|
Name |
Accession |
Description |
Interval |
E-value |
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
1-481 |
0e+00 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 888.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 1 METMPNWLKQRAFLTPDRTAIEIEEEKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAV 80
Cdd:PRK03640 1 METMPNWLKQRAFLTPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 81 LLNTRLSREELLWQMDDAEVVCLVTDQQFDANDVPVYS--FAEVMHGLKVEASIQEEFSLEEAMTIIYTSGTTGKPKGVI 158
Cdd:PRK03640 81 LLNTRLSREELLWQLDDAEVKCLITDDDFEAKLIPGISvkFAELMNGPKEEAEIQEEFDLDEVATIMYTSGTTGKPKGVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 159 LTYGNHWASAVGSSLNLGLRDDDCWLACMPMFHVGGLSLLMKNIMYGMRILLVPKYDADFIHKALQTRGVTIISVVSKML 238
Cdd:PRK03640 161 QTYGNHWWSAVGSALNLGLTEDDCWLAAVPIFHISGLSILMRSVIYGMRVVLVEKFDAEKINKLLQTGGVTIISVVSTML 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 239 TDLLERLGEETYPSSLRCMLLGGGPAPKPLLETCVDKGIPVYQTYGMTETSSQICTLSADYMLTKVGSAGKPLFQCQLRI 318
Cdd:PRK03640 241 QRLLERLGEGTYPSSFRCMLLGGGPAPKPLLEQCKEKGIPVYQSYGMTETASQIVTLSPEDALTKLGSAGKPLFPCELKI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 319 EKDGVVVPPLVEGEIVVKGPNVTGGYFNREDATRETIQNGWLHTGDLGYLDEEGFLYVLDRRSDLIISGGENIYPAQIEE 398
Cdd:PRK03640 321 EKDGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQDGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 399 VLLSHPMVAEAGVVGMTDDKWGQVPAAFVVKNGEVTEEEIIHFCEEKLAKYKVPKKACFLEELPRNASKKLLRRELRQLV 478
Cdd:PRK03640 401 VLLSHPGVAEAGVVGVPDDKWGQVPVAFVVKSGEVTEEELRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHELKQLV 480
|
...
gi 446371684 479 EEM 481
Cdd:PRK03640 481 EEM 483
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
27-476 |
0e+00 |
|
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: 726.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 27 KVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSREELLWQMDDAEVVClvtd 106
Cdd:cd05912 1 SYTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVKL---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 107 qqfdandvpvysfaevmhglkveasiqeefslEEAMTIIYTSGTTGKPKGVILTYGNHWASAVGSSLNLGLRDDDCWLAC 186
Cdd:cd05912 77 --------------------------------DDIATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGLTEDDNWLCA 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 187 MPMFHVGGLSLLMKNIMYGMRILLVPKYDADFIHKALQTRGVTIISVVSKMLTDLLERLGEeTYPSSLRCMLLGGGPAPK 266
Cdd:cd05912 125 LPLFHISGLSILMRSVIYGMTVYLVDKFDAEQVLHLINSGKVTIISVVPTMLQRLLEILGE-GYPNNLRCILLGGGPAPK 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 267 PLLETCVDKGIPVYQTYGMTETSSQICTLSADYMLTKVGSAGKPLFQCQLRIEKDGVvvPPLVEGEIVVKGPNVTGGYFN 346
Cdd:cd05912 204 PLLEQCKEKGIPVYQSYGMTETCSQIVTLSPEDALNKIGSAGKPLFPVELKIEDDGQ--PPYEVGEILLKGPNVTKGYLN 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 347 REDATRETIQNGWLHTGDLGYLDEEGFLYVLDRRSDLIISGGENIYPAQIEEVLLSHPMVAEAGVVGMTDDKWGQVPAAF 426
Cdd:cd05912 282 RPDATEESFENGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAF 361
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 446371684 427 VVKNGEVTEEEIIHFCEEKLAKYKVPKKACFLEELPRNASKKLLRRELRQ 476
Cdd:cd05912 362 VVSERPISEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHELKQ 411
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
4-480 |
6.60e-174 |
|
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: 496.26 E-value: 6.60e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 4 MPNWLKQRAFLTPDRTAIEIEEEKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLN 83
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 84 TRLSREELLWQMDDAEVVCLVTdqqfdandvpvysfaevmhglkveasiqeefsleeaMTIIYTSGTTGKPKGVILTYGN 163
Cdd:COG0318 81 PRLTAEELAYILEDSGARALVT------------------------------------ALILYTSGTTGRPKGVMLTHRN 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 164 HWASAVGSSLNLGLRDDDCWLACMPMFHVGGLSL-LMKNIMYGMRILLVPKYDADFIHKALQTRGVTIISVVSKMLTDLL 242
Cdd:COG0318 125 LLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVgLLAPLLAGATLVLLPRFDPERVLELIERERVTVLFGVPTMLARLL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 243 ERLGEETYP-SSLRCMLLGGGPAPKPLLETCVDK-GIPVYQTYGMTETSSQICTLSADYMLTKVGSAGKPLFQCQLRI-E 319
Cdd:COG0318 205 RHPEFARYDlSSLRLVVSGGAPLPPELLERFEERfGVRIVEGYGLTETSPVVTVNPEDPGERRPGSVGRPLPGVEVRIvD 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 320 KDGVVVPPLVEGEIVVKGPNVTGGYFNREDATRETIQNGWLHTGDLGYLDEEGFLYVLDRRSDLIISGGENIYPAQIEEV 399
Cdd:COG0318 285 EDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAFRDGWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEV 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 400 LLSHPMVAEAGVVGMTDDKWGQVPAAFVVKN--GEVTEEEIIHFCEEKLAKYKVPKKACFLEELPRNASKKLLRRELRQL 477
Cdd:COG0318 365 LAAHPGVAEAAVVGVPDEKWGERVVAFVVLRpgAELDAEELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRER 444
|
...
gi 446371684 478 VEE 480
Cdd:COG0318 445 YAA 447
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
29-474 |
1.76e-165 |
|
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: 474.24 E-value: 1.76e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 29 TFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSREELLWQMDDAEVVCLVTDQQ 108
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 109 FDANDVPVYSFAEVMHGLKVEASIQEEFSLEEAMTIIYTSGTTGKPKGVILTYGNHWASAVGSSLNLGLRDDDCWLACMP 188
Cdd:TIGR01923 81 LEEKDFQADSLDRIEAAGRYETSLSASFNMDQIATLMFTSGTTGKPKAVPHTFRNHYASAVGSKENLGFTEDDNWLLSLP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 189 MFHVGGLSLLMKNIMYGMRILLVPKyDADFIHkALQTRGVTIISVVSKMLTDLLERLGEETypsSLRCMLLGGGPAPKPL 268
Cdd:TIGR01923 161 LYHISGLSILFRWLIEGATLRIVDK-FNQLLE-MIANERVTHISLVPTQLNRLLDEGGHNE---NLRKILLGGSAIPAPL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 269 LETCVDKGIPVYQTYGMTETSSQICTLSADyMLTKVGSAGKPLFQCQLRIEKDGVVVpplvEGEIVVKGPNVTGGYFNRE 348
Cdd:TIGR01923 236 IEEAQQYGLPIYLSYGMTETCSQVTTATPE-MLHARPDVGRPLAGREIKIKVDNKEG----HGEIMVKGANLMKGYLYQG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 349 DATRETIQNGWLHTGDLGYLDEEGFLYVLDRRSDLIISGGENIYPAQIEEVLLSHPMVAEAGVVGMTDDKWGQVPAAFVV 428
Cdd:TIGR01923 311 ELTPAFEQQGWFNTGDIGELDGEGFLYVLGRRDDLIISGGENIYPEEIETVLYQHPGIQEAVVVPKPDAEWGQVPVAYIV 390
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 446371684 429 KNGEVTEEEIIHFCEEKLAKYKVPKKACFLEELPRNASKKLLRREL 474
Cdd:TIGR01923 391 SESDISQAKLIAYLTEKLAKYKVPIAFEKLDELPYNASGKILRNQL 436
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
8-471 |
4.31e-158 |
|
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: 455.53 E-value: 4.31e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 8 LKQRAFLTPDRTAIEIEEEKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLS 87
Cdd:cd17631 1 LRRRARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 88 REELLWQMDDAEvvclvtdqqfdandvpvysfAEVMhglkveasiqeefsLEEAMTIIYTSGTTGKPKGVILTYGNHWAS 167
Cdd:cd17631 81 PPEVAYILADSG--------------------AKVL--------------FDDLALLMYTSGTTGRPKGAMLTHRNLLWN 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 168 AVGSSLNLGLRDDDCWLACMPMFHVGGLSL-LMKNIMYGMRILLVPKYDADFIHKALQTRGVTIISVVSKMLTDLLERLG 246
Cdd:cd17631 127 AVNALAALDLGPDDVLLVVAPLFHIGGLGVfTLPTLLRGGTVVILRKFDPETVLDLIERHRVTSFFLVPTMIQALLQHPR 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 247 EETY-PSSLRCMLLGGGPAPKPLLETCVDKGIPVYQTYGMTETSSQICTLSADYMLTKVGSAGKPLFQCQLRI-EKDGVV 324
Cdd:cd17631 207 FATTdLSSLRAVIYGGAPMPERLLRALQARGVKFVQGYGMTETSPGVTFLSPEDHRRKLGSAGRPVFFVEVRIvDPDGRE 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 325 VPPLVEGEIVVKGPNVTGGYFNREDATRETIQNGWLHTGDLGYLDEEGFLYVLDRRSDLIISGGENIYPAQIEEVLLSHP 404
Cdd:cd17631 287 VPPGEVGEIVVRGPHVMAGYWNRPEATAAAFRDGWFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHP 366
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446371684 405 MVAEAGVVGMTDDKWGQVPAAFVVKN--GEVTEEEIIHFCEEKLAKYKVPKKACFLEELPRNASKKLLR 471
Cdd:cd17631 367 AVAEVAVIGVPDEKWGEAVVAVVVPRpgAELDEDELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
16-476 |
1.61e-151 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 441.93 E-value: 1.61e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 16 PDRTAIEIEEEKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSREELLWQM 95
Cdd:PRK06187 20 PDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPINIRLKPEEIAYIL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 96 DDAEVVCLVTDQQF-------------------------DANDVPVYSFAEVMHGlKVEASIQEEFSLEEAMTIIYTSGT 150
Cdd:PRK06187 100 NDAEDRVVLVDSEFvpllaailpqlptvrtvivegdgpaAPLAPEVGEYEELLAA-ASDTFDFPDIDENDAAAMLYTSGT 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 151 TGKPKGVILTYGNHWASAVGSSLNLGLRDDDCWLACMPMFHVGGLSLLMKNIMYGMRILLVPKYDADFIHKALQTRGVTI 230
Cdd:PRK06187 179 TGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVPMFHVHAWGLPYLALMAGAKQVIPRRFDPENLLDLIETERVTF 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 231 ISVVSKMLTDLL-ERLGEETYPSSLRCMLLGGGPAPKPLLETCVDK-GIPVYQTYGMTETSSQICTL----SADYMLTKV 304
Cdd:PRK06187 259 FFAVPTIWQMLLkAPRAYFVDFSSLRLVIYGGAALPPALLREFKEKfGIDLVQGYGMTETSPVVSVLppedQLPGQWTKR 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 305 GSAGKPLFQCQLRIEK-DGVVVPPLVE--GEIVVKGPNVTGGYFNREDATRETIQNGWLHTGDLGYLDEEGFLYVLDRRS 381
Cdd:PRK06187 339 RSAGRPLPGVEARIVDdDGDELPPDGGevGEIIVRGPWLMQGYWNRPEATAETIDGGWLHTGDVGYIDEDGYLYITDRIK 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 382 DLIISGGENIYPAQIEEVLLSHPMVAEAGVVGMTDDKWGQVPAAFVV-KNGE-VTEEEIIHFCEEKLAKYKVPKKACFLE 459
Cdd:PRK06187 419 DVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVlKPGAtLDAKELRAFLRGRLAKFKLPKRIAFVD 498
|
490
....*....|....*..
gi 446371684 460 ELPRNASKKLLRRELRQ 476
Cdd:PRK06187 499 ELPRTSVGKILKRVLRE 515
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
8-475 |
1.39e-131 |
|
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: 388.84 E-value: 1.39e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 8 LKQRAFLTPDRTAIEIEEEKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLS 87
Cdd:cd05936 5 LEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 88 REELLWQMDDAEVVCLVTDQqfdandvpvySFAEVMHGLKVEASIQEEfSLEEAMTIIYTSGTTGKPKGVILTYGNHWA- 166
Cdd:cd05936 85 PRELEHILNDSGAKALIVAV----------SFTDLLAAGAPLGERVAL-TPEDVAVLQYTSGTTGVPKGAMLTHRNLVAn 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 167 -SAVGSSLNLGLRDDDCWLACMPMFHVGGLSL-LMKNIMYGMRILLVPKYDADFIHKALQTRGVTIISVVSKMLTDLLER 244
Cdd:cd05936 154 aLQIKAWLEDLLEGDDVVLAALPLFHVFGLTVaLLLPLALGATIVLIPRFRPIGVLKEIRKHRVTIFPGVPTMYIALLNA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 245 LGEETY-PSSLRCMLLGGGPAPKPLLETCVDK-GIPVYQTYGMTETSSQICtLSADYMLTKVGSAGKPLFQCQLRI-EKD 321
Cdd:cd05936 234 PEFKKRdFSSLRLCISGGAPLPVEVAERFEELtGVPIVEGYGLTETSPVVA-VNPLDGPRKPGSIGIPLPGTEVKIvDDD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 322 GVVVPPLVEGEIVVKGPNVTGGYFNREDATRETIQNGWLHTGDLGYLDEEGFLYVLDRRSDLIISGGENIYPAQIEEVLL 401
Cdd:cd05936 313 GEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFVDGWLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLY 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446371684 402 SHPMVAEAGVVGMTDDKWGQVPAAFVV-KNGE-VTEEEIIHFCEEKLAKYKVPKKACFLEELPRNASKKLLRRELR 475
Cdd:cd05936 393 EHPAVAEAAVVGVPDPYSGEAVKAFVVlKEGAsLTEEEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
1-481 |
5.15e-131 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 388.45 E-value: 5.15e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 1 METMPNWLKQRAFLTPDRTAIEIEEEKVTFLQLHEKVVSVCEHLTH-VGVKRGQKVAVLMKNGMEMITVIHALSYVGAVA 79
Cdd:PRK06839 1 MQGIAYWIEKRAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIYeLNVKKGERIAILSQNSLEYIVLLFAIAKVECIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 80 VLLNTRLSREELLWQMDDAEVVCLVTDQQFDANDVPVYSFAEVMHGLKVEA---------SIQEEFSLEEAMTIIYTSGT 150
Cdd:PRK06839 81 VPLNIRLTENELIFQLKDSGTTVLFVEKTFQNMALSMQKVSYVQRVISITSlkeiedrkiDNFVEKNESASFIICYTSGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 151 TGKPKGVILTYGNHWASAVGSSLNLGLRDDDCWLACMPMFHVGGLSLL-MKNIMYGMRILLVPKYDADFIHKALQTRGVT 229
Cdd:PRK06839 161 TGKPKGAVLTQENMFWNALNNTFAIDLTMHDRSIVLLPLFHIGGIGLFaFPTLFAGGVIIVPRKFEPTKALSMIEKHKVT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 230 IISVVSKMLTDLLER-LGEETYPSSLRCMLLGGGPAPKPLLETCVDKGIPVYQTYGMTETSSQICTLSADYMLTKVGSAG 308
Cdd:PRK06839 241 VVMGVPTIHQALINCsKFETTNLQSVRWFYNGGAPCPEELMREFIDRGFLFGQGFGMTETSPTVFMLSEEDARRKVGSIG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 309 KPLFQCQLR-IEKDGVVVPPLVEGEIVVKGPNVTGGYFNREDATRETIQNGWLHTGDLGYLDEEGFLYVLDRRSDLIISG 387
Cdd:PRK06839 321 KPVLFCDYElIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEETIQDGWLCTGDLARVDEDGFVYIVGRKKEMIISG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 388 GENIYPAQIEEVLLSHPMVAEAGVVGMTDDKWGQVPAAFVVK--NGEVTEEEIIHFCEEKLAKYKVPKKACFLEELPRNA 465
Cdd:PRK06839 401 GENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKksSSVLIEKDVIEHCRLFLAKYKIPKEIVFLKELPKNA 480
|
490
....*....|....*.
gi 446371684 466 SKKLLRRELRQLVEEM 481
Cdd:PRK06839 481 TGKIQKAQLVNQLKSR 496
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
144-470 |
4.30e-122 |
|
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: 360.06 E-value: 4.30e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 144 IIYTSGTTGKPKGVILTYGNHWASAVGSSLNLGLRDDDCWLACMPMFHVGGLSLLMKNIMYGMRILLVPKYDADFIHKAL 223
Cdd:cd04433 5 ILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKFDPEAALELI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 224 QTRGVTIISVVSKMLTDLLERLGEETYP-SSLRCMLLGGGPAPKPLLETCVDK-GIPVYQTYGMTETSSQICTLSADYML 301
Cdd:cd04433 85 EREKVTILLGVPTLLARLLKAPESAGYDlSSLRALVSGGAPLPPELLERFEEApGIKLVNGYGLTETGGTVATGPPDDDA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 302 TKVGSAGKPLFQCQLRI-EKDGVVVPPLVEGEIVVKGPNVTGGYFNREDATRETIQNGWLHTGDLGYLDEEGFLYVLDRR 380
Cdd:cd04433 165 RKPGSVGRPVPGVEVRIvDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVDEDGWYRTGDLGRLDEDGYLYIVGRL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 381 SDLIISGGENIYPAQIEEVLLSHPMVAEAGVVGMTDDKWGQVPAAFVVKN--GEVTEEEIIHFCEEKLAKYKVPKKACFL 458
Cdd:cd04433 245 KDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRpgADLDAEELRAHVRERLAPYKVPRRVVFV 324
|
330
....*....|..
gi 446371684 459 EELPRNASKKLL 470
Cdd:cd04433 325 DALPRTASGKID 336
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
1-476 |
1.11e-113 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 344.58 E-value: 1.11e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 1 METMPNWLKQRAFLTPDRTAIEIEEEKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAV 80
Cdd:PRK07656 4 WMTLPELLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 81 LLNTRLSREE-----------LLWQMDD--------------AEVVCLVTDQQFDANDVPVYSFAEVM---HGLKVEASI 132
Cdd:PRK07656 84 PLNTRYTADEaayilargdakALFVLGLflgvdysattrlpaLEHVVICETEEDDPHTEKMKTFTDFLaagDPAERAPEV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 133 QEEfsleEAMTIIYTSGTTGKPKGVILTYGNHWASAVGSSLNLGLRDDDCWLACMPMFHVGGLSL-LMKNIMYGMRILLV 211
Cdd:PRK07656 164 DPD----DVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLAANPFFHVFGYKAgVNAPLMRGATILPL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 212 PKYDADFIHKALQTRGVTIISVVSKMLTDLLERLGEETYP-SSLRCMLLGGGPAPKPLLETCVDK-GIPVYQT-YGMTEt 288
Cdd:PRK07656 240 PVFDPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSAEDlSSLRLAVTGAASMPVALLERFESElGVDIVLTgYGLSE- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 289 SSQICTLS--ADYMLTKVGSAGKPLFQCQLRI-EKDGVVVPPLVEGEIVVKGPNVTGGYFNREDATRETI-QNGWLHTGD 364
Cdd:PRK07656 319 ASGVTTFNrlDDDRKTVAGTIGTAIAGVENKIvNELGEEVPVGEVGELLVRGPNVMKGYYDDPEATAAAIdADGWLHTGD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 365 LGYLDEEGFLYVLDRRSDLIISGGENIYPAQIEEVLLSHPMVAEAGVVGMTDDKWGQVPAAFVV-KNG-EVTEEEIIHFC 442
Cdd:PRK07656 399 LGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVlKPGaELTEEELIAYC 478
|
490 500 510
....*....|....*....|....*....|....
gi 446371684 443 EEKLAKYKVPKKACFLEELPRNASKKLLRRELRQ 476
Cdd:PRK07656 479 REHLAKYKVPRSIEFLDELPKNATGKVLKRALRE 512
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
10-476 |
4.70e-106 |
|
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: 324.27 E-value: 4.70e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 10 QRAFLTPDRTaieieeEKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSRE 89
Cdd:cd05926 3 APALVVPGST------PALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 90 ELLWQMDDAEVVCLVTDQQFD-----------------ANDVPVYSFAEVMHGLKVEASIQEEFSLEEAMT------IIY 146
Cdd:cd05926 77 EFEFYLADLGSKLVLTPKGELgpasraasklglailelALDVGVLIRAPSAESLSNLLADKKNAKSEGVPLpddlalILH 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 147 TSGTTGKPKGVILTYGNHWASA--VGSSLNLGlrDDDCWLACMPMFHVGGL-SLLMKNIMYGMRILLVPKYDADFIHKAL 223
Cdd:cd05926 157 TSGTTGRPKGVPLTHRNLAASAtnITNTYKLT--PDDRTLVVMPLFHVHGLvASLLSTLAAGGSVVLPPRFSASTFWPDV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 224 QTRGVTIISVVSKMLTDLLERLGEETY--PSSLRCMLLGGGPAPKPLLETCVDK-GIPVYQTYGMTETSSQICTLSADYM 300
Cdd:cd05926 235 RDYNATWYTAVPTIHQILLNRPEPNPEspPPKLRFIRSCSASLPPAVLEALEATfGAPVLEAYGMTEAAHQMTSNPLPPG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 301 LTKVGSAGKPlFQCQLRI-EKDGVVVPPLVEGEIVVKGPNVTGGYFNREDATRE-TIQNGWLHTGDLGYLDEEGFLYVLD 378
Cdd:cd05926 315 PRKPGSVGKP-VGVEVRIlDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEaAFKDGWFRTGDLGYLDADGYLFLTG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 379 RRSDLIISGGENIYPAQIEEVLLSHPMVAEAGVVGMTDDKWGQVPAAFVV--KNGEVTEEEIIHFCEEKLAKYKVPKKAC 456
Cdd:cd05926 394 RIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVlrEGASVTEEELRAFCRKHLAAFKVPKKVY 473
|
490 500
....*....|....*....|
gi 446371684 457 FLEELPRNASKKLLRRELRQ 476
Cdd:cd05926 474 FVDELPKTATGKIQRRKVAE 493
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
143-478 |
9.39e-104 |
|
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: 312.73 E-value: 9.39e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 143 TIIYTSGTTGKPKGVILTYGNHWASAVGSSLNLGLRDDDCWLACMPMFHVGGLSLLMKNIMYGmRILLVPKYDADFIHKA 222
Cdd:cd17630 4 TVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLYHVGGLAILVRSLLAG-AELVLLERNQALAEDL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 223 LQTrGVTIISVVSKMLTDLLERLGEETYPSSLRCMLLGGGPAPKPLLETCVDKGIPVYQTYGMTETSSQICTLSADymLT 302
Cdd:cd17630 83 APP-GVTHVSLVPTQLQRLLDSGQGPAALKSLRAVLLGGAPIPPELLERAADRGIPLYTTYGMTETASQVATKRPD--GF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 303 KVGSAGKPLFQCQLRIEKDGvvvpplvegEIVVKGPNVTGGYFNReDATRETIQNGWLHTGDLGYLDEEGFLYVLDRRSD 382
Cdd:cd17630 160 GRGGVGVLLPGRELRIVEDG---------EIWVGGASLAMGYLRG-QLVPEFNEDGWFTTKDLGELHADGRLTVLGRADN 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 383 LIISGGENIYPAQIEEVLLSHPMVAEAGVVGMTDDKWGQVPAAFVVKNGEVTEEEIIHFCEEKLAKYKVPKKACFLEELP 462
Cdd:cd17630 230 MIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRGPADPAELRAWLKDKLARFKLPKRIYPVPELP 309
|
330
....*....|....*.
gi 446371684 463 RNASKKLLRRELRQLV 478
Cdd:cd17630 310 RTGGGKVDRRALRAWL 325
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
25-475 |
6.37e-102 |
|
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: 311.53 E-value: 6.37e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 25 EEKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSREELLWQMDDAEVVCLV 104
Cdd:cd05934 1 GRRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 105 TDQQfdandvpvysfaevmhglkveasiqeefsleeamTIIYTSGTTGKPKGVILTYGNHWASAVGSSLNLGLRDDDCWL 184
Cdd:cd05934 81 VDPA----------------------------------SILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGEDDVYL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 185 ACMPMFHVGGLSL-LMKNIMYGMRILLVPKYDADFIHKALQTRGVTIISVVSKMLTDLL---ERLGEETYPssLRCMllG 260
Cdd:cd05934 127 TVLPLFHINAQAVsVLAALSVGATLVLLPRFSASRFWSDVRRYGATVTNYLGAMLSYLLaqpPSPDDRAHR--LRAA--Y 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 261 GGPAPKPLLETCVDK-GIPVYQTYGMTETSsqICTLSADYMLTKVGSAGKPLFQCQLRI-EKDGVVVPPLVEGEIVVK-- 336
Cdd:cd05934 203 GAPNPPELHEEFEERfGVRLLEGYGMTETI--VGVIGPRDEPRRPGSIGRPAPGYEVRIvDDDGQELPAGEPGELVIRgl 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 337 -GPNVTGGYFNREDATRETIQNGWLHTGDLGYLDEEGFLYVLDRRSDLIISGGENIYPAQIEEVLLSHPMVAEAGVVGMT 415
Cdd:cd05934 281 rGWGFFKGYYNMPEATAEAMRNGWFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVP 360
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446371684 416 DDKWG-QVPAAFVVKNGE-VTEEEIIHFCEEKLAKYKVPKKACFLEELPRNASKKLLRRELR 475
Cdd:cd05934 361 DEVGEdEVKAVVVLRPGEtLDPEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
21-476 |
1.41e-99 |
|
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: 308.41 E-value: 1.41e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 21 IEIEEEKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSREELLWQMDDAEV 100
Cdd:cd12119 19 HEGEVHRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAED 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 101 VCLVTDQQF---------------------------DANDVPVYSFAEVMHGlkvEASIQEEFSLEE--AMTIIYTSGTT 151
Cdd:cd12119 99 RVVFVDRDFlplleaiaprlptvehvvvmtddaampEPAGVGVLAYEELLAA---ESPEYDWPDFDEntAAAICYTSGTT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 152 GKPKGVILTYGNHW--ASAVGSSLNLGLRDDDCWLACMPMFHVGGLSLLMKNIMYGMRILLV-PKYDADFIHKALQTRGV 228
Cdd:cd12119 176 GNPKGVVYSHRSLVlhAMAALLTDGLGLSESDVVLPVVPMFHVNAWGLPYAAAMVGAKLVLPgPYLDPASLAELIEREGV 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 229 TIISVVSKMLTDLLERLGEETY-PSSLRCMLLGGGPAPKPLLETCVDKGIPVYQTYGMTETSSqICT----------LSA 297
Cdd:cd12119 256 TFAAGVPTVWQGLLDHLEANGRdLSSLRRVVIGGSAVPRSLIEAFEERGVRVIHAWGMTETSP-LGTvarppsehsnLSE 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 298 DYMLTKVGSAGKPLFQCQLRIEK-DGVVVP--PLVEGEIVVKGPNVTGGYFNREDATRETIQNGWLHTGDLGYLDEEGFL 374
Cdd:cd12119 335 DEQLALRAKQGRPVPGVELRIVDdDGRELPwdGKAVGELQVRGPWVTKSYYKNDEESEALTEDGWLRTGDVATIDEDGYL 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 375 YVLDRRSDLIISGGENIYPAQIEEVLLSHPMVAEAGVVGMTDDKWGQVPAAFVVK--NGEVTEEEIIHFCEEKLAKYKVP 452
Cdd:cd12119 415 TITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLkeGATVTAEELLEFLADKVAKWWLP 494
|
490 500
....*....|....*....|....
gi 446371684 453 KKACFLEELPRNASKKLLRRELRQ 476
Cdd:cd12119 495 DDVVFVDEIPKTSTGKIDKKALRE 518
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
8-387 |
3.43e-97 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 299.23 E-value: 3.43e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 8 LKQRAFLTPDRTAIEI-EEEKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRL 86
Cdd:pfam00501 1 LERQAARTPDKTALEVgEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 87 SREELLWQMDDAEVVCLVTDQQFDAN------------------DVPVYSFAEVMHGLKVEASIQ----EEFSLEEAMTI 144
Cdd:pfam00501 81 PAEELAYILEDSGAKVLITDDALKLEellealgklevvklvlvlDRDPVLKEEPLPEEAKPADVPppppPPPDPDDLAYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 145 IYTSGTTGKPKGVILTYGNHWASAVGSSL----NLGLRDDDCWLACMPMFHVGGLSL-LMKNIMYGMRILLVPK---YDA 216
Cdd:pfam00501 161 IYTSGTTGKPKGVMLTHRNLVANVLSIKRvrprGFGLGPDDRVLSTLPLFHDFGLSLgLLGPLLAGATVVLPPGfpaLDP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 217 DFIHKALQTRGVTIISVVSKMLTDLLE-RLGEETYPSSLRCMLLGGGPAPKPLLETCVDK-GIPVYQTYGMTETSSQICT 294
Cdd:pfam00501 241 AALLELIERYKVTVLYGVPTLLNMLLEaGAPKRALLSSLRLVLSGGAPLPPELARRFRELfGGALVNGYGLTETTGVVTT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 295 -LSADYMLTKVGSAGKPLFQCQLRI--EKDGVVVPPLVEGEIVVKGPNVTGGYFNREDATRETI-QNGWLHTGDLGYLDE 370
Cdd:pfam00501 321 pLPLDEDLRSLGSVGRPLPGTEVKIvdDETGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFdEDGWYRTGDLGRRDE 400
|
410
....*....|....*..
gi 446371684 371 EGFLYVLDRRSDLIISG 387
Cdd:pfam00501 401 DGYLEIVGRKKDQIKLG 417
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
28-474 |
2.77e-96 |
|
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: 299.54 E-value: 2.77e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 28 VTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSREELLWQMDDAEVVCLVTDQ 107
Cdd:cd05904 33 LTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLAFTTA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 108 QFdANDVPVYSFAEVMHGLKVEASIQEEFSLEEA---------------MTIIYTSGTTGKPKGVILTYGNHWASAVG-- 170
Cdd:cd05904 113 EL-AEKLASLALPVVLLDSAEFDSLSFSDLLFEAdeaeppvvvikqddvAALLYSSGTTGRSKGVMLTHRNLIAMVAQfv 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 171 SSLNLGLRDDDCWLACMPMFHVGGLSLLMKNIM-YGMRILLVPKYDADFIHKALQTRGVTIISVVSKMLTDLLERLGEET 249
Cdd:cd05904 192 AGEGSNSDSEDVFLCVLPMFHIYGLSSFALGLLrLGATVVVMPRFDLEELLAAIERYKVTHLPVVPPIVLALVKSPIVDK 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 250 YP-SSLRCMLLGGGPAPKPLLETCVDK--GIPVYQTYGMTEtSSQICT--LSADYMLTKVGSAGKPLFQCQLRI--EKDG 322
Cdd:cd05904 272 YDlSSLRQIMSGAAPLGKELIEAFRAKfpNVDLGQGYGMTE-STGVVAmcFAPEKDRAKYGSVGRLVPNVEAKIvdPETG 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 323 VVVPPLVEGEIVVKGPNVTGGYFNREDATRETI-QNGWLHTGDLGYLDEEGFLYVLDRRSDLIISGGENIYPAQIEEVLL 401
Cdd:cd05904 351 ESLPPNQTGELWIRGPSIMKGYLNNPEATAATIdKEGWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLL 430
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446371684 402 SHPMVAEAGVVGMTDDKWGQVPAAFVVKN--GEVTEEEIIHFCEEKLAKYKVPKKACFLEELPRNASKKLLRREL 474
Cdd:cd05904 431 SHPEILDAAVIPYPDEEAGEVPMAFVVRKpgSSLTEDEIMDFVAKQVAPYKKVRKVAFVDAIPKSPSGKILRKEL 505
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
15-476 |
1.65e-95 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 298.38 E-value: 1.65e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 15 TPDRTAIEIEEEKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSREELLWQ 94
Cdd:PRK08316 24 YPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 95 MDDAEVVCLVTD----------------QQFDANDVPVYSFAEV-MHGLKVEASIQEEFSLEEAMT------IIYTSGTT 151
Cdd:PRK08316 104 LDHSGARAFLVDpalaptaeaalallpvDTLILSLVLGGREAPGgWLDFADWAEAGSVAEPDVELAdddlaqILYTSGTE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 152 GKPKGVILTYGNHWASAVGSSLNLGLRDDDCWLACMPMFHVGGLS-LLMKNIMYGMRILLVPKYDADFIHKALQTRGVTI 230
Cdd:PRK08316 184 SLPKGAMLTHRALIAEYVSCIVAGDMSADDIPLHALPLYHCAQLDvFLGPYLYVGATNVILDAPDPELILRTIEAERITS 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 231 --------ISvvskmltdLLERLGEETYP-SSLRCMLLGGGPAPKPLLETCVDK--GIPVYQTYGMTETSSQICTLSADY 299
Cdd:PRK08316 264 ffapptvwIS--------LLRHPDFDTRDlSSLRKGYYGASIMPVEVLKELRERlpGLRFYNCYGQTEIAPLATVLGPEE 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 300 MLTKVGSAGKPLFQCQLRIE-KDGVVVPPLVEGEIVVKGPNVTGGYFNREDATRETIQNGWLHTGDLGYLDEEGFLYVLD 378
Cdd:PRK08316 336 HLRRPGSAGRPVLNVETRVVdDDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEAFRGGWFHSGDLGVMDEEGYITVVD 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 379 RRSDLIISGGENIYPAQIEEVLLSHPMVAEAGVVGMTDDKWGQ-VPAAFVVKNG-EVTEEEIIHFCEEKLAKYKVPKKAC 456
Cdd:PRK08316 416 RKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEaVTAVVVPKAGaTVTEDELIAHCRARLAGFKVPKRVI 495
|
490 500
....*....|....*....|
gi 446371684 457 FLEELPRNASKKLLRRELRQ 476
Cdd:PRK08316 496 FVDELPRNPSGKILKRELRE 515
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
15-475 |
8.33e-93 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 290.63 E-value: 8.33e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 15 TPDRTAIEIEEEKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSREELLWQ 94
Cdd:PRK06145 15 TPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 95 MDDAEVVCLVTDQQFDAN----------DVPVYSFAEVMHGLKVEASIQEEFSLEEAMTIIYTSGTTGKPKGVILTYGN- 163
Cdd:PRK06145 95 LGDAGAKLLLVDEEFDAIvaletpkiviDAAAQADSRRLAQGGLEIPPQAAVAPTDLVRLMYTSGTTDRPKGVMHSYGNl 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 164 HWASAvGSSLNLGLRDDDCWLACMPMFHVGGLSLLMKNIMY-GMRILLVPKYDADFIHKALQTRGVTIISVVSKMLTDLL 242
Cdd:PRK06145 175 HWKSI-DHVIALGLTASERLLVVGPLYHVGAFDLPGIAVLWvGGTLRIHREFDPEAVLAAIERHRLTCAWMAPVMLSRVL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 243 ERLGEETYP-SSLRCMLLGGGPAPKPLLE--TCVDKGIPVYQTYGMTETSSQICTLSADYMLTKVGSAGKPLFQCQLRI- 318
Cdd:PRK06145 254 TVPDRDRFDlDSLAWCIGGGEKTPESRIRdfTRVFTRARYIDAYGLTETCSGDTLMEAGREIEKIGSTGRALAHVEIRIa 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 319 EKDGVVVPPLVEGEIVVKGPNVTGGYFNREDATRETIQNGWLHTGDLGYLDEEGFLYVLDRRSDLIISGGENIYPAQIEE 398
Cdd:PRK06145 334 DGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGDWFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVER 413
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446371684 399 VLLSHPMVAEAGVVGMTDDKWGQVPAAFVVKN--GEVTEEEIIHFCEEKLAKYKVPKKACFLEELPRNASKKLLRRELR 475
Cdd:PRK06145 414 VIYELPEVAEAAVIGVHDDRWGERITAVVVLNpgATLTLEALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVLR 492
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
6-476 |
9.79e-93 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 291.68 E-value: 9.79e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 6 NWLKQRAFLTPDRTAIEIEEEKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTR 85
Cdd:PRK07786 21 NQLARHALMQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 86 LSREELLWQMDDAEVVCLVTDQQFDA------NDVPVYSFAEVMHGLKVEASIQEEFSLEEA--------------MTII 145
Cdd:PRK07786 101 LTPPEIAFLVSDCGAHVVVTEAALAPvatavrDIVPLLSTVVVAGGSSDDSVLGYEDLLAEAgpahapvdipndspALIM 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 146 YTSGTTGKPKGVILTYGNHWASAVGSSLNLGL-RDDDCWLACMPMFHVGGLSLLMKNIMYGMRILLVP--KYDADFIHKA 222
Cdd:PRK07786 181 YTSGTTGRPKGAVLTHANLTGQAMTCLRTNGAdINSDVGFVGVPLFHIAGIGSMLPGLLLGAPTVIYPlgAFDPGQLLDV 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 223 LQTRGVTIISVVSKMLTDLLERLGEETYPSSLRCMLLGGGPAPKPLLETCVDK--GIPVYQTYGMTETSSQICTLSADYM 300
Cdd:PRK07786 261 LEAEKVTGIFLVPAQWQAVCAEQQARPRDLALRVLSWGAAPASDTLLRQMAATfpEAQILAAFGQTEMSPVTCMLLGEDA 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 301 LTKVGSAGKPLFQCQLRIEKDGVV-VPPLVEGEIVVKGPNVTGGYFNREDATRETIQNGWLHTGDLGYLDEEGFLYVLDR 379
Cdd:PRK07786 341 IRKLGSVGKVIPTVAARVVDENMNdVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFAGGWFHSGDLVRQDEEGYVWVVDR 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 380 RSDLIISGGENIYPAQIEEVLLSHPMVAEAGVVGMTDDKWGQVPAAFVVKNG---EVTEEEIIHFCEEKLAKYKVPKKAC 456
Cdd:PRK07786 421 KKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRNddaALTLEDLAEFLTDRLARYKHPKALE 500
|
490 500
....*....|....*....|
gi 446371684 457 FLEELPRNASKKLLRRELRQ 476
Cdd:PRK07786 501 IVDALPRNPAGKVLKTELRE 520
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
6-480 |
2.43e-92 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 291.25 E-value: 2.43e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 6 NWLKQRAFLTPDRTAIEIEEE-----KVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAV 80
Cdd:COG0365 13 NCLDRHAEGRGDKVALIWEGEdgeerTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 81 LLNTRLSREELLWQMDDAEVVCLVTDQQFDANDVPVYSFAEVMHGLK---------------VEASIQEEFSLEEAMT-- 143
Cdd:COG0365 93 PVFPGFGAEALADRIEDAEAKVLITADGGLRGGKVIDLKEKVDEALEelpslehvivvgrtgADVPMEGDLDWDELLAaa 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 144 ----------------IIYTSGTTGKPKGVILTYGNHWASAVGSSLN-LGLRDDDCWLACMPMFHVGGLSllmkNIMY-- 204
Cdd:COG0365 173 saefepeptdaddplfILYTSGTTGKPKGVVHTHGGYLVHAATTAKYvLDLKPGDVFWCTADIGWATGHS----YIVYgp 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 205 ---GMRILL---VPKY-DADFIHKALQTRGVTIISVVSKMLtDLLERLGEE---TYP-SSLRCMLLGGGPAPKPLLETCV 273
Cdd:COG0365 249 llnGATVVLyegRPDFpDPGRLWELIEKYGVTVFFTAPTAI-RALMKAGDEplkKYDlSSLRLLGSAGEPLNPEVWEWWY 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 274 DK-GIPVYQTYGMTETSSQICTlSADYMLTKVGSAGKPLFQCQLRI-EKDGVVVPPLVEGEIVVKG--PNVTGGYFNRED 349
Cdd:COG0365 328 EAvGVPIVDGWGQTETGGIFIS-NLPGLPVKPGSMGKPVPGYDVAVvDEDGNPVPPGEEGELVIKGpwPGMFRGYWNDPE 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 350 ATRETIQN---GWLHTGDLGYLDEEGFLYVLDRRSDLIISGGENIYPAQIEEVLLSHPMVAEAGVVGMTDDKWGQVPAAF 426
Cdd:COG0365 407 RYRETYFGrfpGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVGVPDEIRGQVVKAF 486
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 446371684 427 VV-KNG----EVTEEEIIHFCEEKLAKYKVPKKACFLEELPRNASKKLLRRELRQLVEE 480
Cdd:COG0365 487 VVlKPGvepsDELAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLRKIAEG 545
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
28-474 |
5.36e-91 |
|
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: 283.60 E-value: 5.36e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 28 VTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSREELLWQMDDAEVVCLVTDQ 107
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 108 qfdandvpvysfaevmhglkveasiqeefSLEEAMTIIYTSGTTGKPKGVILTYGNHWASAVGSSLNLGLRDDDCWLACM 187
Cdd:cd05935 82 -----------------------------ELDDLALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPSDVILACL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 188 PMFHVGGLSLLMKNIMY-GMRILLVPKYDADFIHKALQTRGVTIISVVSKMLTDLLERLGEETYP-SSLRCMLLGGGPAP 265
Cdd:cd05935 133 PLFHVTGFVGSLNTAVYvGGTYVLMARWDRETALELIEKYKVTFWTNIPTMLVDLLATPEFKTRDlSSLKVLTGGGAPMP 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 266 KPLLETCVDK-GIPVYQTYGMTETSSQicTLSADYMLTKVGSAGKPLFQCQLRI--EKDGVVVPPLVEGEIVVKGPNVTG 342
Cdd:cd05935 213 PAVAEKLLKLtGLRFVEGYGLTETMSQ--THTNPPLRPKLQCLGIP*FGVDARVidIETGRELPPNEVGEIVVRGPQIFK 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 343 GYFNREDATRE--TIQNG--WLHTGDLGYLDEEGFLYVLDRRSDLIISGGENIYPAQIEEVLLSHPMVAEAGVVGMTDDK 418
Cdd:cd05935 291 GYWNRPEETEEsfIEIKGrrFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDER 370
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 419 WGQVPAAFVVKN----GEVTEEEIIHFCEEKLAKYKVPKKACFLEELPRNASKKLLRREL 474
Cdd:cd05935 371 VGEEVKAFIVLRpeyrGKVTEEDIIEWAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
27-470 |
2.19e-86 |
|
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: 273.32 E-value: 2.19e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 27 KVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSREELLWQMDDAEVVCLVTD 106
Cdd:cd05911 10 ELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 107 QQFDAN----------DVPVYSFA-------EVMHGLKVEASIQEEF---SLEEA----MTIIYTSGTTGKPKGVILTYG 162
Cdd:cd05911 90 PDGLEKvkeaakelgpKDKIIVLDdkpdgvlSIEDLLSPTLGEEDEDlppPLKDGkddtAAILYSSGTTGLPKGVCLSHR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 163 N--HWASAVGSSLNLGLRDDDCWLACMPMFHVGGLSLLMKNIMYGMRILLVPKYDADFIHKALQTRGVTIISVVSKMLTD 240
Cdd:cd05911 170 NliANLSQVQTFLYGNDGSNDVILGFLPLYHIYGLFTTLASLLNGATVIIMPKFDSELFLDLIEKYKITFLYLVPPIAAA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 241 LLER-LGEETYPSSLRCMLLGGGPAPKPLLETcVDKGIP---VYQTYGMTETSSQICTLSADYmlTKVGSAGKPLFQCQL 316
Cdd:cd05911 250 LAKSpLLDKYDLSSLRVILSGGAPLSKELQEL-LAKRFPnatIKQGYGMTETGGILTVNPDGD--DKPGSVGRLLPNVEA 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 317 RIEKD--GVVVPPLVEGEIVVKGPNVTGGYFNREDATRETI-QNGWLHTGDLGYLDEEGFLYVLDRRSDLIISGGENIYP 393
Cdd:cd05911 327 KIVDDdgKDSLGPNEPGEICVRGPQVMKGYYNNPEATKETFdEDGWLHTGDIGYFDEDGYLYIVDRKKELIKYKGFQVAP 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 394 AQIEEVLLSHPMVAEAGVVGMTDDKWGQVPAAFVVK--NGEVTEEEIIHFCEEKLAKYK------VpkkacFLEELPRNA 465
Cdd:cd05911 407 AELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRkpGEKLTEKEVKDYVAKKVASYKqlrggvV-----FVDEIPKSA 481
|
....*
gi 446371684 466 SKKLL 470
Cdd:cd05911 482 SGKIL 486
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
5-475 |
2.48e-86 |
|
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: 273.41 E-value: 2.48e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 5 PNWLKQR-AFLTPDRTAIEIEEEKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLN 83
Cdd:cd12118 6 PLSFLERaAAVYPDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 84 TRLSREELLWQMDDAEVVCLVTDQQFDANDVpvysfaevMHGLKVEASIQEEFSLEEAMTIIYTSGTTGKPKGVILTYGN 163
Cdd:cd12118 86 TRLDAEEIAFILRHSEAKVLFVDREFEYEDL--------LAEGDPDFEWIPPADEWDPIALNYTSGTTGRPKGVVYHHRG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 164 HWASAVGSSLNLGLRDDDCWLACMPMFHVGGLSLLMKNIMYGMRILLVPKYDADFIHKALQTRGVTIISVVSKMLTDLLE 243
Cdd:cd12118 158 AYLNALANILEWEMKQHPVYLWTLPMFHCNGWCFPWTVAAVGGTNVCLRKVDAKAIYDLIEKHKVTHFCGAPTVLNMLAN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 244 RLGEETYPSSLRC-MLLGGGPAPKPLLETCVDKGIPVYQTYGMTETS--SQICTLSADY----------MLTKVGSAGKP 310
Cdd:cd12118 238 APPSDARPLPHRVhVMTAGAPPPAAVLAKMEELGFDVTHVYGLTETYgpATVCAWKPEWdelpteerarLKARQGVRYVG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 311 LF-------QCQLRIEKDGVVVpplveGEIVVKGPNVTGGYFNREDATRETIQNGWLHTGDLGYLDEEGFLYVLDRRSDL 383
Cdd:cd12118 318 LEevdvldpETMKPVPRDGKTI-----GEIVFRGNIVMKGYLKNPEATAEAFRGGWFHSGDLAVIHPDGYIEIKDRSKDI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 384 IISGGENIYPAQIEEVLLSHPMVAEAGVVGMTDDKWGQVPAAFV-VKNG-EVTEEEIIHFCEEKLAKYKVPKKACFlEEL 461
Cdd:cd12118 393 IISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVeLKEGaKVTEEEIIAFCREHLAGFMVPKTVVF-GEL 471
|
490
....*....|....
gi 446371684 462 PRNASKKLLRRELR 475
Cdd:cd12118 472 PKTSTGKIQKFVLR 485
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
12-477 |
1.08e-85 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 271.68 E-value: 1.08e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 12 AFLTPDRTAIE--IEEEKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSRE 89
Cdd:PRK09088 5 ARLQPQRLAAVdlALGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSAS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 90 ELLWQMDDAEVVCLVTDQQFDANDVPVYSFAEVMHGLKVEASIQEEFSLEEAMTII-YTSGTTGKPKGVILTYGNHWASA 168
Cdd:PRK09088 85 ELDALLQDAEPRLLLGDDAVAAGRTDVEDLAAFIASADALEPADTPSIPPERVSLIlFTSGTSGQPKGVMLSERNLQQTA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 169 VGSSLNLGLRDDDCWLACMPMFHVGGLSLLMKNI-MYGMRILLVPKYDADFIHKAL--QTRGVTIISVVSKMLTDLLERL 245
Cdd:PRK09088 165 HNFGVLGRVDAHSSFLCDAPMFHIIGLITSVRPVlAVGGSILVSNGFEPKRTLGRLgdPALGITHYFCVPQMAQAFRAQP 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 246 GEEtyPSSLR---CMLLGGGPAPKPLLETCVDKGIPVYQTYGMTETSSQI-CTLSADYMLTKVGSAGKPLFQCQLRI-EK 320
Cdd:PRK09088 245 GFD--AAALRhltALFTGGAPHAAEDILGWLDDGIPMVDGFGMSEAGTVFgMSVDCDVIRAKAGAAGIPTPTVQTRVvDD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 321 DGVVVPPLVEGEIVVKGPNVTGGYFNREDATRETI-QNGWLHTGDLGYLDEEGFLYVLDRRSDLIISGGENIYPAQIEEV 399
Cdd:PRK09088 323 QGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFtGDGWFRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAV 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 400 LLSHPMVAEAGVVGMTDDKWGQVPAAFVV-KNGEVTE-EEIIHFCEEKLAKYKVPKKACFLEELPRNASKKLLRRELRQL 477
Cdd:PRK09088 403 LADHPGIRECAVVGMADAQWGEVGYLAIVpADGAPLDlERIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARLRDA 482
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
17-476 |
2.89e-83 |
|
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: 264.15 E-value: 2.89e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 17 DRTAIEIEEEKVTFLQLHEKVVSVCEHLTHVG-VKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSREELLWQM 95
Cdd:cd05941 1 DRIAIVDDGDSITYADLVARAARLANRLLALGkDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 96 DDAEVVCLvtdqqfdandvpvysfaevmhglkveasiqeefsLEEAMtIIYTSGTTGKPKGVILTYGNHWASAVGSSLNL 175
Cdd:cd05941 81 TDSEPSLV----------------------------------LDPAL-ILYTSGTTGRPKGVVLTHANLAANVRALVDAW 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 176 GLRDDDCWLACMPMFHVGGLSL-LMKNIMYGMRILLVPKYDADFIHKALQTRGVTIISVVSKMLTDLLE---------RL 245
Cdd:cd05941 126 RWTEDDVLLHVLPLHHVHGLVNaLLCPLFAGASVEFLPKFDPKEVAISRLMPSITVFMGVPTIYTRLLQyyeahftdpQF 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 246 GEETYPSSLRCMLLGGGPAPKPLLETCVDK-GIPVYQTYGMTETSSQI-CTLSADymlTKVGSAGKPLFQCQLRI--EKD 321
Cdd:cd05941 206 ARAAAAERLRLMVSGSAALPVPTLEEWEAItGHTLLERYGMTEIGMALsNPLDGE---RRPGTVGMPLPGVQARIvdEET 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 322 GVVVPPLVEGEIVVKGPNVTGGYFNREDATRETIQ-NGWLHTGDLGYLDEEGFLYVLDRRSDLII-SGGENIYPAQIEEV 399
Cdd:cd05941 283 GEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTdDGWFKTGDLGVVDEDGYYWILGRSSVDIIkSGGYKVSALEIERV 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 400 LLSHPMVAEAGVVGMTDDKWGQVPAAFVVKNGEV---TEEEIIHFCEEKLAKYKVPKKACFLEELPRNASKKLLRRELRQ 476
Cdd:cd05941 363 LLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGAaalSLEELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
144-466 |
1.28e-82 |
|
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: 258.74 E-value: 1.28e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 144 IIYTSGTTGKPKGVILTYGNHWASAVGSSLNLGLRDDDCWLACMPMFHVGGLSLLMKNIMYGMRILLVPKYDADFIHKAL 223
Cdd:cd17637 5 IIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPLFHIAGLNLALATFHAGGANVVMEKFDPAEALELI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 224 QTRGVTIISVVSKMLTDLLERLGEETY-PSSLRcmLLGGGPAP---KPLLETCvdkGIPVYQTYGMTETSSQICTLSADy 299
Cdd:cd17637 85 EEEKVTLMGSFPPILSNLLDAAEKSGVdLSSLR--HVLGLDAPetiQRFEETT---GATFWSLYGQTETSGLVTLSPYR- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 300 mlTKVGSAGKPLFQCQLRI--EKDGVVvPPLVEGEIVVKGPNVTGGYFNREDATRETIQNGWLHTGDLGYLDEEGFLYVL 377
Cdd:cd17637 159 --ERPGSAGRPGPLVRVRIvdDNDRPV-PAGETGEIVVRGPLVFQGYWNLPELTAYTFRNGWHHTGDLGRFDEDGYLWYA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 378 DRRS--DLIISGGENIYPAQIEEVLLSHPMVAEAGVVGMTDDKWGQ-VPAAFVVKNGE-VTEEEIIHFCEEKLAKYKVPK 453
Cdd:cd17637 236 GRKPekELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEgIKAVCVLKPGAtLTADELIEFVGSRIARYKKPR 315
|
330
....*....|...
