|
Name |
Accession |
Description |
Interval |
E-value |
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
1-509 |
0e+00 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 855.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 1 MNLVSKLEETASEKPDSIACRFKDHMMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVP 80
Cdd:PRK07656 5 MTLPELLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 81 INPLYTPTEIGYMLTNGDVKAIVGVSQLLPLYECMHESLPKVELVILCQTGEAEPEAAdpevrmKMTTFAKILRPTSAAK 160
Cdd:PRK07656 85 LNTRYTADEAAYILARGDAKALFVLGLFLGVDYSATTRLPALEHVVICETEEDDPHTE------KMKTFTDFLAAGDPAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 161 QNQELVPDDTAVILYTSGTTGKPKGAMLTHQNLYSNANDVAGYLGMDERDNVVCALPMFHVFCLTVCMNAPLMSGATVLI 240
Cdd:PRK07656 159 RAPEVDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLAANPFFHVFGYKAGVNAPLMRGATILP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 241 EPQFSPASVFKLVKQQQVTIFAGVPTMYNYLFQHENGKKDDFSSIRLCISGGAAMPVALLTAFEEKFGV-TILEGYGLSE 319
Cdd:PRK07656 239 LPVFDPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSAEDLSSLRLAVTGAASMPVALLERFESELGVdIVLTGYGLSE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 320 ASPVTCFNPFDRGRK--PGSIGTSILHVENKVVDPLGRELPAHQVGELIVKGPNVMKGYYKMPMETEHALK-DGWLYTGD 396
Cdd:PRK07656 319 ASGVTTFNRLDDDRKtvAGTIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDDPEATAAAIDaDGWLHTGD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 397 LARRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVVPKR-SGVTEEDIMQHC 475
Cdd:PRK07656 399 LGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVLKPgAELTEEELIAYC 478
|
490 500 510
....*....|....*....|....*....|....
gi 1816047872 476 ETHLAKYKRPAAITFLDDIPKNATGKMLRRALRD 509
Cdd:PRK07656 479 REHLAKYKVPRSIEFLDELPKNATGKVLKRALRE 512
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
3-508 |
0e+00 |
|
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: 727.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 3 LVSKLEETASEKPDSIACRFKDHMMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPIN 82
Cdd:cd05936 1 LADLLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 83 PLYTPTEIGYMLTNGDVKAIVGVsqllplyecmheslpkvelvilcqtgeaepeaadpevrmkmTTFAKILRPTSAAKQN 162
Cdd:cd05936 81 PLYTPRELEHILNDSGAKALIVA-----------------------------------------VSFTDLLAAGAPLGER 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 163 QELVPDDTAVILYTSGTTGKPKGAMLTHQNLYSNANDVAGYLG--MDERDNVVCALPMFHVFCLTVCMNAPLMSGATVLI 240
Cdd:cd05936 120 VALTPEDVAVLQYTSGTTGVPKGAMLTHRNLVANALQIKAWLEdlLEGDDVVLAALPLFHVFGLTVALLLPLALGATIVL 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 241 EPQFSPASVFKLVKQQQVTIFAGVPTMYNYLFQHENGKKDDFSSIRLCISGGAAMPVALLTAFEEKFGVTILEGYGLSEA 320
Cdd:cd05936 200 IPRFRPIGVLKEIRKHRVTIFPGVPTMYIALLNAPEFKKRDFSSLRLCISGGAPLPVEVAERFEELTGVPIVEGYGLTET 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 321 SPVTCFNPFDRGRKPGSIGTSILHVENKVVDPLGRELPAHQVGELIVKGPNVMKGYYKMPMETEHALKDGWLYTGDLARR 400
Cdd:cd05936 280 SPVVAVNPLDGPRKPGSIGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFVDGWLRTGDIGYM 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 401 DEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVVPKR-SGVTEEDIMQHCETHL 479
Cdd:cd05936 360 DEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEgASLTEEEIIAFCREQL 439
|
490 500
....*....|....*....|....*....
gi 1816047872 480 AKYKRPAAITFLDDIPKNATGKMLRRALR 508
Cdd:cd05936 440 AGYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
3-511 |
0e+00 |
|
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: 614.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 3 LVSKLEETASEKPDSIACRFKDHMMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPIN 82
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 83 PLYTPTEIGYMLTNGDVKAIVgvsqllplyecmheslpkvelvilcqtgeaepeaadpevrmkmttfakilrptsaakqn 162
Cdd:COG0318 81 PRLTAEELAYILEDSGARALV----------------------------------------------------------- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 163 qelvpddTAVILYTSGTTGKPKGAMLTHQNLYSNANDVAGYLGMDERDNVVCALPMFHVFCLTVCMNAPLMSGATVLIEP 242
Cdd:COG0318 102 -------TALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLP 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 243 QFSPASVFKLVKQQQVTIFAGVPTMYNYLFQHENGKKDDFSSIRLCISGGAAMPVALLTAFEEKFGVTILEGYGLSEASP 322
Cdd:COG0318 175 RFDPERVLELIERERVTVLFGVPTMLARLLRHPEFARYDLSSLRLVVSGGAPLPPELLERFEERFGVRIVEGYGLTETSP 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 323 VTCFNPFDRG-RKPGSIGTSILHVENKVVDPLGRELPAHQVGELIVKGPNVMKGYYKMPMETEHALKDGWLYTGDLARRD 401
Cdd:COG0318 255 VVTVNPEDPGeRRPGSVGRPLPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAFRDGWLRTGDLGRLD 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 402 EDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVVPKR-SGVTEEDIMQHCETHLA 480
Cdd:COG0318 335 EDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPgAELDAEELRAFLRERLA 414
|
490 500 510
....*....|....*....|....*....|.
gi 1816047872 481 KYKRPAAITFLDDIPKNATGKMLRRALRDIL 511
Cdd:COG0318 415 RYKVPRRVEFVDELPRTASGKIDRRALRERY 445
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
1-509 |
0e+00 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 551.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 1 MNLVSKLEETASEKPDSIACRFKDHMMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVP 80
Cdd:PRK06187 6 LTIGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 81 INPLYTPTEIGYMLTNGDVKAIVGVSQLLPLYECMHESLPKVELVILcqTGEAEPEAADPEVRmkmtTFAKILRPTSAAK 160
Cdd:PRK06187 86 INIRLKPEEIAYILNDAEDRVVLVDSEFVPLLAAILPQLPTVRTVIV--EGDGPAAPLAPEVG----EYEELLAAASDTF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 161 QNQELVPDDTAVILYTSGTTGKPKGAMLTHQNLYSNANDVAGYLGMDERDNVVCALPMFHVFCLTVCMnAPLMSGATVLI 240
Cdd:PRK06187 160 DFPDIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVPMFHVHAWGLPY-LALMAGAKQVI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 241 EPQFSPASVFKLVKQQQVTIFAGVPTMYNYLFQHENGKKDDFSSIRLCISGGAAMPVALLTAFEEKFGVTILEGYGLSEA 320
Cdd:PRK06187 239 PRRFDPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYFVDFSSLRLVIYGGAALPPALLREFKEKFGIDLVQGYGMTET 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 321 SPVTCFNPFDRG-----RKPGSIGTSILHVENKVVDPLGRELPAH--QVGELIVKGPNVMKGYYKMPMETEHALKDGWLY 393
Cdd:PRK06187 319 SPVVSVLPPEDQlpgqwTKRRSAGRPLPGVEARIVDDDGDELPPDggEVGEIIVRGPWLMQGYWNRPEATAETIDGGWLH 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 394 TGDLARRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVVPKR-SGVTEEDIM 472
Cdd:PRK06187 399 TGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVLKPgATLDAKELR 478
|
490 500 510
....*....|....*....|....*....|....*..
gi 1816047872 473 QHCETHLAKYKRPAAITFLDDIPKNATGKMLRRALRD 509
Cdd:PRK06187 479 AFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVLRE 515
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
7-504 |
4.78e-168 |
|
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: 482.11 E-value: 4.78e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 7 LEETASEKPDSIACRFKDHMMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYT 86
Cdd:cd17631 1 LRRRARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 87 PTEIGYMLTNGDVKAIVgvsqllplyecmheslpkvelvilcqtgeaepeaadpevrmkmttfakilrptsaakqnqelv 166
Cdd:cd17631 81 PPEVAYILADSGAKVLF--------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 167 pDDTAVILYTSGTTGKPKGAMLTHQNLYSNANDVAGYLGMDERDNVVCALPMFHVFCLTVCMNAPLMSGATVLIEPQFSP 246
Cdd:cd17631 98 -DDLALLMYTSGTTGRPKGAMLTHRNLLWNAVNALAALDLGPDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVILRKFDP 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 247 ASVFKLVKQQQVTIFAGVPTMYNYLFQHENGKKDDFSSIRLCISGGAAMPVALLTAFEEkFGVTILEGYGLSEASPVTCF 326
Cdd:cd17631 177 ETVLDLIERHRVTSFFLVPTMIQALLQHPRFATTDLSSLRAVIYGGAPMPERLLRALQA-RGVKFVQGYGMTETSPGVTF 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 327 N-PFDRGRKPGSIGTSILHVENKVVDPLGRELPAHQVGELIVKGPNVMKGYYKMPMETEHALKDGWLYTGDLARRDEDGY 405
Cdd:cd17631 256 LsPEDHRRKLGSAGRPVFFVEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFRDGWFHTGDLGRLDEDGY 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 406 FYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVVPK-RSGVTEEDIMQHCETHLAKYKR 484
Cdd:cd17631 336 LYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRpGAELDEDELIAHCRERLARYKI 415
|
490 500
....*....|....*....|
gi 1816047872 485 PAAITFLDDIPKNATGKMLR 504
Cdd:cd17631 416 PKSVEFVDALPRNATGKILK 435
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
169-501 |
8.14e-152 |
|
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: 436.72 E-value: 8.14e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 169 DTAVILYTSGTTGKPKGAMLTHQNLYSNANDVAGYLGMDERDNVVCALPMFHVFCLTvCMNAPLMSGATVLIEPQFSPAS 248
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLF-GLLGALLAGGTVVLLPKFDPEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 249 VFKLVKQQQVTIFAGVPTMYNYLFQHENGKKDDFSSIRLCISGGAAMPVALLTAFEEKFGVTILEGYGLSEAS-PVTCFN 327
