTGDLVRYLPDGNLEFLGR 377
|
410 420 430
....*....|....*....|....*....|..
gi 21355181 436 IKELIKYKGYQVPPAEIEALLLTNDKIKDAAV 467
Cdd:TIGR01733 378 IDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
25-528 |
2.89e-34 |
|
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: 135.15 E-value: 2.89e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 25 RSLGQYILDKYKSFGDRTVLVDAVNGVEYSAsfMHKSIVRLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGAtv 104
Cdd:cd05920 15 EPLGDLLARSAARHPDRIAVVDGDRRLTYRE--LDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGA-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 105 APLNVTYSDR--EVDHAINLSKPKIIfaskitidrvakvasknkfvkgiiALSGTSKKFKNIYDLKELMEDekfktQPDf 182
Cdd:cd05920 91 VPVLALPSHRrsELSAFCAHAEAVAY------------------------IVPDRHAGFDHRALARELAES-----IPE- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 183 tspaankdedVSLIVCSSGTTGLPKGVQLTQMNL---------LATLDSQiqpTVipmeevtLLTVIPWFHAF--GCLTL 251
Cdd:cd05920 141 ----------VALFLLSGGTTGTPKLIPRTHNDYaynvrasaeVCGLDQD---TV-------YLAVLPAAHNFplACPGV 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 252 ITTACVGARLVYLPKFEEKLFLSAIEKYRVMMAFMVPPLMVFLAKHPIVDKYDLSSLMVLLCGAAPLSRETEDQIKERIG 331
Cdd:cd05920 201 LGTLLAGGRVVLAPDPSPDAAFPLIEREGVTVTALVPALVSLWLDAAASRRADLSSLRLLQVGGARLSPALARRVPPVLG 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 332 VPfIRQGYGLSESTLSVLVQNDefckPGSVGVLKVGIYA------KVIDPDtGKLLGANERGELCFKGDGIMKGYIGDTK 405
Cdd:cd05920 281 CT-LQQVFGMAEGLLNYTRLDD----PDEVIIHTQGRPMspddeiRVVDEE-GNPVPPGEEGELLTRGPYTIRGYYRAPE 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 406 STQTAI-KDGWLHTGDIGYYDDDFEFFIVDRIKELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGELPLAFVV 484
Cdd:cd05920 355 HNARAFtPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVV 434
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 21355181 485 KQaNVQLTENEVIQFVNDNASPAKRLRGGVIFVDEIPKNPSGKI 528
Cdd:cd05920 435 LR-DPPPSAAQLRRFLRERGLAAYKLPDRIEFVDSLPLTAVGKI 477
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
59-469 |
3.29e-34 |
|
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: 136.72 E-value: 3.29e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 59 HKSIVRLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREVDHAINLSKPKIIFASKIT-IDR 137
Cdd:cd05933 15 YEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSEANILVVENQKqLQK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 138 VAKVASKNKFVKGIIALSGTSK-KFKNIYDLKELME------DEKFKTQPDFTSPaankDEDVSLIVcSSGTTGLPKGVQ 210
Cdd:cd05933 95 ILQIQDKLPHLKAIIQYKEPLKeKEPNLYSWDEFMElgrsipDEQLDAIISSQKP----NQCCTLIY-TSGTTGMPKGVM 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 211 LTQMNLL-----ATLDSQIQPTVIPMEevTLLTVIPWFH-------------AFGCL----------TLIT-------TA 255
Cdd:cd05933 170 LSHDNITwtakaASQHMDLRPATVGQE--SVVSYLPLSHiaaqildiwlpikVGGQVyfaqpdalkgTLVKtlrevrpTA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 256 CVGARLVYlPKFEEKL---FLSA---------------IEKYRVMMAFMVPPLMVF-LAKHPIVDK----YDLSSLMVLL 312
Cdd:cd05933 248 FMGVPRVW-EKIQEKMkavGAKSgtlkrkiaswakgvgLETNLKLMGGESPSPLFYrLAKKLVFKKvrkaLGLDRCQKFF 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 313 CGAAPLSRETED-----QIKerigvpfIRQGYGLSESTLSVLVQNDEFCKPGSVGVLKVGIYAKVIDPDtgkllgANERG 387
Cdd:cd05933 327 TGAAPISRETLEfflslNIP-------IMELYGMSETSGPHTISNPQAYRLLSCGKALPGCKTKIHNPD------ADGIG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 388 ELCFKGDGIMKGYIGDTKSTQTAIK-DGWLHTGDIGYYDDDFEFFIVDRIKELIKYKGYQ-VPPAEIEALLLTN-DKIKD 464
Cdd:cd05933 394 EICFWGRHVFMGYLNMEDKTEEAIDeDGWLHSGDLGKLDEDGFLYITGRIKELIITAGGEnVPPVPIEDAVKKElPIISN 473
|
....*
gi 21355181 465 AAVIG 469
Cdd:cd05933 474 AMLIG 478
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
191-530 |
6.97e-34 |
|
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: 131.23 E-value: 6.97e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 191 EDVSLIVCSSGTTGLPKGVQLTQMNLLATLDS-QIQPTVIPMEEVTLLtVIPWFHAFGCLTLITtaCV---GARLVYLPK 266
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFFAVPDIlQKEGLNWVVGDVTYL-PLPATHIGGLWWILT--CLihgGLCVTGGEN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 267 FEEKLFLSAIEKYRVMMAFMVPPLM---VFLAKHPIvdKYDLSSLMVLLCGAAPLsrETEDQIKERIGVPFIRQGYGLSE 343
Cdd:cd17635 78 TTYKSLFKILTTNAVTTTCLVPTLLsklVSELKSAN--ATVPSLRLIGYGGSRAI--AADVRFIEATGLTNTAQVYGLSE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 344 STLSVLVQ-NDEFCKPGSVGVLKVGIYAKVIDPDtGKLLGANERGELCFKGDGIMKGYIGDTKSTQTAIKDGWLHTGDIG 422
Cdd:cd17635 154 TGTALCLPtDDDSIEINAVGRPYPGVDVYLAATD-GIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLIDGWVNTGDLG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 423 YYDDDFEFFIVDRIKELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGELPLAFVVKQAnvQLTENEV--IQFV 500
Cdd:cd17635 233 ERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVASA--ELDENAIraLKHT 310
|
330 340 350
....*....|....*....|....*....|
gi 21355181 501 NDNASPAKRLRGGVIFVDEIPKNPSGKILR 530
Cdd:cd17635 311 IRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
69-540 |
3.03e-33 |
|
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: 133.11 E-value: 3.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 69 LQKLGVKQ--NDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREVDHAINLSKPKIIFASKitidrvakvasknk 146
Cdd:cd05927 22 LRSLGGKPapASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVFCDA-------------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 147 fvkGIialsgtskkfkNIYDLKELMEDEKFKtQPDFTSPaanKDEDVSLIVCSSGTTGLPKGVQLTQMNLLAT---LDSQ 223
Cdd:cd05927 88 ---GV-----------KVYSLEEFEKLGKKN-KVPPPPP---KPEDLATICYTSGTTGNPKGVMLTHGNIVSNvagVFKI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 224 IQPTVIPMEEVTLLTVIPWFHAFGCLTLITTACVGARLVY--------------------------LPKFEEKLFLSAIE 277
Cdd:cd05927 150 LEILNKINPTDVYISYLPLAHIFERVVEALFLYHGAKIGFysgdirlllddikalkptvfpgvprvLNRIYDKIFNKVQA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 278 KyrvmmafmvPPLMVFLA-----------------KHPIVDKYDLS----------SLMVLlcGAAPLSRETEDQIKERI 330
Cdd:cd05927 230 K---------GPLKRKLFnfalnyklaelrsgvvrASPFWDKLVFNkikqalggnvRLMLT--GSAPLSPEVLEFLRVAL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 331 GVPfIRQGYGLSESTLSVLVQN-DEFCkPGSVGVLKVGIYAKVID-PDTGKL-LGANERGELCFKGDGIMKGYIGDTKST 407
Cdd:cd05927 299 GCP-VLEGYGQTECTAGATLTLpGDTS-VGHVGGPLPCAEVKLVDvPEMNYDaKDPNPRGEVCIRGPNVFSGYYKDPEKT 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 408 QTAI-KDGWLHTGDIGYYDDDFEFFIVDRIKELIKY-KGYQVPPAEIEALLLTNDKIKDAAVIGK-----------PDEE 474
Cdd:cd05927 377 AEALdEDGWLHTGDIGEWLPNGTLKIIDRKKNIFKLsQGEYVAPEKIENIYARSPFVAQIFVYGDslksflvaivvPDPD 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 475 A-GELPLAFVVKQANVQ-LTEN-EVIQFV-NDNASPAK--RLRGgviFvdEIPKN----------------PSGKILRRI 532
Cdd:cd05927 457 VlKEWAASKGGGTGSFEeLCKNpEVKKAIlEDLVRLGKenGLKG---F--EQVKAihlepepfsvenglltPTFKLKRPQ 531
|
....*...
gi 21355181 533 LREMLKKQ 540
Cdd:cd05927 532 LKKYYKKQ 539
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
58-534 |
3.67e-33 |
|
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.
Pssm-ID: 341272 [Multi-domain] Cd Length: 610 Bit Score: 133.77 E-value: 3.67e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 58 MHKSIVRLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREVDHAINLSKPKIIFASKITIDR 137
Cdd:cd05968 97 LLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKALITADGFTRR 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 138 ---------VAKVASKNKFVKGIIALSGTSKKFkNIYDLKELMEDEKFKTQPDftSPAANKDEDVSLIVCSSGTTGLPKG 208
Cdd:cd05968 177 grevnlkeeADKACAQCPTVEKVVVVRHLGNDF-TPAKGRDLSYDEEKETAGD--GAERTESEDPLMIIYTSGTTGKPKG 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 209 VQLTQMN--LLATLDSQIQPTVIPMEEVTLLTVIPW----FHAFGCLTLittacvGARLVY---LPKFEEKLFLS-AIEK 278
Cdd:cd05968 254 TVHVHAGfpLKAAQDMYFQFDLKPGDLLTWFTDLGWmmgpWLIFGGLIL------GATMVLydgAPDHPKADRLWrMVED 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 279 YRVMMAFMVPPLMVFLAKH--PIVDKYDLSSLMVLLCGAAPLSRETEDQIKERIG---VPFIRQGYG--LSESTL-SVLV 350
Cdd:cd05968 328 HEITHLGLSPTLIRALKPRgdAPVNAHDLSSLRVLGSTGEPWNPEPWNWLFETVGkgrNPIINYSGGteISGGILgNVLI 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 351 QNdefCKPGSVGVLKVGIYAKVIDpDTGKLLgANERGELCFKGD--GIMKGYIGDTKSTQTA----IKDGWLHtGDIGYY 424
Cdd:cd05968 408 KP---IKPSSFNGPVPGMKADVLD-ESGKPA-RPEVGELVLLAPwpGMTRGFWRDEDRYLETywsrFDNVWVH-GDFAYY 481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 425 DDDFEFFIVDRIKELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGELPLAFVVKQANVQLTE---NEVIQFVN 501
Cdd:cd05968 482 DEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVLKPGVTPTEalaEELMERVA 561
|
490 500 510
....*....|....*....|....*....|...
gi 21355181 502 DNASPAKRLRgGVIFVDEIPKNPSGKILRRILR 534
Cdd:cd05968 562 DELGKPLSPE-RILFVKDLPKTRNAKVMRRVIR 593
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
39-534 |
6.02e-33 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 132.71 E-value: 6.02e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 39 GDRTVL--VDAVNGVEYSASFMHKSIVRLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREV 116
Cdd:PRK04319 58 KDKVALryLDASRKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAV 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 117 DHAINLSKPKIIfaskITIDRVA--KVASKNKFVKGIIALSGTSKKFKNIYDLKELMEDEkfktQPDFTSPAANKdEDVS 194
Cdd:PRK04319 138 RDRLEDSEAKVL----ITTPALLerKPADDLPSLKHVLLVGEDVEEGPGTLDFNALMEQA----SDEFDIEWTDR-EDGA 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 195 LIVCSSGTTGLPKGVQLTQMNLLA-------TLDsqIQPtvipmEEVTLLT-------------VIPWFHAfgcltlITT 254
Cdd:PRK04319 209 ILHYTSGSTGKPKGVLHVHNAMLQhyqtgkyVLD--LHE-----DDVYWCTadpgwvtgtsygiFAPWLNG------ATN 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 255 ACVGARlvylpkFEEKLFLSAIEKYRVMMAFMVPPLMVFLAKH--PIVDKYDLSSLMVLLCGAAPLSRETEDQIKERIGV 332
Cdd:PRK04319 276 VIDGGR------FSPERWYRILEDYKVTVWYTAPTAIRMLMGAgdDLVKKYDLSSLRHILSVGEPLNPEVVRWGMKVFGL 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 333 PfIRQGYGLSEsTLSVLVQN----DefCKPGSVGVLKVGIYAKVIDpDTGKLLGANERGELCFKgDG---IMKGYIGDTK 405
Cdd:PRK04319 350 P-IHDNWWMTE-TGGIMIANypamD--IKPGSMGKPLPGIEAAIVD-DQGNELPPNRMGNLAIK-KGwpsMMRGIWNNPE 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 406 STQTAIKDGWLHTGDIGYYDDDFEFFIVDRIKELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGELPLAFVVK 485
Cdd:PRK04319 424 KYESYFAGDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVAL 503
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 21355181 486 QANVQLTEN---EVIQFVNdnaspaKRLRGGVI-----FVDEIPKNPSGKILRRILR 534
Cdd:PRK04319 504 RPGYEPSEElkeEIRGFVK------KGLGAHAApreieFKDKLPKTRSGKIMRRVLK 554
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
38-527 |
6.47e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 131.93 E-value: 6.47e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 38 FGDRTVLVDAVNGVEYsASFMHKSiVRLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREVD 117
Cdd:PRK07798 16 VPDRVALVCGDRRLTY-AELEERA-NRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 118 HAINLSKPKIIFASKITIDRVAKVASKNKFVKGIIALS-GTSKKFkniydLKELMEDEKFKTQPDFTSPAANKDEDVSLI 196
Cdd:PRK07798 94 YLLDDSDAVALVYEREFAPRVAEVLPRLPKLRTLVVVEdGSGNDL-----LPGAVDYEDALAAGSPERDFGERSPDDLYL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 197 VCSSGTTGLPKGVQLTQ----MNLLATLDSQIQPTVIPMEEV----------TLLTVIPWFHAFGCLTLITTACVGARLV 262
Cdd:PRK07798 169 LYTGGTTGMPKGVMWRQedifRVLLGGRDFATGEPIEDEEELakraaagpgmRRFPAPPLMHGAGQWAAFAALFSGQTVV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 263 YLP--KFEEKLFLSAIEKYRVMMAFMVPPLMvflAKhPIVD------KYDLSSLMVLLCGAAPLSRETEDQIKERIGVPF 334
Cdd:PRK07798 249 LLPdvRFDADEVWRTIEREKVNVITIVGDAM---AR-PLLDaleargPYDLSSLFAIASGGALFSPSVKEALLELLPNVV 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 335 IRQGYGLSES--TLSVLVQNDefckPGSVGVLKVGI--YAKVIDPDTGKLL-GANERGELCfKGDGIMKGYIGDTKSTQT 409
Cdd:PRK07798 325 LTDSIGSSETgfGGSGTVAKG----AVHTGGPRFTIgpRTVVLDEDGNPVEpGSGEIGWIA-RRGHIPLGYYKDPEKTAE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 410 AIK--DG--WLHTGDIGYYDDDFEFFIVDRIKELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGELPLAFVVK 485
Cdd:PRK07798 400 TFPtiDGvrYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVPDERWGQEVVAVVQL 479
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 21355181 486 QANVQLTENEVIQFVndnaspAKRLRG-----GVIFVDEIPKNPSGK 527
Cdd:PRK07798 480 REGARPDLAELRAHC------RSSLAGykvprAIWFVDEVQRSPAGK 520
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
39-541 |
9.09e-33 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 131.80 E-value: 9.09e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 39 GDRTVLVDAVNG--VEYSASFMHKSIVRLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREV 116
Cdd:PRK06018 24 GNREVVTRSVEGpiVRTTYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 117 DHAINLSKPKIIFASKITIDRVAKVASKNKFVKGIIALSGTS----KKFKNIYDLKELME--DEKFKTQpDFtspaankD 190
Cdd:PRK06018 104 AWIINHAEDRVVITDLTFVPILEKIADKLPSVERYVVLTDAAhmpqTTLKNAVAYEEWIAeaDGDFAWK-TF-------D 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 191 EDVSLIVC-SSGTTGLPKGVQLT-QMNLLATLDSQiQPTVIPMEEV-TLLTVIPWFHAFGCLTLITTACVGARLVyLP-- 265
Cdd:PRK06018 176 ENTAAGMCyTSGTTGDPKGVLYShRSNVLHALMAN-NGDALGTSAAdTMLPVVPLFHANSWGIAFSAPSMGTKLV-MPga 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 266 KFEEKLFLSAIEKYRVMMAFMVPPLMVFLAKHPIVDKYDLSSLMVLLCGAAPLSRETedqIK--ERIGVPfIRQGYGLSE 343
Cdd:PRK06018 254 KLDGASVYELLDTEKVTFTAGVPTVWLMLLQYMEKEGLKLPHLKMVVCGGSAMPRSM---IKafEDMGVE-VRHAWGMTE 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 344 S----TLSVLvqNDEFCK-PGSV--------GVLKVGIYAKVIDPDtGKLLGANER--GELCFKGDGIMKGYIGdtksTQ 408
Cdd:PRK06018 330 MsplgTLAAL--KPPFSKlPGDArldvlqkqGYPPFGVEMKITDDA-GKELPWDGKtfGRLKVRGPAVAAAYYR----VD 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 409 TAI--KDGWLHTGDIGYYDDDFEFFIVDRIKELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGELPLAFVVKQ 486
Cdd:PRK06018 403 GEIldDDGFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQLK 482
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 21355181 487 ANVQLTENEVIQFVNDNAspAK-RLRGGVIFVDEIPKNPSGKILRRILREMLKKQK 541
Cdd:PRK06018 483 PGETATREEILKYMDGKI--AKwWMPDDVAFVDAIPHTATGKILKTALREQFKDYK 536
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
38-535 |
1.58e-32 |
|
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: 130.63 E-value: 1.58e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 38 FGDRTVlvdavNGVEYSASFMHKSIVRLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREVD 117
Cdd:cd05915 15 SRLHTG-----EVHRTTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 118 HAINLSKPKIIFASKitidRVAKVASKnkfvkgiiALSGTSKKFKNIYDLKELMEDEKFKT--QPDFtSPAANKDE-DVS 194
Cdd:cd05915 90 YILNHAEDKVLLFDP----NLLPLVEA--------IRGELKTVQHFVVMDEKAPEGYLAYEeaLGEE-ADPVRVPErAAC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 195 LIVCSSGTTGLPKGVQLTQ----MNLLAT-LDSQIQPTVIPMeevtLLTVIPWFHAFGCLTLITTACVGARLVYLPK-FE 268
Cdd:cd05915 157 GMAYTTGTTGLPKGVVYSHralvLHSLAAsLVDGTALSEKDV----VLPVVPMFHVNAWCLPYAATLVGAKQVLPGPrLD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 269 EKLFLSAIEKYRVMMAFMVPPLMVFLAK-HPIVDKYDLSSLMVLLCGAAPlsreTEDQIK-ERIGVPFIRQGYGLSE--- 343
Cdd:cd05915 233 PASLVELFDGEGVTFTAGVPTVWLALADyLESTGHRLKTLRRLVVGGSAA----PRSLIArFERMGVEVRQGYGLTEtsp 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 344 --------STLSVLVQNDEFCKPGSVGVLKVGIYAKVIDPDT------GKLLGAnergeLCFKGDGIMKGYIGDTKSTQ- 408
Cdd:cd05915 309 vvvqnfvkSHLESLSEEEKLTLKAKTGLPIPLVRLRVADEEGrpvpkdGKALGE-----VQLKGPWITGGYYGNEEATRs 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 409 TAIKDGWLHTGDIGYYDDDFEFFIVDRIKELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGELPLAFvVKQAN 488
Cdd:cd05915 384 ALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAV-VVPRG 462
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 21355181 489 VQLTENEVIQFVNDNASPAKRLRGGVIFVDEIPKNPSGKILRRILRE 535
Cdd:cd05915 463 EKPTPEELNEHLLKAGFAKWQLPDAYVFAEEIPRTSAGKFLKRALRE 509
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
32-534 |
2.57e-32 |
|
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: 131.14 E-value: 2.57e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 32 LDK-YKSFGDRTVLV----DAVNGVEYSASFMHKSIVRLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGAtvaP 106
Cdd:cd05966 59 LDRhLKERGDKVAIIwegdEPDQSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGA---V 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 107 LNVTYS--------DREVDhainlSKPKIIfaskITID---RVAKV----------ASKNKFVKGIIAL--SGTSKKFKN 163
Cdd:cd05966 136 HSVVFAgfsaeslaDRIND-----AQCKLV----ITADggyRGGKViplkeivdeaLEKCPSVEKVLVVkrTGGEVPMTE 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 164 IYDL--KELMEDekfktQPDFTSPAANKDEDVSLIVCSSGTTGLPKGVQLTQ--------MNLLATLDsqIQPTVIpmee 233
Cdd:cd05966 207 GRDLwwHDLMAK-----QSPECEPEWMDSEDPLFILYTSGSTGKPKGVVHTTggyllyaaTTFKYVFD--YHPDDI---- 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 234 vtlltvipwfhaFGCltlitTACVG-----ARLVYLP--------KFE-------EKLFLSAIEKYRVMMAFMVPPLMVF 293
Cdd:cd05966 276 ------------YWC-----TADIGwitghSYIVYGPlangattvMFEgtptypdPGRYWDIVEKHKVTIFYTAPTAIRA 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 294 LAKHP--IVDKYDLSSLMVLLCGAAPLSRETEDQIKERIG---VPfIRQGYGLSEsTLSVLVQNDEFC---KPGSVGVLK 365
Cdd:cd05966 339 LMKFGdeWVKKHDLSSLRVLGSVGEPINPEAWMWYYEVIGkerCP-IVDTWWQTE-TGGIMITPLPGAtplKPGSATRPF 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 366 VGIYAKVIDPDTGKLlGANERGELCFKGD--GIMKGYIGDTKS-TQTAIKD--GWLHTGDIGYYDDDFEFFIVDRIKELI 440
Cdd:cd05966 417 FGIEPAILDEEGNEV-EGEVEGYLVIKRPwpGMARTIYGDHERyEDTYFSKfpGYYFTGDGARRDEDGYYWITGRVDDVI 495
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 441 KYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGELPLAFVVKQANVQLT---ENEVIQFVNDN----ASPAKrlrgg 513
Cdd:cd05966 496 NVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGEEPSdelRKELRKHVRKEigpiATPDK----- 570
|
570 580
....*....|....*....|.
gi 21355181 514 VIFVDEIPKNPSGKILRRILR 534
Cdd:cd05966 571 IQFVPGLPKTRSGKIMRRILR 591
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
200-538 |
6.57e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 129.30 E-value: 6.57e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 200 SGTTGLPKGVQLTQ----MNLLatldSQIQPTVIPMEEVTLLTViPWFHAFG-CLTLiTTACVGARLVYLPKFEEKLFLS 274
Cdd:PRK08162 191 SGTTGNPKGVVYHHrgayLNAL----SNILAWGMPKHPVYLWTL-PMFHCNGwCFPW-TVAARAGTNVCLRKVDPKLIFD 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 275 AIEKYRVMMAFMVPPLMVFLAKHPIVDKYDLS-SLMVLLCGAAPLSRETEDQikERIGVPfIRQGYGLSE---------- 343
Cdd:PRK08162 265 LIREHGVTHYCGAPIVLSALINAPAEWRAGIDhPVHAMVAGAAPPAAVIAKM--EEIGFD-LTHVYGLTEtygpatvcaw 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 344 ----STLSVLVQNDEFCKPGSVGVLKVGIyaKVIDPDTGKLLGANER--GELCFKGDGIMKGYIGDTKSTQTAIKDGWLH 417
Cdd:PRK08162 342 qpewDALPLDERAQLKARQGVRYPLQEGV--TVLDPDTMQPVPADGEtiGEIMFRGNIVMKGYLKNPKATEEAFAGGWFH 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 418 TGDIGYYDDDFEFFIVDRIKELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGELPLAFVVKQANVQLTENEVI 497
Cdd:PRK08162 420 TGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDPKWGEVPCAFVELKDGASATEEEII 499
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 21355181 498 QFVNDNASPAKRLRgGVIFvDEIPKNPSGKILRRILREMLK 538
Cdd:PRK08162 500 AHCREHLAGFKVPK-AVVF-GELPKTSTGKIQKFVLREQAK 538
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
25-535 |
7.95e-32 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 128.94 E-value: 7.95e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 25 RSLGQYILDKYKSFGDRTVLVDAVNGVEYSASF--MHKSIVRLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGA 102
Cdd:cd05906 10 RTLLELLLRAAERGPTKGITYIDADGSEEFQSYqdLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 103 TVAPLNVTYSDREVDHAIN--------LSKPKIIfaskITIDRVAKVAsknkfvkGIIALSGtskkfknIYDLKELMEDE 174
Cdd:cd05906 90 VPAPLTVPPTYDEPNARLRklrhiwqlLGSPVVL----TDAELVAEFA-------GLETLSG-------LPGIRVLSIEE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 175 KFKTQPDFTSPAANKDeDVSLIVCSSGTTGLPKGVQLTQMNLLATLDSQIQPTVIPMEEVTLLTViPWFHAFGCLTL-IT 253
Cdd:cd05906 152 LLDTAADHDLPQSRPD-DLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWV-PLDHVGGLVELhLR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 254 TACVGARLVYLPKfEEKL-----FLSAIEKYRVMMAFMvpP-----LMVFLAKHPIVDKYDLSSLMVLLCGAAPLSRETE 323
Cdd:cd05906 230 AVYLGCQQVHVPT-EEILadplrWLDLIDRYRVTITWA--PnfafaLLNDLLEEIEDGTWDLSSLRYLVNAGEAVVAKTI 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 324 D---QIKERIGVP--FIRQGYGLSEsTLSVLVQNDEFCKPG--------SVGVLKVGIYAKVIDpDTGKLLGANERGELC 390
Cdd:cd05906 307 RrllRLLEPYGLPpdAIRPAFGMTE-TCSGVIYSRSFPTYDhsqalefvSLGRPIPGVSMRIVD-DEGQLLPEGEVGRLQ 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 391 FKGDGIMKGYIGDTKSTQTAI-KDGWLHTGDIGYYDDDfEFFIVDRIKELIKYKGYQVPPAEIEALLltndkikdaavig 469
Cdd:cd05906 385 VRGPVVTKGYYNNPEANAEAFtEDGWFRTGDLGFLDNG-NLTITGRTKDTIIVNGVNYYSHEIEAAV------------- 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 470 kpdEEAGELP----LAFVVKQANvQLTENEVIQFV-----NDNASP-AKRLRGGVIFV-------------DEIPKNPSG 526
Cdd:cd05906 451 ---EEVPGVEpsftAAFAVRDPG-AETEELAIFFVpeydlQDALSEtLRAIRSVVSREvgvspayliplpkEEIPKTSLG 526
|
....*....