gi 446371684 454 KACFLEELPRNAS 466
Cdd:cd17637 316 YVVFVEALPKTAD 328
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
28-476 |
5.02e-82 |
|
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: 260.78 E-value: 5.02e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 28 VTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSREELLWQMDDAEVVCLVTDQ 107
Cdd:cd05903 2 LTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVPE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 108 QFDANDvpvysFAEvMHGlkveasiqeefslEEAMtIIYTSGTTGKPKGVILTYGNHWASAVGSSLNLGLRDDDCWLACM 187
Cdd:cd05903 82 RFRQFD-----PAA-MPD-------------AVAL-LLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPGDVFLVAS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 188 PMFHVGG-LSLLMKNIMYGMRILLVPKYDADFIHKALQTRGVTIISVVSKMLTDLL---ERLGEEtyPSSLRCMLLGGGP 263
Cdd:cd05903 142 PMAHQTGfVYGFTLPLLLGAPVVLQDIWDPDKALALMREHGVTFMMGATPFLTDLLnavEEAGEP--LSRLRTFVCGGAT 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 264 APKPLLETCVDKGIP-VYQTYGMTETSSQICTLSADYMLTKVGSAGKPLFQCQLRI-EKDGVVVPPLVEGEIVVKGPNVT 341
Cdd:cd05903 220 VPRSLARRAAELLGAkVCSAYGSTECPGAVTSITPAPEDRRLYTDGRPLPGVEIKVvDDTGATLAPGVEGELLSRGPSVF 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 342 GGYFNREDATRETIQNGWLHTGDLGYLDEEGFLYVLDRRSDLIISGGENIYPAQIEEVLLSHPMVAEAGVVGMTDDKWGQ 421
Cdd:cd05903 300 LGYLDRPDLTADAAPEGWFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGE 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 446371684 422 VPAAFVV-KNG-EVTEEEII-HFCEEKLAKYKVPKKACFLEELPRNASKKLLRRELRQ 476
Cdd:cd05903 380 RACAVVVtKSGaLLTFDELVaYLDRQGVAKQYWPERLVHVDDLPRTPSGKVQKFRLRE 437
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
16-475 |
2.66e-81 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 261.46 E-value: 2.66e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 16 PDRTAIEIEEEKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSREELLWQM 95
Cdd:PRK06188 26 PDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHPLGSLDDHAYVL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 96 DDAEVVCLVTD-QQFD------ANDVP----VYSFAEVMHG--LKVEASIQEEFSLE------EAMTIIYTSGTTGKPKG 156
Cdd:PRK06188 106 EDAGISTLIVDpAPFVeralalLARVPslkhVLTLGPVPDGvdLLAAAAKFGPAPLVaaalppDIAGLAYTGGTTGKPKG 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 157 VILTYGNHWASAVGSSLNLGLRDDDCWLACMPMFHVGGLsLLMKNIMYGMRILLVPKYDADFIHKALQTRGVTIISVVSK 236
Cdd:PRK06188 186 VMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLSHAGGA-FFLPTLLRGGTVIVLAKFDPAEVLRAIEEQRITATFLVPT 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 237 MLTDLLERLGEETYP-SSLRCMLLGGGP-APKPLLETcVDKGIPVY-QTYGMTETSSQICTLS-ADYMLTKV---GSAGK 309
Cdd:PRK06188 265 MIYALLDHPDLRTRDlSSLETVYYGASPmSPVRLAEA-IERFGPIFaQYYGQTEAPMVITYLRkRDHDPDDPkrlTSCGR 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 310 PLFQCQLRI-EKDGVVVPPLVEGEIVVKGPNVTGGYFNREDATRETIQNGWLHTGDLGYLDEEGFLYVLDRRSDLIISGG 388
Cdd:PRK06188 344 PTPGLRVALlDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAFRDGWLHTGDVAREDEDGFYYIVDRKKDMIVTGG 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 389 ENIYPAQIEEVLLSHPMVAEAGVVGMTDDKWGQVPAAFVV-KNGE-VTEEEIIHFCEEKLAKYKVPKKACFLEELPRNAS 466
Cdd:PRK06188 424 FNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVlRPGAaVDAAELQAHVKERKGSVHAPKQVDFVDSLPLTAL 503
|
....*....
gi 446371684 467 KKLLRRELR 475
Cdd:PRK06188 504 GKPDKKALR 512
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
12-475 |
2.84e-81 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 262.17 E-value: 2.84e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 12 AFLTPDRTAIEIEEEKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSREEL 91
Cdd:PRK07788 59 ARRAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 92 LWQMDDAEVVCLVTDQQFDA------NDVPVYSfAEVMHGLKVEASIQEEFSLEEAMT----------------IIYTSG 149
Cdd:PRK07788 139 AEVAAREGVKALVYDDEFTDllsalpPDLGRLR-AWGGNPDDDEPSGSTDETLDDLIAgsstaplpkppkpggiVILTSG 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 150 TTGKPKGVILTYGNHWASaVGSSLN-LGLRDDDCWLACMPMFHVGGLSLLMKNIMYGMRILLVPKYDADFIHKALQTRGV 228
Cdd:PRK07788 218 TTGTPKGAPRPEPSPLAP-LAGLLSrVPFRAGETTLLPAPMFHATGWAHLTLAMALGSTVVLRRRFDPEATLEDIAKHKA 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 229 TIISVVSKMLTDLLErLGEETYP----SSLRCMLLGGGPAPKPLLETCVDKGIPV-YQTYGMTETSsqICTLSADYMLTK 303
Cdd:PRK07788 297 TALVVVPVMLSRILD-LGPEVLAkydtSSLKIIFVSGSALSPELATRALEAFGPVlYNLYGSTEVA--FATIATPEDLAE 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 304 V-GSAGKPLFQCQLRI-EKDGVVVPPLVEGEIVVKGPNVTGGYFNreDATRETIqNGWLHTGDLGYLDEEGFLYVLDRRS 381
Cdd:PRK07788 374 ApGTVGRPPKGVTVKIlDENGNEVPRGVVGRIFVGNGFPFEGYTD--GRDKQII-DGLLSSGDVGYFDEDGLLFVDGRDD 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 382 DLIISGGENIYPAQIEEVLLSHPMVAEAGVVGMTDDKWGQVPAAFVVKN--GEVTEEEIIHFCEEKLAKYKVPKKACFLE 459
Cdd:PRK07788 451 DMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKApgAALDEDAIKDYVRDNLARYKVPRDVVFLD 530
|
490
....*....|....*.
gi 446371684 460 ELPRNASKKLLRRELR 475
Cdd:PRK07788 531 ELPRNPTGKVLKRELR 546
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
24-475 |
5.43e-81 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 259.84 E-value: 5.43e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 24 EEEKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSREELLWQMDDAEVVCL 103
Cdd:PRK08276 8 SGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 104 VTDQQFDANDVPVYsfAEVMHGLKVEASIQEEF----SLEEAM---------------TIIYTSGTTGKPKGVI--LTyG 162
Cdd:PRK08276 88 IVSAALADTAAELA--AELPAGVPLLLVVAGPVpgfrSYEEALaaqpdtpiadetagaDMLYSSGTTGRPKGIKrpLP-G 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 163 NHWASAVGSSLNLGLRD----DDC-WLACMPMFHVGGLSLLMKNIMYGMRILLVPKYDADFIHKALQTRGVTIISVVSKM 237
Cdd:PRK08276 165 LDPDEAPGMMLALLGFGmyggPDSvYLSPAPLYHTAPLRFGMSALALGGTVVVMEKFDAEEALALIERYRVTHSQLVPTM 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 238 LTDLLeRLGEET---YP-SSLRCMLLGGGPAPKPLLETCVD-KGIPVYQTYGMTETSSqICTLSADYMLTKVGSAGKPLf 312
Cdd:PRK08276 245 FVRML-KLPEEVrarYDvSSLRVAIHAAAPCPVEVKRAMIDwWGPIIHEYYASSEGGG-VTVITSEDWLAHPGSVGKAV- 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 313 QCQLRI-EKDGVVVPPLVEGEIVVKGPNVTGGYFNREDATRE-TIQNGWLHTGDLGYLDEEGFLYVLDRRSDLIISGGEN 390
Cdd:PRK08276 322 LGEVRIlDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAaRNPHGWVTVGDVGYLDEDGYLYLTDRKSDMIISGGVN 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 391 IYPAQIEEVLLSHPMVAEAGVVGMTDDKWGQVPAAFV-----VKNGEVTEEEIIHFCEEKLAKYKVPKKACFLEELPRNA 465
Cdd:PRK08276 402 IYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKAVVqpadgADAGDALAAELIAWLRGRLAHYKCPRSIDFEDELPRTP 481
|
490
....*....|
gi 446371684 466 SKKLLRRELR 475
Cdd:PRK08276 482 TGKLYKRRLR 491
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
2-481 |
5.74e-81 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 261.86 E-value: 5.74e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 2 ETMPNWLKQRAFLTPDRTAIEIEEEKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVL 81
Cdd:PRK05605 32 TTLVDLYDNAVARFGDRPALDFFGATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 82 LNTRLSREELLWQMDD--AEVVC-----------LVTDQQFDA------------------------------------- 111
Cdd:PRK05605 112 HNPLYTAHELEHPFEDhgARVAIvwdkvaptverLRRTTPLETivsvnmiaampllqrlalrlpipalrkaraaltgpap 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 112 NDVPVYSFAEVMHGLKVEASIQEEFSLEEAMTIIYTSGTTGKPKGVILTYGNHWASAV-GSSLNLGLRDDD-CWLACMPM 189
Cdd:PRK05605 192 GTVPWETLVDAAIGGDGSDVSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFANAAqGKAWVPGLGDGPeRVLAALPM 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 190 FHVGGLSLLMKNIMY-GMRILLVPKYDADFIHKALQTRGVTIISVVSKMLTDLLERLGEETYP-SSLRCMLLGGGPAPKP 267
Cdd:PRK05605 272 FHAYGLTLCLTLAVSiGGELVLLPAPDIDLILDAMKKHPPTWLPGVPPLYEKIAEAAEERGVDlSGVRNAFSGAMALPVS 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 268 LLET--CVDKGIPVyQTYGMTETSSQIC--TLSADymlTKVGSAGKPLFQCQLRI---EKDGVVVPPLVEGEIVVKGPNV 340
Cdd:PRK05605 352 TVELweKLTGGLLV-EGYGLTETSPIIVgnPMSDD---RRPGYVGVPFPDTEVRIvdpEDPDETMPDGEEGELLVRGPQV 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 341 TGGYFNREDATRETIQNGWLHTGDLGYLDEEGFLYVLDRRSDLIISGGENIYPAQIEEVLLSHPMVAEAGVVGM-TDDKW 419
Cdd:PRK05605 428 FKGYWNRPEETAKSFLDGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLpREDGS 507
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446371684 420 GQVPAAFVVKNGEVTEEEIIH-FCEEKLAKYKVPKKACFLEELPRNASKKLLRRELRQLVEEM 481
Cdd:PRK05605 508 EEVVAAVVLEPGAALDPEGLRaYCREHLTRYKVPRRFYHVDELPRDQLGKVRRREVREELLEK 570
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
2-480 |
2.40e-80 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 260.80 E-value: 2.40e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 2 ETMPNWLKQRAFLTPDRTAIEI----EEEKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGA 77
Cdd:COG1022 11 DTLPDLLRRRAARFPDRVALREkedgIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 78 VAVLLNTRLSREELLWQMDDAEVVCLV--TDQQFD-----------------------ANDVPVYSFAEVmhgLKVEASI 132
Cdd:COG1022 91 VTVPIYPTSSAEEVAYILNDSGAKVLFveDQEQLDkllevrdelpslrhivvldprglRDDPRLLSLDEL---LALGREV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 133 QEEFSLEEAM---------TIIYTSGTTGKPKGVILTYGNHWASAVGSSLNLGLRDDDCWLACMPMFHVGGLSLLMKNIM 203
Cdd:COG1022 168 ADPAELEARRaavkpddlaTIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFLPLAHVFERTVSYYALA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 204 YGMRILLVPkyDADFIHKALQTRGVTIISVV----SKMLTDLLERLGEET------------------------------ 249
Cdd:COG1022 248 AGATVAFAE--SPDTLAEDLREVKPTFMLAVprvwEKVYAGIQAKAEEAGglkrklfrwalavgrryararlagkspsll 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 250 ----YP---------------SSLRCMLLGGGPAPKPLLETCVDKGIPVYQTYGMTETSSQICTLSADYMltKVGSAGKP 310
Cdd:COG1022 326 lrlkHAladklvfsklrealgGRLRFAVSGGAALGPELARFFRALGIPVLEGYGLTETSPVITVNRPGDN--RIGTVGPP 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 311 LFQCQLRIEKDGvvvpplvegEIVVKGPNVTGGYFNREDATRETI-QNGWLHTGDLGYLDEEGFLYVLDRRSDLII-SGG 388
Cdd:COG1022 404 LPGVEVKIAEDG---------EILVRGPNVMKGYYKNPEATAEAFdADGWLHTGDIGELDEDGFLRITGRKKDLIVtSGG 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 389 ENIYPAQIEEVLLSHPMVAEAGVVGmtDDKwgQVPAAFVVKNgevtEEEIIHFCEEKLAKYKVPkkacflEELprnASKK 468
Cdd:COG1022 475 KNVAPQPIENALKASPLIEQAVVVG--DGR--PFLAALIVPD----FEALGEWAEENGLPYTSY------AEL---AQDP 537
|
570
....*....|..
gi 446371684 469 LLRRELRQLVEE 480
Cdd:COG1022 538 EVRALIQEEVDR 549
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
6-480 |
5.79e-80 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 258.05 E-value: 5.79e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 6 NWLKQRAFLTPDRTAIEIEEEKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTR 85
Cdd:PRK07470 11 HFLRQAARRFPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 86 LSREE------------LLWQMDDAEVVCLVTDQQFDANDVPVYSFAEVmhGLKVEASIQEEFSLEEAMTII-------- 145
Cdd:PRK07470 91 QTPDEvaylaeasgaraMICHADFPEHAAAVRAASPDLTHVVAIGGARA--GLDYEALVARHLGARVANAAVdhddpcwf 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 146 -YTSGTTGKPKGVILTYG-------NHWASavgssLNLGLRDDDCWLACMPMFHVGGLSLLMkNIMYGMRILLVP--KYD 215
Cdd:PRK07470 169 fFTSGTTGRPKAAVLTHGqmafvitNHLAD-----LMPGTTEQDASLVVAPLSHGAGIHQLC-QVARGAATVLLPseRFD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 216 ADFIHKALQTRGVTIISVVSKMLTDLLERLGEETYP-SSLRCMLLGGGPAPKPLLETCVDKGIPVY-QTYGMTETSSQIC 293
Cdd:PRK07470 243 PAEVWALVERHRVTNLFTVPTILKMLVEHPAVDRYDhSSLRYVIYAGAPMYRADQKRALAKLGKVLvQYFGLGEVTGNIT 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 294 TLSA------DYMLTKVGSAGKPLFQCQLRIEKD-GVVVPPLVEGEIVVKGPNVTGGYFNREDATRETIQNGWLHTGDLG 366
Cdd:PRK07470 323 VLPPalhdaeDGPDARIGTCGFERTGMEVQIQDDeGRELPPGETGEICVIGPAVFAGYYNNPEANAKAFRDGWFRTGDLG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 367 YLDEEGFLYVLDRRSDLIISGGENIYPAQIEEVLLSHPMVAEAGVVGMTDDKWGQVPAAFVV--KNGEVTEEEIIHFCEE 444
Cdd:PRK07470 403 HLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVarDGAPVDEAELLAWLDG 482
|
490 500 510
....*....|....*....|....*....|....*.
gi 446371684 445 KLAKYKVPKKACFLEELPRNASKKLLRRELRQLVEE 480
Cdd:PRK07470 483 KVARYKLPKRFFFWDALPKSGYGKITKKMVREELEE 518
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
16-474 |
7.68e-80 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 258.35 E-value: 7.68e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 16 PDRTAIEIEEEKVTFLQLHEKVVSVCEHLTHV-GVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSREELLWQ 94
Cdd:PRK08314 24 PDKTAIVFYGRAISYRELLEEAERLAGYLQQEcGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 95 MDDAEVVCLVTDQQFDANDVPVYSFAEVMH--------------------GLKVEASIQEEFS-----LEEAMT------ 143
Cdd:PRK08314 104 VTDSGARVAIVGSELAPKVAPAVGNLRLRHvivaqysdylpaepeiavpaWLRAEPPLQALAPggvvaWKEALAaglapp 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 144 -----------IIYTSGTTGKPKGVILTYGNHWASAVGSSLNLGLRDDDCWLACMPMFHVGGL-SLLMKNIMYGMRILLV 211
Cdd:PRK08314 184 phtagpddlavLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVLPLFHVTGMvHSMNAPIYAGATVVLM 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 212 PKYDADFIHKALQTRGVTIISVVSKMLTDLLERLGEETYP-SSLRCMllGGGPAPKP------LLETCvdkGIPVYQTYG 284
Cdd:PRK08314 264 PRWDREAAARLIERYRVTHWTNIPTMVVDFLASPGLAERDlSSLRYI--GGGGAAMPeavaerLKELT---GLDYVEGYG 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 285 MTETSSQicTLSADYMLTKVGSAGKPLFQCQLRI--EKDGVVVPPLVEGEIVVKGPNVTGGYFNREDATRE---TIqNG- 358
Cdd:PRK08314 339 LTETMAQ--THSNPPDRPKLQCLGIPTFGVDARVidPETLEELPPGEVGEIVVHGPQVFKGYWNRPEATAEafiEI-DGk 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 359 -WLHTGDLGYLDEEGFLYVLDRRSDLIISGGENIYPAQIEEVLLSHPMVAEAGVVGMTDDKWGQVPAAFVVKN----GEV 433
Cdd:PRK08314 416 rFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPDPRRGETVKAVVVLRpearGKT 495
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 446371684 434 TEEEIIHFCEEKLAKYKVPKKACFLEELPRNASKKLLRREL 474
Cdd:PRK08314 496 TEEEIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKILWRQL 536
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
28-481 |
5.83e-79 |
|
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: 253.29 E-value: 5.83e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 28 VTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSREELLWQMDDAEVVCLVTDq 107
Cdd:cd05907 6 ITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFVE- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 108 qfDANDVpvysfaevmhglkveasiqeefsleeaMTIIYTSGTTGKPKGVILTYGNHWASAVGSSLNLGLRDDDCWLACM 187
Cdd:cd05907 85 --DPDDL---------------------------ATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPATEGDRHLSFL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 188 PMFHV-GGLSLLMKNIMYGMRILLVPkyDADFIHKALQTRGVTIISVVSKML------------TDLLERLGEETYPSSL 254
Cdd:cd05907 136 PLAHVfERRAGLYVPLLAGARIYFAS--SAETLLDDLSEVRPTVFLAVPRVWekvyaaikvkavPGLKRKLFDLAVGGRL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 255 RCMLLGGGPAPKPLLETCVDKGIPVYQTYGMTETSSQI-CTLSADYmltKVGSAGKPLFQCQLRIEKDGvvvpplvegEI 333
Cdd:cd05907 214 RFAASGGAPLPAELLHFFRALGIPVYEGYGLTETSAVVtLNPPGDN---RIGTVGKPLPGVEVRIADDG---------EI 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 334 VVKGPNVTGGYFNREDATRETI-QNGWLHTGDLGYLDEEGFLYVLDRRSDLII-SGGENIYPAQIEEVLLSHPMVAEAGV 411
Cdd:cd05907 282 LVRGPNVMLGYYKNPEATAEALdADGWLHTGDLGEIDEDGFLHITGRKKDLIItSGGKNISPEPIENALKASPLISQAVV 361
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446371684 412 VGmtDDKwgQVPAAFVVKNGEVTEeeiiHFCEEKLAKYKVPkkacflEELPRN-ASKKLLRRELRQLVEEM 481
Cdd:cd05907 362 IG--DGR--PFLVALIVPDPEALE----AWAEEHGIAYTDV------AELAANpAVRAEIEAAVEAANARL 418
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
4-474 |
2.16e-78 |
|
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: 252.82 E-value: 2.16e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 4 MPNWLKQRAfltPDRTAIEIEEE--KVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVL 81
Cdd:cd05923 6 MLRRAASRA---PDACAIADPARglRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 82 LNTRLSREELLWQMDDAEVVCLVtdQQFDANDVP--VYSFAEVMH-GLKVEASIQEEFS---------LEEAMTIIYTSG 149
Cdd:cd05923 83 INPRLKAAELAELIERGEMTAAV--IAVDAQVMDaiFQSGVRVLAlSDLVGLGEPESAGpliedpprePEQPAFVFYTSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 150 TTGKPKGVILTYGNHWASAVGSSLNLGLR--DDDCWLACMPMFHVGGL-SLLMKNIMYGMRILLVPKYDADFIHKALQTR 226
Cdd:cd05923 161 TTGLPKGAVIPQRAAESRVLFMSTQAGLRhgRHNVVLGLMPLYHVIGFfAVLVAALALDGTYVVVEEFDPADALKLIEQE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 227 GVTIISVVSKMLTDLLER-LGEETYPSSLRCMLLGGGPAPKPLLETcVDKGIPVYQT--YGMTETSSQICTLSAdymltK 303
Cdd:cd05923 241 RVTSLFATPTHLDALAAAaEFAGLKLSSLRHVTFAGATMPDAVLER-VNQHLPGEKVniYGTTEAMNSLYMRDA-----R 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 304 VGSAGKPLFQCQLRIEKDG----VVVPPLVEGEIVVK--GPNVTGGYFNREDATRETIQNGWLHTGDLGYLDEEGFLYVL 377
Cdd:cd05923 315 TGTEMRPGFFSEVRIVRIGgspdEALANGEEGELIVAaaADAAFTGYLNQPEATAKKLQDGWYRTGDVGYVDPSGDVRIL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 378 DRRSDLIISGGENIYPAQIEEVLLSHPMVAEAGVVGMTDDKWGQVPAAFVVKN-GEVTEEEIIHFC-EEKLAKYKVPKKA 455
Cdd:cd05923 395 GRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPReGTLSADELDQFCrASELADFKRPRRY 474
|
490
....*....|....*....
gi 446371684 456 CFLEELPRNASKKLLRREL 474
Cdd:cd05923 475 FFLDELPKNAMNKVLRRQL 493
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
8-480 |
5.77e-78 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 253.33 E-value: 5.77e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 8 LKQRAFLTPDRTAIEIEEEKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLS 87
Cdd:PRK08162 24 LERAAEVYPDRPAVIHGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 88 REELLWQMDDAEVVCLVTDQQF-------------------DANDvPVYSFAEVMHGLKVEASIQE---EFSLE------ 139
Cdd:PRK08162 104 AASIAFMLRHGEAKVLIVDTEFaevarealallpgpkplviDVDD-PEYPGGRFIGALDYEAFLASgdpDFAWTlpadew 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 140 EAMTIIYTSGTTGKPKGVILTYGNHWASAVGSSLNLGLRDDDCWLACMPMFHVGGLSL--LMKnIMYGMRILLvPKYDAD 217
Cdd:PRK08162 183 DAIALNYTSGTTGNPKGVVYHHRGAYLNALSNILAWGMPKHPVYLWTLPMFHCNGWCFpwTVA-ARAGTNVCL-RKVDPK 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 218 FIHKALQTRGVTIIS---VVSKMLTDLlerlgeetyPSSLR-------CMLLGGGPAPKPLLETCVDKGIPVYQTYGMTE 287
Cdd:PRK08162 261 LIFDLIREHGVTHYCgapIVLSALINA---------PAEWRagidhpvHAMVAGAAPPAAVIAKMEEIGFDLTHVYGLTE 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 288 T--SSQIC-------TLSADYMLTKVGSAGKPlFQCQlriekDGVVV--PPLVE---------GEIVVKGPNVTGGYFNR 347
Cdd:PRK08162 332 TygPATVCawqpewdALPLDERAQLKARQGVR-YPLQ-----EGVTVldPDTMQpvpadgetiGEIMFRGNIVMKGYLKN 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 348 EDATRETIQNGWLHTGDLGYLDEEGFLYVLDRRSDLIISGGENIYPAQIEEVLLSHPMVAEAGVVGMTDDKWGQVPAAFV 427
Cdd:PRK08162 406 PKATEEAFAGGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDPKWGEVPCAFV 485
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 446371684 428 -VKNG-EVTEEEIIHFCEEKLAKYKVPKKACFlEELPRNASKKLLRRELRQLVEE 480
Cdd:PRK08162 486 eLKDGaSATEEEIIAHCREHLAGFKVPKAVVF-GELPKTSTGKIQKFVLREQAKS 539
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
29-475 |
9.37e-77 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 249.21 E-value: 9.37e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 29 TFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSREELLWQMDDAEVVCLVTDQQ 108
Cdd:PRK08008 39 SYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASLLVTSAQ 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 109 FdandVPVYS----------------------FAEVMH--GLKVEASIQEE----FSLEEAMTIIYTSGTTGKPKGVILT 160
Cdd:PRK08008 119 F----YPMYRqiqqedatplrhicltrvalpaDDGVSSftQLKAQQPATLCyappLSTDDTAEILFTSGTTSRPKGVVIT 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 161 YGNHWASAVGSSLNLGLRDDDCWLACMPMFHVG-GLSLLMKNIMYGMRILLVPKYDADFIHKALQTRGVTIISVVSKML- 238
Cdd:PRK08008 195 HYNLRFAGYYSAWQCALRDDDVYLTVMPAFHIDcQCTAAMAAFSAGATFVLLEKYSARAFWGQVCKYRATITECIPMMIr 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 239 TDLLERLGEETYPSSLRCML--LGGGPAPKPLLETCVdkGIPVYQTYGMTETssqICTLSADYMLTKV--GSAGKPLFQC 314
Cdd:PRK08008 275 TLMVQPPSANDRQHCLREVMfyLNLSDQEKDAFEERF--GVRLLTSYGMTET---IVGIIGDRPGDKRrwPSIGRPGFCY 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 315 QLRI-EKDGVVVPPLVEGEIVVKGpnVTG-----GYFNREDATRETIQ-NGWLHTGDLGYLDEEGFLYVLDRRSDLIISG 387
Cdd:PRK08008 350 EAEIrDDHNRPLPAGEIGEICIKG--VPGktifkEYYLDPKATAKVLEaDGWLHTGDTGYVDEEGFFYFVDRRCNMIKRG 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 388 GENIYPAQIEEVLLSHPMVAEAGVVGMTDDKWGQVPAAFVVKN-GE-VTEEEIIHFCEEKLAKYKVPKKACFLEELPRNA 465
Cdd:PRK08008 428 GENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNeGEtLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNC 507
|
490
....*....|
gi 446371684 466 SKKLLRRELR 475
Cdd:PRK08008 508 SGKIIKKNLK 517
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
139-475 |
2.68e-76 |
|
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: 242.95 E-value: 2.68e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 139 EEAMTIIYTSGTTGKPKGVILTYGNHWASAVGSSLNLGLRDDDCWLACMPMFHVGGLSL-LMKNIMYGMRILLV-PKYDA 216
Cdd:cd05917 2 DDVINIQFTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLCIPVPLFHCFGSVLgVLACLTHGATMVFPsPSFDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 217 DFIHKALQTRGVTIISVVSKMLTDLLERLGEETYP-SSLRCMLLGGGPAPKPLLETCVDK-GIPVYQT-YGMTETSSQI- 292
Cdd:cd05917 82 LAVLEAIEKEKCTALHGVPTMFIAELEHPDFDKFDlSSLRTGIMAGAPCPPELMKRVIEVmNMKDVTIaYGMTETSPVSt 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 293 CTLSADYMLTKVGSAGKPLFQCQLRI-EKDGVVVPPL-VEGEIVVKGPNVTGGYFNREDATRETI-QNGWLHTGDLGYLD 369
Cdd:cd05917 162 QTRTDDSIEKRVNTVGRIMPHTEAKIvDPEGGIVPPVgVPGELCIRGYSVMKGYWNDPEKTAEAIdGDGWLHTGDLAVMD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 370 EEGFLYVLDRRSDLIISGGENIYPAQIEEVLLSHPMVAEAGVVGMTDDKWGQVPAAFVV--KNGEVTEEEIIHFCEEKLA 447
Cdd:cd05917 242 EDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRlkEGAELTEEDIKAYCKGKIA 321
|
330 340
....*....|....*....|....*...
gi 446371684 448 KYKVPKKACFLEELPRNASKKLLRRELR 475
Cdd:cd05917 322 HYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
7-474 |
1.51e-73 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 242.25 E-value: 1.51e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 7 WLKQRAFLTPDRTAIEIEEEKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRL 86
Cdd:PRK06710 29 YVEQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLY 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 87 SREELLWQMDDAE---VVCL------VTDQQFD-----------ANDVP-----VYSF-----------AEVMHGLKVEA 130
Cdd:PRK06710 109 TERELEYQLHDSGakvILCLdlvfprVTNVQSAtkiehvivtriADFLPfpknlLYPFvqkkqsnlvvkVSESETIHLWN 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 131 SIQEEFSL--------EEAMTII-YTSGTTGKPKGVILTYGN---------HWasavgssLNLGLRDDDCWLACMPMFHV 192
Cdd:PRK06710 189 SVEKEVNTgvevpcdpENDLALLqYTGGTTGFPKGVMLTHKNlvsntlmgvQW-------LYNCKEGEEVVLGVLPFFHV 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 193 GGLSLLMK-NIMYGMRILLVPKYDADFIHKALQTRGVTIISVVSKMLTDLLER-LGEETYPSSLRCMLLGGGPAPKPLLE 270
Cdd:PRK06710 262 YGMTAVMNlSIMQGYKMVLIPKFDMKMVFEAIKKHKVTLFPGAPTIYIALLNSpLLKEYDISSIRACISGSAPLPVEVQE 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 271 TCVD-KGIPVYQTYGMTETSSqicTLSADYMLTK--VGSAGKPLFQCQLRIE--KDGVVVPPLVEGEIVVKGPNVTGGYF 345
Cdd:PRK06710 342 KFETvTGGKLVEGYGLTESSP---VTHSNFLWEKrvPGSIGVPWPDTEAMIMslETGEALPPGEIGEIVVKGPQIMKGYW 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 346 NREDATRETIQNGWLHTGDLGYLDEEGFLYVLDRRSDLIISGGENIYPAQIEEVLLSHPMVAEAGVVGMTDDKWGQVPAA 425
Cdd:PRK06710 419 NKPEETAAVLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKA 498
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 446371684 426 FVV-KNGEV-TEEEIIHFCEEKLAKYKVPKKACFLEELPRNASKKLLRREL 474
Cdd:PRK06710 499 FVVlKEGTEcSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVL 549
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
28-475 |
9.03e-71 |
|
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: 231.07 E-value: 9.03e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 28 VTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSREELLWQMDDAEVVCLVTDQ 107
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 108 qfdandvpvysfaevmhglkveasiqeefslEEAMTIIYTSGTTGKPKGVILTYGNHWASAVGSSLNLGLRDDDC-WLAC 186
Cdd:cd05972 81 -------------------------------EDPALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGLRPDDIhWNIA 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 187 MPMFHVGGLSLLMKNIMYGMRILLV--PKYDADFIHKALQTRGVTIISVVSKMLTDLLERLGEETYPSSLRCMLLGGGPA 264
Cdd:cd05972 130 DPGWAKGAWSSFFGPWLLGATVFVYegPRFDAERILELLERYGVTSFCGPPTAYRMLIKQDLSSYKFSHLRLVVSAGEPL 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 265 PKPLLETCVDK-GIPVYQTYGMTETSSQICTLSAdyMLTKVGSAGKPL--FQCQLrIEKDGVVVPPLVEGEIVVKGPNVT 341
Cdd:cd05972 210 NPEVIEWWRAAtGLPIRDGYGQTETGLTVGNFPD--MPVKPGSMGRPTpgYDVAI-IDDDGRELPPGEEGDIAIKLPPPG 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 342 --GGYFNREDATRETIQNGWLHTGDLGYLDEEGFLYVLDRRSDLIISGGENIYPAQIEEVLLSHPMVAEAGVVGMTDDKW 419
Cdd:cd05972 287 lfLGYVGDPEKTEASIRGDYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVR 366
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446371684 420 GQVPAAFVV-KNG----EVTEEEIIHFCEEKLAKYKVPKKACFLEELPRNASKKLLRRELR 475
Cdd:cd05972 367 GEVVKAFVVlTSGyepsEELAEELQGHVKKVLAPYKYPREIEFVEELPKTISGKIRRVELR 427
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
2-481 |
1.33e-70 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 234.28 E-value: 1.33e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 2 ETMPNWLKQRAFLTPDRTAIEIEEEKV--TFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVA 79
Cdd:PRK12583 18 QTIGDAFDATVARFPDREALVVRHQALryTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAIL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 80 VLLNTRLSREELLWQMDDAEVVCLVTDQQFDANDVpVYSFAEVMHGLKVE------------------------------ 129
Cdd:PRK12583 98 VNINPAYRASELEYALGQSGVRWVICADAFKTSDY-HAMLQELLPGLAEGqpgalacerlpelrgvvslapapppgflaw 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 130 ---------------ASIQEEFSLEEAMTIIYTSGTTGKPKGVILTYGNHWASAVGSSLNLGLRDDDCWLACMPMFHVGG 194
Cdd:PRK12583 177 helqargetvsrealAERQASLDRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCVPVPLYHCFG 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 195 LSLLMKNIMYGMRILLVPK--YDADFIHKALQTRGVTIISVVSKMLtdllerLGEETYP-------SSLRCMLLGGGPAP 265
Cdd:PRK12583 257 MVLANLGCMTVGACLVYPNeaFDPLATLQAVEEERCTALYGVPTMF------IAELDHPqrgnfdlSSLRTGIMAGAPCP 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 266 KPLLETCVDK--GIPVYQTYGMTETSSQIC-TLSADYMLTKVGSAGK--PLFQCQLrIEKDGVVVPPLVEGEIVVKGPNV 340
Cdd:PRK12583 331 IEVMRRVMDEmhMAEVQIAYGMTETSPVSLqTTAADDLERRVETVGRtqPHLEVKV-VDPDGATVPRGEIGELCTRGYSV 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 341 TGGYFNREDATRETI-QNGWLHTGDLGYLDEEGFLYVLDRRSDLIISGGENIYPAQIEEVLLSHPMVAEAGVVGMTDDKW 419
Cdd:PRK12583 410 MKGYWNNPEATAESIdEDGWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKY 489
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446371684 420 GQVPAAFVV-KNGE-VTEEEIIHFCEEKLAKYKVPKKACFLEELPRNASKKLLRRELRQL-VEEM 481
Cdd:PRK12583 490 GEEIVAWVRlHPGHaASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMREIsIEEL 554
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
2-481 |
5.97e-70 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 232.39 E-value: 5.97e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 2 ETMPNWLKQRAFLTPDRTAIEIEEEKV--TFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVA 79
Cdd:PRK08315 16 QTIGQLLDRTAARYPDREALVYRDQGLrwTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAIL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 80 VLLNTRLSREELLWQMDDAEVVCLVTDQQFDAND--------VP-------------------------------VYSFA 120
Cdd:PRK08315 96 VTINPAYRLSELEYALNQSGCKALIAADGFKDSDyvamlyelAPelatcepgqlqsarlpelrrviflgdekhpgMLNFD 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 121 EVM-HGLKVE----ASIQEEFSLEEAMTIIYTSGTTGKPKGVILTYGN-----HWasaVGSSLNLGLRDDDCwlACMPMF 190
Cdd:PRK08315 176 ELLaLGRAVDdaelAARQATLDPDDPINIQYTSGTTGFPKGATLTHRNilnngYF---IGEAMKLTEEDRLC--IPVPLY 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 191 HVGGLSL-LMKNIMYG--MrILLVPKYDADFIHKALQTRGVTIISVVSKMLTDLLERLGEETYP-SSLRCMLLGGGPAPK 266
Cdd:PRK08315 251 HCFGMVLgNLACVTHGatM-VYPGEGFDPLATLAAVEEERCTALYGVPTMFIAELDHPDFARFDlSSLRTGIMAGSPCPI 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 267 PLLETCVDKgipVYQT-----YGMTETSSQICTLSADYMLTK-VGSAGKPLFQCQLRI--EKDGVVVPPLVEGEIVVKGP 338
Cdd:PRK08315 330 EVMKRVIDK---MHMSevtiaYGMTETSPVSTQTRTDDPLEKrVTTVGRALPHLEVKIvdPETGETVPRGEQGELCTRGY 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 339 NVTGGYFNREDATRETI-QNGWLHTGDLGYLDEEGFLYVLDRRSDLIISGGENIYPAQIEEVLLSHPMVAEAGVVGMTDD 417
Cdd:PRK08315 407 SVMKGYWNDPEKTAEAIdADGWMHTGDLAVMDEEGYVNIVGRIKDMIIRGGENIYPREIEEFLYTHPKIQDVQVVGVPDE 486
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446371684 418 KWGQVPAAFVV-KNGE-VTEEEIIHFCEEKLAKYKVPKKACFLEELPRNASKKLLRRELRQLVEEM 481
Cdd:PRK08315 487 KYGEEVCAWIIlRPGAtLTEEDVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGKIQKFKMREMMIEE 552
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
10-475 |
2.24e-68 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 227.27 E-value: 2.24e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 10 QRAFLTPDRTAIEIEE--EKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLS 87
Cdd:PRK13391 5 IHAQTTPDKPAVIMAStgEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 88 REELLWQMDDAEVVCLVTDQQ------FDANDVP----------------VYSFAEVMHGLKvEASIQEEfSLEEAMtiI 145
Cdd:PRK13391 85 PAEAAYIVDDSGARALITSAAkldvarALLKQCPgvrhrlvldgdgelegFVGYAEAVAGLP-ATPIADE-SLGTDM--L 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 146 YTSGTTGKPKGViltYGNHWASAVGSSLNL--------GLRDDDCWLACMPMFHVGGLSLLMKNIMYGMRILLVPKYDAD 217
Cdd:PRK13391 161 YSSGTTGRPKGI---KRPLPEQPPDTPLPLtaflqrlwGFRSDMVYLSPAPLYHSAPQRAVMLVIRLGGTVIVMEHFDAE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 218 FIHKALQTRGVTIISVVSKMLTDLLeRLGEET---YP-SSLRCMLLGGGPAPKPLLETCVDKGIPV-YQTYGMTETSSqI 292
Cdd:PRK13391 238 QYLALIEEYGVTHTQLVPTMFSRML-KLPEEVrdkYDlSSLEVAIHAAAPCPPQVKEQMIDWWGPIiHEYYAATEGLG-F 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 293 CTLSADYMLTKVGSAGKPLFQcQLRI-EKDGVVVPPLVEGEIVVKGpnvtgG----YFNREDATRET--IQNGWLHTGDL 365
Cdd:PRK13391 316 TACDSEEWLAHPGTVGRAMFG-DLHIlDDDGAELPPGEPGTIWFEG-----GrpfeYLNDPAKTAEArhPDGTWSTVGDI 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 366 GYLDEEGFLYVLDRRSDLIISGGENIYPAQIEEVLLSHPMVAEAGVVGMTDDKWGQVPAAFV-----VKNGEVTEEEIIH 440
Cdd:PRK13391 390 GYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVqpvdgVDPGPALAAELIA 469
|
490 500 510
....*....|....*....|....*....|....*
gi 446371684 441 FCEEKLAKYKVPKKACFLEELPRNASKKLLRRELR 475
Cdd:PRK13391 470 FCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLLR 504
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
33-476 |
4.04e-68 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 226.50 E-value: 4.04e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 33 LHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSREELLWQMDDAEVVCLV--TD---Q 107
Cdd:PRK12406 17 LAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIahADllhG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 108 QFDA--NDVPVYSF---AEVMHGLKVEASI-------------------QEEFSLEEAMTIIYTSGTTGKPKGVILTYGN 163
Cdd:PRK12406 97 LASAlpAGVTVLSVptpPEIAAAYRISPALltppagaidwegwlaqqepYDGPPVPQPQSMIYTSGTTGHPKGVRRAAPT 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 164 HWASAVGS---SLNLGLRDDDCWLACMPMFHVGGLSLLMKNIMYGMRILLVPKYDADFIHKALQTRGVTIISVVSKMLTD 240
Cdd:PRK12406 177 PEQAAAAEqmrALIYGLKPGIRALLTGPLYHSAPNAYGLRAGRLGGVLVLQPRFDPEELLQLIERHRITHMHMVPTMFIR 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 241 LLeRLGEETYP----SSLRCMLLGGGPAPKPLLETCVDKGIPV-YQTYGMTETSSQICTLSADYmLTKVGSAGKPLFQCQ 315
Cdd:PRK12406 257 LL-KLPEEVRAkydvSSLRHVIHAAAPCPADVKRAMIEWWGPViYEYYGSTESGAVTFATSEDA-LSHPGTVGKAAPGAE 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 316 LR-IEKDGVVVPPLVEGEIVVK---GPNVTggYFNREDATRETIQNGWLHTGDLGYLDEEGFLYVLDRRSDLIISGGENI 391
Cdd:PRK12406 335 LRfVDEDGRPLPQGEIGEIYSRiagNPDFT--YHNKPEKRAEIDRGGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNI 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 392 YPAQIEEVLLSHPMVAEAGVVGMTDDKWGQVPAAFVVKNGEVT--EEEIIHFCEEKLAKYKVPKKACFLEELPRNASKKL 469
Cdd:PRK12406 413 YPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPGATldEADIRAQLKARLAGYKVPKHIEIMAELPREDSGKI 492
|
....*..
gi 446371684 470 LRRELRQ 476
Cdd:PRK12406 493 FKRRLRD 499
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
3-476 |
1.06e-67 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 226.17 E-value: 1.06e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 3 TMPNWLKQRAFLTPDRTAIEIEE-EKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVL 81
Cdd:PRK06087 24 SLADYWQQTARAMPDKIAVVDNHgASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 82 LNTRLSREELLWQMDDAEVVCLVTDQQFD-----------ANDVP-------VYSFAEVMHGLKVEASIQEEFSLEEAMT 143
Cdd:PRK06087 104 LLPSWREAELVWVLNKCQAKMFFAPTLFKqtrpvdlilplQNQLPqlqqivgVDKLAPATSSLSLSQIIADYEPLTTAIT 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 144 --------IIYTSGTTGKPKGVILTYGNHWASAVGSSLNLGLRDDDCWLACMPMFHVGG-LSLLMKNIMYGMRILLVPKY 214
Cdd:PRK06087 184 thgdelaaVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGfLHGVTAPFLIGARSVLLDIF 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 215 DADFIHKALQTRGVTIISVVSKMLTDLLERLGE-ETYPSSLRCMLLGGGPAPKPLLETCVDKGIPVYQTYGMTETSSQIC 293
Cdd:PRK06087 264 TPDACLALLEQQRCTCMLGATPFIYDLLNLLEKqPADLSALRFFLCGGTTIPKKVARECQQRGIKLLSVYGSTESSPHAV 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 294 TLSADYMLTKVGSAGKPLFQCQLRI-EKDGVVVPPLVEGEIVVKGPNVTGGYFNREDATRETIQN-GWLHTGDLGYLDEE 371
Cdd:PRK06087 344 VNLDDPLSRFMHTDGYAAAGVEIKVvDEARKTLPPGCEGEEASRGPNVFMGYLDEPELTARALDEeGWYYSGDLCRMDEA 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 372 GFLYVLDRRSDLIISGGENIYPAQIEEVLLSHPMVAEAGVVGMTDDKWGQVPAAFVVKNGEV----TEEEIIHFCEEKLA 447
Cdd:PRK06087 424 GYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVVLKAPHhsltLEEVVAFFSRKRVA 503
|
490 500
....*....|....*....|....*....
gi 446371684 448 KYKVPKKACFLEELPRNASKKLLRRELRQ 476
Cdd:PRK06087 504 KYKYPEHIVVIDKLPRTASGKIQKFLLRK 532
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
144-471 |
1.70e-67 |
|
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: 219.29 E-value: 1.70e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 144 IIYTSGTTGKPKGVILTYGNHWASAVGSSLNLGLRDDDCWLACMPMFHVGGLSL-LMKNIMYGMRILLVPKYDADFIHKA 222
Cdd:cd17638 5 IMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIINPFFHTFGYKAgIVACLLTGATVVPVAVFDVDAILEA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 223 LQTRGVTIISVVSKMLTDLLERLGEETYP-SSLRCMLLGGGPAPKPLLETCVDK-GIPVYQT-YGMTETSSQICTLSADY 299
Cdd:cd17638 85 IERERITVLPGPPTLFQSLLDHPGRKKFDlSSLRAAVTGAATVPVELVRRMRSElGFETVLTaYGLTEAGVATMCRPGDD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 300 MLTKVGSAGKPLFQCQLRIEKDGvvvpplvegEIVVKGPNVTGGYFNREDATRETI-QNGWLHTGDLGYLDEEGFLYVLD 378
Cdd:cd17638 165 AETVATTCGRACPGFEVRIADDG---------EVLVRGYNVMQGYLDDPEATAEAIdADGWLHTGDVGELDERGYLRITD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 379 RRSDLIISGGENIYPAQIEEVLLSHPMVAEAGVVGMTDDKWGQVPAAFVV-KNGE-VTEEEIIHFCEEKLAKYKVPKKAC 456
Cdd:cd17638 236 RLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVaRPGVtLTEEDVIAWCRERLANYKVPRFVR 315
|
330
....*....|....*
gi 446371684 457 FLEELPRNASKKLLR 471
Cdd:cd17638 316 FLDELPRNASGKVMK 330
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
26-476 |
7.43e-67 |
|
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: 221.15 E-value: 7.43e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 26 EKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSREELLWQMDDAEVVCLVT 105
Cdd:cd05971 5 EKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 106 DqqfdANDVPVYsfaevmhglkveasiqeefsleeamtIIYTSGTTGKPKGVI----LTYGNhwASAVGSSLNLGLRDDD 181
Cdd:cd05971 85 D----GSDDPAL--------------------------IIYTSGTTGPPKGALhahrVLLGH--LPGVQFPFNLFPRDGD 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 182 CWLACMPMFHVGGL-SLLMKNIMYGMRILL--VPKYDADFIHKALQTRGVTIISVVSKMLTdLLERLGEET--YPSSLRC 256
Cdd:cd05971 133 LYWTPADWAWIGGLlDVLLPSLYFGVPVLAhrMTKFDPKAALDLMSRYGVTTAFLPPTALK-MMRQQGEQLkhAQVKLRA 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 257 MLLGGGPAPKPLLETCVDK-GIPVYQTYGMTETSSqICTLSADYMLTKVGSAGKPLFQCQLRIEKD-GVVVPPLVEGEIV 334
Cdd:cd05971 212 IATGGESLGEELLGWAREQfGVEVNEFYGQTECNL-VIGNCSALFPIKPGSMGKPIPGHRVAIVDDnGTPLPPGEVGEIA 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 335 VKGPNVTG--GYFNREDATRETIQNGWLHTGDLGYLDEEGFLYVLDRRSDLIISGGENIYPAQIEEVLLSHPMVAEAGVV 412
Cdd:cd05971 291 VELPDPVAflGYWNNPSATEKKMAGDWLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVV 370
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446371684 413 GMTDDKWGQVPAAFVVKN-GEVTEE----EIIHFCEEKLAKYKVPKKACFLEELPRNASKKLLRRELRQ 476
Cdd:cd05971 371 GIPDPIRGEIVKAFVVLNpGETPSDalarEIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRRELRA 439
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
44-475 |
2.10e-66 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 222.55 E-value: 2.10e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 44 LTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSREELLWQMDDAEVVCLVTDQQF--------DANDVP 115
Cdd:PLN02246 67 LHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAKLIITQSCYvdklkglaEDDGVT 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 116 VY----------SFAEVMHGlkVEASIQE-EFSLEEAMTIIYTSGTTGKPKGVILTYGNHWASAV----GSSLNLGLRDD 180
Cdd:PLN02246 147 VVtiddppegclHFSELTQA--DENELPEvEISPDDVVALPYSSGTTGLPKGVMLTHKGLVTSVAqqvdGENPNLYFHSD 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 181 DCWLACMPMFHVGGL-SLLMKNIMYGMRILLVPKYDADFIHKALQTRGVTIISVVSKMLTDLLERLGEETYP-SSLRCML 258
Cdd:PLN02246 225 DVILCVLPMFHIYSLnSVLLCGLRVGAAILIMPKFEIGALLELIQRHKVTIAPFVPPIVLAIAKSPVVEKYDlSSIRMVL 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 259 LGGGPAPKPLLETCVDKgIP---VYQTYGMTETSSQI--CTLSADYML-TKVGSAGKPLFQCQLRI--EKDGVVVPPLVE 330
Cdd:PLN02246 305 SGAAPLGKELEDAFRAK-LPnavLGQGYGMTEAGPVLamCLAFAKEPFpVKSGSCGTVVRNAELKIvdPETGASLPRNQP 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 331 GEIVVKGPNVTGGYFNREDATRETI-QNGWLHTGDLGYLDEEGFLYVLDRRSDLIISGGENIYPAQIEEVLLSHPMVAEA 409
Cdd:PLN02246 384 GEICIRGPQIMKGYLNDPEATANTIdKDGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADA 463
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446371684 410 GVVGMTDDKWGQVPAAFVVK-NG-EVTEEEIIHFCEEKLAKYKVPKKACFLEELPRNASKKLLRRELR 475
Cdd:PLN02246 464 AVVPMKDEVAGEVPVAFVVRsNGsEITEDEIKQFVAKQVVFYKRIHKVFFVDSIPKAPSGKILRKDLR 531
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
9-481 |
2.68e-66 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 221.19 E-value: 2.68e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 9 KQRAFLTPDRTAIEIEEEKVTFLQLHEKVVSVCEHLtHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSR 88
Cdd:PRK07638 8 KKHASLQPNKIAIKENDRVLTYKDWFESVCKVANWL-NEKESKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 89 EELLWQMDDAEVVCLVTDQQF----DANDVPVYSFAEVMHglKVEASIQEEFSLEEAMTIIY----TSGTTGKPKGVILT 160
Cdd:PRK07638 87 DELKERLAISNADMIVTERYKlndlPDEEGRVIEIDEWKR--MIEKYLPTYAPIENVQNAPFymgfTSGSTGKPKAFLRA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 161 YGNHWASAVGSSLNLGLRDDDCWLACMPMFH----VGGLSLLMknimYGMRILLVPKYDADFIHKALQTRGVTIISVVSK 236
Cdd:PRK07638 165 QQSWLHSFDCNVHDFHMKREDSVLIAGTLVHslflYGAISTLY----VGQTVHLMRKFIPNQVLDKLETENISVMYTVPT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 237 MLTDLLErlgEETYPSSLRCMLLGGGPAPKPLLETCVDK--GIPVYQTYGMTETSSqICTLSADYMLTKVGSAGKPLFQC 314
Cdd:PRK07638 241 MLESLYK---ENRVIENKMKIISSGAKWEAEAKEKIKNIfpYAKLYEFYGASELSF-VTALVDEESERRPNSVGRPFHNV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 315 QLRIEK-DGVVVPPLVEGEIVVKGPNVTGGYFNREDATRETIQNGWLHTGDLGYLDEEGFLYVLDRRSDLIISGGENIYP 393
Cdd:PRK07638 317 QVRICNeAGEEVQKGEIGTVYVKSPQFFMGYIIGGVLARELNADGWMTVRDVGYEDEEGFIYIVGREKNMILFGGINIFP 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 394 AQIEEVLLSHPMVAEAGVVGMTDDKWGQVPAAFVvkNGEVTEEEIIHFCEEKLAKYKVPKKACFLEELPRNASKKLLRRE 473
Cdd:PRK07638 397 EEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAII--KGSATKQQLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARME 474
|
....*...