Cdd:cd04433 80 ALELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGgTVATGP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 328 PFDRGRKPGSIGTSILHVENKVVDPLGRELPAHQVGELIVKGPNVMKGYYKMPMETEHALKDGWLYTGDLARRDEDGYFY 407
Cdd:cd04433 160 PDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVDEDGWYRTGDLGRLDEDGYLY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 408 IVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVVPKR-SGVTEEDIMQHCETHLAKYKRPA 486
Cdd:cd04433 240 IVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPgADLDAEELRAHVRERLAPYKVPR 319
|
330
....*....|....*
gi 1816047872 487 AITFLDDIPKNATGK 501
Cdd:cd04433 320 RVVFVDALPRTASGK 334
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
7-419 |
4.18e-148 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 430.58 E-value: 4.18e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 7 LEETASEKPDSIAC-RFKDHMMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLY 85
Cdd:pfam00501 1 LERQAARTPDKTALeVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 86 TPTEIGYMLTNGDVKAIVGVSqlLPLYECMHESLPKVELVILCQTGEAEPEAADPEVrmkmttFAKILRPTSAAKQNQEL 165
Cdd:pfam00501 81 PAEELAYILEDSGAKVLITDD--ALKLEELLEALGKLEVVKLVLVLDRDPVLKEEPL------PEEAKPADVPPPPPPPP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 166 VPDDTAVILYTSGTTGKPKGAMLTHQNLYSNANDVAGY----LGMDERDNVVCALPMFHVFCLTVCMNAPLMSGATVLI- 240
Cdd:pfam00501 153 DPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVrprgFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVVLp 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 241 --EPQFSPASVFKLVKQQQVTIFAGVPTMYNYLFQHENGKKDDFSSIRLCISGGAAMPVALLTAFEEKFGVTILEGYGLS 318
Cdd:pfam00501 233 pgFPALDPAALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSSLRLVLSGGAPLPPELARRFRELFGGALVNGYGLT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 319 EASPVTC--FNPFDRGRKPGSIGTSILHVENKVVDPL-GRELPAHQVGELIVKGPNVMKGYYKMPMETEHALK-DGWLYT 394
Cdd:pfam00501 313 ETTGVVTtpLPLDEDLRSLGSVGRPLPGTEVKIVDDEtGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDeDGWYRT 392
|
410 420
....*....|....*....|....*
gi 1816047872 395 GDLARRDEDGYFYIVDRKKDMIIVG 419
Cdd:pfam00501 393 GDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
2-509 |
7.09e-148 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 435.25 E-value: 7.09e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 2 NLVSKLEETASEKPDSIACRFKDHMMTYQELNEHIQRFADGLQ-EAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVP 80
Cdd:PRK08974 24 SLVDMFEQAVARYADQPAFINMGEVMTFRKLEERSRAFAAYLQnGLGLKKGDRVALMMPNLLQYPIALFGILRAGMIVVN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 81 INPLYTPTEIGYMLTNGDVKAIVGVSQLLPLYECMHESLPkVELVILCQTGEAEPEAADPEVRM------KM-------- 146
Cdd:PRK08974 104 VNPLYTPRELEHQLNDSGAKAIVIVSNFAHTLEKVVFKTP-VKHVILTRMGDQLSTAKGTLVNFvvkyikRLvpkyhlpd 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 147 -TTFAKILrptSAAKQNQ----ELVPDDTAVILYTSGTTGKPKGAMLTHQNLYSN---ANDVAGYLGMDERDNVVCALPM 218
Cdd:PRK08974 183 aISFRSAL---HKGRRMQyvkpELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANleqAKAAYGPLLHPGKELVVTALPL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 219 FHVFCLTV-CMNAPLMSGATVLI-EPQFSPASVfKLVKQQQVTIFAGVPTMYNYLFQHENGKKDDFSSIRLCISGGAAMP 296
Cdd:PRK08974 260 YHIFALTVnCLLFIELGGQNLLItNPRDIPGFV-KELKKYPFTAITGVNTLFNALLNNEEFQELDFSSLKLSVGGGMAVQ 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 297 VALLTAFEEKFGVTILEGYGLSEASPVTCFNPFDRGRKPGSIGTSILHVENKVVDPLGRELPAHQVGELIVKGPNVMKGY 376
Cdd:PRK08974 339 QAVAERWVKLTGQYLLEGYGLTECSPLVSVNPYDLDYYSGSIGLPVPSTEIKLVDDDGNEVPPGEPGELWVKGPQVMLGY 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 377 YKMPMETEHALKDGWLYTGDLARRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVK 456
Cdd:PRK08974 419 WQRPEATDEVIKDGWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAVK 498
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1816047872 457 GYVVPKRSGVTEEDIMQHCETHLAKYKRPAAITFLDDIPKNATGKMLRRALRD 509
Cdd:PRK08974 499 IFVVKKDPSLTEEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELRD 551
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
24-509 |
1.37e-147 |
|
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: 432.12 E-value: 1.37e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 24 DHMMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYTPTEIGYMLTNGDVKAIV 103
Cdd:cd05926 12 TPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 104 gvSQLLPLYECMhESLPKVELVILcqtgEAEPEAADPEVRMKMTTFAKILRPTSAAKQNQELVPDDTAVILYTSGTTGKP 183
Cdd:cd05926 92 --TPKGELGPAS-RAASKLGLAIL----ELALDVGVLIRAPSAESLSNLLADKKNAKSEGVPLPDDLALILHTSGTTGRP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 184 KGAMLTHQNLYSNANDVAGYLGMDERDNVVCALPMFHVFCLTVCMNAPLMSGATVLIEPQFSPASVFKLVKQQQVTIFAG 263
Cdd:cd05926 165 KGVPLTHRNLAASATNITNTYKLTPDDRTLVVMPLFHVHGLVASLLSTLAAGGSVVLPPRFSASTFWPDVRDYNATWYTA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 264 VPTMYNYLFQHENGKKDD-FSSIRLCISGGAAMPVALLTAFEEKFGVTILEGYGLSEASP-VTCfNPFDRG-RKPGSIGT 340
Cdd:cd05926 245 VPTIHQILLNRPEPNPESpPPKLRFIRSCSASLPPAVLEALEATFGAPVLEAYGMTEAAHqMTS-NPLPPGpRKPGSVGK 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 341 SIlHVENKVVDPLGRELPAHQVGELIVKGPNVMKGYYKMPMET-EHALKDGWLYTGDLARRDEDGYFYIVDRKKDMIIVG 419
Cdd:cd05926 324 PV-GVEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANaEAAFKDGWFRTGDLGYLDADGYLFLTGRIKELINRG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 420 GYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVVPKR-SGVTEEDIMQHCETHLAKYKRPAAITFLDDIPKNA 498
Cdd:cd05926 403 GEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREgASVTEEELRAFCRKHLAAFKVPKKVYFVDELPKTA 482
|
490
....*....|.
gi 1816047872 499 TGKMLRRALRD 509
Cdd:cd05926 483 TGKIQRRKVAE 493
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
7-509 |
4.44e-146 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 429.35 E-value: 4.44e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 7 LEETASEKPDSIACRFKDHMMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYT 86
Cdd:PRK08316 17 LRRSARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 87 PTEIGYMLTNGDVKAIVGVSQLLPLYECMHESLPKVELVILCQTGEAEPEAadpevrmKMTTFAKILRPTSAAKQNQELV 166
Cdd:PRK08316 97 GEELAYILDHSGARAFLVDPALAPTAEAALALLPVDTLILSLVLGGREAPG-------GWLDFADWAEAGSVAEPDVELA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 167 PDDTAVILYTSGTTGKPKGAMLTHQNLysnandVAGY------LGMDERDNVVCALPMFHVFCLTVCMNAPLMSGATVLI 240
Cdd:PRK08316 170 DDDLAQILYTSGTESLPKGAMLTHRAL------IAEYvscivaGDMSADDIPLHALPLYHCAQLDVFLGPYLYVGATNVI 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 241 EPQFSPASVFKLVKQQQVTIFAGVPTMYNYLFQHENGKKDDFSSIRLCISGGAAMPVALLTAFEEKF-GVTILEGYGLSE 319
Cdd:PRK08316 244 LDAPDPELILRTIEAERITSFFAPPTVWISLLRHPDFDTRDLSSLRKGYYGASIMPVEVLKELRERLpGLRFYNCYGQTE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 320 ASPV-TCFNPFDRGRKPGSIGTSILHVENKVVDPLGRELPAHQVGELIVKGPNVMKGYYKMPMETEHALKDGWLYTGDLA 398
Cdd:PRK08316 324 IAPLaTVLGPEEHLRRPGSAGRPVLNVETRVVDDDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEAFRGGWFHSGDLG 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 399 RRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVVPKR-SGVTEEDIMQHCET 477
Cdd:PRK08316 404 VMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAgATVTEDELIAHCRA 483
|
490 500 510
....*....|....*....|....*....|..
gi 1816047872 478 HLAKYKRPAAITFLDDIPKNATGKMLRRALRD 509
Cdd:PRK08316 484 RLAGFKVPKRVIFVDELPRNPSGKILKRELRE 515
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
27-503 |
3.94e-140 |
|
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: 412.76 E-value: 3.94e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 27 MTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYTPTEIGYMLTNGDVKAIVGVS 106
Cdd:cd05911 11 LTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTDP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 107 QLLPLYECMHESLPKVELVILcqTGEAEPEAADPEvrmkMTTFAKILRPTSAAKQNQELVPDDTAVILYTSGTTGKPKGA 186
Cdd:cd05911 91 DGLEKVKEAAKELGPKDKIIV--LDDKPDGVLSIE----DLLSPTLGEEDEDLPPPLKDGKDDTAAILYSSGTTGLPKGV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 187 MLTHQNLYSNANDVAGYLG-MDERDNVV-CALPMFHVFCLTVCMNAPLmSGATVLIEPQFSPASVFKLVKQQQVTIFAGV 264
Cdd:cd05911 165 CLSHRNLIANLSQVQTFLYgNDGSNDVIlGFLPLYHIYGLFTTLASLL-NGATVIIMPKFDSELFLDLIEKYKITFLYLV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 265 PTMYNYLFQHENGKKDDFSSIRLCISGGAAMPVALLTAFEEKFG-VTILEGYGLSEASPVTCFNPfDRGRKPGSIGTSIL 343
Cdd:cd05911 244 PPIAAALAKSPLLDKYDLSSLRVILSGGAPLSKELQELLAKRFPnATIKQGYGMTETGGILTVNP-DGDDKPGSVGRLLP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 344 HVENKVVDPLGRE-LPAHQVGELIVKGPNVMKGYYKMPMET-EHALKDGWLYTGDLARRDEDGYFYIVDRKKDMIIVGGY 421
Cdd:cd05911 323 NVEAKIVDDDGKDsLGPNEPGEICVRGPQVMKGYYNNPEATkETFDEDGWLHTGDIGYFDEDGYLYIVDRKKELIKYKGF 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 422 NVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVVPKRSGV-TEEDIMQHCETHLAKYKR-PAAITFLDDIPKNAT 499
Cdd:cd05911 403 QVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGEKlTEKEVKDYVAKKVASYKQlRGGVVFVDEIPKSAS 482
|
....