gi 21355181 527 KILRRILRE 535
Cdd:cd05906 527 KIQRSKLKA 535
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
40-533 |
7.97e-32 |
|
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: 127.75 E-value: 7.97e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 40 DRTVLVdaVNGVEYSASFMHKSIVRLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYsdrevdha 119
Cdd:cd05945 6 DRPAVV--EGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASS-------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 120 inlskpkiifaskiTIDRVAKVAsknkfvkgiialsgtskkfkniydlkelmedekfktqpDFTSPAA--NKDEDVSLIV 197
Cdd:cd05945 76 --------------PAERIREIL--------------------------------------DAAKPALliADGDDNAYII 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 198 CSSGTTGLPKGVQLTQMNLLATLDSQIQPTVIPMEEVTLLTviPWFHaFGC--LTLITTACVGARLVYLPKFE---EKLF 272
Cdd:cd05945 104 FTSGSTGRPKGVQISHDNLVSFTNWMLSDFPLGPGDVFLNQ--APFS-FDLsvMDLYPALASGATLVPVPRDAtadPKQL 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 273 LSAIEKYRVMMAFMVPPLMVFLAKHPIVDKYDLSSL-MVLLCGAaPLSRETEDQIKERIGVPFIRQGYGLSESTLSV--- 348
Cdd:cd05945 181 FRFLAEHGITVWVSTPSFAAMCLLSPTFTPESLPSLrHFLFCGE-VLPHKTARALQQRFPDARIYNTYGPTEATVAVtyi 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 349 ------LVQNDefckPGSVGVLKVGIYAKVIDPDtGKLLGANERGELCFKGDGIMKGYIGDTKSTQTAI----KDGWLHT 418
Cdd:cd05945 260 evtpevLDGYD----RLPIGYAKPGAKLVILDED-GRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFfpdeGQRAYRT 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 419 GDIGYYDDDFEFFIVDRIKELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGELPLAFVV-----KQANVQLTE 493
Cdd:cd05945 335 GDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVpkpgaEAGLTKAIK 414
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 21355181 494 NEVIQFVNDNASPAKrlrggVIFVDEIPKNPSGKILRRIL 533
Cdd:cd05945 415 AELAERLPPYMIPRR-----FVYLDELPLNANGKIDRKAL 449
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
64-534 |
1.53e-31 |
|
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: 127.46 E-value: 1.53e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 64 RLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREVDHAINLSKPKIIfaskITIDRVAkvas 143
Cdd:cd17651 32 RLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERLAFMLADAGPVLV----LTHPALA---- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 144 knkFVKGIIALSGTskkfkniydlkeLMEDEKFKTQPDfTSPAANKD-EDVSLIVCSSGTTGLPKGVQLTQMNLLATLDS 222
Cdd:cd17651 104 ---GELAVELVAVT------------LLDQPGAAAGAD-AEPDPALDaDDLAYVIYTSGSTGRPKGVVMPHRSLANLVAW 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 223 QIQPTVIPMEEVTLLTVIPWFHAFgCLTLITTACVGARLVyLPKFEEKL----FLSAIEKYRVMMAFMVPPLMVFLAKHP 298
Cdd:cd17651 168 QARASSLGPGARTLQFAGLGFDVS-VQEIFSTLCAGATLV-LPPEEVRTdppaLAAWLDEQRISRVFLPTVALRALAEHG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 299 IVDKYDLSSLMVLLCGAAPLSreTEDQIKERI-GVPFIR--QGYGLSEST----LSVLVQNDEFCKPGSVGVLKVGIYAK 371
Cdd:cd17651 246 RPLGVRLAALRYLLTGGEQLV--LTEDLREFCaGLPGLRlhNHYGPTETHvvtaLSLPGDPAAWPAPPPIGRPIDNTRVY 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 372 VIDPDtGKLLGANERGELCFKGDGIMKGYIGDTKSTQTA-IKDGWL------HTGDIGYYDDDFEFFIVDRIKELIKYKG 444
Cdd:cd17651 324 VLDAA-LRPVPPGVPGELYIGGAGLARGYLNRPELTAERfVPDPFVpgarmyRTGDLARWLPDGELEFLGRADDQVKIRG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 445 YQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGELPLAFVVKQANVQLTENEVIQFVNDnASPAKRLRGGVIFVDEIPKNP 524
Cdd:cd17651 403 FRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPEAPVDAAELRAALAT-HLPEYMVPSAFVLLDALPLTP 481
|
490
....*....|
gi 21355181 525 SGKILRRILR 534
Cdd:cd17651 482 NGKLDRRALP 491
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
58-535 |
7.15e-31 |
|
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: 125.52 E-value: 7.15e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 58 MHKSIVRLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREVDHAINLSKPKIIFASKitidr 137
Cdd:cd17655 28 LNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEERIQYILEDSGADILLTQS----- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 138 vaKVASKNKFVKGIIalsgtskkfkniydlkeLMEDEKFKTQPDFTSPAANKDEDVSLIVCSSGTTGLPKGVQLTQMNLL 217
Cdd:cd17655 103 --HLQPPIAFIGLID-----------------LLDEDTIYHEESENLEPVSKSDDLAYVIYTSGSTGKPKGVMIEHRGVV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 218 ATLDSqIQPTVIPMEEVTLLTVIPW-FHAFgcLTLITTACV-GARLVYLPKFE---EKLFLSAIEKYRVMMAFMVPPLMV 292
Cdd:cd17655 164 NLVEW-ANKVIYQGEHLRVALFASIsFDAS--VTEIFASLLsGNTLYIVRKETvldGQALTQYIRQNRITIIDLTPAHLK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 293 FLAKhpiVDKYDLSSLMVLLCGAAPLSRETEDQIKERIGV-PFIRQGYGLSESTLSVLVQNDEFCKPGSVGV------LK 365
Cdd:cd17655 241 LLDA---ADDSEGLSLKHLIVGGEALSTELAKKIIELFGTnPTITNAYGPTETTVDASIYQYEPETDQQVSVpigkplGN 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 366 VGIYakVIDpDTGKLLGANERGELCFKGDGIMKGYIgdTKSTQTAIK---------DGWLHTGDIGYY--DDDFEFfiVD 434
Cdd:cd17655 318 TRIY--ILD-QYGRPQPVGVAGELYIGGEGVARGYL--NRPELTAEKfvddpfvpgERMYRTGDLARWlpDGNIEF--LG 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 435 RIKELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGELPLAFVVkqANVQLTENEVIQFVndnaspAKRLRGGV 514
Cdd:cd17655 391 RIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIV--SEKELPVAQLREFL------ARELPDYM 462
|
490 500
....*....|....*....|....*.
gi 21355181 515 I---FV--DEIPKNPSGKILRRILRE 535
Cdd:cd17655 463 IpsyFIklDEIPLTPNGKVDRKALPE 488
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
40-533 |
8.90e-30 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 122.80 E-value: 8.90e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 40 DRTVLVDAVNGVEYSAsfMHKSIVRLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREVDHA 119
Cdd:PRK13383 50 GRTAIIDDDGALSYRE--LQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 120 INLSKPKIIFASKITIDRVAkvaSKNKFVKGIIALSGTSkkfkniydlkelmedEKFKTQPDFTSPAankdedvSLIVCS 199
Cdd:PRK13383 128 LRAHHISTVVADNEFAERIA---GADDAVAVIDPATAGA---------------EESGGRPAVAAPG-------RIVLLT 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 200 SGTTGLPKGVQLTqmnllATLDSQIQPTVIPMEEVTLLT------VIPWFHAFGCLTLITTACVGARLVYLPKFEEKLFL 273
Cdd:PRK13383 183 SGTTGKPKGVPRA-----PQLRSAVGVWVTILDRTRLRTgsrisvAMPMFHGLGLGMLMLTIALGGTVLTHRHFDAEAAL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 274 SAIEKYRVMMAFMVPPLMVFLAKHP--IVDKYDLSSLMVLLCGAAPLSRETEDQIKERIGvPFIRQGYGLSESTLSVLVQ 351
Cdd:PRK13383 258 AQASLHRADAFTAVPVVLARILELPprVRARNPLPQLRVVMSSGDRLDPTLGQRFMDTYG-DILYNGYGSTEVGIGALAT 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 352 NDEFCK-PGSVGVLKVGIYAKVIDPDtGKLLGANERGELCFKGDGIMKGYigdTKSTQTAIKDGWLHTGDIGYYDDDFEF 430
Cdd:PRK13383 337 PADLRDaPETVGKPVAGCPVRILDRN-NRPVGPRVTGRIFVGGELAGTRY---TDGGGKAVVDGMTSTGDMGYLDNAGRL 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 431 FIVDRIKELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGELPLAFVVKQANVQLTENEVIQFVNDNASPAKRL 510
Cdd:PRK13383 413 FIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPGSGVDAAQLRDYLKDRVSRFEQP 492
|
490 500
....*....|....*....|...
gi 21355181 511 RgGVIFVDEIPKNPSGKILRRIL 533
Cdd:PRK13383 493 R-DINIVSSIPRNPTGKVLRKEL 514
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
24-540 |
1.28e-29 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 124.31 E-value: 1.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 24 SRSLGQYILDKYKSFGDRTVLVDAVNG--VEYSASFMhKSIVrLAYILQKlGVKQNDVVGLSSENSVNFALAMFAGLAVG 101
Cdd:PRK06814 630 DRTLFEALIEAAKIHGFKKLAVEDPVNgpLTYRKLLT-GAFV-LGRKLKK-NTPPGENVGVMLPNANGAAVTFFALQSAG 706
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 102 ATVAPLNVTYSDREVDHAINLSKPKIIFASKITIDrvakvasKNKFVKGIIALSgtsKKFKNIY--DLKE---LMEDEKF 176
Cdd:PRK06814 707 RVPAMINFSAGIANILSACKAAQVKTVLTSRAFIE-------KARLGPLIEALE---FGIRIIYleDVRAqigLADKIKG 776
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 177 KTQPDF--TSPAANKDEDVSLIVCSSGTTGLPKGVQLTQMNLLATLdSQIQpTVI---PMEEVtlLTVIPWFHAFGcLT- 250
Cdd:PRK06814 777 LLAGRFplVYFCNRDPDDPAVILFTSGSEGTPKGVVLSHRNLLANR-AQVA-ARIdfsPEDKV--FNALPVFHSFG-LTg 851
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 251 -LITTACVGARLVYLPkfeeklflSAIEkYRVmmafmVPPLM------------VFLA-----KHPivdkYDLSSLMVLL 312
Cdd:PRK06814 852 gLVLPLLSGVKVFLYP--------SPLH-YRI-----IPELIydtnatilfgtdTFLNgyaryAHP----YDFRSLRYVF 913
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 313 CGAAPLSRETEDQIKERIGVPfIRQGYGLSESTLSVLVQNDEFCKPGSVGVLKVGIYAKViDPdtgkLLGANERGELCFK 392
Cdd:PRK06814 914 AGAEKVKEETRQTWMEKFGIR-ILEGYGVTETAPVIALNTPMHNKAGTVGRLLPGIEYRL-EP----VPGIDEGGRLFVR 987
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 393 GDGIMKGYI-GDTKSTQTAIKDGWLHTGDIGYYDDDFEFFIVDRIKELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKP 471
Cdd:PRK06814 988 GPNVMLGYLrAENPGVLEPPADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELWPDALHAAVSIP 1067
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21355181 472 DEEAGElPLAFVVKQAnvQLTENEVIQFVNDNASPAKRLRGGVIFVDEIPKNPSGKI----LRRILREMLKKQ 540
Cdd:PRK06814 1068 DARKGE-RIILLTTAS--DATRAAFLAHAKAAGASELMVPAEIITIDEIPLLGTGKIdyvaVTKLAEEAAAKP 1137
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
32-529 |
1.80e-29 |
|
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341289 [Multi-domain] Cd Length: 587 Bit Score: 122.69 E-value: 1.80e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 32 LDKY-KSFGDRTVLV----DAVNGVEYSASFMHKSIVRLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAP 106
Cdd:cd17634 59 LDRHlRENGDRTAIIyegdDTSQSRTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSV 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 107 LNVTYSDREVDHAINLSKPKIIfaskITID---RVAKVASKNKFVKGIIALSGTS-------KKFKNIYDLKE---LMED 173
Cdd:cd17634 139 IFGGFAPEAVAGRIIDSSSRLL----ITADggvRAGRSVPLKKNVDDALNPNVTSvehvivlKRTGSDIDWQEgrdLWWR 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 174 EKFKTQPDFTSPAANKDEDVSLIVCSSGTTGLPKGVQLTQ--MNLLATLDSQIQPTVIPMEEVTLLTVIPWFHAFGCLTL 251
Cdd:cd17634 215 DLIAKASPEHQPEAMNAEDPLFILYTSGTTGKPKGVLHTTggYLVYAATTMKYVFDYGPGDIYWCTADVGWVTGHSYLLY 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 252 ITTACVGARLVY--LPKF-EEKLFLSAIEKYRVMMAFMVPPLMVFLAKH--PIVDKYDLSSLMVLLCGAAPLSRETEDQI 326
Cdd:cd17634 295 GPLACGATTLLYegVPNWpTPARMWQVVDKHGVNILYTAPTAIRALMAAgdDAIEGTDRSSLRILGSVGEPINPEAYEWY 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 327 KERIG---VPFIRQGYGLSESTLSV-LVQNDEFCKPGSVGVLKVGIYAKVIDPDTGKLLGANErGELCFKGD--GIMKGY 400
Cdd:cd17634 375 WKKIGkekCPVVDTWWQTETGGFMItPLPGAIELKAGSATRPVFGVQPAVVDNEGHPQPGGTE-GNLVITDPwpGQTRTL 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 401 IGDTKS---TQTAIKDGWLHTGDIGYYDDDFEFFIVDRIKELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGE 477
Cdd:cd17634 454 FGDHERfeqTYFSTFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQ 533
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 21355181 478 LPLAFVVKQANVQLTE---NEVIQFVNDNASPAKRLRgGVIFVDEIPKNPSGKIL 529
Cdd:cd17634 534 APYAYVVLNHGVEPSPelyAELRNWVRKEIGPLATPD-VVHWVDSLPKTRSGKIM 587
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
64-533 |
3.31e-29 |
|
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: 120.77 E-value: 3.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 64 RLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREVDHAINLSKPKIIFASKITIDRVAKvas 143
Cdd:cd12117 34 RLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAERLAFMLADAGAKVLLTDRSLAGRAGG--- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 144 knkfvkgiialsgtskkfkniyDLKELMEDEKFKTQPDFTSPAANKDEDVSLIVCSSGTTGLPKGVQLTQMNL--LATLD 221
Cdd:cd12117 111 ----------------------LEVAVVIDEALDAGPAGNPAVPVSPDDLAYVMYTSGSTGRPKGVAVTHRGVvrLVKNT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 222 SQIQPTVipmEEVTLLTVIPWFHA-----FGCLTlittacVGARLVYLPKfeEKL-----FLSAIEKYRVMMAFMVPPLm 291
Cdd:cd12117 169 NYVTLGP---DDRVLQTSPLAFDAstfeiWGALL------NGARLVLAPK--GTLldpdaLGALIAEEGVTVLWLTAAL- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 292 vFlakHPIVDKYD--LSSLMVLLCGAAPLSRETEDQIKERIGVPFIRQGYGLSESTLSVL--VQNDEFCKPGSV--GVLK 365
Cdd:cd12117 237 -F---NQLADEDPecFAGLRELLTGGEVVSPPHVRRVLAACPGLRLVNGYGPTENTTFTTshVVTELDEVAGSIpiGRPI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 366 VGIYAKVIDPDtGKLLGANERGELCFKGDGIMKGYIGDTKSTQTA-IKDGWL------HTGDIGYYDDD--FEFfiVDRI 436
Cdd:cd12117 313 ANTRVYVLDED-GRPVPPGVPGELYVGGDGLALGYLNRPALTAERfVADPFGpgerlyRTGDLARWLPDgrLEF--LGRI 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 437 KELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGELPLAFVVkqANVQLTENEVIQFVndnaspAKRLRGG--- 513
Cdd:cd12117 390 DDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVV--AEGALDAAELRAFL------RERLPAYmvp 461
|
490 500
....*....|....*....|..
gi 21355181 514 --VIFVDEIPKNPSGKILRRIL 533
Cdd:cd12117 462 aaFVVLDELPLTANGKVDRRAL 483
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
64-534 |
3.58e-29 |
|
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: 119.93 E-value: 3.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 64 RLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREVDHAINLSKPKIIfaskitidrVAKVAS 143
Cdd:cd05973 12 RFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLV---------VTDAAN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 144 KNKFvkgiialsgtskkfkniydlkelmedekfktqpdftspaankDEDVSLIVCSSGTTGLPKGVQLTQMNLLATLDSQ 223
Cdd:cd05973 83 RHKL------------------------------------------DSDPFVMMFTSGTTGLPKGVPVPLRALAAFGAYL 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 224 IQPTVIPMEEVTLLTVIP-WfhAFGcltlITTACVGARLVYLPK-FEEKLFlSAIEKYRVMMAFMVPPLM-------VFL 294
Cdd:cd05973 121 RDAVDLRPEDSFWNAADPgW--AYG----LYYAITGPLALGHPTiLLEGGF-SVESTWRVIERLGVTNLAgsptayrLLM 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 295 AKHPIVDKYDLSSLMVLLCGAAPLSRETEDQIKERIGVPfIRQGYGLSEstLSVLVQN----DEFCKPGSVGVLKVGIYA 370
Cdd:cd05973 194 AAGAEVPARPKGRLRRVSSAGEPLTPEVIRWFDAALGVP-IHDHYGQTE--LGMVLANhhalEHPVHAGSAGRAMPGWRV 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 371 KVIDpDTGKLLGANERGELCFKGDG--IM--KGYigdTKSTQTAIKDGWLHTGDIGYYDDDFEFFIVDRIKELIKYKGYQ 446
Cdd:cd05973 271 AVLD-DDGDELGPGEPGRLAIDIANspLMwfRGY---QLPDTPAIDGGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYR 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 447 VPPAEIEALLLTNDKIKDAAVIGKPDEEAGELPLAFVVKQANVQLT---ENEVIQFVNDNASPAKRLRgGVIFVDEIPKN 523
Cdd:cd05973 347 IGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHEGTpalADELQLHVKKRLSAHAYPR-TIHFVDELPKT 425
|
490
....*....|.
gi 21355181 524 PSGKILRRILR 534
Cdd:cd05973 426 PSGKIQRFLLR 436
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
171-544 |
7.43e-29 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 120.33 E-value: 7.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 171 MEDEKF--KTQPDFT-SPAANKDEDVSLIVcSSGTTGLPKGVQLTQMNllATLDSQIQPTVIPMEE--VTLLTvIPWFHA 245
Cdd:PLN02479 173 IEYEKFleTGDPEFAwKPPADEWQSIALGY-TSGTTASPKGVVLHHRG--AYLMALSNALIWGMNEgaVYLWT-LPMFHC 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 246 FG-CLTLITTACVGARlVYLPKFEEKLFLSAIEKYRVMMAFMVPPLMVFLAKHPIVDKY-DLSSLM-VLLCGAAP----L 318
Cdd:PLN02479 249 NGwCFTWTLAALCGTN-ICLRQVTAKAIYSAIANYGVTHFCAAPVVLNTIVNAPKSETIlPLPRVVhVMTAGAAPppsvL 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 319 SRETEDQIKerigvpfIRQGYGLSES--------------TLSVLVQNDEFCKPGsvgVLKVGIYA-KVIDPDTGKLLGA 383
Cdd:PLN02479 328 FAMSEKGFR-------VTHTYGLSETygpstvcawkpewdSLPPEEQARLNARQG---VRYIGLEGlDVVDTKTMKPVPA 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 384 NER--GELCFKGDGIMKGYIGDTKSTQTAIKDGWLHTGDIGYYDDDFEFFIVDRIKELIKYKGYQVPPAEIEALLLTNDK 461
Cdd:PLN02479 398 DGKtmGEIVMRGNMVMKGYLKNPKANEEAFANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPA 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 462 IKDAAVIGKPDEEAGELPLAFV-----VKQANVQLTENEVIQFVNDNAsPAKRLRGGVIFvDEIPKNPSGKILRRILR-- 534
Cdd:PLN02479 478 VLEASVVARPDERWGESPCAFVtlkpgVDKSDEAALAEDIMKFCRERL-PAYWVPKSVVF-GPLPKTATGKIQKHVLRak 555
|
410
....*....|..
gi 21355181 535 --EMLKKQKSKL 544
Cdd:PLN02479 556 akEMGPVKKSRL 567
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
203-526 |
7.65e-29 |
|
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: 117.02 E-value: 7.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 203 TGLPKGVQLTQMNLLAtldsqiQPTVIPM-----EEVTLLTVIPWFHAFGCLTLITTACVGARLVYLPKFEEKLFLSAIE 277
Cdd:cd17636 12 SGRPNGALLSHQALLA------QALVLAVlqaidEGTVFLNSGPLFHIGTLMFTLATFHAGGTNVFVRRVDAEEVLELIE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 278 KYRVMMAFMVPPLMVFLAKHPIVDKYDLSSLMvllcgAAPLSRETEDQIKERIGvPFIRQGYGLSESTLSVLVQNDEFCK 357
Cdd:cd17636 86 AERCTHAFLLPPTIDQIVELNADGLYDLSSLR-----SSPAAPEWNDMATVDTS-PWGRKPGGYGQTEVMGLATFAALGG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 358 PGSVGVLKVGIYAKV--IDPDtGKLLGANERGELCFKGDGIMKGYIGDTKSTQTAIKDGWLHTGDIGYYDDDFEFFIVDR 435
Cdd:cd17636 160 GAIGGAGRPSPLVQVriLDED-GREVPDGEVGEIVARGPTVMAGYWNRPEVNARRTRGGWHHTNDLGRREPDGSLSFVGP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 436 IKELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGELPLAFVVKQANVQLTENEVIQFVNDNASPAKRLRgGVI 515
Cdd:cd17636 239 KTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPGASVTEAELIEHCRARIASYKKPK-SVE 317
|
330
....*....|.
gi 21355181 516 FVDEIPKNPSG 526
Cdd:cd17636 318 FADALPRTAGG 328
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
64-537 |
1.19e-28 |
|
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: 118.80 E-value: 1.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 64 RLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREVDHAINLSKPKIIFASkiTIDRVAKVAs 143
Cdd:cd05918 36 RLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLDPSHPLQRLQEILQDTGAKVVLTS--SPSDAAYVI- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 144 knkfvkgiialsgtskkfkniydlkelmedekfktqpdFTSpaankdedvslivcssGTTGLPKGVQLTQMNLLATLDSQ 223
Cdd:cd05918 113 --------------------------------------FTS----------------GSTGKPKGVVIEHRALSTSALAH 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 224 IQPtvIPMEEVT-LLtvipWF--HAFG------CLTLITTACV-----GARLVYLPKFeeklflsaIEKYRVMMAFMVPP 289
Cdd:cd05918 139 GRA--LGLTSESrVL----QFasYTFDvsileiFTTLAAGGCLcipseEDRLNDLAGF--------INRLRVTWAFLTPS 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 290 LMvflakhPIVDKYDLSSLMVLLCGAAPLSRETEDQIKERIGVpfiRQGYGLSEST-LSVLVQNDEFCKPGSVGvLKVGI 368
Cdd:cd05918 205 VA------RLLDPEDVPSLRTLVLGGEALTQSDVDTWADRVRL---INAYGPAECTiAATVSPVVPSTDPRNIG-RPLGA 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 369 YAKVIDPDT-GKLLGANERGELCFKGDGIMKGYIGDTKSTQTA-IKD-GWLH------------TGDIGYYDDDFEFFIV 433
Cdd:cd05918 275 TCWVVDPDNhDRLVPIGAVGELLIEGPILARGYLNDPEKTAAAfIEDpAWLKqegsgrgrrlyrTGDLVRYNPDGSLEYV 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 434 DRIKELIKYKGYQVPPAEIEA---LLLTNDKIKDAAVIGKPDEEAGELPLAFVV--KQANVQLTENEVIQFVNDNASP-A 507
Cdd:cd05918 355 GRKDTQVKIRGQRVELGEIEHhlrQSLPGAKEVVVEVVKPKDGSSSPQLVAFVVldGSSSGSGDGDSLFLEPSDEFRAlV 434
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 21355181 508 KRLRGGV-------------IFVDEIPKNPSGKILRRILREML 537
Cdd:cd05918 435 AELRSKLrqrlpsymvpsvfLPLSHLPLTASGKIDRRALRELA 477
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
178-535 |
1.49e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 119.40 E-value: 1.49e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 178 TQPDFTSPAAnkdEDVSLIVCSSGTTGLPKGVQLTQMNLLATLDSQIQPTVIPMEEVTLLTvIPWFHAFGCLTLITTA-C 256
Cdd:PRK07867 142 AEPPFRVADP---DDLFMLIFTSGTSGDPKAVRCTHRKVASAGVMLAQRFGLGPDDVCYVS-MPLFHSNAVMAGWAVAlA 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 257 VGARLVYLPKFEEKLFLSAIEKYRVMMAFMV-PPLMVFLAKHPIVDKYDLSSLMVLLCGAAPLSRETedqIKERIGVPFI 335
Cdd:PRK07867 218 AGASIALRRKFSASGFLPDVRRYGATYANYVgKPLSYVLATPERPDDADNPLRIVYGNEGAPGDIAR---FARRFGCVVV 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 336 rQGYGLSEstLSVLVQNDEFCKPGSVGVLKVGIyaKVIDPDTGK-----------LLGANER-GELC-FKGDGIMKGYIG 402
Cdd:PRK07867 295 -DGFGSTE--GGVAITRTPDTPPGALGPLPPGV--AIVDPDTGTecppaedadgrLLNADEAiGELVnTAGPGGFEGYYN 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 403 DTKSTQTAIKDGWLHTGDIGYYDDDFEFFIVDRIKELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGELPLAF 482
Cdd:PRK07867 370 DPEADAERMRGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVMAA 449
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 21355181 483 VVKQANVQLTENEVIQFV--NDNASPaKRLRGGVIFVDEIPKNPSGKILRRILRE 535
Cdd:PRK07867 450 LVLAPGAKFDPDAFAEFLaaQPDLGP-KQWPSYVRVCAELPRTATFKVLKRQLSA 503
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
64-535 |
2.95e-28 |
|
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: 119.96 E-value: 2.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 64 RLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTY-SDReVDHAINLSKPKIIFASKITIDRVAKVA 142
Cdd:COG1020 513 RLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYpAER-LAYMLEDAGARLVLTQSALAARLPELG 591
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 143 SKnkfvkgIIALsgtskkfkniydlkelmEDEKFKTQPDFTSPAANKDEDVSLIVCSSGTTGLPKGVQLTQMNLLATLDS 222
Cdd:COG1020 592 VP------VLAL-----------------DALALAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAW 648
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 223 QIQPTVIPMEEVTLLtvipwFHAFG--------CLTLittaCVGARLVYLPKFEEK---LFLSAIEKYRVMMAFMVPPLM 291
Cdd:COG1020 649 MQRRYGLGPGDRVLQ-----FASLSfdasvweiFGAL----LSGATLVLAPPEARRdpaALAELLARHRVTVLNLTPSLL 719
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 292 -VFLAkhpiVDKYDLSSLMVLLCGAAPLSRETEDQIKERI-GVPFIrQGYGLSE----STLSVLVQNDEFCKPGSVG--V 363
Cdd:COG1020 720 rALLD----AAPEALPSLRLVLVGGEALPPELVRRWRARLpGARLV-NLYGPTEttvdSTYYEVTPPDADGGSVPIGrpI 794
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 364 LKVGIYakVIDPDtGKLLGANERGELCFKGDGIMKGYIGDtkSTQTA---IKDGWLH-------TGDIGYYDDD--FEFf 431
Cdd:COG1020 795 ANTRVY--VLDAH-LQPVPVGVPGELYIGGAGLARGYLNR--PELTAerfVADPFGFpgarlyrTGDLARWLPDgnLEF- 868
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 432 iVDRIKELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGELpLAFVVKQANVQLTENEVIQFVNDNASPAKRLR 511
Cdd:COG1020 869 -LGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKR-LVAYVVPEAGAAAAAALLRLALALLLPPYMVP 946
|
490 500
....*....|....*....|....