gi 446371684 474 LRQLVEEM 481
Cdd:PRK07638 475 AKSWIENQ 482
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
8-475 |
2.83e-66 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 224.45 E-value: 2.83e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 8 LKQRAFLTPDRTAIEI--------EEEKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHAlSYVGAVA 79
Cdd:PRK07529 31 LSRAAARHPDAPALSFlldadpldRPETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWG-GEAAGIA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 80 VLLNTRLSREELLWQMDDAEVVCLVTDQQFDANDV---------------------------PVYSFAEVMHGLKVEASI 132
Cdd:PRK07529 110 NPINPLLEPEQIAELLRAAGAKVLVTLGPFPGTDIwqkvaevlaalpelrtvvevdlarylpGPKRLAVPLIRRKAHARI 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 133 Q---EEFSLEEAMTII--------------YTSGTTGKPKGVILTYGNHWASAVGSSLNLGLRDDDCWLACMPMFHVGGL 195
Cdd:PRK07529 190 LdfdAELARQPGDRLFsgrpigpddvaayfHTGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPGDTVFCGLPLFHVNAL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 196 -SLLMKNIMYGMRILLV-------PKYDADFiHKALQTRGVTIISVVSKMLTDLLERLGEETYPSSLRCMLLGGGPAPKP 267
Cdd:PRK07529 270 lVTGLAPLARGAHVVLAtpqgyrgPGVIANF-WKIVERYRINFLSGVPTVYAALLQVPVDGHDISSLRYALCGAAPLPVE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 268 LLETCVDK-GIPVYQTYGMTETSSqICTLSADYMLTKVGSAGKPLFQCQLRIEK---DGVVVPPLVE---GEIVVKGPNV 340
Cdd:PRK07529 349 VFRRFEAAtGVRIVEGYGLTEATC-VSSVNPPDGERRIGSVGLRLPYQRVRVVIlddAGRYLRDCAVdevGVLCIAGPNV 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 341 TGGYFNREDATRETIQNGWLHTGDLGYLDEEGFLYVLDRRSDLIISGGENIYPAQIEEVLLSHPMVAEAGVVGMTDDKWG 420
Cdd:PRK07529 428 FSGYLEAAHNKGLWLEDGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAG 507
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 446371684 421 QVPAAFV--VKNGEVTEEEIIHFCEEKLA-KYKVPKKACFLEELPRNASKKLLRRELR 475
Cdd:PRK07529 508 ELPVAYVqlKPGASATEAELLAFARDHIAeRAAVPKHVRILDALPKTAVGKIFKPALR 565
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
48-475 |
5.44e-66 |
|
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: 219.94 E-value: 5.44e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 48 GVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSREELLWQMD---DAEVVCLVTDQqfDANDVPVySFAEVmh 124
Cdd:cd05929 38 GVWIADGVYIYLINSILTVFAAAAAWKCGACPAYKSSRAPRAEACAIIEikaAALVCGLFTGG--GALDGLE-DYEAA-- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 125 glkvEASIQEEFSLEEAMT--IIYTSGTTGKPKGVILTYG---NHWASAVGSSLNLGLRDDDCWLACMPMFHVGGLSLLM 199
Cdd:cd05929 113 ----EGGSPETPIEDEAAGwkMLYSGGTTGRPKGIKRGLPggpPDNDTLMAAALGFGPGADSVYLSPAPLYHAAPFRWSM 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 200 KNIMYGMRILLVPKYDADFIHKALQTRGVTIISVVSKMLTDLLERLGEETYP---SSLRCMLLGGGPAPKPLLETCVDKG 276
Cdd:cd05929 189 TALFMGGTLVLMEKFDPEEFLRLIERYRVTFAQFVPTMFVRLLKLPEAVRNAydlSSLKRVIHAAAPCPPWVKEQWIDWG 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 277 IP-VYQTYGMTETSSqICTLSADYMLTKVGSAGKPLfQCQLRI-EKDGVVVPPLVEGEIVVKGPNvTGGYFNREDATRET 354
Cdd:cd05929 269 GPiIWEYYGGTEGQG-LTIINGEEWLTHPGSVGRAV-LGKVHIlDEDGNEVPPGEIGEVYFANGP-GFEYTNDPEKTAAA 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 355 I-QNGWLHTGDLGYLDEEGFLYVLDRRSDLIISGGENIYPAQIEEVLLSHPMVAEAGVVGMTDDKWGQVPAAFV-----V 428
Cdd:cd05929 346 RnEGGWSTLGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVqpapgA 425
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 446371684 429 KNGEVTEEEIIHFCEEKLAKYKVPKKACFLEELPRNASKKLLRRELR 475
Cdd:cd05929 426 DAGTALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLR 472
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
3-477 |
6.64e-66 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 221.56 E-value: 6.64e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 3 TMPNWLKQRAFLTPDRTAIEIEEEKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLL 82
Cdd:PRK06155 22 TLPAMLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 83 NTRLSREELLWQMDDAEVVCLVTDQQF----DANDVPVYSFAEV-MHGLKVEASIQEEFSLE-----------------E 140
Cdd:PRK06155 102 NTALRGPQLEHILRNSGARLLVVEAALlaalEAADPGDLPLPAVwLLDAPASVSVPAGWSTAplppldapapaaavqpgD 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 141 AMTIIYTSGTTGKPKGVILTYGNHWASAVGSSLNLGLRDDDCWLACMPMFHVGGLSLLMKNIMYGMRILLVPKYDADFIH 220
Cdd:PRK06155 182 TAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADDVLYTTLPLFHTNALNAFFQALLAGATYVLEPRFSASGFW 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 221 KALQTRGVTIISVVSKMLTDLLER-LGEETYPSSLRCMLLGGGPAP--KPLLETCvdkGIPVYQTYGMTETSSQICTLSA 297
Cdd:PRK06155 262 PAVRRHGATVTYLLGAMVSILLSQpARESDRAHRVRVALGPGVPAAlhAAFRERF---GVDLLDGYGSTETNFVIAVTHG 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 298 DymlTKVGSAGK--PLFQCQLrIEKDGVVVPPLVEGEIVVKGPN---VTGGYFNREDATRETIQNGWLHTGDLGYLDEEG 372
Cdd:PRK06155 339 S---QRPGSMGRlaPGFEARV-VDEHDQELPDGEPGELLLRADEpfaFATGYFGMPEKTVEAWRNLWFHTGDRVVRDADG 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 373 FLYVLDRRSDLIISGGENIYPAQIEEVLLSHPMVAEAGVVG----MTDDkwgQVPAAFVVKNGEVTE-EEIIHFCEEKLA 447
Cdd:PRK06155 415 WFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPvpseLGED---EVMAAVVLRDGTALEpVALVRHCEPRLA 491
|
490 500 510
....*....|....*....|....*....|
gi 446371684 448 KYKVPKKACFLEELPRNASKKLLRRELRQL 477
Cdd:PRK06155 492 YFAVPRYVEFVAALPKTENGKVQKFVLREQ 521
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
12-476 |
3.36e-65 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 218.59 E-value: 3.36e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 12 AFLTPDRTAIEIEE-EKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSREE 90
Cdd:PRK07514 12 AFADRDAPFIETPDgLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 91 LLWQMDDAE---VVC------LVTDQQFDANDVPVYSFAEVMHGLKVEASIQEEFSLEEA-------MTIIYTSGTTGKP 154
Cdd:PRK07514 92 LDYFIGDAEpalVVCdpanfaWLSKIAAAAGAPHVETLDADGTGSLLEAAAAAPDDFETVprgaddlAAILYTSGTTGRS 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 155 KGVILTYGNHWASAVGSSLNLGLRDDDCWLACMPMFHVGGLsLLMKNI--MYGMRILLVPKYDADFIHKALQTrgVTIIS 232
Cdd:PRK07514 172 KGAMLSHGNLLSNALTLVDYWRFTPDDVLIHALPIFHTHGL-FVATNValLAGASMIFLPKFDPDAVLALMPR--ATVMM 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 233 VVSKMLTDLLE--RLGEETyPSSLRcmLLGGGPAPKpLLETCVD----KGIPVYQTYGMTETSsqictlsadyMLT---- 302
Cdd:PRK07514 249 GVPTFYTRLLQepRLTREA-AAHMR--LFISGSAPL-LAETHREfqerTGHAILERYGMTETN----------MNTsnpy 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 303 ----KVGSAGKPLFQCQLRI--EKDGVVVPPLVEGEIVVKGPNVTGGYFNREDATRETIQ-NGWLHTGDLGYLDEEGFLY 375
Cdd:PRK07514 315 dgerRAGTVGFPLPGVSLRVtdPETGAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRaDGFFITGDLGKIDERGYVH 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 376 VLDRRSDLIISGGENIYPAQIEEVLLSHPMVAEAGVVGMTDDKWGQVPAAFVV--KNGEVTEEEIIHFCEEKLAKYKVPK 453
Cdd:PRK07514 395 IVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVpkPGAALDEAAILAALKGRLARFKQPK 474
|
490 500
....*....|....*....|...
gi 446371684 454 KACFLEELPRNASKKLLRRELRQ 476
Cdd:PRK07514 475 RVFFVDELPRNTMGKVQKNLLRE 497
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
16-476 |
8.86e-65 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 218.47 E-value: 8.86e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 16 PDRTAIEIEEEKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSREELLWQM 95
Cdd:PRK13382 57 PDRPGLIDELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPALAEVV 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 96 DDAEVVCLVTDQQF------DANDVP----VYSFAEVMHGLKVEASIQE------EFSLEEAMTIIYTSGTTGKPKGvil 159
Cdd:PRK13382 137 TREGVDTVIYDEEFsatvdrALADCPqatrIVAWTDEDHDLTVEVLIAAhagqrpEPTGRKGRVILLTSGTTGTPKG--- 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 160 tyGNHwaSAVGSSLNL-GLRDDDCWLA------CMPMFHVGGLSLLMKNIMYGMRILLVPKYDADFIHKALQTRGVTIIS 232
Cdd:PRK13382 214 --ARR--SGPGGIGTLkAILDRTPWRAeeptviVAPMFHAWGFSQLVLAASLACTIVTRRRFDPEATLDLIDRHRATGLA 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 233 VVSKMLTDLLErLGEETYPS----SLRCMLLGGGPAPKPLLETCVDK-GIPVYQTYGMTEtSSQICTLSADYMLTKVGSA 307
Cdd:PRK13382 290 VVPVMFDRIMD-LPAEVRNRysgrSLRFAAASGSRMRPDVVIAFMDQfGDVIYNNYNATE-AGMIATATPADLRAAPDTA 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 308 GKPLFQCQLRI-EKDGVVVPPLVEGEIVVKGPNVTGGYfnREDATRETIQnGWLHTGDLGYLDEEGFLYVLDRRSDLIIS 386
Cdd:PRK13382 368 GRPAEGTEIRIlDQDFREVPTGEVGTIFVRNDTQFDGY--TSGSTKDFHD-GFMASGDVGYLDENGRLFVVGRDDEMIVS 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 387 GGENIYPAQIEEVLLSHPMVAEAGVVGMTDDKWGQVPAAFVVKNGEV--TEEEIIHFCEEKLAKYKVPKKACFLEELPRN 464
Cdd:PRK13382 445 GGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPGAsaTPETLKQHVRDNLANYKVPRDIVVLDELPRG 524
|
490
....*....|..
gi 446371684 465 ASKKLLRRELRQ 476
Cdd:PRK13382 525 ATGKILRRELQA 536
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
32-478 |
1.04e-64 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 218.90 E-value: 1.04e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 32 QLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSREELLWQMDDAEVVCLVTDQQ--- 108
Cdd:PLN02860 37 EFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWSFEEAKSAMLLVRPVMLVTDETcss 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 109 ----FDANDVP---------------------VYSFAEVMHGLKVEASIQEEFSLEEAMTIIYTSGTTGKPKGVILTygn 163
Cdd:PLN02860 117 wyeeLQNDRLPslmwqvflespsssvfiflnsFLTTEMLKQRALGTTELDYAWAPDDAVLICFTSGTTGRPKGVTIS--- 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 164 HWASAVGSSLNL---GLRDDDCWLACMPMFHVGGLSLLMKNIMYGMRILLVPKYDADFIHKALQTRGVTIISVVSKMLTD 240
Cdd:PLN02860 194 HSALIVQSLAKIaivGYGEDDVYLHTAPLCHIGGLSSALAMLMVGACHVLLPKFDAKAALQAIKQHNVTSMITVPAMMAD 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 241 LLeRLGEETYPS----SLRCMLLGGGPAPKPLLETCVdKGIP---VYQTYGMTETSSQI-------------CTLSADYM 300
Cdd:PLN02860 274 LI-SLTRKSMTWkvfpSVRKILNGGGSLSSRLLPDAK-KLFPnakLFSAYGMTEACSSLtfmtlhdptlespKQTLQTVN 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 301 LTKVGSA--------GKPLFQCQLRIEKDGvvvpPLVEGEIVVKGPNVTGGYF--NREDATrETIQNGWLHTGDLGYLDE 370
Cdd:PLN02860 352 QTKSSSVhqpqgvcvGKPAPHVELKIGLDE----SSRVGRILTRGPHVMLGYWgqNSETAS-VLSNDGWLDTGDIGWIDK 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 371 EGFLYVLDRRSDLIISGGENIYPAQIEEVLLSHPMVAEAGVVGMTDDKWGQVPAAFV----------------VKNGEVT 434
Cdd:PLN02860 427 AGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEMVVACVrlrdgwiwsdnekenaKKNLTLS 506
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 446371684 435 EEEIIHFCEEK-LAKYKVPKKACFLEE-LPRNASKKLLRRELRQLV 478
Cdd:PLN02860 507 SETLRHHCREKnLSRFKIPKLFVQWRKpFPLTTTGKIRRDEVRREV 552
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
1-480 |
1.10e-64 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 215.89 E-value: 1.10e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 1 METMPNWLKQR-AFLTPDRTAIEIEEEKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVA 79
Cdd:PRK09029 1 MMIFSDWPWRHwAQVRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 80 VLLNTRLSREELlwqmdDAEVVCLVTDQQFDANDVPVYSFAEVMHGLKVEASIQEEFSLEEAMTIIYTSGTTGKPKGVIL 159
Cdd:PRK09029 81 LPLNPQLPQPLL-----EELLPSLTLDFALVLEGENTFSALTSLHLQLVEGAHAVAWQPQRLATMTLTSGSTGLPKAAVH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 160 TYGNHWASAVG--SSLNLGlrDDDCWLACMPMFHVGGLSllmknIMYgmRIL-----LVPKYDADFIHkALQtrGVTIIS 232
Cdd:PRK09029 156 TAQAHLASAEGvlSLMPFT--AQDSWLLSLPLFHVSGQG-----IVW--RWLyagatLVVRDKQPLEQ-ALA--GCTHAS 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 233 VVSKMLTDLLERLGEetyPSSLRCMLLGGGPAPKPLLETCVDKGIPVYQTYGMTETSSQICTLSADymltKVGSAGKPLF 312
Cdd:PRK09029 224 LVPTQLWRLLDNRSE---PLSLKAVLLGGAAIPVELTEQAEQQGIRCWCGYGLTEMASTVCAKRAD----GLAGVGSPLP 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 313 QCQLRiekdgvvvppLVEGEIVVKGPNVTGGYFNREDATRETIQNGWLHTGDLGYLDEeGFLYVLDRRSDLIISGGENIY 392
Cdd:PRK09029 297 GREVK----------LVDGEIWLRGASLALGYWRQGQLVPLVNDEGWFATRDRGEWQN-GELTILGRLDNLFFSGGEGIQ 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 393 PAQIEEVLLSHPMVAEAGVVGMTDDKWGQVPAAFVVKNGEVTEEEIIHFCEEKLAKYKVPkKACFL--EELPrNASKKLL 470
Cdd:PRK09029 366 PEEIERVINQHPLVQQVFVVPVADAEFGQRPVAVVESDSEAAVVNLAEWLQDKLARFQQP-VAYYLlpPELK-NGGIKIS 443
|
490
....*....|
gi 446371684 471 RRELRQLVEE 480
Cdd:PRK09029 444 RQALKEWVAQ 453
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
7-480 |
1.14e-64 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 218.76 E-value: 1.14e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 7 WLKQRAFLTPDRTAIEIEEEKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTrL 86
Cdd:PRK06178 38 YLRAWARERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSP-L 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 87 SRE-ELLWQMDDAEVVCLVTDQQFDANDVPVYSFAEVMHGLKVEAS------------------------IQEEFSLEEA 141
Cdd:PRK06178 117 FREhELSYELNDAGAEVLLALDQLAPVVEQVRAETSLRHVIVTSLAdvlpaeptlplpdslraprlaaagAIDLLPALRA 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 142 MT---------------IIYTSGTTGKPKGVILTYGNH-WASAVGSSLNLGLRDDDCWLACMPMFHVGGLSL-LMKNIMY 204
Cdd:PRK06178 197 CTapvplpppaldalaaLNYTGGTTGMPKGCEHTQRDMvYTAAAAYAVAVVGGEDSVFLSFLPEFWIAGENFgLLFPLFS 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 205 GMRILLVPKYDADFIHKALQTRGVTIISVVSKMLTDLLE--RLGEETYpSSLRcmllgggpapKPLLETCVDKGIPVYQ- 281
Cdd:PRK06178 277 GATLVLLARWDAVAFMAAVERYRVTRTVMLVDNAVELMDhpRFAEYDL-SSLR----------QVRVVSFVKKLNPDYRq 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 282 -------------TYGMTETssQIC-TLSA-----DYMLTkvgsaGKPLFqCQLRI---------EKDGVVVPPLVEGEI 333
Cdd:PRK06178 346 rwraltgsvlaeaAWGMTET--HTCdTFTAgfqddDFDLL-----SQPVF-VGLPVpgtefkicdFETGELLPLGAEGEI 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 334 VVKGPNVTGGYFNREDATRETIQNGWLHTGDLGYLDEEGFLYVLDRRSDLIISGGENIYPAQIEEVLLSHPMVAEAGVVG 413
Cdd:PRK06178 418 VVRTPSLLKGYWNKPEATAEALRDGWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVG 497
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446371684 414 MTDDKWGQVPAAFVV-KNG-EVTEEEIIHFCEEKLAKYKVPKKAcFLEELPRNASKKLLRRELRQLVEE 480
Cdd:PRK06178 498 RPDPDKGQVPVAFVQlKPGaDLTAAALQAWCRENMAVYKVPEIR-IVDALPMTATGKVRKQDLQALAEE 565
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
15-476 |
1.37e-63 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 215.30 E-value: 1.37e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 15 TPDRTAI------EIEEEKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSR 88
Cdd:PRK13295 37 CPDKTAVtavrlgTGAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 89 EELLWQMDDAEVVCLVTDQQFDANDVP---------------VY--------SFAEVMHGLKVEASIQEEFSL------- 138
Cdd:PRK13295 117 RELSFMLKHAESKVLVVPKTFRGFDHAamarrlrpelpalrhVVvvggdgadSFEALLITPAWEQEPDAPAILarlrpgp 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 139 EEAMTIIYTSGTTGKPKGVILTYGNHWASAVGSSLNLGLRDDDCWLACMPMFHVGG-LSLLMKNIMYGMRILLVPKYDAD 217
Cdd:PRK13295 197 DDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILMASPMAHQTGfMYGLMMPVMLGATAVLQDIWDPA 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 218 FIHKALQTRGVTIISVVSKMLTDLLERLGEETYP-SSLRCMLLGGGPAPKPLLETCVDK-GIPVYQTYGMTETSSQICTL 295
Cdd:PRK13295 277 RAAELIRTEGVTFTMASTPFLTDLTRAVKESGRPvSSLRTFLCAGAPIPGALVERARAAlGAKIVSAWGMTENGAVTLTK 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 296 SADYMLTKVGSAGKPLFQCQLRI-EKDGVVVPPLVEGEIVVKGPNVTGGYFNREDATReTIQNGWLHTGDLGYLDEEGFL 374
Cdd:PRK13295 357 LDDPDERASTTDGCPLPGVEVRVvDADGAPLPAGQIGRLQVRGCSNFGGYLKRPQLNG-TDADGWFDTGDLARIDADGYI 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 375 YVLDRRSDLIISGGENIYPAQIEEVLLSHPMVAEAGVVGMTDDKWGQVPAAFVV-KNGE-VTEEEIIHFCEE-KLAKYKV 451
Cdd:PRK13295 436 RISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVpRPGQsLDFEEMVEFLKAqKVAKQYI 515
|
490 500
....*....|....*....|....*....
gi 446371684 452 PKKACFLEELPRNASKKL----LRRELRQ 476
Cdd:PRK13295 516 PERLVVRDALPRTPSGKIqkfrLREMLRG 544
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
26-477 |
2.80e-63 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 215.09 E-value: 2.80e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 26 EKVTFLQLHEKVVSVCEHLTHV-GVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSREELLWQMDDAEVvCLV 104
Cdd:PLN02574 65 FSISYSELQPLVKSMAAGLYHVmGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSV-GLA 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 105 -----TDQQFDANDVPVYSFAEVMHglkvEASIQEEFSL-------------------EEAMTIIYTSGTTGKPKGVILT 160
Cdd:PLN02574 144 ftspeNVEKLSPLGVPVIGVPENYD----FDSKRIEFPKfyelikedfdfvpkpvikqDDVAAIMYSSGTTGASKGVVLT 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 161 YGNHWASA-----VGSSLNLGLRDDDCWLACMPMFHVGGLSLLMKNIM-YGMRILLVPKYDADFIHKALQTRGVTIISVV 234
Cdd:PLN02574 220 HRNLIAMVelfvrFEASQYEYPGSDNVYLAALPMFHIYGLSLFVVGLLsLGSTIVVMRRFDASDMVKVIDRFKVTHFPVV 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 235 SKMLTDLLeRLGEETYPSSLRCMLL---GGGPAPKPLLETCVdKGIP---VYQTYGMTEtSSQICTLSADY-MLTKVGSA 307
Cdd:PLN02574 300 PPILMALT-KKAKGVCGEVLKSLKQvscGAAPLSGKFIQDFV-QTLPhvdFIQGYGMTE-STAVGTRGFNTeKLSKYSSV 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 308 G--KPLFQCQLRIEKDGVVVPPLVEGEIVVKGPNVTGGYFNREDATRETIQN-GWLHTGDLGYLDEEGFLYVLDRRSDLI 384
Cdd:PLN02574 377 GllAPNMQAKVVDWSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKdGWLRTGDIAYFDEDGYLYIVDRLKEII 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 385 ISGGENIYPAQIEEVLLSHPMVAEAGVVGMTDDKWGQVPAAFVVKNGE--VTEEEIIHFCEEKLAKYKVPKKACFLEELP 462
Cdd:PLN02574 457 KYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQGstLSQEAVINYVAKQVAPYKKVRKVVFVQSIP 536
|
490
....*....|....*
gi 446371684 463 RNASKKLLRRELRQL 477
Cdd:PLN02574 537 KSPAGKILRRELKRS 551
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
16-474 |
6.83e-63 |
|
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: 210.85 E-value: 6.83e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 16 PDRTAIEIEEEKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSREELLWQM 95
Cdd:cd05930 1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 96 DDAEVVCLVTDqqfdANDvPVYsfaevmhglkveasiqeefsleeamtIIYTSGTTGKPKGVILTYGN-----HWASAVg 170
Cdd:cd05930 81 EDSGAKLVLTD----PDD-LAY--------------------------VIYTSGSTGKPKGVMVEHRGlvnllLWMQEA- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 171 sslnLGLRDDDCWLACMPM-FHVGGLSLLMKnIMYGMRILLVPK---YDADFIHKALQTRGVTIISVVSKMLTDLLERLG 246
Cdd:cd05930 129 ----YPLTPGDRVLQFTSFsFDVSVWEIFGA-LLAGATLVVLPEevrKDPEALADLLAEEGITVLHLTPSLLRLLLQELE 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 247 EETYPsSLRCMLLGGGPAPKPLLE--TCVDKGIPVYQTYGMTETS--SQICTLSADYMLTKVGSAGKPLFQCQLRI-EKD 321
Cdd:cd05930 204 LAALP-SLRLVLVGGEALPPDLVRrwRELLPGARLVNLYGPTEATvdATYYRVPPDDEEDGRVPIGRPIPNTRVYVlDEN 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 322 GVVVPPLVEGEIVVKGPNVTGGYFNREDATRETI------QNGWLH-TGDLGYLDEEGFLYVLDRRSDLI-ISGgeniY- 392
Cdd:cd05930 283 LRPVPPGVPGELYIGGAGLARGYLNRPELTAERFvpnpfgPGERMYrTGDLVRWLPDGNLEFLGRIDDQVkIRG----Yr 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 393 --PAQIEEVLLSHPMVAEAGVVGMTDDKWGQVPAAFVV--KNGEVTEEEIIHFCEEKLAKYKVPKKACFLEELPRNASKK 468
Cdd:cd05930 359 ieLGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVpdEGGELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGK 438
|
....*.
gi 446371684 469 LLRREL 474
Cdd:cd05930 439 VDRKAL 444
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
18-475 |
2.37e-62 |
|
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: 209.26 E-value: 2.37e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 18 RTAIEIEEEKVTFLQLHEKVVSVCEHLTHVGVKR-GQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSREELLWQMD 96
Cdd:cd05958 1 RTCLRSPEREWTYRDLLALANRIANVLVGELGIVpGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 97 DAEV-VCLVTDQQFDANDVPVYSFaevmhglkveasiqeefsleeamtiiyTSGTTGKPKGVILTYGNHWASAVGSSLN- 174
Cdd:cd05958 81 KARItVALCAHALTASDDICILAF---------------------------TSGTTGAPKATMHFHRDPLASADRYAVNv 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 175 LGLRDDDCWLACMPMFHVGGLSLLMKNIMY-GMRILLVPKYDADFIHKALQTRGVTIISVVSKMLTDLLErLGEETYP-- 251
Cdd:cd05958 134 LRLREDDRFVGSPPLAFTFGLGGVLLFPFGvGASGVLLEEATPDLLLSAIARYKPTVLFTAPTAYRAMLA-HPDAAGPdl 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 252 SSLRCMLLGGGPAPKPLLETCVDK-GIPVYQTYGMTETSSQIctLSADYMLTKVGSAGKPLFQCQLRI-EKDGVVVPPLV 329
Cdd:cd05958 213 SSLRKCVSAGEALPAALHRAWKEAtGIPIIDGIGSTEMFHIF--ISARPGDARPGATGKPVPGYEAKVvDDEGNPVPDGT 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 330 EGEIVVKGPnvTGGYFNREDATRETIQNGWLHTGDLGYLDEEGFLYVLDRRSDLIISGGENIYPAQIEEVLLSHPMVAEA 409
Cdd:cd05958 291 IGRLAVRGP--TGCRYLADKRQRTYVQGGWNITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAEC 368
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446371684 410 GVVGMTDDKWGQVPAAFVV-----KNGEVTEEEIIHFCEEKLAKYKVPKKACFLEELPRNASKKLLRRELR 475
Cdd:cd05958 369 AVVGHPDESRGVVVKAFVVlrpgvIPGPVLARELQDHAKAHIAPYKYPRAIEFVTELPRTATGKLQRFALR 439
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
24-471 |
3.48e-62 |
|
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: 209.61 E-value: 3.48e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 24 EEEKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSREELLWQMDDAEVVCL 103
Cdd:cd05914 4 GGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 104 VTDQQfdandvpvysfaevmhglkveasiqeefslEEAMTIIYTSGTTGKPKGVILTYGNHWASAVGSSLNLGLRDDDCW 183
Cdd:cd05914 84 FVSDE------------------------------DDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLLGKGDKI 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 184 LACMPMFHVGGLSL-LMKNIMYGMRILLVPKYDADFIhKALQTRGVTIISVVSKML-------TDLLERLG--------- 246
Cdd:cd05914 134 LSILPLHHIYPLTFtLLLPLLNGAHVVFLDKIPSAKI-IALAFAQVTPTLGVPVPLviekifkMDIIPKLTlkkfkfkla 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 247 ----------------EETYPSSLRCMLLGGGPAPKPLLETCVDKGIPVYQTYGMTETSSQICtlSADYMLTKVGSAGKP 310
Cdd:cd05914 213 kkinnrkirklafkkvHEAFGGNIKEFVIGGAKINPDVEEFLRTIGFPYTIGYGMTETAPIIS--YSPPNRIRLGSAGKV 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 311 LFQCQLRIEKDGvvvPPLVEGEIVVKGPNVTGGYFNREDATRETI-QNGWLHTGDLGYLDEEGFLYVLDRRSDLIISG-G 388
Cdd:cd05914 291 IDGVEVRIDSPD---PATGEGEIIVRGPNVMKGYYKNPEATAEAFdKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSsG 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 389 ENIYPAQIEEVLLSHPMVAEAgVVGMTDDK----------WGQVPAAFVVKNGEVTEEEIIHFCEEKLAKY-KVPKKACF 457
Cdd:cd05914 368 KNIYPEEIEAKINNMPFVLES-LVVVQEKKlvalayidpdFLDVKALKQRNIIDAIKWEVRDKVNQKVPNYkKISKVKIV 446
|
490
....*....|....
gi 446371684 458 LEELPRNASKKLLR 471
Cdd:cd05914 447 KEEFEKTPKGKIKR 460
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
10-475 |
4.56e-62 |
|
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: 208.47 E-value: 4.56e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 10 QRAFLTPDRTaieieeekVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSRE 89
Cdd:cd05919 1 KTAFYAADRS--------VTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 90 ELLWQMDDAEVVCLVTDQqfdandvpvysfaevmhglkveasiqeefslEEAMTIIYTSGTTGKPKGVILTYGNH--WAS 167
Cdd:cd05919 73 DYAYIARDCEARLVVTSA-------------------------------DDIAYLLYSSGTTGPPKGVMHAHRDPllFAD 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 168 AVGSSLnLGLRDDDCWLACMPMFHVGGL-SLLMKNIMYGMRILLVPKY-DADFIHKALQTRGVTIISVVSKMLTDLL-ER 244
Cdd:cd05919 122 AMAREA-LGLTPGDRVFSSAKMFFGYGLgNSLWFPLAVGASAVLNPGWpTAERVLATLARFRPTVLYGVPTFYANLLdSC 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 245 LGEETYPSSLRCMLLGGGPAPKPLLETCVDK-GIPVYQTYGMTETSSQ-ICTLSADYmltKVGSAGKPL--FQCQLRIEk 320
Cdd:cd05919 201 AGSPDALRSLRLCVSAGEALPRGLGERWMEHfGGPILDGIGATEVGHIfLSNRPGAW---RLGSTGRPVpgYEIRLVDE- 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 321 DGVVVPPLVEGEIVVKGPNVTGGYFNREDATRETIQNGWLHTGDLGYLDEEGFLYVLDRRSDLIISGGENIYPAQIEEVL 400
Cdd:cd05919 277 EGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLI 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 401 LSHPMVAEAGVVGMTDDKWGQVPAAFVV-----KNGEVTEEEIIHFCEEKLAKYKVPKKACFLEELPRNASKKLLRRELR 475
Cdd:cd05919 357 IQHPAVAEAAVVAVPESTGLSRLTAFVVlkspaAPQESLARDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKLR 436
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
16-475 |
1.17e-61 |
|
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: 209.15 E-value: 1.17e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 16 PDRTAIEIEEEKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSREELLWQM 95
Cdd:cd05959 18 GDKTAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 96 DDAEVVCLVTDQQFDANDVPVYSFAEVM---------HGLKVEASIQEEF------SLEEAMTI-------IYTSGTTGK 153
Cdd:cd05959 98 EDSRARVVVVSGELAPVLAAALTKSEHTlvvlivsggAGPEAGALLLAELvaaeaeQLKPAATHaddpafwLYSSGSTGR 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 154 PKGVILTYGNHWASAVGSSLN-LGLRDDDCWLACMPMFHVGGLSllmkNIMY-----GMRILLVPKY-DADFIHKALQTR 226
Cdd:cd05959 178 PKGVVHLHADIYWTAELYARNvLGIREDDVCFSAAKLFFAYGLG----NSLTfplsvGATTVLMPERpTPAAVFKRIRRY 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 227 GVTIISVVSKMLTDLL--ERLGEETyPSSLRCMLLGGGPAPKPLLETCVDK-GIPVYQTYGMTETSSQICTLSADYMltK 303
Cdd:cd05959 254 RPTVFFGVPTLYAAMLaaPNLPSRD-LSSLRLCVSAGEALPAEVGERWKARfGLDILDGIGSTEMLHIFLSNRPGRV--R 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 304 VGSAGKPL--FQCQLRiEKDGVVVPPLVEGEIVVKGPNVTGGYFNREDATRETIQNGWLHTGDLGYLDEEGFLYVLDRRS 381
Cdd:cd05959 331 YGTTGKPVpgYEVELR-DEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQGEWTRTGDKYVRDDDGFYTYAGRAD 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 382 DLIISGGENIYPAQIEEVLLSHPMVAEAGVVGMTDDKWGQVPAAFVV-----KNGEVTEEEIIHFCEEKLAKYKVPKKAC 456
Cdd:cd05959 410 DMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVlrpgyEDSEALEEELKEFVKDRLAPYKYPRWIV 489
|
490
....*....|....*....
gi 446371684 457 FLEELPRNASKKLLRRELR 475
Cdd:cd05959 490 FVDELPKTATGKIQRFKLR 508
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
17-476 |
1.57e-61 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 207.92 E-value: 1.57e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 17 DRTAIEIEEEKVTFLQLHEKVVSVCEHLThvGVKRgqkVAVLMKNGME-MITVIHALsYVGAVAVLLNTRLSREELLWQM 95
Cdd:PRK07787 15 IADAVRIGGRVLSRSDLAGAATAVAERVA--GARR---VAVLATPTLAtVLAVVGAL-IAGVPVVPVPPDSGVAERRHIL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 96 DDAEVVCLVTDQQFDAND---VPVYSFAEVMHGLkveasiqEEFSLEEAMTIIYTSGTTGKPKGVILTygnhwASAVGSS 172
Cdd:PRK07787 89 ADSGAQAWLGPAPDDPAGlphVPVRLHARSWHRY-------PEPDPDAPALIVYTSGTTGPPKGVVLS-----RRAIAAD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 173 LNlGLRD------DDCWLACMPMFHVGGLSL-LMKNIMYGMRILLVPKYDADFIHKALQTRGvTIISVVSKMLTDLLERL 245
Cdd:PRK07787 157 LD-ALAEawqwtaDDVLVHGLPLFHVHGLVLgVLGPLRIGNRFVHTGRPTPEAYAQALSEGG-TLYFGVPTVWSRIAADP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 246 GEETYPSSLRCMLLGGGPAPKPLLETCVD-KGIPVYQTYGMTETssqICTLS--ADYMlTKVGSAGKPLFQCQLRI-EKD 321
Cdd:PRK07787 235 EAARALRGARLLVSGSAALPVPVFDRLAAlTGHRPVERYGMTET---LITLStrADGE-RRPGWVGLPLAGVETRLvDED 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 322 GVVVPPLVE--GEIVVKGPNVTGGYFNREDATRETI-QNGWLHTGDLGYLDEEGFLYVLDRRS-DLIISGGENIYPAQIE 397
Cdd:PRK07787 311 GGPVPHDGEtvGELQVRGPTLFDGYLNRPDATAAAFtADGWFRTGDVAVVDPDGMHRIVGREStDLIKSGGYRIGAGEIE 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446371684 398 EVLLSHPMVAEAGVVGMTDDKWGQVPAAFVVKNGEVTEEEIIHFCEEKLAKYKVPKKACFLEELPRNASKKLLRRELRQ 476
Cdd:PRK07787 391 TALLGHPGVREAAVVGVPDDDLGQRIVAYVVGADDVAADELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLLS 469
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
16-475 |
1.61e-61 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 210.30 E-value: 1.61e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 16 PDRTAIEIEEEKVTFLQLHEKVVSVCEHLTH-VGVKRGQKVAVLMKN--------------GMEMITV---------IHA 71
Cdd:PRK08974 37 ADQPAFINMGEVMTFRKLEERSRAFAAYLQNgLGLKKGDRVALMMPNllqypialfgilraGMIVVNVnplytprelEHQ 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 72 LSYVGAVAVLLNTRLSR--EELLWQMDDAEVVCLVTDQQFDAND--------------VPVY------SFAEVMHGLKVE 129
Cdd:PRK08974 117 LNDSGAKAIVIVSNFAHtlEKVVFKTPVKHVILTRMGDQLSTAKgtlvnfvvkyikrlVPKYhlpdaiSFRSALHKGRRM 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 130 ASIQEEFSLEEAMTIIYTSGTTGKPKGVILTYGN-----HWASAVGSSLnlgLRDDDCW-LACMPMFHVGGLS---LLMk 200
Cdd:PRK08974 197 QYVKPELVPEDLAFLQYTGGTTGVAKGAMLTHRNmlanlEQAKAAYGPL---LHPGKELvVTALPLYHIFALTvncLLF- 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 201 nIMYGMRILLV--PKyDADFIHKALQTRGVTIISVVSKMLTDLL--ERLGEETYpSSLRCMLLGGGPAPKPLLETCVD-K 275
Cdd:PRK08974 273 -IELGGQNLLItnPR-DIPGFVKELKKYPFTAITGVNTLFNALLnnEEFQELDF-SSLKLSVGGGMAVQQAVAERWVKlT 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 276 GIPVYQTYGMTETSSQICtlSADYMLTKV-GSAGKPLFQCQLRIEKD-GVVVPPLVEGEIVVKGPNVTGGYFNREDATRE 353
Cdd:PRK08974 350 GQYLLEGYGLTECSPLVS--VNPYDLDYYsGSIGLPVPSTEIKLVDDdGNEVPPGEPGELWVKGPQVMLGYWQRPEATDE 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 354 TIQNGWLHTGDLGYLDEEGFLYVLDRRSDLIISGGENIYPAQIEEVLLSHPMVAEAGVVGMTDDKWGQVPAAFVVKNGE- 432
Cdd:PRK08974 428 VIKDGWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAVKIFVVKKDPs 507
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 446371684 433 VTEEEIIHFCEEKLAKYKVPKKACFLEELPRNASKKLLRRELR 475
Cdd:PRK08974 508 LTEEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELR 550
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
16-474 |
3.69e-61 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 208.31 E-value: 3.69e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 16 PDRTAIEIEEEKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSREELLWQM 95
Cdd:PRK13383 49 PGRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAAL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 96 DDAEVVCLVTDQQF--------DANDV--PVYSFAEVMHGL-KVEASiqeefsleeAMTIIYTSGTTGKPKGVilTYGNH 164
Cdd:PRK13383 129 RAHHISTVVADNEFaeriagadDAVAVidPATAGAEESGGRpAVAAP---------GRIVLLTSGTTGKPKGV--PRAPQ 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 165 WASAVGSSLNL----GLRDDDCWLACMPMFHVGGLSLLMKNIMYGMRILLVPKYDADF------IHKAlqtRGVTIISVV 234
Cdd:PRK13383 198 LRSAVGVWVTIldrtRLRTGSRISVAMPMFHGLGLGMLMLTIALGGTVLTHRHFDAEAalaqasLHRA---DAFTAVPVV 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 235 SKMLTDLLERLGEETYPSSLRCMLLGGGPAPKPLLETCVDK-GIPVYQTYGMTETSSQICTLSADyMLTKVGSAGKPLFQ 313
Cdd:PRK13383 275 LARILELPPRVRARNPLPQLRVVMSSGDRLDPTLGQRFMDTyGDILYNGYGSTEVGIGALATPAD-LRDAPETVGKPVAG 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 314 CQLRI-EKDGVVVPPLVEGEIVVKGPNVTGGYfnrEDATRETIQNGWLHTGDLGYLDEEGFLYVLDRRSDLIISGGENIY 392
Cdd:PRK13383 354 CPVRIlDRNNRPVGPRVTGRIFVGGELAGTRY---TDGGGKAVVDGMTSTGDMGYLDNAGRLFIVGREDDMIISGGENVY 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 393 PAQIEEVLLSHPMVAEAGVVGMTDDKWGQVPAAFVVKN--GEVTEEEIIHFCEEKLAKYKVPKKACFLEELPRNASKKLL 470
Cdd:PRK13383 431 PRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHpgSGVDAAQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVL 510
|
....
gi 446371684 471 RREL 474
Cdd:PRK13383 511 RKEL 514
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
48-475 |
4.78e-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: 341246 [Multi-domain] Cd Length: 457 Bit Score: 206.52 E-value: 4.78e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 48 GVKRGQKVAVLMKNGME----MITVIHALSYVGAVAVLLNTRLSREELLWQMDDAE---VVCLVTDQQFDANDVPVYSFA 120
Cdd:cd05922 14 GGVRGERVVLILPNRFTyielSFAVAYAGGRLGLVFVPLNPTLKESVLRYLVADAGgriVLADAGAADRLRDALPASPDP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 121 EVMhgLKVEASIQEEFSL-------EEAMTIIYTSGTTGKPKGVILTYGNHWASAVGSSLNLGLRDDDCWLACMPMFHVG 193
Cdd:cd05922 94 GTV--LDADGIRAARASApahevshEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADDRALTVLPLSYDY 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 194 GLSLLMKNIMYGMRILLVPKY--DADFIhKALQTRGVTIISVVSKmLTDLLERLG--EETYPSsLRCMLLGGGPAPKPLL 269
Cdd:cd05922 172 GLSVLNTHLLRGATLVLTNDGvlDDAFW-EDLREHGATGLAGVPS-TYAMLTRLGfdPAKLPS-LRYLTQAGGRLPQETI 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 270 ETCVDK--GIPVYQTYGMTETSSQICTLSADYMLTKVGSAGKPLFQCQLRIEK-DGVVVPPLVEGEIVVKGPNVTGGYFN 346
Cdd:cd05922 249 ARLRELlpGAQVYVMYGQTEATRRMTYLPPERILEKPGSIGLAIPGGEFEILDdDGTPTPPGEPGEIVHRGPNVMKGYWN 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 347 REDA-TRETIQNGWLHTGDLGYLDEEGFLYVLDRRSDLIISGGENIYPAQIEEVLLSHPMVAEAGVVGMtDDKWGQVPAA 425
Cdd:cd05922 329 DPPYrRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGL-PDPLGEKLAL 407
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 446371684 426 FVVKNGEVTEEEIIHFCEEKLAKYKVPKKACFLEELPRNASKKLLRRELR 475
Cdd:cd05922 408 FVTAPDKIDPKDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
29-475 |
1.33e-60 |
|
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: 204.66 E-value: 1.33e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 29 TFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSREELLWQMDDAEVVCLVTDQq 108
Cdd:cd05969 2 TFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTE- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 109 fdandvpvysfaevmhglkveaSIQEEFSLEEAMTIIYTSGTTGKPKGVILTYGNHWASAVGSSLNLGLRDDDC-WLACM 187
Cdd:cd05969 81 ----------------------ELYERTDPEDPTLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLDLHPDDIyWCTAD 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 188 PMFHVGGLSLLMKNIMYGMRILLVP-KYDADFIHKALQTRGVTIISVVSKMLTdLLERLGEE---TYP-SSLRCMLLGGG 262
Cdd:cd05969 139 PGWVTGTVYGIWAPWLNGVTNVVYEgRFDAESWYGIIERVKVTVWYTAPTAIR-MLMKEGDElarKYDlSSLRFIHSVGE 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 263 PAPKPLLETCVDK-GIPVYQTYGMTETSSQictLSADY--MLTKVGSAGKPLFQCQ-LRIEKDGVVVPPLVEGEIVVKG- 337
Cdd:cd05969 218 PLNPEAIRWGMEVfGVPIHDTWWQTETGSI---MIANYpcMPIKPGSMGKPLPGVKaAVVDENGNELPPGTKGILALKPg 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 338 -PNVTGGYFNREDATRETIQNGWLHTGDLGYLDEEGFLYVLDRRSDLIISGGENIYPAQIEEVLLSHPMVAEAGVVGMTD 416
Cdd:cd05969 295 wPSMFRGIWNDEERYKNSFIDGWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPD 374
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446371684 417 DKWGQVPAAFVVKN-----GEVTEEEIIHFCEEKLAKYKVPKKACFLEELPRNASKKLLRRELR 475
Cdd:cd05969 375 PLRGEIIKAFISLKegfepSDELKEEIINFVRQKLGAHVAPREIEFVDNLPKTRSGKIMRRVLK 438
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
7-481 |
2.49e-60 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 207.56 E-value: 2.49e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 7 WLKQRAFLTPDRTAIEIEEEKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRL 86
Cdd:PLN03102 19 FLKRASECYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 87 SREELLWQMDDAEVVCLVTDQQFDA-------------------------NDVPVYSFAE-------VMHGLKVEASIQE 134
Cdd:PLN03102 99 DATSIAAILRHAKPKILFVDRSFEPlarevlhllssedsnlnlpvifiheIDFPKRPSSEeldyeclIQRGEPTPSLVAR 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 135 EFSLE---EAMTIIYTSGTTGKPKGVILTYGNHWASAVGSSLNLGLRDDDCWLACMPMFHVGGLSLLMKNIMYGMRILLV 211
Cdd:PLN03102 179 MFRIQdehDPISLNYTSGTTADPKGVVISHRGAYLSTLSAIIGWEMGTCPVYLWTLPMFHCNGWTFTWGTAARGGTSVCM 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 212 PKYDADFIHKALQTRGVTIISVVSKMLTDLLE--RLgEETYPSSLRCMLLGGGPAPKPLLETCVDKGIPVYQTYGMTETS 289
Cdd:PLN03102 259 RHVTAPEIYKNIEMHNVTHMCCVPTVFNILLKgnSL-DLSPRSGPVHVLTGGSPPPAALVKKVQRLGFQVMHAYGLTEAT 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 290 SQI--CTLSADY--------------------MLTKVGSAGKplfQCQLRIEKDGVVVpplveGEIVVKGPNVTGGYFNR 347
Cdd:PLN03102 338 GPVlfCEWQDEWnrlpenqqmelkarqgvsilGLADVDVKNK---ETQESVPRDGKTM-----GEIVIKGSSIMKGYLKN 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 348 EDATRETIQNGWLHTGDLGYLDEEGFLYVLDRRSDLIISGGENIYPAQIEEVLLSHPMVAEAGVVGMTDDKWGQVPAAFV 427
Cdd:PLN03102 410 PKATSEAFKHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFV 489
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446371684 428 V-KNGEVT-----------EEEIIHFCEEKLAKYKVPKKACFLEELPRNASKKLLRRELRQLVEEM 481
Cdd:PLN03102 490 VlEKGETTkedrvdklvtrERDLIEYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKLRDIAKGL 555
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
29-477 |
7.36e-60 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 205.33 E-value: 7.36e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 29 TFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSREELLWQMDDAE--VVC---- 102
Cdd:PRK07008 41 TYRDCERRAKQLAQALAALGVEPGDRVGTLAWNGYRHLEAYYGVSGSGAVCHTINPRLFPEQIAYIVNHAEdrYVLfdlt 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 103 -------------------LVTDQ-QFDANDVPVYSFAEVMHGlkvEASIQEEFSLEE--AMTIIYTSGTTGKPKGVILT 160
Cdd:PRK07008 121 flplvdalapqcpnvkgwvAMTDAaHLPAGSTPLLCYETLVGA---QDGDYDWPRFDEnqASSLCYTSGTTGNPKGALYS 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 161 YGNHWASAVGSSL--NLGLRDDDCWLACMPMFHVGGLSLLMKNIMYGMRILLV-PKYDADFIHKALQTRGVTIISVVSKM 237
Cdd:PRK07008 198 HRSTVLHAYGAALpdAMGLSARDAVLPVVPMFHVNAWGLPYSAPLTGAKLVLPgPDLDGKSLYELIEAERVTFSAGVPTV 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 238 LTDLLERLGEETYP-SSLRCMLLGGGPAPKPLLETCVDK-GIPVYQTYGMTETS--SQICTLSADYM----------LTK 303
Cdd:PRK07008 278 WLGLLNHMREAGLRfSTLRRTVIGGSACPPAMIRTFEDEyGVEVIHAWGMTEMSplGTLCKLKWKHSqlpldeqrklLEK 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 304 vgsAGKPLFQCQLRI-EKDGVVVP--PLVEGEIVVKGPNVTGGYFNREDATretIQNGWLHTGDLGYLDEEGFLYVLDRR 380
Cdd:PRK07008 358 ---QGRVIYGVDMKIvGDDGRELPwdGKAFGDLQVRGPWVIDRYFRGDASP---LVDGWFPTGDVATIDADGFMQITDRS 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 381 SDLIISGGENIYPAQIEEVLLSHPMVAEAGVVGMTDDKWGQVPAAFVVK--NGEVTEEEIIHFCEEKLAKYKVPKKACFL 458
Cdd:PRK07008 432 KDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLVVVKrpGAEVTREELLAFYEGKVAKWWIPDDVVFV 511
|
490
....*....|....*....