gi 1816047872 500 GKML 503
Cdd:cd05911 483 GKIL 486
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
3-511 |
1.48e-139 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 414.40 E-value: 1.48e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 3 LVSKLEETASEKPDSIACRFKDHMMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPIN 82
Cdd:PRK05605 34 LVDLYDNAVARFGDRPALDFFGATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVEHN 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 83 PLYTPTEIGYMLTNGDVKAIVGVSQLLPLYECMHESLPkVELVILCQTGEAEPEA----------ADPEVRMKMTTFAKI 152
Cdd:PRK05605 114 PLYTAHELEHPFEDHGARVAIVWDKVAPTVERLRRTTP-LETIVSVNMIAAMPLLqrlalrlpipALRKARAALTGPAPG 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 153 LRP----TSAA-------KQNQELVPDDTAVILYTSGTTGKPKGAMLTHQNLYSNAND----VAGYLGMDERdnVVCALP 217
Cdd:PRK05605 193 TVPwetlVDAAiggdgsdVSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFANAAQgkawVPGLGDGPER--VLAALP 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 218 MFHVFCLTVCMNAPLMSGATVLIEPQFSPASVFKLVKQQQVTIFAGVPTMYNYLFQHENGKKDDFSSIRLCISGGAAMPV 297
Cdd:PRK05605 271 MFHAYGLTLCLTLAVSIGGELVLLPAPDIDLILDAMKKHPPTWLPGVPPLYEKIAEAAEERGVDLSGVRNAFSGAMALPV 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 298 ALLTAFEEKFGVTILEGYGLSEASPVTCFNPFDRGRKPGSIGTSILHVENKVVDP--LGRELPAHQVGELIVKGPNVMKG 375
Cdd:PRK05605 351 STVELWEKLTGGLLVEGYGLTETSPIIVGNPMSDDRRPGYVGVPFPDTEVRIVDPedPDETMPDGEEGELLVRGPQVFKG 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 376 YYKMPMETEHALKDGWLYTGDLARRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAV 455
Cdd:PRK05605 431 YWNRPEETAKSFLDGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEV 510
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1816047872 456 KGYVVPKrSGVT--EEDIMQHCETHLAKYKRPAAITFLDDIPKNATGKMLRRALRDIL 511
Cdd:PRK05605 511 VAAVVLE-PGAAldPEGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRREVREEL 567
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
2-509 |
1.55e-139 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 413.20 E-value: 1.55e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 2 NLVSKLEETASEKPDSIACRFKDHMMTYQELNEHIQRFADGLQ-EAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVP 80
Cdd:PRK08314 11 SLFHNLEVSARRYPDKTAIVFYGRAISYRELLEEAERLAGYLQqECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 81 INPLYTPTEIGYMLTNGDVKAIVGVSQLLPLYECMHESLPkVELVILCQTGEAEPEAADPEVRMKMTTFAKI--LRPTSA 158
Cdd:PRK08314 91 VNPMNREEELAHYVTDSGARVAIVGSELAPKVAPAVGNLR-LRHVIVAQYSDYLPAEPEIAVPAWLRAEPPLqaLAPGGV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 159 AKQNQELV-----------PDDTAVILYTSGTTGKPKGAMLTHQNLYSNANDVAGYLGMDERDNVVCALPMFHVFCLTVC 227
Cdd:PRK08314 170 VAWKEALAaglappphtagPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVLPLFHVTGMVHS 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 228 MNAPLMSGATVLIEPQFSPASVFKLVKQQQVTIFAGVPTMYNYLFQHENGKKDDFSSIRLCISGGAAMPVALLTAFEEKF 307
Cdd:PRK08314 250 MNAPIYAGATVVLMPRWDREAAARLIERYRVTHWTNIPTMVVDFLASPGLAERDLSSLRYIGGGGAAMPEAVAERLKELT 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 308 GVTILEGYGLSEASPVTCFNPFDRgRKPGSIGTSILHVENKVVDP-LGRELPAHQVGELIVKGPNVMKGYYKMPMETEHA 386
Cdd:PRK08314 330 GLDYVEGYGLTETMAQTHSNPPDR-PKLQCLGIPTFGVDARVIDPeTLEELPPGEVGEIVVHGPQVFKGYWNRPEATAEA 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 387 L--KDG--WLYTGDLARRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVVPK 462
Cdd:PRK08314 409 FieIDGkrFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPDPRRGETVKAVVVLR 488
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1816047872 463 ---RSGVTEEDIMQHCETHLAKYKRPAAITFLDDIPKNATGKMLRRALRD 509
Cdd:PRK08314 489 peaRGKTTEEEIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKILWRQLQE 538
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
28-507 |
3.93e-136 |
|
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: 403.15 E-value: 3.93e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 28 TYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYTPTEIGYMLTNGDVKAIVGVSQ 107
Cdd:cd05904 34 TYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLAFTTAE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 108 LLplyecmhESLPKVELVILCqTGEAEPEAADPEVRMKMTTFAKILRPtsaakqnqELVPDDTAVILYTSGTTGKPKGAM 187
Cdd:cd05904 114 LA-------EKLASLALPVVL-LDSAEFDSLSFSDLLFEADEAEPPVV--------VIKQDDVAALLYSSGTTGRSKGVM 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 188 LTHQNLYSNAND-VAGYLGMDERDNVV-CALPMFHVFCLTVCMNAPLMSGATVLIEPQFSPASVFKLVKQQQVTIFAGVP 265
Cdd:cd05904 178 LTHRNLIAMVAQfVAGEGSNSDSEDVFlCVLPMFHIYGLSSFALGLLRLGATVVVMPRFDLEELLAAIERYKVTHLPVVP 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 266 TMYNYLFQHENGKKDDFSSIRLCISGGAAMPVALLTAFEEKF-GVTILEGYGLSEASPVT--CFNPFDRGRKPGSIGTSI 342
Cdd:cd05904 258 PIVLALVKSPIVDKYDLSSLRQIMSGAAPLGKELIEAFRAKFpNVDLGQGYGMTESTGVVamCFAPEKDRAKYGSVGRLV 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 343 LHVENKVVDP-LGRELPAHQVGELIVKGPNVMKGYYKMPMETEHAL-KDGWLYTGDLARRDEDGYFYIVDRKKDMIIVGG 420
Cdd:cd05904 338 PNVEAKIVDPeTGESLPPNQTGELWIRGPSIMKGYLNNPEATAATIdKEGWLHTGDLCYIDEDGYLFIVDRLKELIKYKG 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 421 YNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVVPKR-SGVTEEDIMQHCETHLAKYKRPAAITFLDDIPKNAT 499
Cdd:cd05904 418 FQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKPgSSLTEDEIMDFVAKQVAPYKKVRKVAFVDAIPKSPS 497
|
....*...
gi 1816047872 500 GKMLRRAL 507
Cdd:cd05904 498 GKILRKEL 505
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
3-509 |
2.68e-133 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 397.85 E-value: 2.68e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 3 LVSKLEETASEKPDSIACRFKDHMMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPIN 82
Cdd:PRK07059 25 LADLLEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 83 PLYTPTEIGYMLTNGDVKAIV-------GVSQLLPLYECMHeslpkvelVILCQTGE---AEPEAADPEVR--MKM---- 146
Cdd:PRK07059 105 PLYTPRELEHQLKDSGAEAIVvlenfatTVQQVLAKTAVKH--------VVVASMGDllgFKGHIVNFVVRrvKKMvpaw 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 147 -----TTFAKILRPTSAAK-QNQELVPDDTAVILYTSGTTGKPKGAMLTHQNLYSNANDVAGYL-------GMDERDNVV 213
Cdd:PRK07059 177 slpghVRFNDALAEGARQTfKPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVLQMEAWLqpafekkPRPDQLNFV 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 214 CALPMFHVFCLTVCMNAPLMSGAT-VLI-EPQFSPASVfKLVKQQQVTIFAGVPTMYNYLFQHENGKKDDFSSIRLCISG 291
Cdd:PRK07059 257 CALPLYHIFALTVCGLLGMRTGGRnILIpNPRDIPGFI-KELKKYQVHIFPAVNTLYNALLNNPDFDKLDFSKLIVANGG 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 292 GAAMPVALLTAFEEKFGVTILEGYGLSEASPVTCFNPFDRGRKPGSIGTSILHVENKVVDPLGRELPAHQVGELIVKGPN 371
Cdd:PRK07059 336 GMAVQRPVAERWLEMTGCPITEGYGLSETSPVATCNPVDATEFSGTIGLPLPSTEVSIRDDDGNDLPLGEPGEICIRGPQ 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 372 VMKGYYKMPMETEHAL-KDGWLYTGDLARRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQ 450
Cdd:PRK07059 416 VMAGYWNRPDETAKVMtADGFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEH 495
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1816047872 451 SGEAVKGYVVPKRSGVTEEDIMQHCETHLAKYKRPAAITFLDDIPKNATGKMLRRALRD 509
Cdd:PRK07059 496 SGEAVKLFVVKKDPALTEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRRELRD 554
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
7-507 |
3.00e-131 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 392.86 E-value: 3.00e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 7 LEETASEKPDSIACRFKDHMMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYT 86
Cdd:PRK06710 30 VEQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYT 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 87 PTEIGYMLTNGDVKAIVGVSQLLPLYECMhESLPKVELVILCQTGEAEPEAAD---PEVRMKMTTFAKILRPT------- 156
Cdd:PRK06710 110 ERELEYQLHDSGAKVILCLDLVFPRVTNV-QSATKIEHVIVTRIADFLPFPKNllyPFVQKKQSNLVVKVSESetihlwn 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 157 SAAKQNQELV------PDDTAVILYTSGTTGKPKGAMLTHQNLYSNAndVAG----YLGMDERDNVVCALPMFHVFCLTV 226
Cdd:PRK06710 189 SVEKEVNTGVevpcdpENDLALLQYTGGTTGFPKGVMLTHKNLVSNT--LMGvqwlYNCKEGEEVVLGVLPFFHVYGMTA 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 227 CMNAPLMSGATVLIEPQFSPASVFKLVKQQQVTIFAGVPTMYNYLFQHENGKKDDFSSIRLCISGGAAMPVALLTAFEEK 306
Cdd:PRK06710 267 VMNLSIMQGYKMVLIPKFDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLLKEYDISSIRACISGSAPLPVEVQEKFETV 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 307 FGVTILEGYGLSEASPVTCFNPFDRGRKPGSIGTSILHVENKVVD-PLGRELPAHQVGELIVKGPNVMKGYYKMPMETEH 385
Cdd:PRK06710 347 TGGKLVEGYGLTESSPVTHSNFLWEKRVPGSIGVPWPDTEAMIMSlETGEALPPGEIGEIVVKGPQIMKGYWNKPEETAA 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 386 ALKDGWLYTGDLARRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVVPKRSG 465
Cdd:PRK06710 427 VLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVLKEGT 506
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1816047872 466 V-TEEDIMQHCETHLAKYKRPAAITFLDDIPKNATGKMLRRAL 507
Cdd:PRK06710 507 EcSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVL 549
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
11-511 |
7.67e-129 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 386.39 E-value: 7.67e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 11 ASEKPDSIACRFKDHM-----MTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLY 85
Cdd:COG0365 19 AEGRGDKVALIWEGEDgeertLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPVFPGF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 86 TPTEIGYMLTNGDVKAIV---------GVSQLLPLYECMHESLPKVELVILCQ-TGEAEPEAADpevrmkmTTFAKILRP 155
Cdd:COG0365 99 GAEALADRIEDAEAKVLItadgglrggKVIDLKEKVDEALEELPSLEHVIVVGrTGADVPMEGD-------LDWDELLAA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 156 TSAAKQNQELVPDDTAVILYTSGTTGKPKGAMLTHQNLYSNANDVAGY-LGMDERDNVVCALPMFHVFCLTVCMNAPLMS 234
Cdd:COG0365 172 ASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYvLDLKPGDVFWCTADIGWATGHSYIVYGPLLN 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 235 GATVLI---EPQF-SPASVFKLVKQQQVTIFAGVPTMYNYLFQH--ENGKKDDFSSIRLCISGGAAMPVALLTAFEEKFG 308
Cdd:COG0365 252 GATVVLyegRPDFpDPGRLWELIEKYGVTVFFTAPTAIRALMKAgdEPLKKYDLSSLRLLGSAGEPLNPEVWEWWYEAVG 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 309 VTILEGYGLSEAspVTCF--NPFDRGRKPGSIGTSILHVENKVVDPLGRELPAHQVGELIVKG--PNVMKGYYKMPMETE 384
Cdd:COG0365 332 VPIVDGWGQTET--GGIFisNLPGLPVKPGSMGKPVPGYDVAVVDEDGNPVPPGEEGELVIKGpwPGMFRGYWNDPERYR 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 385 HALKD---GWLYTGDLARRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVVP 461
Cdd:COG0365 410 ETYFGrfpGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVGVPDEIRGQVVKAFVVL 489
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1816047872 462 KrSGVT-----EEDIMQHCETHLAKYKRPAAITFLDDIPKNATGKMLRRALRDIL 511
Cdd:COG0365 490 K-PGVEpsdelAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLRKIA 543
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
7-511 |
1.20e-128 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 383.83 E-value: 1.20e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 7 LEETASEKPDSIACRFKDHMMTYQELNEHIQRFADGLQ-EAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLY 85
Cdd:PRK06839 8 IEKRAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 86 TPTEIGYMLTNGDVKAIVgvsqLLPLYECMHESLPKVELVilcqtgeaepeaaDPEVRMkmTTFAKIL--RPTSAAKQNQ 163
Cdd:PRK06839 88 TENELIFQLKDSGTTVLF----VEKTFQNMALSMQKVSYV-------------QRVISI--TSLKEIEdrKIDNFVEKNE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 164 elvpDDTAVILYTSGTTGKPKGAMLTHQNLYSNA--NDVAGYLGMDERDNVVcaLPMFHVFCLTVCMNAPLMSGATVLIE 241
Cdd:PRK06839 149 ----SASFIICYTSGTTGKPKGAVLTQENMFWNAlnNTFAIDLTMHDRSIVL--LPLFHIGGIGLFAFPTLFAGGVIIVP 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 242 PQFSPASVFKLVKQQQVTIFAGVPTMYNYLFQHENGKKDDFSSIRLCISGGAAMPVALLTAFEEKfGVTILEGYGLSEAS 321
Cdd:PRK06839 223 RKFEPTKALSMIEKHKVTVVMGVPTIHQALINCSKFETTNLQSVRWFYNGGAPCPEELMREFIDR-GFLFGQGFGMTETS 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 322 P-VTCFNPFDRGRKPGSIGTSILHVENKVVDPLGRELPAHQVGELIVKGPNVMKGYYKMPMETEHALKDGWLYTGDLARR 400
Cdd:PRK06839 302 PtVFMLSEEDARRKVGSIGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEETIQDGWLCTGDLARV 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 401 DEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVVPKRSGV-TEEDIMQHCETHL 479
Cdd:PRK06839 382 DEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVlIEKDVIEHCRLFL 461
|
490 500 510
....*....|....*....|....*....|..