gi 21355181 512 GGVIFVDEIPKNPSGKILRRILRE 535
Cdd:COG1020 947 AAVVLLLPLPLTGNGKLDRLALPA 970
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
61-469 |
4.47e-28 |
|
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: 117.07 E-value: 4.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 61 SIVRLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREVDHAINLSKPKIIFASkitidrvak 140
Cdd:cd17640 14 EILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALVVE--------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 141 vasknkfvkgiialsgtskkfkniydlkelmedekfktqpdftspaaNKDEDVSLIVCSSGTTGLPKGVQLTQMNLLATL 220
Cdd:cd17640 85 -----------------------------------------------NDSDDLATIIYTSGTTGNPKGVMLTHANLLHQI 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 221 DS-----QIQPTVIpmeevtLLTVIPWFHAFGCL---TLITTACVGA-----------------RLVYLPKFEEKLFLSA 275
Cdd:cd17640 118 RSlsdivPPQPGDR------FLSILPIWHSYERSaeyFIFACGCSQAytsirtlkddlkrvkphYIVSVPRLWESLYSGI 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 276 IEKYRVMmafmvPPLMVFLAKHPIVdkydLSSLMVLLCGAAPLSRETeDQIKERIGVPfIRQGYGLSEstLSVLVQNDEF 355
Cdd:cd17640 192 QKQVSKS-----SPIKQFLFLFFLS----GGIFKFGISGGGALPPHV-DTFFEAIGIE-VLNGYGLTE--TSPVVSARRL 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 356 CKP--GSVGVLKVGIYAKVIDPDTGKLLGANERGELCFKGDGIMKGYIGDTKSTQTAI-KDGWLHTGDIGYYDDDFEFFI 432
Cdd:cd17640 259 KCNvrGSVGRPLPGTEIKIVDPEGNVVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLdSDGWFNTGDLGWLTCGGELVL 338
|
410 420 430
....*....|....*....|....*....|....*...
gi 21355181 433 VDRIKELIKYK-GYQVPPAEIEALLLTNDKIKDAAVIG 469
Cdd:cd17640 339 TGRAKDTIVLSnGENVEPQPIEEALMRSPFIEQIMVVG 376
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
190-538 |
1.45e-27 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 116.25 E-value: 1.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 190 DEDVSLIVCSSGTTGLPKGVQLTQMNLLATLDSQIQPTVIPMEEVTLLTVIPWFHAFGCLTLITTA-CVGARLVYLPKFE 268
Cdd:PRK07768 151 EDDLALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEFDVETDVMVSWLPLFHDMGMVGFLTVPmYFGAELVKVTPMD 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 269 eklFLSA-------IEKYRVMM----AFMVPPLMVFLAKHPIVDKYDLSSLMVLLCGAAPLSRET-EDQIKEriGVPF-- 334
Cdd:PRK07768 231 ---FLRDpllwaelISKYRGTMtaapNFAYALLARRLRRQAKPGAFDLSSLRFALNGAEPIDPADvEDLLDA--GARFgl 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 335 ----IRQGYGLSESTLSV-----------------LVQNDEFCKPGSVGVLKV---------GIYAKVIDPDtGKLLGAN 384
Cdd:PRK07768 306 rpeaILPAYGMAEATLAVsfspcgaglvvdevdadLLAALRRAVPATKGNTRRlatlgpplpGLEVRVVDED-GQVLPPR 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 385 ERGELCFKGDGIMKGYI--GDTKSTQTAikDGWLHTGDIGYYDDDFEFFIVDRIKELIKYKGYQVPPAEIEALLLTNDKI 462
Cdd:PRK07768 385 GVGVIELRGESVTPGYLtmDGFIPAQDA--DGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGV 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 463 K--DAAVIGKPDEEAGElPLAFVVK------QANVQLTENEVIQFVNDN--ASPAKRLrggVIFVDEIPKNPSGKILRRI 532
Cdd:PRK07768 463 RpgNAVAVRLDAGHSRE-GFAVAVEsnafedPAEVRRIRHQVAHEVVAEvgVRPRNVV---VLGPGSIPKTPSGKLRRAN 538
|
....*.
gi 21355181 533 LREMLK 538
Cdd:PRK07768 539 AAELVT 544
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
51-519 |
3.16e-27 |
|
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: 115.26 E-value: 3.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 51 VEYSASFMHKSIVRLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREVDHAINLSKPKIIFA 130
Cdd:cd05932 5 VEFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 131 SKITidrvAKVASKNKFVKGIIALSgtskkfknIYDLKELMEDEKFKT----QPDFTSPAANKDEDVSLIVCSSGTTGLP 206
Cdd:cd05932 85 GKLD----DWKAMAPGVPEGLISIS--------LPPPSAANCQYQWDDliaqHPPLEERPTRFPEQLATLIYTSGTTGQP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 207 KGVQLTQMNLLATLDSQIQpTVIPMEEVTLLTVIPWFHAFGCLTLITTACVGARLVYlpkFEEKL--FLSAIEKYRVMMA 284
Cdd:cd05932 153 KGVMLTFGSFAWAAQAGIE-HIGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVA---FAESLdtFVEDVQRARPTLF 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 285 FMVP-------------------------PLMVFLAKHPIVDKYDLSSLMVLLCGAAPLSRETEDQIKeRIGVPfIRQGY 339
Cdd:cd05932 229 FSVPrlwtkfqqgvqdkipqqklnlllkiPVVNSLVKRKVLKGLGLDQCRLAGCGSAPVPPALLEWYR-SLGLN-ILEAY 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 340 GLSE----STLSVLVQNdefcKPGSVGVLKVGIYAKvIDPDtgkllganerGELCFKGDGIMKGYIGDTKSTQTAI-KDG 414
Cdd:cd05932 307 GMTEnfaySHLNYPGRD----KIGTVGNAGPGVEVR-ISED----------GEILVRSPALMMGYYKDPEATAEAFtADG 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 415 WLHTGDIGYYDDDFEFFIVDRIKELIKY-KGYQVPPAEIEALLLTNDKIKDAAVIGK----------PDEEAGELPLAFV 483
Cdd:cd05932 372 FLRTGDKGELDADGNLTITGRVKDIFKTsKGKYVAPAPIENKLAEHDRVEMVCVIGSglpaplalvvLSEEARLRADAFA 451
|
490 500 510
....*....|....*....|....*....|....*.
gi 21355181 484 vkQANVQLTENEVIQFVNDNASPAKRLRGGVIFVDE 519
Cdd:cd05932 452 --RAELEASLRAHLARVNSTLDSHEQLAGIVVVKDP 485
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
53-534 |
6.31e-27 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 115.05 E-value: 6.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 53 YSASFMHKSIVRLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREVDHAINLSKPKIIfask 132
Cdd:PRK10524 85 YTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLACARIGAIHSVVFGGFASHSLAARIDDAKPVLI---- 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 133 ITID---RVAKVASKNKFVKGIIALSGTSKKfkniydlKELMEDE---KFKTQP----DFTS-PAANKDEDV-------- 193
Cdd:PRK10524 161 VSADagsRGGKVVPYKPLLDEAIALAQHKPR-------HVLLVDRglaPMARVAgrdvDYATlRAQHLGARVpvewlesn 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 194 --SLIVCSSGTTGLPKGVQLT----QMNLLATLDsqiqptvipmeevtlltvipwfHAFGCL---TLITTACVG------ 258
Cdd:PRK10524 234 epSYILYTSGTTGKPKGVQRDtggyAVALATSMD----------------------TIFGGKageTFFCASDIGwvvghs 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 259 -----------ARLVY--LP-KFEEKLFLSAIEKYRVMMAFMVPPLMVFLAKHP--IVDKYDLSSLMVLLCGAAPLSRET 322
Cdd:PRK10524 292 yivyapllagmATIMYegLPtRPDAGIWWRIVEKYKVNRMFSAPTAIRVLKKQDpaLLRKHDLSSLRALFLAGEPLDEPT 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 323 EDQIKERIGVPFIrQGYGLSESTLSVL-VQN---DEFCKPGSVGVLKVGIYAKVIDPDTGKLLGANERGELCFKGD---G 395
Cdd:PRK10524 372 ASWISEALGVPVI-DNYWQTETGWPILaIARgveDRPTRLGSPGVPMYGYNVKLLNEVTGEPCGPNEKGVLVIEGPlppG 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 396 IMKGYIGD----TKSTQTAIKDGWLHTGDIGYYDDDFEFFIVDRIKELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKP 471
Cdd:PRK10524 451 CMQTVWGDddrfVKTYWSLFGRQVYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVK 530
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21355181 472 DEEAGELPLAFVV-KQANVQLT-------ENEVIQFVNDN----ASPAKrlrggVIFVDEIPKNPSGKILRRILR 534
Cdd:PRK10524 531 DALKGQVAVAFVVpKDSDSLADrearlalEKEIMALVDSQlgavARPAR-----VWFVSALPKTRSGKLLRRAIQ 600
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
10-469 |
1.22e-26 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 114.20 E-value: 1.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 10 IVYGGPVTERQAQDS-RSLGQYILDKYKSFGDRTVLVDavNGVEYSASFMHKSIVRLAYILQKLGVKQNDVVGLSSENSV 88
Cdd:PRK08279 21 ILRGLKRTALITPDSkRSLGDVFEEAAARHPDRPALLF--EDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 89 NFALAMFAGLAVGATVAPLNVTYSDREVDHAINLSKPKIIFASKITIDRVAKVASKNKFVKGIIALSGTSKKFKNIY-DL 167
Cdd:PRK08279 99 EYLAAWLGLAKLGAVVALLNTQQRGAVLAHSLNLVDAKHLIVGEELVEAFEEARADLARPPRLWVAGGDTLDDPEGYeDL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 168 KELMEdekfkTQPDfTSPAANKD---EDVSLIVCSSGTTGLPKGVQLTQMNLLATLDSQIQPTVIPMEEVtLLTVIPWFH 244
Cdd:PRK08279 179 AAAAA-----GAPT-TNPASRSGvtaKDTAFYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLTPDDV-LYCCLPLYH 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 245 AFGCLTLITTA-CVGARLVYLPKFEEKLFLSAIEKYRVmMAFM-VPPLMVFLAKHPIVDKyDLSSLMVLLCGAApLSRET 322
Cdd:PRK08279 252 NTGGTVAWSSVlAAGATLALRRKFSASRFWDDVRRYRA-TAFQyIGELCRYLLNQPPKPT-DRDHRLRLMIGNG-LRPDI 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 323 EDQIKERIGVPFIRQGYGLSESTLSVLvqnDEFCKPGSVGVLKVGI---YAKV-IDPDTGKLL-GANERGELCFKGD-GI 396
Cdd:PRK08279 329 WDEFQQRFGIPRILEFYAASEGNVGFI---NVFNFDGTVGRVPLWLahpYAIVkYDVDTGEPVrDADGRCIKVKPGEvGL 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 397 MKGYIGD-------TKSTQTAIK---------DGWLHTGDIGYYDDDFEFFIVDRIKELIKYKGYQVPPAEIEALLLTND 460
Cdd:PRK08279 406 LIGRITDrgpfdgyTDPEASEKKilrdvfkkgDAWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVATTEVENALSGFP 485
|
....*....
gi 21355181 461 KIKDAAVIG 469
Cdd:PRK08279 486 GVEEAVVYG 494
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
39-533 |
1.49e-26 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.
Pssm-ID: 341281 [Multi-domain] Cd Length: 470 Bit Score: 112.77 E-value: 1.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 39 GDRTVLVDavNGVEYSASFMHKSIVRLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREVDH 118
Cdd:cd12116 1 PDATAVRD--DDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 119 AINLSKPKIIFASKITIDRVAKVASKNKFVKGIIALSGTSkkfkniydlkelmedekfktqpdftSPAANKDEDVSLIVC 198
Cdd:cd12116 79 ILEDAEPALVLTDDALPDRLPAGLPVLLLALAAAAAAPAA-------------------------PRTPVSPDDLAYVIY 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 199 SSGTTGLPKGVQLTQMNLLATLDSQIQ-PTVIPMEEVTLLTVIpwfhAF--GCLTLITTACVGARLVYLP----KFEEKL 271
Cdd:cd12116 134 TSGSTGRPKGVVVSHRNLVNFLHSMRErLGLGPGDRLLAVTTY----AFdiSLLELLLPLLAGARVVIAPretqRDPEAL 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 272 fLSAIEKYRVMMAFMVPPLMVFLAKhpiVDKYDLSSLMvLLCGAAPLSRETEDQIKERIGVpfIRQGYGLSESTL-SVLV 350
Cdd:cd12116 210 -ARLIEAHSITVMQATPATWRMLLD---AGWQGRAGLT-ALCGGEALPPDLAARLLSRVGS--LWNLYGPTETTIwSTAA 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 351 QNDEFCKPGSVG--VLKVGIYakVIDPDtGKLLGANERGELCFKGDGIMKGYIGDTKSTQTAIKDG--------WLHTGD 420
Cdd:cd12116 283 RVTAAAGPIPIGrpLANTQVY--VLDAA-LRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDpfagpgsrLYRTGD 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 421 IGYYDDDFEFFIVDRIKELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGELpLAFVVKQANVQLTENEVIQFV 500
Cdd:cd12116 360 LVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGGDRRL-VAYVVLKAGAAPDAAALRAHL 438
|
490 500 510
....*....|....*....|....*....|...
gi 21355181 501 NDnASPAKRLRGGVIFVDEIPKNPSGKILRRIL 533
Cdd:cd12116 439 RA-TLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
182-484 |
2.24e-26 |
|
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: 112.69 E-value: 2.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 182 FTSPaanKDEDVSLIVCSSGTTGLPKGVQLTQMNLLATLDSQIQPTVIPMEEV-TLLTVIPWFHAF-----------GC- 248
Cdd:cd17639 82 FTDG---KPDDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDRVPELLGPDdRYLAYLPLAHIFelaaenvclyrGGt 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 249 ------LTLITTACVG----------------------------ARLVYLPKFEEKLFLSAIE-KYRVMMAFMVPPL--- 290
Cdd:cd17639 159 igygspRTLTDKSKRGckgdltefkptlmvgvpaiwdtirkgvlAKLNPMGGLKRTLFWTAYQsKLKALKEGPGTPLlde 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 291 MVFlAKhpiVDKYDLSSLMVLLCGAAPLSRETEDQIKErIGVPFIrQGYGLSESTLSVLVQNDEFCKPGSVGVLKVGIYA 370
Cdd:cd17639 239 LVF-KK---VRAALGGRLRYMLSGGAPLSADTQEFLNI-VLCPVI-QGYGLTETCAGGTVQDPGDLETGRVGPPLPCCEI 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 371 KVID-PDTGKLLGANE-RGELCFKGDGIMKGYIGDTKSTQTAIK-DGWLHTGDIGYYDDDFEFFIVDRIKELIKYK-GYQ 446
Cdd:cd17639 313 KLVDwEEGGYSTDKPPpRGEILIRGPNVFKGYYKNPEKTKEAFDgDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQnGEY 392
|
330 340 350
....*....|....*....|....*....|....*...
gi 21355181 447 VPPAEIEALLLTNDKIKDAAVIGKPDEEAgelPLAFVV 484
Cdd:cd17639 393 IALEKLESIYRSNPLVNNICVYADPDKSY---PVAIVV 427
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
65-535 |
2.41e-26 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 112.95 E-value: 2.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 65 LAYILQ-KLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREVDHAINLSKPKIIFASKITIDRVAKVAS 143
Cdd:PRK05620 51 LAHALHdELGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIVADPRLAEQLGEILK 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 144 KNKFVKGIIALSGTSKKFK--------NIYDLKELMeDEKfktQPDFTSPaaNKDEDVSLIVC-SSGTTGLPKGVQ---- 210
Cdd:PRK05620 131 ECPCVRAVVFIGPSDADSAaahmpegiKVYSYEALL-DGR---STVYDWP--ELDETTAAAICySTGTTGAPKGVVyshr 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 211 ---LTQMNLLATLDSQIQptvipmEEVTLLTVIPWFHAFGCLTLITTACVGARLVYL-PKFEEKLFLSAIEKYRVMMAFM 286
Cdd:PRK05620 205 slyLQSLSLRTTDSLAVT------HGESFLCCVPIYHVLSWGVPLAAFMSGTPLVFPgPDLSAPTLAKIIATAMPRVAHG 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 287 VPP----LMVFLAKHPIvdkyDLSSLMVLLCGAAPLSRETEDQIKERIGVPFIrQGYGLSESTLSVLVQNDEFCKPG--- 359
Cdd:PRK05620 279 VPTlwiqLMVHYLKNPP----ERMSLQEIYVGGSAVPPILIKAWEERYGVDVV-HVWGMTETSPVGTVARPPSGVSGear 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 360 -----SVGVLKVGIYAKVIDpdTGKLLGANER--GELCFKGDGIMKGY-------------------IGDTKSTQTAikD 413
Cdd:PRK05620 354 wayrvSQGRFPASLEYRIVN--DGQVMESTDRneGEIQVRGNWVTASYyhspteegggaastfrgedVEDANDRFTA--D 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 414 GWLHTGDIGYYDDDFEFFIVDRIKELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGELPLAFVVKQANVQLTE 493
Cdd:PRK05620 430 GWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLAVTVLAPGIEPTR 509
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 21355181 494 NEVIQFvndnaspAKRLRGGV---------IFVDEIPKNPSGKI----LRRILRE 535
Cdd:PRK05620 510 ETAERL-------RDQLRDRLpnwmlpeywTFVDEIDKTSVGKFdkkdLRQHLAD 557
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
191-527 |
3.16e-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: 341248 [Multi-domain] Cd Length: 364 Bit Score: 110.16 E-value: 3.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 191 EDVSLIVCSSGTTGLPKGVQLTQMNLLATL-------------DSQIQPTVIPMEEVTLLTVIPWFHAFGCLTLITTACV 257
Cdd:cd05924 3 ADDLYILYTGGTTGMPKGVMWRQEDIFRMLmggadfgtgeftpSEDAHKAAAAAAGTVMFPAPPLMHGTGSWTAFGGLLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 258 GARLVYL-PKFEEKLFLSAIEKYRVMMAFMVPPLMvflAKhPIVDK------YDLSSLMVLLCGAAPLSRETEDQIKERI 330
Cdd:cd05924 83 GQTVVLPdDRFDPEEVWRTIEKHKVTSMTIVGDAM---AR-PLIDAlrdagpYDLSSLFAISSGGALLSPEVKQGLLELV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 331 GVPFIRQGYGLSESTLSVLVQNDEfcKPGSVGVLK-VGIYAKVIDPDTGKLLGANERGELCFKGDGIMKGYIGDTKSTQT 409
Cdd:cd05924 159 PNITLVDAFGSSETGFTGSGHSAG--SGPETGPFTrANPDTVVLDDDGRVVPPGSGGVGWIARRGHIPLGYYGDEAKTAE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 410 AIK--DG--WLHTGDIGYYDDDFEFFIVDRIKELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGELPLAFVVK 485
Cdd:cd05924 237 TFPevDGvrYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQEVVAVVQL 316
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 21355181 486 QANVQLTENEVIQFVNDNASPAKRLRgGVIFVDEIPKNPSGK 527
Cdd:cd05924 317 REGAGVDLEELREHCRTRIARYKLPK-QVVFVDEIERSPAGK 357
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
62-470 |
5.70e-26 |
|
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: 111.75 E-value: 5.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 62 IVRLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREVDHAINLSKPKIIFAS-KITIDRVAK 140
Cdd:cd17641 21 VRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIAEdEEQVDKLLE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 141 VASKNKFVKGIIALS--GTSKKFKN-IYDLKELME--DEKFKTQPDFTSP--AANKDEDVSLIVCSSGTTGLPKGVQLTQ 213
Cdd:cd17641 101 IADRIPSVRYVIYCDprGMRKYDDPrLISFEDVVAlgRALDRRDPGLYERevAAGKGEDVAVLCTTSGTTGKPKLAMLSH 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 214 MNLLAT-LDSQIQPTVIPMEEVTLLTVIPW----FHAFGcLTLITTACV----------------GARLVYLP------- 265
Cdd:cd17641 181 GNFLGHcAAYLAADPLGPGDEYVSVLPLPWigeqMYSVG-QALVCGFIVnfpeepetmmedlreiGPTFVLLPprvwegi 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 266 ------------KFEEKLFLSAIEK-YRVM---MAFMVPPLMVFLAK--------HPIVDKYDLSSLMVLLCGAAPLSRE 321
Cdd:cd17641 260 aadvrarmmdatPFKRFMFELGMKLgLRALdrgKRGRPVSLWLRLASwladallfRPLRDRLGFSRLRSAATGGAALGPD 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 322 TEDQIKErIGVPfIRQGYGLSESTLSVLVQNDEFCKPGSVGVlkvgiyakvidPDTGKLLGANERGELCFKGDGIMKGYI 401
Cdd:cd17641 340 TFRFFHA-IGVP-LKQLYGQTELAGAYTVHRDGDVDPDTVGV-----------PFPGTEVRIDEVGEILVRSPGVFVGYY 406
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21355181 402 GDTKSTQTAI-KDGWLHTGDIGYYDDDFEFFIVDRIKELIK-YKGYQVPPAEIEALLLTNDKIKDAAVIGK 470
Cdd:cd17641 407 KNPEATAEDFdEDGWLHTGDAGYFKENGHLVVIDRAKDVGTtSDGTRFSPQFIENKLKFSPYIAEAVVLGA 477
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
68-544 |
7.44e-26 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 111.76 E-value: 7.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 68 ILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREVDHAINLSKPKIIFASKITI--DRVAKVASKn 145
Cdd:PTZ00237 108 VLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGATHCVLFDGYSVKSLIDRIETITPKLIITTNYGIlnDEIITFTPN- 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 146 kfVKGIIALSgTSKKFKNIYDLKELMEDEKFKTQPDFTSPAAN-----------KDEDVS--------------LIVCSS 200
Cdd:PTZ00237 187 --LKEAIELS-TFKPSNVITLFRNDITSESDLKKIETIPTIPNtlswydeikkiKENNQSpfyeyvpvesshplYILYTS 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 201 GTTGLPKGVQLTQMNLLATLDSQIQPTVIPMEEVTLL--TVIPW--FHAF--GCLTLITTACVGARLVYLPKFEEKLFLS 274
Cdd:PTZ00237 264 GTTGNSKAVVRSNGPHLVGLKYYWRSIIEKDIPTVVFshSSIGWvsFHGFlyGSLSLGNTFVMFEGGIIKNKHIEDDLWN 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 275 AIEKYRVMMAFMVPPLMVFLAKHP-----IVDKYDLSSLMVLLCGAAPLSRETEDQIKERIGVPFIRqGYGLSESTLSVL 349
Cdd:PTZ00237 344 TIEKHKVTHTLTLPKTIRYLIKTDpeatiIRSKYDLSNLKEIWCGGEVIEESIPEYIENKLKIKSSR-GYGQTEIGITYL 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 350 VQNDEFCKP-GSVGVLKVGIYAKVIDPDtGKLLGANERGELCFK----GDGIMKGYIGDTKSTQTAIK-DGWLHTGDIGY 423
Cdd:PTZ00237 423 YCYGHINIPyNATGVPSIFIKPSILSED-GKELNVNEIGEVAFKlpmpPSFATTFYKNDEKFKQLFSKfPGYYNSGDLGF 501
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 424 YDDDFEFFIVDRIKELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGELPLAF-VVKQAN-------VQLtENE 495
Cdd:PTZ00237 502 KDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPIGLlVLKQDQsnqsidlNKL-KNE 580
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 21355181 496 VIQFVNDNASPAKRLRgGVIFVDEIPKNPSGKILRRILREMLKKQKSKL 544
Cdd:PTZ00237 581 INNIITQDIESLAVLR-KIIIVNQLPKTKTGKIPRQIISKFLNDSNYQL 628
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
40-533 |
8.65e-26 |
|
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: 110.10 E-value: 8.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 40 DRTVLVDAVNGVEYSAsfMHKSIVRLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREVDHA 119
Cdd:cd12115 14 DAIALVCGDESLTYAE--LNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPERLRFI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 120 INLSKPKIIFaskitidrvakvasknkfvkgiialsgtskkfkniydlkelmedekfkTQPDftspaankdeDVSLIVCS 199
Cdd:cd12115 92 LEDAQARLVL------------------------------------------------TDPD----------DLAYVIYT 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 200 SGTTGLPKGVQLTQMNLLATLdsQIQPTVIPMEEVT-LLTVIPWFHAFGCLTLITTACVGARLVyLPKFEEKLFLSAIEK 278
Cdd:cd12115 114 SGSTGRPKGVAIEHRNAAAFL--QWAAAAFSAEELAgVLASTSICFDLSVFELFGPLATGGKVV-LADNVLALPDLPAAA 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 279 yRVMMAFMVPPLMVFLAKHpivDKYDLSSLMVLLCGAaPLSRETEDQIKERIGVPFIRQGYGLSE----STLSVLVQNDE 354
Cdd:cd12115 191 -EVTLINTVPSAAAELLRH---DALPASVRVVNLAGE-PLPRDLVQRLYARLQVERVVNLYGPSEdttySTVAPVPPGAS 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 355 fcKPGSVGVLKVGIYAKVIDpDTGKLLGANERGELCFKGDGIMKGYIGDtkSTQTAIK---DGWL------HTGDIGYYD 425
Cdd:cd12115 266 --GEVSIGRPLANTQAYVLD-RALQPVPLGVPGELYIGGAGVARGYLGR--PGLTAERflpDPFGpgarlyRTGDLVRWR 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 426 DDFEFFIVDRIKELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGELPLAFVVKQANVQLTENEVIQFVNDNAs 505
Cdd:cd12115 341 PDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEPGAAGLVEDLRRHLGTRL- 419
|
490 500
....*....|....*....|....*...