gi 446371684 459 EELPRNASKKLLRRELRQL 477
Cdd:PRK07008 512 DAIPHTATGKLQKLKLREQ 530
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
16-477 |
3.28e-59 |
|
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: 203.53 E-value: 3.28e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 16 PDRTAI--EIEEEKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSREELLW 93
Cdd:cd17642 31 PGTIAFtdAHTGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDH 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 94 QMDDAE-VVCLVTDQQFD-----ANDVPV-------------------YSFAE--VMHGLKVEASIQEEFSLEEAMT-II 145
Cdd:cd17642 111 SLNISKpTIVFCSKKGLQkvlnvQKKLKIiktiiildskedykgyqclYTFITqnLPPGFNEYDFKPPSFDRDEQVAlIM 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 146 YTSGTTGKPKGVILTYGN---HWASAVGSSLNLGLRDDDCWLACMPMFHVGGLSLLMKNIMYGMRILLVPKYDADFIHKA 222
Cdd:cd17642 191 NSSGSTGLPKGVQLTHKNivaRFSHARDPIFGNQIIPDTAILTVIPFHHGFGMFTTLGYLICGFRVVLMYKFEEELFLRS 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 223 LQTRGVTIISVVSKMLTDLLERLGEETYP-SSLRCMLLGGGPAPKPLLETCVDK-GIP-VYQTYGMTETSSQI-CTLSAD 298
Cdd:cd17642 271 LQDYKVQSALLVPTLFAFFAKSTLVDKYDlSNLHEIASGGAPLSKEVGEAVAKRfKLPgIRQGYGLTETTSAIlITPEGD 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 299 ymlTKVGSAGK--PLFQCQLRIEKDGVVVPPLVEGEIVVKGPNVTGGYFNREDATRETI-QNGWLHTGDLGYLDEEGFLY 375
Cdd:cd17642 351 ---DKPGAVGKvvPFFYAKVVDLDTGKTLGPNERGELCVKGPMIMKGYVNNPEATKALIdKDGWLHSGDIAYYDEDGHFF 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 376 VLDRRSDLIISGGENIYPAQIEEVLLSHPMVAEAGVVGMTDDKWGQVPAAFVVK--NGEVTEEEIIHFCEEKLAKYKVPK 453
Cdd:cd17642 428 IVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVVLeaGKTMTEKEVMDYVASQVSTAKRLR 507
|
490 500
....*....|....*....|....*
gi 446371684 454 KAC-FLEELPRNASKKLLRRELRQL 477
Cdd:cd17642 508 GGVkFVDEVPKGLTGKIDRRKIREI 532
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
27-476 |
6.10e-59 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 203.06 E-value: 6.10e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 27 KVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSREELLWQMDDAEVVCLVTD 106
Cdd:PRK06018 39 RTTYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVITD 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 107 QQF------DANDVP------VYSFAEVMHGLKVEASIQEEFSLEE--------------AMTIIYTSGTTGKPKGVILT 160
Cdd:PRK06018 119 LTFvpilekIADKLPsveryvVLTDAAHMPQTTLKNAVAYEEWIAEadgdfawktfdentAAGMCYTSGTTGDPKGVLYS 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 161 YGNHWASAVGSSLN--LGLRDDDCWLACMPMFHVGGLSLLMKNIMYGMRILLV-PKYDADFIHKALQTRGVTIISVVSKM 237
Cdd:PRK06018 199 HRSNVLHALMANNGdaLGTSAADTMLPVVPLFHANSWGIAFSAPSMGTKLVMPgAKLDGASVYELLDTEKVTFTAGVPTV 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 238 LTDLLERLGEE--TYPSsLRCMLLGGGPAPKPLLETCVDKGIPVYQTYGMTETS---------SQICTLSADYMLTKVGS 306
Cdd:PRK06018 279 WLMLLQYMEKEglKLPH-LKMVVCGGSAMPRSMIKAFEDMGVEVRHAWGMTEMSplgtlaalkPPFSKLPGDARLDVLQK 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 307 AGKPLFQCQLRI-EKDGVVVP--PLVEGEIVVKGPNVTGGYFNREDATREtiQNGWLHTGDLGYLDEEGFLYVLDRRSDL 383
Cdd:PRK06018 358 QGYPPFGVEMKItDDAGKELPwdGKTFGRLKVRGPAVAAAYYRVDGEILD--DDGFFDTGDVATIDAYGYMRITDRSKDV 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 384 IISGGENIYPAQIEEVLLSHPMVAEAGVVGMTDDKWGQVPAAFVV-KNGE-VTEEEIIHFCEEKLAKYKVPKKACFLEEL 461
Cdd:PRK06018 436 IKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQlKPGEtATREEILKYMDGKIAKWWMPDDVAFVDAI 515
|
490
....*....|....*
gi 446371684 462 PRNASKKLLRRELRQ 476
Cdd:PRK06018 516 PHTATGKILKTALRE 530
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
137-480 |
1.54e-58 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 199.45 E-value: 1.54e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 137 SLEEAMTIIYTSGTTGKPKGVILTYGNHWASAVG--SSLNLGLRDDDCWLacmPMFHVGGLSLLMKNIMYGMRILLVPky 214
Cdd:PRK07445 118 NLETGWIMIPTGGSSGQIRFAIHTWETLTASVQGfqRYFQLQQVNSFCVL---PLYHVSGLMQFMRSFLTGGKLVILP-- 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 215 dadfiHKALQTRGVT-------IISVVSKMLTDLLERLGEetYPSSLRCMLLGGGPAPKPLLETCVDKGIPVYQTYGMTE 287
Cdd:PRK07445 193 -----YKRLKSGQELppnpsdfFLSLVPTQLQRLLQLRPQ--WLAQFRTILLGGAPAWPSLLEQARQLQLRLAPTYGMTE 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 288 TSSQICTLSADYMLTKVGSAGKPLFQCQLRIEKDGVvvpplveGEIVVKGPNVTGGYF-NREDATREtiqngwLHTGDLG 366
Cdd:PRK07445 266 TASQIATLKPDDFLAGNNSSGQVLPHAQITIPANQT-------GNITIQAQSLALGYYpQILDSQGI------FETDDLG 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 367 YLDEEGFLYVLDRRSDLIISGGENIYPAQIEEVLLSHPMVAEAGVVGMTDDKWGQVPAAFVV-KNGEVTEEEIIHFCEEK 445
Cdd:PRK07445 333 YLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYVpKDPSISLEELKTAIKDQ 412
|
330 340 350
....*....|....*....|....*....|....*
gi 446371684 446 LAKYKVPKKACFLEELPRNASKKLLRRELRQLVEE 480
Cdd:PRK07445 413 LSPFKQPKHWIPVPQLPRNPQGKINRQQLQQIAVQ 447
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
5-481 |
5.84e-58 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 200.84 E-value: 5.84e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 5 PNWLKQR-AFLTPDRTAIEIEEEKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLN 83
Cdd:PLN02479 22 PLWFLERaAVVHPTRKSVVHGSVRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 84 TRLSREELLWQMDDAEVVCLVTDQQFdandvpvYSFAE-------------------------------VMHGLKVEASI 132
Cdd:PLN02479 102 IRLNAPTIAFLLEHSKSEVVMVDQEF-------FTLAEealkilaekkkssfkppllivigdptcdpksLQYALGKGAIE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 133 QEEFsLEE---------------AMTIIYTSGTTGKPKGVILTYGNHWASAVGSSLNLGLRDDDCWLACMPMFHVGGLSL 197
Cdd:PLN02479 175 YEKF-LETgdpefawkppadewqSIALGYTSGTTASPKGVVLHHRGAYLMALSNALIWGMNEGAVYLWTLPMFHCNGWCF 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 198 LMK-NIMYGMRILLvPKYDADFIHKALQTRGVTIISVVSKMLTDLLERLGEETY---PSSLRCMLLGGGPAPKpLLETCV 273
Cdd:PLN02479 254 TWTlAALCGTNICL-RQVTAKAIYSAIANYGVTHFCAAPVVLNTIVNAPKSETIlplPRVVHVMTAGAAPPPS-VLFAMS 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 274 DKGIPVYQTYGMTET--SSQICT---------------LSADYMLTKVGSAGKPLFQcqlriEKDGVVVPP--LVEGEIV 334
Cdd:PLN02479 332 EKGFRVTHTYGLSETygPSTVCAwkpewdslppeeqarLNARQGVRYIGLEGLDVVD-----TKTMKPVPAdgKTMGEIV 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 335 VKGPNVTGGYFNREDATRETIQNGWLHTGDLGYLDEEGFLYVLDRRSDLIISGGENIYPAQIEEVLLSHPMVAEAGVVGM 414
Cdd:PLN02479 407 MRGNMVMKGYLKNPKANEEAFANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVAR 486
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446371684 415 TDDKWGQVPAAFVVKNGEV-------TEEEIIHFCEEKLAKYKVPKKACFlEELPRNASKKLLRRELRQLVEEM 481
Cdd:PLN02479 487 PDERWGESPCAFVTLKPGVdksdeaaLAEDIMKFCRERLPAYWVPKSVVF-GPLPKTATGKIQKHVLRAKAKEM 559
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
146-477 |
7.24e-58 |
|
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: 195.39 E-value: 7.24e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 146 YTSGTTGKPKGVILTYGNHWASAVGSSLNLGLRDDDCWLACMPMFHVGG-LSLLMKNIMYGMRILLV-------PKYDAD 217
Cdd:cd05944 9 HTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFHVNGsVVTLLTPLASGAHVVLAgpagyrnPGLFDN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 218 FiHKALQTRGVTIISVVSKMLTDLLERLGEETYpSSLRCMLLGGGPAPKPLLETCVDK-GIPVYQTYGMTETSsqiCTLS 296
Cdd:cd05944 89 F-WKLVERYRITSLSTVPTVYAALLQVPVNADI-SSLRFAMSGAAPLPVELRARFEDAtGLPVVEGYGLTEAT---CLVA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 297 ADYMLT--KVGSAGKPLFQCQLRI-EKDGV------VVPPLVeGEIVVKGPNVTGGYFNREDATRETIQNGWLHTGDLGY 367
Cdd:cd05944 164 VNPPDGpkRPGSVGLRLPYARVRIkVLDGVgrllrdCAPDEV-GEICVAGPGVFGGYLYTEGNKNAFVADGWLNTGDLGR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 368 LDEEGFLYVLDRRSDLIISGGENIYPAQIEEVLLSHPMVAEAGVVGMTDDKWGQVPAAFV--VKNGEVTEEEIIHFCEEK 445
Cdd:cd05944 243 LDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVqlKPGAVVEEEELLAWARDH 322
|
330 340 350
....*....|....*....|....*....|...
gi 446371684 446 LA-KYKVPKKACFLEELPRNASKKLLRRELRQL 477
Cdd:cd05944 323 VPeRAAVPKHIEVLEELPVTAVGKVFKPALRAD 355
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
16-475 |
7.03e-57 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 197.55 E-value: 7.03e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 16 PDRTAIEIEEEKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSREELLWQM 95
Cdd:PRK07059 37 ADRPAFICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVNPLYTPRELEHQL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 96 DDAEVVCLV-------TDQQFDAN----DVPVYSFAEvMHGLK--------------VEA-SIQEEFSLEEAMT------ 143
Cdd:PRK07059 117 KDSGAEAIVvlenfatTVQQVLAKtavkHVVVASMGD-LLGFKghivnfvvrrvkkmVPAwSLPGHVRFNDALAegarqt 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 144 -------------IIYTSGTTGKPKGVILTYGNHWASAVGSS------LNLGLRDDDCWLAC-MPMFHVGGLSLlmkNIM 203
Cdd:PRK07059 196 fkpvklgpddvafLQYTGGTTGVSKGATLLHRNIVANVLQMEawlqpaFEKKPRPDQLNFVCaLPLYHIFALTV---CGL 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 204 YGMRI----LLV--PKYDADFIhKALQTRGVTIISVVSKMLTDLLERLGEETYP-SSLRcMLLGGGPA-PKPLLETCVDK 275
Cdd:PRK07059 273 LGMRTggrnILIpnPRDIPGFI-KELKKYQVHIFPAVNTLYNALLNNPDFDKLDfSKLI-VANGGGMAvQRPVAERWLEM 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 276 -GIPVYQTYGMTETSSQIC---TLSADYmltkVGSAGKPLFQCQLRI-EKDGVVVPPLVEGEIVVKGPNVTGGYFNREDA 350
Cdd:PRK07059 351 tGCPITEGYGLSETSPVATcnpVDATEF----SGTIGLPLPSTEVSIrDDDGNDLPLGEPGEICIRGPQVMAGYWNRPDE 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 351 TRETI-QNGWLHTGDLGYLDEEGFLYVLDRRSDLIISGGENIYPAQIEEVLLSHPMVAEAGVVGMTDDKWGQVPAAFVV- 428
Cdd:PRK07059 427 TAKVMtADGFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGEAVKLFVVk 506
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 446371684 429 KNGEVTEEEIIHFCEEKLAKYKVPKKACFLEELPRNASKKLLRRELR 475
Cdd:PRK07059 507 KDPALTEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRRELR 553
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
144-466 |
4.21e-56 |
|
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: 189.82 E-value: 4.21e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 144 IIYTSGTTGKPKGVILTYGNHWASAVGSSLNLGLRDDDCWLACMPMFHVGGLSLLMKNIMYGMRILLVPKYDADFIHKAL 223
Cdd:cd17636 5 AIYTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTVFLNSGPLFHIGTLMFTLATFHAGGTNVFVRRVDAEEVLELI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 224 QTRGVTIISVVSKMLTDLLERLGEETYP-SSLRcmllggGPAPKPLLETCVDKGIPVYQT----YGMTETSSQICTlsAD 298
Cdd:cd17636 85 EAERCTHAFLLPPTIDQIVELNADGLYDlSSLR------SSPAAPEWNDMATVDTSPWGRkpggYGQTEVMGLATF--AA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 299 YMLTKVGSAGKPLFQCQLRI-EKDGVVVPPLVEGEIVVKGPNVTGGYFNREDATRETIQNGWLHTGDLGYLDEEGFLYVL 377
Cdd:cd17636 157 LGGGAIGGAGRPSPLVQVRIlDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRTRGGWHHTNDLGRREPDGSLSFV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 378 DRRSDLIISGGENIYPAQIEEVLLSHPMVAEAGVVGMTDDKWGQ-VPAAFVVKNG-EVTEEEIIHFCEEKLAKYKVPKKA 455
Cdd:cd17636 237 GPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQsVKAIVVLKPGaSVTEAELIEHCRARIASYKKPKSV 316
|
330
....*....|.
gi 446371684 456 CFLEELPRNAS 466
Cdd:cd17636 317 EFADALPRTAG 327
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
16-468 |
1.24e-55 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 193.95 E-value: 1.24e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 16 PDRTAIEIEEEKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGME-MITVIHALSyVGAVAVLLNTRLSREELLWQ 94
Cdd:PRK07798 17 PDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEyVEAMLGAFK-ARAVPVNVNYRYVEDELRYL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 95 MDDAEVVCLVTDQQFDAndvpvySFAEVMHGL-KVEASIQ------EEF-----SLEEAMT-----------------II 145
Cdd:PRK07798 96 LDDSDAVALVYEREFAP------RVAEVLPRLpKLRTLVVvedgsgNDLlpgavDYEDALAagsperdfgerspddlyLL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 146 YTSGTTGKPKGVILTYGNHW-ASAVGSSLNLG--LRDDD------------CWLACMPMFHVGGLSLLMKNIMYGMRILL 210
Cdd:PRK07798 170 YTGGTTGMPKGVMWRQEDIFrVLLGGRDFATGepIEDEEelakraaagpgmRRFPAPPLMHGAGQWAAFAALFSGQTVVL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 211 VP--KYDADFIHKALQTRGVTIISVVSK-MLTDLLERL--GEETYPSSLRCMLLGGGP----APKPLLEtcVDKGIPVYQ 281
Cdd:PRK07798 250 LPdvRFDADEVWRTIEREKVNVITIVGDaMARPLLDALeaRGPYDLSSLFAIASGGALfspsVKEALLE--LLPNVVLTD 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 282 TYGMTETSSQICTLSADymltKVGSAGKPLFQ----CQLRIEKDGVVVPPLVEGEIVVKGPNVTGGYFNREDATRETIQ- 356
Cdd:PRK07798 328 SIGSSETGFGGSGTVAK----GAVHTGGPRFTigprTVVLDEDGNPVEPGSGEIGWIARRGHIPLGYYKDPEKTAETFPt 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 357 -NG--WLHTGDLGYLDEEGFLYVLDRRSDLIISGGENIYPAQIEEVLLSHPMVAEAGVVGMTDDKWGQVPAAFVVKNG-- 431
Cdd:PRK07798 404 iDGvrYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVPDERWGQEVVAVVQLREga 483
|
490 500 510
....*....|....*....|....*....|....*..
gi 446371684 432 EVTEEEIIHFCEEKLAKYKVPKKACFLEELPRNASKK 468
Cdd:PRK07798 484 RPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
15-474 |
5.21e-54 |
|
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an AMP-binding domain (pfam00501) associated with acyl CoA-ligases. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present next to a decarboxylase enzyme. A number of sequences from Burkholderia species also hit this model, but the genomic context is obviously different. The hypothesis of a constant substrate for this family is only strong where the exosortase context is present.
Pssm-ID: 211788 [Multi-domain] Cd Length: 517 Bit Score: 189.22 E-value: 5.21e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 15 TPDRTAIEIEEEKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSREELLWQ 94
Cdd:TIGR03098 13 LPDATALVHHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLKAEQVAHI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 95 MDDAEVVCLVTD-QQFDANDVPVYSFAEVMHGLKVEASIQ--------EEFSLEEAMT-----------------IIYTS 148
Cdd:TIGR03098 93 LADCNVRLLVTSsERLDLLHPALPGCHDLRTLIIVGDPAHaseghpgeEPASWPKLLAlgdadpphpvidsdmaaILYTS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 149 GTTGKPKGVILTYGNHWASAVGSSLNLGLRDDDCWLACMPMFHVGGLSLLMKNIMYGMRIL----LVPKydaDFIhKALQ 224
Cdd:TIGR03098 173 GSTGRPKGVVLSHRNLVAGAQSVATYLENRPDDRLLAVLPLSFDYGFNQLTTAFYVGATVVlhdyLLPR---DVL-KALE 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 225 TRGVTIISVVSKMLTDLLERLGEETYPSSLRCMLLGGGPAPKPLLeTCVDKGIP---VYQTYGMTEtSSQICTLSADYML 301
Cdd:TIGR03098 249 KHGITGLAAVPPLWAQLAQLDWPESAAPSLRYLTNSGGAMPRATL-SRLRSFLPnarLFLMYGLTE-AFRSTYLPPEEVD 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 302 TKVGSAGKPLFQCQ-LRIEKDGVVVPPLVEGEIVVKGPNVTGGYFNREDATRE-----TIQNGWLH-------TGDLGYL 368
Cdd:TIGR03098 327 RRPDSIGKAIPNAEvLVLREDGSECAPGEEGELVHRGALVAMGYWNDPEKTAErfrplPPFPGELHlpelavwSGDTVRR 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 369 DEEGFLYVLDRRSDLIISGGENIYPAQIEEVLLSHPMVAEAGVVGMTDDKWGQVPAAFVVKNGEVTE--EEIIHFCEEKL 446
Cdd:TIGR03098 407 DEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAFGVPDPTLGQAIVLVVTPPGGEELdrAALLAECRARL 486
|
490 500
....*....|....*....|....*...
gi 446371684 447 AKYKVPKKACFLEELPRNASKKLLRREL 474
Cdd:TIGR03098 487 PNYMVPALIHVRQALPRNANGKIDRKAL 514
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
3-476 |
8.58e-54 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 189.42 E-value: 8.58e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 3 TMPNWLKQRAFLTPDRTAI--EIEEEKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAV 80
Cdd:PLN02330 29 TLPDFVLQDAELYADKVAFveAVTGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 81 LLNTRLSREELLWQMDDAEVVCLVTDqqfDAN-------DVPVYSFAEVMHGLKV-------------EASIQEEFSLEE 140
Cdd:PLN02330 109 GANPTALESEIKKQAEAAGAKLIVTN---DTNygkvkglGLPVIVLGEEKIEGAVnwkelleaadragDTSDNEEILQTD 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 141 AMTIIYTSGTTGKPKGVILTYGNHWASAVGSSLNLG--LRDDDCWLACMPMFHVGGLSLL----MKNimyGMRILLVPKY 214
Cdd:PLN02330 186 LCALPFSSGTTGISKGVMLTHRNLVANLCSSLFSVGpeMIGQVVTLGLIPFFHIYGITGIccatLRN---KGKVVVMSRF 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 215 DADFIHKALQTRGVTIISVVSKMLTDLLERLGEETYPSS---LRCMLLGGGPAPKPLLETCVDK--GIPVYQTYGMTETS 289
Cdd:PLN02330 263 ELRTFLNALITQEVSFAPIVPPIILNLVKNPIVEEFDLSklkLQAIMTAAAPLAPELLTAFEAKfpGVQVQEAYGLTEHS 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 290 SQICTL---SADYMLTKVGSAGKPLFQCQLR-IEKD-GVVVPPLVEGEIVVKGPNVTGGYFNREDATRETI-QNGWLHTG 363
Cdd:PLN02330 343 CITLTHgdpEKGHGIAKKNSVGFILPNLEVKfIDPDtGRSLPKNTPGELCVRSQCVMQGYYNNKEETDRTIdEDGWLHTG 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 364 DLGYLDEEGFLYVLDRRSDLIISGGENIYPAQIEEVLLSHPMVAEAGVVGMTDDKWGQVPAAFVVKNGEVT--EEEIIHF 441
Cdd:PLN02330 423 DIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVVINPKAKesEEDILNF 502
|
490 500 510
....*....|....*....|....*....|....*
gi 446371684 442 CEEKLAKYKVPKKACFLEELPRNASKKLLRRELRQ 476
Cdd:PLN02330 503 VAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLKE 537
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
12-481 |
1.64e-53 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 188.41 E-value: 1.64e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 12 AFLTPDRTAIEIEEEKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSREEL 91
Cdd:PRK06164 20 ARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 92 --------------------------LWQMDDAEVVCL----VTDQQFDANDVPVYSFAEVMHGLKVEASIQ---EEFSL 138
Cdd:PRK06164 100 ahilgrgrarwlvvwpgfkgidfaaiLAAVPPDALPPLraiaVVDDAADATPAPAPGARVQLFALPDPAPPAaagERAAD 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 139 EEAMTIIYT-SGTTGKPKGVILTYGNHWASAVGSSLNLGLRDDDCWLACMPMFHVGGLSLLMKNIMYGMRILLVPKYDAD 217
Cdd:PRK06164 180 PDAGALLFTtSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFGFSTLLGALAGGAPLVCEPVFDAA 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 218 FIHKALQTRGVTIISVVSKMLTDLLERLGEET-YPSSLRCMLLGGGPAPKPLLETCVDKGIPVYQTYGMTETSS--QICT 294
Cdd:PRK06164 260 RTARALRRHRVTHTFGNDEMLRRILDTAGERAdFPSARLFGFASFAPALGELAALARARGVPLTGLYGSSEVQAlvALQP 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 295 LSADYMLTKVGsAGKPLF-QCQLRIE--KDGVVVPPLVEGEIVVKGPNVTGGYFNREDATRETIQ-NGWLHTGDLGYLDE 370
Cdd:PRK06164 340 ATDPVSVRIEG-GGRPASpEARVRARdpQDGALLPDGESGEIEIRAPSLMRGYLDNPDATARALTdDGYFRTGDLGYTRG 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 371 EG-FLYVLdRRSDLIISGGENIYPAQIEEVLLSHPMVAEAGVVGMTDDkwGQ-VPAAFVV-KNGEVT-EEEIIHFCEEKL 446
Cdd:PRK06164 419 DGqFVYQT-RMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGATRD--GKtVPVAFVIpTDGASPdEAGLMAACREAL 495
|
490 500 510
....*....|....*....|....*....|....*...
gi 446371684 447 AKYKVPKKACFLEELPRNASK---KLLRRELRQLVEEM 481
Cdd:PRK06164 496 AGFKVPARVQVVEAFPVTESAngaKIQKHRLREMAQAR 533
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
16-477 |
2.05e-52 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 185.09 E-value: 2.05e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 16 PDRTAIEIEEEK--VTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSREELL- 92
Cdd:PRK05852 30 PEAPALVVTADRiaISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRv 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 93 -WQMDDAEVVCLVTDQQFD----------------ANDVPVYSFAEVMHGLKVE----ASIQEEFSLEEAMtIIYTSGTT 151
Cdd:PRK05852 110 rSQAAGARVVLIDADGPHDraepttrwwpltvnvgGDSGPSGGTLSVHLDAATEptpaTSTPEGLRPDDAM-IMFTGGTT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 152 GKPKGVILTYGNHWASAVGSSLNLGLRDDDCWLACMPMFHVGGL-SLLMKNIMYGMRILLvP---KYDADFIHKALQTRG 227
Cdd:PRK05852 189 GLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHGHGLiAALLATLASGGAVLL-PargRFSAHTFWDDIKAVG 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 228 VTIISVVSKMLTDLLERLGEETYPS---SLRCMLLGGGPAPKPLLETCVDK-GIPVYQTYGMTETSSQICTLSADYMLTK 303
Cdd:PRK05852 268 ATWYTAVPTIHQILLERAATEPSGRkpaALRFIRSCSAPLTAETAQALQTEfAAPVVCAFGMTEATHQVTTTQIEGIGQT 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 304 ---------VGSAGKPLFQCqlrIEKDGVVVPPLVEGEIVVKGPNVTGGYFNREDATRETIQNGWLHTGDLGYLDEEGFL 374
Cdd:PRK05852 348 enpvvstglVGRSTGAQIRI---VGSDGLPLPAGAVGEVWLRGTTVVRGYLGDPTITAANFTDGWLRTGDLGSLSAAGDL 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 375 YVLDRRSDLIISGGENIYPAQIEEVLLSHPMVAEAGVVGMTDDKWGQVPAAFVVKNG--EVTEEEIIHFCEEKLAKYKVP 452
Cdd:PRK05852 425 SIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIVPREsaPPTAEELVQFCRERLAAFEIP 504
|
490 500
....*....|....*....|....*
gi 446371684 453 KKACFLEELPRNASKKLLRRELRQL 477
Cdd:PRK05852 505 ASFQEASGLPHTAKGSLDRRAVAEQ 529
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
15-474 |
7.47e-52 |
|
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: 181.68 E-value: 7.47e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 15 TPDRTAIEIEEEKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSREELLWQ 94
Cdd:cd05945 4 NPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERIREI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 95 MDDAEVVCLVTDQqfdanDVPVYsfaevmhglkveasiqeefsleeamtIIYTSGTTGKPKGVILTYGNhWASAVGSSLN 174
Cdd:cd05945 84 LDAAKPALLIADG-----DDNAY--------------------------IIFTSGSTGRPKGVQISHDN-LVSFTNWMLS 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 175 LGLRDDDCWLACMPMFH----VGGL--SLLMknimyGMRILLVPKYDADF---IHKALQTRGVTI-ISVVS--KMLTdLL 242
Cdd:cd05945 132 DFPLGPGDVFLNQAPFSfdlsVMDLypALAS-----GATLVPVPRDATADpkqLFRFLAEHGITVwVSTPSfaAMCL-LS 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 243 ERLGEETYPSsLRCMLLGGGPAPKPLLETCVDK--GIPVYQTYGMTETSSQiCT-------LSADYMLTKVGSAgKPLFQ 313
Cdd:cd05945 206 PTFTPESLPS-LRHFLFCGEVLPHKTARALQQRfpDARIYNTYGPTEATVA-VTyievtpeVLDGYDRLPIGYA-KPGAK 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 314 CQLrIEKDGVVVPPLVEGEIVVKGPNVTGGYFNREDATRETI----QNGWLHTGDLGYLDEEGFLYVLDRRSDLIISGGE 389
Cdd:cd05945 283 LVI-LDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFfpdeGQRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGY 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 390 NIYPAQIEEVLLSHPMVAEAGVVGMTDDKWGQVPAAFVVKNGEVTEE---EIIHFCEEKLAKYKVPKKACFLEELPRNAS 466
Cdd:cd05945 362 RIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPGAEAGltkAIKAELAERLPPYMIPRRFVYLDELPLNAN 441
|
....*...
gi 446371684 467 KKLLRREL 474
Cdd:cd05945 442 GKIDRKAL 449
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
146-475 |
1.06e-50 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 181.23 E-value: 1.06e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 146 YTSGTTGKPKGVILTYGN---------HWASAVGSsLNLGlrdDDCWLACMPMFHVGGLS----LLMKniMYGMRILLVP 212
Cdd:PRK08751 215 YTGGTTGVAKGAMLTHRNlvanmqqahQWLAGTGK-LEEG---CEVVITALPLYHIFALTanglVFMK--IGGCNHLISN 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 213 KYDADFIHKALQTRGVTIISVVSKMLTDLLERLG-EETYPSSLRCMLLGGGPAPKPLLETCVD-KGIPVYQTYGMTETSS 290
Cdd:PRK08751 289 PRDMPGFVKELKKTRFTAFTGVNTLFNGLLNTPGfDQIDFSSLKMTLGGGMAVQRSVAERWKQvTGLTLVEAYGLTETSP 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 291 QICTLSADyMLTKVGSAGKPLFQCQLRIEKDGVVVPPLVE-GEIVVKGPNVTGGYFNREDATRETIQ-NGWLHTGDLGYL 368
Cdd:PRK08751 369 AACINPLT-LKEYNGSIGLPIPSTDACIKDDAGTVLAIGEiGELCIKGPQVMKGYWKRPEETAKVMDaDGWLHTGDIARM 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 369 DEEGFLYVLDRRSDLIISGGENIYPAQIEEVLLSHPMVAEAGVVGMTDDKWGQVPAAFVV-KNGEVTEEEIIHFCEEKLA 447
Cdd:PRK08751 448 DEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEIVKVVIVkKDPALTAEDVKAHARANLT 527
|
330 340
....*....|....*....|....*...
gi 446371684 448 KYKVPKKACFLEELPRNASKKLLRRELR 475
Cdd:PRK08751 528 GYKQPRIIEFRKELPKTNVGKILRRELR 555
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
137-477 |
1.67e-50 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 180.79 E-value: 1.67e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 137 SLEEAMTIIYTSGTTGKPKGVILTYGNHWASAVGSSLNLGLRDDD----------CWLACMPMFHVGGLSllmKNIMYGM 206
Cdd:PRK12492 205 GLDDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVRACLSQLGPDgqplmkegqeVMIAPLPLYHIYAFT---ANCMCMM 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 207 -----RILLV-PKYDADFIhKALQTRGVTIISVVSKMLTDLLERLGEETYP-SSLRCMLLGGGPAPKPLLETCVD-KGIP 278
Cdd:PRK12492 282 vsgnhNVLITnPRDIPGFI-KELGKWRFSALLGLNTLFVALMDHPGFKDLDfSALKLTNSGGTALVKATAERWEQlTGCT 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 279 VYQTYGMTETSSQICTlSADYMLTKVGSAGKPLFQCQLR-IEKDGVVVPPLVEGEIVVKGPNVTGGYFNREDATRETIQ- 356
Cdd:PRK12492 361 IVEGYGLTETSPVAST-NPYGELARLGTVGIPVPGTALKvIDDDGNELPLGERGELCIKGPQVMKGYWQQPEATAEALDa 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 357 NGWLHTGDLGYLDEEGFLYVLDRRSDLIISGGENIYPAQIEEVLLSHPMVAEAGVVGMTDDKWGQVPAAFVV-KNGEVTE 435
Cdd:PRK12492 440 EGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVKLFVVaRDPGLSV 519
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 446371684 436 EEIIHFCEEKLAKYKVPKKACFLEELPRNASKKLLRRELRQL 477
Cdd:PRK12492 520 EELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRRELRDI 561
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
2-480 |
2.16e-50 |
|
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: 179.57 E-value: 2.16e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 2 ETMPNWLKQRAFLTPDRTAIEIEEEKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVL 81
Cdd:COG1021 25 ETLGDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAIPVF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 82 LNTRLSREELLWQMDDAEVVCLVTDQQ---FD----ANDVpVYSFAEVMHGLkVEASIQEEFSLEEAMT-----IIYTS- 148
Cdd:COG1021 105 ALPAHRRAEISHFAEQSEAVAYIIPDRhrgFDyralAREL-QAEVPSLRHVL-VVGDAGEFTSLDALLAapadlSEPRPd 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 149 -----------GTTGKPKGVILTYGNHWASAVGSSLNLGLRDDDCWLACMPM--------------FHVGGlsllmknim 203
Cdd:COG1021 183 pddvaffqlsgGTTGLPKLIPRTHDDYLYSVRASAEICGLDADTVYLAALPAahnfplsspgvlgvLYAGG--------- 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 204 ygmRILLVPKYDADFIHKALQTRGVTIISVVSKMLTDLLERLGEETY-PSSLRCMLLGGGPAP-------KPLLetcvdk 275
Cdd:COG1021 254 ---TVVLAPDPSPDTAFPLIERERVTVTALVPPLALLWLDAAERSRYdLSSLRVLQVGGAKLSpelarrvRPAL------ 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 276 GIPVYQTYGMTEtSSQICTLSADYMLTKVGSAGKPLfqC---QLRI-EKDGVVVPPLVEGEIVVKGPNVTGGYFNREDAT 351
Cdd:COG1021 325 GCTLQQVFGMAE-GLVNYTRLDDPEEVILTTQGRPI--SpddEVRIvDEDGNPVPPGEVGELLTRGPYTIRGYYRAPEHN 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 352 RE--TiQNGWLHTGDLGYLDEEGFLYVLDRRSDLIISGGENIYPAQIEEVLLSHPMVAEAGVVGMTDDKWGQVPAAFVVK 429
Cdd:COG1021 402 ARafT-PDGFYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGERSCAFVVP 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 446371684 430 NGE-VTEEEIIHFCEEK-LAKYKVPKKACFLEELPRNASKKLLRRELRQLVEE 480
Cdd:COG1021 481 RGEpLTLAELRRFLRERgLAAFKLPDRLEFVDALPLTAVGKIDKKALRAALAA 533
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
19-480 |
3.16e-50 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 179.98 E-value: 3.16e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 19 TAIEIEEEKVTFLQLHEKVVSvCEHLTH--VGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSREELLWQMD 96
Cdd:PRK05620 30 TWGGAEQEQTTFAAIGARAAA-LAHALHdeLGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIIN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 97 DAEVVCLVTDQQ-------------------------------FDANDVPVYSFAEVMHGlkvEASIQEEFSLEE--AMT 143
Cdd:PRK05620 109 HAEDEVIVADPRlaeqlgeilkecpcvravvfigpsdadsaaaHMPEGIKVYSYEALLDG---RSTVYDWPELDEttAAA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 144 IIYTSGTTGKPKGVILTYGNHWASAVG--SSLNLGLRDDDCWLACMPMFHVGGLSLLMKNIMYGMRIL-----LVPKYDA 216
Cdd:PRK05620 186 ICYSTGTTGAPKGVVYSHRSLYLQSLSlrTTDSLAVTHGESFLCCVPIYHVLSWGVPLAAFMSGTPLVfpgpdLSAPTLA 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 217 DFIHKAL--QTRGV-TI-ISVVSKMLTDLLERLgeetypsSLRCMLLGGGPAPKPLLETCVDK-GIPVYQTYGMTETSSq 291
Cdd:PRK05620 266 KIIATAMprVAHGVpTLwIQLMVHYLKNPPERM-------SLQEIYVGGSAVPPILIKAWEERyGVDVVHVWGMTETSP- 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 292 ICTLS-----------ADYMLtkvgSAGKPLFQCQLRIEKDGVVVPPL--VEGEIVVKGPNVTGGYFNR----------- 347
Cdd:PRK05620 338 VGTVArppsgvsgearWAYRV----SQGRFPASLEYRIVNDGQVMESTdrNEGEIQVRGNWVTASYYHSpteegggaast 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 348 ------EDATRETIQNGWLHTGDLGYLDEEGFLYVLDRRSDLIISGGENIYPAQIEEVLLSHPMVAEAGVVGMTDDKWGQ 421
Cdd:PRK05620 414 frgedvEDANDRFTADGWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGE 493
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446371684 422 VPAAFVVKNGEV-----TEEEIIHFCEEKLAKYKVPKKACFLEELPRNASKKLLRRELRQLVEE 480
Cdd:PRK05620 494 RPLAVTVLAPGIeptreTAERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDLRQHLAD 557
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
15-479 |
2.84e-49 |
|
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: 178.28 E-value: 2.84e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 15 TPDRTAI------EIEEEKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSR 88
Cdd:cd05967 64 RGDQIALiydspvTGTERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGFAA 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 89 EELLWQMDDAEVVCLVT----------------------DQQFDANDVPVYS----------------FAEVMHG----- 125
Cdd:cd05967 144 KELASRIDDAKPKLIVTascgiepgkvvpykplldkaleLSGHKPHHVLVLNrpqvpadltkpgrdldWSELLAKaepvd 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 126 -LKVEAsiqeefslEEAMTIIYTSGTTGKPKGVILTYGNHwasAVGSSLNL----GLRDDDCWLACMPMFHVGGLSLL-- 198
Cdd:cd05967 224 cVPVAA--------TDPLYILYTSGTTGKPKGVVRDNGGH---AVALNWSMrniyGIKPGDVWWAASDVGWVVGHSYIvy 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 199 ------MKNIMYGMRILLVPkyDADFIHKALQTRGV-------TIISVVSKmlTDLLERLGEETYPSSLRCMLLGGGPAP 265
Cdd:cd05967 293 gpllhgATTVLYEGKPVGTP--DPGAFWRVIEKYQVnalftapTAIRAIRK--EDPDGKYIKKYDLSSLRTLFLAGERLD 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 266 KPLLETCVDK-GIPVYQTYGMTETSSQICT--LSADYMLTKVGSAGKPLFQCQLRI-EKDGVVVPPLVEGEIVVKGP--- 338
Cdd:cd05967 369 PPTLEWAENTlGVPVIDHWWQTETGWPITAnpVGLEPLPIKAGSPGKPVPGYQVQVlDEDGEPVGPNELGNIVIKLPlpp 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 339 -NVTGGYFNREDATRETIQN--GWLHTGDLGYLDEEGFLYVLDRRSDLIISGGENIYPAQIEEVLLSHPMVAEAGVVGMT 415
Cdd:cd05967 449 gCLLTLWKNDERFKKLYLSKfpGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVR 528
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 416 DDKWGQVPAAFVV-KNG-----EVTEEEIIHFCEEKLAKYKVPKKACFLEELPRNASKKLLRRELRQLVE 479
Cdd:cd05967 529 DELKGQVPLGLVVlKEGvkitaEELEKELVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTLRKIAD 598
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
2-475 |
9.58e-49 |
|
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: 180.05 E-value: 9.58e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 2 ETMPNWLKQRAFLTPDRTAIEIEEEKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVL 81
Cdd:COG1020 476 ATLHELFEAQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVP 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 82 LNTRLSREELLWQMDDAEVVCLVTDQQ----FDANDVPVysfaevmhgLKVEASIQEEFSLEEAMT---------IIYTS 148
Cdd:COG1020 556 LDPAYPAERLAYMLEDAGARLVLTQSAlaarLPELGVPV---------LALDALALAAEPATNPPVpvtpddlayVIYTS 626
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 149 GTTGKPKGVILTYGN-----HWASAvgsslNLGLRDDDCWLACMPM-FHVGGLSLLMKnIMYGMRILLVPK---YDADFI 219
Cdd:COG1020 627 GSTGRPKGVMVEHRAlvnllAWMQR-----RYGLGPGDRVLQFASLsFDASVWEIFGA-LLSGATLVLAPPearRDPAAL 700
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 220 HKALQTRGVTIISVVSKMLTDLLERLGEEtyPSSLRCMLLGGGPAPKPLLETCVDK--GIPVYQTYGMTETSsqICTLSA 297
Cdd:COG1020 701 AELLARHRVTVLNLTPSLLRALLDAAPEA--LPSLRLVLVGGEALPPELVRRWRARlpGARLVNLYGPTETT--VDSTYY 776
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 298 DYMLTKVGSA----GKPLFQCQLRI-EKDGVVVPPLVEGEIVVKGPNVTGGYFNREDATRE------TIQNG--WLHTGD 364
Cdd:COG1020 777 EVTPPDADGGsvpiGRPIANTRVYVlDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAErfvadpFGFPGarLYRTGD 856
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 365 LGYLDEEGFLYVLDRRSDLI-ISG-----GEniypaqIEEVLLSHPMVAEAGVVGMTDDKWGQVPAAFVVKNGEVTEEEI 438
Cdd:COG1020 857 LARWLPDGNLEFLGRADDQVkIRGfrielGE------IEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAA 930
|
490 500 510
....*....|....*....|....*....|....*..
gi 446371684 439 IHFCEEKLAKYKVPKKACFLEELPRNASKKLLRRELR 475
Cdd:COG1020 931 LLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLA 967
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
7-474 |
1.03e-48 |
|
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: 173.93 E-value: 1.03e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 7 WLKQRAFLTPDRTAIEIEEEKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRL 86
Cdd:cd12117 2 LFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 87 SREELLWQMDDAEVVCLVTDQQfDANDVPVYSFAEVMHGLKVEASIQEE---FSLEEAMTIIYTSGTTGKPKGVILTygn 163
Cdd:cd12117 82 PAERLAFMLADAGAKVLLTDRS-LAGRAGGLEVAVVIDEALDAGPAGNPavpVSPDDLAYVMYTSGSTGRPKGVAVT--- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 164 HwASAVGSSLN---LGLRDDDCWLACMP------MFHVGGlSLLmknimYGMRILLVPKY---DADFIHKALQTRGVTII 231
Cdd:cd12117 158 H-RGVVRLVKNtnyVTLGPDDRVLQTSPlafdasTFEIWG-ALL-----NGARLVLAPKGtllDPDALGALIAEEGVTVL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 232 svvskMLTDLLERLGEETYP---SSLRCMLLGGGPAPKPLLETCVDK--GIPVYQTYGMTETSsqicTLSADYMLTKVGS 306
Cdd:cd12117 231 -----WLTAALFNQLADEDPecfAGLRELLTGGEVVSPPHVRRVLAAcpGLRLVNGYGPTENT----TFTTSHVVTELDE 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 307 A------GKPLFQCQLRI-EKDGVVVPPLVEGEIVVKGPNVTGGYFNREDATRET-IQNGWL------HTGDLGYLDEEG 372
Cdd:cd12117 302 VagsipiGRPIANTRVYVlDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERfVADPFGpgerlyRTGDLARWLPDG 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 373 FLYVLDRRSDLIISGGENIYPAQIEEVLLSHPMVAEAGVVGMTDDKWGQVPAAFVVKNGEVTEEEIIHFCEEKLAKYKVP 452
Cdd:cd12117 382 RLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVVAEGALDAAELRAFLRERLPAYMVP 461
|
490 500
....*....|....*....|..
gi 446371684 453 KKACFLEELPRNASKKLLRREL 474
Cdd:cd12117 462 AAFVVLDELPLTANGKVDRRAL 483
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
126-477 |
1.05e-48 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 171.00 E-value: 1.05e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 126 LKVEASIQEEFSLeeamtIIYTSGTTGKPKGVILTYGNHWASAVGSSLNLGlrDDDCWLACMPMFHVGGLSLLMKNIMYG 205
Cdd:PRK07824 27 LRVGEPIDDDVAL-----VVATSGTTGTPKGAMLTAAALTASADATHDRLG--GPGQWLLALPAHHIAGLQVLVRSVIAG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 206 MR--ILLVPK-YDADFIHKALQ--TRGVTIISVVSKMLTDLLERLGEETYPSSLRCMLLGGGPAPKPLLETCVDKGIPVY 280
Cdd:PRK07824 100 SEpvELDVSAgFDPTALPRAVAelGGGRRYTSLVPMQLAKALDDPAATAALAELDAVLVGGGPAPAPVLDAAAAAGINVV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 281 QTYGMTETSSQiCTLSadymltkvgsaGKPLFQCQLRIEkdgvvvpplvEGEIVVKGPNVTGGYFNREDATrETIQNGWL 360
Cdd:PRK07824 180 RTYGMSETSGG-CVYD-----------GVPLDGVRVRVE----------DGRIALGGPTLAKGYRNPVDPD-PFAEPGWF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 361 HTGDLGYLDEeGFLYVLDRRSDLIISGGENIYPAQIEEVLLSHPMVAEAGVVGMTDDKWGQVPAAFVVKNGEVTE--EEI 438
Cdd:PRK07824 237 RTDDLGALDD-GVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAVVGDGGPAPtlEAL 315
|
330 340 350
....*....|....*....|....*....|....*....
gi 446371684 439 IHFCEEKLAKYKVPKKACFLEELPRNASKKLLRRELRQL 477
Cdd:PRK07824 316 RAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALVRR 354
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
12-475 |
1.56e-48 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 174.04 E-value: 1.56e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 12 AFLTPDRTAIEIEE--EKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSRE 89
Cdd:PRK13390 7 AQIAPDRPAVIVAEtgEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 90 ELLWQMDDAEVVCLVTDQQFDA------NDVPVysfaEVMHGLKVEASIQEEFSLEEA----------MTIIYTSGTTGK 153
Cdd:PRK13390 87 EADYIVGDSGARVLVASAALDGlaakvgADLPL----RLSFGGEIDGFGSFEAALAGAgprlteqpcgAVMLYSSGTTGF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 154 PKGVILTYGNHWASAVGSSLN------LGLRDDDCWLACMPMFHVGGLSLLMKNIMYGMRILLVPKYDADFIHKALQTRG 227
Cdd:PRK13390 163 PKGIQPDLPGRDVDAPGDPIVaiarafYDISESDIYYSSAPIYHAAPLRWCSMVHALGGTVVLAKRFDAQATLGHVERYR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 228 VTIISVVSKMLTDLLeRLGEETYP----SSLRCMLLGGGPAPKPLLETCVD-KGIPVYQTYGMTETSSQICTLSADYmLT 302
Cdd:PRK13390 243 ITVTQMVPTMFVRLL-KLDADVRTrydvSSLRAVIHAAAPCPVDVKHAMIDwLGPIVYEYYSSTEAHGMTFIDSPDW-LA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 303 KVGSAGKPLFQCQLRIEKDGVVVPPLVEGEIVVKGPNVTGGYFNREDATRETIQNG---WLHTGDLGYLDEEGFLYVLDR 379
Cdd:PRK13390 321 HPGSVGRSVLGDLHICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAAAQHPAhpfWTTVGDLGSVDEDGYLYLADR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 380 RSDLIISGGENIYPAQIEEVLLSHPMVAEAGVVGMTDDKWGQVPAAFV-----VKNGEVTEEEIIHFCEEKLAKYKVPKK 454
Cdd:PRK13390 401 KSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIqlvegIRGSDELARELIDYTRSRIAHYKAPRS 480
|
490 500
....*....|....*....|.
gi 446371684 455 ACFLEELPRNASKKLLRRELR 475
Cdd:PRK13390 481 VEFVDELPRTPTGKLVKGLLR 501
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
114-475 |
2.00e-48 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 174.95 E-value: 2.00e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 114 VPVYS------FAEVM---HGLKV-EASIQeefsLEEAMTIIYTSGTTGKPKGVILTYGNHWASA------VGSSLNLGL 177
Cdd:PRK05677 176 VPAYHlpqavkFNDALakgAGQPVtEANPQ----ADDVAVLQYTGGTTGVAKGAMLTHRNLVANMlqcralMGSNLNEGC 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 178 rddDCWLACMPMFHVGGLSL-LMKNIMYGMRILLVPK-YDADFIHKALQTRGVTIISVVSKMLTDLLERLGEETYPSSLR 255
Cdd:PRK05677 252 ---EILIAPLPLYHIYAFTFhCMAMMLIGNHNILISNpRDLPAMVKELGKWKFSGFVGLNTLFVALCNNEAFRKLDFSAL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 256 CMLLGGGPApkplLETCVDK------GIPVYQTYGMTETSSQICTLSADYMltKVGSAGKPLFQCQLR-IEKDGVVVPPL 328
Cdd:PRK05677 329 KLTLSGGMA----LQLATAErwkevtGCAICEGYGMTETSPVVSVNPSQAI--QVGTIGIPVPSTLCKvIDDDGNELPLG 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 329 VEGEIVVKGPNVTGGYFNREDATRETI-QNGWLHTGDLGYLDEEGFLYVLDRRSDLIISGGENIYPAQIEEVLLSHPMVA 407
Cdd:PRK05677 403 EVGELCVKGPQVMKGYWQRPEATDEILdSDGWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVL 482
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 408 EAGVVGMTDDKWGQVPAAFVV-KNGE-VTEEEIIHFCEEKLAKYKVPKKACFLEELPRNASKKLLRRELR 475
Cdd:PRK05677 483 QCAAIGVPDEKSGEAIKVFVVvKPGEtLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRRELR 552
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
16-474 |
5.48e-48 |
|
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: 171.34 E-value: 5.48e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 16 PDRTAIEIEEEKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSREELLWQM 95
Cdd:cd17643 1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 96 DDAEVVCLVTDqqfdaNDVPVYsfaevmhglkveasiqeefsleeamtIIYTSGTTGKPKGVILTYGNHWASAVGSSLNL 175
Cdd:cd17643 81 ADSGPSLLLTD-----PDDLAY--------------------------VIYTSGSTGRPKGVVVSHANVLALFAATQRWF 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 176 GLRDDDCWLACMPM---FHV----GGLSllmknimYGMRILLVPKY---DADFIHKALQTRGVTIISVV-SKMLTDLLER 244
Cdd:cd17643 130 GFNEDDVWTLFHSYafdFSVweiwGALL-------HGGRLVVVPYEvarSPEDFARLLRDEGVTVLNQTpSAFYQLVEAA 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 245 LGEETYPSSLRCMLLGGGPAPKPLL----ETCVDKGIPVYQTYGMTETS--SQICTLSADYMLTKVGSA-GKPLFQCQLR 317
Cdd:cd17643 203 DRDGRDPLALRYVIFGGEALEAAMLrpwaGRFGLDRPQLVNMYGITETTvhVTFRPLDAADLPAAAASPiGRPLPGLRVY 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 318 I-EKDGVVVPPLVEGEIVVKGPNVTGGYFNREDATRETIQNG--------WLHTGDLGYLDEEGFLYVLDRRSDLIISGG 388
Cdd:cd17643 283 VlDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANpfggpgsrMYRTGDLARRLPDGELEYLGRADEQVKIRG 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 389 ENIYPAQIEEVLLSHPMVAEAGVVGMTDDKWGQVPAAFVVKNGEVTE--EEIIHFCEEKLAKYKVPKKACFLEELPRNAS 466
Cdd:cd17643 363 FRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVADDGAAAdiAELRALLKELLPDYMVPARYVPLDALPLTVN 442
|
....*...