gi 1816047872 480 AKYKRPAAITFLDDIPKNATGKMLRRALRDIL 511
Cdd:PRK06839 462 AKYKIPKEIVFLKELPKNATGKIQKAQLVNQL 493
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
16-509 |
5.84e-128 |
|
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: 380.10 E-value: 5.84e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 16 DSIACRFKDHMMTYQELNEHIQRFADGLQEAGME-KGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYTPTEIGYML 94
Cdd:cd05941 1 DRIAIVDDGDSITYADLVARAARLANRLLALGKDlRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 95 TNGDVKAIVgvsqllplyecmheslpkvelvilcqtgeaepeaadpevrmkmttfakilrptsaakqnqelvpdDTAVIL 174
Cdd:cd05941 81 TDSEPSLVL-----------------------------------------------------------------DPALIL 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 175 YTSGTTGKPKGAMLTHQNLYSNANDVAGYLGMDERDNVVCALPMFHVFCLTVCMNAPLMSGATVLIEPQFSPASVFKLVK 254
Cdd:cd05941 96 YTSGTTGRPKGVVLTHANLAANVRALVDAWRWTEDDVLLHVLPLHHVHGLVNALLCPLFAGASVEFLPKFDPKEVAISRL 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 255 QQQVTIFAGVPTMYNYLFQ--------HENGKKDDFSSIRLCISGGAAMPVALLTAFEEKFGVTILEGYGLSEASPVTCf 326
Cdd:cd05941 176 MPSITVFMGVPTIYTRLLQyyeahftdPQFARAAAAERLRLMVSGSAALPVPTLEEWEAITGHTLLERYGMTEIGMALS- 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 327 NPFDRGRKPGSIGTSILHVENKVVDPL-GRELPAHQVGELIVKGPNVMKGYYKMPMETEHALK-DGWLYTGDLARRDEDG 404
Cdd:cd05941 255 NPLDGERRPGTVGMPLPGVQARIVDEEtGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTdDGWFKTGDLGVVDEDG 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 405 YFYIVDRKKDMII-VGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVVPKRSG--VTEEDIMQHCETHLAK 481
Cdd:cd05941 335 YYWILGRSSVDIIkSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGAaaLSLEELKEWAKQRLAP 414
|
490 500
....*....|....*....|....*...
gi 1816047872 482 YKRPAAITFLDDIPKNATGKMLRRALRD 509
Cdd:cd05941 415 YKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
27-509 |
3.17e-127 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 382.19 E-value: 3.17e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 27 MTYQELNEHIQRFADGLQ-EAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYTPTEIGYMLTNGDVKAIVGV 105
Cdd:PRK05677 50 LTYGELYKLSGAFAAWLQqHTDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVNTNPLYTAREMEHQFNDSGAKALVCL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 106 SQLLPLYEcmhESLPK--VELVILCQTGEAEPeaadPEVRMKMTTFAKILRPT-------SAAKQNQELV---------- 166
Cdd:PRK05677 130 ANMAHLAE---KVLPKtgVKHVIVTEVADMLP----PLKRLLINAVVKHVKKMvpayhlpQAVKFNDALAkgagqpvtea 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 167 ---PDDTAVILYTSGTTGKPKGAMLTHQNLYSNANDVAGYLGM---DERDNVVCALPMFHVFCLTV-CMNAPLMSGATVL 239
Cdd:PRK05677 203 npqADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCRALMGSnlnEGCEILIAPLPLYHIYAFTFhCMAMMLIGNHNIL 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 240 I-EPQFSPASVfKLVKQQQVTIFAGVPTMYNYLFQHENGKKDDFSSIRLCISGGAAMPVALLTAFEEKFGVTILEGYGLS 318
Cdd:PRK05677 283 IsNPRDLPAMV-KELGKWKFSGFVGLNTLFVALCNNEAFRKLDFSALKLTLSGGMALQLATAERWKEVTGCAICEGYGMT 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 319 EASPVTCFNPFDrGRKPGSIGTSILHVENKVVDPLGRELPAHQVGELIVKGPNVMKGYYKMPMETEHAL-KDGWLYTGDL 397
Cdd:PRK05677 362 ETSPVVSVNPSQ-AIQVGTIGIPVPSTLCKVIDDDGNELPLGEVGELCVKGPQVMKGYWQRPEATDEILdSDGWLKTGDI 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 398 ARRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVVPK-RSGVTEEDIMQHCE 476
Cdd:PRK05677 441 ALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIKVFVVVKpGETLTKEQVMEHMR 520
|
490 500 510
....*....|....*....|....*....|...
gi 1816047872 477 THLAKYKRPAAITFLDDIPKNATGKMLRRALRD 509
Cdd:PRK05677 521 ANLTGYKVPKAVEFRDELPTTNVGKILRRELRD 553
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
28-508 |
7.93e-127 |
|
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: 376.25 E-value: 7.93e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 28 TYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYTPTEIGYMLTNGDVKAIVGvsq 107
Cdd:cd05934 5 TYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 108 llplyecmheslpkvelvilcqtgeaepeaadpevrmkmttfakilrptsaakqnqelvpdDTAVILYTSGTTGKPKGAM 187
Cdd:cd05934 82 -------------------------------------------------------------DPASILYTSGTTGPPKGVV 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 188 LTHQNLYSNANDVAGYLGMDERDNVVCALPMFHVFCLTVCMNAPLMSGATVLIEPQFSPASVFKLVKQQQVTIFAGVPTM 267
Cdd:cd05934 101 ITHANLTFAGYYSARRFGLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLLPRFSASRFWSDVRRYGATVTNYLGAM 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 268 YNYLFQHENGKKDDFSSIRLCisGGAAMPVALLTAFEEKFGVTILEGYGLSEASpVTCFNPFDRGRKPGSIGTSILHVEN 347
Cdd:cd05934 181 LSYLLAQPPSPDDRAHRLRAA--YGAPNPPELHEEFEERFGVRLLEGYGMTETI-VGVIGPRDEPRRPGSIGRPAPGYEV 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 348 KVVDPLGRELPAHQVGELIVK---GPNVMKGYYKMPMETEHALKDGWLYTGDLARRDEDGYFYIVDRKKDMIIVGGYNVY 424
Cdd:cd05934 258 RIVDDDGQELPAGEPGELVIRglrGWGFFKGYYNMPEATAEAMRNGWFHTGDLGYRDADGFFYFVDRKKDMIRRRGENIS 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 425 PREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVV-PKRSGVTEEDIMQHCETHLAKYKRPAAITFLDDIPKNATGKML 503
Cdd:cd05934 338 SAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVlRPGETLDPEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVA 417
|
....*
gi 1816047872 504 RRALR 508
Cdd:cd05934 418 KAQLR 422
|
|
| pimA |
TIGR03205 |
dicarboxylate--CoA ligase PimA; PimA, a member of a large family of acyl-CoA ligases, is found ... |
7-508 |
2.67e-122 |
|
dicarboxylate--CoA ligase PimA; PimA, a member of a large family of acyl-CoA ligases, is found in a characteristic operon pimFABCDE for the metabolism of pimelate and related compounds. It is found, so far, in Bradyrhizobium japonicum and several strains of Rhodopseudomonas palustris. PimA from R. palustris was shown to be active as a CoA ligase for C(7) to C(14) dicarboxylates and fatty acids.
Pssm-ID: 132249 [Multi-domain] Cd Length: 541 Bit Score: 368.90 E-value: 2.67e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 7 LEETASEKPDSIACRFKDHMMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYT 86
Cdd:TIGR03205 27 LSKAAADYGPRPALEFRDRPITYTELEAMAETAAAALLRAGYGKDASVALYLGNTPDHPINFFGALKAGARVVHLSPLDG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 87 PTEIGYMLTNGDVKAIV--GVSQLLPLYEcmhESLPK--VELVILCQT---GE-AEPEAADPEvRMKMTTFAKILRPTSA 158
Cdd:TIGR03205 107 ERALSHKLSDSGARLLItsDLAALLPMAL---KFLEKglLDRLIVCEDdnwGKvGTPQAPIPA-DPRIVTYADFVKGAAA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 159 AKQNQELVPDDTAVILYTSGTTGKPKGAMLTHQNLYSNAN--DVAGYLGMDER---DNVVCALPMFHVFCLTVCMNAPLM 233
Cdd:TIGR03205 183 PAEWPAVTPDDVALLQYTGGTTGLPKGAMLTHGNLTSAVSiyDVWGKPSRATRgdvERVICVLPLFHIYALTVILLRSLR 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 234 SGATVLIEPQFSPASVFKLVKQQQVTIFAGVPTMYNYLFQHENGKKDDFSSIRLCISGGAAMPVALLTAFEEKFGVTILE 313
Cdd:TIGR03205 263 RGDLISLHQRFDVAAVFRDIEEKRATVFPGVPTMWIALANDPSLEKRDLSSLATIGSGGAPLPVEVANFFERKTGLKLKS 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 314 GYGLSEA-SPVTCfNPFDRGRKPGSIGTSILHVENKVV--DPLGRELPAHQVGELIVKGPNVMKGYYKMPMETEHALKDG 390
Cdd:TIGR03205 343 GWGMTETcSPGTG-HPPEGPDKPGSIGLMLPGIELDVVslDDPTKVLPPGEVGELRIRGPNVTRGYWNRPEESAEAFVGD 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 391 WLYTGDLARRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYvVPKRSGV---T 467
Cdd:TIGR03205 422 RFLTGDIGYMDTDGYFFLVDRKKDMIISGGFNVYPQMIEQAIYEHPGVQEVIVIGIPDQYRGEAAKAF-VKLRPGAkpfS 500
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1816047872 468 EEDIMQHCETHLAKYKRPAAITFLDDIPKNATGKMLRRALR 508
Cdd:TIGR03205 501 LDELRAFLAGKLGKHELPVAVEFVDELPRTPVGKLSRHELR 541
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
1-509 |
4.41e-122 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 367.28 E-value: 4.41e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 1 MNLVSKLEeTASEKPDSIACRFKD-HMMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVV 79
Cdd:PRK07514 3 NNLFDALR-AAFADRDAPFIETPDgLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 80 PINPLYTPTEIGYMLTN-------------GDVKAI---VGVSQLLPLYECMHESLPkvelvilcQTGEAEPEAADPEVR 143
Cdd:PRK07514 82 PLNTAYTLAELDYFIGDaepalvvcdpanfAWLSKIaaaAGAPHVETLDADGTGSLL--------EAAAAAPDDFETVPR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 144 MkmttfakilrptsaakqnqelvPDDTAVILYTSGTTGKPKGAMLTHQNLYSNANDVAGYLGMDERDNVVCALPMFHVFC 223
Cdd:PRK07514 154 G----------------------ADDLAAILYTSGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPDDVLIHALPIFHTHG 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 224 LTVCMNAPLMSGATVLIEPQFSPASVFKLVKQqqVTIFAGVPTMYNYLFQHENGKKDDFSSIRLCISGGAAMPVALLTAF 303
Cdd:PRK07514 212 LFVATNVALLAGASMIFLPKFDPDAVLALMPR--ATVMMGVPTFYTRLLQEPRLTREAAAHMRLFISGSAPLLAETHREF 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 304 EEKFGVTILEGYGLSEASPVTCfNPFDRGRKPGSIGTSILHVENKVVDP-LGRELPAHQVGELIVKGPNVMKGYYKMPME 382
Cdd:PRK07514 290 QERTGHAILERYGMTETNMNTS-NPYDGERRAGTVGFPLPGVSLRVTDPeTGAELPPGEIGMIEVKGPNVFKGYWRMPEK 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 383 TEHALK-DGWLYTGDLARRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVVP 461
Cdd:PRK07514 369 TAEEFRaDGFFITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVP 448
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1816047872 462 KRSG-VTEEDIMQHCETHLAKYKRPAAITFLDDIPKNATGKMLRRALRD 509
Cdd:PRK07514 449 KPGAaLDEAAILAALKGRLARFKQPKRVFFVDELPRNTMGKVQKNLLRE 497
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
27-507 |
5.60e-121 |
|
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: 361.80 E-value: 5.60e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 27 MTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYTPTEIGYMLTNGDVKAIVGVS 106
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 107 QLlplyecmheslpkvelvilcqtgeaepeaadpevrmkmttfakilrptsaakqnqelvpDDTAVILYTSGTTGKPKGA 186
Cdd:cd05935 82 EL-----------------------------------------------------------DDLALIPYTSGTTGLPKGC 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 187 MLTHQNLYSNANDVAGYLGMDERDNVVCALPMFHVFCLTVCMNAPLMSGATVLIEPQFSPASVFKLVKQQQVTIFAGVPT 266
Cdd:cd05935 103 MHTHFSAAANALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMARWDRETALELIEKYKVTFWTNIPT 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 267 MYNYLFQHENGKKDDFSSIRLCISGGAAMPVALLTAFEEKFGVTILEGYGLSEASPVTCFNPFDRgRKPGSIGTSILHVE 346
Cdd:cd05935 183 MLVDLLATPEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTETMSQTHTNPPLR-PKLQCLGIP*FGVD 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 347 NKVVDP-LGRELPAHQVGELIVKGPNVMKGYYKMPMETEHAL--KDG--WLYTGDLARRDEDGYFYIVDRKKDMIIVGGY 421
Cdd:cd05935 262 ARVIDIeTGRELPPNEVGEIVVRGPQIFKGYWNRPEETEESFieIKGrrFFRTGDLGYMDEEGYFFFVDRVKRMINVSGF 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 422 NVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVVPK---RSGVTEEDIMQHCETHLAKYKRPAAITFLDDIPKNA 498
Cdd:cd05935 342 KVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRpeyRGKVTEEDIIEWAREQMAAYKYPREVEFVDELPRSA 421
|
....*....