gi 21355181 506 PAKRLRGGVIFVDEIPKNPSGKILRRIL 533
Cdd:cd12115 420 PAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
64-538 |
2.17e-25 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 109.80 E-value: 2.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 64 RLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREVDHAINLSKPKIIFASKITIDRVAKVAS 143
Cdd:PRK07008 51 QLAQALAALGVEPGDRVGTLAWNGYRHLEAYYGVSGSGAVCHTINPRLFPEQIAYIVNHAEDRYVLFDLTFLPLVDALAP 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 144 KNKFVKGIIALSGTSKKFKNIYDL---KELMEDEKfktqPDFTSPAAnkDEDVSLIVC-SSGTTGLPKGVQLTQMNLLAT 219
Cdd:PRK07008 131 QCPNVKGWVAMTDAAHLPAGSTPLlcyETLVGAQD----GDYDWPRF--DENQASSLCyTSGTTGNPKGALYSHRSTVLH 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 220 LDSQIQPTVIPMEEV-TLLTVIPWFH--AFGclTLITTACVGARLVYL-PKFEEKLFLSAIEKYRVMMAFMVPPLMVFLA 295
Cdd:PRK07008 205 AYGAALPDAMGLSARdAVLPVVPMFHvnAWG--LPYSAPLTGAKLVLPgPDLDGKSLYELIEAERVTFSAGVPTVWLGLL 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 296 KHPIVDKYDLSSLMVLLCG--AAPLSRETedQIKERIGVPFIrQGYGLSE----STLSVL----------VQNDEFCKPG 359
Cdd:PRK07008 283 NHMREAGLRFSTLRRTVIGgsACPPAMIR--TFEDEYGVEVI-HAWGMTEmsplGTLCKLkwkhsqlpldEQRKLLEKQG 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 360 SVgvlKVGIYAKVIDPDtGKLLGANER--GELCFKGDGIMKGYIgdtKSTQTAIKDGWLHTGDIGYYDDDFEFFIVDRIK 437
Cdd:PRK07008 360 RV---IYGVDMKIVGDD-GRELPWDGKafGDLQVRGPWVIDRYF---RGDASPLVDGWFPTGDVATIDADGFMQITDRSK 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 438 ELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGELPLAFVVKQANVQLTENEVIQFVNDNAspAK-RLRGGVIF 516
Cdd:PRK07008 433 DVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLVVVKRPGAEVTREELLAFYEGKV--AKwWIPDDVVF 510
|
490 500
....*....|....*....|..
gi 21355181 517 VDEIPKNPSGKILRRILREMLK 538
Cdd:PRK07008 511 VDAIPHTATGKLQKLKLREQFR 532
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
64-533 |
2.26e-25 |
|
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: 108.71 E-value: 2.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 64 RLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREVDHAINLSKPKIIFaskitidrvakvas 143
Cdd:cd17650 24 QLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYMLEDSGAKLLL-------------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 144 knkfvkgiialsgtskkfkniydlkelmedekfkTQPdftspaankdEDVSLIVCSSGTTGLPKGVQLTQMNLLAT---- 219
Cdd:cd17650 90 ----------------------------------TQP----------EDLAYVIYTSGTTGKPKGVMVEHRNVAHAahaw 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 220 -----LDSQiQPTVIPMEEVTlltvipwFHAFGClTLITTACVGARLVYLP---KFEEKLFLSAIEKYRVMMAFMVP--- 288
Cdd:cd17650 126 rreyeLDSF-PVRLLQMASFS-------FDVFAG-DFARSLLNGGTLVICPdevKLDPAALYDLILKSRITLMESTPali 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 289 -PLMVFLAKHpivdKYDLSSLMVLLCGAAPLSRETEDQIKERIGVPF-IRQGYGLSESTLSVLV---QNDEFCKPGSVGV 363
Cdd:cd17650 197 rPVMAYVYRN----GLDLSAMRLLIVGSDGCKAQDFKTLAARFGQGMrIINSYGVTEATIDSTYyeeGRDPLGDSANVPI 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 364 LK----VGIYakVIDPdTGKLLGANERGELCFKGDGIMKGYIGDTKSTQTAIKDGWL-------HTGDIGYYDDDFEFFI 432
Cdd:cd17650 273 GRplpnTAMY--VLDE-RLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFapgermyRTGDLARWRADGNVEL 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 433 VDRIKELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDeEAGELPL-AFVVKQANVQLteNEVIQFVNDNAsPAKRLR 511
Cdd:cd17650 350 LGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVRED-KGGEARLcAYVVAAATLNT--AELRAFLAKEL-PSYMIP 425
|
490 500
....*....|....*....|..
gi 21355181 512 GGVIFVDEIPKNPSGKILRRIL 533
Cdd:cd17650 426 SYYVQLDALPLTPNGKVDRRAL 447
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
191-536 |
2.37e-25 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 109.73 E-value: 2.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 191 EDVSLIVCSSGTTGLPKGVQLTQMNLLATLDSQIQPTVIPMEEVTLLtVIPWFHAFGCLTLITTA-CVGARLVYLPKFEE 269
Cdd:PRK13388 150 MDPFMLIFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLTRDDVCYV-SMPLFHSNAVMAGWAPAvASGAAVALPAKFSA 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 270 KLFLSAIEKYRV-MMAFMVPPLMVFLA--KHPivDKYDlsslmvllcgaAPLSR----ETEDQIKERIGVPF---IRQGY 339
Cdd:PRK13388 229 SGFLDDVRRYGAtYFNYVGKPLAYILAtpERP--DDAD-----------NPLRVafgnEASPRDIAEFSRRFgcqVEDGY 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 340 GLSEStlSVLVQNDEFCKPGSVGVLKVGIyaKVIDPDT------------GKLLGANER-GELCFK-GDGIMKGYIGDTK 405
Cdd:PRK13388 296 GSSEG--AVIVVREPGTPPGSIGRGAPGV--AIYNPETltecavarfdahGALLNADEAiGELVNTaGAGFFEGYYNNPE 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 406 STQTAIKDGWLHTGDIGYYDDDFEFFIVDRIKELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGELPLAFVVK 485
Cdd:PRK13388 372 ATAERMRHGMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVGDQVMAALVL 451
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 21355181 486 QANVQLTENEVIQFVNDNAS-PAKRLRGGVIFVDEIPKNPSGKILRRILREM 536
Cdd:PRK13388 452 RDGATFDPDAFAAFLAAQPDlGTKAWPRYVRIAADLPSTATNKVLKRELIAQ 503
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
20-536 |
3.95e-25 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 109.80 E-value: 3.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 20 QAQDSRSLGQYILDKYKSFGDRTVLVDAVNGVEYSASFMHKSIVRLAYILQKLGVkQNDVVGLSSENSVNFALAMFAGLA 99
Cdd:PRK08043 199 AVRPRETLYEALLSAQYRYGAGKPCIEDVNFTPDSYRKLLKKTLFVGRILEKYSV-EGERIGLMLPNATISAAVIFGASL 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 100 VGATVAPLNVTYSDREVDHAINLSKPKIIFASKITIDrvakvasknkfvKG-IIALSGTSKKFKNIY--DLK-ELMEDEK 175
Cdd:PRK08043 278 RRRIPAMMNYTAGVKGLTSAITAAEIKTIFTSRQFLD------------KGkLWHLPEQLTQVRWVYleDLKdDVTTADK 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 176 FKTQPDFTSPA----ANKDEDVSLIVCSSGTTGLPKGVQLTQMNLLATLDsQIQPTVIPMEEVTLLTVIPWFHAFGcLT- 250
Cdd:PRK08043 346 LWIFAHLLMPRlaqvKQQPEDAALILFTSGSEGHPKGVVHSHKSLLANVE-QIKTIADFTPNDRFMSALPLFHSFG-LTv 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 251 -LITTACVGARLVYLPkfeeklflSAIEkYRVmmafmVPPLM------------VFLAK-----HPivdkYDLSSLMVLL 312
Cdd:PRK08043 424 gLFTPLLTGAEVFLYP--------SPLH-YRI-----VPELVydrnctvlfgtsTFLGNyarfaNP----YDFARLRYVV 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 313 CGAAPLSRETEDQIKERIGVPfIRQGYGLSESTLSVLVQNDEFCKPGSVGVLKVGIYAKVIdpdtgKLLGANERGELCFK 392
Cdd:PRK08043 486 AGAEKLQESTKQLWQDKFGLR-ILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLL-----SVPGIEQGGRLQLK 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 393 GDGIMKGYI----------GDTKSTQTAIKDGWLHTGDIGYYDDDFEFFIVDRIKELIKYKGYQVPPAEIEALLLTNDKI 462
Cdd:PRK08043 560 GPNIMNGYLrvekpgvlevPTAENARGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPD 639
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21355181 463 KDAAVIGKPDEEAGElplAFVVKQANVQLTENEVIQFVNDNASPAKRLRGGVIFVDEIPKNPSGKILRRILREM 536
Cdd:PRK08043 640 KQHATAIKSDASKGE---ALVLFTTDSELTREKLQQYAREHGVPELAVPRDIRYLKQLPLLGSGKPDFVTLKSM 710
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
64-535 |
4.05e-25 |
|
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: 107.78 E-value: 4.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 64 RLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTY-SDReVDHAINLSKPKIIfaskitidrvakva 142
Cdd:cd17653 34 ALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLpSAR-IQAILRTSGATLL-------------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 143 sknkfvkgiialsgtskkfknIYdlkelmedekfktqpdftspaANKDEDVSLIVCSSGTTGLPKGVQLTQMNLL----- 217
Cdd:cd17653 99 ---------------------LT---------------------TDSPDDLAYIIFTSGSTGIPKGVMVPHRGVLnyvsq 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 218 --ATLDSQIQPTVIPMEEVtlltvipwfhAFGC--LTLITTACVGARLVylPKFEEKLFLSAIekyRVMMAFMVPPlmVF 293
Cdd:cd17653 137 ppARLDVGPGSRVAQVLSI----------AFDAciGEIFSTLCNGGTLV--LADPSDPFAHVA---RTVDALMSTP--SI 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 294 LAKhpiVDKYDLSSL-MVLLCGAAPlsreTEDQIKERIGVPFIRQGYGLSESTLSVLVQNDEFCKPGSVG--VLKVGIYa 370
Cdd:cd17653 200 LST---LSPQDFPNLkTIFLGGEAV----PPSLLDRWSPGRRLYNAYGPTECTISSTMTELLPGQPVTIGkpIPNSTCY- 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 371 kVIDPDTgKLLGANERGELCFKGDGIMKGYIGDTKSTQTAIK-----DGWLH--TGDIGYYDDDFEFFIVDRIKELIKYK 443
Cdd:cd17653 272 -ILDADL-QPVPEGVVGEICISGVQVARGYLGNPALTASKFVpdpfwPGSRMyrTGDYGRWTEDGGLEFLGREDNQVKVR 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 444 GYQVPPAEIEALLLTNDKikdaavigkpdeeagelplafVVKQANVQLTENEVIQFVN----DNASPAKRLR-------- 511
Cdd:cd17653 350 GFRINLEEIEEVVLQSQP---------------------EVTQAAAIVVNGRLVAFVTpetvDVDGLRSELAkhlpsyav 408
|
490 500
....*....|....*....|....*
gi 21355181 512 -GGVIFVDEIPKNPSGKILRRILRE 535
Cdd:cd17653 409 pDRIIALDSFPLTANGKVDRKALRE 433
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
58-469 |
9.09e-25 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 108.36 E-value: 9.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 58 MHKSIVRLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREVDHAINLSKPKIIFAskitidr 137
Cdd:PLN02430 82 VYEEVLQIGSALRASGAEPGSRVGIYGSNCPQWIVAMEACAAHSLICVPLYDTLGPGAVDYIVDHAEIDFVFV------- 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 138 vakvasKNKFVKGII-ALSGTSKKFKNIYDLKELMEDEKFKT-------------------QPDFTSPAanKDEDVSLIV 197
Cdd:PLN02430 155 ------QDKKIKELLePDCKSAKRLKAIVSFTSVTEEESDKAsqigvktyswidflhmgkeNPSETNPP--KPLDICTIM 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 198 CSSGTTGLPKGVQLTQMNLLATLDSqiqpTVIPMEEV--------TLLTVIPWFHAFGCLT----LITTACVG------- 258
Cdd:PLN02430 227 YTSGTSGDPKGVVLTHEAVATFVRG----VDLFMEQFedkmthddVYLSFLPLAHILDRMIeeyfFRKGASVGyyhgdln 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 259 -----------ARLVYLPKFEEKLFlSAIEK----------------YRVMMAFM--------VPPLMVFLAKHPIVDKY 303
Cdd:PLN02430 303 alrddlmelkpTLLAGVPRVFERIH-EGIQKalqelnprrrlifnalYKYKLAWMnrgyshkkASPMADFLAFRKVKAKL 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 304 DlSSLMVLLCGAAPLSRETEDQIKErIGVPFIRQGYGLSEST-LSVLVQNDEFCKPGSVGVlkVGIYAKV---------I 373
Cdd:PLN02430 382 G-GRLRLLISGGAPLSTEIEEFLRV-TSCAFVVQGYGLTETLgPTTLGFPDEMCMLGTVGA--PAVYNELrleevpemgY 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 374 DPdtgklLGANERGELCFKGDGIMKGYIGDTKSTQTAIKDGWLHTGDIGYYDDDFEFFIVDRIKELIKY-KGYQVPPAEI 452
Cdd:PLN02430 458 DP-----LGEPPRGEICVRGKCLFSGYYKNPELTEEVMKDGWFHTGDIGEILPNGVLKIIDRKKNLIKLsQGEYVALEYL 532
|
490
....*....|....*..
gi 21355181 453 EALLLTNDKIKDAAVIG 469
Cdd:PLN02430 533 ENVYGQNPIVEDIWVYG 549
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
64-533 |
9.87e-25 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 109.66 E-value: 9.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 64 RLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREVDHAINLSKPKIIFASKITIDRVAKVAs 143
Cdd:PRK12316 2040 RLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQRHLLERLPLPA- 2118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 144 knkfvkGIIALsgtskkfkniydlkELMEDEKFKTQPDfTSPAANKD-EDVSLIVCSSGTTGLPKGVQLTQMNLLATLDS 222
Cdd:PRK12316 2119 ------GVARL--------------PLDRDAEWADYPD-TAPAVQLAgENLAYVIYTSGSTGLPKGVAVSHGALVAHCQA 2177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 223 -----QIQPTVIPMEEVTLL---TVIPWFHAFgcltlittaCVGARLV------YLPkfeEKLFlSAIEKYRVMMAFMVP 288
Cdd:PRK12316 2178 ageryELSPADCELQFMSFSfdgAHEQWFHPL---------LNGARVLirddelWDP---EQLY-DEMERHGVTILDFPP 2244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 289 PLMVFLAKHPIVDKYDLSsLMVLLCGAAPLSRETEDQIKERIGVPFIRQGYGLSESTLSVLV---QNDEFCKPGSV--GV 363
Cdd:PRK12316 2245 VYLQQLAEHAERDGRPPA-VRVYCFGGEAVPAASLRLAWEALRPVYLFNGYGPTEAVVTPLLwkcRPQDPCGAAYVpiGR 2323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 364 LKVGIYAKVIDPDTgKLLGANERGELCFKGDGIMKGYIGdtKSTQTA---IKDGWLH-------TGDIGYYDDDFEFFIV 433
Cdd:PRK12316 2324 ALGNRRAYILDADL-NLLAPGMAGELYLGGEGLARGYLN--RPGLTAerfVPDPFSAsgerlyrTGDLARYRADGVVEYL 2400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 434 DRIKELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKpDEEAGELPLAFVVKQaNVQLTENEVIQFVNDNASPAKRLRGG 513
Cdd:PRK12316 2401 GRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQ-DGASGKQLVAYVVPD-DAAEDLLAELRAWLAARLPAYMVPAH 2478
|
490 500
....*....|....*....|
gi 21355181 514 VIFVDEIPKNPSGKILRRIL 533
Cdd:PRK12316 2479 WVVLERLPLNPNGKLDRKAL 2498
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
59-538 |
4.92e-23 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 103.00 E-value: 4.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 59 HKSIVRLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREVDHAINLSKPKIIFASKITIDRV 138
Cdd:PLN02861 84 YDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVSIAFVQESKISSI 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 139 AKVASK-NKFVKGIIALSGTSKKFKNiyDLKEL----MEDEKFKT--QPDFTSPAANKDeDVSLIVCSSGTTGLPKGVQL 211
Cdd:PLN02861 164 LSCLPKcSSNLKTIVSFGDVSSEQKE--EAEELgvscFSWEEFSLmgSLDCELPPKQKT-DICTIMYTSGTTGEPKGVIL 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 212 TQMNLLA---TLDSQIQPT-VIPMEEVTLLTVIPWFHAFGclTLITTACV---------GARLVYL-------------- 264
Cdd:PLN02861 241 TNRAIIAevlSTDHLLKVTdRVATEEDSYFSYLPLAHVYD--QVIETYCIskgasigfwQGDIRYLmedvqalkptifcg 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 265 -PKFEEKLFLSAIEK-----------YRVMMAFMVPPLMVFLAKH---PIVDKYDLSSLM--------VLLCGAAPLSRE 321
Cdd:PLN02861 319 vPRVYDRIYTGIMQKissggmlrkklFDFAYNYKLGNLRKGLKQEeasPRLDRLVFDKIKeglggrvrLLLSGAAPLPRH 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 322 TEDQIKErIGVPFIRQGYGLSESTLSVLVQ-NDEFCKPGSVGVLKVGIYAKVID-PDTG-KLLGANERGELCFKGDGIMK 398
Cdd:PLN02861 399 VEEFLRV-TSCSVLSQGYGLTESCGGCFTSiANVFSMVGTVGVPMTTIEARLESvPEMGyDALSDVPRGEICLRGNTLFS 477
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 399 GYIGDTKSTQTAIKDGWLHTGDIGYYDDDFEFFIVDRIKELIKY-KGYQVPPAEIEALLLTNDKIKDAAVIGKPDEeagE 477
Cdd:PLN02861 478 GYHKRQDLTEEVLIDGWFHTGDIGEWQPNGAMKIIDRKKNIFKLsQGEYVAVENLENTYSRCPLIASIWVYGNSFE---S 554
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21355181 478 LPLAFVV--KQANVQLTENEviQFVNDNASPAKRLRGGVIFVDEIpkNPSGKILRRILREMLK 538
Cdd:PLN02861 555 FLVAVVVpdRQALEDWAANN--NKTGDFKSLCKNLKARKYILDEL--NSTGKKLQLRGFEMLK 613
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
62-441 |
5.46e-23 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 103.18 E-value: 5.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 62 IVRLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREVDHAINLSKPKIIFASKITIDRVAKV 141
Cdd:PLN02614 89 VIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIVFVEEKKISELFKT 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 142 A-SKNKFVKGIIALSGTSKKFKN--------IYDLKELMedeKFKTQPDFTSPAaNKDEDVSLIVCSSGTTGLPKGVQLT 212
Cdd:PLN02614 169 CpNSTEYMKTVVSFGGVSREQKEeaetfglvIYAWDEFL---KLGEGKQYDLPI-KKKSDICTIMYTSGTTGDPKGVMIS 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 213 Q----------MNLLATLDSQIQptvipmEEVTLLTVIPWFHAFGCLTLITTACVGARLVYLpKFEEKLFLSAIEKYRVM 282
Cdd:PLN02614 245 NesivtliagvIRLLKSANAALT------VKDVYLSYLPLAHIFDRVIEECFIQHGAAIGFW-RGDVKLLIEDLGELKPT 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 283 MAFMVPPLM--------------------VF-----------------LAKHPIVDKYDLS--------SLMVLLCGAAP 317
Cdd:PLN02614 318 IFCAVPRVLdrvysglqkklsdggflkkfVFdsafsykfgnmkkgqshVEASPLCDKLVFNkvkqglggNVRIILSGAAP 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 318 LSRETEDQIKErIGVPFIRQGYGLSESTLSVLVQ-NDEFCKPGSVG--VLKVGIYAKVIDPDTGKLLGANERGELCFKGD 394
Cdd:PLN02614 398 LASHVESFLRV-VACCHVLQGYGLTESCAGTFVSlPDELDMLGTVGppVPNVDIRLESVPEMEYDALASTPRGEICIRGK 476
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 21355181 395 GIMKGYIGDTKSTQTAIKDGWLHTGDIGYYDDDFEFFIVDRIKELIK 441
Cdd:PLN02614 477 TLFSGYYKREDLTKEVLIDGWLHTGDVGEWQPNGSMKIIDRKKNIFK 523
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
64-469 |
7.29e-23 |
|
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: 101.28 E-value: 7.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 64 RLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREVDHAINLSKPKIIFAskitidrvakvas 143
Cdd:cd05940 15 RYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLVV------------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 144 knkfvkgiialsgtskkfkniydlkelmedekfktqpdftspaankdeDVSLIVCSSGTTGLPKGVQLTQMNLLATLdSQ 223
Cdd:cd05940 82 ------------------------------------------------DAALYIYTSGTTGLPKAAIISHRRAWRGG-AF 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 224 IQPTVIPMEEVTLLTVIPWFHAFGcLTLITTAC--VGARLVYLPKFEEKLFLSAIEKYRVMMAFMVPPLMVFLAKHPIVD 301
Cdd:cd05940 113 FAGSGGALPSDVLYTCLPLYHSTA-LIVGWSAClaSGATLVIRKKFSASNFWDDIRKYQATIFQYIGELCRYLLNQPPKP 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 302 kYDLSSLMVLLCGAApLSRETEDQIKERIGVPFIRQGYGLSESTLSVLvqnDEFCKPGSVGV-----LKVGIYAKV-IDP 375
Cdd:cd05940 192 -TERKHKVRMIFGNG-LRPDIWEEFKERFGVPRIAEFYAATEGNSGFI---NFFGKPGAIGRnpsllRKVAPLALVkYDL 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 376 DTGKLL----------GANERGELCFK--GDGIMKGYIGDTKST----QTAIKDG--WLHTGDIGYYDDDFEFFIVDRIK 437
Cdd:cd05940 267 ESGEPIrdaegrcikvPRGEPGLLISRinPLEPFDGYTDPAATEkkilRDVFKKGdaWFNTGDLMRLDGEGFWYFVDRLG 346
|
410 420 430
....*....|....*....|....*....|..
gi 21355181 438 ELIKYKGYQVPPAEIEALLLTNDKIKDAAVIG 469
Cdd:cd05940 347 DTFRWKGENVSTTEVAAVLGAFPGVEEANVYG 378
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
164-538 |
2.18e-22 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 100.35 E-value: 2.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 164 IYDLKELMEDEKFKTQPDFTSPAanKDEDVSLIVCSSGTTGLPKGVQLTQMNLLATLDSQIQPTVIPMEEVTL------- 236
Cdd:PRK04813 118 VITLDELKDIFATGNPYDFDHAV--KGDDNYYIIFTSGTTGKPKGVQISHDNLVSFTNWMLEDFALPEGPQFLnqapysf 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 237 -LTVIPWfhaFGCLTLittacvGARLVYLPK-----FeeKLFLSAIEKYR----------VMMAFMVPPlmvFLAKHpiv 300
Cdd:PRK04813 196 dLSVMDL---YPTLAS------GGTLVALPKdmtanF--KQLFETLPQLPinvwvstpsfADMCLLDPS---FNEEH--- 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 301 dkydLSSLMV-LLCGAApLSRETEDQIKERIGVPFIRQGYGLSESTLSV---------LVQNDEfckpgsvgvLKVGiYA 370
Cdd:PRK04813 259 ----LPNLTHfLFCGEE-LPHKTAKKLLERFPSATIYNTYGPTEATVAVtsieitdemLDQYKR---------LPIG-YA 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 371 K-----VIDPDTGKLLGANERGELCFKGDGIMKGYIGDTKSTQTAIK--DGW--LHTGDIGYYDDDFeFFIVDRIKELIK 441
Cdd:PRK04813 324 KpdsplLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFFtfDGQpaYHTGDAGYLEDGL-LFYQGRIDFQIK 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 442 YKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGELPLAFVVKQAN-----VQLT---ENEVIQFVNDNASPAKrlrgg 513
Cdd:PRK04813 403 LNGYRIELEEIEQNLRQSSYVESAVVVPYNKDHKVQYLIAYVVPKEEdfereFELTkaiKKELKERLMEYMIPRK----- 477
|
410 420
....*....|....*....|....*.
gi 21355181 514 VIFVDEIPKNPSGKILR-RILREMLK 538
Cdd:PRK04813 478 FIYRDSLPLTPNGKIDRkALIEEVNK 503
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
39-533 |
4.13e-22 |
|
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: 99.27 E-value: 4.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 39 GDRTVLVDAVNGVEYSAsfMHKSIVRLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREVDH 118
Cdd:cd17646 12 PDAPAVVDEGRTLTYRE--LDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRLAY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 119 AINLSKPKIIFASKITIDRVAKVasknkfvkgiialsgtskkfkniyDLKELMEDEKFKTQPDFTSPAANKDEDVSLIVC 198
Cdd:cd17646 90 MLADAGPAVVLTTADLAARLPAG------------------------GDVALLGDEALAAPPATPPLVPPRPDNLAYVIY 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 199 SSGTTGLPKGVQLTQ---MNLLATLDSQIQPTviPMEEVTLLT-----VIPW--FHAFgcltlittaCVGARLV------ 262
Cdd:cd17646 146 TSGSTGRPKGVMVTHagiVNRLLWMQDEYPLG--PGDRVLQKTplsfdVSVWelFWPL---------VAGARLVvarpgg 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 263 -----YLpkfeeklfLSAIEKYRVMMAFMVPPLM-VFLAKhpiVDKYDLSSLMVLLCGAAPLSRETEDQIKERIGVPFiR 336
Cdd:cd17646 215 hrdpaYL--------AALIREHGVTTCHFVPSMLrVFLAE---PAAGSCASLRRVFCSGEALPPELAARFLALPGAEL-H 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 337 QGYGLSESTLSVL---VQNDEFCKPGSVG--VLKVGIYakVIDPDtGKLLGANERGELCFKGDGIMKGYIGdtKSTQTA- 410
Cdd:cd17646 283 NLYGPTEAAIDVThwpVRGPAETPSVPIGrpVPNTRLY--VLDDA-LRPVPVGVPGELYLGGVQLARGYLG--RPALTAe 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 411 --IKDGWLH------TGDIGYYDDDFEFFIVDRIKELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGELPLAF 482
Cdd:cd17646 358 rfVPDPFGPgsrmyrTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGY 437
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 21355181 483 VVKQA-NVQLTENEVIQFVNDnASPAKRLRGGVIFVDEIPKNPSGKILRRIL 533
Cdd:cd17646 438 VVPAAgAAGPDTAALRAHLAE-RLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
357-540 |
5.78e-22 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 99.83 E-value: 5.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 357 KPGSVGVLKVGIYAKVIDpDTGKLLGANERGELCFKGD--GIMKGYIGDT----KSTQTAIKDGWLhTGDIGYYDDDFEF 430
Cdd:PRK00174 422 KPGSATRPLPGIQPAVVD-EEGNPLEGGEGGNLVIKDPwpGMMRTIYGDHerfvKTYFSTFKGMYF-TGDGARRDEDGYY 499
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 431 FIVDRIKELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGELPLAFVVKQANVQLTE---NEVIQFVNDN---- 503
Cdd:PRK00174 500 WITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLKGGEEPSDelrKELRNWVRKEigpi 579
|
170 180 190
....*....|....*....|....*....|....*..