gi 446371684 467 KKLLRREL 474
Cdd:cd17643 443 GKLDRAAL 450
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
32-411 |
3.18e-47 |
|
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: 168.21 E-value: 3.18e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 32 QLHEKVVSVCEHL-THVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRL--SREELLwqMDDAEVVCLVTDQQ 108
Cdd:TIGR01733 4 ELDERANRLARHLrAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYpaERLAFI--LEDAGARLLLTDSA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 109 FDANDVPVYsFAEVMHGLKVEASIQEEFSLEEA---------MTIIYTSGTTGKPKGVILTYG---NHWASAVGsslNLG 176
Cdd:TIGR01733 82 LASRLAGLV-LPVILLDPLELAALDDAPAPPPPdapsgpddlAYVIYTSGSTGRPKGVVVTHRslvNLLAWLAR---RYG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 177 LRDDDCWLACMPM-FHVGGLSLLMKnIMYGMRILLVP----KYDADFIHKALQTRGVTIISVVSKMLTDLLERLGEEtyP 251
Cdd:TIGR01733 158 LDPDDRVLQFASLsFDASVEEIFGA-LLAGATLVVPPedeeRDDAALLAALIAEHPVTVLNLTPSLLALLAAALPPA--L 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 252 SSLRCMLLGGGPAPKPLLETCVDK--GIPVYQTYGMTETSsqICTLSADYMLTKVGSA-----GKPLFQCQLRI-EKDGV 323
Cdd:TIGR01733 235 ASLRLVILGGEALTPALVDRWRARgpGARLINLYGPTETT--VWSTATLVDPDDAPREspvpiGRPLANTRLYVlDDDLR 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 324 VVPPLVEGEIVVKGPNVTGGYFNREDATRE---------TIQNGWLHTGDLGYLDEEGFLYVLDRRSDLIISGGENIYPA 394
Cdd:TIGR01733 313 PVPVGVVGELYIGGPGVARGYLNRPELTAErfvpdpfagGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELG 392
|
410
....*....|....*..
gi 446371684 395 QIEEVLLSHPMVAEAGV 411
Cdd:TIGR01733 393 EIEAALLRHPGVREAVV 409
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
25-479 |
5.68e-47 |
|
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: 169.08 E-value: 5.68e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 25 EEKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSREELLWQMDDAEVVCLV 104
Cdd:cd17640 3 PKRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 105 TDQqfDANDVPvysfaevmhglkveasiqeefsleeamTIIYTSGTTGKPKGVILTYGNHWASAVGSSLNLGLRDDDCWL 184
Cdd:cd17640 83 VEN--DSDDLA---------------------------TIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQPGDRFL 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 185 ACMPMFHV-----------GGLSLLMKNIMYGMR---------ILLVPK-YDADF--IHKALQTRgvtiiSVVSKMLTDL 241
Cdd:cd17640 134 SILPIWHSyersaeyfifaCGCSQAYTSIRTLKDdlkrvkphyIVSVPRlWESLYsgIQKQVSKS-----SPIKQFLFLF 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 242 LERLGEetypssLRCMLLGGGPAPKPlletcVDK-----GIPVYQTYGMTETSSQIC--TLSADymltKVGSAGKPLFQC 314
Cdd:cd17640 209 FLSGGI------FKFGISGGGALPPH-----VDTffeaiGIEVLNGYGLTETSPVVSarRLKCN----VRGSVGRPLPGT 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 315 QLRI--EKDGVVVPPLVEGEIVVKGPNVTGGYFNREDATRETI-QNGWLHTGDLGYLDEEGFLYVLDRRSDLII-SGGEN 390
Cdd:cd17640 274 EIKIvdPEGNVVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLdSDGWFNTGDLGWLTCGGELVLTGRAKDTIVlSNGEN 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 391 IYPAQIEEVLLSHPMVAEAGVVGMTDDKWGqvpaAFVVKNGEVTEEEIihfceeKLAKYKVPKkacflEELPRNASK--- 467
Cdd:cd17640 354 VEPQPIEEALMRSPFIEQIMVVGQDQKRLG----ALIVPNFEELEKWA------KESGVKLAN-----DRSQLLASKkvl 418
|
490
....*....|..
gi 446371684 468 KLLRRELRQLVE 479
Cdd:cd17640 419 KLYKNEIKDEIS 430
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
146-471 |
9.27e-47 |
|
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: 164.50 E-value: 9.27e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 146 YTSGTTGKPKGVILTYGNHWASAVGSSLNLGLRDDDCWLACMPMFHVGGLSLLMKNIMYGMRILLVPKYDADFIHKALQT 225
Cdd:cd17633 7 FTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSHSLFLYGAISALYLGGTFIGQRKFNPKSWIRKINQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 226 RGVTIISVVSKMLTDLLErlgEETYPSSLRCMLLGGGPAPKPLLETcVDKGIP---VYQTYGMTETSsqICTLSADYMLT 302
Cdd:cd17633 87 YNATVIYLVPTMLQALAR---TLEPESKIKSIFSSGQKLFESTKKK-LKNIFPkanLIEFYGTSELS--FITYNFNQESR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 303 KVGSAGKPLFQCQLRI-EKDGVVVpplveGEIVVKGPNVTGGYFNredaTRETIQNGWLHTGDLGYLDEEGFLYVLDRRS 381
Cdd:cd17633 161 PPNSVGRPFPNVEIEIrNADGGEI-----GKIFVKSEMVFSGYVR----GGFSNPDGWMSVGDIGYVDEEGYLYLVGRES 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 382 DLIISGGENIYPAQIEEVLLSHPMVAEAGVVGMTDDKWGQVpAAFVVKNGEVTEEEIIHFCEEKLAKYKVPKKACFLEEL 461
Cdd:cd17633 232 DMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEI-AVALYSGDKLTYKQLKRFLKQKLSRYEIPKKIIFVDSL 310
|
330
....*....|
gi 446371684 462 PRNASKKLLR 471
Cdd:cd17633 311 PYTSSGKIAR 320
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
16-470 |
1.39e-46 |
|
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: 170.45 E-value: 1.39e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 16 PDRTAIEIEEEK------VTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSRE 89
Cdd:cd17634 67 GDRTAIIYEGDDtsqsrtISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 90 ELLWQMDDAEVVCLVT-----------------DQQFDANDVPVYSFAEV----------------MHGLKVEASIQEE- 135
Cdd:cd17634 147 AVAGRIIDSSSRLLITadggvragrsvplkknvDDALNPNVTSVEHVIVLkrtgsdidwqegrdlwWRDLIAKASPEHQp 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 136 --FSLEEAMTIIYTSGTTGKPKGVILTYGNHWASAVGSSLN---LGLRD------DDCWLACMPMFHVGGLSLLMKNIMY 204
Cdd:cd17634 227 eaMNAEDPLFILYTSGTTGKPKGVLHTTGGYLVYAATTMKYvfdYGPGDiywctaDVGWVTGHSYLLYGPLACGATTLLY 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 205 GMrillVPKY-DADFIHKALQTRGV-------TIISVVSKMLTDLLERlgeeTYPSSLRCMLLGGGP-APKP---LLETC 272
Cdd:cd17634 307 EG----VPNWpTPARMWQVVDKHGVnilytapTAIRALMAAGDDAIEG----TDRSSLRILGSVGEPiNPEAyewYWKKI 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 273 VDKGIPVYQTYGMTETSSQICTLSADYMLTKVGSAGKPLFQCQLRI-EKDGVVVPPLVEGEIVVKG--PNVTGGYFNRED 349
Cdd:cd17634 379 GKEKCPVVDTWWQTETGGFMITPLPGAIELKAGSATRPVFGVQPAVvDNEGHPQPGGTEGNLVITDpwPGQTRTLFGDHE 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 350 ATRET----IQNGWLHtGDLGYLDEEGFLYVLDRRSDLIISGGENIYPAQIEEVLLSHPMVAEAGVVGMTDDKWGQVPAA 425
Cdd:cd17634 459 RFEQTyfstFKGMYFS-GDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYA 537
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 446371684 426 FVVKNGEVTE-----EEIIHFCEEKLAKYKVPKKACFLEELPRNASKKLL 470
Cdd:cd17634 538 YVVLNHGVEPspelyAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKIM 587
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
139-471 |
1.53e-45 |
|
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: 162.04 E-value: 1.53e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 139 EEAMTIIYTSGTTGKPKGVILTYGNHWASAVG-SSLNLGLRDDDCWLACMPMFHVGGLS-LLMKNIMYGMRILLVPKYDA 216
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFFAVPDIlQKEGLNWVVGDVTYLPLPATHIGGLWwILTCLIHGGLCVTGGENTTY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 217 DFIHKALQTRGVTIISVVSKMLTDLLERLGEE-TYPSSLRCMLLGGG-PAPKPLLETCVDKGIPVYQTYGMTETSSQICt 294
Cdd:cd17635 81 KSLFKILTTNAVTTTCLVPTLLSKLVSELKSAnATVPSLRLIGYGGSrAIAADVRFIEATGLTNTAQVYGLSETGTALC- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 295 LSADYMLTKVGSAGKPLFQCQLRI-EKDGVVVPPLVEGEIVVKGPNVTGGYFNREDATRETIQNGWLHTGDLGYLDEEGF 373
Cdd:cd17635 160 LPTDDDSIEINAVGRPYPGVDVYLaATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLIDGWVNTGDLGERREDGF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 374 LYVLDRRSDLIISGGENIYPAQIEEVLLSHPMVAEAGVVGMTDDKWGQVPAAFVVKNGEVTEEEI---IHFCEEKLAKYK 450
Cdd:cd17635 240 LFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVASAELDENAIralKHTIRRELEPYA 319
|
330 340
....*....|....*....|.
gi 446371684 451 VPKKACFLEELPRNASKKLLR 471
Cdd:cd17635 320 RPSTIVIVTDIPRTQSGKVKR 340
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
15-476 |
1.67e-45 |
|
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: 166.52 E-value: 1.67e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 15 TPDRTAI-----EIEEEKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSRE 89
Cdd:cd05970 30 YPDKLALvwcddAGEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQLTAK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 90 ELLWQMDDAEVVCLVTDQQFD--------ANDVPVYSFAEVMHGLKVEASIQEEFSLEEAMTII---------------- 145
Cdd:cd05970 110 DIVYRIESADIKMIVAIAEDNipeeiekaAPECPSKPKLVWVGDPVPEGWIDFRKLIKNASPDFerptansypcgedill 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 146 --YTSGTTGKPK----------GVILTyGNHWASAVGSSLNLGLRDDDcWLACMpmfhVGGLsllmknimYGMRIL--LV 211
Cdd:cd05970 190 vyFSSGTTGMPKmvehdftyplGHIVT-AKYWQNVREGGLHLTVADTG-WGKAV----WGKI--------YGQWIAgaAV 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 212 PKYDAD-FIHKAL----QTRGVTIISVVSKMLTDLLERLGEETYPSSLRCMLLGGGPAPKPLLETCVDK-GIPVYQTYGM 285
Cdd:cd05970 256 FVYDYDkFDPKALleklSKYGVTTFCAPPTIYRFLIREDLSRYDLSSLRYCTTAGEALNPEVFNTFKEKtGIKLMEGFGQ 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 286 TETSSQICTLSadYMLTKVGSAGKPLFQCQLR-IEKDGVVVPPLVEGEIVV---KGPNVT--GGYFNREDATRETIQNGW 359
Cdd:cd05970 336 TETTLTIATFP--WMEPKPGSMGKPAPGYEIDlIDREGRSCEAGEEGEIVIrtsKGKPVGlfGGYYKDAEKTAEVWHDGY 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 360 LHTGDLGYLDEEGFLYVLDRRSDLIISGGENIYPAQIEEVLLSHPMVAEAGVVGMTDDKWGQVPAAFVV-----KNGEVT 434
Cdd:cd05970 414 YHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIVlakgyEPSEEL 493
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 446371684 435 EEEIIHFCEEKLAKYKVPKKACFLEELPRNASKKLLRRELRQ 476
Cdd:cd05970 494 KKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEIRE 535
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
15-474 |
1.93e-45 |
|
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: 164.41 E-value: 1.93e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 15 TPDRTAIEIEEEKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSREELLWQ 94
Cdd:cd12115 12 TPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPERLRFI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 95 MDDAEVVCLVTDQqfdanDVPVYsfaevmhglkveasiqeefsleeamtIIYTSGTTGKPKGVILTYGN-----HWASAV 169
Cdd:cd12115 92 LEDAQARLVLTDP-----DDLAY--------------------------VIYTSGSTGRPKGVAIEHRNaaaflQWAAAA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 170 GSSLNL-GLrdddcwLACMPM-FHvggLSL--LMKNIMYGMRILLVPKYDADFIHKALQtrGVTIISVVSKMLTDLLErl 245
Cdd:cd12115 141 FSAEELaGV------LASTSIcFD---LSVfeLFGPLATGGKVVLADNVLALPDLPAAA--EVTLINTVPSAAAELLR-- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 246 gEETYPSSLRCMLLGGGPAPKPLLETCVDK--GIPVYQTYGMTETSsqicTLSADYMLTKVG----SAGKPLFQCQLRI- 318
Cdd:cd12115 208 -HDALPASVRVVNLAGEPLPRDLVQRLYARlqVERVVNLYGPSEDT----TYSTVAPVPPGAsgevSIGRPLANTQAYVl 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 319 EKDGVVVPPLVEGEIVVKGPNVTGGYFNREDATRET-IQNGWL------HTGDLGYLDEEGFLYVLDRRSDLIISGGENI 391
Cdd:cd12115 283 DRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERfLPDPFGpgarlyRTGDLVRWRPDGLLEFLGRADNQVKVRGFRI 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 392 YPAQIEEVLLSHPMVAEAGVVGMTDDKWGQVPAAFVVKNG--EVTEEEIIHFCEEKLAKYKVPKKACFLEELPRNASKKL 469
Cdd:cd12115 363 ELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEPgaAGLVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKI 442
|
....*
gi 446371684 470 LRREL 474
Cdd:cd12115 443 DRSAL 447
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
17-475 |
2.06e-45 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 166.61 E-value: 2.06e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 17 DRTAI----EIEEEKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEM-ITVIHALSyVGAVA------------ 79
Cdd:PRK04319 59 DKVALryldASRKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELyFALLGALK-NGAIVgplfeafmeeav 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 80 ----------VLLNT-RLSREELLWQMDDAEVVCLVTDQqfDANDVPVYSFAEVMHGLKVEASIqEEFSLEEAMTIIYTS 148
Cdd:PRK04319 138 rdrledseakVLITTpALLERKPADDLPSLKHVLLVGED--VEEGPGTLDFNALMEQASDEFDI-EWTDREDGAILHYTS 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 149 GTTGKPKGVILTYG---NHWASAvgsSLNLGLRDDDC-WLACMPMFhVGGLS------LLM--KNIMYGMRillvpkYDA 216
Cdd:PRK04319 215 GSTGKPKGVLHVHNamlQHYQTG---KYVLDLHEDDVyWCTADPGW-VTGTSygifapWLNgaTNVIDGGR------FSP 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 217 DFIHKALQTRGVTI-------ISVVSKMLTDLLERlgeetYP-SSLRCMLLGGGP--------APKPLletcvdkGIPVY 280
Cdd:PRK04319 285 ERWYRILEDYKVTVwytaptaIRMLMGAGDDLVKK-----YDlSSLRHILSVGEPlnpevvrwGMKVF-------GLPIH 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 281 QTYGMTETSSQ-ICTLSAdyMLTKVGSAGKPLFQCQLRI-EKDGVVVPPLVEGEIVVKG--PNVTGGYFNREDATRETIQ 356
Cdd:PRK04319 353 DNWWMTETGGImIANYPA--MDIKPGSMGKPLPGIEAAIvDDQGNELPPNRMGNLAIKKgwPSMMRGIWNNPEKYESYFA 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 357 NGWLHTGDLGYLDEEGFLYVLDRRSDLIISGGENIYPAQIEEVLLSHPMVAEAGVVGMTDDKWGQVPAAFVV-KNG-EVT 434
Cdd:PRK04319 431 GDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVAlRPGyEPS 510
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 446371684 435 EE---EIIHFCEEKLAKYKVPKKACFLEELPRNASKKLLRRELR 475
Cdd:PRK04319 511 EElkeEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKIMRRVLK 554
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
10-479 |
3.43e-45 |
|
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: 165.87 E-value: 3.43e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 10 QRAFLTPDRTAI------EIEEEKVTFLQLHEKVVSVCEHLTHVGvKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLL- 82
Cdd:cd05931 1 RRAAARPDRPAYtflddeGGREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLp 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 83 --NTRLSREELLWQMDDAEVVCLVTDQQFDA-----------NDVPVYSFAEVMHGLKVEASIQEEFSLEEAMTIIYTSG 149
Cdd:cd05931 80 ppTPGRHAERLAAILADAGPRVVLTTAAALAavrafaasrpaAGTPRLLVVDLLPDTSAADWPPPSPDPDDIAYLQYTSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 150 TTGKPKGVILTYGNHWASAVGSSLNLGLRDDD---CWLacmPMFHVGGL-SLLMKNIMYGMRILLVPKydADFIH----- 220
Cdd:cd05931 160 STGTPKGVVVTHRNLLANVRQIRRAYGLDPGDvvvSWL---PLYHDMGLiGGLLTPLYSGGPSVLMSP--AAFLRrplrw 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 221 -KALQTRGVTIiSVVSKMLTDL-LERLGEETYP----SSLRCMLLGGGPAPKPLLETCVDKGIP-------VYQTYGMTE 287
Cdd:cd05931 235 lRLISRYRATI-SAAPNFAYDLcVRRVRDEDLEgldlSSWRVALNGAEPVRPATLRRFAEAFAPfgfrpeaFRPSYGLAE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 288 TS---------SQICTLSADYML---------------TKVGSAGKPLFQCQLRI--EKDGVVVPPLVEGEIVVKGPNVT 341
Cdd:cd05931 314 ATlfvsggppgTGPVVLRVDRDAlagravavaaddpaaRELVSCGRPLPDQEVRIvdPETGRELPDGEVGEIWVRGPSVA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 342 GGYFNREDATRETIQ-------NGWLHTGDLGYLDeEGFLYVLDRRSDLIISGGENIYPAQIE-EVLLSHPMVAEAGVV- 412
Cdd:cd05931 394 SGYWGRPEATAETFGalaatdeGGWLRTGDLGFLH-DGELYITGRLKDLIIVRGRNHYPQDIEaTAEEAHPALRPGCVAa 472
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446371684 413 -GMTDDKWGQVPAAFVVKNGEVTEE--EIIHFCEEKLAK-YKV-PKKACFLE--ELPRNASKKLLRRELRQLVE 479
Cdd:cd05931 473 fSVPDDGEERLVVVAEVERGADPADlaAIAAAIRAAVAReHGVaPADVVLVRpgSIPRTSSGKIQRRACRAAYL 546
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
2-474 |
8.52e-45 |
|
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: 163.27 E-value: 8.52e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 2 ETMPNWLKQRAFLTPDRTAIEIEEEKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVL 81
Cdd:cd05920 15 EPLGDLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 82 LNTRLSREELLWQMDDAEVVCLVTDQQFDANDvPVYSFAEVMHglkveasiqeefSLEEAMTIIYTSGTTGKPKGVILTY 161
Cdd:cd05920 95 ALPSHRRSELSAFCAHAEAVAYIVPDRHAGFD-HRALARELAE------------SIPEVALFLLSGGTTGTPKLIPRTH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 162 GNHWASAVGSSLNLGLRDDDCWLACMPMFHVGGLSL--LMKNIMYGMRILLVPKYDADFIHKALQTRGVTIISVVSKMLT 239
Cdd:cd05920 162 NDYAYNVRASAEVCGLDQDTVYLAVLPAAHNFPLACpgVLGTLLAGGRVVLAPDPSPDAAFPLIEREGVTVTALVPALVS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 240 DLLERLGEETY-PSSLRCMLLGGGPAPKPLLETCVDK-GIPVYQTYGMTEtsSQIC-TLSADYMLTKVGSAGKPLfqC-- 314
Cdd:cd05920 242 LWLDAAASRRAdLSSLRLLQVGGARLSPALARRVPPVlGCTLQQVFGMAE--GLLNyTRLDDPDEVIIHTQGRPM--Spd 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 315 -QLRI-EKDGVVVPPLVEGEIVVKGPNVTGGYFNREDA-TRETIQNGWLHTGDLGYLDEEGFLYVLDRRSDLIISGGENI 391
Cdd:cd05920 318 dEIRVvDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHnARAFTPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 392 YPAQIEEVLLSHPMVAEAGVVGMTDDKWGQVPAAFVV-KNGEVTEEEIIHFCEEK-LAKYKVPKKACFLEELPRNASKKL 469
Cdd:cd05920 398 AAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVlRDPPPSAAQLRRFLRERgLAAYKLPDRIEFVDSLPLTAVGKI 477
|
....*
gi 446371684 470 LRREL 474
Cdd:cd05920 478 DKKAL 482
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
27-478 |
2.20e-44 |
|
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: 162.50 E-value: 2.20e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 27 KVTFLQLHEKVVSVCEHLtHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSREELLWQMDDAEVVCLVTD 106
Cdd:cd05909 7 SLTYRKLLTGAIALARKL-AKMTKEGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVLTS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 107 QQF-----DANDVPVYSFAEVMH----------GLKVEASIQEEFS--------------LEEAMTIIYTSGTTGKPKGV 157
Cdd:cd05909 86 KQFieklkLHHLFDVEYDARIVYledlrakiskADKCKAFLAGKFPpkwllrifgvapvqPDDPAVILFTSGSEGLPKGV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 158 ILTYGNHWASAVGSSLNLGLRDDDCWLACMPMFHVGGLSL-LMKNIMYGMRILLVPK-YDADFIHKALQTRGVTIISVVS 235
Cdd:cd05909 166 VLSHKNLLANVEQITAIFDPNPEDVVFGALPFFHSFGLTGcLWLPLLSGIKVVFHPNpLDYKKIPELIYDKKATILLGTP 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 236 KMLTDLLERLGEETYpSSLRCMLLGGGPAPKPLLETCVDK-GIPVYQTYGMTETSSQIcTLSADYMLTKVGSAGKPLFQC 314
Cdd:cd05909 246 TFLRGYARAAHPEDF-SSLRLVVAGAEKLKDTLRQEFQEKfGIRILEGYGTTECSPVI-SVNTPQSPNKEGTVGRPLPGM 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 315 QLRIEK--DGVVVPPLVEGEIVVKGPNVTGGYFNREDATRETIQNGWLHTGDLGYLDEEGFLYVLDRRSDLIISGGENIY 392
Cdd:cd05909 324 EVKIVSveTHEEVPIGEGGLLLVRGPNVMLGYLNEPELTSFAFGDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVS 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 393 PAQIEEVLLSH-PMVAEAGVVGMTDDKWGQVPAAFVVKNGEVTEEEIIHFCEEKLAKYKVPKKACFLEELPRNASKKLLR 471
Cdd:cd05909 404 LEAIEDILSEIlPEDNEVAVVSVPDGRKGEKIVLLTTTTDTDPSSLNDILKNAGISNLAKPSYIHQVEEIPLLGTGKPDY 483
|
....*..
gi 446371684 472 RELRQLV 478
Cdd:cd05909 484 VTLKALA 490
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
29-423 |
3.95e-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: 341236 [Multi-domain] Cd Length: 457 Bit Score: 161.09 E-value: 3.95e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 29 TFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSREELLWQMDDAEvvclvtdqq 108
Cdd:cd05910 4 SFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEAE--------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 109 fdandvPvysfaevmhglkvEASIQEeFSLEEAMTIIYTSGTTGKPKGVILTYGNHWASAVGSSLNLGLRDDDCWLACMP 188
Cdd:cd05910 75 ------P-------------DAFIGI-PKADEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGEVDLATFP 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 189 MFHVGGLSLLMKNIMYGMRILLVPKYDADFIHKALQTRGVTIIsVVSKMLTDLLERLGEE---TYPSsLRCMLLGGGPAP 265
Cdd:cd05910 135 LFALFGPALGLTSVIPDMDPTRPARADPQKLVGAIRQYGVSIV-FGSPALLERVARYCAQhgiTLPS-LRRVLSAGAPVP 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 266 KPLLET---CVDKGIPVYQTYGMTEtSSQICTLSADYMLTKVGSA---------GKPLFQCQLRI----------EKDGV 323
Cdd:cd05910 213 IALAARlrkMLSDEAEILTPYGATE-ALPVSSIGSRELLATTTAAtsggagtcvGRPIPGVRVRIieiddepiaeWDDTL 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 324 VVPPLVEGEIVVKGPNVTGGYFNREDATR----ETIQNGWLH-TGDLGYLDEEGFLYVLDRRSDLIISGGENIYPAQIEE 398
Cdd:cd05910 292 ELPRGEIGEITVTGPTVTPTYVNRPVATAlakiDDNSEGFWHrMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVER 371
|
410 420
....*....|....*....|....*
gi 446371684 399 VLLSHPMVAEAGVVGMTdDKWGQVP 423
Cdd:cd05910 372 VFNTHPGVRRSALVGVG-KPGCQLP 395
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
16-474 |
6.10e-44 |
|
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: 160.92 E-value: 6.10e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 16 PDRTAIEIEEEKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSREELLWQM 95
Cdd:cd12116 1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 96 DDAEVVCLVTDQQ----FDANDVPVYSFAEVMHGLKveASIQEEFSLEEAMTIIYTSGTTGKPKGVILTYGN--HWASAV 169
Cdd:cd12116 81 EDAEPALVLTDDAlpdrLPAGLPVLLLALAAAAAAP--AAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNlvNFLHSM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 170 GSSlnLGLRDDDCWLACM-PMFHVGGLSLLMKnIMYGMRILLVPK---YDADFIHKALQTRGVTIIS---VVSKMLTDll 242
Cdd:cd12116 159 RER--LGLGPGDRLLAVTtYAFDISLLELLLP-LLAGARVVIAPRetqRDPEALARLIEAHSITVMQatpATWRMLLD-- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 243 erlGEETYPSSLRcMLLGGGPAPKPLLETCVDKGIPVYQTYGMTETS--SQICTLSADymLTKVgSAGKPLFQCQLRI-E 319
Cdd:cd12116 234 ---AGWQGRAGLT-ALCGGEALPPDLAARLLSRVGSLWNLYGPTETTiwSTAARVTAA--AGPI-PIGRPLANTQVYVlD 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 320 KDGVVVPPLVEGEIVVKGPNVTGGYFNREDATRE------TIQNG--WLHTGDLGYLDEEGFLYVLDRRSDLIISGGENI 391
Cdd:cd12116 307 AALRPVPPGVPGELYIGGDGVAQGYLGRPALTAErfvpdpFAGPGsrLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRI 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 392 YPAQIEEVLLSHPMVAEAGVVGMTDDKWGQVpAAFVVKNGEVT--EEEIIHFCEEKLAKYKVPKKACFLEELPRNASKKL 469
Cdd:cd12116 387 ELGEIEAALAAHPGVAQAAVVVREDGGDRRL-VAYVVLKAGAApdAAALRAHLRATLPAYMVPSAFVRLDALPLTANGKL 465
|
....*
gi 446371684 470 LRREL 474
Cdd:cd12116 466 DRKAL 470
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
16-474 |
8.54e-43 |
|
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: 157.82 E-value: 8.54e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 16 PDRTAIEIEEEKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSREELLWQM 95
Cdd:cd12114 1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 96 DDAEVVCLVTDQQFDANDVPVysFAEVMHGLKVEASIQEEFSLEEAMT----IIYTSGTTGKPKGVILTYGNhwASAVGS 171
Cdd:cd12114 81 ADAGARLVLTDGPDAQLDVAV--FDVLILDLDALAAPAPPPPVDVAPDdlayVIFTSGSTGTPKGVMISHRA--ALNTIL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 172 SLN--LGLRDDDCWLAC------MPMFHV-GGLSLlmknimyGMRILLVP---KYDADFIHKALQTRGVTII-SV--VSK 236
Cdd:cd12114 157 DINrrFAVGPDDRVLALsslsfdLSVYDIfGALSA-------GATLVLPDearRRDPAHWAELIERHGVTLWnSVpaLLE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 237 MLTDLLErlGEETYPSSLRCMLLGGG--PAPKP--LLETCVDkgIPVYQTYGMTETS--SQICTLSADYMLTKVGSAGKP 310
Cdd:cd12114 230 MLLDVLE--AAQALLPSLRLVLLSGDwiPLDLParLRALAPD--ARLISLGGATEASiwSIYHPIDEVPPDWRSIPYGRP 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 311 LFQCQLRI-EKDGVVVPPLVEGEIVVKGPNVTGGYFNREDATRE---TIQNG--WLHTGDLGYLDEEGFLYVLDRRSDLI 384
Cdd:cd12114 306 LANQRYRVlDPRGRDCPDWVPGELWIGGRGVALGYLGDPELTAArfvTHPDGerLYRTGDLGRYRPDGTLEFLGRRDGQV 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 385 ISGGENIYPAQIEEVLLSHPMVAEAGVVGMTDDKWGQVPAAFVVKNG--EVTEEEIIHFCEEKLAKYKVPKKACFLEELP 462
Cdd:cd12114 386 KVRGYRIELGEIEAALQAHPGVARAVVVVLGDPGGKRLAAFVVPDNDgtPIAPDALRAFLAQTLPAYMIPSRVIALEALP 465
|
490
....*....|..
gi 446371684 463 RNASKKLLRREL 474
Cdd:cd12114 466 LTANGKVDRAAL 477
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
5-474 |
1.24e-42 |
|
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: 157.82 E-value: 1.24e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 5 PNWLKQRAFLTPDRTAIEIEEEKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNT 84
Cdd:cd17646 1 HALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 85 RLSREELLWQMDDAEVVCLVTDQqfDANDVPVysfAEVMHGLKVEASIQEEFSLEEAMT--------IIYTSGTTGKPKG 156
Cdd:cd17646 81 GYPADRLAYMLADAGPAVVLTTA--DLAARLP---AGGDVALLGDEALAAPPATPPLVPprpdnlayVIYTSGSTGRPKG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 157 VILTYGnhwasAVGSSL-----NLGLRDDDCWLACMPM-FHVGGLSLLMKnIMYGMRILLVP---KYDADFIHKALQTRG 227
Cdd:cd17646 156 VMVTHA-----GIVNRLlwmqdEYPLGPGDRVLQKTPLsFDVSVWELFWP-LVAGARLVVARpggHRDPAYLAALIREHG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 228 VTIISVVSKMLTDLLERLGEETYPSsLRCMLLGGGPAPKPLLETCVDK-GIPVYQTYGMTETSSQI--CTLSADYMLTKV 304
Cdd:cd17646 230 VTTCHFVPSMLRVFLAEPAAGSCAS-LRRVFCSGEALPPELAARFLALpGAELHNLYGPTEAAIDVthWPVRGPAETPSV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 305 gSAGKPLFQCQLRI-EKDGVVVPPLVEGEIVVKGPNVTGGYFNREDATRETIQNGWL-------HTGDLGYLDEEGFLYV 376
Cdd:cd17646 309 -PIGRPVPNTRLYVlDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPFgpgsrmyRTGDLARWRPDGALEF 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 377 LDRRSDLIISGGENIYPAQIEEVLLSHPMVAEAGVVGMTDDKWGQVPAAFVV---KNGEVTEEEIIHFCEEKLAKYKVPK 453
Cdd:cd17646 388 LGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVpaaGAAGPDTAALRAHLAERLPEYMVPA 467
|
490 500
....*....|....*....|.
gi 446371684 454 KACFLEELPRNASKKLLRREL 474
Cdd:cd17646 468 AFVVLDALPLTANGKLDRAAL 488
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
139-468 |
1.53e-42 |
|
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: 154.46 E-value: 1.53e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 139 EEAMTIIYTSGTTGKPKGVILTYGNHWASAVGSSL------------------NLGLRdddcWLACMPMFHVGGLSLLMK 200
Cdd:cd05924 3 ADDLYILYTGGTTGMPKGVMWRQEDIFRMLMGGADfgtgeftpsedahkaaaaAAGTV----MFPAPPLMHGTGSWTAFG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 201 NIMYGMRILLV-PKYDADFIHKALQTRGVTIISVVSK-MLTDLLERL-GEETYP-SSLRCMLLGGGPAPKPLLETCVD-- 274
Cdd:cd05924 79 GLLGGQTVVLPdDRFDPEEVWRTIEKHKVTSMTIVGDaMARPLIDALrDAGPYDlSSLFAISSGGALLSPEVKQGLLElv 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 275 KGIPVYQTYGMTETSSQIcTLSADYMLTKVGSAGKPLFQCQLrIEKDGVVVPPL--VEGEIVVKGpNVTGGYFNREDATR 352
Cdd:cd05924 159 PNITLVDAFGSSETGFTG-SGHSAGSGPETGPFTRANPDTVV-LDDDGRVVPPGsgGVGWIARRG-HIPLGYYGDEAKTA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 353 ETIQ--NG--WLHTGDLGYLDEEGFLYVLDRRSDLIISGGENIYPAQIEEVLLSHPMVAEAGVVGMTDDKWGQVPAAfVV 428
Cdd:cd05924 236 ETFPevDGvrYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQEVVA-VV 314
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 446371684 429 K---NGEVTEEEIIHFCEEKLAKYKVPKKACFLEELPRNASKK 468
Cdd:cd05924 315 QlreGAGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
10-474 |
1.57e-42 |
|
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: 157.49 E-value: 1.57e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 10 QRAFLTPDRTAIEIEEEKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSRE 89
Cdd:cd17655 5 EQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 90 ELLWQMDDAEVVCLVTDQQFDANDvpvySFAEVMHGLKVEA-SIQEEFSLEEAMT------IIYTSGTTGKPKGVILTYG 162
Cdd:cd17655 85 RIQYILEDSGADILLTQSHLQPPI----AFIGLIDLLDEDTiYHEESENLEPVSKsddlayVIYTSGSTGKPKGVMIEHR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 163 N--HWASAVGSSLNLGLRDDdcwlacMPMFHVGGLSLLMKNI----MYGMRILLVPKYDADFIHKALQTRGVTIISVVS- 235
Cdd:cd17655 161 GvvNLVEWANKVIYQGEHLR------VALFASISFDASVTEIfaslLSGNTLYIVRKETVLDGQALTQYIRQNRITIIDl 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 236 -----KMLTDllERLGEEtypSSLRCMLLGGGPAPKPLLETCVDK---GIPVYQTYGMTETSSQICTLSADYMLTKVGSA 307
Cdd:cd17655 235 tpahlKLLDA--ADDSEG---LSLKHLIVGGEALSTELAKKIIELfgtNPTITNAYGPTETTVDASIYQYEPETDQQVSV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 308 --GKPLFQCQLRI-EKDGVVVPPLVEGEIVVKGPNVTGGYFNREDATRET-IQNGWL------HTGDLGYLDEEGFLYVL 377
Cdd:cd17655 310 piGKPLGNTRIYIlDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKfVDDPFVpgermyRTGDLARWLPDGNIEFL 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 378 DRRSDLIISGGENIYPAQIEEVLLSHPMVAEAGVVGMTDDKWGQVPAAFVVKNGEVTEEEIIHFCEEKLAKYKVPkkACF 457
Cdd:cd17655 390 GRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEKELPVAQLREFLARELPDYMIP--SYF 467
|
490
....*....|....*....
gi 446371684 458 --LEELPRNASKKLLRREL 474
Cdd:cd17655 468 ikLDEIPLTPNGKVDRKAL 486
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
16-474 |
2.66e-42 |
|
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: 155.49 E-value: 2.66e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 16 PDRTAIEIEEEKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSREELLWQM 95
Cdd:cd17652 1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 96 DDAEVVCLVTdqqfdandvpvysfaevmhglkveasiqeefSLEEAMTIIYTSGTTGKPKGVILTYGNHWASAVGSSLNL 175
Cdd:cd17652 81 ADARPALLLT-------------------------------TPDNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQIAAF 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 176 GLRDDDCWLACM-PMFHVGGLSLLMKnIMYGMRILLVPKYDADF---IHKALQTRGVTIISvvskMLTDLLERLGEETYP 251
Cdd:cd17652 130 DVGPGSRVLQFAsPSFDASVWELLMA-LLAGATLVLAPAEELLPgepLADLLREHRITHVT----LPPAALAALPPDDLP 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 252 sSLRCMLLGGGPAPKPLLETCVdKGIPVYQTYGMTETssqicTLSADYMLTKVGSA----GKPLFQCQLRIEKDGV-VVP 326
Cdd:cd17652 205 -DLRTLVVAGEACPAELVDRWA-PGRRMINAYGPTET-----TVCATMAGPLPGGGvppiGRPVPGTRVYVLDARLrPVP 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 327 PLVEGEIVVKGPNVTGGYFNREDATRET-IQN------GWLH-TGDLGYLDEEGFLYVLDRRSDLIISGGENIYPAQIEE 398
Cdd:cd17652 278 PGVPGELYIAGAGLARGYLNRPGLTAERfVADpfgapgSRMYrTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEA 357
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446371684 399 VLLSHPMVAEAGVVGMTDDKWGQVPAAFVVKNGE--VTEEEIIHFCEEKLAKYKVPKKACFLEELPRNASKKLLRREL 474
Cdd:cd17652 358 ALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAPGaaPTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
1-413 |
1.69e-41 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 155.44 E-value: 1.69e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 1 METMPN---WLKQRAFLTPDRTAI----------EIEEEKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMIT 67
Cdd:PRK09274 2 MASMANiarHLPRAAQERPDQLAVavpggrgadgKLAYDELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 68 VIHALSYVGAVAVLLN-------------------------TRLSREELLWQMDDAEVVCLVTDQQFdandVPVYSFAEV 122
Cdd:PRK09274 82 LTFALFKAGAVPVLVDpgmgiknlkqclaeaqpdafigipkAHLARRLFGWGKPSVRRLVTVGGRLL----WGGTTLATL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 123 MHGLKVEASIQEEFSLEEAMTIIYTSGTTGKPKGVILTYGNHWA--SAVGSSLnlGLRDDDCWLACMPMFHVGGLSLLMK 200
Cdd:PRK09274 158 LRDGAAAPFPMADLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAqiEALREDY--GIEPGEIDLPTFPLFALFGPALGMT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 201 NImygmrillVPKYDA--------DFIHKALQTRGVTIISVVSKmltdLLERLGEE------TYPSsLRCMLLGGGPAPK 266
Cdd:PRK09274 236 SV--------IPDMDPtrpatvdpAKLFAAIERYGVTNLFGSPA----LLERLGRYgeangiKLPS-LRRVISAGAPVPI 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 267 PLLETC---VDKGIPVYQTYGMTEtSSQICTLSADYMLTKVGSA---------GKPLFQCQLRI----------EKDGVV 324
Cdd:PRK09274 303 AVIERFramLPPDAEILTPYGATE-ALPISSIESREILFATRAAtdngagicvGRPVDGVEVRIiaisdapipeWDDALR 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 325 VPPLVEGEIVVKGPNVTGGYFNREDATRET-IQNG----WLHTGDLGYLDEEGFLYVLDRRSDLIISGGENIYPAQIEEV 399
Cdd:PRK09274 382 LATGEIGEIVVAGPMVTRSYYNRPEATRLAkIPDGqgdvWHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERI 461
|
490
....*....|....
gi 446371684 400 LLSHPMVAEAGVVG 413
Cdd:PRK09274 462 FNTHPGVKRSALVG 475
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
29-476 |
1.96e-41 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 153.44 E-value: 1.96e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 29 TFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSRE--ELLWQMDDAEVVclVTD 106
Cdd:cd05973 2 TFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKaiEHRLRTSGARLV--VTD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 107 qqfdandvpvysfAEVMHGLKveasiqeefslEEAMTIIYTSGTTGKPKGV------ILTYGNHWASAVGsslnlgLRDD 180
Cdd:cd05973 80 -------------AANRHKLD-----------SDPFVMMFTSGTTGLPKGVpvplraLAAFGAYLRDAVD------LRPE 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 181 DC-WLACMPMFHVGGLSLLMKNIMYGMRILLvpkYDADFihkalqtrgvtiiSVVSKMltDLLERLGEETY---PSSLRC 256
Cdd:cd05973 130 DSfWNAADPGWAYGLYYAITGPLALGHPTIL---LEGGF-------------SVESTW--RVIERLGVTNLagsPTAYRL 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 257 MLLGGGPAP--------------KPLLETCVD-----KGIPVYQTYGMTETSSQICTLSADYMLTKVGSAGKPL--FQCQ 315
Cdd:cd05973 192 LMAAGAEVParpkgrlrrvssagEPLTPEVIRwfdaaLGVPIHDHYGQTELGMVLANHHALEHPVHAGSAGRAMpgWRVA 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 316 LrIEKDGVVVPPLVEGEIVV---KGPNVT-GGYFNREDATretIQNGWLHTGDLGYLDEEGFLYVLDRRSDLIISGGENI 391
Cdd:cd05973 272 V-LDDDGDELGPGEPGRLAIdiaNSPLMWfRGYQLPDTPA---IDGGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRI 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 392 YPAQIEEVLLSHPMVAEAGVVGMTDDKWGQVPAAFVV-KNG----EVTEEEIIHFCEEKLAKYKVPKKACFLEELPRNAS 466
Cdd:cd05973 348 GPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVlRGGhegtPALADELQLHVKKRLSAHAYPRTIHFVDELPKTPS 427
|
490
....*....|
gi 446371684 467 KKLLRRELRQ 476
Cdd:cd05973 428 GKIQRFLLRR 437
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
29-471 |
2.03e-41 |
|
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: 155.45 E-value: 2.03e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 29 TFLQLHEKVVSVCEHLTHVGVKR--GQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSREELLWQMDDAEVVCLVTD 106
Cdd:cd05927 7 SYKEVAERADNIGSALRSLGGKPapASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVFCD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 107 qqfdaNDVPVYSFAEVMhglKVEASIQEEFSL---EEAMTIIYTSGTTGKPKGVILTYGNhWASAVgSSLNLGLRD---- 179
Cdd:cd05927 87 -----AGVKVYSLEEFE---KLGKKNKVPPPPpkpEDLATICYTSGTTGNPKGVMLTHGN-IVSNV-AGVFKILEIlnki 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 180 --DDCWLACMPMFH----------------VGGLSLLMKNIMYGMRIL------LVPK-----YDAdfIHKALQTRGV-- 228
Cdd:cd05927 157 npTDVYISYLPLAHifervvealflyhgakIGFYSGDIRLLLDDIKALkptvfpGVPRvlnriYDK--IFNKVQAKGPlk 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 229 -----TIISVVSKMLT----------DLL------ERLGeetypSSLRCMLLGGGPAPKPLLETC-VDKGIPVYQTYGMT 286
Cdd:cd05927 235 rklfnFALNYKLAELRsgvvraspfwDKLvfnkikQALG-----GNVRLMLTGSAPLSPEVLEFLrVALGCPVLEGYGQT 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 287 ETSSQIC-TLSADymlTKVGSAGKPLFQCQLRIekdgVVVP--------PLVEGEIVVKGPNVTGGYFNREDATRETI-Q 356
Cdd:cd05927 310 ECTAGATlTLPGD---TSVGHVGGPLPCAEVKL----VDVPemnydakdPNPRGEVCIRGPNVFSGYYKDPEKTAEALdE 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 357 NGWLHTGDLGYLDEEGFLYVLDRRSDLI-ISGGENIYPAQIEEVLLSHPMVAEAGVVGmtdDKWGQVPAAFVVKNGEV-- 433
Cdd:cd05927 383 DGWLHTGDIGEWLPNGTLKIIDRKKNIFkLSQGEYVAPEKIENIYARSPFVAQIFVYG---DSLKSFLVAIVVPDPDVlk 459
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 446371684 434 ---TEEEIIHFCEEKLAKYKVPKKAcFLEELPRNASKKLLR 471
Cdd:cd05927 460 ewaASKGGGTGSFEELCKNPEVKKA-ILEDLVRLGKENGLK 499
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
7-475 |
2.10e-41 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 157.12 E-value: 2.10e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 7 WLKQRAFLTPDrtaieieeeKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRL 86
Cdd:PRK06060 19 WYDRPAFYAAD---------VVTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 87 SREELLWQMDDAEVVCLVTD----QQFDANDV--PVYSFAEVMhglKVEASIQEEFSLEEAMTIIYTSGTTGKPKGVILT 160
Cdd:PRK06060 90 HRDDHALAARNTEPALVVTSdalrDRFQPSRVaeAAELMSEAA---RVAPGGYEPMGGDALAYATYTSGTTGPPKAAIHR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 161 YGNHWASAVGSSLN-LGLRDDDCWLACMPMFHVGGL-SLLMKNIMYGMRILLVPKYDADFIHKALQTR-GVTIISVVSKM 237
Cdd:PRK06060 167 HADPLTFVDAMCRKaLRLTPEDTGLCSARMYFAYGLgNSVWFPLATGGSAVINSAPVTPEAAAILSARfGPSVLYGVPNF 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 238 LTDLLERLGEETYpSSLRCMLLGGGPAPKPLLETCVD--KGIPVYQTYGMTETSSQICTLSADYMltKVGSAGKPLFQCQ 315
Cdd:PRK06060 247 FARVIDSCSPDSF-RSLRCVVSAGEALELGLAERLMEffGGIPILDGIGSTEVGQTFVSNRVDEW--RLGTLGRVLPPYE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 316 LRI-EKDGVVVPPLVEGEIVVKGPNVTGGYFNREDATREtiQNGWLHTGDLGYLDEEGFLYVLDRRSDLIISGGENIYPA 394
Cdd:PRK06060 324 IRVvAPDGTTAGPGVEGDLWVRGPAIAKGYWNRPDSPVA--NEGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPR 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 395 QIEEVLLSHPMVAEAGVVGMTDDKWGQVPAAFVV-KNGEVTEEEIIHFCEEK----LAKYKVPKKACFLEELPRNASKKL 469
Cdd:PRK06060 402 EVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVaTSGATIDGSVMRDLHRGllnrLSAFKVPHRFAVVDRLPRTPNGKL 481
|
....*.
gi 446371684 470 LRRELR 475
Cdd:PRK06060 482 VRGALR 487
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
16-475 |
2.44e-41 |
|
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: 153.29 E-value: 2.44e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 16 PDRTAIEIEEEKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSREELLWQM 95
Cdd:cd17649 1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 96 DDAEVVCLVTDqqfdandvpvysfaevmHGlkveasiqeefslEEAMTIIYTSGTTGKPKGVILTYGNHWASAVGSSLNL 175
Cdd:cd17649 81 EDSGAGLLLTH-----------------HP-------------RQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAERY 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 176 GLRDDDCWLACMPMFHVGGLSLLMKNIMYGMRILLVPK---YDADFIHKALQTRGVTIISVVSKMLTDLLERLGEETY-- 250
Cdd:cd17649 131 GLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDelwASADELAEMVRELGVTVLDLPPAYLQQLAEEADRTGDgr 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 251 PSSLRCMLLGG-GPAPKPLLETCvdkGIPVY--QTYGMTET--SSQICTLSADymLTKVGSA---GKPLFQCQLRI-EKD 321
Cdd:cd17649 211 PPSLRLYIFGGeALSPELLRRWL---KAPVRlfNAYGPTEAtvTPLVWKCEAG--AARAGASmpiGRPLGGRSAYIlDAD 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 322 GVVVPPLVEGEIVVKGPNVTGGYFNREDATRET-IQNG-------WLHTGDLGYLDEEGFLYVLDRRSDLIISGGENIYP 393
Cdd:cd17649 286 LNPVPVGVTGELYIGGEGLARGYLGRPELTAERfVPDPfgapgsrLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIEL 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 394 AQIEEVLLSHPMVAEAGVVGMTDDKWGQVpAAFVV----KNGEVTEEEIIHFCEEKLAKYKVPKKACFLEELPRNASKKL 469
Cdd:cd17649 366 GEIEAALLEHPGVREAAVVALDGAGGKQL-VAYVVlraaAAQPELRAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKL 444
|
....*.