gi 1816047872 499 TGKMLRRAL 507
Cdd:cd05935 422 SGKILWRLL 430
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
28-508 |
8.29e-121 |
|
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: 364.00 E-value: 8.29e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 28 TYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYTPTEIGYMLTNGDVKAIVGVSQ 107
Cdd:cd05959 31 TYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVVSGE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 108 LLPLYECMHESL-PKVELVILCqtGEAEPEAADPEVRMKMTTFAKILRPtsAAKQnqelvPDDTAVILYTSGTTGKPKGA 186
Cdd:cd05959 111 LAPVLAAALTKSeHTLVVLIVS--GGAGPEAGALLLAELVAAEAEQLKP--AATH-----ADDPAFWLYSSGSTGRPKGV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 187 MLTHQNLYSNANDVA-GYLGMDERDNVVCALPMFHVFCLTVCMNAPLMSGATVLIEPQF-SPASVFKLVKQQQVTIFAGV 264
Cdd:cd05959 182 VHLHADIYWTAELYArNVLGIREDDVCFSAAKLFFAYGLGNSLTFPLSVGATTVLMPERpTPAAVFKRIRRYRPTVFFGV 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 265 PTMYNYLFQHENGKKDDFSSIRLCISGGAAMPVALLTAFEEKFGVTILEGYGLSEASPVTCFNpFDRGRKPGSIGTSILH 344
Cdd:cd05959 262 PTLYAAMLAAPNLPSRDLSSLRLCVSAGEALPAEVGERWKARFGLDILDGIGSTEMLHIFLSN-RPGRVRYGTTGKPVPG 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 345 VENKVVDPLGRELPAHQVGELIVKGPNVMKGYYKMPMETEHALKDGWLYTGDLARRDEDGYFYIVDRKKDMIIVGGYNVY 424
Cdd:cd05959 341 YEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQGEWTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVS 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 425 PREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVVPKR----SGVTEEDIMQHCETHLAKYKRPAAITFLDDIPKNATG 500
Cdd:cd05959 421 PFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPgyedSEALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATG 500
|
....*...
gi 1816047872 501 KMLRRALR 508
Cdd:cd05959 501 KIQRFKLR 508
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
7-510 |
8.64e-121 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 365.67 E-value: 8.64e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 7 LEETASEKPDSIACRFKDH--MMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPL 84
Cdd:PRK08315 22 LDRTAARYPDREALVYRDQglRWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVTINPA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 85 YTPTEIGYMLTNGDVKAIVG------------VSQLLPlyECMH--------ESLPKVELVIlcQTGEAEPEAadpevrm 144
Cdd:PRK08315 102 YRLSELEYALNQSGCKALIAadgfkdsdyvamLYELAP--ELATcepgqlqsARLPELRRVI--FLGDEKHPG------- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 145 kMTTFAKILRPTSAAKQNQ------ELVPDDTAVILYTSGTTGKPKGAMLTHQNLYSNANDVAGYLGMDERDNVVCALPM 218
Cdd:PRK08315 171 -MLNFDELLALGRAVDDAElaarqaTLDPDDPINIQYTSGTTGFPKGATLTHRNILNNGYFIGEAMKLTEEDRLCIPVPL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 219 FHVF--------CLTVcmnaplmsGAT-VLIEPQFSPASVFKLVKQQQVTIFAGVPTMYNYLFQHENGKKDDFSSIRLCI 289
Cdd:PRK08315 250 YHCFgmvlgnlaCVTH--------GATmVYPGEGFDPLATLAAVEEERCTALYGVPTMFIAELDHPDFARFDLSSLRTGI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 290 SGGAAMPVALLTAFEEKFG---VTIleGYGLSEASPVTCF----NPFDRgrKPGSIGTSILHVENKVVDP-LGRELPAHQ 361
Cdd:PRK08315 322 MAGSPCPIEVMKRVIDKMHmseVTI--AYGMTETSPVSTQtrtdDPLEK--RVTTVGRALPHLEVKIVDPeTGETVPRGE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 362 VGELIVKGPNVMKGYYKMPMETEHAL-KDGWLYTGDLARRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKE 440
Cdd:PRK08315 398 QGELCTRGYSVMKGYWNDPEKTAEAIdADGWMHTGDLAVMDEEGYVNIVGRIKDMIIRGGENIYPREIEEFLYTHPKIQD 477
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1816047872 441 AVVVGVPDPQSGEAVKGYVVPkRSGV--TEEDIMQHCETHLAKYKRPAAITFLDDIPKNATGKMLRRALRDI 510
Cdd:PRK08315 478 VQVVGVPDEKYGEEVCAWIIL-RPGAtlTEEDVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGKIQKFKMREM 548
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
28-509 |
6.67e-120 |
|
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: 358.20 E-value: 6.67e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 28 TYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYTPTEIGYMLTNGDVKAivgvsq 107
Cdd:cd05912 3 TFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVKL------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 108 llplyecmheslpkvelvilcqtgeaepeaadpevrmkmttfakilrptsaakqnqelvpDDTAVILYTSGTTGKPKGAM 187
Cdd:cd05912 77 ------------------------------------------------------------DDIATIMYTSGTTGKPKGVQ 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 188 LTHQNLYSNANDVAGYLGMDERDNVVCALPMFHVFCLTVCMNApLMSGATVLIEPQFSPASVFKLVKQQQVTIFAGVPTM 267
Cdd:cd05912 97 QTFGNHWWSAIGSALNLGLTEDDNWLCALPLFHISGLSILMRS-VIYGMTVYLVDKFDAEQVLHLINSGKVTIISVVPTM 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 268 YNYLFQHENGKKDdfSSIRLCISGGAAMPVALLTAFEEKfGVTILEGYGLSE-ASPVTCFNPFDRGRKPGSIGTSILHVE 346
Cdd:cd05912 176 LQRLLEILGEGYP--NNLRCILLGGGPAPKPLLEQCKEK-GIPVYQSYGMTEtCSQIVTLSPEDALNKIGSAGKPLFPVE 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 347 NKVVDPLGrelPAHQVGELIVKGPNVMKGYYKMPMETEHALKDGWLYTGDLARRDEDGYFYIVDRKKDMIIVGGYNVYPR 426
Cdd:cd05912 253 LKIEDDGQ---PPYEVGEILLKGPNVTKGYLNRPDATEESFENGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPA 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 427 EVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVVPKRSgVTEEDIMQHCETHLAKYKRPAAITFLDDIPKNATGKMLRRA 506
Cdd:cd05912 330 EIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSERP-ISEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHE 408
|
...