gi 21355181 504 ASPAKrlrggVIFVDEIPKNPSGKILRRILREMLKKQ 540
Cdd:PRK00174 580 AKPDV-----IQFAPGLPKTRSGKIMRRILRKIAEGE 611
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
65-537 |
9.46e-22 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 98.92 E-value: 9.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 65 LAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLN--VTYSDRE--VDHAINL---SKPKIIFASKITIDR 137
Cdd:PRK09192 62 GARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPLPlpMGFGGREsyIAQLRGMlasAQPAAIITPDELLPW 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 138 VAKVASKNKFVKgiiALSGTskkfkniyDLKELMEdekfktqPDFTSPAANKDeDVSLIVCSSGTTGLPKGVQLTQMNLL 217
Cdd:PRK09192 142 VNEATHGNPLLH---VLSHA--------WFKALPE-------ADVALPRPTPD-DIAYLQYSSGSTRFPRGVIITHRALM 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 218 ATLDS------QIQPtviPMEEVTLLtviPWFHAFGCLTLITTAcVGARLV--YLP--KFEEK--LFLSAIEKYRVMMAF 285
Cdd:PRK09192 203 ANLRAishdglKVRP---GDRCVSWL---PFYHDMGLVGFLLTP-VATQLSvdYLPtrDFARRplQWLDLISRNRGTISY 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 286 mVPPLMVFLAKHPIVDK----YDLSSLMVLLCGAAPLSRETEDQIKERIG---------VPfirqGYGLSESTLSV---- 348
Cdd:PRK09192 276 -SPPFGYELCARRVNSKdlaeLDLSCWRVAGIGADMIRPDVLHQFAEAFApagfddkafMP----SYGLAEATLAVsfsp 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 349 -------------LVQNDEFCKPGSVGVLKV-----------GIYAKVIDPDtGKLLGANERGELCFKGDGIMKGYIGDT 404
Cdd:PRK09192 351 lgsgivveevdrdRLEYQGKAVAPGAETRRVrtfvncgkalpGHEIEIRNEA-GMPLPERVVGHICVRGPSLMSGYFRDE 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 405 KSTQTAIKDGWLHTGDIGYYDDDfEFFIVDRIKELIKYKGYQVPPAEIEALLLTNDKIK--DAAVIGKPDEEaGELPLAF 482
Cdd:PRK09192 430 ESQDVLAADGWLDTGDLGYLLDG-YLYITGRAKDLIIINGRNIWPQDIEWIAEQEPELRsgDAAAFSIAQEN-GEKIVLL 507
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21355181 483 VvkQAnvQLTENEVIQFVNDNASPAKRLRGGVIFVDE------IPKNPSGKILRRILREML 537
Cdd:PRK09192 508 V--QC--RISDEERRGQLIHALAALVRSEFGVEAAVElvpphsLPRTSSGKLSRAKAKKRY 564
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
64-534 |
2.03e-21 |
|
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: 97.05 E-value: 2.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 64 RLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREVDHAINLSKPKIIFASkiTIDRVAKVas 143
Cdd:cd17649 24 RLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYMLEDSGAGLLLTH--HPRQLAYV-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 144 knkfvkgiialsgtskkfknIYdlkelmedekfktqpdftspaankdedvslivcSSGTTGLPKGVQLTQMNLLATLDSQ 223
Cdd:cd17649 100 --------------------IY---------------------------------TSGSTGTPKGVAVSHGPLAAHCQAT 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 224 IQPTVIPMEEVTL--------LTVIPWFHAFGCltlittacvGARLVYLPkfeEKLFLSA------IEKYRVMMAFMVPP 289
Cdd:cd17649 127 AERYGLTPGDRELqfasfnfdGAHEQLLPPLIC---------GACVVLRP---DELWASAdelaemVRELGVTVLDLPPA 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 290 LMVFLAKHpIVDKYDLS--SLMVLLCGAAPLSRETEDQIKeRIGVPFIrQGYGLSESTLSVLV---QNDEFCKPGSVGVL 364
Cdd:cd17649 195 YLQQLAEE-ADRTGDGRppSLRLYIFGGEALSPELLRRWL-KAPVRLF-NAYGPTEATVTPLVwkcEAGAARAGASMPIG 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 365 KV--GIYAKVIDPDTGkLLGANERGELCFKGDGIMKGYIGDTKST-QTAIKDG-------WLHTGDIGYYDDDFEFFIVD 434
Cdd:cd17649 272 RPlgGRSAYILDADLN-PVPVGVTGELYIGGEGLARGYLGRPELTaERFVPDPfgapgsrLYRTGDLARWRDDGVIEYLG 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 435 RIKELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGELpLAFVVKQANVQLTEneviqfvnDNASPAKRLRGG- 513
Cdd:cd17649 351 RVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAGGKQL-VAYVVLRAAAAQPE--------LRAQLRTALRASl 421
|
490 500
....*....|....*....|....*....
gi 21355181 514 --------VIFVDEIPKNPSGKILRRILR 534
Cdd:cd17649 422 pdymvpahLVFLARLPLTPNGKLDRKALP 450
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
64-533 |
3.01e-21 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 98.69 E-value: 3.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 64 RLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREVDHAINLSKPKIIFASKITIDRVAKVAs 143
Cdd:PRK12467 549 RLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQSHLLAQLPVPA- 627
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 144 knkfvkGIIALsgtskkfkniydLKELMEDEKFKTQPDFTSPAANKDeDVSLIVCSSGTTGLPKGVQLTQMNLLATLDS- 222
Cdd:PRK12467 628 ------GLRSL------------CLDEPADLLCGYSGHNPEVALDPD-NLAYVIYTSGSTGQPKGVAISHGALANYVCVi 688
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 223 QIQPTVIPMEEVTLLTVIPWfhAFGCLTLITTACVGARLVYLPK---FEEKLFLSAIEKYRVMMAFMVPPLMVFLAKHPI 299
Cdd:PRK12467 689 AERLQLAADDSMLMVSTFAF--DLGVTELFGALASGATLHLLPPdcaRDAEAFAALMADQGVTVLKIVPSHLQALLQASR 766
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 300 VDKydLSSLMVLLCGAAPLSRETEDQIKE-RIGVPFIRQgYGLSESTLSVLV------QNDEFCKPGSVGVLKVGIYakV 372
Cdd:PRK12467 767 VAL--PRPQRALVCGGEALQVDLLARVRAlGPGARLINH-YGPTETTVGVSTyelsdeERDFGNVPIGQPLANLGLY--I 841
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 373 IDPDTgKLLGANERGELCFKGDGIMKGYIGDTKSTQT-------AIKDGWLH-TGDIGYYDDDFEFFIVDRIKELIKYKG 444
Cdd:PRK12467 842 LDHYL-NPVPVGVVGELYIGGAGLARGYHRRPALTAErfvpdpfGADGGRLYrTGDLARYRADGVIEYLGRMDHQVKIRG 920
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 445 YQVPPAEIEALLLTNDKIKDAAVIGKPdEEAGELPLAFVVKQANVQLTE----NEVIQFVNDNASPAKRLRGGVIFVDEI 520
Cdd:PRK12467 921 FRIELGEIEARLLAQPGVREAVVLAQP-GDAGLQLVAYLVPAAVADGAEhqatRDELKAQLRQVLPDYMVPAHLLLLDSL 999
|
490
....*....|...
gi 21355181 521 PKNPSGKILRRIL 533
Cdd:PRK12467 1000 PLTPNGKLDRKAL 1012
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
64-533 |
3.96e-21 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 98.31 E-value: 3.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 64 RLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREVDHAINLSKPKIIFASKITIDRVAKVAs 143
Cdd:PRK12467 1611 RLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQSHLQARLPLPD- 1689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 144 knkfvkGIIALsgtskkfknIYDlkelMEDEKFKTQPDfTSPAANKD-EDVSLIVCSSGTTGLPKGVQLTQMNLLATLDS 222
Cdd:PRK12467 1690 ------GLRSL---------VLD----QEDDWLEGYSD-SNPAVNLApQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCA 1749
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 223 QIQPTVIPMEEVTLL--------TVIPWFHAFgcltlittaCVGARLVYLPKFEEKL---FLSAIEKYRVMMAFMVPPLM 291
Cdd:PRK12467 1750 TQEAYQLSAADVVLQftsfafdvSVWELFWPL---------INGARLVIAPPGAHRDpeqLIQLIERQQVTTLHFVPSML 1820
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 292 VFLAKHPIVDKYDLSsLMVLLCGAAPLSRETEDQIKERIGVPFIRQGYGLSESTLSVL-----VQNDEFCKPGSVGVLKV 366
Cdd:PRK12467 1821 QQLLQMDEQVEHPLS-LRRVVCGGEALEVEALRPWLERLPDTGLFNLYGPTETAVDVThwtcrRKDLEGRDSVPIGQPIA 1899
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 367 GIYAKVIDpDTGKLLGANERGELCFKGDGIMKGYIGDTKSTQT-------AIKDGWLH-TGDIGYYDDDFEFFIVDRIKE 438
Cdd:PRK12467 1900 NLSTYILD-ASLNPVPIGVAGELYLGGVGLARGYLNRPALTAErfvadpfGTVGSRLYrTGDLARYRADGVIEYLGRIDH 1978
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 439 LIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKpDEEAGELPLAFVVKQANVQLTENEVIQFVND-------NASPAKRLR 511
Cdd:PRK12467 1979 QVKIRGFRIELGEIEARLREQGGVREAVVIAQ-DGANGKQLVAYVVPTDPGLVDDDEAQVALRAilknhlkASLPEYMVP 2057
|
490 500
....*....|....*....|..
gi 21355181 512 GGVIFVDEIPKNPSGKILRRIL 533
Cdd:PRK12467 2058 AHLVFLARMPLTPNGKLDRKAL 2079
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
64-533 |
7.05e-21 |
|
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: 95.45 E-value: 7.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 64 RLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREVDHAINLSKPKIIFaskitidrvakvas 143
Cdd:cd17643 24 RLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFILADSGPSLLL-------------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 144 knkfvkgiialsgtskkfkniydlkelmedekfkTQPDftspaankdeDVSLIVCSSGTTGLPKGVQLTQMNLLATLDSQ 223
Cdd:cd17643 90 ----------------------------------TDPD----------DLAYVIYTSGSTGRPKGVVVSHANVLALFAAT 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 224 IQPTVIPMEEVTLLtvipwFHA----------FGCLTlittacVGARLVYLPKF---EEKLFLSAIEKYRVMMAFMVPPL 290
Cdd:cd17643 126 QRWFGFNEDDVWTL-----FHSyafdfsvweiWGALL------HGGRLVVVPYEvarSPEDFARLLRDEGVTVLNQTPSA 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 291 MVFLAKHPIVDKYDLSSLMVLLCGAAPLSRETEDQIKERIGV--PFIRQGYGLSESTLSV---LVQNDEFcKPGSVGVLK 365
Cdd:cd17643 195 FYQLVEAADRDGRDPLALRYVIFGGEALEAAMLRPWAGRFGLdrPQLVNMYGITETTVHVtfrPLDAADL-PAAAASPIG 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 366 VGIyakvidPDTG-KLLGANER-------GELCFKGDGIMKGYIGDTKSTQT--------AIKDGWLHTGDIGYYDDDFE 429
Cdd:cd17643 274 RPL------PGLRvYVLDADGRpvppgvvGELYVSGAGVARGYLGRPELTAErfvanpfgGPGSRMYRTGDLARRLPDGE 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 430 FFIVDRIKELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGELPLAFVVKQANVQLTENEVIQFVNDNAsPAKR 509
Cdd:cd17643 348 LEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVADDGAAADIAELRALLKELL-PDYM 426
|
490 500
....*....|....*....|....
gi 21355181 510 LRGGVIFVDEIPKNPSGKILRRIL 533
Cdd:cd17643 427 VPARYVPLDALPLTVNGKLDRAAL 450
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
17-533 |
8.91e-21 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 96.95 E-value: 8.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 17 TERQAQDSRSLGQYILDKYKSFGDRTVLVdaVNGVEYSASFMHKSIVRLAYILQKLGVKQNDVVGLSSENSVNFALAMFA 96
Cdd:PRK12316 4543 TDAGYPATRCVHQLVAERARMTPDAVAVV--FDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLA 4620
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 97 GLAVGATVAPLNVTYsdrevdhainlskPKIIFASKITIDRVAKVASKNKFVKGIIALSGTSKKFkniydlkeLMEDEKF 176
Cdd:PRK12316 4621 VLKAGGAYVPLDPEY-------------PRERLAYMMEDSGAALLLTQSHLLQRLPIPDGLASLA--------LDRDEDW 4679
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 177 KTQPDfTSPAANKD-EDVSLIVCSSGTTGLPKGVQLTQMNLLATLDSQIQ-PTVIPMEEVTLLT-------VIPWFHAfg 247
Cdd:PRK12316 4680 EGFPA-HDPAVRLHpDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGErYELTPDDRVLQFMsfsfdgsHEGLYHP-- 4756
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 248 cltLITTACVGAR--LVYLPKFeeklFLSAIEKYRVMMAFMVPPLMVFLAKHPIVDKyDLSSLMVLLCGAAPLSRETEDQ 325
Cdd:PRK12316 4757 ---LINGASVVIRddSLWDPER----LYAEIHEHRVTVLVFPPVYLQQLAEHAERDG-EPPSLRVYCFGGEAVAQASYDL 4828
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 326 IKERIGVPFIRQGYGLSESTLSVLVQNdefCKPGS--------VGVLKVGIYAKVIDpDTGKLLGANERGELCFKGDGIM 397
Cdd:PRK12316 4829 AWRALKPVYLFNGYGPTETTVTVLLWK---ARDGDacgaaympIGTPLGNRSGYVLD-GQLNPLPVGVAGELYLGGEGVA 4904
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 398 KGYIgdTKSTQTA---IKD------GWLH-TGDIGYYDDDFEFFIVDRIKELIKYKGYQVPPAEIEALLLTNDKIKDAAV 467
Cdd:PRK12316 4905 RGYL--ERPALTAerfVPDpfgapgGRLYrTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVV 4982
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21355181 468 IGKPDEEAGELpLAFVVKQANVQLTENEVIQFVNDNASPAkrLRGGV---------IFVDEIPKNPSGKILRRIL 533
Cdd:PRK12316 4983 IAQEGAVGKQL-VGYVVPQDPALADADEAQAELRDELKAA--LRERLpeymvpahlVFLARMPLTPNGKLDRKAL 5054
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
451-527 |
8.99e-20 |
|
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: 83.36 E-value: 8.99e-20
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21355181 451 EIEALLLTNDKIKDAAVIGKPDEEAGELPLAFVVKQANVQLTENEVIQFVNDNASPAKRLRgGVIFVDEIPKNPSGK 527
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVELLEEELVAHVREELGPYAVPK-EVVFVDELPKTRSGK 76
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
183-537 |
1.31e-19 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 92.14 E-value: 1.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 183 TSPAANKDEDVSLIVCSSGTTGLPKGVQLTQMNLLATLDSQIQPTVIPMEEVTLLTVIPWFHAFGCLTLITTACVGARLV 262
Cdd:PRK05851 144 ASLTPPDSGGPAVLQGTAGSTGTPRTAILSPGAVLSNLRGLNARVGLDAATDVGCSWLPLYHDMGLAFLLTAALAGAPLW 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 263 YLPK--FEEKLF--LSAIEKYRVMMAfmVPPLMVFlakhPIVDKY-------DLSSLMVLLCGAAPLSRETedqiKERIG 331
Cdd:PRK05851 224 LAPTtaFSASPFrwLSWLSDSRATLT--AAPNFAY----NLIGKYarrvsdvDLGALRVALNGGEPVDCDG----FERFA 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 332 VPFIRQG---------YGLSESTLSVLV-------QNDEFCKPGSVGVLKVGIYAKVID--------PDTGKLLGANERG 387
Cdd:PRK05851 294 TAMAPFGfdagaaapsYGLAESTCAVTVpvpgiglRVDEVTTDDGSGARRHAVLGNPIPgmevrispGDGAAGVAGREIG 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 388 ELCFKGDGIMKGYIGDtkstQTAIKDGWLHTGDIGYYDDDfEFFIVDRIKELIKYKGYQVPPAEIEALLLTNDKIKDAAV 467
Cdd:PRK05851 374 EIEIRGASMMSGYLGQ----APIDPDDWFPTGDLGYLVDG-GLVVCGRAKELITVAGRNIFPTEIERVAAQVRGVREGAV 448
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21355181 468 IGKPDEEAGELP---LAFVVKQANVQLTENEVIQFVndnASPAKRLRGGVIFVD--EIPKNPSGKILRRILREML 537
Cdd:PRK05851 449 VAVGTGEGSARPglvIAAEFRGPDEAGARSEVVQRV---ASECGVVPSDVVFVApgSLPRTSSGKLRRLAVKRSL 520
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
40-535 |
3.29e-19 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 92.15 E-value: 3.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 40 DRTVLVDAVNGVEYSAsfMHKSIVRLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREVDHA 119
Cdd:PRK05691 1146 ERIALVWDGGSLDYAE--LHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYM 1223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 120 INLSKPKIIFASKITIDRVAKVAsknkfvkGIIALSgtskkfkniydlkelMEDEKFKTQPDfTSPAAN-KDEDVSLIVC 198
Cdd:PRK05691 1224 LADSGVELLLTQSHLLERLPQAE-------GVSAIA---------------LDSLHLDSWPS-QAPGLHlHGDNLAYVIY 1280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 199 SSGTTGLPKGVQLTQMNLLATLdSQIQPTVIPMEEVTLLTVIP-------WfHAFgcLTLITtacvGARLVYLPKFEEK- 270
Cdd:PRK05691 1281 TSGSTGQPKGVGNTHAALAERL-QWMQATYALDDSDVLMQKAPisfdvsvW-ECF--WPLIT----GCRLVLAGPGEHRd 1352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 271 --LFLSAIEKYRVMMAFMVPPLMVFLAKHPIVDkyDLSSLMVLLCGAAPLSRETEDQIKERIGVPFIRQGYGLSESTLSV 348
Cdd:PRK05691 1353 pqRIAELVQQYGVTTLHFVPPLLQLFIDEPLAA--ACTSLRRLFSGGEALPAELRNRVLQRLPQVQLHNRYGPTETAINV 1430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 349 L-----VQNDEFckpGSVGVLKVGIYAKVIDPDTgKLLGANERGELCFKGDGIMKGYIGdtKSTQTAIK--------DG- 414
Cdd:PRK05691 1431 ThwqcqAEDGER---SPIGRPLGNVLCRVLDAEL-NLLPPGVAGELCIGGAGLARGYLG--RPALTAERfvpdplgeDGa 1504
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 415 -WLHTGDIGYYDDDFEFFIVDRIKELIKYKGYQVPPAEIEALLLTNDKIKDAAV-----------IGKPDEEAGELPLAF 482
Cdd:PRK05691 1505 rLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVlvregaagaqlVGYYTGEAGQEAEAE 1584
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 21355181 483 VVKQA-NVQLTENEViqfvndnasPAKRLRggvifVDEIPKNPSGKILRRILRE 535
Cdd:PRK05691 1585 RLKAAlAAELPEYMV---------PAQLIR-----LDQMPLGPSGKLDRRALPE 1624
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
64-533 |
7.57e-19 |
|
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: 89.23 E-value: 7.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 64 RLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREVDHAINLSKPKIIFaskitidrvakvas 143
Cdd:cd17652 24 RLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYMLADARPALLL-------------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 144 knkfvkgiialsgtskkfkniydlkelmedekfkTQPDftSPAankdedvsLIVCSSGTTGLPKGVQLTQMNLLATLDSQ 223
Cdd:cd17652 90 ----------------------------------TTPD--NLA--------YVIYTSGSTGRPKGVVVTHRGLANLAAAQ 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 224 IQPTVIPMEEVTLLTVIPWFHAFgCLTLITTACVGARLVYLPkfEEKL-----FLSAIEKYRVMMAFMVPPLMVFLakhp 298
Cdd:cd17652 126 IAAFDVGPGSRVLQFASPSFDAS-VWELLMALLAGATLVLAP--AEELlpgepLADLLREHRITHVTLPPAALAAL---- 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 299 ivDKYDLSSLMVLLCGAAPLSRETEDQIKEriGVPFIrQGYGLSESTLSVLVQNdefCKPGSvGVLKVGIyakvidPDTG 378
Cdd:cd17652 199 --PPDDLPDLRTLVVAGEACPAELVDRWAP--GRRMI-NAYGPTETTVCATMAG---PLPGG-GVPPIGR------PVPG 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 379 K---LLGANER-------GELCFKGDGIMKGYIGdtKSTQTA---IKD------GWLH-TGDIGYYDDDFEFFIVDRIKE 438
Cdd:cd17652 264 TrvyVLDARLRpvppgvpGELYIAGAGLARGYLN--RPGLTAerfVADpfgapgSRMYrTGDLARWRADGQLEFLGRADD 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 439 LIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGELPLAFVVKQANVQLTENEVIQFVNdNASPAKRLRGGVIFVD 518
Cdd:cd17652 342 QVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAPGAAPTAAELRAHLA-ERLPGYMVPAAFVVLD 420
|
490
....*....|....*
gi 21355181 519 EIPKNPSGKILRRIL 533
Cdd:cd17652 421 ALPLTPNGKLDRRAL 435
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
190-540 |
1.09e-18 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 87.79 E-value: 1.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 190 DEDVSLIVCSSGTTGLPKGVQLTQMNLLATLDSQIQPTVIPMeevTLLTVIPWFHAFGCLTLITTACVGARLVYLP---K 266
Cdd:PRK07824 34 DDDVALVVATSGTTGTPKGAMLTAAALTASADATHDRLGGPG---QWLLALPAHHIAGLQVLVRSVIAGSEPVELDvsaG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 267 FEEKLFLSAIE------KYrvmmAFMVPplmVFLAK---HPIVDKyDLSSLMVLLCGAAPLSRETEDQIKErIGVPFIRQ 337
Cdd:PRK07824 111 FDPTALPRAVAelgggrRY----TSLVP---MQLAKaldDPAATA-ALAELDAVLVGGGPAPAPVLDAAAA-AGINVVRT 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 338 gYGLSESTlsvlvqndefckPGSV--GVLKVGIYAKVIDpdtgkllganERGELcfKGDGIMKGYIGDTKSTQTAiKDGW 415
Cdd:PRK07824 182 -YGMSETS------------GGCVydGVPLDGVRVRVED----------GRIAL--GGPTLAKGYRNPVDPDPFA-EPGW 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 416 LHTGDIGYYDDDFeFFIVDRIKELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGELPLAFVVKQANVQLTENE 495
Cdd:PRK07824 236 FRTDDLGALDDGV-LTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAVVGDGGPAPTLEA 314
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 21355181 496 VIQFVNDN----ASPaKRLRggviFVDEIPKNPSGKILRRILREMLKKQ 540
Cdd:PRK07824 315 LRAHVARTldrtAAP-RELH----VVDELPRRGIGKVDRRALVRRFAGE 358
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
49-535 |
1.12e-18 |
|
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: 88.64 E-value: 1.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 49 NGVEYSASFMHKSIVRLAYILQK-LGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREVDHAINLSKPKI 127
Cdd:cd05937 2 EGKTWTYSETYDLVLRYAHWLHDdLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLSGSRF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 128 IfaskitidrvakvasknkfvkgiialsgtskkfknIYDlkelmedekfktqpdftspaankDEDVSLIVCSSGTTGLPK 207
Cdd:cd05937 82 V-----------------------------------IVD-----------------------PDDPAILIYTSGTTGLPK 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 208 GVQLTQMNLLATldSQIQPTVIPME-EVTLLTVIPWFHAFGCLTLITTACVGARLVYL-PKFEEKLFLSAIEKYRVMMAF 285
Cdd:cd05937 104 AAAISWRRTLVT--SNLLSHDLNLKnGDRTYTCMPLYHGTAAFLGACNCLMSGGTLALsRKFSASQFWKDVRDSGATIIQ 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 286 MVPPLMVFLAKHPIvDKYDLSSLMVLLCGAApLSRETEDQIKERIGVPFIRQGYGLSESTLSVLVQNdefckPGSVGVLK 365
Cdd:cd05937 182 YVGELCRYLLSTPP-SPYDRDHKVRVAWGNG-LRPDIWERFRERFNVPEIGEFYAATEGVFALTNHN-----VGDFGAGA 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 366 VGIYAKV-------------IDPDTG-----------KLLGANERGELCF----KGDGIMKGYIGDTKSTQTAI------ 411
Cdd:cd05937 255 IGHHGLIrrwkfenqvvlvkMDPETDdpirdpktgfcVRAPVGEPGEMLGrvpfKNREAFQGYLHNEDATESKLvrdvfr 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 412 -KDGWLHTGDIGYYDDDFEFFIVDRIKELIKYKGYQVPPAEIEALLLTNDKIKDAAVIG----KPDEEAGelplafvvkQ 486
Cdd:cd05937 335 kGDIYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGvkvpGHDGRAG---------C 405
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 21355181 487 ANVQLTENEVIQFVNDNASPAKRLRGG---------VIFVDEIPKNPSGKILRRILRE 535
Cdd:cd05937 406 AAITLEESSAVPTEFTKSLLASLARKNlpsyavplfLRLTEEVATTDNHKQQKGVLRD 463
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
64-533 |
1.32e-18 |
|
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: 88.65 E-value: 1.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 64 RLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYsdrevdhainlskPKiifaskitiDRvakvas 143
Cdd:cd17644 37 QLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLDPNY-------------PQ---------ER------ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 144 knkfvkgiialsgtskkfkniydLKELMEDEKFK---TQPdftspaankdEDVSLIVCSSGTTGLPKGVQLTQMNLLATL 220
Cdd:cd17644 89 -----------------------LTYILEDAQISvllTQP----------ENLAYVIYTSGSTGKPKGVMIEHQSLVNLS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 221 DSQIQPTVIPMEEVTLLTVIPWFHAfGCLTLITTACVGARLVYLPK---FEEKLFLSAIEKYRVMMAFMVPPLMVFLAKH 297
Cdd:cd17644 136 HGLIKEYGITSSDRVLQFASIAFDV-AAEEIYVTLLSGATLVLRPEemrSSLEDFVQYIQQWQLTVLSLPPAYWHLLVLE 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 298 PIVDKYDL-SSLMVLLCGAAPLSRETEDQIKERIGvPFIR--QGYGLSESTLSVLVQNdeFCKPGSVGVLKVGI------ 368
Cdd:cd17644 215 LLLSTIDLpSSLRLVIVGGEAVQPELVRQWQKNVG-NFIQliNVYGPTEATIAATVCR--LTQLTERNITSVPIgrpian 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 369 -YAKVIDpDTGKLLGANERGELCFKGDGIMKGYIGDTKSTQTA-IKDGWLH--------TGDIGYY--DDDFEFFivDRI 436
Cdd:cd17644 292 tQVYILD-ENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKfISHPFNSseserlykTGDLARYlpDGNIEYL--GRI 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 437 KELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGELPLAFVVKQANVQLTENEVIQFVNdNASPAKRLRGGVIF 516
Cdd:cd17644 369 DNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIVPHYEESPSTVELRQFLK-AKLPDYMIPSAFVV 447
|
490
....*....|....*..