gi 446371684 470 LRRELR 475
Cdd:cd17649 445 DRKALP 450
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
15-475 |
3.46e-41 |
|
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: 155.73 E-value: 3.46e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 15 TPDRTAIEIEEEK-----VTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSRE 89
Cdd:cd05968 74 TRTRPALRWEGEDgtsrtLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 90 ELLWQMDDAEVVCLVTDQQFDANDVPV------------------------------------YSFAEVMHGLKVEAsiq 133
Cdd:cd05968 154 AAATRLQDAEAKALITADGFTRRGREVnlkeeadkacaqcptvekvvvvrhlgndftpakgrdLSYDEEKETAGDGA--- 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 134 EEFSLEEAMTIIYTSGTTGKPKGVILTYGN---HWASAVGSSLNLGLRDDDCWLACM-----PMFHVGGLSLLMKNIMY- 204
Cdd:cd05968 231 ERTESEDPLMIIYTSGTTGKPKGTVHVHAGfplKAAQDMYFQFDLKPGDLLTWFTDLgwmmgPWLIFGGLILGATMVLYd 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 205 GmrillVPKYD-ADFIHKALQTRGVTIISVvSKMLTDLLERLGEETYP----SSLRCMLLGGGP-APKP---LLETCVDK 275
Cdd:cd05968 311 G-----APDHPkADRLWRMVEDHEITHLGL-SPTLIRALKPRGDAPVNahdlSSLRVLGSTGEPwNPEPwnwLFETVGKG 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 276 GIPVYQTYGMTETSSQICtlsADYMLtkvgsagKPLFQCQLR----------IEKDGVVVPPLVeGEIVVKGP--NVTGG 343
Cdd:cd05968 385 RNPIINYSGGTEISGGIL---GNVLI-------KPIKPSSFNgpvpgmkadvLDESGKPARPEV-GELVLLAPwpGMTRG 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 344 YFNREDATRET----IQNGWLHtGDLGYLDEEGFLYVLDRRSDLIISGGENIYPAQIEEVLLSHPMVAEAGVVGMTDDKW 419
Cdd:cd05968 454 FWRDEDRYLETywsrFDNVWVH-GDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVK 532
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446371684 420 GQVPAAFVV-----KNGEVTEEEIIHFCEEKLAKYKVPKKACFLEELPRNASKKLLRRELR 475
Cdd:cd05968 533 GEAIVCFVVlkpgvTPTEALAEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIR 593
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
55-475 |
3.47e-41 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 154.41 E-value: 3.47e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 55 VAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSREELLWQMDDAEVVCLVTDQQ-------FDANDVPVY-----SFAEV 122
Cdd:PRK13388 55 VGVLLGNTPEMLFWLAAAALGGYVLVGLNTTRRGAALAADIRRADCQLLVTDAEhrplldgLDLPGVRVLdvdtpAYAEL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 123 MHGlKVEASIQEEFSLEEAMTIIYTSGTTGKPKGVILTYGNHWASAVGSSLNLGL-RDDDCWLaCMPMFHVGG-LSLLMK 200
Cdd:PRK13388 135 VAA-AGALTPHREVDAMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLtRDDVCYV-SMPLFHSNAvMAGWAP 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 201 NIMYGMRILLVPKYDADFIHKALQTRGVTIISVVSKMLTDLL---ERLGEETYPssLRcMLLGGGPAPKPLLETCVDKGI 277
Cdd:PRK13388 213 AVASGAAVALPAKFSASGFLDDVRRYGATYFNYVGKPLAYILatpERPDDADNP--LR-VAFGNEASPRDIAEFSRRFGC 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 278 PVYQTYGMTETSSQIcTLSADymlTKVGSAGKP-----------LFQCQL-RIEKDGVVV-PPLVEGEIVVK-GPNVTGG 343
Cdd:PRK13388 290 QVEDGYGSSEGAVIV-VREPG---TPPGSIGRGapgvaiynpetLTECAVaRFDAHGALLnADEAIGELVNTaGAGFFEG 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 344 YFNREDATRETIQNGWLHTGDLGYLDEEGFLYVLDRRSDLIISGGENIYPAQIEEVLLSHPMVAEAGVVGMTDDKWG-QV 422
Cdd:PRK13388 366 YYNNPEATAERMRHGMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVGdQV 445
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 446371684 423 PAAFVVKNGE-VTEEEIIHF--CEEKLAKYKVPKKACFLEELPRNASKKLLRRELR 475
Cdd:PRK13388 446 MAALVLRDGAtFDPDAFAAFlaAQPDLGTKAWPRYVRIAADLPSTATNKVLKRELI 501
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
55-475 |
3.73e-41 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 154.45 E-value: 3.73e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 55 VAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSREELLWQMDDAEVVCLVTDQQF------DANDVPVYSFAEVMHGLKV 128
Cdd:PRK07867 57 VGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARDIAHADCQLVLTESAHaelldgLDPGVRVINVDSPAWADEL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 129 EASIQEEFSLEEA-----MTIIYTSGTTGKPKGVILTYGNhWASAvGSSL--NLGLRDDDCWLACMPMFH----VGGLSL 197
Cdd:PRK07867 137 AAHRDAEPPFRVAdpddlFMLIFTSGTSGDPKAVRCTHRK-VASA-GVMLaqRFGLGPDDVCYVSMPLFHsnavMAGWAV 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 198 LMKNimyGMRILLVPKYDADFIHKALQTRGVTIISVVSKMLTDLL---ERLGEETYPssLRcMLLGGGPAPKPLLETCVD 274
Cdd:PRK07867 215 ALAA---GASIALRRKFSASGFLPDVRRYGATYANYVGKPLSYVLatpERPDDADNP--LR-IVYGNEGAPGDIARFARR 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 275 KGIPVYQTYGMTETSSQIcTLSADymlTKVGSAGKPLFQCQL------------RIEKDGVVVPPLVEGEIV-VKGPNVT 341
Cdd:PRK07867 289 FGCVVVDGFGSTEGGVAI-TRTPD---TPPGALGPLPPGVAIvdpdtgtecppaEDADGRLLNADEAIGELVnTAGPGGF 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 342 GGYFNREDATRETIQNGWLHTGDLGYLDEEGFLYVLDRRSDLIISGGENIYPAQIEEVLLSHPMVAEAGVVGMTDDKWG- 420
Cdd:PRK07867 365 EGYYNDPEADAERMRGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGd 444
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 446371684 421 QVPAAFVVKNG-EVTEEEIIHFCEEK--LAKYKVPKKACFLEELPRNASKKLLRRELR 475
Cdd:PRK07867 445 QVMAALVLAPGaKFDPDAFAEFLAAQpdLGPKQWPSYVRVCAELPRTATFKVLKRQLS 502
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
9-476 |
3.95e-41 |
|
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: 152.46 E-value: 3.95e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 9 KQRAFLTPDRTAIEIEEEKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSR 88
Cdd:cd17653 4 ERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 89 EELLWQMDDAEVVCLVTDqqfDANDVPVYsfaevmhglkveasiqeefsleeamtIIYTSGTTGKPKGVILTYGN--HWA 166
Cdd:cd17653 84 ARIQAILRTSGATLLLTT---DSPDDLAY--------------------------IIFTSGSTGIPKGVMVPHRGvlNYV 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 167 SAVGSSLNLGLRDDDCwLACMPMFHVGGLSLLmKNIMYGMRILLVpKYDADFIHKAlqtRGVTIIsvvskMLT-DLLERL 245
Cdd:cd17653 135 SQPPARLDVGPGSRVA-QVLSIAFDACIGEIF-STLCNGGTLVLA-DPSDPFAHVA---RTVDAL-----MSTpSILSTL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 246 GEETYPsSLRCMLLGGGPAPKPLLETCVdKGIPVYQTYGMTETSSqICTLSADYMLTKVgSAGKPLFQCQLRI-EKDGVV 324
Cdd:cd17653 204 SPQDFP-NLKTIFLGGEAVPPSLLDRWS-PGRRLYNAYGPTECTI-SSTMTELLPGQPV-TIGKPIPNSTCYIlDADLQP 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 325 VPPLVEGEIVVKGPNVTGGYFNREDATRE-----TIQNGWLH--TGDLGYLDEEGFLYVLDRRSDLIISGGENIYPAQIE 397
Cdd:cd17653 280 VPEGVVGEICISGVQVARGYLGNPALTASkfvpdPFWPGSRMyrTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIE 359
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446371684 398 EVLLSHPMVAEAGVVGMTDDkwgqVPAAFVVKNGeVTEEEIIHFCEEKLAKYKVPKKACFLEELPRNASKKLLRRELRQ 476
Cdd:cd17653 360 EVVLQSQPEVTQAAAIVVNG----RLVAFVTPET-VDVDGLRSELAKHLPSYAVPDRIIALDSFPLTANGKVDRKALRE 433
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
48-475 |
5.45e-41 |
|
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: 153.78 E-value: 5.45e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 48 GVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSREELLWQMDDAEVVCLVTD----QQFD--ANDVPVY---- 117
Cdd:cd05928 63 GLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSdelaPEVDsvASECPSLktkl 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 118 -----------SFAEVMHGLKVEASIQEEFSlEEAMTIIYTSGTTGKPKgviLTYGNHWASAVGSSLN----LGLRDDDC 182
Cdd:cd05928 143 lvseksrdgwlNFKELLNEASTEHHCVETGS-QEPMAIYFTSGTTGSPK---MAEHSHSSLGLGLKVNgrywLDLTASDI 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 183 -WLACMPMFHVGGLSLLMKNIMYGMRIL--LVPKYDADFIHKALQTRGVTII---SVVSKMLtdLLERLGEETYPSsLRC 256
Cdd:cd05928 219 mWNTSDTGWIKSAWSSLFEPWIQGACVFvhHLPRFDPLVILKTLSSYPITTFcgaPTVYRML--VQQDLSSYKFPS-LQH 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 257 MLLGGGPA-PKPLLETCVDKGIPVYQTYGMTETSsQICTLSADyMLTKVGSAGK--PLFQCQLrIEKDGVVVPPLVEGEI 333
Cdd:cd05928 296 CVTGGEPLnPEVLEKWKAQTGLDIYEGYGQTETG-LICANFKG-MKIKPGSMGKasPPYDVQI-IDDNGNVLPPGTEGDI 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 334 VVK-GPNVTGGYFNR----EDATRETIQNGWLHTGDLGYLDEEGFLYVLDRRSDLIISGGENIYPAQIEEVLLSHPMVAE 408
Cdd:cd05928 373 GIRvKPIRPFGLFSGyvdnPEKTAATIRGDFYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVE 452
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446371684 409 AGVVGMTDDKWGQVPAAFVV-------KNGEVTEEEIIHFCEEKLAKYKVPKKACFLEELPRNASKKLLRRELR 475
Cdd:cd05928 453 SAVVSSPDPIRGEVVKAFVVlapqflsHDPEQLTKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNELR 526
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
26-413 |
1.33e-40 |
|
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: 152.62 E-value: 1.33e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 26 EKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSREELLWQMDDAEV-VCLV 104
Cdd:cd05932 5 VEFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESkALFV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 105 TdqQFDAND-----VP----------------VYSFAEV--MHGLKVEASIQEEfslEEAMTIIYTSGTTGKPKGVILTY 161
Cdd:cd05932 85 G--KLDDWKamapgVPeglisislpppsaancQYQWDDLiaQHPPLEERPTRFP---EQLATLIYTSGTTGQPKGVMLTF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 162 GNH-WASAVGSSLnLGLRDDDCWLACMPMFHVGGLSLL-MKNIMYGMRILLVPKYDAdFIHKALQTRGVTIISV------ 233
Cdd:cd05932 160 GSFaWAAQAGIEH-IGTEENDRMLSYLPLAHVTERVFVeGGSLYGGVLVAFAESLDT-FVEDVQRARPTLFFSVprlwtk 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 234 -----VSKMLTDLLERLGEETYPSSL------------RCMLLGGGPAPKP--LLETCVDKGIPVYQTYGMTETS--SQI 292
Cdd:cd05932 238 fqqgvQDKIPQQKLNLLLKIPVVNSLvkrkvlkglgldQCRLAGCGSAPVPpaLLEWYRSLGLNILEAYGMTENFaySHL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 293 CTLSADymltKVGSAGKPLFQCQLRIEKDgvvvpplveGEIVVKGPNVTGGYFNREDATRETI-QNGWLHTGDLGYLDEE 371
Cdd:cd05932 318 NYPGRD----KIGTVGNAGPGVEVRISED---------GEILVRSPALMMGYYKDPEATAEAFtADGFLRTGDKGELDAD 384
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 446371684 372 GFLYVLDRRSDLI-ISGGENIYPAQIEEVLLSHPMVAEAGVVG 413
Cdd:cd05932 385 GNLTITGRVKDIFkTSKGKYVAPAPIENKLAEHDRVEMVCVIG 427
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
10-475 |
3.33e-40 |
|
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: 150.96 E-value: 3.33e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 10 QRAFLTPDRTAIEIEEEKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSRE 89
Cdd:cd17651 3 RQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 90 ELLWQMDDAEVVCLVTDQ--QFDANDVPVYSFAEVMHGL--KVEASIQEEFSLEEAMTIIYTSGTTGKPKGVILTYGNhW 165
Cdd:cd17651 83 RLAFMLADAGPVLVLTHPalAGELAVELVAVTLLDQPGAaaGADAEPDPALDADDLAYVIYTSGSTGRPKGVVMPHRS-L 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 166 ASAVG---SSLNLGLRDDDCWLAcMPMFHVGGLSLLmKNIMYGMRILLVP---KYDADFIHKALQTRGVTIISVVSKMLT 239
Cdd:cd17651 162 ANLVAwqaRASSLGPGARTLQFA-GLGFDVSVQEIF-STLCAGATLVLPPeevRTDPPALAAWLDEQRISRVFLPTVALR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 240 DLLERLGEE-TYPSSLRCMLLGGGPAP-KPLL-ETCVDK-GIPVYQTYGMTETSSQIC-TLSADYML-TKVGSAGKPLFQ 313
Cdd:cd17651 240 ALAEHGRPLgVRLAALRYLLTGGEQLVlTEDLrEFCAGLpGLRLHNHYGPTETHVVTAlSLPGDPAAwPAPPPIGRPIDN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 314 CQLRI-EKDGVVVPPLVEGEIVVKGPNVTGGYFNREDATRET-IQNGWL------HTGDLGYLDEEGFLYVLDRRSDLII 385
Cdd:cd17651 320 TRVYVlDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERfVPDPFVpgarmyRTGDLARWLPDGELEFLGRADDQVK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 386 SGGENIYPAQIEEVLLSHPMVAEAGVVGMTDDKWGQVPAAFVV--KNGEVTEEEIIHFCEEKLAKYKVPKKACFLEELPR 463
Cdd:cd17651 400 IRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVgdPEAPVDAAELRAALATHLPEYMVPSAFVLLDALPL 479
|
490
....*....|..
gi 446371684 464 NASKKLLRRELR 475
Cdd:cd17651 480 TPNGKLDRRALP 491
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
10-481 |
2.82e-39 |
|
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: 148.07 E-value: 2.82e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 10 QRAFLTPDRTAIEIEEEKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRL--S 87
Cdd:cd05918 7 ERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLDPSHplQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 88 REELLWQMDDAEVVclVTDQQFDAndvpvysfaevmhglkveasiqeefsleeaMTIIYTSGTTGKPKGVILTYGNHWAS 167
Cdd:cd05918 87 RLQEILQDTGAKVV--LTSSPSDA------------------------------AYVIFTSGSTGKPKGVVIEHRALSTS 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 168 AVGSSLNLGLRDDDCWLA-CMPMFhvgGLSLLmkNIMYGMRI---LLVPKYD------ADFIhkalQTRGVTIISVVSKM 237
Cdd:cd05918 135 ALAHGRALGLTSESRVLQfASYTF---DVSIL--EIFTTLAAggcLCIPSEEdrlndlAGFI----NRLRVTWAFLTPSV 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 238 LtDLLERlgeETYPSsLRCMLLGGGPAPKPLLETCVDKgIPVYQTYGMTETSsqI-CTLSADYMLTKVGSAGKPlFQCQL 316
Cdd:cd05918 206 A-RLLDP---EDVPS-LRTLVLGGEALTQSDVDTWADR-VRLINAYGPAECT--IaATVSPVVPSTDPRNIGRP-LGATC 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 317 RI---EKDGVVVPPLVEGEIVVKGPNVTGGYFNREDATRET-IQN-GWLH------------TGDLGYLDEEGFLYVLDR 379
Cdd:cd05918 277 WVvdpDNHDRLVPIGAVGELLIEGPILARGYLNDPEKTAAAfIEDpAWLKqegsgrgrrlyrTGDLVRYNPDGSLEYVGR 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 380 RSDLIISGGENIYPAQIEEVLLSHP---MVAEAGVVGMTDDKWGQVPAAFVVKNGEVTE-------------------EE 437
Cdd:cd05918 357 KDTQVKIRGQRVELGEIEHHLRQSLpgaKEVVVEVVKPKDGSSSPQLVAFVVLDGSSSGsgdgdslflepsdefralvAE 436
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 446371684 438 IIHFCEEKLAKYKVPKKACFLEELPRNASKKLLRRELRQLVEEM 481
Cdd:cd05918 437 LRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRALRELAESL 480
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
26-413 |
6.24e-39 |
|
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: 149.04 E-value: 6.24e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 26 EKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGME-MITVIHALsYVGAVAVLLNTRLSREELLWQMDDAEV-VCL 103
Cdd:cd05933 7 HTLTYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEwFIAAVGAI-FAGGIAVGIYTTNSPEACQYVAETSEAnILV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 104 VTDQQ------------------------FDANDVPVYSFAEVMHGLKVEASIQEEFSLE-----EAMTIIYTSGTTGKP 154
Cdd:cd05933 86 VENQKqlqkilqiqdklphlkaiiqykepLKEKEPNLYSWDEFMELGRSIPDEQLDAIISsqkpnQCCTLIYTSGTTGMP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 155 KGVILTYGN-HW-ASAVGSSLNLGLRDD-------------------DCWLacmPMFHVGGLSLLMKNIMYG-------- 205
Cdd:cd05933 166 KGVMLSHDNiTWtAKAASQHMDLRPATVgqesvvsylplshiaaqilDIWL---PIKVGGQVYFAQPDALKGtlvktlre 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 206 ---MRILLVPKydadfIHKALQTRGVTIIS---VVSKMLTDLLERLGEETY--------PSSL----------------- 254
Cdd:cd05933 243 vrpTAFMGVPR-----VWEKIQEKMKAVGAksgTLKRKIASWAKGVGLETNlklmggesPSPLfyrlakklvfkkvrkal 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 255 ---RCMLL--GGGPAPKPLLETCVDKGIPVYQTYGMTETSSQIcTLSADYMLTkVGSAGKPLFQCQLRIEK---DGVvvp 326
Cdd:cd05933 318 gldRCQKFftGAAPISRETLEFFLSLNIPIMELYGMSETSGPH-TISNPQAYR-LLSCGKALPGCKTKIHNpdaDGI--- 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 327 plveGEIVVKGPNVTGGYFNREDATRETI-QNGWLHTGDLGYLDEEGFLYVLDRRSDLII-SGGENIYPAQIEE-VLLSH 403
Cdd:cd05933 393 ----GEICFWGRHVFMGYLNMEDKTEEAIdEDGWLHSGDLGKLDEDGFLYITGRIKELIItAGGENVPPVPIEDaVKKEL 468
|
490
....*....|
gi 446371684 404 PMVAEAGVVG 413
Cdd:cd05933 469 PIISNAMLIG 478
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
24-412 |
4.01e-37 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 143.21 E-value: 4.01e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 24 EEEKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSREEL-LWQMDDAEVVC 102
Cdd:PRK07768 26 APVRHTWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASLTMLHQPTPRTDLaVWAEDTLRVIG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 103 LVtdqqfDANDV----PVYSFAEVM--HGLKV--------EASIQEEFSLEEAMTII-YTSGTTGKPKGVILTYGNHWAS 167
Cdd:PRK07768 106 MI-----GAKAVvvgePFLAAAPVLeeKGIRVltvadllaADPIDPVETGEDDLALMqLTSGSTGSPKAVQITHGNLYAN 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 168 AVGSSLNLGLR-DDDCWLACMPMFH----VGGLSLLMKnimYGMRILLV-PkydADFIHKAL-------QTRGvTII--- 231
Cdd:PRK07768 181 AEAMFVAAEFDvETDVMVSWLPLFHdmgmVGFLTVPMY---FGAELVKVtP---MDFLRDPLlwaelisKYRG-TMTaap 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 232 ----SVVSKmltdLLERLGEE-TYP-SSLRCMLLGGGPAPKPLLETCVDKGIP-------VYQTYGMTETSSQI------ 292
Cdd:PRK07768 254 nfayALLAR----RLRRQAKPgAFDlSSLRFALNGAEPIDPADVEDLLDAGARfglrpeaILPAYGMAEATLAVsfspcg 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 293 -----CTLSADyMLTKVGSA--------------GKPLFQCQLRI-EKDGVVVPPLVEGEIVVKGPNVTGGYFNREDATR 352
Cdd:PRK07768 330 aglvvDEVDAD-LLAALRRAvpatkgntrrlatlGPPLPGLEVRVvDEDGQVLPPRGVGVIELRGESVTPGYLTMDGFIP 408
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 353 ETIQNGWLHTGDLGYLDEEGFLYVLDRRSDLIISGGENIYPAQIEEVLLSHPMVAEAGVV 412
Cdd:PRK07768 409 AQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVRPGNAV 468
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
32-474 |
5.66e-37 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 142.84 E-value: 5.66e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 32 QLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSREEL--LWQMDDAEVVCLVTDQQF 109
Cdd:PRK05857 46 ELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLPIAAIerFCQITDPAAALVAPGSKM 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 110 DANDVPVYSFA-------------EVMHGLKVE-ASIQEEFSLEEAMTIIYTSGTTGKPKGVILTygNHWASAVGSSL-N 174
Cdd:PRK05857 126 ASSAVPEALHSipviavdiaavtrESEHSLDAAsLAGNADQGSEDPLAMIFTSGTTGEPKAVLLA--NRTFFAVPDILqK 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 175 LGLR-----DDDCWLACMPMFHVGGLSLLMKNIMYGMRILLVPKYDADfIHKALQTRGVTIISVVSKMLTDLLERL--GE 247
Cdd:PRK05857 204 EGLNwvtwvVGETTYSPLPATHIGGLWWILTCLMHGGLCVTGGENTTS-LLEILTTNAVATTCLVPTLLSKLVSELksAN 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 248 ETYPSsLRCMLLGGGPAPKPLLETCVDKGIPVYQTYGMTETS-SQICTLSADYMLTKV--GSAGKPLFQCQLRIEKDGVV 324
Cdd:PRK05857 283 ATVPS-LRLVGYGGSRAIAADVRFIEATGVRTAQVYGLSETGcTALCLPTDDGSIVKIeaGAVGRPYPGVDVYLAATDGI 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 325 VPPLVE-------GEIVVKGPNVTGGYFNREDATRETIQNGWLHTGDLGYLDEEGFLYVLDRRSDLIISGGENIYPAQIE 397
Cdd:PRK05857 362 GPTAPGagpsasfGTLWIKSPANMLGYWNNPERTAEVLIDGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVD 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 398 EVLLSHPMVAEAGVVGMTDDKWGQVPAAFVVKNGEVTEEEIIHFCEEKLAKYK-------VPKKACFLEELPRNASKKLL 470
Cdd:PRK05857 442 RIAEGVSGVREAACYEIPDEEFGALVGLAVVASAELDESAARALKHTIAARFRresepmaRPSTIVIVTDIPRTQSGKVM 521
|
....
gi 446371684 471 RREL 474
Cdd:PRK05857 522 RASL 525
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
16-479 |
1.19e-36 |
|
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: 142.70 E-value: 1.19e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 16 PDRTAIEIE------EEKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSRE 89
Cdd:cd05966 67 GDKVAIIWEgdepdqSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFAGFSAE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 90 ELLWQMDDAEVVCLVT-DQQF-------------DA-----------------NDVPVYS-----FAEVMHGLKVEASIq 133
Cdd:cd05966 147 SLADRINDAQCKLVITaDGGYrggkviplkeivdEAlekcpsvekvlvvkrtgGEVPMTEgrdlwWHDLMAKQSPECEP- 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 134 EEFSLEEAMTIIYTSGTTGKPKGVILTYGNHwasAVGSSLNL----GLRDDDCWlACMP--------MFHV-GGLSLLMK 200
Cdd:cd05966 226 EWMDSEDPLFILYTSGSTGKPKGVVHTTGGY---LLYAATTFkyvfDYHPDDIY-WCTAdigwitghSYIVyGPLANGAT 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 201 NIMY-GmrillVPKY-DADFIHKALQTRGVTIIsVVSKMLTDLLERLGEEtYP-----SSLRcmLLG--GGP----APKP 267
Cdd:cd05966 302 TVMFeG-----TPTYpDPGRYWDIVEKHKVTIF-YTAPTAIRALMKFGDE-WVkkhdlSSLR--VLGsvGEPinpeAWMW 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 268 LLETCVDKGIPVYQTYGMTETSSQICTLSADYMLTKVGSAGKPLFQCQLRI-EKDGVVVPPLVEGEIVVKGP------NV 340
Cdd:cd05966 373 YYEVIGKERCPIVDTWWQTETGGIMITPLPGATPLKPGSATRPFFGIEPAIlDEEGNEVEGEVEGYLVIKRPwpgmarTI 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 341 TGG-------YFNREdatretiqNGWLHTGDLGYLDEEGFLYVLDRRSDLIISGGENIYPAQIEEVLLSHPMVAEAGVVG 413
Cdd:cd05966 453 YGDheryedtYFSKF--------PGYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVG 524
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446371684 414 MTDDKWGQVPAAFVV-KNG----EVTEEEIIHFCEEKLAKYKVPKKACFLEELPRNASKKLLRRELRQLVE 479
Cdd:cd05966 525 RPHDIKGEAIYAFVTlKDGeepsDELRKELRKHVRKEIGPIATPDKIQFVPGLPKTRSGKIMRRILRKIAA 595
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
7-479 |
4.40e-36 |
|
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called acetyl-CoA synthetase and acetyl-activating enzyme. It catalyzes the reaction ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA and belongs to the family of AMP-binding enzymes described by pfam00501.
Pssm-ID: 274022 [Multi-domain] Cd Length: 626 Bit Score: 141.23 E-value: 4.40e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 7 WLKQRafltPDRTAIEIEEE------KVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAV 80
Cdd:TIGR02188 66 HLEAR----PDKVAIIWEGDepgevrKITYRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLACARIGAIHS 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 81 LLNTRLSREELLWQMDDAEVVCLVT-DQQF-------------DA------------------NDVPVYS------FAEV 122
Cdd:TIGR02188 142 VVFGGFSAEALADRINDAGAKLVITaDEGLrggkviplkaivdEAlekcpvsvehvlvvrrtgNPVVPWVegrdvwWHDL 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 123 MHGLKVEASIqEEFSLEEAMTIIYTSGTTGKPKGVILTYGNH--WASAVGSSLnLGLRDDD---C-----WLACMPMFHV 192
Cdd:TIGR02188 222 MAKASAYCEP-EPMDSEDPLFILYTSGSTGKPKGVLHTTGGYllYAAMTMKYV-FDIKDGDifwCtadvgWITGHSYIVY 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 193 GGLSLLMKNIMY-GmrillVPKY-DADFIHKALQTRGVTIIsVVSKMLTDLLERLGEETYP----SSLRcmLLG--GGP- 263
Cdd:TIGR02188 300 GPLANGATTVMFeG-----VPTYpDPGRFWEIIEKHKVTIF-YTAPTAIRALMRLGDEWVKkhdlSSLR--LLGsvGEPi 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 264 ---APKPLLETCVDKGIPVYQTYGMTETSSQICTLSADYMLTKVGSAGKPLFQCQLRI-EKDGVVVP-PLVEGEIVVKG- 337
Cdd:TIGR02188 372 npeAWMWYYKVVGKERCPIVDTWWQTETGGIMITPLPGATPTKPGSATLPFFGIEPAVvDEEGNPVEgPGEGGYLVIKQp 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 338 -PNVTGGYFNREDATRETIQN---GWLHTGDLGYLDEEGFLYVLDRRSDLIISGGENIYPAQIEEVLLSHPMVAEAGVVG 413
Cdd:TIGR02188 452 wPGMLRTIYGDHERFVDTYFSpfpGYYFTGDGARRDKDGYIWITGRVDDVINVSGHRLGTAEIESALVSHPAVAEAAVVG 531
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446371684 414 MTDDKWGQVPAAFVV-KNG----EVTEEEIIHFCEEKLAKYKVPKKACFLEELPRNASKKLLRRELRQLVE 479
Cdd:TIGR02188 532 IPDDIKGQAIYAFVTlKDGyepdDELRKELRKHVRKEIGPIAKPDKIRFVPGLPKTRSGKIMRRLLRKIAA 602
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
6-476 |
4.43e-36 |
|
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: 139.87 E-value: 4.43e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 6 NWLKQRAFLTPDRTAIEIEeekVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTR 85
Cdd:cd05915 6 ALFGRKEVVSRLHTGEVHR---TTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 86 LSREELLWQMDDAEVVCLVTDQQFDANDVPVYSFAEVMHGLKVEASIQEEFS---------------LEEA--MTIIYTS 148
Cdd:cd05915 83 LSPKEIAYILNHAEDKVLLFDPNLLPLVEAIRGELKTVQHFVVMDEKAPEGYlayeealgeeadpvrVPERaaCGMAYTT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 149 GTTGKPKGVILTYGNHW--ASAVGSSLNLGLRDDDCWLACMPMFHVGGLSLLMKNIMYGMRILLVPK-------YDADFI 219
Cdd:cd05915 163 GTTGLPKGVVYSHRALVlhSLAASLVDGTALSEKDVVLPVVPMFHVNAWCLPYAATLVGAKQVLPGPrldpaslVELFDG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 220 HKALQTRGVtiiSVVSKMLTDLLERLgEETYPSSLRCMlLGGGPAPKPLLETCVDKGIPVYQTYGMTET----------- 288
Cdd:cd05915 243 EGVTFTAGV---PTVWLALADYLEST-GHRLKTLRRLV-VGGSAAPRSLIARFERMGVEVRQGYGLTETspvvvqnfvks 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 289 ------SSQICTLSADYMLTKVGSAGKPLFQCQLRIEKDGVVVPPlvegeIVVKGPNVTGGYFNREDATR-ETIQNGWLH 361
Cdd:cd05915 318 hleslsEEEKLTLKAKTGLPIPLVRLRVADEEGRPVPKDGKALGE-----VQLKGPWITGGYYGNEEATRsALTPDGFFR 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 362 TGDLGYLDEEGFLYVLDRRSDLIISGGENIYPAQIEEVLLSHPMVAEAGVVGMTDDKWGQVPAAFV-VKNGEVTEEEIIH 440
Cdd:cd05915 393 TGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVVvPRGEKPTPEELNE 472
|
490 500 510
....*....|....*....|....*....|....*..
gi 446371684 441 FCEEKLAKYK-VPKKACFLEELPRNASKKLLRRELRQ 476
Cdd:cd05915 473 HLLKAGFAKWqLPDAYVFAEEIPRTSAGKFLKRALRE 509
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
9-474 |
1.21e-35 |
|
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: 137.30 E-value: 1.21e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 9 KQRAFLTPDRTAIEIEEEKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSR 88
Cdd:cd17645 5 EEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 89 EELLWQMDDAEVVCLVTDQqfdandvpvysfaevmhglkveasiqeefslEEAMTIIYTSGTTGKPKGVILTYGN--HWA 166
Cdd:cd17645 85 ERIAYMLADSSAKILLTNP-------------------------------DDLAYVIYTSGSTGLPKGVMIEHHNlvNLC 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 167 SAVGSSLNLGLRDDDCWLACmpmFHVGGLSL-LMKNIMYGMRILLVP---KYDADFIHKALQTRGVTIisvvSKMLTDLL 242
Cdd:cd17645 134 EWHRPYFGVTPADKSLVYAS---FSFDASAWeIFPHLTAGAALHVVPserRLDLDALNDYFNQEGITI----SFLPTGAA 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 243 ERLgEETYPSSLRCMLLGGGpapkpLLETCVDKGIPVYQTYGMTETSSQICTLSADYMLTKVgSAGKPLFQCQLRIEKDG 322
Cdd:cd17645 207 EQF-MQLDNQSLRVLLTGGD-----KLKKIERKGYKLVNNYGPTENTVVATSFEIDKPYANI-PIGKPIDNTRVYILDEA 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 323 VVVPPL-VEGEIVVKGPNVTGGYFNREDATRET-IQNGWL------HTGDLGYLDEEGFLYVLDRRSDLIISGGENIYPA 394
Cdd:cd17645 280 LQLQPIgVAGELCIAGEGLARGYLNRPELTAEKfIVHPFVpgermyRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPG 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 395 QIEEVLLSHPMVAEAGVVGMTDDKWGQVPAAFVVKNGEVTEEEIIHFCEEKLAKYKVPKKACFLEELPRNASKKLLRREL 474
Cdd:cd17645 360 EIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTAPEEIPHEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
71-481 |
1.60e-35 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 140.83 E-value: 1.60e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 71 ALSYVGAVAVLLNTRLSREELLWQMDDAEVVCLVTDQQF--------DANDVP-----VY--SFAEVMHGLK-------- 127
Cdd:PRK08633 684 ALLLAGKVPVNLNYTASEAALKSAIEQAQIKTVITSRKFleklknkgFDLELPenvkvIYleDLKAKISKVDkltallaa 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 128 -------VEASIQEEFSLEEAMTIIYTSGTTGKPKGVILTYGNHWASAVGSSLNLGLRDDDCWLACMPMFHVGGLS--LL 198
Cdd:PRK08633 764 rllparlLKRLYGPTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSSLPFFHSFGLTvtLW 843
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 199 MKNIMyGMRILLVPK-YDADFIHKALQTRGVTIISVVSKMLTDLL--ERLGEETYpSSLRCMLLGGGPAPKPLLETCVDK 275
Cdd:PRK08633 844 LPLLE-GIKVVYHPDpTDALGIAKLVAKHRATILLGTPTFLRLYLrnKKLHPLMF-ASLRLVVAGAEKLKPEVADAFEEK 921
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 276 -GIPVYQTYGMTETSSQIC-----TLSADYML---TKVGSAGKPLFQCQLRI--EKDGVVVPPLVEGEIVVKGPNVTGGY 344
Cdd:PRK08633 922 fGIRILEGYGATETSPVASvnlpdVLAADFKRqtgSKEGSVGMPLPGVAVRIvdPETFEELPPGEDGLILIGGPQVMKGY 1001
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 345 FNREDATRETIQN----GWLHTGDLGYLDEEGFLYVLDRRSDLIISGGENIYPAQIEEvLLSHPMVAEAG---VVGMTDD 417
Cdd:PRK08633 1002 LGDPEKTAEVIKDidgiGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEE-ELAKALGGEEVvfaVTAVPDE 1080
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446371684 418 KWGQvPAAFVVKNGEVTEEEII-HFCEEKLAKYKVPKKACFLEELPRNASKKLLRRELRQLVEEM 481
Cdd:PRK08633 1081 KKGE-KLVVLHTCGAEDVEELKrAIKESGLPNLWKPSRYFKVEALPLLGSGKLDLKGLKELALAL 1144
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
28-477 |
4.92e-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: 135.77 E-value: 4.92e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 28 VTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSREELLWQMDDAEVVCLVTDQ 107
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRDRVDRGGAVYAAVDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 108 QFDANDvpvysfaevmhglkveasiqeefsleeAMTIIYTSGTTGKPKGVILTYGNHWASAVGSSLNLGLRDDDC-WLAC 186
Cdd:cd05974 81 NTHADD---------------------------PMLLYFTSGTTSKPKLVEHTHRSYPVGHLSTMYWIGLKPGDVhWNIS 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 187 MPMFHVGGLSLLMKNIMYGMRILLV--PKYDADFIHKALQTRGVTII---SVVSKMLtdLLERLGeeTYPSSLRCMLLGG 261
Cdd:cd05974 134 SPGWAKHAWSCFFAPWNAGATVFLFnyARFDAKRVLAALVRYGVTTLcapPTVWRML--IQQDLA--SFDVKLREVVGAG 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 262 GPAPKPLLETcVDK--GIPVYQTYGMTETSSQICTLSADYMltKVGSAGKPLfqCQLRIEKDGVVVPPLVEGEIVV---- 335
Cdd:cd05974 210 EPLNPEVIEQ-VRRawGLTIRDGYGQTETTALVGNSPGQPV--KAGSMGRPL--PGYRVALLDPDGAPATEGEVALdlgd 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 336 -KGPNVTGGYFNREDATRETIQNGWLHTGDLGYLDEEGFLYVLDRRSDLIISGGENIYPAQIEEVLLSHPMVAEAGVVGM 414
Cdd:cd05974 285 tRPVGLMKGYAGDPDKTAHAMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPS 364
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446371684 415 TDDKWGQVPAAFVV-----KNGEVTEEEIIHFCEEKLAKYKVPKKACFLeELPRNASKKLLRRELRQL 477
Cdd:cd05974 365 PDPVRLSVPKAFIVlragyEPSPETALEIFRFSRERLAPYKRIRRLEFA-ELPKTISGKIRRVELRRR 431
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
3-441 |
1.08e-34 |
|
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: 136.26 E-value: 1.08e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 3 TMPNWLKQRAFLTPDRTAIEI----EEEKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAV 78
Cdd:cd05906 11 TLLELLLRAAERGPTKGITYIdadgSEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 79 AVLL---------NTRLSREELLWQMDDAEVVclVTDQqfdandvpvySFAEVMHGLKVEASIQE--EFSLEEAMT---- 143
Cdd:cd05906 91 PAPLtvpptydepNARLRKLRHIWQLLGSPVV--LTDA----------ELVAEFAGLETLSGLPGirVLSIEELLDtaad 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 144 -------------IIYTSGTTGKPKGVILTYGNHWASAVGSSLNLGLRDDDCWLACMPMFHVGGLsllmknIMYGMRILL 210
Cdd:cd05906 159 hdlpqsrpddlalLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVPLDHVGGL------VELHLRAVY 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 211 vpkYDADFIHKA--------------LQTRGVTIISVVSKMLTDLLERLGEETYP----SSLRCMLLGGGPAPKP----- 267
Cdd:cd05906 233 ---LGCQQVHVPteeiladplrwldlIDRYRVTITWAPNFAFALLNDLLEEIEDGtwdlSSLRYLVNAGEAVVAKtirrl 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 268 --LLETCvdkGIP---VYQTYGMTETSSQI--CTLSADYMLT---KVGSAGKPLFQCQLRI-EKDGVVVPPLVEGEIVVK 336
Cdd:cd05906 310 lrLLEPY---GLPpdaIRPAFGMTETCSGViySRSFPTYDHSqalEFVSLGRPIPGVSMRIvDDEGQLLPEGEVGRLQVR 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 337 GPNVTGGYFNREDATRETIQN-GWLHTGDLGYLDeEGFLYVLDRRSDLIISGGENIYPAQIEEVLLSHPMVAeagvVGMT 415
Cdd:cd05906 387 GPVVTKGYYNNPEANAEAFTEdGWFRTGDLGFLD-NGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVE----PSFT 461
|
490 500
....*....|....*....|....*..
gi 446371684 416 ddkwgqvpAAFVVKN-GEVTEEEIIHF 441
Cdd:cd05906 462 --------AAFAVRDpGAETEELAIFF 480
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
15-474 |
1.22e-34 |
|
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: 135.29 E-value: 1.22e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 15 TPDRTAIEIEEEKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSREELLWQ 94
Cdd:cd17656 1 TPDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 95 MDDAEVVCLVTdqQFDANDVPVYSFAEVM-------HGLkvEASIQEEFSLEEAMTIIYTSGTTGKPKGVILTYGNhwas 167
Cdd:cd17656 81 MLDSGVRVVLT--QRHLKSKLSFNKSTILledpsisQED--TSNIDYINNSDDLLYIIYTSGTTGKPKGVQLEHKN---- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 168 avgsSLNL---------GLRDDDCWLACMPMFHVGgLSLLMKNIMYGMRILLVP---KYDADFIHKALQTRGVTIISVVS 235
Cdd:cd17656 153 ----MVNLlhferektnINFSDKVLQFATCSFDVC-YQEIFSTLLSGGTLYIIReetKRDVEQLFDLVKRHNIEVVFLPV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 236 KMLTDLL-ERLGEETYPSSLRCMLLGGGP--APKPLLETCVDKGIPVYQTYGMTETS-SQICTLSADYMLTKVGSAGKPL 311
Cdd:cd17656 228 AFLKFIFsEREFINRFPTCVKHIITAGEQlvITNEFKEMLHEHNVHLHNHYGPSETHvVTTYTINPEAEIPELPPIGKPI 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 312 FQCQLRI-EKDGVVVPPLVEGEIVVKGPNVTGGYFNREDATRETI------QNGWLH-TGDLGYLDEEGFLYVLDRRSDL 383
Cdd:cd17656 308 SNTWIYIlDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFfpdpfdPNERMYrTGDLARYLPDGNIEFLGRADHQ 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 384 IISGGENIYPAQIEEVLLSHPMVAEAGVVGMTDDKWGQVPAAFVVKNGEVTEEEIIHFCEEKLAKYKVPKKACFLEELPR 463
Cdd:cd17656 388 VKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFVMEQELNISQLREYLAKQLPEYMIPSFFVPLDQLPL 467
|
490
....*....|.
gi 446371684 464 NASKKLLRREL 474
Cdd:cd17656 468 TPNGKVDRKAL 478
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
7-479 |
1.38e-34 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 137.00 E-value: 1.38e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 7 WLKQRafltPDRTAI-----EIEEEKV-TFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGME----M-----ITVIHA 71
Cdd:PRK10524 62 HLAKR----PEQLALiavstETDEERTyTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEaafaMlacarIGAIHS 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 72 LSYVGAVAVLLNTRlsreellwqMDDAEVVCLVT-DQQFDANDVPVY--------SFAE--------VMHGL----KVE- 129
Cdd:PRK10524 138 VVFGGFASHSLAAR---------IDDAKPVLIVSaDAGSRGGKVVPYkplldeaiALAQhkprhvllVDRGLapmaRVAg 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 130 -----ASIQEEFS--------LE--EAMTIIYTSGTTGKPKGVILTYGNHwASAVGSSLNL--GLRDDDCWLACMPMFHV 192
Cdd:PRK10524 209 rdvdyATLRAQHLgarvpvewLEsnEPSYILYTSGTTGKPKGVQRDTGGY-AVALATSMDTifGGKAGETFFCASDIGWV 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 193 GGLS------LL--MKNIMY-GMRIL--------LVPKYDADFIHKAlqtrgVTIISVVSKMLTDLLERlgeetYP-SSL 254
Cdd:PRK10524 288 VGHSyivyapLLagMATIMYeGLPTRpdagiwwrIVEKYKVNRMFSA-----PTAIRVLKKQDPALLRK-----HDlSSL 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 255 RCMLLGGGPAPKPLLETCVDK-GIPVYQTYGMTETSSQICTL--SADYMLTKVGSAGKPLFQCQLRI--EKDGVVVPPLV 329
Cdd:PRK10524 358 RALFLAGEPLDEPTASWISEAlGVPVIDNYWQTETGWPILAIarGVEDRPTRLGSPGVPMYGYNVKLlnEVTGEPCGPNE 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 330 EGEIVVKGP-------NVTGgyfnreDATReTIQNGWLH-------TGDLGYLDEEGFLYVLDRRSDLIISGGENIYPAQ 395
Cdd:PRK10524 438 KGVLVIEGPlppgcmqTVWG------DDDR-FVKTYWSLfgrqvysTFDWGIRDADGYYFILGRTDDVINVAGHRLGTRE 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 396 IEEVLLSHPMVAEAGVVGMTDDKWGQVPAAFVV-KNGEVT---------EEEIIHFCEEKLAKYKVPKKACFLEELPRNA 465
Cdd:PRK10524 511 IEESISSHPAVAEVAVVGVKDALKGQVAVAFVVpKDSDSLadrearlalEKEIMALVDSQLGAVARPARVWFVSALPKTR 590
|
570
....*....|....
gi 446371684 466 SKKLLRRELRQLVE 479
Cdd:PRK10524 591 SGKLLRRAIQAIAE 604
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
24-476 |
2.56e-34 |
|
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: 134.10 E-value: 2.56e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 24 EEEKVTFLQLHEKVVSVCEHL-THVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSREELLwqmddaevvc 102
Cdd:cd05937 2 EGKTWTYSETYDLVLRYAHWLhDDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLI---------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 103 lvtdqqfdandvpvysfaevmHGLKVEASIQEEFSLEEAMTIIYTSGTTGKPKGVILTYGNHWASAVGSSLNLGLRDDDC 182
Cdd:cd05937 72 ---------------------HCLKLSGSRFVIVDPDDPAILIYTSGTTGLPKAAAISWRRTLVTSNLLSHDLNLKNGDR 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 183 WLACMPMFHVGGLSL-LMKNIMYGMRILLVPKYDADFIHKALQTRGVTIISVVSKMLTDLLErlgeeTYPS------SLR 255
Cdd:cd05937 131 TYTCMPLYHGTAAFLgACNCLMSGGTLALSRKFSASQFWKDVRDSGATIIQYVGELCRYLLS-----TPPSpydrdhKVR 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 256 CMLlGGGPAPKpLLETCVDK-GIP-VYQTYGMTETSSQICTLSA-DYMLTKVGSAGkPLFQCQL---------------- 316
Cdd:cd05937 206 VAW-GNGLRPD-IWERFRERfNVPeIGEFYAATEGVFALTNHNVgDFGAGAIGHHG-LIRRWKFenqvvlvkmdpetddp 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 317 -RIEKDG--VVVPPLVEGEIVVKGP--NVTG--GYFNREDAT-----RETIQNG--WLHTGDLGYLDEEGFLYVLDRRSD 382
Cdd:cd05937 283 iRDPKTGfcVRAPVGEPGEMLGRVPfkNREAfqGYLHNEDATesklvRDVFRKGdiYFRTGDLLRQDADGRWYFLDRLGD 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 383 LIISGGENIYPAQIEEVLLSHPMVAEAGVVGMTDDKW-GQV-PAAFVVKNGEVTEEEIIHFCEEKLAKYKVPKKAC---- 456
Cdd:cd05937 363 TFRWKSENVSTTEVADVLGAHPDIAEANVYGVKVPGHdGRAgCAAITLEESSAVPTEFTKSLLASLARKNLPSYAVplfl 442
|
490 500
....*....|....*....|.
gi 446371684 457 -FLEELPRNASKKLLRRELRQ 476
Cdd:cd05937 443 rLTEEVATTDNHKQQKGVLRD 463
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
10-474 |
3.41e-34 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 137.40 E-value: 3.41e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 10 QRAFLTPDRTAIEIEEEKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSRE 89
Cdd:PRK12316 2011 EQAARAPEAIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAE 2090
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 90 ELLWQMDDAEVVCLVTDQQFDAnDVPVYSFAEVMhGLKVEASIQE--------EFSLEEAMTIIYTSGTTGKPKGVILTY 161
Cdd:PRK12316 2091 RLAYMLEDSGAALLLTQRHLLE-RLPLPAGVARL-PLDRDAEWADypdtapavQLAGENLAYVIYTSGSTGLPKGVAVSH 2168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 162 GNHWASAVGSSLNLGLRDDDCWLACMPMFHVGGLSLLMKNIMYGMRILLVPK--YDADFIHKALQTRGVTIISVVSKMLT 239
Cdd:PRK12316 2169 GALVAHCQAAGERYELSPADCELQFMSFSFDGAHEQWFHPLLNGARVLIRDDelWDPEQLYDEMERHGVTILDFPPVYLQ 2248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 240 DLLERLGEETYPSSLRCMLLGGGPAPKPLLETCVDKGIPVY--QTYGMTETSSQICTLSADYMlTKVGSAGKPLFQCQLR 317
Cdd:PRK12316 2249 QLAEHAERDGRPPAVRVYCFGGEAVPAASLRLAWEALRPVYlfNGYGPTEAVVTPLLWKCRPQ-DPCGAAYVPIGRALGN 2327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 318 -----IEKDGVVVPPLVEGEIVVKGPNVTGGYFNREDATRETI-------QNGWLH-TGDLGYLDEEGFLYVLDRRSDLI 384
Cdd:PRK12316 2328 rrayiLDADLNLLAPGMAGELYLGGEGLARGYLNRPGLTAERFvpdpfsaSGERLYrTGDLARYRADGVVEYLGRIDHQV 2407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 385 ISGGENIYPAQIEEVLLSHPMVAEAGVVGMtDDKWGQVPAAFVVKN--GEVTEEEIIHFCEEKLAKYKVPKKACFLEELP 462
Cdd:PRK12316 2408 KIRGFRIELGEIEARLQAHPAVREAVVVAQ-DGASGKQLVAYVVPDdaAEDLLAELRAWLAARLPAYMVPAHWVVLERLP 2486
|
490
....*....|..
gi 446371684 463 RNASKKLLRREL 474
Cdd:PRK12316 2487 LNPNGKLDRKAL 2498
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
12-474 |
3.61e-34 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 137.21 E-value: 3.61e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 12 AFLTPDRTAIEIEEEKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSREEL 91
Cdd:PRK12467 522 ARQHPERPALVFGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRL 601
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 92 LWQMDDAEVVCLVTD-QQFDANDVPVYSFAEVMHGLKVEASIQEEFSLEEAMT------IIYTSGTTGKPKGVILTYGNH 164
Cdd:PRK12467 602 AYMLDDSGVRLLLTQsHLLAQLPVPAGLRSLCLDEPADLLCGYSGHNPEVALDpdnlayVIYTSGSTGQPKGVAISHGAL 681
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 165 WASAVGSSLNLGLRDDDCWLACMPMFHVGGLSLLMKNIMYGMRILLVPK---YDADFIHKALQTRGVTIISVVSKMLTDL 241
Cdd:PRK12467 682 ANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLPPdcaRDAEAFAALMADQGVTVLKIVPSHLQAL 761
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 242 LERlGEETYPSSLRCMLLGGGPAPKPLLETCVDK--GIPVYQTYGMTETS--SQICTLSADYMLTKVGSAGKPLFQCQLR 317
Cdd:PRK12467 762 LQA-SRVALPRPQRALVCGGEALQVDLLARVRALgpGARLINHYGPTETTvgVSTYELSDEERDFGNVPIGQPLANLGLY 840
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 318 I-EKDGVVVPPLVEGEIVVKGPNVTGGYFNREDATRETI-------QNGWLH-TGDLGYLDEEGFLYVLDRRSDLIISGG 388
Cdd:PRK12467 841 IlDHYLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFvpdpfgaDGGRLYrTGDLARYRADGVIEYLGRMDHQVKIRG 920
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 389 ENIYPAQIEEVLLSHPMVAEAGVVGMTDDKWGQVpAAFVVKN-------GEVTEEEIIHFCEEKLAKYKVPKKACFLEEL 461
Cdd:PRK12467 921 FRIELGEIEARLLAQPGVREAVVLAQPGDAGLQL-VAYLVPAavadgaeHQATRDELKAQLRQVLPDYMVPAHLLLLDSL 999
|
490
....*....|...
gi 446371684 462 PRNASKKLLRREL 474
Cdd:PRK12467 1000 PLTPNGKLDRKAL 1012
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
28-474 |
7.34e-34 |
|
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: 133.49 E-value: 7.34e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 28 VTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSREELLWQMDDAEVVCLVTDQ 107
Cdd:cd17639 6 MSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECSAIFTDG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 108 qfDANDVPVysfaevmhglkveasiqeefsleeamtIIYTSGTTGKPKGVILTYGNHWASAVGSSLNLG--LRDDDCWLA 185
Cdd:cd17639 86 --KPDDLAC---------------------------IMYTSGSTGNPKGVMLTHGNLVAGIAGLGDRVPelLGPDDRYLA 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 186 CMPMFHVGGLSLLMKNIMYGMRI-------LLV-----PKYDA---------------DFIHK----------------- 221
Cdd:cd17639 137 YLPLAHIFELAAENVCLYRGGTIgygsprtLTDkskrgCKGDLtefkptlmvgvpaiwDTIRKgvlaklnpmgglkrtlf 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 222 --ALQTRGVTIISVVSKMLTDLL------ERLGeetypSSLRCMLLGGGP---APKPLLETCvdkGIPVYQTYGMTETSS 290
Cdd:cd17639 217 wtAYQSKLKALKEGPGTPLLDELvfkkvrAALG-----GRLRYMLSGGAPlsaDTQEFLNIV---LCPVIQGYGLTETCA 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 291 QICTLSADYMLTkvGSAGKPLFQCQLR---IEKDGVVV---PPlvEGEIVVKGPNVTGGYFNREDATRETI-QNGWLHTG 363
Cdd:cd17639 289 GGTVQDPGDLET--GRVGPPLPCCEIKlvdWEEGGYSTdkpPP--RGEILIRGPNVFKGYYKNPEKTKEAFdGDGWFHTG 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 364 DLGYLDEEGFLYVLDRRSDLI-ISGGENIYPAQIEEVLLSHPMVAEAGVVGmtdDKWGQVPAAFVVKN------------ 430
Cdd:cd17639 365 DIGEFHPDGTLKIIDRKKDLVkLQNGEYIALEKLESIYRSNPLVNNICVYA---DPDKSYPVAIVVPNekhltklaekhg 441
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446371684 431 -GEVTEEEIIH-------FCEE--------KLAKYKVPKKACFLEEL--PRN----ASKKLLRREL 474
Cdd:cd17639 442 vINSEWEELCEdkklqkaVLKSlaetaraaGLEKFEIPQGVVLLDEEwtPENglvtAAQKLKRKEI 507
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
9-474 |
3.33e-33 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 134.31 E-value: 3.33e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 9 KQRAFLTPDRTAIEIEEEKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSR 88
Cdd:PRK12316 3064 EEQVERTPDAVALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPE 3143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 89 EELLWQMDDAEVVCLVTDQQFDANDVPVYSFAEVMHGLK--VEASIQEEFSLEEAMTIIYTSGTTGKPKGVILTYGNHWA 166
Cdd:PRK12316 3144 ERLAYMLEDSGAQLLLSQSHLRLPLAQGVQVLDLDRGDEnyAEANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHSALSN 3223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 167 SAVGSSLNLGLRDDDCWLACMPMFHVGGLSLLMKNIMYGMRILLVPKYDADFIHKA---LQTRGVTIISVVSKMLTDLLE 243
Cdd:PRK12316 3224 HLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDWRDPALLvelINSEGVDVLHAYPSMLQAFLE 3303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 244 RLGEETYPSSLRCMLlgGGPAPKPLLETCVDKGIPVYQTYGMTETSSQICTLSADYMLTKVGSAGKPLFQCQLRIEKDGV 323
Cdd:PRK12316 3304 EEDAHRCTSLKRIVC--GGEALPADLQQQVFAGLPLYNLYGPTEATITVTHWQCVEEGKDAVPIGRPIANRACYILDGSL 3381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 324 V-VPPLVEGEIVVKGPNVTGGYFNREDATRETI------QNGWLH-TGDLGYLDEEGFLYVLDRRSDLIISGGENIYPAQ 395
Cdd:PRK12316 3382 EpVPVGALGELYLGGEGLARGYHNRPGLTAERFvpdpfvPGERLYrTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGE 3461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 396 IEEVLLSHPMVAEAGVVgmtdDKWGQVPAAFVVKNGEVTE--EEIIHFCEEKLAKYKVPKKACFLEELPRNASKKLLRRE 473
Cdd:PRK12316 3462 IEARLLEHPWVREAVVL----AVDGRQLVAYVVPEDEAGDlrEALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKA 3537
|
.