gi 1816047872 507 LRD 509
Cdd:cd05912 409 LKQ 411
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
7-508 |
9.28e-120 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 365.43 E-value: 9.28e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 7 LEETASEKPDSIACRF--------KDHMMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVV 78
Cdd:PRK07529 31 LSRAAARHPDAPALSFlldadpldRPETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGEAAGIAN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 79 vPINPLYTPTEIGYMLTNGDVKAIVGV-----SQLLPLYECMHESLPKVELVILCQTGEAEPEAADPEVRMkmttfakiL 153
Cdd:PRK07529 111 -PINPLLEPEQIAELLRAAGAKVLVTLgpfpgTDIWQKVAEVLAALPELRTVVEVDLARYLPGPKRLAVPL--------I 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 154 RP----------TSAAKQNQELV-------PDDTAVILYTSGTTGKPKGAMLTHQNLYSNANDVAGYLGMDERDNVVCAL 216
Cdd:PRK07529 182 RRkaharildfdAELARQPGDRLfsgrpigPDDVAAYFHTGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPGDTVFCGL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 217 PMFHVF-CLTVCMnAPLMSGATVLI-EPQ-FSPASVF----KLVKQQQVTIFAGVPTMYNYLFQHENGKKDdFSSIRLCI 289
Cdd:PRK07529 262 PLFHVNaLLVTGL-APLARGAHVVLaTPQgYRGPGVIanfwKIVERYRINFLSGVPTVYAALLQVPVDGHD-ISSLRYAL 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 290 SGGAAMPVALLTAFEEKFGVTILEGYGLSEASPVTCFNPFDRGRKPGSIGTSILHVENKVV--DPLG---RELPAHQVGE 364
Cdd:PRK07529 340 CGAAPLPVEVFRRFEAATGVRIVEGYGLTEATCVSSVNPPDGERRIGSVGLRLPYQRVRVVilDDAGrylRDCAVDEVGV 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 365 LIVKGPNVMKGYykmpMETEHA----LKDGWLYTGDLARRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKE 440
Cdd:PRK07529 420 LCIAGPNVFSGY----LEAAHNkglwLEDGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVAL 495
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1816047872 441 AVVVGVPDPQSGEAVKGYV--VPKrSGVTEEDIMQHCETHLAkyKR---PAAITFLDDIPKNATGKMLRRALR 508
Cdd:PRK07529 496 AAAVGRPDAHAGELPVAYVqlKPG-ASATEAELLAFARDHIA--ERaavPKHVRILDALPKTAVGKIFKPALR 565
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
15-512 |
1.17e-118 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 357.74 E-value: 1.17e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 15 PDSIACRFKDHMMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYTPTEIGYML 94
Cdd:PRK03640 16 PDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 95 TNGDVKAIVG----VSQLLPLYECMHESLPKVELVilcqtgEAEPEAADPEvrmkmttfakilrptsaakqnqelvpDDT 170
Cdd:PRK03640 96 DDAEVKCLITdddfEAKLIPGISVKFAELMNGPKE------EAEIQEEFDL--------------------------DEV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 171 AVILYTSGTTGKPKGAMLTHQNLYSNANDVAGYLGMDERDNVVCALPMFHVFCLTVCMNApLMSGATVLIEPQFSPASVF 250
Cdd:PRK03640 144 ATIMYTSGTTGKPKGVIQTYGNHWWSAVGSALNLGLTEDDCWLAAVPIFHISGLSILMRS-VIYGMRVVLVEKFDAEKIN 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 251 KLVKQQQVTIFAGVPTMYNYLFQ--HENGKKDDFSSIRLcisGGAAMPVALLTAFEEKfGVTILEGYGLSE-ASPVTCFN 327
Cdd:PRK03640 223 KLLQTGGVTIISVVSTMLQRLLErlGEGTYPSSFRCMLL---GGGPAPKPLLEQCKEK-GIPVYQSYGMTEtASQIVTLS 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 328 PFDRGRKPGSIGTSILHVENKVVDPlGRELPAHQVGELIVKGPNVMKGYYKMPMETEHALKDGWLYTGDLARRDEDGYFY 407
Cdd:PRK03640 299 PEDALTKLGSAGKPLFPCELKIEKD-GVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQDGWFKTGDIGYLDEEGFLY 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 408 IVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVVpKRSGVTEEDIMQHCETHLAKYKRPAA 487
Cdd:PRK03640 378 VLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVV-KSGEVTEEELRHFCEEKLAKYKVPKR 456
|
490 500
....*....|....*....|....*
gi 1816047872 488 ITFLDDIPKNATGKMLRRALRDILP 512
Cdd:PRK03640 457 FYFVEELPRNASGKLLRHELKQLVE 481
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
27-509 |
4.78e-117 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 356.11 E-value: 4.78e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 27 MTYQELNEHIQRFADGL-QEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYTPTEIGYMLTNGDVKAIVGV 105
Cdd:PRK08751 51 ITYREADQLVEQFAAYLlGELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVLVVI 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 106 SQLLPLYECMHESLPkVELVILCQTGE--AEPEAA------------DPEVRMKMTT-FAKILRPTSAAK-QNQELVPDD 169
Cdd:PRK08751 131 DNFGTTVQQVIADTP-VKQVITTGLGDmlGFPKAAlvnfvvkyvkklVPEYRINGAIrFREALALGRKHSmPTLQIEPDD 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 170 TAVILYTSGTTGKPKGAMLTHQNLYSNANDVAGYLG-----MDERDNVVCALPMFHVFCLT----VCMNaplMSGATVLI 240
Cdd:PRK08751 210 IAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQWLAgtgklEEGCEVVITALPLYHIFALTanglVFMK---IGGCNHLI 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 241 E-PQFSPASVfKLVKQQQVTIFAGVPTMYNYLFQHENGKKDDFSSIRLCISGGAAMPVALLTAFEEKFGVTILEGYGLSE 319
Cdd:PRK08751 287 SnPRDMPGFV-KELKKTRFTAFTGVNTLFNGLLNTPGFDQIDFSSLKMTLGGGMAVQRSVAERWKQVTGLTLVEAYGLTE 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 320 ASPVTCFNPFDRGRKPGSIGTSILHVENKVVDPLGRELPAHQVGELIVKGPNVMKGYYKMPMETEHALK-DGWLYTGDLA 398
Cdd:PRK08751 366 TSPAACINPLTLKEYNGSIGLPIPSTDACIKDDAGTVLAIGEIGELCIKGPQVMKGYWKRPEETAKVMDaDGWLHTGDIA 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 399 RRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVVPKRSGVTEEDIMQHCETH 478
Cdd:PRK08751 446 RMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEIVKVVIVKKDPALTAEDVKAHARAN 525
|
490 500 510
....*....|....*....|....*....|.
gi 1816047872 479 LAKYKRPAAITFLDDIPKNATGKMLRRALRD 509
Cdd:PRK08751 526 LTGYKQPRIIEFRKELPKTNVGKILRRELRD 556
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
27-510 |
1.67e-113 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 347.19 E-value: 1.67e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 27 MTYQELNEHIQRFADGLQE-AGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYTPTEIGYMLTNGDVKAIVGV 105
Cdd:PRK12492 50 LSYAELERHSAAFAAYLQQhTDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVNTNPLYTAREMRHQFKDSGARALVYL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 106 SQLLPLYEcmhESLP--KVELVILCQTGEAEPEAAD--------------PEVRM-KMTTFAKILRptSAAKQNQELVP- 167
Cdd:PRK12492 130 NMFGKLVQ---EVLPdtGIEYLIEAKMGDLLPAAKGwlvntvvdkvkkmvPAYHLpQAVPFKQALR--QGRGLSLKPVPv 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 168 --DDTAVILYTSGTTGKPKGAMLTHQNLYSNANDVAGYLG---------MDERDNVVCA-LPMFHVFCLTV-CMNAPLMS 234
Cdd:PRK12492 205 glDDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVRACLSqlgpdgqplMKEGQEVMIApLPLYHIYAFTAnCMCMMVSG 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 235 GATVLIEPQFSPASVFKLVKQQQVTIFAGVPTMYNYLFQHENGKKDDFSSIRLCISGGAAMPVALLTAFEEKFGVTILEG 314
Cdd:PRK12492 285 NHNVLITNPRDIPGFIKELGKWRFSALLGLNTLFVALMDHPGFKDLDFSALKLTNSGGTALVKATAERWEQLTGCTIVEG 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 315 YGLSEASPVTCFNPFDRGRKPGSIGTSILHVENKVVDPLGRELPAHQVGELIVKGPNVMKGYYKMPMETEHAL-KDGWLY 393
Cdd:PRK12492 365 YGLTETSPVASTNPYGELARLGTVGIPVPGTALKVIDDDGNELPLGERGELCIKGPQVMKGYWQQPEATAEALdAEGWFK 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 394 TGDLARRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVVPKRSGVTEEDIMQ 473
Cdd:PRK12492 445 TGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVKLFVVARDPGLSVEELKA 524
|
490 500 510
....*....|....*....|....*....|....*..
gi 1816047872 474 HCETHLAKYKRPAAITFLDDIPKNATGKMLRRALRDI 510
Cdd:PRK12492 525 YCKENFTGYKVPKHIVLRDSLPMTPVGKILRRELRDI 561
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
25-509 |
1.16e-112 |
|
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: 343.46 E-value: 1.16e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 25 HMMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYTPTEIGYMLTNGDVKAIVG 104
Cdd:cd12119 24 HRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAEDRVVFV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 105 VSQLLPLYECMHESLPKVELVILCQTGEAEPEAADPEVrmkmTTFAKILRPTSAAKQNQELVPDDTAVILYTSGTTGKPK 184
Cdd:cd12119 104 DRDFLPLLEAIAPRLPTVEHVVVMTDDAAMPEPAGVGV----LAYEELLAAESPEYDWPDFDENTAAAICYTSGTTGNPK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 185 GAMLTHQNLY-----SNANDVagyLGMDERDNVVCALPMFHVfcltvcmNA---P---LMSGAT-VLIEPQFSPASVFKL 252
Cdd:cd12119 180 GVVYSHRSLVlhamaALLTDG---LGLSESDVVLPVVPMFHV-------NAwglPyaaAMVGAKlVLPGPYLDPASLAEL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 253 VKQQQVTIFAGVPTMYNYLFQHENGKKDDFSSIRLCISGGAAMPVALLTAFEEKfGVTILEGYGLSEASPVTCFN---PF 329
Cdd:cd12119 250 IEREGVTFAAGVPTVWQGLLDHLEANGRDLSSLRRVVIGGSAVPRSLIEAFEER-GVRVIHAWGMTETSPLGTVArppSE 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 330 DRGRKPG-------SIGTSILHVENKVVDPLGRELPA--HQVGELIVKGPNVMKGYYKMPMETEHALKDGWLYTGDLARR 400
Cdd:cd12119 329 HSNLSEDeqlalraKQGRPVPGVELRIVDDDGRELPWdgKAVGELQVRGPWVTKSYYKNDEESEALTEDGWLRTGDVATI 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 401 DEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVVPKR-SGVTEEDIMQHCETHL 479
Cdd:cd12119 409 DEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLKEgATVTAEELLEFLADKV 488
|
490 500 510
....*....|....*....|....*....|
gi 1816047872 480 AKYKRPAAITFLDDIPKNATGKMLRRALRD 509
Cdd:cd12119 489 AKWWLPDDVVFVDEIPKTSTGKIDKKALRE 518
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
7-510 |
4.12e-111 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 340.60 E-value: 4.12e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 7 LEETASEKPDSIACRFKDH----------MMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGI 76
Cdd:PRK12583 16 LTQTIGDAFDATVARFPDRealvvrhqalRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 77 VVVPINPLYTPTEIGYMLTNGDVKAIVG------------VSQLLP------LYECMHESLPKVELVILCQTGEAEPEAA 138
Cdd:PRK12583 96 ILVNINPAYRASELEYALGQSGVRWVICadafktsdyhamLQELLPglaegqPGALACERLPELRGVVSLAPAPPPGFLA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 139 DPEVRMKmttfAKILRPTSAAKQNQELVPDDTAVILYTSGTTGKPKGAMLTHQNLYSNANDVAGYLGMDERDNVVCALPM 218
Cdd:PRK12583 176 WHELQAR----GETVSREALAERQASLDRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCVPVPL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 219 FHVFCLTVCMNAPLMSGATVLIePQ--FSPASVFKLVKQQQVTIFAGVPTMYNYLFQHENGKKDDFSSIRLCISGGAAMP 296
Cdd:PRK12583 252 YHCFGMVLANLGCMTVGACLVY-PNeaFDPLATLQAVEEERCTALYGVPTMFIAELDHPQRGNFDLSSLRTGIMAGAPCP 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 297 VALLTAFEEKFGVT-ILEGYGLSEASPVTCF----NPFDRgrKPGSIGTSILHVENKVVDPLGRELPAHQVGELIVKGPN 371