gi 21355181 517 VDEIPKNPSGKILRRIL 533
Cdd:cd17644 448 LEELPLTPNGKIDRRAL 464
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
58-457 |
1.41e-18 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 88.72 E-value: 1.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 58 MHKSIVRLAYILQKLgvkQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREVDHAINLSKPKIIFASKITIDR 137
Cdd:PRK06334 51 VRKAVIALATKVSKY---PDQHIGIMMPASAGAYIAYFATLLSGKIPVMINWSQGLREVTACANLVGVTHVLTSKQLMQH 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 138 VAKVASKN-KFVKGIIALSGTSKKFKniydLKELMEDEKFKTQPD------FTSPAANKdEDVSLIVCSSGTTGLPKGVQ 210
Cdd:PRK06334 128 LAQTHGEDaEYPFSLIYMEEVRKELS----FWEKCRIGIYMSIPFewlmrwFGVSDKDP-EDVAVILFTSGTEKLPKGVP 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 211 LTQMNLLATLDSQIQpTVIPMEEVTLLTVIPWFHAFG---CLTLITTACVGARLVYLPKFEEKLfLSAIEKYRVMMAFMV 287
Cdd:PRK06334 203 LTHANLLANQRACLK-FFSPKEDDVMMSFLPPFHAYGfnsCTLFPLLSGVPVVFAYNPLYPKKI-VEMIDEAKVTFLGST 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 288 PPLMVFLAKHPIVDKYDLSSLMVLLCGAAPLSRETEDQIKERIGVPFIRQGYGLSESTLSVLVQNDEFCKPGS-VGVLKV 366
Cdd:PRK06334 281 PVFFDYILKTAKKQESCLPSLRFVVIGGDAFKDSLYQEALKTFPHIQLRQGYGTTECSPVITINTVNSPKHEScVGMPIR 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 367 GIYAKVIDPDTGKLLGANERGELCFKGDGIMKGYIGDtKSTQTAIK---DGWLHTGDIGYYDDDFEFFIVDRIKELIKYK 443
Cdd:PRK06334 361 GMDVLIVSEETKVPVSSGETGLVLTRGTSLFSGYLGE-DFGQGFVElggETWYVTGDLGYVDRHGELFLKGRLSRFVKIG 439
|
410
....*....|....
gi 21355181 444 GYQVPPAEIEALLL 457
Cdd:PRK06334 440 AEMVSLEALESILM 453
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
40-540 |
1.79e-18 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 88.51 E-value: 1.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 40 DRTVLVDavNGVEYSASFMHKSIVRLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGatVAPLNVTYSDR--EVD 117
Cdd:PRK10946 38 DAIAVIC--GERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLG--VAPVNALFSHQrsELN 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 118 HAINLSKPKIIFAskitiDRVAKVASKNKFVKGIIALSGTSKK--FKN---IYDLKELMEDEkfktQPDFTSPAANKDEd 192
Cdd:PRK10946 114 AYASQIEPALLIA-----DRQHALFSDDDFLNTLVAEHSSLRVvlLLNddgEHSLDDAINHP----AEDFTATPSPADE- 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 193 VSLIVCSSGTTGLPKGVQLTQ---------MNLLATLDSQIQ-------PTVIPMEEVTLLTVipwFHAFGCLTLIT--- 253
Cdd:PRK10946 184 VAFFQLSGGSTGTPKLIPRTHndyyysvrrSVEICGFTPQTRylcalpaAHNYPMSSPGALGV---FLAGGTVVLAPdps 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 254 -TACvgarlvylpkfeeklfLSAIEKYRVMMAFMVPPlMVFL---AKHPIVDKYDLSSLMVLLCGAAPLSRETEDQIKER 329
Cdd:PRK10946 261 aTLC----------------FPLIEKHQVNVTALVPP-AVSLwlqAIAEGGSRAQLASLKLLQVGGARLSETLARRIPAE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 330 IGVPfIRQGYGLSEStlsvLVQ---------------------NDEfckpgsvgvlkvgiyAKVIDPDtGKLLGANERGE 388
Cdd:PRK10946 324 LGCQ-LQQVFGMAEG----LVNytrlddsderifttqgrpmspDDE---------------VWVADAD-GNPLPQGEVGR 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 389 LCFKGDGIMKGYIGDTKSTQTAI-KDGWLHTGDIGYYDDDFEFFIVDRIKELIKYKGYQVPPAEIEALLLTNDKIKDAAV 467
Cdd:PRK10946 383 LMTRGPYTFRGYYKSPQHNASAFdANGFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAAL 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 468 IGKPDEEAGELPLAFVVKQANVQ-------LTENEVIQFvndnaspakRLRGGVIFVDEIPKNPSGKILRRILREMLKKQ 540
Cdd:PRK10946 463 VSMEDELMGEKSCAFLVVKEPLKavqlrrfLREQGIAEF---------KLPDRVECVDSLPLTAVGKVDKKQLRQWLASR 533
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
40-533 |
2.56e-18 |
|
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: 87.61 E-value: 2.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 40 DRTVLVDavNGVEYSASFMHKSIVRLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREVDHA 119
Cdd:cd17645 13 DHVAVVD--RGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGERIAYM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 120 INLSKPKIIFaskitidrvakvasknkfvkgiialsgtskkfkniydlkelmedekfkTQPDftspaankdeDVSLIVCS 199
Cdd:cd17645 91 LADSSAKILL------------------------------------------------TNPD----------DLAYVIYT 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 200 SGTTGLPKGVQLTQMNLLaTLDSQIQP--TVIPMEEVTLLTVIPwFHAFgCLTLITTACVGARLVYLPKfEEKLFLSAIE 277
Cdd:cd17645 113 SGSTGLPKGVMIEHHNLV-NLCEWHRPyfGVTPADKSLVYASFS-FDAS-AWEIFPHLTAGAALHVVPS-ERRLDLDALN 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 278 KY----RVMMAFMVPPLM-VFLAkhpivdkYDLSSLMVLLCGAAPLSRETEDQIKerigvpfIRQGYGLSESTlsVLVQN 352
Cdd:cd17645 189 DYfnqeGITISFLPTGAAeQFMQ-------LDNQSLRVLLTGGDKLKKIERKGYK-------LVNNYGPTENT--VVATS 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 353 DEFCKP-GSVGVLKVGIYAKVIDPDTG-KLLGANERGELCFKGDGIMKGYIGDTKST-QTAIKDGWL------HTGDIGY 423
Cdd:cd17645 253 FEIDKPyANIPIGKPIDNTRVYILDEAlQLQPIGVAGELCIAGEGLARGYLNRPELTaEKFIVHPFVpgermyRTGDLAK 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 424 YDDDFEFFIVDRIKELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGELPLAFVVKQANVqltENEVIQFVNDN 503
Cdd:cd17645 333 FLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTAPEEI---PHEELREWLKN 409
|
490 500 510
....*....|....*....|....*....|
gi 21355181 504 ASPAKRLRGGVIFVDEIPKNPSGKILRRIL 533
Cdd:cd17645 410 DLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
64-533 |
3.15e-18 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 89.25 E-value: 3.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 64 RLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREVDHAINLSKPKIIFASKitidrvaKVAS 143
Cdd:PRK12316 548 RLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQS-------HLGR 620
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 144 KNKFVKGIIALSgtskkfkniYDLKELMEDEKFKTQPDFTSPAankdEDVSLIVCSSGTTGLPKGVQLTQMNLLATLDSQ 223
Cdd:PRK12316 621 KLPLAAGVQVLD---------LDRPAAWLEGYSEENPGTELNP----ENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWM 687
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 224 IQPTVIPMEEvTLLTVIPWFHAFGCLTLITTACVGARLVYLPK---FEEKLFLSAIEKYRVMMAFMVPPLMVFLAKHPIV 300
Cdd:PRK12316 688 QQAYGLGVGD-TVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPgdhRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDV 766
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 301 DkyDLSSLMVLLCGAAPLSRETEDQIKERIGVPFIRQGYGLSESTLSVLVQN--DEFCKPGSVGVLKVGIYAKVIDPDTG 378
Cdd:PRK12316 767 A--SCTSLRRIVCSGEALPADAQEQVFAKLPQAGLYNLYGPTEAAIDVTHWTcvEEGGDSVPIGRPIANLACYILDANLE 844
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 379 KL-LGAneRGELCFKGDGIMKGYIGdtKSTQTAIK-------DG--WLHTGDIGYYDDDFEFFIVDRIKELIKYKGYQVP 448
Cdd:PRK12316 845 PVpVGV--LGELYLAGRGLARGYHG--RPGLTAERfvpspfvAGerMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIE 920
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 449 PAEIEALLLTNDKIKDAAVIGkpdeEAGELPLAFVVKQaNVQLTENEVIQFVNDNASPAKRLRGGVIFVDEIPKNPSGKI 528
Cdd:PRK12316 921 LGEIEARLLEHPWVREAAVLA----VDGKQLVGYVVLE-SEGGDWREALKAHLAASLPEYMVPAQWLALERLPLTPNGKL 995
|
....*
gi 21355181 529 LRRIL 533
Cdd:PRK12316 996 DRKAL 1000
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
64-533 |
9.60e-18 |
|
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: 85.79 E-value: 9.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 64 RLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYsdrevdhainlskPKiifaskitiDRVAKVAS 143
Cdd:cd12114 24 RVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQ-------------PA---------ARREAILA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 144 KNKfVKGIIALSGTSkkFKNIYDLKELMEDEKFKTQPDFTSPAANKDEDVSLIVCSSGTTGLPKGVQLTQMNLLATLDSQ 223
Cdd:cd12114 82 DAG-ARLVLTDGPDA--QLDVAVFDVLILDLDALAAPAPPPPVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTILDI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 224 IQPTVIPMEEVTL--------LTVipwFHAFGCLtlittaCVGARLVyLPKFEE----KLFLSAIEKYRVMMAFMVPPLM 291
Cdd:cd12114 159 NRRFAVGPDDRVLalsslsfdLSV---YDIFGAL------SAGATLV-LPDEARrrdpAHWAELIERHGVTLWNSVPALL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 292 VFLAKHPIVDKYDLSSL-MVLLCGA-APLSreTEDQIKERI-GVPFIRQGyGLSE----STLSVLVQNDEFCKPGSVGVL 364
Cdd:cd12114 229 EMLLDVLEAAQALLPSLrLVLLSGDwIPLD--LPARLRALApDARLISLG-GATEasiwSIYHPIDEVPPDWRSIPYGRP 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 365 KVGIYAKVIDPDtGKLLGANERGELCFKGDGIMKGYIGDTKSTQTA---IKDG--WLHTGDIGYYDDD--FEFfiVDRIK 437
Cdd:cd12114 306 LANQRYRVLDPR-GRDCPDWVPGELWIGGRGVALGYLGDPELTAARfvtHPDGerLYRTGDLGRYRPDgtLEF--LGRRD 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 438 ELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGELpLAFVVKQANVQLTENEVIQFVNDNASPAKRLRGGVIFV 517
Cdd:cd12114 383 GQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDPGGKRL-AAFVVPDNDGTPIAPDALRAFLAQTLPAYMIPSRVIAL 461
|
490
....*....|....*.
gi 21355181 518 DEIPKNPSGKILRRIL 533
Cdd:cd12114 462 EALPLTANGKVDRAAL 477
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
58-533 |
1.04e-17 |
|
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: 85.99 E-value: 1.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 58 MHKSIVRLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREVDHAINLSKPKIIFASkitidr 137
Cdd:cd17656 19 LNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGVRVVLTQ------ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 138 vAKVASKNKFVKGIIALsgtskkfknIYDLKELMEDEKFKTQpdftspaaNKDEDVSLIVCSSGTTGLPKGVQLTQMNLL 217
Cdd:cd17656 93 -RHLKSKLSFNKSTILL---------EDPSISQEDTSNIDYI--------NNSDDLLYIIYTSGTTGKPKGVQLEHKNMV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 218 ATLDSQIQPTVIPMEEVTLLTVIPWFHAfgCLTLI-TTACVGARLvYLPKFEEKLflsaiekyrvmmafMVPPLMVFLAK 296
Cdd:cd17656 155 NLLHFEREKTNINFSDKVLQFATCSFDV--CYQEIfSTLLSGGTL-YIIREETKR--------------DVEQLFDLVKR 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 297 HPIVDKYDLSSLMVLLCGAAPLSRETEDQIKERIGV--------PFIR----------QGYGLSES---TLSVLVQNDEF 355
Cdd:cd17656 218 HNIEVVFLPVAFLKFIFSEREFINRFPTCVKHIITAgeqlvitnEFKEmlhehnvhlhNHYGPSEThvvTTYTINPEAEI 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 356 CKPGSVG--VLKVGIYakvIDPDTGKLLGANERGELCFKGDGIMKGYIGDTK-STQTAIKDGW------LHTGDIGYY-- 424
Cdd:cd17656 298 PELPPIGkpISNTWIY---ILDQEQQLQPQGIVGELYISGASVARGYLNRQElTAEKFFPDPFdpnermYRTGDLARYlp 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 425 DDDFEFfiVDRIKELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGELPLAFVVkqANVQLTENEVIQFVNDnA 504
Cdd:cd17656 375 DGNIEF--LGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFV--MEQELNISQLREYLAK-Q 449
|
490 500
....*....|....*....|....*....
gi 21355181 505 SPAKRLRGGVIFVDEIPKNPSGKILRRIL 533
Cdd:cd17656 450 LPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
69-460 |
1.20e-17 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 86.32 E-value: 1.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 69 LQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREVDHAINLSKPKIIFASKITIDRVAKVASKNKFV 148
Cdd:PLN02387 123 LVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVICDSKQLKKLIDISSQLETV 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 149 KGII---------ALSGTSKKFKNIYDLKELME-DEKFKTQPDFTSPAankdeDVSLIVCSSGTTGLPKGVQLTQMNLLA 218
Cdd:PLN02387 203 KRVIymddegvdsDSSLSGSSNWTVSSFSEVEKlGKENPVDPDLPSPN-----DIAVIMYTSGSTGLPKGVMMTHGNIVA 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 219 TLDSQIqpTVIPM--EEVTLLTVIPWFHAF-----------GC-------LTLITT--------------------ACVG 258
Cdd:PLN02387 278 TVAGVM--TVVPKlgKNDVYLAYLPLAHILelaaesvmaavGAaigygspLTLTDTsnkikkgtkgdasalkptlmTAVP 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 259 A-----RLVYLPKFEEK------LF-------LSAIEKY--------RVMMAFMV-PPLMVFLAKHpivdkydlssLMVL 311
Cdd:PLN02387 356 AildrvRDGVRKKVDAKgglakkLFdiaykrrLAAIEGSwfgawgleKLLWDALVfKKIRAVLGGR----------IRFM 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 312 LCGAAPLSRETEDQIKERIGVPfIRQGYGLSES----TLSvlvqndEFCKPgSVGvlKVG-----IYAKVIDPDTGKLLG 382
Cdd:PLN02387 426 LSGGAPLSGDTQRFINICLGAP-IGQGYGLTETcagaTFS------EWDDT-SVG--RVGpplpcCYVKLVSWEEGGYLI 495
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 383 ANE---RGELCFKGDGIMKGYIGDTKSTQTAIKDG-----WLHTGDIGYYDDDFEFFIVDRIKELIKYK-GYQVPPAEIE 453
Cdd:PLN02387 496 SDKpmpRGEIVIGGPSVTLGYFKNQEKTDEVYKVDergmrWFYTGDIGQFHPDGCLEIIDRKKDIVKLQhGEYVSLGKVE 575
|
....*..
gi 21355181 454 ALLLTND 460
Cdd:PLN02387 576 AALSVSP 582
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
67-535 |
1.42e-17 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 85.62 E-value: 1.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 67 YILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVtysDREVDHAINLSKpkiifaskitidrvakvasknk 146
Cdd:cd05908 30 GALQELGIKPGQEVVFQITHNNKFLYLFWACLLGGMIAVPVSI---GSNEEHKLKLNK---------------------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 147 fvkgIIalsgtsKKFKNIYdlkeLMEDEKFKTQpdftspaaNKDEdVSLIVCSSGTTGLPKGVQLTQMNLLATLDSQIQP 226
Cdd:cd05908 85 ----VW------NTLKNPY----LITEEEVLCE--------LADE-LAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 227 TVIPMEEvTLLTVIPWFHAFGCLTL-ITTACVGARLVYLPKFE----EKLFLSAIEKYRVMMA----FMVPPLMVFLAKH 297
Cdd:cd05908 142 TEWKTKD-RILSWMPLTHDMGLIAFhLAPLIAGMNQYLMPTRLfirrPILWLKKASEHKATIVsspnFGYKYFLKTLKPE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 298 PIVDkYDLSSLMVLLCGAAPLSRETEDQIKERIGVPFIRQG-----YGLSESTLSVLVQN-DEFCKPGSVG--------- 362
Cdd:cd05908 221 KAND-WDLSSIRMILNGAEPIDYELCHEFLDHMSKYGLKRNailpvYGLAEASVGASLPKaQSPFKTITLGrrhvthgep 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 363 -------------VLKVGiyaKVID-------PDTGKLLGANERGELCFKGDGIMKGYIGDTKSTQTAI-KDGWLHTGDI 421
Cdd:cd05908 300 epevdkkdsecltFVEVG---KPIDetdiricDEDNKILPDGYIGHIQIRGKNVTPGYYNNPEATAKVFtDDGWLKTGDL 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 422 GYYDDDfEFFIVDRIKELIKYKGYQVPPAEIE--ALLLTNDKIKDAAVIGKPDEEA-GELPLAFVVKQAnvqlTENEVIQ 498
Cdd:cd05908 377 GFIRNG-RLVITGREKDIIFVNGQNVYPHDIEriAEELEGVELGRVVACGVNNSNTrNEEIFCFIEHRK----SEDDFYP 451
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 21355181 499 FVNDNASPAKRlRGG-----VIFVDEIPKNPSGKILRRILRE 535
Cdd:cd05908 452 LGKKIKKHLNK-RGGwqineVLPIRRIPKTTSGKVKRYELAQ 492
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
184-441 |
1.12e-16 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 83.49 E-value: 1.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 184 SPAANKDeDVSLIVCSSGTTGLPKGVQLTQMNLLA---TLDSQIQPTVIPMEEV-TLLTVIPWFHAF-----------GC 248
Cdd:PTZ00216 258 NIPENND-DLALIMYTSGTTGDPKGVMHTHGSLTAgilALEDRLNDLIGPPEEDeTYCSYLPLAHIMefgvtniflarGA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 249 L-------TLI-TTA--------------------------CVGARLVYLPKFEEKLFLSAIE-KYRVMMAFMVPPLM-- 291
Cdd:PTZ00216 337 LigfgsprTLTdTFArphgdltefrpvfligvprifdtikkAVEAKLPPVGSLKRRVFDHAYQsRLRALKEGKDTPYWne 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 292 -VFLAKHPIVDkydlSSLMVLLCGAAPLSRETEdqikERIGVPF--IRQGYGLSESTLSVLVQNDEFCKPGSVGVLKVGI 368
Cdd:PTZ00216 417 kVFSAPRAVLG----GRVRAMLSGGGPLSAATQ----EFVNVVFgmVIQGWGLTETVCCGGIQRTGDLEPNAVGQLLKGV 488
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21355181 369 YAKVIDPDTGKLLGANE-RGELCFKGDGIMKGYIGDTKSTQTAI-KDGWLHTGDIGYYDDDFEFFIVDRIKELIK 441
Cdd:PTZ00216 489 EMKLLDTEEYKHTDTPEpRGEILLRGPFLFKGYYKQEELTREVLdEDGWFHTGDVGSIAANGTLRIIGRVKALAK 563
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
176-544 |
4.87e-16 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 80.82 E-value: 4.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 176 FKTQPDFTSPAANKD---EDVSLIVCSSGTTGLPKGVQLTQMNLLATLDSQIQPTVIPMEEV---TLLTVIPWFHAFGCL 249
Cdd:PRK05857 151 SEHSLDAASLAGNADqgsEDPLAMIFTSGTTGEPKAVLLANRTFFAVPDILQKEGLNWVTWVvgeTTYSPLPATHIGGLW 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 250 TLITTACVGARLVylPKFEEKLFLSAI-EKYRVMMAFMVPPLMVFLAKHPIVDKYDLSSLMVLLCGAaplSRETEDQIK- 327
Cdd:PRK05857 231 WILTCLMHGGLCV--TGGENTTSLLEIlTTNAVATTCLVPTLLSKLVSELKSANATVPSLRLVGYGG---SRAIAADVRf 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 328 -ERIGVPfIRQGYGLSESTLSVL---VQNDEFCK--PGSVGVLKVGIYAKVIDPDTG--KLLGANER---GELCFKGDGI 396
Cdd:PRK05857 306 iEATGVR-TAQVYGLSETGCTALclpTDDGSIVKieAGAVGRPYPGVDVYLAATDGIgpTAPGAGPSasfGTLWIKSPAN 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 397 MKGYIGDTKSTQTAIKDGWLHTGDIGYYDDDFEFFIVDRIKELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAG 476
Cdd:PRK05857 385 MLGYWNNPERTAEVLIDGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFG 464
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21355181 477 EL------PLAFVVKQANVQLTENEVIQFVNDNASPAKrlRGGVIFVDEIPKNPSGKILRRILREMLKKQKSKL 544
Cdd:PRK05857 465 ALvglavvASAELDESAARALKHTIAARFRRESEPMAR--PSTIVIVTDIPRTQSGKVMRASLAAAATADKARV 536
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
69-453 |
7.19e-16 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 80.53 E-value: 7.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 69 LQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREVDHAINLSKPKIIFASKITIDRVAKVASKNKFV 148
Cdd:PLN02736 95 LVQHGIPKGACVGLYFINRPEWLIVDHACSAYSYVSVPLYDTLGPDAVKFIVNHAEVAAIFCVPQTLNTLLSCLSEIPSV 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 149 KGIIALSGTSKKFKNIYDLK--ELMEDEKFKTQ--PDFTSPAANKDEDVSLIVCSSGTTGLPKGVQLTQMNLLA-----T 219
Cdd:PLN02736 175 RLIVVVGGADEPLPSLPSGTgvEIVTYSKLLAQgrSSPQPFRPPKPEDVATICYTSGTTGTPKGVVLTHGNLIAnvagsS 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 220 LDSQIQP-----TVIPM----EEVTLLTVIPWFHAFG-----CLTLI--------TTACVGARL---VYLP--------- 265
Cdd:PLN02736 255 LSTKFYPsdvhiSYLPLahiyERVNQIVMLHYGVAVGfyqgdNLKLMddlaalrpTIFCSVPRLynrIYDGitnavkesg 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 266 KFEEKLFLSAIEKYRVMMAFMVPPlmvflakHPIVDKYDLSSLM--------VLLCGAAPLSRETEDQIKERIGvPFIRQ 337
Cdd:PLN02736 335 GLKERLFNAAYNAKKQALENGKNP-------SPMWDRLVFNKIKaklggrvrFMSSGASPLSPDVMEFLRICFG-GRVLE 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 338 GYGLSEST--LSVLVQNDEFCkpGSVGVLKVGIYAKVID-PDTGKllgANE-----RGELCFKGDGIMKGYIGDTKSTQT 409
Cdd:PLN02736 407 GYGMTETScvISGMDEGDNLS--GHVGSPNPACEVKLVDvPEMNY---TSEdqpypRGEICVRGPIIFKGYYKDEVQTRE 481
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 21355181 410 AI-KDGWLHTGDIGYYDDDFEFFIVDRIKELIKY-KGYQVPPAEIE 453
Cdd:PLN02736 482 VIdEDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLaQGEYIAPEKIE 527
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
64-533 |
8.70e-16 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 81.36 E-value: 8.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 64 RLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREVDHAINLSKPKIIFASKITIDRVAKVAS 143
Cdd:PRK12467 3132 RLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLLTQAHLLEQLPAPAG 3211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 144 KNKFVKGIIALSGTSKKfkniydlkelmedekfktqpdftSPAANKD-EDVSLIVCSSGTTGLPKGVQLTQMNL------ 216
Cdd:PRK12467 3212 DTALTLDRLDLNGYSEN-----------------------NPSTRVMgENLAYVIYTSGSTGKPKGVGVRHGALanhlcw 3268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 217 ------LATLDSQIQPTVIPMEevtlLTVIPWFhafgcltliTTACVGARLVYLPKFE---EKLFlSAIEKYRVMMAFMV 287
Cdd:PRK12467 3269 iaeayeLDANDRVLLFMSFSFD----GAQERFL---------WTLICGGCLVVRDNDLwdpEELW-QAIHAHRISIACFP 3334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 288 PP-LMVFLAKHpivDKYDLSSLMVLLCGAAPLSRETEDQIKERIGVPFIRQGYGLSESTLSVLVQN---DEFCKPGSV-- 361
Cdd:PRK12467 3335 PAyLQQFAEDA---GGADCASLDIYVFGGEAVPPAAFEQVKRKLKPRGLTNGYGPTEAVVTVTLWKcggDAVCEAPYApi 3411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 362 --GVLKVGIYakVIDPDTGKL-LGAneRGELCFKGDGIMKGYigDTKSTQTA---IKD------GWLH-TGDIGYYDDDF 428
Cdd:PRK12467 3412 grPVAGRSIY--VLDGQLNPVpVGV--AGELYIGGVGLARGY--HQRPSLTAerfVADpfsgsgGRLYrTGDLARYRADG 3485
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 429 EFFIVDRIKELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKpDEEAGELPLAFVVKQAnvqLTENEVIQFVNDNAS--P 506
Cdd:PRK12467 3486 VIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLAR-DGAGGKQLVAYVVPAD---PQGDWRETLRDHLAAslP 3561
|
490 500
....*....|....*....|....*..
gi 21355181 507 AKRLRGGVIFVDEIPKNPSGKILRRIL 533
Cdd:PRK12467 3562 DYMVPAQLLVLAAMPLGPNGKVDRKAL 3588
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
339-537 |
4.57e-15 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 77.34 E-value: 4.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 339 YGLSE--STLSVLVQnDEFCKpGSVGVLKVGIYAKVIdpdtgklLGANERGELCFKGDGIMKGYIGDTKSTQtaikdGWL 416
Cdd:PRK07445 261 YGMTEtaSQIATLKP-DDFLA-GNNSSGQVLPHAQIT-------IPANQTGNITIQAQSLALGYYPQILDSQ-----GIF 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 417 HTGDIGYYDDDFEFFIVDRIKELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGELPLAFVVKQANvQLTENEV 496
Cdd:PRK07445 327 ETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYVPKDP-SISLEEL 405
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 21355181 497 IQFVNDNASPAKRLRGGvIFVDEIPKNPSGKILRRILREML 537
Cdd:PRK07445 406 KTAIKDQLSPFKQPKHW-IPVPQLPRNPQGKINRQQLQQIA 445
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
182-534 |
4.75e-15 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 78.23 E-value: 4.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 182 FTSPAANKDeDVSLIVCSSGTTGLPKGVQLTQMNLlATLDSQIQPTVIPMEEVTLLTVIPWFHAFGCLTLITTACVGARL 261
Cdd:PRK07769 172 WVPPEANED-TIAYLQYTSGSTRIPAGVQITHLNL-PTNVLQVIDALEGQEGDRGVSWLPFFHDMGLITVLLPALLGHYI 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 262 VYLpkfEEKLFLSAIEKYRVMMA---------FMVPPLMVF-LAKHPIVDK-----YDLSSLMVLLCGAAPLSRETEDQI 326
Cdd:PRK07769 250 TFM---SPAAFVRRPGRWIRELArkpggtggtFSAAPNFAFeHAAARGLPKdgeppLDLSNVKGLLNGSEPVSPASMRKF 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 327 KERIGvPF------IRQGYGLSESTLSV------------LVQNDEFCK----------PGSV-----GVLKVGIYAKVI 373
Cdd:PRK07769 327 NEAFA-PYglpptaIKPSYGMAEATLFVsttpmdeeptviYVDRDELNAgrfvevpadaPNAVaqvsaGKVGVSEWAVIV 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 374 DPDTGKLLGANERGELCFKGDGIMKGYIGDTKSTQ------------------TAIKDGWLHTGDIGYYDDDfEFFIVDR 435
Cdd:PRK07769 406 DPETASELPDGQIGEIWLHGNNIGTGYWGKPEETAatfqnilksrlseshaegAPDDALWVRTGDYGVYFDG-ELYITGR 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 436 IKELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGELPlAFVVKQANVQLT-------ENEVI----------- 497
Cdd:PRK07769 485 VKDLVIIDGRNHYPQDLEYTAQEATKALRTGYVAAFSVPANQLP-QVVFDDSHAGLKfdpedtsEQLVIvaerapgahkl 563
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 21355181 498 --QFVNDNASPAKRLRGGVIFVD-------EIPKNPSGKILRRILR 534
Cdd:PRK07769 564 dpQPIADDIRAAIAVRHGVTVRDvllvpagSIPRTSSGKIARRACR 609
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
58-478 |
5.83e-15 |
|
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.