gi 446371684 474 L 474
Cdd:PRK12316 3538 L 3538
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
28-413 |
6.23e-33 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 132.15 E-value: 6.23e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 28 VTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHAL---SYV--------GAVAV---------------- 80
Cdd:PLN02736 79 MTYGEAGTARTAIGSGLVQHGIPKGACVGLYFINRPEWLIVDHACsaySYVsvplydtlGPDAVkfivnhaevaaifcvp 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 81 -LLNTRLSreeLLWQMDDAEVVCLVTDQQFDANDVPVYSFAEVMHGLKVEA---SIQEEFSL---EEAMTIIYTSGTTGK 153
Cdd:PLN02736 159 qTLNTLLS---CLSEIPSVRLIVVVGGADEPLPSLPSGTGVEIVTYSKLLAqgrSSPQPFRPpkpEDVATICYTSGTTGT 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 154 PKGVILTYGNHWASAVGSSLNLGLRDDDCWLACMPMFHVGGLSLLMKNIMYGMRI---------LL-------------V 211
Cdd:PLN02736 236 PKGVVLTHGNLIANVAGSSLSTKFYPSDVHISYLPLAHIYERVNQIVMLHYGVAVgfyqgdnlkLMddlaalrptifcsV 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 212 PK-----YDAdfIHKALQTRGVtiisvvskmltdLLERLGEETYPSSLRCMLLGGGPAP--------------------- 265
Cdd:PLN02736 316 PRlynriYDG--ITNAVKESGG------------LKERLFNAAYNAKKQALENGKNPSPmwdrlvfnkikaklggrvrfm 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 266 ----KPL-------LETCVdkGIPVYQTYGMTETSSQICTLSADYMLTkvGSAGKPLFQCQLRIEKdgvvVP-------- 326
Cdd:PLN02736 382 ssgaSPLspdvmefLRICF--GGRVLEGYGMTETSCVISGMDEGDNLS--GHVGSPNPACEVKLVD----VPemnytsed 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 327 -PLVEGEIVVKGPNVTGGYFNREDATRETI-QNGWLHTGDLGYLDEEGFLYVLDRRSDLI-ISGGENIYPAQIEEVLLSH 403
Cdd:PLN02736 454 qPYPRGEICVRGPIIFKGYYKDEVQTREVIdEDGWLHTGDIGLWLPGGRLKIIDRKKNIFkLAQGEYIAPEKIENVYAKC 533
|
490
....*....|
gi 446371684 404 PMVAEAGVVG 413
Cdd:PLN02736 534 KFVAQCFVYG 543
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
9-474 |
1.71e-32 |
|
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: 129.09 E-value: 1.71e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 9 KQRAFLTPDRTAIEIEEEKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSR 88
Cdd:cd17644 7 EEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLDPNYPQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 89 EELLWQMDDAEVVCLVTDQqfdandvpvysfaevmhglkveasiqeefslEEAMTIIYTSGTTGKPKGVILTY------- 161
Cdd:cd17644 87 ERLTYILEDAQISVLLTQP-------------------------------ENLAYVIYTSGSTGKPKGVMIEHqslvnls 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 162 -GNHWASAVGSSLNLGLRDDDCWLACM----PMFHVGGLSLLMKNIMygmriLLVPKYDADFIhkalQTRGVTIISVVSK 236
Cdd:cd17644 136 hGLIKEYGITSSDRVLQFASIAFDVAAeeiyVTLLSGATLVLRPEEM-----RSSLEDFVQYI----QQWQLTVLSLPPA 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 237 MLTDLLERLGEETY--PSSLRCMLLGGG---PAPKPLLETCVDKGIPVYQTYGMTETS--SQICTLSADY--MLTKVgSA 307
Cdd:cd17644 207 YWHLLVLELLLSTIdlPSSLRLVIVGGEavqPELVRQWQKNVGNFIQLINVYGPTEATiaATVCRLTQLTerNITSV-PI 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 308 GKPLFQCQLRI-EKDGVVVPPLVEGEIVVKGPNVTGGYFNREDATRET-IQNGWLH--------TGDLGYLDEEGFLYVL 377
Cdd:cd17644 286 GRPIANTQVYIlDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKfISHPFNSseserlykTGDLARYLPDGNIEYL 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 378 DRRSDLIISGGENIYPAQIEEVLLSHPMVAEAGVVGMTDDKWGQVPAAFVV--KNGEVTEEEIIHFCEEKLAKYKVPKKA 455
Cdd:cd17644 366 GRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIVphYEESPSTVELRQFLKAKLPDYMIPSAF 445
|
490
....*....|....*....
gi 446371684 456 CFLEELPRNASKKLLRREL 474
Cdd:cd17644 446 VVLEELPLTPNGKIDRRAL 464
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
2-474 |
7.01e-32 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 130.28 E-value: 7.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 2 ETMPNWLKQRAFLTPDRTAIEIEEEKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVL 81
Cdd:PRK12467 1574 RLVHQLIEDQAAATPEAVALVFGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVP 1653
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 82 LNTRLSREELLWQMDDAEVVCLVTdQQFDANDVPVysfAEVMHGLKVEA-----SIQEEFSLEEAMT------IIYTSGT 150
Cdd:PRK12467 1654 LDPEYPRERLAYMIEDSGIELLLT-QSHLQARLPL---PDGLRSLVLDQeddwlEGYSDSNPAVNLApqnlayVIYTSGS 1729
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 151 TGKPKGVILTYGNHWASAVGSSLNLGLRDDDCWLACMPMFHVGGLSLLMKNIMYGMRILLVP----KYDADFIHkALQTR 226
Cdd:PRK12467 1730 TGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTSFAFDVSVWELFWPLINGARLVIAPpgahRDPEQLIQ-LIERQ 1808
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 227 GVTIISVVSKMLTDLLERLGEETYPSSLRCMLLGGGPAP----KPLLETCVDKGIpvYQTYGMTETSSQICTLSADYMLT 302
Cdd:PRK12467 1809 QVTTLHFVPSMLQQLLQMDEQVEHPLSLRRVVCGGEALEvealRPWLERLPDTGL--FNLYGPTETAVDVTHWTCRRKDL 1886
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 303 KVGSA---GKPLFQCQLRIEKDGV-VVPPLVEGEIVVKGPNVTGGYFNREDATRE--------TIQNGWLHTGDLGYLDE 370
Cdd:PRK12467 1887 EGRDSvpiGQPIANLSTYILDASLnPVPIGVAGELYLGGVGLARGYLNRPALTAErfvadpfgTVGSRLYRTGDLARYRA 1966
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 371 EGFLYVLDRRSDLIISGGENIYPAQIEEVLLSHPMVAEAGVVGMtDDKWGQVPAAFVVKNGE--VTEEEIIHFCEEKLAK 448
Cdd:PRK12467 1967 DGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIAQ-DGANGKQLVAYVVPTDPglVDDDEAQVALRAILKN 2045
|
490 500 510
....*....|....*....|....*....|....
gi 446371684 449 --------YKVPKKACFLEELPRNASKKLLRREL 474
Cdd:PRK12467 2046 hlkaslpeYMVPAHLVFLARMPLTPNGKLDRKAL 2079
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
16-474 |
4.05e-31 |
|
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: 124.89 E-value: 4.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 16 PDRTAIEIEEEKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSREELLWQM 95
Cdd:cd17650 1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 96 DDAEVVCLVTDQqfdanDVPVYsfaevmhglkveasiqeefsleeamtIIYTSGTTGKPKGVILTYgNHWASAVGSslnl 175
Cdd:cd17650 81 EDSGAKLLLTQP-----EDLAY--------------------------VIYTSGTTGKPKGVMVEH-RNVAHAAHA---- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 176 glRDDDCWLACMPMFHVGGLSL--------LMKNIMYGMRILLVP---KYDADFIHKALQTRGVTIISVVSKMLTDLLER 244
Cdd:cd17650 125 --WRREYELDSFPVRLLQMASFsfdvfagdFARSLLNGGTLVICPdevKLDPAALYDLILKSRITLMESTPALIRPVMAY 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 245 LGEETY-PSSLRCMLLGGGPAPKPLLETCVDK---GIPVYQTYGMTETS--SQICTLSADymlTKVGSA----GKPLFQC 314
Cdd:cd17650 203 VYRNGLdLSAMRLLIVGSDGCKAQDFKTLAARfgqGMRIINSYGVTEATidSTYYEEGRD---PLGDSAnvpiGRPLPNT 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 315 QLRI--EKDGVVvPPLVEGEIVVKGPNVTGGYFNREDATRETIQNGWL-------HTGDLGYLDEEGFLYVLDRRSDLII 385
Cdd:cd17650 280 AMYVldERLQPQ-PVGVAGELYIGGAGVARGYLNRPELTAERFVENPFapgermyRTGDLARWRADGNVELLGRVDHQVK 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 386 SGGENIYPAQIEEVLLSHPMVAEAGVVGMTDDKWGQVPAAFVVKNGEVTEEEIIHFCEEKLAKYKVPKKACFLEELPRNA 465
Cdd:cd17650 359 IRGFRIELGEIESQLARHPAIDEAVVAVREDKGGEARLCAYVVAAATLNTAELRAFLAKELPSYMIPSYYVQLDALPLTP 438
|
....*....
gi 446371684 466 SKKLLRREL 474
Cdd:cd17650 439 NGKVDRRAL 447
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
9-474 |
9.66e-31 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 127.00 E-value: 9.66e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 9 KQRAFLTPDRTAIEIEEEKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSR 88
Cdd:PRK12316 518 EEQVERTPEAPALAFGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPA 597
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 89 EELLWQMDDAEVVCLVTdQQFDANDVPVYSFAEVMH----GLKVEASIQEEFSL----EEAMTIIYTSGTTGKPKGVILT 160
Cdd:PRK12316 598 ERLAYMLEDSGVQLLLS-QSHLGRKLPLAAGVQVLDldrpAAWLEGYSEENPGTelnpENLAYVIYTSGSTGKPKGAGNR 676
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 161 YGNHWASAVGSSLNLGLRDDDCWLACMPMFHVGGLSLLMKNIMYGMRILLVPK---YDADFIHKALQTRGVTIISVVSKM 237
Cdd:PRK12316 677 HRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPgdhRDPAKLVELINREGVDTLHFVPSM 756
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 238 LTDLLErlgEETYPS--SLRCMLLGGGPAPKPLLETcVDKGIP---VYQTYGMTETSSQICTLSADYMLTKVGSAGKPLF 312
Cdd:PRK12316 757 LQAFLQ---DEDVASctSLRRIVCSGEALPADAQEQ-VFAKLPqagLYNLYGPTEAAIDVTHWTCVEEGGDSVPIGRPIA 832
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 313 QCQLRI-EKDGVVVPPLVEGEIVVKGPNVTGGYFNREDATRE-----TIQNG--WLHTGDLGYLDEEGFLYVLDRRSDLI 384
Cdd:PRK12316 833 NLACYIlDANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAErfvpsPFVAGerMYRTGDLARYRADGVIEYAGRIDHQV 912
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 385 ISGGENIYPAQIEEVLLSHPMVAEAGVVGMTddkwGQVPAAFVV--KNGEVTEEEIIHFCEEKLAKYKVPKKACFLEELP 462
Cdd:PRK12316 913 KLRGLRIELGEIEARLLEHPWVREAAVLAVD----GKQLVGYVVleSEGGDWREALKAHLAASLPEYMVPAQWLALERLP 988
|
490
....*....|..
gi 446371684 463 RNASKKLLRREL 474
Cdd:PRK12316 989 LTPNGKLDRKAL 1000
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
11-477 |
3.96e-30 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 125.07 E-value: 3.96e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 11 RAFLTPDRTAIEIEEEKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSREE 90
Cdd:PRK12316 4560 RARMTPDAVAVVFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRER 4639
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 91 LLWQMDDAEVVCLVTdQQFDANDVPVysfAEVMHGLKV----------EASIQEEFSLEEAMTIIYTSGTTGKPKGVILT 160
Cdd:PRK12316 4640 LAYMMEDSGAALLLT-QSHLLQRLPI---PDGLASLALdrdedwegfpAHDPAVRLHPDNLAYVIYTSGSTGRPKGVAVS 4715
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 161 YGNHWASAVGSSLNLGLRDDDCWLACMPMFHVGGLSLLMKNIMYGMRILLVPK--YDADFIHKALQTRGVTIISVVSKML 238
Cdd:PRK12316 4716 HGSLVNHLHATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLINGASVVIRDDslWDPERLYAEIHEHRVTVLVFPPVYL 4795
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 239 TDLLERLGEETYPSSLRCMLLGGGPAPKPLLETCVDKGIPVY--QTYGMTETS-SQICTLSADYMLTKVGSA--GKPLFQ 313
Cdd:PRK12316 4796 QQLAEHAERDGEPPSLRVYCFGGEAVAQASYDLAWRALKPVYlfNGYGPTETTvTVLLWKARDGDACGAAYMpiGTPLGN 4875
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 314 CQLRIEKDGVVVPPL-VEGEIVVKGPNVTGGYFNREDATRETI-------QNGWLH-TGDLGYLDEEGFLYVLDRRSDLI 384
Cdd:PRK12316 4876 RSGYVLDGQLNPLPVgVAGELYLGGEGVARGYLERPALTAERFvpdpfgaPGGRLYrTGDLARYRADGVIDYLGRVDHQV 4955
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 385 ISGGENIYPAQIEEVLLSHPMVAEAGVVGMtDDKWGQVPAAFVVKNGEVTEEEIIHFCE----------EKLAKYKVPKK 454
Cdd:PRK12316 4956 KIRGFRIELGEIEARLREHPAVREAVVIAQ-EGAVGKQLVGYVVPQDPALADADEAQAElrdelkaalrERLPEYMVPAH 5034
|
490 500
....*....|....*....|...
gi 446371684 455 ACFLEELPRNASKKLLRRELRQL 477
Cdd:PRK12316 5035 LVFLARMPLTPNGKLDRKALPQP 5057
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
17-479 |
6.95e-30 |
|
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: 121.83 E-value: 6.95e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 17 DRTAIEIEEEK----VTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNtrlsreell 92
Cdd:cd05908 1 PEGIIFILGDKkekfVSYRHLREEALGYLGALQELGIKPGQEVVFQITHNNKFLYLFWACLLGGMIAVPVS--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 93 wqmddaevvclvtdqqFDANDVPVYSFAEVMHGLK-----VEASIQEEFSLEEAMtIIYTSGTTGKPKGVILTYGN--HW 165
Cdd:cd05908 72 ----------------IGSNEEHKLKLNKVWNTLKnpyliTEEEVLCELADELAF-IQFSSGSTGDPKGVMLTHENlvHN 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 166 ASAVGSSLNLGLRDDdcWLACMPMFHVGGL-SLLMKNIMYGMRILLVPKydADFIH------KALQTRGVTIISVVSKML 238
Cdd:cd05908 135 MFAILNSTEWKTKDR--ILSWMPLTHDMGLiAFHLAPLIAGMNQYLMPT--RLFIRrpilwlKKASEHKATIVSSPNFGY 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 239 TDLLERLGEETYP----SSLRCMLLGGGPAPKPLLETCVDKGIP-------VYQTYGMTETSSQIC-----------TLS 296
Cdd:cd05908 211 KYFLKTLKPEKANdwdlSSIRMILNGAEPIDYELCHEFLDHMSKyglkrnaILPVYGLAEASVGASlpkaqspfktiTLG 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 297 ADYMLTKVG---------------SAGKPLFQCQLRI-EKDGVVVPPLVEGEIVVKGPNVTGGYFNREDATRETI-QNGW 359
Cdd:cd05908 291 RRHVTHGEPepevdkkdsecltfvEVGKPIDETDIRIcDEDNKILPDGYIGHIQIRGKNVTPGYYNNPEATAKVFtDDGW 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 360 LHTGDLGYLdEEGFLYVLDRRSDLIISGGENIYPAQIEEVllshpmvaeagVVGMTDDKWGQVpAAFVVKNGEVTEEEII 439
Cdd:cd05908 371 LKTGDLGFI-RNGRLVITGREKDIIFVNGQNVYPHDIERI-----------AEELEGVELGRV-VACGVNNSNTRNEEIF 437
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 446371684 440 HFC-----EEKLAKY--KVPK-----------KACFLEELPRNASKKLLRRELRQLVE 479
Cdd:cd05908 438 CFIehrksEDDFYPLgkKIKKhlnkrggwqinEVLPIRRIPKTTSGKVKRYELAQRYQ 495
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
24-406 |
9.70e-30 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 122.92 E-value: 9.70e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 24 EEEKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSREELLWQMDDAEVVCL 103
Cdd:PLN02387 103 EYEWITYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTV 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 104 VTDQQ------------------------FDANDVP--------VYSFAEVmHGLKVEASIQEEFSLEEAMTII-YTSGT 150
Cdd:PLN02387 183 ICDSKqlkklidissqletvkrviymddeGVDSDSSlsgssnwtVSSFSEV-EKLGKENPVDPDLPSPNDIAVImYTSGS 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 151 TGKPKGVILTYGNHWASAVG-SSLNLGLRDDDCWLACMPMFHVggLSLLMKNIM--------YGMRILLV---------P 212
Cdd:PLN02387 262 TGLPKGVMMTHGNIVATVAGvMTVVPKLGKNDVYLAYLPLAHI--LELAAESVMaavgaaigYGSPLTLTdtsnkikkgT 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 213 KYDADFIHKALQTRGVTIISVV--------------SKMLTDL------------------LER--------------LG 246
Cdd:PLN02387 340 KGDASALKPTLMTAVPAILDRVrdgvrkkvdakgglAKKLFDIaykrrlaaiegswfgawgLEKllwdalvfkkiravLG 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 247 eetypSSLRCMLLGGGPAP---KPLLETCVdkGIPVYQTYGMTETssqiC---TLSaDYMLTKVGSAGKPLFQCQLRI-- 318
Cdd:PLN02387 420 -----GRIRFMLSGGAPLSgdtQRFINICL--GAPIGQGYGLTET----CagaTFS-EWDDTSVGRVGPPLPCCYVKLvs 487
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 319 -EKDGVVVP--PLVEGEIVVKGPNVTGGYFNREDATRETI---QNG--WLHTGDLGYLDEEGFLYVLDRRSDLI-ISGGE 389
Cdd:PLN02387 488 wEEGGYLISdkPMPRGEIVIGGPSVTLGYFKNQEKTDEVYkvdERGmrWFYTGDIGQFHPDGCLEIIDRKKDIVkLQHGE 567
|
490
....*....|....*..
gi 446371684 390 NIYPAQIEEVLLSHPMV 406
Cdd:PLN02387 568 YVSLGKVEAALSVSPYV 584
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
26-477 |
1.12e-29 |
|
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: 120.99 E-value: 1.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 26 EKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSREELLWQMDDAEVVCLVT 105
Cdd:cd05939 2 RHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALIF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 106 DQQfdandVPVYSFAevmhglKVEASIQEEFSLEEAMTIIYTSGTTGKPKGVILTYGNHWASAVGSSLNLGLRDDDCWLA 185
Cdd:cd05939 82 NLL-----DPLLTQS------STEPPSQDDVNFRDKLFYIYTSGTTGLPKAAVIVHSRYYRIAAGAYYAFGMRPEDVVYD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 186 CMPMFH-VGGLSLLMKNIMYGMRILLVPKYDADFIHKALQTRGVTIISVVSKMLTDLL-ERLGEETYPSSLRcMLLGGGP 263
Cdd:cd05939 151 CLPLYHsAGGIMGVGQALLHGSTVVIRKKFSASNFWDDCVKYNCTIVQYIGEICRYLLaQPPSEEEQKHNVR-LAVGNGL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 264 APKpLLETCVDK-GIP-VYQTYGMTETSSQICTLSadymlTKVGSAG----KPLFQCQLRI------------EKDGVVV 325
Cdd:cd05939 230 RPQ-IWEQFVRRfGIPqIGEFYGATEGNSSLVNID-----NHVGACGfnsrILPSVYPIRLikvdedtgelirDSDGLCI 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 326 P--P----LVEGEIVVKGPNVT-GGYFNREDATRETIQNGWLH------TGDLGYLDEEGFLYVLDRRSDLIISGGENIY 392
Cdd:cd05939 304 PcqPgepgLLVGKIIQNDPLRRfDGYVNEGATNKKIARDVFKKgdsaflSGDVLVMDELGYLYFKDRTGDTFRWKGENVS 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 393 PAQIEEVlLSHPM----VAEAGV-VGMTDDKWGQvpAAFVVKNGEVTEEEIIHFCEEKLAKYKVPKKACFLEELPRNASK 467
Cdd:cd05939 384 TTEVEGI-LSNVLgledVVVYGVeVPGVEGRAGM--AAIVDPERKVDLDRFSAVLAKSLPPYARPQFIRLLPEVDKTGTF 460
|
490
....*....|
gi 446371684 468 KLLRRELRQL 477
Cdd:cd05939 461 KLQKTDLQKE 470
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
25-471 |
1.21e-28 |
|
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: 117.84 E-value: 1.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 25 EEKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSREELLWQMDDAEVVCLV 104
Cdd:cd05940 1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 105 TDQQFdandvpvysfaevmhglkveasiqeefsleeamtIIYTSGTTGKPKGVILTYGNHWASAVGSSLNLGLRDDDCWL 184
Cdd:cd05940 81 VDAAL----------------------------------YIYTSGTTGLPKAAIISHRRAWRGGAFFAGSGGALPSDVLY 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 185 ACMPMFH-VGGLSLLMKNIMYGMRILLVPKYDADFIHKALQTRGVTIISVVSKMLTDLLERLGEET-YPSSLRCMLlGGG 262
Cdd:cd05940 127 TCLPLYHsTALIVGWSACLASGATLVIRKKFSASNFWDDIRKYQATIFQYIGELCRYLLNQPPKPTeRKHKVRMIF-GNG 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 263 PAPKPLLETCVDKGIP-VYQTYGMTE----------------TSSQICTLSADYMLTKVG-SAGKPLFQCQLRIEKDGVV 324
Cdd:cd05940 206 LRPDIWEEFKERFGVPrIAEFYAATEgnsgfinffgkpgaigRNPSLLRKVAPLALVKYDlESGEPIRDAEGRCIKVPRG 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 325 VPPLVEGEIVVKGPnvTGGYFNREDATRETIQN------GWLHTGDLGYLDEEGFLYVLDRRSDLIISGGENIYPAQIEE 398
Cdd:cd05940 286 EPGLLISRINPLEP--FDGYTDPAATEKKILRDvfkkgdAWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAA 363
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446371684 399 VLLSHPMVAEAGVVGM----TDDKWGQvpAAFVVKNGEvteeeiiHFCEEKLAKYkvpkkacFLEELPRNASKKLLR 471
Cdd:cd05940 364 VLGAFPGVEEANVYGVqvpgTDGRAGM--AAIVLQPNE-------EFDLSALAAH-------LEKNLPGYARPLFLR 424
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
8-479 |
2.87e-28 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 118.32 E-value: 2.87e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 8 LKQRAfltpDRTAIEIEEE------KVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKngmeMItvIHAlsyvgAVAVL 81
Cdd:PRK00174 77 LKTRG----DKVAIIWEGDdpgdsrKITYRELHREVCRFANALKSLGVKKGDRVAIYMP----MI--PEA-----AVAML 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 82 LNTRL-----------SREELLWQMDDAEVVCLVT-DQQF-------------DA-------NDVPVY--SFAEV----- 122
Cdd:PRK00174 142 ACARIgavhsvvfggfSAEALADRIIDAGAKLVITaDEGVrggkpiplkanvdEAlancpsvEKVIVVrrTGGDVdwveg 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 123 ----MHGLKVEASIQ---EEFSLEEAMTIIYTSGTTGKPKGVILTYGNH--WASA----VgsslnLGLRDDD---C---- 182
Cdd:PRK00174 222 rdlwWHELVAGASDEcepEPMDAEDPLFILYTSGSTGKPKGVLHTTGGYlvYAAMtmkyV-----FDYKDGDvywCtadv 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 183 -W-----------LACmpmfhvGGLSLlmkniMY-GmrillVPKY-DADFIHKALQTRGVTI-------ISvvskmltdL 241
Cdd:PRK00174 297 gWvtghsyivygpLAN------GATTL-----MFeG-----VPNYpDPGRFWEVIDKHKVTIfytaptaIR--------A 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 242 LERLGEEtYP-----SSLRcmLLG------------------GGpapkpllETCvdkgiPVYQTYGMTETSSqictlsad 298
Cdd:PRK00174 353 LMKEGDE-HPkkydlSSLR--LLGsvgepinpeawewyykvvGG-------ERC-----PIVDTWWQTETGG-------- 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 299 YMLT--------KVGSAGKPLFQCQLRI-EKDGVVVPPLVEGEIVVKGP------NVTG-------GYFNREDatretiq 356
Cdd:PRK00174 410 IMITplpgatplKPGSATRPLPGIQPAVvDEEGNPLEGGEGGNLVIKDPwpgmmrTIYGdherfvkTYFSTFK------- 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 357 nGWLHTGDLGYLDEEGFLYVLDRRSDLIISGGENIYPAQIEEVLLSHPMVAEAGVVGMTDDKWGQVPAAFVV-KNGEVTE 435
Cdd:PRK00174 483 -GMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTlKGGEEPS 561
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 446371684 436 EEII-----HFCEE--KLAKykvPKKACFLEELPRNASKKLLRRELRQLVE 479
Cdd:PRK00174 562 DELRkelrnWVRKEigPIAK---PDVIQFAPGLPKTRSGKIMRRILRKIAE 609
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
26-413 |
2.96e-27 |
|
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: 114.83 E-value: 2.96e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 26 EKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSREELLWQMDDAE-VVCLV 104
Cdd:cd17641 10 QEFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGaRVVIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 105 TDQ-QFD-----ANDVP-----VY---------------SFAEVM---------HGLKVEASIQEEfSLEEAMTIIYTSG 149
Cdd:cd17641 90 EDEeQVDklleiADRIPsvryvIYcdprgmrkyddprliSFEDVValgraldrrDPGLYEREVAAG-KGEDVAVLCTTSG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 150 TTGKPKGVILTYGNHWASAVGSSLNLGLRDDDCWLACMPMFHVG------GLSLLMKNI----------MYGMR------ 207
Cdd:cd17641 169 TTGKPKLAMLSHGNFLGHCAAYLAADPLGPGDEYVSVLPLPWIGeqmysvGQALVCGFIvnfpeepetmMEDLReigptf 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 208 ILLVPKY-------------DADFIHKAL----------------QTRGVTIISVVSKMLTDLL------ERLGEetypS 252
Cdd:cd17641 249 VLLPPRVwegiaadvrarmmDATPFKRFMfelgmklglraldrgkRGRPVSLWLRLASWLADALlfrplrDRLGF----S 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 253 SLRCMLLGGGPAPKPLLETCVDKGIPVYQTYGMTETSSQIcTLSADYMLtKVGSAGKPLFQCQLRIEKdgvvvpplvEGE 332
Cdd:cd17641 325 RLRSAATGGAALGPDTFRFFHAIGVPLKQLYGQTELAGAY-TVHRDGDV-DPDTVGVPFPGTEVRIDE---------VGE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 333 IVVKGPNVTGGYFNREDATRETI-QNGWLHTGDLGYLDEEGFLYVLDRRSDL-IISGGENIYPAQIEEVLLSHPMVAEAG 410
Cdd:cd17641 394 ILVRSPGVFVGYYKNPEATAEDFdEDGWLHTGDAGYFKENGHLVVIDRAKDVgTTSDGTRFSPQFIENKLKFSPYIAEAV 473
|
...
gi 446371684 411 VVG 413
Cdd:cd17641 474 VLG 476
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
7-474 |
3.01e-27 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 116.41 E-value: 3.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 7 WLKQRAFLTPDRTAIEIEEEKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRL 86
Cdd:PRK12467 3100 LIEAQVARTPEAPALVFGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEY 3179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 87 SREELLWQMDDAEVVCLVTdQQFDANDVPVysfAEVMHGLKVEASIQEEFSLEEAMT---------IIYTSGTTGKPKGV 157
Cdd:PRK12467 3180 PRERLAYMIEDSGVKLLLT-QAHLLEQLPA---PAGDTALTLDRLDLNGYSENNPSTrvmgenlayVIYTSGSTGKPKGV 3255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 158 ILTYGN-----HWASAVgsslnLGLRDDDCWLACMPMFHVGGLSLLMKNIMYGMRILLVPK--YDADFIHKALQTRGVTI 230
Cdd:PRK12467 3256 GVRHGAlanhlCWIAEA-----YELDANDRVLLFMSFSFDGAQERFLWTLICGGCLVVRDNdlWDPEELWQAIHAHRISI 3330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 231 ISVVSKMLTDLLERLGEETYPsSLRCMLLGGGPAPKPLLETCVDKGIPV--YQTYGMTETSSQI----CTLSADYMLTKV 304
Cdd:PRK12467 3331 ACFPPAYLQQFAEDAGGADCA-SLDIYVFGGEAVPPAAFEQVKRKLKPRglTNGYGPTEAVVTVtlwkCGGDAVCEAPYA 3409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 305 gSAGKPLFQCQLRI-EKDGVVVPPLVEGEIVVKGPNVTGGYFNREDATRE-------TIQNGWLH-TGDLGYLDEEGFLY 375
Cdd:PRK12467 3410 -PIGRPVAGRSIYVlDGQLNPVPVGVAGELYIGGVGLARGYHQRPSLTAErfvadpfSGSGGRLYrTGDLARYRADGVIE 3488
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 376 VLDRRSDLIISGGENIYPAQIEEVLLSHPMVAEAGVVGMtDDKWGQVPAAFVVKNGEVTE--EEIIHFCEEKLAKYKVPK 453
Cdd:PRK12467 3489 YLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLAR-DGAGGKQLVAYVVPADPQGDwrETLRDHLAASLPDYMVPA 3567
|
490 500
....*....|....*....|.
gi 446371684 454 KACFLEELPRNASKKLLRREL 474
Cdd:PRK12467 3568 QLLVLAAMPLGPNGKVDRKAL 3588
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
15-474 |
1.10e-26 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 112.68 E-value: 1.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 15 TPDRTAIEIEEEKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITvihalSYVGAV-------AVLLNTRLS 87
Cdd:PRK04813 15 QPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLA-----TFLGAVkaghayiPVDVSSPAE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 88 REELLWQMDDAEVVCLVTDQQFDANDVPVYSFAEVMHGLKVEASIQEEFSLEEAMT--IIYTSGTTGKPKGVILTYGN-- 163
Cdd:PRK04813 90 RIEMIIEVAKPSLIIATEELPLEILGIPVITLDELKDIFATGNPYDFDHAVKGDDNyyIIFTSGTTGKPKGVQISHDNlv 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 164 ---HWAsavgssLNL-GLRDDDCWLACMPM-FHvggLSllmknIMY-------GMRILLVPKyD--ADF--IHKALQTRG 227
Cdd:PRK04813 170 sftNWM------LEDfALPEGPQFLNQAPYsFD---LS-----VMDlyptlasGGTLVALPK-DmtANFkqLFETLPQLP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 228 VTI-ISVVSKMLTDLLER-LGEETYPSsLRCMLLGGGPAPKPLLETCVDKgIP---VYQTYGMTE-----TSSQIctlsA 297
Cdd:PRK04813 235 INVwVSTPSFADMCLLDPsFNEEHLPN-LTHFLFCGEELPHKTAKKLLER-FPsatIYNTYGPTEatvavTSIEI----T 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 298 DYMLTK-----VGSAgKPlfQCQLRIEK-DGVVVPPLVEGEIVVKGPNVTGGYFNREDATRE---TIQNGW-LHTGDLGY 367
Cdd:PRK04813 309 DEMLDQykrlpIGYA-KP--DSPLLIIDeEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEaffTFDGQPaYHTGDAGY 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 368 LDEEGFLYvlDRRSDLIIS-GGENIYPAQIEEVLLSHPMVAEAGVVG-MTDDKWGQVPAAFVVKNGEVTEE-EIIHFCEE 444
Cdd:PRK04813 386 LEDGLLFY--QGRIDFQIKlNGYRIELEEIEQNLRQSSYVESAVVVPyNKDHKVQYLIAYVVPKEEDFEREfELTKAIKK 463
|
490 500 510
....*....|....*....|....*....|....
gi 446371684 445 KLAK----YKVPKKACFLEELPRNASKKLLRREL 474
Cdd:PRK04813 464 ELKErlmeYMIPRKFIYRDSLPLTPNGKIDRKAL 497
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
29-434 |
5.03e-26 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 111.45 E-value: 5.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 29 TFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSREELLWQMDDAEV-------- 100
Cdd:PLN02430 78 TYKEVYEEVLQIGSALRASGAEPGSRVGIYGSNCPQWIVAMEACAAHSLICVPLYDTLGPGAVDYIVDHAEIdfvfvqdk 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 101 -------------------VCL--VTDQQFDAND---VPVYSFAEVMHGLK---VEASIQEEFSLeeaMTIIYTSGTTGK 153
Cdd:PLN02430 158 kikellepdcksakrlkaiVSFtsVTEEESDKASqigVKTYSWIDFLHMGKenpSETNPPKPLDI---CTIMYTSGTSGD 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 154 PKGVILTYGNHWASAVGSSLNL-----GLRDDDCWLACMPMFHV--------------------GGLSLLMKNIMYGMRI 208
Cdd:PLN02430 235 PKGVVLTHEAVATFVRGVDLFMeqfedKMTHDDVYLSFLPLAHIldrmieeyffrkgasvgyyhGDLNALRDDLMELKPT 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 209 LL--VPK-----YDAdfIHKALQT---RGVTIISVVSKMLTDLLERLGEETYPSSLRCML--------LGG-------GP 263
Cdd:PLN02430 315 LLagVPRvferiHEG--IQKALQElnpRRRLIFNALYKYKLAWMNRGYSHKKASPMADFLafrkvkakLGGrlrllisGG 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 264 APkplLETCVDKGIPV------YQTYGMTETSSQICTLSADYMlTKVGSAGKPLFQCQLRIEKdgvvVP-----PLVE-- 330
Cdd:PLN02430 393 AP---LSTEIEEFLRVtscafvVQGYGLTETLGPTTLGFPDEM-CMLGTVGAPAVYNELRLEE----VPemgydPLGEpp 464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 331 -GEIVVKGPNVTGGYFNREDATRETIQNGWLHTGDLGYLDEEGFLYVLDRRSDLI-ISGGENIYPAQIEEVLLSHPMVAE 408
Cdd:PLN02430 465 rGEICVRGKCLFSGYYKNPELTEEVMKDGWFHTGDIGEILPNGVLKIIDRKKNLIkLSQGEYVALEYLENVYGQNPIVED 544
|
490 500
....*....|....*....|....*.
gi 446371684 409 AGVVGmtdDKWGQVPAAFVVKNGEVT 434
Cdd:PLN02430 545 IWVYG---DSFKSMLVAVVVPNEENT 567
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
16-474 |
9.52e-26 |
|
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: 109.41 E-value: 9.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 16 PDRTAIEIEEEKVTFLQLHEKVVSVCEHLTHVGVKRG-QKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSREELLWQ 94
Cdd:cd17648 1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAEIRPdDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 95 MDDAEVVCLVTDQQfdandvpvysfaevmhglkveasiqeefsleEAMTIIYTSGTTGKPKGVILTYGNHWASAVGSSLN 174
Cdd:cd17648 81 LEDTGARVVITNST-------------------------------DLAYAIYTSGTTGKPKGVLVEHGSVVNLRTSLSER 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 175 LGLRDDDCWLACMPMFHVGGLSL--LMKNIMYGMRILLVP---KYDADFIHKALQTRGVTIISVVSKMLTDL-LERLgee 248
Cdd:cd17648 130 YFGRDNGDEAVLFFSNYVFDFFVeqMTLALLNGQKLVVPPdemRFDPDRFYAYINREKVTYLSGTPSVLQQYdLARL--- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 249 typSSLRCMLLGGGPAPKPLLETCVDK-GIPVYQTYGMTETS--SQICTLSADYMLTKvgSAGKPLFQCQLRIEKDGV-V 324
Cdd:cd17648 207 ---PHLKRVDAAGEEFTAPVFEKLRSRfAGLIINAYGPTETTvtNHKRFFPGDQRFDK--SLGRPVRNTKCYVLNDAMkR 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 325 VPPLVEGEIVVKGPNVTGGYFNREDATRET-IQNG-----------------------WLHTGDLGYLDeegflyvldrR 380
Cdd:cd17648 282 VPVGAVGELYLGGDGVARGYLNRPELTAERfLPNPfqteqerargrnarlyktgdlvrWLPSGELEYLG----------R 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 381 SDLIIS-GGENIYPAQIEEVLLSHPMVAEAGVVGMTDDKWGQVPAA------FVVKNGEVTEEEIIHFCEEKLAKYKVPK 453
Cdd:cd17648 352 NDFQVKiRGQRIEPGEVEAALASYPGVRECAVVAKEDASQAQSRIQkylvgyYLPEPGHVPESDLLSFLRAKLPRYMVPA 431
|
490 500
....*....|....*....|.
gi 446371684 454 KACFLEELPRNASKKLLRREL 474
Cdd:cd17648 432 RLVRLEGIPVTINGKLDVRAL 452
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
8-452 |
1.96e-25 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 109.58 E-value: 1.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 8 LKQRAFLTPDRTAIEIEEEKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLS 87
Cdd:PRK08279 43 FEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLNTQQR 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 88 REELLWQMD---------DAEVVCLVTDQQFDANDVPVYSFAEVMHG--------LKVEASIQEEFSLEEAMTI------ 144
Cdd:PRK08279 123 GAVLAHSLNlvdakhlivGEELVEAFEEARADLARPPRLWVAGGDTLddpegyedLAAAAAGAPTTNPASRSGVtakdta 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 145 --IYTSGTTGKPKGVILTYGnHWASAVGS-SLNLGLRDDDCWLACMPMFH-VGGLSLLMKNIMYGMRILLVPKYDADFIH 220
Cdd:PRK08279 203 fyIYTSGTTGLPKAAVMSHM-RWLKAMGGfGGLLRLTPDDVLYCCLPLYHnTGGTVAWSSVLAAGATLALRRKFSASRFW 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 221 KALQTRGVTIISVVSKMLTDLLErlgeetYPSS-------LRCMlLGGGPAPKpLLETCVDK-GIP-VYQTYGMTETSSQ 291
Cdd:PRK08279 282 DDVRRYRATAFQYIGELCRYLLN------QPPKptdrdhrLRLM-IGNGLRPD-IWDEFQQRfGIPrILEFYAASEGNVG 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 292 ICTLsadymLTKVGSAGK-PLF-QCQLRIEK------------DG--VVVPP----LVEGEIVVKGPnvTGGYFNREdAT 351
Cdd:PRK08279 354 FINV-----FNFDGTVGRvPLWlAHPYAIVKydvdtgepvrdaDGrcIKVKPgevgLLIGRITDRGP--FDGYTDPE-AS 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 352 -----RETIQNG--WLHTGDLGYLDEEGFLYVLDRRSDLIISGGENIYPAQIEEVLLSHPMVAEAGVVGMtddkwgQVP- 423
Cdd:PRK08279 426 ekkilRDVFKKGdaWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVATTEVENALSGFPGVEEAVVYGV------EVPg 499
|
490 500 510
....*....|....*....|....*....|....*..
gi 446371684 424 -------AAFVVKNGEVTEEEIIH-FCEEKLAKYKVP 452
Cdd:PRK08279 500 tdgragmAAIVLADGAEFDLAALAaHLYERLPAYAVP 536
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
2-474 |
2.02e-25 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 110.52 E-value: 2.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 2 ETMPNWLKQRAFLTPDRTAIEIEEEKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVL 81
Cdd:PRK10252 458 TTLSALVAQQAAKTPDAPALADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLP 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 82 LNTRLSREELLWQMDDAEVVCLVT--DQQFDANDVPVYSFAEVMHGLKVEASIQEEFSL-EEAMTIIYTSGTTGKPKGVI 158
Cdd:PRK10252 538 LDTGYPDDRLKMMLEDARPSLLITtaDQLPRFADVPDLTSLCYNAPLAPQGAAPLQLSQpHHTAYIIFTSGSTGRPKGVM 617
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 159 LTYgnhwaSAVGSSL-----NLGLRDDDCWLACMPM-FHVGGLSLLMKnIMYGMRILLV-------PKYDADFIHKalqt 225
Cdd:PRK10252 618 VGQ-----TAIVNRLlwmqnHYPLTADDVVLQKTPCsFDVSVWEFFWP-FIAGAKLVMAepeahrdPLAMQQFFAE---- 687
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 226 RGVTIISVVSKMLTDLLERLGEETYP---SSLRCMLLGGGPAPKPL---LETCVdkGIPVYQTYGMTETSSQIC--TLSA 297
Cdd:PRK10252 688 YGVTTTHFVPSMLAAFVASLTPEGARqscASLRQVFCSGEALPADLcreWQQLT--GAPLHNLYGPTEAAVDVSwyPAFG 765
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 298 DYMLTKVGSA---GKPLFQCQLRIeKDGVV--VPPLVEGEIVVKGPNVTGGYFNREDATRET-IQNGWL------HTGDL 365
Cdd:PRK10252 766 EELAAVRGSSvpiGYPVWNTGLRI-LDARMrpVPPGVAGDLYLTGIQLAQGYLGRPDLTASRfIADPFApgermyRTGDV 844
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 366 GYLDEEGFLYVLDRRSDLIISGGENIYPAQIEEVLLSHPMVAEAGVV-------GMTDDKWGQVPAAFVVKNGEVTEEEI 438
Cdd:PRK10252 845 ARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAVTHacvinqaAATGGDARQLVGYLVSQSGLPLDTSA 924
|
490 500 510
....*....|....*....|....*....|....*..
gi 446371684 439 IH-FCEEKLAKYKVPKKACFLEELPRNASKKLLRREL 474
Cdd:PRK10252 925 LQaQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKAL 961
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
25-477 |
4.91e-25 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 108.17 E-value: 4.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 25 EEKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLS---REELLWQMD----- 96
Cdd:PRK09192 47 EEALPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPLPLPMGfggRESYIAQLRgmlas 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 97 -DAEVVClvtdqqfdANDVPVYSFAEVMHGLK-VEASIQEEFSLEEAMTII-------------YTSGTTGKPKGVILTY 161
Cdd:PRK09192 127 aQPAAII--------TPDELLPWVNEATHGNPlLHVLSHAWFKALPEADVAlprptpddiaylqYSSGSTRFPRGVIITH 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 162 GNHWASAVGSSLN-LGLRDDD-C--WLacmPMFHVGGL-SLLMKNIMYGMRILLVPKydADFIHKALQ-----TRGVTII 231
Cdd:PRK09192 199 RALMANLRAISHDgLKVRPGDrCvsWL---PFYHDMGLvGFLLTPVATQLSVDYLPT--RDFARRPLQwldliSRNRGTI 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 232 SVVSKMLTDLLERLGEETYPSSL-----RCMLLGGGPAPKPLLETCVDKGIPV-------YQTYGMTETssqicTLSADY 299
Cdd:PRK09192 274 SYSPPFGYELCARRVNSKDLAELdlscwRVAGIGADMIRPDVLHQFAEAFAPAgfddkafMPSYGLAEA-----TLAVSF 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 300 M---------------LTKVGSA----------------GKPLFQCQLRI-EKDGVVVPPLVEGEIVVKGPNVTGGYFNR 347
Cdd:PRK09192 349 SplgsgivveevdrdrLEYQGKAvapgaetrrvrtfvncGKALPGHEIEIrNEAGMPLPERVVGHICVRGPSLMSGYFRD 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 348 EDATRETIQNGWLHTGDLGYLdEEGFLYVLDRRSDLIISGGENIYPAQIEEVLLSHPMV--AEAGVVGMTDDKwGQVPAA 425
Cdd:PRK09192 429 EESQDVLAADGWLDTGDLGYL-LDGYLYITGRAKDLIIINGRNIWPQDIEWIAEQEPELrsGDAAAFSIAQEN-GEKIVL 506
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 426 FVVKNG--EVTEEEIIHFCEEKL-AKYKVPkkaCFLE-----ELPRNASKKLLRRELRQL 477
Cdd:PRK09192 507 LVQCRIsdEERRGQLIHALAALVrSEFGVE---AAVElvpphSLPRTSSGKLSRAKAKKR 563
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
122-474 |
9.83e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 105.89 E-value: 9.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 122 VMHGLKVEASIQEEFSLEEAMTIIYTSGTTGKPKgvilTYGNHWAS------AVGSSLNlGLRDDDCWLACmPMFHVGGL 195
Cdd:PRK08308 84 LYGESDFTKLEAVNYLAEEPSLLQYSSGTTGEPK----LIRRSWTEidreieAYNEALN-CEQDETPIVAC-PVTHSYGL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 196 -SLLMKNIMYGMRILLVPKYDADFIHKALQTRGVTIISVVSKMLTdLLERL--GEETYPSslrcMLLGGGPAPKPLLETC 272
Cdd:PRK08308 158 iCGVLAALTRGSKPVIITNKNPKFALNILRNTPQHILYAVPLMLH-ILGRLlpGTFQFHA----VMTSGTPLPEAWFYKL 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 273 VDKGIPVYQTYGMTETSsqiC-TLSADymLTKVGSAGKPLFQCQLRIEKDgvvvpPLVEGEIVVKgpnvtggyfnredAT 351
Cdd:PRK08308 233 RERTTYMMQQYGCSEAG---CvSICPD--MKSHLDLGNPLPHVSVSAGSD-----ENAPEEIVVK-------------MG 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 352 RETIqngwlHTGDLGYLDEEGFLYVLDRRSDLIISGGENIYPAQIEEVLLSHPMVAEAGVVGMTDDKWGQVPAAFVVKNG 431
Cdd:PRK08308 290 DKEI-----FTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVISHE 364
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 446371684 432 EVTEEEIIHFCEEKLAKYKVPKKACFLEELPRNASKKLLRREL 474
Cdd:PRK08308 365 EIDPVQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLL 407
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
3-474 |
2.35e-23 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 104.48 E-value: 2.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 3 TMPNWLKQRAFLTPDRTAIEIEEEKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLL 82
Cdd:PRK05691 1132 WLPELLNEQARQTPERIALVWDGGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPL 1211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 83 NTRLSREELLWQMDD------------------AEVVCLVTDQQFDANDVPVYSFAEVMHGlkveasiqeefslEEAMTI 144
Cdd:PRK05691 1212 DPDYPAERLAYMLADsgvellltqshllerlpqAEGVSAIALDSLHLDSWPSQAPGLHLHG-------------DNLAYV 1278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 145 IYTSGTTGKPKGVILTYGN-----HWASAvgsslNLGLRDDDCWLACMPM-FHVGGLSLLMKNIMyGMRILLV---PKYD 215
Cdd:PRK05691 1279 IYTSGSTGQPKGVGNTHAAlaerlQWMQA-----TYALDDSDVLMQKAPIsFDVSVWECFWPLIT-GCRLVLAgpgEHRD 1352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 216 ADFIHKALQTRGVTIISVVSKMLTDLLE--RLGEETypsSLRcMLLGGGPAPKPLLETCVDKGIPVYQ---TYGMTETSS 290
Cdd:PRK05691 1353 PQRIAELVQQYGVTTLHFVPPLLQLFIDepLAAACT---SLR-RLFSGGEALPAELRNRVLQRLPQVQlhnRYGPTETAI 1428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 291 QICTLSADYMLTKVGSAGKPLFQCQLRIEKDGV-VVPPLVEGEIVVKGPNVTGGYFNREDATRETI------QNG--WLH 361
Cdd:PRK05691 1429 NVTHWQCQAEDGERSPIGRPLGNVLCRVLDAELnLLPPGVAGELCIGGAGLARGYLGRPALTAERFvpdplgEDGarLYR 1508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 362 TGDLGYLDEEGFLYVLDRRSDLIISGGENIYPAQIEEVLLSHPMVAEAGVVGMTDDKWGQVPAAFVVKNG-EVTEEEIIH 440
Cdd:PRK05691 1509 TGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLVREGAAGAQLVGYYTGEAGqEAEAERLKA 1588
|
490 500 510
....*....|....*....|....*....|....