Cdd:PRK12583 331 IEVMRRVMDEMHMAeVQIAYGMTETSPVSLQttaaDDLER--RVETVGRTQPHLEVKVVDPDGATVPRGEIGELCTRGYS 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 372 VMKGYYKMPMETEHAL-KDGWLYTGDLARRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQ 450
Cdd:PRK12583 409 VMKGYWNNPEATAESIdEDGWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEK 488
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1816047872 451 SGEAVKGYVVpKRSG--VTEEDIMQHCETHLAKYKRPAAITFLDDIPKNATGKMLRRALRDI 510
Cdd:PRK12583 489 YGEEIVAWVR-LHPGhaASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMREI 549
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
1-458 |
2.28e-108 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 335.15 E-value: 2.28e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 1 MNLVSKLEETASEKPDSIACRFKD----HMMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGI 76
Cdd:COG1022 11 DTLPDLLRRRAARFPDRVALREKEdgiwQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 77 VVVPINPLYTPTEIGYMLTNGDVKAIVgVS---QLLPLYECMHEsLPKVELVILCqtgEAEPEAADPEVrmkmTTFAKIL 153
Cdd:COG1022 91 VTVPIYPTSSAEEVAYILNDSGAKVLF-VEdqeQLDKLLEVRDE-LPSLRHIVVL---DPRGLRDDPRL----LSLDELL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 154 RpTSAAKQNQELV--------PDDTAVILYTSGTTGKPKGAMLTHQNLYSNANDVAGYLGMDERDNVVCALPMFHVF--C 223
Cdd:COG1022 162 A-LGREVADPAELearraavkPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFLPLAHVFerT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 224 LTVCMnapLMSGATVLIEPqfSPASVFKLVKQQQVTIFAGVP----TMYN--------------YLFQH----------- 274
Cdd:COG1022 241 VSYYA---LAAGATVAFAE--SPDTLAEDLREVKPTFMLAVPrvweKVYAgiqakaeeagglkrKLFRWalavgrryara 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 275 -ENGKKDDF----------------------SSIRLCISGGAAMPVALLTAFEEkFGVTILEGYGLSEASPVTCFNPFDR 331
Cdd:COG1022 316 rLAGKSPSLllrlkhaladklvfsklrealgGRLRFAVSGGAALGPELARFFRA-LGIPVLEGYGLTETSPVITVNRPGD 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 332 gRKPGSIGTSILHVENKVVDPlgrelpahqvGELIVKGPNVMKGYYKMPMETEHAL-KDGWLYTGDLARRDEDGYFYIVD 410
Cdd:COG1022 395 -NRIGTVGPPLPGVEVKIAED----------GEILVRGPNVMKGYYKNPEATAEAFdADGWLHTGDIGELDEDGFLRITG 463
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1816047872 411 RKKDMIIV-GGYNVYPREVEEVLYSHPDVKEAVVVG----------VPDPqsgEAVKGY 458
Cdd:COG1022 464 RKKDLIVTsGGKNVAPQPIENALKASPLIEQAVVVGdgrpflaaliVPDF---EALGEW 519
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
15-508 |
2.43e-108 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 332.34 E-value: 2.43e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 15 PDSIACRFKDHMMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYTPTEIGYML 94
Cdd:PRK06188 26 PDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHPLGSLDDHAYVL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 95 TNGDVKA-IVGVSQLLPLYECMHESLPKVELVIlcqTGEAEPEAADpevrmkmttFAKILRPTSAAKQNQELVPDDTAVI 173
Cdd:PRK06188 106 EDAGISTlIVDPAPFVERALALLARVPSLKHVL---TLGPVPDGVD---------LLAAAAKFGPAPLVAAALPPDIAGL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 174 LYTSGTTGKPKGAMLTHQNLYSNANDVAGYLGMDERDNVVCALPMFHVFCLTVcmnAP-LMSGATVLIEPQFSPASVFKL 252
Cdd:PRK06188 174 AYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLSHAGGAFF---LPtLLRGGTVIVLAKFDPAEVLRA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 253 VKQQQVTIFAGVPTMYNYLFQHENGKKDDFSSIRLCISGGAAM-PVALLTAFEeKFGVTILEGYGLSEA-SPVTCFNPFD 330
Cdd:PRK06188 251 IEEQRITATFLVPTMIYALLDHPDLRTRDLSSLETVYYGASPMsPVRLAEAIE-RFGPIFAQYYGQTEApMVITYLRKRD 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 331 RGRKP----GSIGTSILHVENKVVDPLGRELPAHQVGELIVKGPNVMKGYYKMPMETEHALKDGWLYTGDLARRDEDGYF 406
Cdd:PRK06188 330 HDPDDpkrlTSCGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAFRDGWLHTGDVAREDEDGFY 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 407 YIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVVPkRSG--VTEEDIMQHCETHLAKYKR 484
Cdd:PRK06188 410 YIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVL-RPGaaVDAAELQAHVKERKGSVHA 488
|
490 500
....*....|....*....|....
gi 1816047872 485 PAAITFLDDIPKNATGKMLRRALR 508
Cdd:PRK06188 489 PKQVDFVDSLPLTALGKPDKKALR 512
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
167-508 |
1.22e-107 |
|
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: 324.62 E-value: 1.22e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 167 PDDTAVILYTSGTTGKPKGAMLTHQNLYSNANDVAGYLGMDERDNVVCALPMFHVFCLTVCMNAPLMSGAT-VLIEPQFS 245
Cdd:cd05917 1 PDDVINIQFTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLCIPVPLFHCFGSVLGVLACLTHGATmVFPSPSFD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 246 PASVFKLVKQQQVTIFAGVPTMYNYLFQHENGKKDDFSSIRLCISGGAAMPVALLTAFEEKFGVT-ILEGYGLSEASPVt 324
Cdd:cd05917 81 PLAVLEAIEKEKCTALHGVPTMFIAELEHPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEVMNMKdVTIAYGMTETSPV- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 325 CFN-----PFDRgrKPGSIGTSILHVENKVVDPLGRELPA-HQVGELIVKGPNVMKGYYKMPMETEHAL-KDGWLYTGDL 397
Cdd:cd05917 160 STQtrtddSIEK--RVNTVGRIMPHTEAKIVDPEGGIVPPvGVPGELCIRGYSVMKGYWNDPEKTAEAIdGDGWLHTGDL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 398 ARRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVVPKRSG-VTEEDIMQHCE 476
Cdd:cd05917 238 AVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLKEGAeLTEEDIKAYCK 317
|
330 340 350
....*....|....*....|....*....|..
gi 1816047872 477 THLAKYKRPAAITFLDDIPKNATGKMLRRALR 508
Cdd:cd05917 318 GKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
7-507 |
1.09e-106 |
|
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: 327.89 E-value: 1.09e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 7 LEETASEKPDSIACRFKDHMMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYT 86
Cdd:TIGR03098 6 LEDAAARLPDATALVHHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 87 PTEIGYMLTNGDVKAIVGVSQLLPLyecMHESLPKV-ELVILCQTGEAEPEAADPEVRMkMTTFAKiLRPTSAAKQNQEL 165
Cdd:TIGR03098 86 AEQVAHILADCNVRLLVTSSERLDL---LHPALPGChDLRTLIIVGDPAHASEGHPGEE-PASWPK-LLALGDADPPHPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 166 VPDDTAVILYTSGTTGKPKGAMLTHQNLYSNANDVAGYLGMDERDNVVCALPMFHVFCLTVCMNApLMSGATVLIEPQFS 245
Cdd:TIGR03098 161 IDSDMAAILYTSGSTGRPKGVVLSHRNLVAGAQSVATYLENRPDDRLLAVLPLSFDYGFNQLTTA-FYVGATVVLHDYLL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 246 PASVFKLVKQQQVTIFAGVPTMYNYLFQhENGKKDDFSSIRLCISGGAAMPVALLTAFEEKFGVT-ILEGYGLSEASPVT 324
Cdd:TIGR03098 240 PRDVLKALEKHGITGLAAVPPLWAQLAQ-LDWPESAAPSLRYLTNSGGAMPRATLSRLRSFLPNArLFLMYGLTEAFRST 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 325 CFNPFDRGRKPGSIGTSILHVENKVVDPLGRELPAHQVGELIVKGPNVMKGYYKMPMET------------EHALKDGWL 392
Cdd:TIGR03098 319 YLPPEEVDRRPDSIGKAIPNAEVLVLREDGSECAPGEEGELVHRGALVAMGYWNDPEKTaerfrplppfpgELHLPELAV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 393 YTGDLARRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVVPkRSGVTE--ED 470
Cdd:TIGR03098 399 WSGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAFGVPDPTLGQAIVLVVTP-PGGEELdrAA 477
|
490 500 510
....*....|....*....|....*....|....*..
gi 1816047872 471 IMQHCETHLAKYKRPAAITFLDDIPKNATGKMLRRAL 507
Cdd:TIGR03098 478 LLAECRARLPNYMVPALIHVRQALPRNANGKIDRKAL 514
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
28-508 |
1.93e-106 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 327.41 E-value: 1.93e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 28 TYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYTPTEIGYMLTNGDVKAIVGVSQ 107
Cdd:PRK08008 39 SYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASLLVTSAQ 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 108 LLPLYECMHESLPKvELVILCQTGEAEPEAADpevrmkMTTFAKILrptsaAKQNQEL---VP---DDTAVILYTSGTTG 181
Cdd:PRK08008 119 FYPMYRQIQQEDAT-PLRHICLTRVALPADDG------VSSFTQLK-----AQQPATLcyaPPlstDDTAEILFTSGTTS 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 182 KPKGAMLTHQNLYsnandVAGYLG-----MDERDNVVCALPMFHVFC-LTVCMnAPLMSGAT-VLIEpQFSPASVFKLVK 254
Cdd:PRK08008 187 RPKGVVITHYNLR-----FAGYYSawqcaLRDDDVYLTVMPAFHIDCqCTAAM-AAFSAGATfVLLE-KYSARAFWGQVC 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 255 QQQVTIFAGVPTMYNYLFQHENGKKDDFSSIR-----LCISggaampVALLTAFEEKFGVTILEGYGLSEaSPVTCFN-- 327
Cdd:PRK08008 260 KYRATITECIPMMIRTLMVQPPSANDRQHCLRevmfyLNLS------DQEKDAFEERFGVRLLTSYGMTE-TIVGIIGdr 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 328 PFDRGRKPgSIGTSILHVENKVVDPLGRELPAHQVGELIVKG---PNVMKGYYKMPMETEHALK-DGWLYTGDLARRDED 403
Cdd:PRK08008 333 PGDKRRWP-SIGRPGFCYEAEIRDDHNRPLPAGEIGEICIKGvpgKTIFKEYYLDPKATAKVLEaDGWLHTGDTGYVDEE 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 404 GYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVVPKR-SGVTEEDIMQHCETHLAKY 482
Cdd:PRK08008 412 GFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEgETLSEEEFFAFCEQNMAKF 491
|
490 500
....*....|....*....|....*.
gi 1816047872 483 KRPAAITFLDDIPKNATGKMLRRALR 508
Cdd:PRK08008 492 KVPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
1-508 |
2.40e-106 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 327.89 E-value: 2.40e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 1 MNLVSKLEETASEKPDSIACRFKDHMMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVP 80
Cdd:PRK07786 17 QNWVNQLARHALMQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 81 INPLYTPTEIGYMLTNGDVKAIVGVSQLLPLYECMHESLPKVELVILCqTGEAEPEAADPEvrmkmttfaKILRPTSAAK 160
Cdd:PRK07786 97 VNFRLTPPEIAFLVSDCGAHVVVTEAALAPVATAVRDIVPLLSTVVVA-GGSSDDSVLGYE---------DLLAEAGPAH 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 161 QNQElVPDDT-AVILYTSGTTGKPKGAMLTHQNLYSNANDVAGYLGMDERDNV-VCALPMFHVFCLTvCMNAPLMSGATV 238
Cdd:PRK07786 167 APVD-IPNDSpALIMYTSGTTGRPKGAVLTHANLTGQAMTCLRTNGADINSDVgFVGVPLFHIAGIG-SMLPGLLLGAPT 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 239 LIEP--QFSPASVFKLVKQQQVTIFAGVPTMYNYLFQHENGKKDDFSsIRLCISGGAAMPVALLTAFEEKF-GVTILEGY 315
Cdd:PRK07786 245 VIYPlgAFDPGQLLDVLEAEKVTGIFLVPAQWQAVCAEQQARPRDLA-LRVLSWGAAPASDTLLRQMAATFpEAQILAAF 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 316 GLSEASPVTC-FNPFDRGRKPGSIGTSILHVENKVVDPLGRELPAHQVGELIVKGPNVMKGYYKMPMETEHALKDGWLYT 394
Cdd:PRK07786 324 GQTEMSPVTCmLLGEDAIRKLGSVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFAGGWFHS 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 395 GDLARRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVVPKRSG--VTEEDIM 472
Cdd:PRK07786 404 GDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRNDDaaLTLEDLA 483
|
490 500 510
....*....|....*....|....*....|....*.