Pssm-ID: 341245 [Multi-domain] Cd Length: 561 Bit Score: 77.47 E-value: 5.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 58 MHKSIVRLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREVDHA-----INLSKPKIIFAS- 131
Cdd:cd05921 31 ALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSPAYSLMSQDLAklkhlFELLKPGLVFAQd 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 132 ---------KITIDRVAKVASKNKfVKGIIALSgtskkfkniydLKELME-------DEKF-KTQPDftspaankdeDVS 194
Cdd:cd05921 111 aapfaralaAIFPLGTPLVVSRNA-VAGRGAIS-----------FAELAAtpptaavDAAFaAVGPD----------TVA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 195 LIVCSSGTTGLPKGVQLTQMNLLATLDSQIQPTVIPMEEV-TLLTVIPWFHAFGCLTLITTACVGARLVYL----P---K 266
Cdd:cd05921 169 KFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFFGEEPpVLVDWLPWNHTFGGNHNFNLVLYNGGTLYIddgkPmpgG 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 267 FEEKLF-LSAIEKyrvMMAFMVPP----LMVFLAKHPIVDKYDLSSLMVLLCGAAPLSRETEDQIK--------ERIgvP 333
Cdd:cd05921 249 FEETLRnLREISP---TVYFNVPAgwemLVAALEKDEALRRRFFKRLKLMFYAGAGLSQDVWDRLQalavatvgERI--P 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 334 FIrQGYGLSESTLSVLVQNDEFCKPGSVGVLKVGIYAKVIdPDTGKLlganergELCFKGDGIMKGYIGDTKSTQTAI-K 412
Cdd:cd05921 324 MM-AGLGATETAPTATFTHWPTERSGLIGLPAPGTELKLV-PSGGKY-------EVRVKGPNVTPGYWRQPELTAQAFdE 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21355181 413 DGWLHTGDIGYYDDDFE----FFIVDRIKELIKYKG---YQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGEL 478
Cdd:cd05921 395 EGFYCLGDAAKLADPDDpakgLVFDGRVAEDFKLASgtwVSVGPLRARAVAACAPLVHDAVVAGEDRAEVGAL 467
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
143-441 |
5.10e-14 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 75.14 E-value: 5.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 143 SKNKFVKGIIALSGTSKKFKNIYDLKE--------LMEDEKFKTQPDFTSPAANKDED-VSLIVCSSGTTGLPKGVQLTQ 213
Cdd:PTZ00342 247 SNELEDISLGPLEYDKEKLEKIKDLKEkakklgisIILFDDMTKNKTTNYKIQNEDPDfITSIVYTSGTSGKPKGVMLSN 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 214 MNLLATLDSQIQPTVIP-MEEVTLLTVIPWFH------AFGCLTLITT----------------ACVGARLVYLPKFEEK 270
Cdd:PTZ00342 327 KNLYNTVVPLCKHSIFKkYNPKTHLSYLPISHiyerviAYLSFMLGGTiniwskdinyfskdiyNSKGNILAGVPKVFNR 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 271 LF---LSAIEKYRVMMAFMVPPLMV------------FLAK-----HPIVDKYDlSSLMVLLCGAAPLSRETEDQIKERI 330
Cdd:PTZ00342 407 IYtniMTEINNLPPLKRFLVKKILSlrksnnnggfskFLEGithisSKIKDKVN-PNLEVILNGGGKLSPKIAEELSVLL 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 331 GVPFIrQGYGLSESTLSVLVQNDEFCKPGSVGV-LKVGIYAKVIDPDTGKLLGANERGELCFKGDGIMKGYIGDTKSTQT 409
Cdd:PTZ00342 486 NVNYY-QGYGLTETTGPIFVQHADDNNTESIGGpISPNTKYKVRTWETYKATDTLPKGELLIKSDSIFSGYFLEKEQTKN 564
|
330 340 350
....*....|....*....|....*....|...
gi 21355181 410 AI-KDGWLHTGDIGYYDDDFEFFIVDRIKELIK 441
Cdd:PTZ00342 565 AFtEDGYFKTGDIVQINKNGSLTFLDRSKGLVK 597
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
189-533 |
9.45e-14 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 73.26 E-value: 9.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 189 KDEDVSLIVCSSGTTGLPKGVQLTQMNLLATLDSQIQPTVIPMEEVTLLTvIPWFHAFGCLTLITTAcvgarlvyLPKFE 268
Cdd:cd05910 83 KADEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGEVDLAT-FPLFALFGPALGLTSV--------IPDMD 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 269 ---------EKLFlSAIEKYRVMMAFMVPPLMVFLAKHPIVDKYDLSSLMVLLCGAAPLSRETEDQIKERI--GVPFIRQ 337
Cdd:cd05910 154 ptrparadpQKLV-GAIRQYGVSIVFGSPALLERVARYCAQHGITLPSLRRVLSAGAPVPIALAARLRKMLsdEAEILTP 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 338 gYGLSES-------TLSVLVQNDEFCKPGS---VGVLKVGIYAKVIDPDTG--------KLLGANERGELCFKGDGIMKG 399
Cdd:cd05910 233 -YGATEAlpvssigSRELLATTTAATSGGAgtcVGRPIPGVRVRIIEIDDEpiaewddtLELPRGEIGEITVTGPTVTPT 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 400 YIGDTKSTQTA-IKDG----WLHTGDIGYYDDDFEFFIVDRIKELIKYKGYQVPPAEIEALLLTNDKIKDAAV--IGKPD 472
Cdd:cd05910 312 YVNRPVATALAkIDDNsegfWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALvgVGKPG 391
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21355181 473 EEAGELplafvvkqanvqlteneVIQFVNDNASPAKRLRGGVIFVDEipKNPSGKILRRIL 533
Cdd:cd05910 392 CQLPVL-----------------CVEPLPGTITPRARLEQELRALAK--DYPHTQRIGRFL 433
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
62-544 |
2.14e-13 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 73.01 E-value: 2.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 62 IVRLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREVDHAINLSKPKIIfaskITIDRVaKV 141
Cdd:PLN02654 130 VCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQRIVDCKPKVV----ITCNAV-KR 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 142 ASKNKFVKGII--ALSGTSKKFKNI-----YDLKELMEDEKFKTQP-------DFTSPAANK-------DEDVSLIVCSS 200
Cdd:PLN02654 205 GPKTINLKDIVdaALDESAKNGVSVgicltYENQLAMKREDTKWQEgrdvwwqDVVPNYPTKcevewvdAEDPLFLLYTS 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 201 GTTGLPKGVQLTQ---MNLLATLDS---QIQPTvipmeEVTLLTV-IPWFHAFGCLT---LITTACVgarLVY--LPKFE 268
Cdd:PLN02654 285 GSTGKPKGVLHTTggyMVYTATTFKyafDYKPT-----DVYWCTAdCGWITGHSYVTygpMLNGATV---LVFegAPNYP 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 269 EK-LFLSAIEKYRVMMAFMVPPLMVFLAKH--PIVDKYDLSSLMVLLCGAAPLSRETEDQIKERIG---VPfIRQGYGLS 342
Cdd:PLN02654 357 DSgRCWDIVDKYKVTIFYTAPTLVRSLMRDgdEYVTRHSRKSLRVLGSVGEPINPSAWRWFFNVVGdsrCP-ISDTWWQT 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 343 EsTLSVLVQNDEFC---KPGSVGVLKVGIYAKVIDpDTGKLLGANERGELCFKGD--GIMKGYIGDTKSTQTAIKD---G 414
Cdd:PLN02654 436 E-TGGFMITPLPGAwpqKPGSATFPFFGVQPVIVD-EKGKEIEGECSGYLCVKKSwpGAFRTLYGDHERYETTYFKpfaG 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 415 WLHTGDIGYYDDDFEFFIVDRIKELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGELPLAFVVKQANVQLTEN 494
Cdd:PLN02654 514 YYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEVKGQGIYAFVTLVEGVPYSEE 593
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 21355181 495 ---EVIQFVNDN----ASPAKrlrggVIFVDEIPKNPSGKILRRILREMLKKQKSKL 544
Cdd:PLN02654 594 lrkSLILTVRNQigafAAPDK-----IHWAPGLPKTRSGKIMRRILRKIASRQLDEL 645
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
58-420 |
5.64e-13 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 71.45 E-value: 5.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 58 MHKSIVRLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREVD-----HAINLSKPKIIFAS- 131
Cdd:PRK08180 75 ALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALAAMYAGVPYAPVSPAYSLVSQDfgklrHVLELLTPGLVFADd 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 132 --------KITIDRVAKVASKNKFVKGIIALSgtskkFKNIYDLKELME-DEKF-KTQPDftspaankdeDVSLIVCSSG 201
Cdd:PRK08180 155 gaafaralAAVVPADVEVVAVRGAVPGRAATP-----FAALLATPPTAAvDAAHaAVGPD----------TIAKFLFTSG 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 202 TTGLPKGVQLTQMNLLATLdSQIQPTVIPMEE--VTLLTVIPWFHAFGcltliTTACVGARL-----VYL----P---KF 267
Cdd:PRK08180 220 STGLPKAVINTHRMLCANQ-QMLAQTFPFLAEepPVLVDWLPWNHTFG-----GNHNLGIVLynggtLYIddgkPtpgGF 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 268 EEKLflsaiEKYRVMMA---FMVPP----LMVFLAKHPIVDKYDLSSLMVLLCGAAPLS--------RETEDQIKERIgv 332
Cdd:PRK08180 294 DETL-----RNLREISPtvyFNVPKgwemLVPALERDAALRRRFFSRLKLLFYAGAALSqdvwdrldRVAEATCGERI-- 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 333 pFIRQGYGLSESTLSVLVQNDEFCKPGSVGVLKVGIYAKVIdPDTGKLlganergELCFKGDGIMKGYIGDTKSTQTAI- 411
Cdd:PRK08180 367 -RMMTGLGMTETAPSATFTTGPLSRAGNIGLPAPGCEVKLV-PVGGKL-------EVRVKGPNVTPGYWRAPELTAEAFd 437
|
....*....
gi 21355181 412 KDGWLHTGD 420
Cdd:PRK08180 438 EEGYYRSGD 446
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
64-469 |
8.40e-13 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 70.53 E-value: 8.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 64 RLAYILQKLGVKQNDVVGLSSENSVNFaLAMFAGLA-VGATVAPLNVTYSDREVDHAINLSKPKIIfaskitidrvakva 142
Cdd:cd05939 15 KVANFFQAQGYRSGDVVALFMENRLEF-VALWLGLAkIGVETALINSNLRLESLLHCITVSKAKAL-------------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 143 sknkfvkgiialsgtskkfknIYDLKELMEDEKFKTQPdfTSPAANKDeDVSLIVCSSGTTGLPKGVQLTQ-----MNLL 217
Cdd:cd05939 80 ---------------------IFNLLDPLLTQSSTEPP--SQDDVNFR-DKLFYIYTSGTTGLPKAAVIVHsryyrIAAG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 218 ATLDSQIQPTVIpmeevtLLTVIPWFHAFGCLTLITTACV-GARLVYLPKFEEKLFLSAIEKYRVMMAFMVPPLMVFLAK 296
Cdd:cd05939 136 AYYAFGMRPEDV------VYDCLPLYHSAGGIMGVGQALLhGSTVVIRKKFSASNFWDDCVKYNCTIVQYIGEICRYLLA 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 297 HPIVDkYDLSSLMVLLCGAApLSRETEDQIKERIGVPFIRQGYGLSESTLSvLVQNDEfcKPGSVGVLKVgIYAKV---- 372
Cdd:cd05939 210 QPPSE-EEQKHNVRLAVGNG-LRPQIWEQFVRRFGIPQIGEFYGATEGNSS-LVNIDN--HVGACGFNSR-ILPSVypir 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 373 ---IDPDTGKLL----------GANERGELC---FKGDGIMK--GYIGDTKSTQTAIKDGWLH------TGDIGYYDDDF 428
Cdd:cd05939 284 likVDEDTGELIrdsdglcipcQPGEPGLLVgkiIQNDPLRRfdGYVNEGATNKKIARDVFKKgdsaflSGDVLVMDELG 363
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 21355181 429 EFFIVDRIKELIKYKGYQVPPAEIEALLLTNDKIKDAAVIG 469
Cdd:cd05939 364 YLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVYG 404
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
180-533 |
1.00e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 70.07 E-value: 1.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 180 PDFTSPAANK--DEDVSLIVCSSGTTGLPKGVQLTqmnlLATLDSQIQPTVIPMEEVTLLTVI---PWFHAFG--CLTLi 252
Cdd:PRK08308 88 SDFTKLEAVNylAEEPSLLQYSSGTTGEPKLIRRS----WTEIDREIEAYNEALNCEQDETPIvacPVTHSYGliCGVL- 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 253 ttACV--GARLVYLPKFEEKLFLSAIEKYRVMMAFMVPPLMVFLAKHPIVDkYDLSSLMVllcGAAPLSRETEDQIKERI 330
Cdd:PRK08308 163 --AALtrGSKPVIITNKNPKFALNILRNTPQHILYAVPLMLHILGRLLPGT-FQFHAVMT---SGTPLPEAWFYKLRERT 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 331 GVPFirQGYGLSESTlsvlvqndefCkpgsvgvlkVGIYAKVIDP-DTGKLL-------GANErgelcfkgdgimkgyiG 402
Cdd:PRK08308 237 TYMM--QQYGCSEAG----------C---------VSICPDMKSHlDLGNPLphvsvsaGSDE----------------N 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 403 DTKSTQTAIKDGWLHTGDIGYYDDDFEFFIVDRIKELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGELPLAF 482
Cdd:PRK08308 280 APEEIVVKMGDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAK 359
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 21355181 483 VVkqANVQLTENEVIQFVNDNASPAKrLRGGVIFVDEIPKNPSGKILRRIL 533
Cdd:PRK08308 360 VI--SHEEIDPVQLREWCIQHLAPYQ-VPHEIESVTEIPKNANGKVSRKLL 407
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
62-540 |
5.86e-12 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 67.97 E-value: 5.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 62 IVRLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREVDHainlskpkiiFASKITIDrvakv 141
Cdd:PRK09029 38 IDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLLEE----------LLPSLTLD----- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 142 asknkfvkgIIALSGTSKKFKNIYDLKELMEDEKFKTQPDFTSPAankdedvSLIVcSSGTTGLPKGVQLTQMN------ 215
Cdd:PRK09029 103 ---------FALVLEGENTFSALTSLHLQLVEGAHAVAWQPQRLA-------TMTL-TSGSTGLPKAAVHTAQAhlasae 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 216 -LLATLDSQIQPTvipmeevTLLTvIPWFHAFGcltlitTACV------GARLVyLPkfEEKLFLSAIEKyrVMMAFMVP 288
Cdd:PRK09029 166 gVLSLMPFTAQDS-------WLLS-LPLFHVSG------QGIVwrwlyaGATLV-VR--DKQPLEQALAG--CTHASLVP 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 289 PLMVFLAKHPIVDkydLSSLMVLLCGAA-P--LSRETEDQikeriGvpfIRQ--GYGLSE--STlsvlvqndefckpgsv 361
Cdd:PRK09029 227 TQLWRLLDNRSEP---LSLKAVLLGGAAiPveLTEQAEQQ-----G---IRCwcGYGLTEmaST---------------- 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 362 gvlkvgIYAKVID--PDTGKLLGANE----RGELCFKGDGIMKGYIGDTKSTQTAIKDGWLHTGDIGYYDDDfEFFIVDR 435
Cdd:PRK09029 280 ------VCAKRADglAGVGSPLPGREvklvDGEIWLRGASLALGYWRQGQLVPLVNDEGWFATRDRGEWQNG-ELTILGR 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 436 IKELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGELPLAFVvkQANVQLTENEVIQFVNDN-----------A 504
Cdd:PRK09029 353 LDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVPVADAEFGQRPVAVV--ESDSEAAVVNLAEWLQDKlarfqqpvayyL 430
|
490 500 510
....*....|....*....|....*....|....*.
gi 21355181 505 SPAKRLRGGVifvdeipknpsgKILRRILREMLKKQ 540
Cdd:PRK09029 431 LPPELKNGGI------------KISRQALKEWVAQQ 454
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
8-533 |
1.11e-11 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 68.06 E-value: 1.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 8 GNIVYGGPVTERQAQDSRSLGQYILDKYKSFGDRTVLVDAVNGVEYSAsfMHKSIVRLAYILQKLGVKQNDVVGLSSENS 87
Cdd:PRK12316 3040 GQLLEAWNATAAEYPLERGVHRLFEEQVERTPDAVALAFGEQRLSYAE--LNRRANRLAHRLIERGVGPDVLVGVAVERS 3117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 88 VNFALAMFAGLAVGATVAPLNVTYSDREVDHAINLSKPKIIfaskitidrvakvasknkfvkgiiaLSGTSKKFKNIYDL 167
Cdd:PRK12316 3118 LEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLL-------------------------LSQSHLRLPLAQGV 3172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 168 KELMEDEKFKTQPDFTSPAANKDEDVSLIVCSSGTTGLPKGVQLTQMNLLATLDSQIQPTVIPMEEVTLLTVIPWFHAFg 247
Cdd:PRK12316 3173 QVLDLDRGDENYAEANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFSFDVF- 3251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 248 CLTLITTACVGARLVyLPKFEEKLFLSAIEKYRVMMAFMVPP-----LMVFLAKhpiVDKYDLSSLMVLLCGAAPLSRET 322
Cdd:PRK12316 3252 VEELFWPLMSGARVV-LAGPEDWRDPALLVELINSEGVDVLHaypsmLQAFLEE---EDAHRCTSLKRIVCGGEALPADL 3327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 323 EDQIKERIGVpfiRQGYGLSESTLSVLVQNDEFCKPGSVGVLK-VGIYAKVIDPDTGKLLGANERGELCFKGDGIMKGYI 401
Cdd:PRK12316 3328 QQQVFAGLPL---YNLYGPTEATITVTHWQCVEEGKDAVPIGRpIANRACYILDGSLEPVPVGALGELYLGGEGLARGYH 3404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 402 GDTKSTQT-------AIKDGWLHTGDIGYYDDDFEFFIVDRIKELIKYKGYQVPPAEIEALLLTNDKIKDAAVIgkpdEE 474
Cdd:PRK12316 3405 NRPGLTAErfvpdpfVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVL----AV 3480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 21355181 475 AGELPLAFVVKQANVQlTENEVIQFVNDNASPAKRLRGGVIFVDEIPKNPSGKILRRIL 533
Cdd:PRK12316 3481 DGRQLVAYVVPEDEAG-DLREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKAL 3538
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
185-427 |
1.71e-11 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 66.46 E-value: 1.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 185 PAANKDEDVSLIVCSSGTTGLPKGVQLTQMNLLATL-----DSQIQPtvipmEEVTLLTvIPWFHAFGcltlittACVGA 259
Cdd:PRK09274 168 MADLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIealreDYGIEP-----GEIDLPT-FPLFALFG-------PALGM 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 260 RLVyLPKFE---------EKLFlSAIEKYRVMMAFMVPPLMVFLAKHPIVDKYDLSSLMVLLCGAAPLSRETEDQIKERI 330
Cdd:PRK09274 235 TSV-IPDMDptrpatvdpAKLF-AAIERYGVTNLFGSPALLERLGRYGEANGIKLPSLRRVISAGAPVPIAVIERFRAML 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 331 --GVPfIRQGYGLSES--------------TLSVLVQNDEFCkpgsVGVLKVGIYAKVIDPDTG--------KLLGANER 386
Cdd:PRK09274 313 ppDAE-ILTPYGATEAlpissiesreilfaTRAATDNGAGIC----VGRPVDGVEVRIIAISDApipewddaLRLATGEI 387
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 21355181 387 GELCFKGDGIMKGYIGDTKSTQTA-IKDG----WLHTGDIGYYDDD 427
Cdd:PRK09274 388 GEIVVAGPMVTRSYYNRPEATRLAkIPDGqgdvWHRMGDLGYLDAQ 433
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
192-532 |
3.42e-11 |
|
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: 65.50 E-value: 3.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 192 DVSLIVCSSGTTGLPKGVQLTQ---MNLLATLDSQIQPTVIPMEEVTLLT--VIPWFHAFGCLTLITtacvGARLVYLP- 265
Cdd:cd17648 95 DLAYAIYTSGTTGKPKGVLVEHgsvVNLRTSLSERYFGRDNGDEAVLFFSnyVFDFFVEQMTLALLN----GQKLVVPPd 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 266 --KFEEKLFLSAIEKYRVmmafmvpplmVFLAKHP-IVDKYDLSSL----MVLLCGAApLSRETEDQIKERIGVPfIRQG 338
Cdd:cd17648 171 emRFDPDRFYAYINREKV----------TYLSGTPsVLQQYDLARLphlkRVDAAGEE-FTAPVFEKLRSRFAGL-IINA 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 339 YGLSESTLSVLVQNDEFCKP--GSVGVLKVGIYAKVIDPDTgKLLGANERGELCFKGDGIMKGYIGDTKST--------- 407
Cdd:cd17648 239 YGPTETTVTNHKRFFPGDQRfdKSLGRPVRNTKCYVLNDAM-KRVPVGAVGELYLGGDGVARGYLNRPELTaerflpnpf 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 408 QTA--IKDG-------------WLHTGDIGYYD-DDFEffivdrikelIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKP 471
Cdd:cd17648 318 QTEqeRARGrnarlyktgdlvrWLPSGELEYLGrNDFQ----------VKIRGQRIEPGEVEAALASYPGVRECAVVAKE 387
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 472 DEEAGELP-----LAFVVKQANVqLTENEVIQFVNDNASPA---KRLrggvIFVDEIPKNPSGKI-LRRI 532
Cdd:cd17648 388 DASQAQSRiqkylVGYYLPEPGH-VPESDLLSFLRAKLPRYmvpARL----VRLEGIPVTINGKLdVRAL 452
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
47-530 |
4.44e-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: 65.45 E-value: 4.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 47 AVNGVEYSASFMHKSIVRLAYILQ-KLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREVDHAINLSKP 125
Cdd:cd05905 9 GKEATTLTWGKLLSRAEKIAAVLQkKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLGFLLGTCKV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 126 KIIFASKITIdRVAKVASKNKFVKGIIALSGTSKKFKNIYDLKElmedEKFKTQPDFTSPAANKDEDVSLIVCSSGTTGL 205
Cdd:cd05905 89 RVALTVEACL-KGLPKKLLKSKTAAEIAKKKGWPKILDFVKIPK----SKRSKLKKWGPHPPTRDGDTAYIEYSFSSDGS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 206 PKGVQLTQMNLLATLDSQIQpTVIPMEEVTLLTVIPWFHA----FGCLTLITTacvGARLVYLPKFEEK----LFLSAIE 277
Cdd:cd05905 164 LSGVAVSHSSLLAHCRALKE-ACELYESRPLVTVLDFKSGlglwHGCLLSVYS---GHHTILIPPELMKtnplLWLQTLS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 278 KYRVMMAF----------MVPPLMVFLAKHPIVDKYDLSSLMVLlCGAAPlSRETEDQIKERIG---------------- 331
Cdd:cd05905 240 QYKVRDAYvklrtlhwclKDLSSTLASLKNRDVNLSSLRMCMVP-CENRP-RISSCDSFLKLFQtlglspravstefgtr 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 332 -VPFI-RQGYG--------LSESTLSVLVQN-DEFCKPGSVGVLKVGI---YAKVI--DPDTGKLLGANERGELCFKGDG 395
Cdd:cd05905 318 vNPFIcWQGTSgpepsrvyLDMRALRHGVVRlDERDKPNSLPLQDSGKvlpGAQVAivNPETKGLCKDGEIGEIWVNSPA 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 396 IMKGYI---GDTKSTQTAI----------KDGWLHTGDIGY------YDDDFE----FFIVDRIKELIKYKGYQVPPAEI 452
Cdd:cd05905 398 NASGYFlldGETNDTFKVFpstrlstgitNNSYARTGLLGFlrptkcTDLNVEehdlLFVVGSIDETLEVRGLRHHPSDI 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 453 EA-LLLTNDKIKDAAVIG-----------KPDEEAGELPLAFVVKQAnvQLTENEVIQFVndnaspakrlrggVIFVD-- 518
Cdd:cd05905 478 EAtVMRVHPYRGRCAVFSitglvvvvaeqPPGSEEEALDLVPLVLNA--ILEEHQVIVDC-------------VALVPpg 542
|
570
....*....|..
gi 21355181 519 EIPKNPSGKILR 530
Cdd:cd05905 543 SLPKNPLGEKQR 554
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
184-484 |
6.99e-11 |
|
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.