gi 446371684 441 FCEEKLAKYKVPKKACFLEELPRNASKKLLRREL 474
Cdd:PRK05691 1589 ALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRAL 1622
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
16-480 |
3.04e-23 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 102.76 E-value: 3.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 16 PDRTAIEIEEEKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAV--LLNTRlsREELLW 93
Cdd:PRK10946 37 SDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLGVAPVnaLFSHQ--RSELNA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 94 QMDDAEVVCLVTDQQFD--ANDVPVYSFAEVMHGLKVEASIQE--EFSLEEAM-----TIIYTS-------------GTT 151
Cdd:PRK10946 115 YASQIEPALLIADRQHAlfSDDDFLNTLVAEHSSLRVVLLLNDdgEHSLDDAInhpaeDFTATPspadevaffqlsgGST 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 152 GKPKGVILTYGNHWASAVGSSLNLGLRDDDCWLACMPMFH------VGGLSLLMKnimyGMRILLVPKYDADFIHKALQT 225
Cdd:PRK10946 195 GTPKLIPRTHNDYYYSVRRSVEICGFTPQTRYLCALPAAHnypmssPGALGVFLA----GGTVVLAPDPSATLCFPLIEK 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 226 RGVTIISVVSKMLTDLLERLGEETYP---SSLRCMLLGGGPapkpLLETcVDKGIP------VYQTYGMTET-------- 288
Cdd:PRK10946 271 HQVNVTALVPPAVSLWLQAIAEGGSRaqlASLKLLQVGGAR----LSET-LARRIPaelgcqLQQVFGMAEGlvnytrld 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 289 -------SSQICTLSADYMLTKVGSAGKPlfqcqlriekdgvvVPPLVEGEIVVKGPNVTGGYFNREDATRETI-QNGWL 360
Cdd:PRK10946 346 dsderifTTQGRPMSPDDEVWVADADGNP--------------LPQGEVGRLMTRGPYTFRGYYKSPQHNASAFdANGFY 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 361 HTGDLGYLDEEGFLYVLDRRSDLIISGGENIYPAQIEEVLLSHPMVAEAGVVGMTDDKWGQVPAAFVVKNGEVTEEEIIH 440
Cdd:PRK10946 412 CSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAFLVVKEPLKAVQLRR 491
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 446371684 441 FCEEK-LAKYKVPKKACFLEELPRNASKKLLRRELRQLVEE 480
Cdd:PRK10946 492 FLREQgIAEFKLPDRVECVDSLPLTAVGKVDKKQLRQWLAS 532
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
396-468 |
5.17e-23 |
|
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: 92.22 E-value: 5.17e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446371684 396 IEEVLLSHPMVAEAGVVGMTDDKWGQVPAAFVV-KNG-EVTEEEIIHFCEEKLAKYKVPKKACFLEELPRNASKK 468
Cdd:pfam13193 2 VESALVSHPAVAEAAVVGVPDELKGEAPVAFVVlKPGvELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
28-413 |
7.07e-23 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 101.84 E-value: 7.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 28 VTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSREELLWQMDDAEV-VCLVTD 106
Cdd:PLN02861 78 LTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVsIAFVQE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 107 QQFD----------ANDVPVYSFAEVMHGLKVEASIQ-------EEFSL-------------EEAMTIIYTSGTTGKPKG 156
Cdd:PLN02861 158 SKISsilsclpkcsSNLKTIVSFGDVSSEQKEEAEELgvscfswEEFSLmgsldcelppkqkTDICTIMYTSGTTGEPKG 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 157 VILTYGNHWASAVGSSLNLGLRD-----DDCWLACMPMFHV--------------------GGLSLLMKNI--MYGMRIL 209
Cdd:PLN02861 238 VILTNRAIIAEVLSTDHLLKVTDrvateEDSYFSYLPLAHVydqvietyciskgasigfwqGDIRYLMEDVqaLKPTIFC 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 210 LVPK-YDADF--IHKALQTRGVtiisvVSKMLTD---------------------LLERL----GEETYPSSLRCMLLGG 261
Cdd:PLN02861 318 GVPRvYDRIYtgIMQKISSGGM-----LRKKLFDfaynyklgnlrkglkqeeaspRLDRLvfdkIKEGLGGRVRLLLSGA 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 262 GPAPKPLLETC-VDKGIPVYQTYGMTETSSQiCTLSADYMLTKVGSAGKPLFQCQLRIEK------DGVVVPPlvEGEIV 334
Cdd:PLN02861 393 APLPRHVEEFLrVTSCSVLSQGYGLTESCGG-CFTSIANVFSMVGTVGVPMTTIEARLESvpemgyDALSDVP--RGEIC 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 335 VKGPNVTGGYFNREDATRETIQNGWLHTGDLGYLDEEGFLYVLDRRSDLI-ISGGENIYPAQIEEVLLSHPMVAEAGVVG 413
Cdd:PLN02861 470 LRGNTLFSGYHKRQDLTEEVLIDGWFHTGDIGEWQPNGAMKIIDRKKNIFkLSQGEYVAVENLENTYSRCPLIASIWVYG 549
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
17-477 |
1.95e-20 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 94.58 E-value: 1.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 17 DRTAIEIE------EEKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSREE 90
Cdd:PLN02654 104 DKIAIYWEgnepgfDASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAES 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 91 LLWQMDDAEVVCLVTDQQFDANDVPVY-------SFAE-VMHGLKVEASIQEEFSL------------------------ 138
Cdd:PLN02654 184 LAQRIVDCKPKVVITCNAVKRGPKTINlkdivdaALDEsAKNGVSVGICLTYENQLamkredtkwqegrdvwwqdvvpny 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 139 -----------EEAMTIIYTSGTTGKPKGVILTYGNHWA-SAVGSSLNLGLRDDDCWLACMPMFHVGGLSLLMKNIMYGM 206
Cdd:PLN02654 264 ptkcevewvdaEDPLFLLYTSGSTGKPKGVLHTTGGYMVyTATTFKYAFDYKPTDVYWCTADCGWITGHSYVTYGPMLNG 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 207 RILLV----PKY-DADFIHKALQTRGVTIISVVSKMLTDLLeRLGEETYP----SSLRCMLLGGGP----APKPLLETCV 273
Cdd:PLN02654 344 ATVLVfegaPNYpDSGRCWDIVDKYKVTIFYTAPTLVRSLM-RDGDEYVTrhsrKSLRVLGSVGEPinpsAWRWFFNVVG 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 274 DKGIPVYQTYGMTETSSQICTLSADYMLTKVGSAGKPLFQCQ-LRIEKDGVVVPPLVEGEIVVKGP-----NVTGGYFNR 347
Cdd:PLN02654 423 DSRCPISDTWWQTETGGFMITPLPGAWPQKPGSATFPFFGVQpVIVDEKGKEIEGECSGYLCVKKSwpgafRTLYGDHER 502
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 348 EDATRETIQNGWLHTGDLGYLDEEGFLYVLDRRSDLIISGGENIYPAQIEEVLLSHPMVAEAGVVGMTDDKWGQVPAAFV 427
Cdd:PLN02654 503 YETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEVKGQGIYAFV 582
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 446371684 428 --VKNGEVTEE---EIIHFCEEKLAKYKVPKKACFLEELPRNASKKLLRRELRQL 477
Cdd:PLN02654 583 tlVEGVPYSEElrkSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRKI 637
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
10-474 |
3.79e-19 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 91.38 E-value: 3.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 10 QRAFLTPDRTAIEIEEEKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSRE 89
Cdd:PRK05691 2196 AQAARTPQAPALTFAGQTLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLE 2275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 90 ELLWQMDDAEVVCLVTDQQ-FDA-----NDVPVYSFAEVMHGLKVEASIQEEF-SLEEAMT-IIYTSGTTGKPKGVILTY 161
Cdd:PRK05691 2276 RLHYMIEDSGIGLLLSDRAlFEAlgelpAGVARWCLEDDAAALAAYSDAPLPFlSLPQHQAyLIYTSGSTGKPKGVVVSH 2355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 162 GN---HWASAVGSslnLGLRDDDCWLACMPMFHVGGLSLLMKNIMYGMRILLVPK--YDADFIHKALQTRGVTIISVVSK 236
Cdd:PRK05691 2356 GEiamHCQAVIER---FGMRADDCELHFYSINFDAASERLLVPLLCGARVVLRAQgqWGAEEICQLIREQQVSILGFTPS 2432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 237 MLTDLLERLGEETYPSSLRCMLLGGGPAPKPLLETCVDKGIP--VYQTYGMTETSSQ-ICTLSADYMLTKVGSA--GKPL 311
Cdd:PRK05691 2433 YGSQLAQWLAGQGEQLPVRMCITGGEALTGEHLQRIRQAFAPqlFFNAYGPTETVVMpLACLAPEQLEEGAASVpiGRVV 2512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 312 FQCQLRI-EKDGVVVPPLVEGEIVVKGPNVTGGYFNREDATRE-------TIQNGWLH-TGDLGYLDEEGFLYVLDRRSD 382
Cdd:PRK05691 2513 GARVAYIlDADLALVPQGATGELYVGGAGLAQGYHDRPGLTAErfvadpfAADGGRLYrTGDLVRLRADGLVEYVGRIDH 2592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 383 LIISGGENIYPAQIEEVLLSHPMVAEAGVVGMTDDKWGQVPAAFVVKNGEVTEEEIIHFCE-------EKLAKYKVPKKA 455
Cdd:PRK05691 2593 QVKIRGFRIELGEIESRLLEHPAVREAVVLALDTPSGKQLAGYLVSAVAGQDDEAQAALREalkahlkQQLPDYMVPAHL 2672
|
490
....*....|....*....
gi 446371684 456 CFLEELPRNASKKLLRREL 474
Cdd:PRK05691 2673 ILLDSLPLTANGKLDRRAL 2691
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
29-399 |
9.65e-19 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 89.31 E-value: 9.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 29 TFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSREELLWQMDDAEV-VCLVTDQ 107
Cdd:PLN02614 81 TYQEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVsIVFVEEK 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 108 QFDA--NDVP--------VYSFAEVMHGLKVEA--------SIQEEFSLEEAM-------------TIIYTSGTTGKPKG 156
Cdd:PLN02614 161 KISElfKTCPnsteymktVVSFGGVSREQKEEAetfglviyAWDEFLKLGEGKqydlpikkksdicTIMYTSGTTGDPKG 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 157 VILTYGNHWASAVG-----SSLNLGLRDDDCWLACMPMFHV--------------------GGLSLLMKNI--MYGMRIL 209
Cdd:PLN02614 241 VMISNESIVTLIAGvirllKSANAALTVKDVYLSYLPLAHIfdrvieecfiqhgaaigfwrGDVKLLIEDLgeLKPTIFC 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 210 LVPK-----------------------YDADFIHK-ALQTRGVTIISVvSKMLTDLLERLGEETYPSSLRCMLLGGGPAP 265
Cdd:PLN02614 321 AVPRvldrvysglqkklsdggflkkfvFDSAFSYKfGNMKKGQSHVEA-SPLCDKLVFNKVKQGLGGNVRIILSGAAPLA 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 266 KPL-----LETCVDkgipVYQTYGMTETSSQICTLSADyMLTKVGSAGKPLFQCQLRIEK------DGVVVPPlvEGEIV 334
Cdd:PLN02614 400 SHVesflrVVACCH----VLQGYGLTESCAGTFVSLPD-ELDMLGTVGPPVPNVDIRLESvpemeyDALASTP--RGEIC 472
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446371684 335 VKGPNVTGGYFNREDATRETIQNGWLHTGDLGYLDEEGFLYVLDRRSDLI-ISGGENIYPAQIEEV 399
Cdd:PLN02614 473 IRGKTLFSGYYKREDLTKEVLIDGWLHTGDVGEWQPNGSMKIIDRKKNIFkLSQGEYVAVENIENI 538
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
3-476 |
1.56e-18 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 89.46 E-value: 1.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 3 TMPNWLKQRAFLTPDRTAI----EIEEEKV--TFLQLHEKVVSVCEHLTHVGVKrGQKVAVLMKNGMEMITVIHALSYVG 76
Cdd:PRK05691 10 TLVQALQRRAAQTPDRLALrflaDDPGEGVvlSYRDLDLRARTIAAALQARASF-GDRAVLLFPSGPDYVAAFFGCLYAG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 77 AVAVLL-----NTRLSREELLWQMDDAEVVCLVTD-------QQFD---ANDVPVYSFAEVMHGLKVEASIQEEFSLEEA 141
Cdd:PRK05691 89 VIAVPAyppesARRHHQERLLSIIADAEPRLLLTVadlrdslLQMEelaAANAPELLCVDTLDPALAEAWQEPALQPDDI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 142 MTIIYTSGTTGKPKGVILTYGNHWASA--VGSSLNLGLRDDDCWLACMPMFHVGGL-SLLMKNIMYGMR-ILLVPKYdad 217
Cdd:PRK05691 169 AFLQYTSGSTALPKGVQVSHGNLVANEqlIRHGFGIDLNPDDVIVSWLPLYHDMGLiGGLLQPIFSGVPcVLMSPAY--- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 218 FIHK------ALQTRGVTI-------ISVVSKMLTD-LLERLGEetypSSLRCMLLGGGPAPKPLLETCVDKGIPV---- 279
Cdd:PRK05691 246 FLERplrwleAISEYGGTIsggpdfaYRLCSERVSEsALERLDL----SRWRVAYSGSEPIRQDSLERFAEKFAACgfdp 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 280 ---YQTYGMTETS---------SQICTLSADYMLTKVGSA----GKPLFQC-------QLRI--EKDGVVVPPLVEGEIV 334
Cdd:PRK05691 322 dsfFASYGLAEATlfvsggrrgQGIPALELDAEALARNRAepgtGSVLMSCgrsqpghAVLIvdPQSLEVLGDNRVGEIW 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 335 VKGPNVTGGYFNREDATRETIQN----GWLHTGDLGYLdEEGFLYVLDRRSDLIISGGENIYPAQIEEVLLSHPMVAEAG 410
Cdd:PRK05691 402 ASGPSIAHGYWRNPEASAKTFVEhdgrTWLRTGDLGFL-RDGELFVTGRLKDMLIVRGHNLYPQDIEKTVEREVEVVRKG 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 411 VVgmtddkwgqvpAAFVVK-NGE----------------VTEEEIIHFCEEKLAK--YKVPKKACFLE--ELPRNASKKL 469
Cdd:PRK05691 481 RV-----------AAFAVNhQGEegigiaaeisrsvqkiLPPQALIKSIRQAVAEacQEAPSVVLLLNpgALPKTSSGKL 549
|
....*..
gi 446371684 470 LRRELRQ 476
Cdd:PRK05691 550 QRSACRL 556
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
28-411 |
2.44e-18 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 88.11 E-value: 2.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 28 VTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSREELLWQMDDAEVVCLVTDQ 107
Cdd:PTZ00216 122 ITYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAIVCNG 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 108 Q----------------------------FDANDVPVYSFAEVmhgLKVEASIQEEFSL-------EEAMtIIYTSGTTG 152
Cdd:PTZ00216 202 KnvpnllrlmksggmpnttiiyldslpasVDTEGCRLVAWTDV---VAKGHSAGSHHPLnipenndDLAL-IMYTSGTTG 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 153 KPKGVILTYGNHWASAVG-----SSLNLGLRDDDCWLACMPMFHV---GGLSLLMKN---IMYGM-RILL---------- 210
Cdd:PTZ00216 278 DPKGVMHTHGSLTAGILAledrlNDLIGPPEEDETYCSYLPLAHImefGVTNIFLARgalIGFGSpRTLTdtfarphgdl 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 211 ----------VPK-YDAdfIHKALQTR----GVTIISVVSKMLTDLLERL--GEETyP---------------SSLRCML 258
Cdd:PTZ00216 358 tefrpvfligVPRiFDT--IKKAVEAKlppvGSLKRRVFDHAYQSRLRALkeGKDT-PywnekvfsapravlgGRVRAML 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 259 LGGGPAPKPLLE-TCVDKGiPVYQTYGMTETssqICT----LSADymlTKVGSAGKPLFQCQLR---IEKDGVVVPPLVE 330
Cdd:PTZ00216 435 SGGGPLSAATQEfVNVVFG-MVIQGWGLTET---VCCggiqRTGD---LEPNAVGQLLKGVEMKlldTEEYKHTDTPEPR 507
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 331 GEIVVKGPNVTGGYFNREDATRETIQN-GWLHTGDLGYLDEEGFLYVLDRRSDLII-SGGENIYPAQIEEVLLSHPMVAE 408
Cdd:PTZ00216 508 GEILLRGPFLFKGYYKQEELTREVLDEdGWFHTGDVGSIAANGTLRIIGRVKALAKnCLGEYIALEALEALYGQNELVVP 587
|
...
gi 446371684 409 AGV 411
Cdd:PTZ00216 588 NGV 590
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
147-480 |
6.83e-18 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 86.36 E-value: 6.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 147 TSGTTGKPKGVILTYGNHWASAVGSSLNLGL---RDDDC-WLacmPMFHVGGLSLLMKNIMYGMRILLVPKydADFihKA 222
Cdd:PRK05851 160 TAGSTGTPRTAILSPGAVLSNLRGLNARVGLdaaTDVGCsWL---PLYHDMGLAFLLTAALAGAPLWLAPT--TAF--SA 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 223 LQTRGVTIISVVSKMLT-------DLLERLGE---ETYPSSLRCMLLGGGPAPKPLLETCVDKGIP-------VYQTYGM 285
Cdd:PRK05851 233 SPFRWLSWLSDSRATLTaapnfayNLIGKYARrvsDVDLGALRVALNGGEPVDCDGFERFATAMAPfgfdagaAAPSYGL 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 286 TETSSQICT------LSADYMLTKVGSA-------GKPLFQCQLRI---EKDGVVVPPLVeGEIVVKGPNVTGGYFNRED 349
Cdd:PRK05851 313 AESTCAVTVpvpgigLRVDEVTTDDGSGarrhavlGNPIPGMEVRIspgDGAAGVAGREI-GEIEIRGASMMSGYLGQAP 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 350 ATREtiqnGWLHTGDLGYLDEEGfLYVLDRRSDLIISGGENIYPAQIEEVLLSHPMVAEAGVVGM-TDDKWGQ----VPA 424
Cdd:PRK05851 392 IDPD----DWFPTGDLGYLVDGG-LVVCGRAKELITVAGRNIFPTEIERVAAQVRGVREGAVVAVgTGEGSARpglvIAA 466
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 425 AFVVKNGEVTEEEIIhfceEKLAKY--KVPKKACFLE--ELPRNASKKLLRRELRQLVEE 480
Cdd:PRK05851 467 EFRGPDEAGARSEVV----QRVASEcgVVPSDVVFVApgSLPRTSSGKLRRLAVKRSLEA 522
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
137-404 |
7.33e-18 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 85.59 E-value: 7.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 137 SLEEAMTIIYTSGTTGKPKGVILTYG--NHWASAVGSSLNL-GLRDDDCWLACMPM-FHVGGLSLLmknimYGMRIL--- 209
Cdd:COG1541 81 PLEEIVRIHASSGTTGKPTVVGYTRKdlDRWAELFARSLRAaGVRPGDRVQNAFGYgLFTGGLGLH-----YGAERLgat 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 210 LVPKY--DADFIHKALQTRGVTIISVVS---KMLTDLLERLGEETYPSSLRCMLLGGGPAPKPLLETCVDK-GIPVYQTY 283
Cdd:COG1541 156 VIPAGggNTERQLRLMQDFGPTVLVGTPsylLYLAEVAEEEGIDPRDLSLKKGIFGGEPWSEEMRKEIEERwGIKAYDIY 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 284 GMTETSSQICT---------LSADYMLTKVgsagkplfqcqLRIEkDGVVVPPLVEGEIVvkgpnVTGgyFNREdAT--- 351
Cdd:COG1541 236 GLTEVGPGVAYeceaqdglhIWEDHFLVEI-----------IDPE-TGEPVPEGEEGELV-----VTT--LTKE-AMpli 295
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446371684 352 RetiqngwLHTGDLGYLDEEG---------FLYVLDRRSDLIISGGENIYPAQIEEVLLSHP 404
Cdd:COG1541 296 R-------YRTGDLTRLLPEPcpcgrthprIGRILGRADDMLIIRGVNVFPSQIEEVLLRIP 350
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
44-415 |
2.49e-17 |
|
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: 84.65 E-value: 2.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 44 LTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSREELLWQMDDAEVVCLVTDQQF-----------DAN 112
Cdd:cd05938 23 LAHAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAKVLVVAPELqeaveevlpalRAD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 113 DVPVYSFAEVMH-------GLKVEASIQEEF--SLEEAMTI------IYTSGTTGKPKGVILTYGNHWASAVGSSLnLGL 177
Cdd:cd05938 103 GVSVWYLSHTSNtegvislLDKVDAASDEPVpaSLRAHVTIkspalyIYTSGTTGLPKAARISHLRVLQCSGFLSL-CGV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 178 RDDDCWLACMPMFHVGGLSL-LMKNIMYGMRILLVPKYDADFIHKALQTRGVTIISVVSKM---LTDLLERLGEETYpsS 253
Cdd:cd05938 182 TADDVIYITLPLYHSSGFLLgIGGCIELGATCVLKPKFSASQFWDDCRKHNVTVIQYIGELlryLCNQPQSPNDRDH--K 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 254 LRcMLLGGGPAPKpLLETCVDK--GIPVYQTYGMTETSsqICTLsaDYMlTKVGSAGK---------PLFQCQLRIEKD- 321
Cdd:cd05938 260 VR-LAIGNGLRAD-VWREFLRRfgPIRIREFYGSTEGN--IGFF--NYT-GKIGAVGRvsylykllfPFELIKFDVEKEe 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 322 --------GVVVPP----LVEGEIVVKGPNVtgGYFNREDAT-----RETIQNG--WLHTGDLGYLDEEGFLYVLDRRSD 382
Cdd:cd05938 333 pvrdaqgfCIPVAKgepgLLVAKITQQSPFL--GYAGDKEQTekkllRDVFKKGdvYFNTGDLLVQDQQNFLYFHDRVGD 410
|
410 420 430
....*....|....*....|....*....|...
gi 446371684 383 LIISGGENIYPAQIEEVLLSHPMVAEAGVVGMT 415
Cdd:cd05938 411 TFRWKGENVATTEVADVLGLLDFLQEVNVYGVT 443
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
52-480 |
4.41e-17 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 84.63 E-value: 4.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 52 GQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSREELLWQMDDAEVVCLVTDQQF--DAN----------------- 112
Cdd:PRK06814 682 GENVGVMLPNANGAAVTFFALQSAGRVPAMINFSAGIANILSACKAAQVKTVLTSRAFieKARlgpliealefgiriiyl 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 113 -DVPvysfAEVMHGLKVEASIQEEFSL--------EEAMTIIYTSGTTGKPKGVILTYGNHWASAVGSSLNLGLRDDDCW 183
Cdd:PRK06814 762 eDVR----AQIGLADKIKGLLAGRFPLvyfcnrdpDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARIDFSPEDKV 837
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 184 LACMPMFHVGGLS--LLMKnIMYGMRILLVPK-----------YDAdfihkalqtrGVTIIsvvskmltdllerLGEETY 250
Cdd:PRK06814 838 FNALPVFHSFGLTggLVLP-LLSGVKVFLYPSplhyriipeliYDT----------NATIL-------------FGTDTF 893
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 251 PS------------SLRCMLLGGGPAPKPLLETCVDK-GIPVYQTYGMTETSSQICTLSAdyMLTKVGSAGKPLFQCQLR 317
Cdd:PRK06814 894 LNgyaryahpydfrSLRYVFAGAEKVKEETRQTWMEKfGIRILEGYGVTETAPVIALNTP--MHNKAGTVGRLLPGIEYR 971
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 318 IEKdgvvVPPLVEGE-IVVKGPNVTGGYFnREDATR--ETIQNGWLHTGDLGYLDEEGFLYVLDRRSDLIISGGENIYPA 394
Cdd:PRK06814 972 LEP----VPGIDEGGrLFVRGPNVMLGYL-RAENPGvlEPPADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLA 1046
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 395 QIEEvllshpMVAEAgvvgmtddkWGQVPAAFVV----KNGE----VTEEEII-------HFCEEKLAKYKVPKKACFLE 459
Cdd:PRK06814 1047 AVEE------LAAEL---------WPDALHAAVSipdaRKGEriilLTTASDAtraaflaHAKAAGASELMVPAEIITID 1111
|
490 500
....*....|....*....|.
gi 446371684 460 ELPRNASKKLLRRELRQLVEE 480
Cdd:PRK06814 1112 EIPLLGTGKIDYVAVTKLAEE 1132
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
15-439 |
4.96e-17 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 83.64 E-value: 4.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 15 TPDRTAIEieeekVTFLQLHEKVVSVCEHLTHVgVKRGQKVAVLMKNGMEMITVIHALSYVGAVAV-LLNTRLS--REEL 91
Cdd:PRK12476 61 SAAGCAVE-----LTWTQLGVRLRAVGARLQQV-AGPGDRVAILAPQGIDYVAGFFAAIKAGTIAVpLFAPELPghAERL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 92 LWQMDDAEVVCLVTDQqfdANDVPVYSFAEVMHGLK---------VEASIQEEFSLEEAMT-----IIYTSGTTGKPKGV 157
Cdd:PRK12476 135 DTALRDAEPTVVLTTT---AAAEAVEGFLRNLPRLRrprviaidaIPDSAGESFVPVELDTddvshLQYTSGSTRPPVGV 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 158 ILTYGNHWASAVGSSLNLGLRDDD----CWLacmPMFHVGGLSLLMKNIMYGMRI-LLVPkydADFIH------KALqTR 226
Cdd:PRK12476 212 EITHRAVGTNLVQMILSIDLLDRNthgvSWL---PLYHDMGLSMIGFPAVYGGHStLMSP---TAFVRrpqrwiKAL-SE 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 227 GVTIISVVSKMLTDLLERLGEETYPSS-----LR--CMLLGGGP-------------APKPLLETCVDKgipvyqTYGMT 286
Cdd:PRK12476 285 GSRTGRVVTAAPNFAYEWAAQRGLPAEgddidLSnvVLIIGSEPvsidavttfnkafAPYGLPRTAFKP------SYGIA 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 287 ETSSQICTLSADYMLTKVG------SAGK------------PLFQC-QLRIEKDGVVVPPLVE--------GEIVVKGPN 339
Cdd:PRK12476 359 EATLFVATIAPDAEPSVVYldreqlGAGRavrvaadapnavAHVSCgQVARSQWAVIVDPDTGaelpdgevGEIWLHGDN 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 340 VTGGYFNREDATRETIQN-------------------GWLHTGDLG-YLDEEgfLYVLDRRSDLIISGGENIYPAQIE-E 398
Cdd:PRK12476 439 IGRGYWGRPEETERTFGAklqsrlaegshadgaaddgTWLRTGDLGvYLDGE--LYITGRIADLIVIDGRNHYPQDIEaT 516
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 446371684 399 VLLSHPMVaEAGVVgmtddkwgqvpAAFVVKnGEVTEEEII 439
Cdd:PRK12476 517 VAEASPMV-RRGYV-----------TAFTVP-AEDNERLVI 544
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
24-406 |
5.60e-17 |
|
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: 83.66 E-value: 5.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 24 EEEKVTFLQLHEKVVSVC-EHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSREELLWQMDDAEVVC 102
Cdd:cd17632 64 RFETITYAELWERVGAVAaAHDPEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRL 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 103 LVTDQqfDANDVPVYSFAEV----------------MHGLKVEAS-----------------------------IQEEFS 137
Cdd:cd17632 144 LAVSA--EHLDLAVEAVLEGgtpprlvvfdhrpevdAHRAALESArerlaavgipvttltliavrgrdlppaplFRPEPD 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 138 LEEAMTIIYTSGTTGKPKGVILTYGNHWASAVGSSLNLGLR-DDDCWLACMPMFHVGGLSLLMKNIMYG----------- 205
Cdd:cd17632 222 DDPLALLIYTSGSTGTPKGAMYTERLVATFWLKVSSIQDIRpPASITLNFMPMSHIAGRISLYGTLARGgtayfaaasdm 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 206 ------------MRILLVPKYdADFIHKALQtRGVTIISVVSKMLTDLLERLGEEtypssLRCMLLGG-------GPAP- 265
Cdd:cd17632 302 stlfddlalvrpTELFLVPRV-CDMLFQRYQ-AELDRRSVAGADAETLAERVKAE-----LRERVLGGrllaavcGSAPl 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 266 ----KPLLETCVDkgIPVYQTYGMTETSSQICTLSA------DYMLTKVGSAGkplfqcQLRIEKdgvvvpPLVEGEIVV 335
Cdd:cd17632 375 saemKAFMESLLD--LDLHDGYGSTEAGAVILDGVIvrppvlDYKLVDVPELG------YFRTDR------PHPRGELLV 440
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446371684 336 KGPNVTGGYFNREDATRETI-QNGWLHTGD-LGYLDEEGFLYVlDRRSDLI-ISGGENIYPAQIEEVLLSHPMV 406
Cdd:cd17632 441 KTDTLFPGYYKRPEVTAEVFdEDGFYRTGDvMAELGPDRLVYV-DRRNNVLkLSQGEFVTVARLEAVFAASPLV 513
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
2-373 |
1.52e-16 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 82.40 E-value: 1.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 2 ETMPNWLKQRAFLTPDRTAIEIEE------EKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEmitviHALSYV 75
Cdd:PRK12582 49 RSIPHLLAKWAAEAPDRPWLAQREpghgqwRKVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIE-----HALMTL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 76 GAVAV------------LLNTRLSR---------------------EELLWQMDDAEVVCLVTDQqfDANDVPVYSFAEV 122
Cdd:PRK12582 124 AAMQAgvpaapvspaysLMSHDHAKlkhlfdlvkprvvfaqsgapfARALAALDLLDVTVVHVTG--PGEGIASIAFADL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 123 MH---GLKVEASIqEEFSLEEAMTIIYTSGTTGKPKGVILTYGNHWASAVGSslnLGLRDDD------CWLACMPMFHVG 193
Cdd:PRK12582 202 AAtppTAAVAAAI-AAITPDTVAKYLFTSGSTGMPKAVINTQRMMCANIAMQ---EQLRPREpdppppVSLDWMPWNHTM 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 194 GLSLLMKNIMYGMRILLVP--KYDADFIHKALqtRGVTIISVVS--------KMLTDLLER---LGEETYpSSLRCMLLG 260
Cdd:PRK12582 278 GGNANFNGLLWGGGTLYIDdgKPLPGMFEETI--RNLREISPTVygnvpagyAMLAEAMEKddaLRRSFF-KNLRLMAYG 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 261 GGPAPKPLLE-------TCVDKGIPVYQTYGMTETssQICTLSADYMLTKVGSAGKPLFQCQLRiekdgvVVPPLVEGEI 333
Cdd:PRK12582 355 GATLSDDLYErmqalavRTTGHRIPFYTGYGATET--APTTTGTHWDTERVGLIGLPLPGVELK------LAPVGDKYEV 426
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 446371684 334 VVKGPNVTGGYFNREDATRETiqngwlhtgdlgyLDEEGF 373
Cdd:PRK12582 427 RVKGPNVTPGYHKDPELTAAA-------------FDEEGF 453
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
144-471 |
5.24e-16 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 80.56 E-value: 5.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 144 IIYTSGTTGKPKGVILTYGNHWASAVGSSLNLGLRDDDC---------WLAcMPMFHVGGLSLLMKNIMYGMRILlVPKY 214
Cdd:PTZ00237 259 ILYTSGTTGNSKAVVRSNGPHLVGLKYYWRSIIEKDIPTvvfshssigWVS-FHGFLYGSLSLGNTFVMFEGGII-KNKH 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 215 DADFIHKALQTRGVTIISVVSKMLTDLL------ERLGEETYPSSLRCMLLGGGPAPKPLLETCVDK-GIPVYQTYGMTE 287
Cdd:PTZ00237 337 IEDDLWNTIEKHKVTHTLTLPKTIRYLIktdpeaTIIRSKYDLSNLKEIWCGGEVIEESIPEYIENKlKIKSSRGYGQTE 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 288 TSsqiCTLSADYMLTKV--GSAGKP-LFQCQLRIEKDGVVVPPLVEGEIVVK---GPNVTGGYFNREDATRETIQN--GW 359
Cdd:PTZ00237 417 IG---ITYLYCYGHINIpyNATGVPsIFIKPSILSEDGKELNVNEIGEVAFKlpmPPSFATTFYKNDEKFKQLFSKfpGY 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 360 LHTGDLGYLDEEGFLYVLDRRSDLIISGGENIYPAQIEEVLLSHPMVAEAGVVGMTDDKWGQVPAAF-VVKNGEVTEE-- 436
Cdd:PTZ00237 494 YNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPIGLlVLKQDQSNQSid 573
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 446371684 437 ------EIIHFCEEKLAKYKVPKKACFLEELPRNASKKLLR 471
Cdd:PTZ00237 574 lnklknEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPR 614
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
139-403 |
5.72e-14 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 74.08 E-value: 5.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 139 EEAMTIIYTSGTTGKPKGVILTYGNHWASAVGSSLNLGLRDDDCWLACMPMFHVGGL-SLLMKNIMYGMRIL-----LVP 212
Cdd:PRK06334 183 EDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSFLPPFHAYGFnSCTLFPLLSGVPVVfaynpLYP 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 213 KYDADFIHKALQT-RGVT------IISVVSKmltdllerlgEETYPSSLRCMLLGGGpAPKPLLETCVDKGIP---VYQT 282
Cdd:PRK06334 263 KKIVEMIDEAKVTfLGSTpvffdyILKTAKK----------QESCLPSLRFVVIGGD-AFKDSLYQEALKTFPhiqLRQG 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 283 YGMTETSSQIcTLSADYMLTKVGSAGKPLFQCQLRI--EKDGVVVPPLVEGEIVVKGPNVTGGYFNrEDATRETIQNG-- 358
Cdd:PRK06334 332 YGTTECSPVI-TINTVNSPKHESCVGMPIRGMDVLIvsEETKVPVSSGETGLVLTRGTSLFSGYLG-EDFGQGFVELGge 409
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 446371684 359 -WLHTGDLGYLDEEGFLYVLDRRSDLIISGGENIYPAQIEEVLLSH 403
Cdd:PRK06334 410 tWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEG 455
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
16-474 |
1.82e-13 |
|
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: 72.12 E-value: 1.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 16 PDRTAIEIEEEK----VTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSREEL 91
Cdd:cd17654 1 PDRPALIIDQTTsdttVSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 92 LWQMDDAEVVCLVTDQQFDandvpvySFAEVMHGLKVEASIQEEFSLeeaMTIIYTSGTTGKPKGVILTYGNHWASAVGS 171
Cdd:cd17654 81 LTVMKKCHVSYLLQNKELD-------NAPLSFTPEHRHFNIRTDECL---AYVIHTSGTTGTPKIVAVPHKCILPNIQHF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 172 SLNLGLRDDDCWLACMPM------------FHVGGLSLLMKNIMYGMRILLVpkyDADFIHKALQTRGVTiisvvskmlT 239
Cdd:cd17654 151 RSLFNITSEDILFLTSPLtfdpsvveiflsLSSGATLLIVPTSVKVLPSKLA---DILFKRHRITVLQAT---------P 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 240 DLLERLGEETYP-------SSLRCMLLGGGPAPKPLLETC---VDKGIPVYQTYGMTETSSQictlsADYMLTKVGSA-- 307
Cdd:cd17654 219 TLFRRFGSQSIKstvlsatSSLRVLALGGEPFPSLVILSSwrgKGNRTRIFNIYGITEVSCW-----ALAYKVPEEDSpv 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 308 --GKPLFQCQLRIEKdgvVVPPLVEGEIVVKGPNvtGGYFNREDATRETIQngWLHTGDLGYLdEEGFLYVLDRRSDLII 385
Cdd:cd17654 294 qlGSPLLGTVIEVRD---QNGSEGTGQVFLGGLN--RVCILDDEVTVPKGT--MRATGDFVTV-KDGELFFLGRKDSQIK 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 386 SGGENIYPAQIEEVLLSHPMVaEAGVVGMTDDkwgQVPAAFVVKNGEVTEEeiihFCE---EKLAKYKVPKKACFLEELP 462
Cdd:cd17654 366 RRGKRINLDLIQQVIESCLGV-ESCAVTLSDQ---QRLIAFIVGESSSSRI----HKElqlTLLSSHAIPDTFVQIDKLP 437
|
490
....*....|..
gi 446371684 463 RNASKKLLRREL 474
Cdd:cd17654 438 LTSHGKVDKSEL 449
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
139-480 |
2.34e-12 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 69.35 E-value: 2.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 139 EEAMTIIYTSGTTGKPKGVILTYGNHWASAVGSSLNLGLRDDDCWLACMPMFHVGGLSL-LMKNIMYGMRILLVPK---- 213
Cdd:PRK08043 365 EDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPNDRFMSALPLFHSFGLTVgLFTPLLTGAEVFLYPSplhy 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 214 -------YDadfihkalqtRGVTIISVVSKMLTDLlERLGEETYPSSLRCMLLGGGPAPKPLLETCVDK-GIPVYQTYGM 285
Cdd:PRK08043 445 rivpelvYD----------RNCTVLFGTSTFLGNY-ARFANPYDFARLRYVVAGAEKLQESTKQLWQDKfGLRILEGYGV 513
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 286 TETSSQICTLSAdyMLTKVGSAGKPLFQCQLRIekdgVVVPPLVEG-EIVVKGPNVTGGYFNRE----------DATRET 354
Cdd:PRK08043 514 TECAPVVSINVP--MAAKPGTVGRILPGMDARL----LSVPGIEQGgRLQLKGPNIMNGYLRVEkpgvlevptaENARGE 587
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 355 IQNGWLHTGDLGYLDEEGFLYVLDRRSDLIISGGENIYPAQIEEVLLSHPMVAEAGVVGMTDDKWGQVPAAFVVkNGEVT 434
Cdd:PRK08043 588 MERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKQHATAIKSDASKGEALVLFTT-DSELT 666
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 446371684 435 EEEIIHFCEEK-LAKYKVPKKACFLEELPRNASKKLLRRELRQLVEE 480
Cdd:PRK08043 667 REKLQQYAREHgVPELAVPRDIRYLKQLPLLGSGKPDFVTLKSMVDE 713
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
24-397 |
2.69e-12 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 68.99 E-value: 2.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 24 EEEKVTFLQLHEKVVSVCEHLTHVGvKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLntrLSREE------LLWQMDD 97
Cdd:PRK07769 52 VARDLTWSQFGARNRAVGARLQQVT-KPGDRVAILAPQNLDYLIAFFGALYAGRIAVPL---FDPAEpghvgrLHAVLDD 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 98 AEVVCLVTD-------QQF----DANDVP----VYSFAEVMHGLKVEASIQEEfsleeamTIIY---TSGTTGKPKGVIL 159
Cdd:PRK07769 128 CTPSAILTTtdsaegvRKFfrarPAKERPrviaVDAVPDEVGATWVPPEANED-------TIAYlqyTSGSTRIPAGVQI 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 160 TYGNHWASAVGSSLNLGLRDDDCWLACMPMFHVGGLSLLMKNIMYGMRI-LLVPkydADFIHK---------ALQTRGVT 229
Cdd:PRK07769 201 THLNLPTNVLQVIDALEGQEGDRGVSWLPFFHDMGLITVLLPALLGHYItFMSP---AAFVRRpgrwirelaRKPGGTGG 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 230 IISVVSKMLTDL-----LERLGEETYP-SSLRCMLLGGGP----APKPLLETCVDKGIP---VYQTYGMTETSSQICT-- 294
Cdd:PRK07769 278 TFSAAPNFAFEHaaargLPKDGEPPLDlSNVKGLLNGSEPvspaSMRKFNEAFAPYGLPptaIKPSYGMAEATLFVSTtp 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 295 --------------LSADYMLTKVGSAGKPLFQC---QLRIEKDGVVVPP--LVE------GEIVVKGPNVTGGYFNRED 349
Cdd:PRK07769 358 mdeeptviyvdrdeLNAGRFVEVPADAPNAVAQVsagKVGVSEWAVIVDPetASElpdgqiGEIWLHGNNIGTGYWGKPE 437
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446371684 350 ATRETIQN------------------GWLHTGDLG-YLDEEgfLYVLDRRSDLIISGGENIYPAQIE 397
Cdd:PRK07769 438 ETAATFQNilksrlseshaegapddaLWVRTGDYGvYFDGE--LYITGRVKDLVIIDGRNHYPQDLE 502
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
8-373 |
4.84e-12 |
|
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: 68.23 E-value: 4.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 8 LKQRAFLTPDRTAIEIEE-----EKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAV-- 80
Cdd:cd05921 1 LAHWARQAPDRTWLAEREgnggwRRVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAApv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 81 -----LLNTRLSREELLWQM--------DDAE--------VVCLVTDQQFDANDVP---VYSFAEVMH---GLKVEASiq 133
Cdd:cd05921 81 spaysLMSQDLAKLKHLFELlkpglvfaQDAApfaralaaIFPLGTPLVVSRNAVAgrgAISFAELAAtppTAAVDAA-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 134 eeFSLEEAMTI---IYTSGTTGKPKGVILTYGNHWASAVGSSLNLGLRDDD--CWLACMPMFHVGGLSLLMKNIMYGMRI 208
Cdd:cd05921 159 --FAAVGPDTVakfLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFFGEEppVLVDWLPWNHTFGGNHNFNLVLYNGGT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 209 LL------VPKYDADFIhKALQTRGVTIISVVSK---MLTDLLER---LGEETYpSSLRCMLLGGGPAPKPLLETC---- 272
Cdd:cd05921 237 LYiddgkpMPGGFEETL-RNLREISPTVYFNVPAgweMLVAALEKdeaLRRRFF-KRLKLMFYAGAGLSQDVWDRLqala 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 273 ---VDKGIPVYQTYGMTETSSQICTLSADymLTKVGSAGKPLFQCQLRIekdgvvVPPLVEGEIVVKGPNVTGGYFNRED 349
Cdd:cd05921 315 vatVGERIPMMAGLGATETAPTATFTHWP--TERSGLIGLPAPGTELKL------VPSGGKYEVRVKGPNVTPGYWRQPE 386
|
410 420
....*....|....*....|....
gi 446371684 350 ATRETiqngwlhtgdlgyLDEEGF 373
Cdd:cd05921 387 LTAQA-------------FDEEGF 397
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
144-474 |
1.52e-11 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 67.12 E-value: 1.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 144 IIYTSGTTGKPKGVILTYG---NHWASAVgSSLNLGLRDDDCWLACMPmFHVGGLSLLMKNiMYGMRILLVPK---YDAD 217
Cdd:PRK05691 3874 VIYTSGSTGLPKGVMVEQRgmlNNQLSKV-PYLALSEADVIAQTASQS-FDISVWQFLAAP-LFGARVEIVPNaiaHDPQ 3950
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 218 FIHKALQTRGVTIISVVSKMLTDLLERlgEETYPSSLRCMLLGGGPAPKPLLETCVDK--GIPVYQTYGMTETSSQICTL 295
Cdd:PRK05691 3951 GLLAHVQAQGITVLESVPSLIQGMLAE--DRQALDGLRWMLPTGEAMPPELARQWLQRypQIGLVNAYGPAECSDDVAFF 4028
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 296 SADYMLTKvGS---AGKPLFQCQLRIEKDGVVVPPL-VEGEIVVKGPNVTGGYFNreDATReTIQNGWLH---------- 361
Cdd:PRK05691 4029 RVDLASTR-GSylpIGSPTDNNRLYLLDEALELVPLgAVGELCVAGTGVGRGYVG--DPLR-TALAFVPHpfgapgerly 4104
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 362 -TGDLGYLDEEGFLYVLDRRSDLIISGGENIYPAQIEEVLLSHPMVAEAgVVGMTDDKWGQVPAAFVV-KNGEVTEEEII 439
Cdd:PRK05691 4105 rTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREA-AVAVQEGVNGKHLVGYLVpHQTVLAQGALL 4183
|
330 340 350
....*....|....*....|....*....|....*....
gi 446371684 440 HFCEEKL----AKYKVPKKACFLEELPRNASKKLLRREL 474
Cdd:PRK05691 4184 ERIKQRLraelPDYMVPLHWLWLDRLPLNANGKLDRKAL 4222
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
143-391 |
1.88e-11 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 66.28 E-value: 1.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 143 TIIYTSGTTGKPKGVILTYGNHWaSAVGSSLNLGLRDD---DCWLACMPMFHVGGLSLLMKNIMYGMRILLVPKyDADFI 219
Cdd:PTZ00342 308 SIVYTSGTSGKPKGVMLSNKNLY-NTVVPLCKHSIFKKynpKTHLSYLPISHIYERVIAYLSFMLGGTINIWSK-DINYF 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 220 HKALQTRGVTIISVVSKM-------------------------------------LTDLLE-------RLGEETYPSsLR 255
Cdd:PTZ00342 386 SKDIYNSKGNILAGVPKVfnriytnimteinnlpplkrflvkkilslrksnnnggFSKFLEgithissKIKDKVNPN-LE 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 256 CMLLGGGP-APKPLLETCVDKGIPVYQTYGMTETSSQICTLSA-DYMLTKVGSAGKPLFQCQLRI-EK-DGVVVPPlvEG 331
Cdd:PTZ00342 465 VILNGGGKlSPKIAEELSVLLNVNYYQGYGLTETTGPIFVQHAdDNNTESIGGPISPNTKYKVRTwETyKATDTLP--KG 542
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446371684 332 EIVVKGPNVTGGYFNREDATRETIQN-GWLHTGDLGYLDEEGFLYVLDRRSDLI-ISGGENI 391
Cdd:PTZ00342 543 ELLIKSDSIFSGYFLEKEQTKNAFTEdGYFKTGDIVQINKNGSLTFLDRSKGLVkLSQGEYI 604
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
3-397 |
1.94e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 66.12 E-value: 1.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 3 TMPNWLKQRAFLTPDRTA---IEIE------EEKVTFLQLHEKVVSVCEHLTHVGVKrGQKVAVLMKNGMEMItvihaLS 73
Cdd:PRK05850 2 SVPSLLRERASLQPDDAAftfIDYEqdpagvAETLTWSQLYRRTLNVAEELRRHGST-GDRAVILAPQGLEYI-----VA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 74 YVGA-----VAVLLNT---RLSREELLWQMDDAE-VVCLVTDQqfDANDVPVY----------SFAEVmHGLKVEASIQE 134
Cdd:PRK05850 76 FLGAlqaglIAVPLSVpqgGAHDERVSAVLRDTSpSVVLTTSA--VVDDVTEYvapqpgqsapPVIEV-DLLDLDSPRGS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 135 EF---SLEEAMTIIYTSGTTGKPKGVILTYGNHWASaVGSSLNLGLRDDDC----------WL-----------ACMPMf 190
Cdd:PRK05850 153 DArprDLPSTAYLQYTSGSTRTPAGVMVSHRNVIAN-FEQLMSDYFGDTGGvpppdttvvsWLpfyhdmglvlgVCAPI- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 191 hVGG--------LSLLMKNIMYgMRIL--------LVPKY----------DADFIhkALQTRGV-TIIS----VVSKMLT 239
Cdd:PRK05850 231 -LGGcpavltspVAFLQRPARW-MQLLasnphafsAAPNFafelavrktsDDDMA--GLDLGGVlGIISgserVHPATLK 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 240 DLLERLgeetypsslrcmllgggpAPKPLLETCVDkgiPvyqTYGMTETSSQICT----------------LSADYMLTK 303
Cdd:PRK05850 307 RFADRF------------------APFNLRETAIR---P---SYGLAEATVYVATrepgqppesvrfdyekLSAGHAKRC 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 304 VGSAGKPLFQCQ------LRI--EKDGVVVPPLVEGEIVVKGPNVTGGYFNREDATRETIQ------------NGWLHTG 363
Cdd:PRK05850 363 ETGGGTPLVSYGsprsptVRIvdPDTCIECPAGTVGEIWVHGDNVAAGYWQKPEETERTFGatlvdpspgtpeGPWLRTG 442
|
490 500 510
....*....|....*....|....*....|....
gi 446371684 364 DLGYLDeEGFLYVLDRRSDLIISGGENIYPAQIE 397
Cdd:PRK05850 443 DLGFIS-EGELFIVGRIKDLLIVDGRNHYPDDIE 475
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
2-375 |
1.48e-10 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 63.36 E-value: 1.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 2 ETMPNWLKQRAFLTPDRTAI-----EIEEEKVTFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVG 76
Cdd:PRK08180 39 RRLTDRLVHWAQEAPDRVFLaergaDGGWRRLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALAAMYAG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 77 AVAV-------LLNTRLSR-----EEL---LWQMDDAEV------------VCLVTDQQfDANDVPVYSFAEVMhGLKVE 129
Cdd:PRK08180 119 VPYApvspaysLVSQDFGKlrhvlELLtpgLVFADDGAAfaralaavvpadVEVVAVRG-AVPGRAATPFAALL-ATPPT 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 130 ASIQEEFsleEAMT------IIYTSGTTGKPKGVILTYGNHWASAVGSSLNLG-LRDDD----CWLacmPMFHVGGLSLL 198
Cdd:PRK08180 197 AAVDAAH---AAVGpdtiakFLFTSGSTGLPKAVINTHRMLCANQQMLAQTFPfLAEEPpvlvDWL---PWNHTFGGNHN 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 199 MKNIMY-G--MRIllvpkyD-----ADFIHKALQT-RGV--TIISVVSK---MLTDLLERLGE--ETYPSSLRCMLLGGG 262
Cdd:PRK08180 271 LGIVLYnGgtLYI------DdgkptPGGFDETLRNlREIspTVYFNVPKgweMLVPALERDAAlrRRFFSRLKLLFYAGA 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 263 PAPKPLLE--------TCVDKgIPVYQTYGMTETSSqiCTLSADYMLTKVGSAGKPLFQCQLRIekdgvvVPplVEG--E 332
Cdd:PRK08180 345 ALSQDVWDrldrvaeaTCGER-IRMMTGLGMTETAP--SATFTTGPLSRAGNIGLPAPGCEVKL------VP--VGGklE 413
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 446371684 333 IVVKGPNVTGGYFNREDATRETI-QNGWLHTGDLG-YLDEE----GFLY 375
Cdd:PRK08180 414 VRVKGPNVTPGYWRAPELTAEAFdEEGYYRSGDAVrFVDPAdperGLMF 462
|
|
| PRK07868 |
PRK07868 |
acyl-CoA synthetase; Validated |
29-475 |
7.21e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236121 [Multi-domain] Cd Length: 994 Bit Score: 61.66 E-value: 7.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 29 TFLQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLL--------NTRLSR-EELLWQMDDAE 99
Cdd:PRK07868 474 TYEAVNRRINNVVRGLIAVGVRQGDRVGVLMETRPSALVAIAALSRLGAVAVLMppdtdlaaAVRLGGvTEIITDPTNLE 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 100 VVCLVTDQQF-----DANDVPVYSFAEVMHGLKVEASIQE---------EFSLEEAMTIIYTSGTTGKPKGVIltygNH- 164
Cdd:PRK07868 554 AARQLPGRVLvlgggESRDLDLPDDADVIDMEKIDPDAVElpgwyrpnpGLARDLAFIAFSTAGGELVAKQIT----NYr 629
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 165 WA-SAVG--SSLNLGLRDDDCWLAcmPMFHVGGLSL-LMKNIMYGMRILLVPKYDADFIHKALQTRGVTIISVVSKMLTD 240
Cdd:PRK07868 630 WAlSAFGtaSAAALDRRDTVYCLT--PLHHESGLLVsLGGAVVGGSRIALSRGLDPDRFVQEVRQYGVTVVSYTWAMLRE 707
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 241 LLERLGEETYPSSLRCMLLGGGpAPKPLLETCVDKGIP--VYQTYGMTETSSQICTLSADymltKVGSAGKPL------- 311
Cdd:PRK07868 708 VVDDPAFVLHGNHPVRLFIGSG-MPTGLWERVVEAFAPahVVEFFATTDGQAVLANVSGA----KIGSKGRPLpgagrve 782
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 312 -----FQCQLRIEKDGVVVPPLVEGEIVV-----KGP-----NVTGGYFNREDAtretiqngWLHTGDLGYLDEEGFLYV 376
Cdd:PRK07868 783 laaydPEHDLILEDDRGFVRRAEVNEVGVllaraRGPidptaSVKRGVFAPADT--------WISTEYLFRRDDDGDYWL 854
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 377 LDRRSDLIISGGENIYPAQIEEVLLSHPMVAEAGVVGMTDDKWGQVPAAFVVKNGE-VTEEEIihfcEEKLAKYKV---P 452
Cdd:PRK07868 855 VDRRGSVIRTARGPVYTEPVTDALGRIGGVDLAVTYGVEVGGRQLAVAAVTLRPGAaITAADL----TEALASLPVglgP 930
|
490 500
....*....|....*....|...
gi 446371684 453 KKACFLEELPRNASKKLLRRELR 475
Cdd:PRK07868 931 DIVHVVPEIPLSATYRPTVSALR 953
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
331-411 |
1.87e-04 |
|
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: 43.88 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371684 331 GEIVVKGPNVTGGYF--------NREDATRETIQ-----NGWLHTGDLGYL----------DEEGFLYVLDRRSDLIISG 387
Cdd:cd05905 389 GEIWVNSPANASGYFlldgetndTFKVFPSTRLStgitnNSYARTGLLGFLrptkctdlnvEEHDLLFVVGSIDETLEVR 468
|
90 100
....*....|....*....|....*
gi 446371684 388 GENIYPAQIEE-VLLSHPMVAEAGV 411
Cdd:cd05905 469 GLRHHPSDIEAtVMRVHPYRGRCAV 493
|
|
| |