Pssm-ID: 341287 [Multi-domain] Cd Length: 588 Bit Score: 64.78 E-value: 6.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 184 SPAANKDEDVSLIVCSSGTTGLPKGVQLTQmNLLATLDSQIQPTVIP-MEEVTLLTVIPWFHAFGCLTLITTACVGARLV 262
Cdd:cd17632 216 FRPEPDDDPLALLIYTSGSTGTPKGAMYTE-RLVATFWLKVSSIQDIrPPASITLNFMPMSHIAGRISLYGTLARGGTAY 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 263 YLPKFEEKLFLSAIEKYRVMMAFMVPPL--MVF----------------------LAKHPIVDKYDLSSLMVLLCGAAPL 318
Cdd:cd17632 295 FAAASDMSTLFDDLALVRPTELFLVPRVcdMLFqryqaeldrrsvagadaetlaeRVKAELRERVLGGRLLAAVCGSAPL 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 319 SRETEDQIKERIGVPfIRQGYGLSESTLSVLvqNDEFCKPgsvgvlKVGIYaKVID-PDTGKLL--GANERGELCFKGDG 395
Cdd:cd17632 375 SAEMKAFMESLLDLD-LHDGYGSTEAGAVIL--DGVIVRP------PVLDY-KLVDvPELGYFRtdRPHPRGELLVKTDT 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 396 IMKGYIGDTKST-QTAIKDGWLHTGDI----GyyDDDFEFfiVDRIKELIKY-KGYQVPPAEIEALLLTNDKIKDAAVIG 469
Cdd:cd17632 445 LFPGYYKRPEVTaEVFDEDGFYRTGDVmaelG--PDRLVY--VDRRNNVLKLsQGEFVTVARLEAVFAASPLVRQIFVYG 520
|
330
....*....|....*
gi 21355181 470 KpDEEAgeLPLAFVV 484
Cdd:cd17632 521 N-SERA--YLLAVVV 532
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
64-426 |
8.54e-11 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 64.68 E-value: 8.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 64 RLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREVDHA-----INLSKPKIIFASkitidrv 138
Cdd:PRK12582 92 ALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAGVPAAPVSPAYSLMSHDHAklkhlFDLVKPRVVFAQ------- 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 139 akvaSKNKFVKGIIAL------------SGTSKKFKNIYDLKELMEDEKFKTQPDFTSPAAnkdedVSLIVCSSGTTGLP 206
Cdd:PRK12582 165 ----SGAPFARALAALdlldvtvvhvtgPGEGIASIAFADLAATPPTAAVAAAIAAITPDT-----VAKYLFTSGSTGMP 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 207 KGVQLTQMNLLATLDSQIQPTV-IPMEEV-TLLTVIPWFHAFGCLTLITTACVGARLVY------LP-KFEEKL------ 271
Cdd:PRK12582 236 KAVINTQRMMCANIAMQEQLRPrEPDPPPpVSLDWMPWNHTMGGNANFNGLLWGGGTLYiddgkpLPgMFEETIrnlrei 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 272 ----FLSAIEKYRVMMAFMvpplmvflAKHPIVDKYDLSSLMVLLCGAAPLSRETEDQIK--------ERIgvPFIrQGY 339
Cdd:PRK12582 316 sptvYGNVPAGYAMLAEAM--------EKDDALRRSFFKNLRLMAYGGATLSDDLYERMQalavrttgHRI--PFY-TGY 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 340 GLSES---TLSVLVQNDefcKPGSVGVLKVGIYAKVIdPDTGKLlganergELCFKGDGIMKGYIGDTKSTQTAI-KDGW 415
Cdd:PRK12582 385 GATETaptTTGTHWDTE---RVGLIGLPLPGVELKLA-PVGDKY-------EVRVKGPNVTPGYHKDPELTAAAFdEEGF 453
|
410
....*....|.
gi 21355181 416 LHTGDIGYYDD 426
Cdd:PRK12582 454 YRLGDAARFVD 464
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
58-534 |
3.10e-10 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 62.74 E-value: 3.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 58 MHKSIVRLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVT-----YSDREVDHAINLskpkiIFASK 132
Cdd:PRK06060 36 IHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPElhrddHALAARNTEPAL-----VVTSD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 133 ITIDRVAKvasknkfvkgiialsgtskkfKNIYDLKELMEDEKfKTQPDFTSPAANkdEDVSLIVCSSGTTGLPKGVQLT 212
Cdd:PRK06060 111 ALRDRFQP---------------------SRVAEAAELMSEAA-RVAPGGYEPMGG--DALAYATYTSGTTGPPKAAIHR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 213 QMNLLATLDS------QIQPTVIPMEEVTL-----LTVIPWFH-AFGCLTLITTACVGArlvylpkfEEKLFLSAieKYR 280
Cdd:PRK06060 167 HADPLTFVDAmcrkalRLTPEDTGLCSARMyfaygLGNSVWFPlATGGSAVINSAPVTP--------EAAAILSA--RFG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 281 VMMAFMVPPlmvFLAKhpIVDKYDLSSLMVLLCgAAPLSRETEDQIKERI-----GVPfIRQGYGLSESTLSVLVQNDEF 355
Cdd:PRK06060 237 PSVLYGVPN---FFAR--VIDSCSPDSFRSLRC-VVSAGEALELGLAERLmeffgGIP-ILDGIGSTEVGQTFVSNRVDE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 356 CKPGSVGVLKVGIYAKVIDPDtGKLLGANERGELCFKGDGIMKGYIGDTKSTQTaiKDGWLHTGDIGYYDDDFEFFIVDR 435
Cdd:PRK06060 310 WRLGTLGRVLPPYEIRVVAPD-GTTAGPGVEGDLWVRGPAIAKGYWNRPDSPVA--NEGWLDTRDRVCIDSDGWVTYRCR 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 436 IKELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGELPLAFVVKqANVQLTENEVIQFVND---NASPAKRLRG 512
Cdd:PRK06060 387 ADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVA-TSGATIDGSVMRDLHRgllNRLSAFKVPH 465
|
490 500
....*....|....*....|..
gi 21355181 513 GVIFVDEIPKNPSGKILRRILR 534
Cdd:PRK06060 466 RFAVVDRLPRTPNGKLVRGALR 487
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
189-456 |
3.15e-10 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 63.26 E-value: 3.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 189 KDEDVSLIVCSSGTTGLPKGVQLTQMNLLATLDSQIQPTVIPM-EEVTLLTVIPWFHAFGCL-TLITTACVGARLVYL-P 265
Cdd:PRK05691 164 QPDDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGIDLnPDDVIVSWLPLYHDMGLIgGLLQPIFSGVPCVLMsP 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 266 KF--EEKL-FLSAIEKYRVMMAFMvPPLMVFLAKHPIVD----KYDLSSLMVLLCGAAPLSRETEDQIKERI-GVPFIRQ 337
Cdd:PRK05691 244 AYflERPLrWLEAISEYGGTISGG-PDFAYRLCSERVSEsaleRLDLSRWRVAYSGSEPIRQDSLERFAEKFaACGFDPD 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 338 G----YGLSESTLSV------------------LVQNDEFCKPGSV----GVLKVGIYAKVIDPDTGKLLGANERGELCF 391
Cdd:PRK05691 323 SffasYGLAEATLFVsggrrgqgipaleldaeaLARNRAEPGTGSVlmscGRSQPGHAVLIVDPQSLEVLGDNRVGEIWA 402
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21355181 392 KGDGIMKGYIGDTKSTQTAI--KDG--WLHTGDIGYYDDDfEFFIVDRIKELIKYKGYQVPPAEIEALL 456
Cdd:PRK05691 403 SGPSIAHGYWRNPEASAKTFveHDGrtWLRTGDLGFLRDG-ELFVTGRLKDMLIVRGHNLYPQDIEKTV 470
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
32-531 |
7.86e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 61.50 E-value: 7.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 32 LDKYKSFGDRTVLVdAVNGVEYSASFmhksivrlayilqkLGvkqndvvglssensvnfalAMFAGL-AVgatvaPLNVT 110
Cdd:PRK05850 52 LRRHGSTGDRAVIL-APQGLEYIVAF--------------LG-------------------ALQAGLiAV-----PLSVP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 111 Y---SDREVDHAINLSKPKIIFASKITIDRVAK-VASKNKFVKG-IIALsgtskkfkniyDLKELMEDEKfktqPDFTSP 185
Cdd:PRK05850 93 QggaHDERVSAVLRDTSPSVVLTTSAVVDDVTEyVAPQPGQSAPpVIEV-----------DLLDLDSPRG----SDARPR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 186 AAnkdEDVSLIVCSSGTTGLPKGVQLTQMNLLATLDsQI------QPTVIPMEEVTLLTVIPWFHAFGcltLITTAC--- 256
Cdd:PRK05850 158 DL---PSTAYLQYTSGSTRTPAGVMVSHRNVIANFE-QLmsdyfgDTGGVPPPDTTVVSWLPFYHDMG---LVLGVCapi 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 257 VGARLVYLpkfeeklfLSAiekyrvmMAFMVPPL--MVFLAKHP-----------------IVDK----YDLSSLMVLLC 313
Cdd:PRK05850 231 LGGCPAVL--------TSP-------VAFLQRPArwMQLLASNPhafsaapnfafelavrkTSDDdmagLDLGGVLGIIS 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 314 GAAPLSRETEDQIKERIGvPF------IRQGYGLSESTLSV----------LVQND---------EFCKPG------SVG 362
Cdd:PRK05850 296 GSERVHPATLKRFADRFA-PFnlretaIRPSYGLAEATVYVatrepgqppeSVRFDyeklsaghaKRCETGggtplvSYG 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 363 VLKVGIyAKVIDPDTGKLLGANERGELCFKGDGIMKGYIGDTKSTQT-----------AIKDG-WLHTGDIGYYDDDfEF 430
Cdd:PRK05850 375 SPRSPT-VRIVDPDTCIECPAGTVGEIWVHGDNVAAGYWQKPEETERtfgatlvdpspGTPEGpWLRTGDLGFISEG-EL 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 431 FIVDRIKELIKYKGYQVPPAEIEALL--LT-----------NDKIKDAAVI-----GKPDEEAGELpLAFVvkqanvqlt 492
Cdd:PRK05850 453 FIVGRIKDLLIVDGRNHYPDDIEATIqeITggrvaaisvpdDGTEKLVAIIelkkrGDSDEEAMDR-LRTV--------- 522
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 21355181 493 ENEVIQFVndnaSPAKRLR-GGVIFV--DEIPKNPSGKILRR 531
Cdd:PRK05850 523 KREVTSAI----SKSHGLSvADLVLVapGSIPITTSGKIRRA 560
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
64-469 |
4.16e-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: 4.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 64 RLAYILQK-LGVKQNDVVGLSSENSVNFaLAMFAGLA-VGATVAPLNVTYSDREVDHAINLSKPKIIFASKITIDRVAKV 141
Cdd:cd05938 17 QAARALLAhAGLRPGDTVALLLGNEPAF-LWIWLGLAkLGCPVAFLNTNIRSKSLLHCFRCCGAKVLVVAPELQEAVEEV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 142 --ASKNKFVKgIIALSGTSKKfKNIYDLKELMED-------EKFKTQPDFTSPAankdedvsLIVCSSGTTGLPKGVQLT 212
Cdd:cd05938 96 lpALRADGVS-VWYLSHTSNT-EGVISLLDKVDAasdepvpASLRAHVTIKSPA--------LYIYTSGTTGLPKAARIS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 213 QMNLLATldSQIQPTVIPMEEVTLLTVIPWFHAFGCLTLItTACV--GARLVYLPKFEEKLFLSAIEKYRVMMAFMVPPL 290
Cdd:cd05938 166 HLRVLQC--SGFLSLCGVTADDVIYITLPLYHSSGFLLGI-GGCIelGATCVLKPKFSASQFWDDCRKHNVTVIQYIGEL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 291 MVFLAKHPivDKYDLSSLMVLLCGAAPLSRETEDQIKERIGVPFIRQGYGLSESTLSVLVQNDefcKPGSVGvlKVGIYA 370
Cdd:cd05938 243 LRYLCNQP--QSPNDRDHKVRLAIGNGLRADVWREFLRRFGPIRIREFYGSTEGNIGFFNYTG---KIGAVG--RVSYLY 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 371 KVI--------DPDTGKLLgANERGeLCF---KGD-GIM----------KGYIGDTKSTQTAI-------KDGWLHTGDI 421
Cdd:cd05938 316 KLLfpfelikfDVEKEEPV-RDAQG-FCIpvaKGEpGLLvakitqqspfLGYAGDKEQTEKKLlrdvfkkGDVYFNTGDL 393
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 21355181 422 GYYD-DDFEFFIvDRIKELIKYKGYQVPPAEIEALLLTNDKIKDAAVIG 469
Cdd:cd05938 394 LVQDqQNFLYFH-DRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVYG 441
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
39-528 |
7.49e-09 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341309 [Multi-domain] Cd Length: 449 Bit Score: 57.87 E-value: 7.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 39 GDRTVLVDAVNG--VEYSASFMHKSIVRLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREV 116
Cdd:cd17654 1 PDRPALIIDQTTsdTTVSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 117 DHainlskpkiiFASKITIDRVAKvaskNKFVkGIIALSGTSkkfkniydlkelmEDEKFKTQPDFTSpaankdedvSLI 196
Cdd:cd17654 81 LT----------VMKKCHVSYLLQ----NKEL-DNAPLSFTP-------------EHRHFNIRTDECL---------AYV 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 197 VCSSGTTGLPKGVQLTQMNLLATLDSQIQPTVIPMEEVTLLTVIPWFHAFgCLTLITTACVGARLVYLP---KFEEKLFL 273
Cdd:cd17654 124 IHTSGTTGTPKIVAVPHKCILPNIQHFRSLFNITSEDILFLTSPLTFDPS-VVEIFLSLSSGATLLIVPtsvKVLPSKLA 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 274 SAI-EKYRVMMAFMVPPLMVFLAKHPIVDKY--DLSSLMVLLCGAAPLSRETEDQIKERIGVPF-IRQGYGLSE----ST 345
Cdd:cd17654 203 DILfKRHRITVLQATPTLFRRFGSQSIKSTVlsATSSLRVLALGGEPFPSLVILSSWRGKGNRTrIFNIYGITEvscwAL 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 346 LSVLVQNDEFCKPGS-VGVLKVGIYAKVIDPDTGKL-LGANERGelcfkgdGIMKGYIGDTKSTqtaikdgWLHTGDIGY 423
Cdd:cd17654 283 AYKVPEEDSPVQLGSpLLGTVIEVRDQNGSEGTGQVfLGGLNRV-------CILDDEVTVPKGT-------MRATGDFVT 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 424 YDDDfEFFIVDRIKELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAgelpLAFVVKQANVQLTENEVIQFVndn 503
Cdd:cd17654 349 VKDG-ELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGVESCAVTLSDQQRL----IAFIVGESSSSRIHKELQLTL--- 420
|
490 500
....*....|....*....|....*
gi 21355181 504 aSPAKRLRGGVIFVDEIPKNPSGKI 528
Cdd:cd17654 421 -LSSHAIPDTFVQIDKLPLTSHGKV 444
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
181-454 |
1.83e-08 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 57.06 E-value: 1.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 181 DFTsPAANKDEDVSLIVCSSGTTGLPKGVQLT---------QMNL-LATLDSQIQptvipmeEVTLLtviPWFHAFGCLT 250
Cdd:PRK12476 184 SFV-PVELDTDDVSHLQYTSGSTRPPVGVEIThravgtnlvQMILsIDLLDRNTH-------GVSWL---PLYHDMGLSM 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 251 LITTACVGARL--------VYLPKFEEKLFLSAIEKYRVMMAfmVPPLMVFLAKH----PIVDKYDLSSLmVLLCGAAPL 318
Cdd:PRK12476 253 IGFPAVYGGHStlmsptafVRRPQRWIKALSEGSRTGRVVTA--APNFAYEWAAQrglpAEGDDIDLSNV-VLIIGSEPV 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 319 SRETEDQIKERIGvPF------IRQGYGLSESTL-----------SVLVQNDEFCKPG----------------SVGVLK 365
Cdd:PRK12476 330 SIDAVTTFNKAFA-PYglprtaFKPSYGIAEATLfvatiapdaepSVVYLDREQLGAGravrvaadapnavahvSCGQVA 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 366 VGIYAKVIDPDTGKLLGANERGELCFKGDGIMKGYIGDTKSTQ-------------------TAIKDGWLHTGDIGYYDD 426
Cdd:PRK12476 409 RSQWAVIVDPDTGAELPDGEVGEIWLHGDNIGRGYWGRPEETErtfgaklqsrlaegshadgAADDGTWLRTGDLGVYLD 488
|
330 340
....*....|....*....|....*...
gi 21355181 427 DfEFFIVDRIKELIKYKGYQVPPAEIEA 454
Cdd:PRK12476 489 G-ELYITGRIADLIVIDGRNHYPQDIEA 515
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
40-213 |
2.95e-08 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 56.59 E-value: 2.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 40 DRTVLVDAVNGVEYSAsfMHKSIVRLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREVDHA 119
Cdd:PRK10252 473 DAPALADARYQFSYRE--MREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMM 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 120 INLSKPKIIFASkitidrvakvasknkfvkgiialSGTSKKFKNIYDLKELMEDEKFkTQPDFTSPAANKDEDVSLIVCS 199
Cdd:PRK10252 551 LEDARPSLLITT-----------------------ADQLPRFADVPDLTSLCYNAPL-APQGAAPLQLSQPHHTAYIIFT 606
|
170
....*....|....
gi 21355181 200 SGTTGLPKGVQLTQ 213
Cdd:PRK10252 607 SGSTGRPKGVMVGQ 620
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
64-533 |
8.19e-08 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 55.56 E-value: 8.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 64 RLAYILQKLGVKQNDVVGLSSENSVNFaLAMFAG-LAVGATVAPLNVTYSDREVDHAINLSKPKIIfaskitidrVAKVA 142
Cdd:PRK05691 3757 RLGHALRAAGVGVDQPVALLAERGLDL-LGMIVGsFKAGAGYLPLDPGLPAQRLQRIIELSRTPVL---------VCSAA 3826
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 143 SKNKFVKGIIALSGTSKKFKNIYDlkELMEDEKFKTQPDFTSPAANkdedVSLIVCSSGTTGLPKGVQLTQMNLLATLDS 222
Cdd:PRK05691 3827 CREQARALLDELGCANRPRLLVWE--EVQAGEVASHNPGIYSGPDN----LAYVIYTSGSTGLPKGVMVEQRGMLNNQLS 3900
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 223 QIQPTVIPMEEVTLLTVIPWFHaFGCLTLITTACVGARLVYLPK---FEEKLFLSAIEKYRVMMAFMVPPLMV-FLAKhp 298
Cdd:PRK05691 3901 KVPYLALSEADVIAQTASQSFD-ISVWQFLAAPLFGARVEIVPNaiaHDPQGLLAHVQAQGITVLESVPSLIQgMLAE-- 3977
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 299 ivDKYDLSSLMVLLCGAAPLSRETEDQIKER---IGvpfIRQGYGLSESTLSV-LVQNDEFCKPGSvgvlkvgiYAKVID 374
Cdd:PRK05691 3978 --DRQALDGLRWMLPTGEAMPPELARQWLQRypqIG---LVNAYGPAECSDDVaFFRVDLASTRGS--------YLPIGS 4044
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 375 P-DTGKL-----------LGAneRGELCFKGDGIMKGYIGDTKSTQTA--------IKDGWLHTGDIGYYDDDFEFFIVD 434
Cdd:PRK05691 4045 PtDNNRLylldealelvpLGA--VGELCVAGTGVGRGYVGDPLRTALAfvphpfgaPGERLYRTGDLARRRSDGVLEYVG 4122
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 435 RIKELIKYKGYQVPPAEIEALLLTNDKIKDAAViGKPDEEAGELPLAFVVKQANVQLTENEVIQFVNdnaspakRLRGGV 514
Cdd:PRK05691 4123 RIDHQVKIRGYRIELGEIEARLHEQAEVREAAV-AVQEGVNGKHLVGYLVPHQTVLAQGALLERIKQ-------RLRAEL 4194
|
490 500
....*....|....*....|....*...
gi 21355181 515 ---------IFVDEIPKNPSGKILRRIL 533
Cdd:PRK05691 4195 pdymvplhwLWLDRLPLNANGKLDRKAL 4222
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
306-468 |
1.13e-07 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 54.00 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 306 SSLMVLLCGAAPLSRETEDQIKERIGVPfIRQGYGLSESTLSVLVQNDEfcKPGsvgvLKVG---IYAKVIDPDTGKLLG 382
Cdd:COG1541 203 LSLKKGIFGGEPWSEEMRKEIEERWGIK-AYDIYGLTEVGPGVAYECEA--QDG----LHIWedhFLVEIIDPETGEPVP 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 383 ANERGELCFkgdgimkgyigdtkstqTAI-KDGW----LHTGDIGYYDDD----------FEfFIVDRIKELIKYKGYQV 447
Cdd:COG1541 276 EGEEGELVV-----------------TTLtKEAMplirYRTGDLTRLLPEpcpcgrthprIG-RILGRADDMLIIRGVNV 337
|
170 180
....*....|....*....|.
gi 21355181 448 PPAEIEALLLTNDKIKDAAVI 468
Cdd:COG1541 338 FPSQIEEVLLRIPEVGPEYQI 358
|
|
| PaaK |
cd05913 |
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic ... |
306-391 |
5.50e-06 |
|
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic degradation pathway, by converting phenylacetic acid (PA) into phenylacetyl-CoA (PA-CoA). Phenylacetate-CoA ligase has been found in proteobacteria as well as gram positive prokaryotes. The enzyme is specifically induced after aerobic growth in a chemically defined medium containing PA or phenylalanine (Phe) as the sole carbon source. PaaKs are members of the adenylate-forming enzyme (AFE) family. However, sequence comparison reveals divergent features of PaaK with respect to the superfamily, including a novel N-terminal sequence.
Pssm-ID: 341239 [Multi-domain] Cd Length: 425 Bit Score: 48.77 E-value: 5.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 306 SSLMVLLCGAAPLSRETEDQIKERIGVpFIRQGYGLSESTLsVLVQNDEFCKPGSVGVlKVGIYAKVIDPDTGKLLGANE 385
Cdd:cd05913 198 LSLKVGIFGAEPWTEEMRKRIERRLGI-KAYDIYGLTEIIG-PGVAFECEEKDGLHIW-EDHFIPEIIDPETGEPVPPGE 274
|
....*.
gi 21355181 386 RGELCF 391
Cdd:cd05913 275 VGELVF 280
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
64-534 |
7.64e-05 |
|
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.
Pssm-ID: 341265 [Multi-domain] Cd Length: 629 Bit Score: 45.34 E-value: 7.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 64 RLAYILQKLGVKQND-VVGLSSeNSVNFALAMFAGLAVGAT---VAPlnvtysDREVDHAIN-LS--KPKIIFA------ 130
Cdd:cd05943 110 RLAAALRALGVKPGDrVAGYLP-NIPEAVVAMLATASIGAIwssCSP------DFGVPGVLDrFGqiEPKVLFAvdayty 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 131 SKITIDRVAKVASknkFVKG------IIALSGTSKKFKNiydlkELMEDEKFKTQPDFTSP-AANKDEDVSL-------I 196
Cdd:cd05943 183 NGKRHDVREKVAE---LVKGlpsllaVVVVPYTVAAGQP-----DLSKIAKALTLEDFLATgAAGELEFEPLpfdhplyI 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 197 VCSSGTTGLPK-------GVQLTQMNLLAtLDSQIQPTvipmeevtllTVIPWFHAFGCLT---LITTACVGARLV-Y-- 263
Cdd:cd05943 255 LYSSGTTGLPKcivhgagGTLLQHLKEHI-LHCDLRPG----------DRLFYYTTCGWMMwnwLVSGLAVGATIVlYdg 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 264 ---------LPKFEEKL----------FLSAIEKyrvmmAFMVPPlmvflakhpivDKYDLSSLMVLLCGAAPLSRETED 324
Cdd:cd05943 324 spfypdtnaLWDLADEEgitvfgtsakYLDALEK-----AGLKPA-----------ETHDLSSLRTILSTGSPLKPESFD 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 325 ----QIKERIGVPFIRQG------YGLSESTLSVlvqndefcKPGSVGVLKVGIYAKVIDPDTGKLLGanERGEL-CFKG 393
Cdd:cd05943 388 yvydHIKPDVLLASISGGtdiiscFVGGNPLLPV--------YRGEIQCRGLGMAVEAFDEEGKPVWG--EKGELvCTKP 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 394 DGIMK-GYIGDT-----KSTQTAIKDG-WLHtGDIGYYDDDFEFFIVDRIKELIKYKGYQVPPAEIEALLLTNDKIKDAA 466
Cdd:cd05943 458 FPSMPvGFWNDPdgsryRAAYFAKYPGvWAH-GDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSL 536
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21355181 467 VIGKPDEEAGELPLAFVVKQANVQLTEnEVIQFVND----NASPaKRLRGGVIFVDEIPKNPSGKIL----RRILR 534
Cdd:cd05943 537 VVGQEWKDGDERVILFVKLREGVELDD-ELRKRIRStirsALSP-RHVPAKIIAVPDIPRTLSGKKVevavKKIIA 610
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
64-533 |
2.68e-04 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 44.00 E-value: 2.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 64 RLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREVDHAINLSkpkiifaskitidrvakvas 143
Cdd:PRK05691 2225 RLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHYMIEDS-------------------- 2284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 144 knkfvkGIIALSGTSKKFKNIYDL-----KELMEDEK--FKTQPDFTSPAANKDEDVSLIVCSSGTTGLPKGVQLTQMNL 216
Cdd:PRK05691 2285 ------GIGLLLSDRALFEALGELpagvaRWCLEDDAaaLAAYSDAPLPFLSLPQHQAYLIYTSGSTGKPKGVVVSHGEI 2358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 217 LATLDSQIQPTVIPMEEVTLLTVIPWFHAFGCLTLITTACvGARLVYLPK--FEEKLFLSAIEKYRVMMAFMVPPLMVFL 294
Cdd:PRK05691 2359 AMHCQAVIERFGMRADDCELHFYSINFDAASERLLVPLLC-GARVVLRAQgqWGAEEICQLIREQQVSILGFTPSYGSQL 2437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 295 AKHPIVDKYDLSSLMVLLCGAApLSRETEDQIKERIGVPFIRQGYGLSEST---LSVLVQNDEFCKPGSVGVLKVgIYAK 371
Cdd:PRK05691 2438 AQWLAGQGEQLPVRMCITGGEA-LTGEHLQRIRQAFAPQLFFNAYGPTETVvmpLACLAPEQLEEGAASVPIGRV-VGAR 2515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 372 V---IDPDTGkLLGANERGELCFKGDGIMKGYIGDTKSTQT-------AIKDGWLH-TGDIGYYDDDFEFFIVDRIKELI 440
Cdd:PRK05691 2516 VayiLDADLA-LVPQGATGELYVGGAGLAQGYHDRPGLTAErfvadpfAADGGRLYrTGDLVRLRADGLVEYVGRIDHQV 2594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 441 KYKGYQVPPAEIEALLLTNDKIKDAAVIGKpDEEAGELPLAFVVKQ-------ANVQLTE---NEVIQFVNDNASPAKrl 510
Cdd:PRK05691 2595 KIRGFRIELGEIESRLLEHPAVREAVVLAL-DTPSGKQLAGYLVSAvagqddeAQAALREalkAHLKQQLPDYMVPAH-- 2671
|
490 500
....*....|....*....|...
gi 21355181 511 rggVIFVDEIPKNPSGKILRRIL 533
Cdd:PRK05691 2672 ---LILLDSLPLTANGKLDRRAL 2691
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
450-533 |
1.30e-03 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 41.70 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 450 AEI----EALlltnDKIKDAAVIGKPDEEAGE-LPLaFVVKQANVQLTEnEVIQFVND----NAS----PAKrlrggVIF 516
Cdd:PRK03584 534 AEIyrqvEAL----PEVLDSLVIGQEWPDGDVrMPL-FVVLAEGVTLDD-ALRARIRTtirtNLSprhvPDK-----IIA 602
|
90 100
....*....|....*....|.
gi 21355181 517 VDEIPKNPSGKIL----RRIL 533
Cdd:PRK03584 603 VPDIPRTLSGKKVelpvKKLL 623
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
64-213 |
1.68e-03 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 41.22 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 64 RLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREVDHAINLSKPKIIFASKITI-------- 135
Cdd:PLN03052 220 RVANALDALGFEKGDAIAIDMPMNVHAVIIYLAIILAGCVVVSIADSFAPSEIATRLKISKAKAIFTQDVIVrggksipl 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355181 136 -DRVAKVASKNKFVkgiIALSGTS--KKFKNiYDL--KELMEDEKFKTQPDFTSPAANKDEDVSLIVCSSGTTGLPKGVQ 210
Cdd:PLN03052 300 ySRVVEAKAPKAIV---LPADGKSvrVKLRE-GDMswDDFLARANGLRRPDEYKAVEQPVEAFTNILFSSGTTGEPKAIP 375
|
...
gi 21355181 211 LTQ 213
Cdd:PLN03052 376 WTQ 378
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
514-542 |
5.97e-03 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 39.41 E-value: 5.97e-03
10 20
....*....|....*....|....*....
gi 21355181 514 VIFVDEIPKNPSGKILRRILREMLKKQKS 542
Cdd:PLN03051 466 VKIVPELPRNASNKLLRRVLRDQLKKELS 494
|
|
| |