gi 1816047872 473 QHCETHLAKYKRPAAITFLDDIPKNATGKMLRRALR 508
Cdd:PRK07786 484 EFLTDRLARYKHPKALEIVDALPRNPAGKVLKTELR 519
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
25-511 |
4.44e-104 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 321.93 E-value: 4.44e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 25 HMMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYTPTEIGYMLTNGDVKAIVG 104
Cdd:PLN02246 49 RVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAKLIIT 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 105 VSQLlplYECMHESLPKVELVILCQTGEAEpeaadpevrmKMTTFAKILRPTSAAKQNQELVPDDTAVILYTSGTTGKPK 184
Cdd:PLN02246 129 QSCY---VDKLKGLAEDDGVTVVTIDDPPE----------GCLHFSELTQADENELPEVEISPDDVVALPYSSGTTGLPK 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 185 GAMLTHQNLYSN-ANDVAG---YLGMDERDNVVCALPMFHVFCLTVCMNAPLMSGATVLIEPQFSPASVFKLVKQQQVTI 260
Cdd:PLN02246 196 GVMLTHKGLVTSvAQQVDGenpNLYFHSDDVILCVLPMFHIYSLNSVLLCGLRVGAAILIMPKFEIGALLELIQRHKVTI 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 261 FAGVPTMYNYLFQHENGKKDDFSSIRLCISGGAAMPVALLTAFEEKFGVTIL-EGYGLSEASPV--TCF----NPFDRgr 333
Cdd:PLN02246 276 APFVPPIVLAIAKSPVVEKYDLSSIRMVLSGAAPLGKELEDAFRAKLPNAVLgQGYGMTEAGPVlaMCLafakEPFPV-- 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 334 KPGSIGTSILHVENKVVDP-LGRELPAHQVGELIVKGPNVMKGYYKMPMETEHAL-KDGWLYTGDLARRDEDGYFYIVDR 411
Cdd:PLN02246 354 KSGSCGTVVRNAELKIVDPeTGASLPRNQPGEICIRGPQIMKGYLNDPEATANTIdKDGWLHTGDIGYIDDDDELFIVDR 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 412 KKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVV-PKRSGVTEEDIMQHCETHLAKYKRPAAITF 490
Cdd:PLN02246 434 LKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVVrSNGSEITEDEIKQFVAKQVVFYKRIHKVFF 513
|
490 500
....*....|....*....|.
gi 1816047872 491 LDDIPKNATGKMLRRALRDIL 511
Cdd:PLN02246 514 VDSIPKAPSGKILRKDLRAKL 534
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
24-508 |
1.90e-102 |
|
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: 314.40 E-value: 1.90e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 24 DHMMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYTPTEIGYMLTNGDVKAIV 103
Cdd:cd05919 8 DRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 104 gvsqllplyecmheslpkvelvilcqtgeaepeaadpevrmkmttfakilrpTSAakqnqelvpDDTAVILYTSGTTGKP 183
Cdd:cd05919 88 ----------------------------------------------------TSA---------DDIAYLLYSSGTTGPP 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 184 KGAMLTHQNLYSNANDVA-GYLGMDERDNVVCALPMFHVFCLTVCMNAPLMSGATVLIEPQF-SPASVFKLVKQQQVTIF 261
Cdd:cd05919 107 KGVMHAHRDPLLFADAMArEALGLTPGDRVFSSAKMFFGYGLGNSLWFPLAVGASAVLNPGWpTAERVLATLARFRPTVL 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 262 AGVPTMYNYLFQHENGKKDDFSSIRLCISGGAAMPVALLTAFEEKFGVTILEGYGLSEASPVTCFNPFDRGRkPGSIGTS 341
Cdd:cd05919 187 YGVPTFYANLLDSCAGSPDALRSLRLCVSAGEALPRGLGERWMEHFGGPILDGIGATEVGHIFLSNRPGAWR-LGSTGRP 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 342 ILHVENKVVDPLGRELPAHQVGELIVKGPNVMKGYYKMPMETEHALKDGWLYTGDLARRDEDGYFYIVDRKKDMIIVGGY 421
Cdd:cd05919 266 VPGYEIRLVDEEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQ 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 422 NVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVVPKR----SGVTEEDIMQHCETHLAKYKRPAAITFLDDIPKN 497
Cdd:cd05919 346 WVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSpaapQESLARDIHRHLLERLSAHKVPRRIAFVDELPRT 425
|
490
....*....|.
gi 1816047872 498 ATGKMLRRALR 508
Cdd:cd05919 426 ATGKLQRFKLR 436
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
11-511 |
4.86e-101 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 312.51 E-value: 4.86e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 11 ASEKPDSIACR--FKDHMMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYTPT 88
Cdd:PRK09088 5 ARLQPQRLAAVdlALGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSAS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 89 EIGYMLTNGDVKAIVGVSQLlplyecmheslpkvelvilcQTGEAEPEAADpevrmKMTTFAKILRPTSAAKqnqeLVPD 168
Cdd:PRK09088 85 ELDALLQDAEPRLLLGDDAV--------------------AAGRTDVEDLA-----AFIASADALEPADTPS----IPPE 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 169 DTAVILYTSGTTGKPKGAMLTHQNLYSNANDVaGYLG-MDERDNVVCALPMFHVFCLTVCMNAPLMSGATVLIEPQFSPA 247
Cdd:PRK09088 136 RVSLILFTSGTSGQPKGVMLSERNLQQTAHNF-GVLGrVDAHSSFLCDAPMFHIIGLITSVRPVLAVGGSILVSNGFEPK 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 248 SVFKLVKQQQ--VTIFAGVPTMYNYLFQHENGKKDDFSSIRLCISGGAAMPVALLTAFEEKfGVTILEGYGLSEASpvTC 325
Cdd:PRK09088 215 RTLGRLGDPAlgITHYFCVPQMAQAFRAQPGFDAAALRHLTALFTGGAPHAAEDILGWLDD-GIPMVDGFGMSEAG--TV 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 326 FN-PFDRGR---KPGSIGTSILHVENKVVDPLGRELPAHQVGELIVKGPNVMKGYYKMPMETEHAL-KDGWLYTGDLARR 400
Cdd:PRK09088 292 FGmSVDCDViraKAGAAGIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFtGDGWFRTGDIARR 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 401 DEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVVPKRSGVTE-EDIMQHCETHL 479
Cdd:PRK09088 372 DADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADGAPLDlERIRSHLSTRL 451
|
490 500 510
....*....|....*....|....*....|..
gi 1816047872 480 AKYKRPAAITFLDDIPKNATGKMLRRALRDIL 511
Cdd:PRK09088 452 AKYKVPKHLRLVDALPRTASGKLQKARLRDAL 483
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
5-509 |
5.00e-99 |
|
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: 307.30 E-value: 5.00e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 5 SKLEETASEKPDSIACRFKDHMMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPL 84
Cdd:cd12118 8 SFLERAAAVYPDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 85 YTPTEIGYMLTNGDVKAIVGVSQLLplYECmheslpkvelviLCQTGEAEPEAadpevrmkmttfakiLRPTSAakqnqe 164
Cdd:cd12118 88 LDAEEIAFILRHSEAKVLFVDREFE--YED------------LLAEGDPDFEW---------------IPPADE------ 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 165 lvpDDTAVILYTSGTTGKPKGAMLTHQNLYSNANDVAGYLGMDERDNVVCALPMFHV--FCLTVCMNAplmSGATVLIEP 242
Cdd:cd12118 133 ---WDPIALNYTSGTTGRPKGVVYHHRGAYLNALANILEWEMKQHPVYLWTLPMFHCngWCFPWTVAA---VGGTNVCLR 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 243 QFSPASVFKLVKQQQVTIFAGVPTMYNYLFQHENGKKDDFSSIRLCISGGAAMPVALLTAFEEKfGVTILEGYGLSEASP 322
Cdd:cd12118 207 KVDAKAIYDLIEKHKVTHFCGAPTVLNMLANAPPSDARPLPHRVHVMTAGAPPPAAVLAKMEEL-GFDVTHVYGLTETYG 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 323 VTCFNPF----------DRGRKPGSIGTSILHVEN-KVVDP-LGRELPA--HQVGELIVKGPNVMKGYYKMPMETEHALK 388
Cdd:cd12118 286 PATVCAWkpewdelpteERARLKARQGVRYVGLEEvDVLDPeTMKPVPRdgKTIGEIVFRGNIVMKGYLKNPEATAEAFR 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 389 DGWLYTGDLARRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVVPKR-SGVT 467
Cdd:cd12118 366 GGWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVELKEgAKVT 445
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1816047872 468 EEDIMQHCETHLAKYKRPAAITFlDDIPKNATGKMLRRALRD 509
Cdd:cd12118 446 EEEIIAFCREHLAGFMVPKTVVF-GELPKTSTGKIQKFVLRD 486
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
7-513 |
7.11e-99 |
|
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: 308.23 E-value: 7.11e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 7 LEETASEKPDSIACRFKDHMMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGivVVPINPLYT 86
Cdd:COG1021 31 LRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAG--AIPVFALPA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 87 --PTEIGYMLTNGDVKAIVGVSQ-----LLPLYECMHESLPKVELVILCqtGEAEPEAADPEvrmkmttfakiLRPTSAA 159
Cdd:COG1021 109 hrRAEISHFAEQSEAVAYIIPDRhrgfdYRALARELQAEVPSLRHVLVV--GDAGEFTSLDA-----------LLAAPAD 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 160 KQNQELVPDDTAVILYTSGTTGKPKGAMLTHQNLYSNANDVAGYLGMDERDNVVCALPMFHVFCLTV-CMNAPLMSGATV 238
Cdd:COG1021 176 LSEPRPDPDDVAFFQLSGGTTGLPKLIPRTHDDYLYSVRASAEICGLDADTVYLAALPAAHNFPLSSpGVLGVLYAGGTV 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 239 LIEPQFSPASVFKLVKQQQVTIFAGVPTMYNYLFQHENGKKDDFSSIRLCISGGAAMPVALLTAFEEKFGVTILEGYGLS 318
Cdd:COG1021 256 VLAPDPSPDTAFPLIERERVTVTALVPPLALLWLDAAERSRYDLSSLRVLQVGGAKLSPELARRVRPALGCTLQQVFGMA 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 319 EAsPVtCFNPFD---------RGRkPGSIGTSIlhvenKVVDPLGRELPAHQVGELIVKGPNVMKGYYKMPMETEHAL-K 388
Cdd:COG1021 336 EG-LV-NYTRLDdpeevilttQGR-PISPDDEV-----RIVDEDGNPVPPGEVGELLTRGPYTIRGYYRAPEHNARAFtP 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 389 DGWLYTGDLARRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVVPKRSGVTE 468
Cdd:COG1021 408 DGFYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGERSCAFVVPRGEPLTL 487
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1816047872 469 EDIMQHC-ETHLAKYKRPAAITFLDDIPKNATGKMLRRALRDILPQ 513
Cdd:COG1021 488 AELRRFLrERGLAAFKLPDRLEFVDALPLTAVGKIDKKALRAALAA 533
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
40-508 |
7.15e-98 |
|
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: 303.21 E-value: 7.15e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 40 ADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAG----IVVVPINPLYTPTEIGYMLTNGDVKaivgvsqllplyecm 115
Cdd:cd05922 7 ASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGgrlgLVFVPLNPTLKESVLRYLVADAGGR--------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 116 heslpkvelVILCQTG------EAEPEAADPEVRMKMTTFAKILRPTSAakqnQELVPDDTAVILYTSGTTGKPKGAMLT 189
Cdd:cd05922 72 ---------IVLADAGaadrlrDALPASPDPGTVLDADGIRAARASAPA----HEVSHEDLALLLYTSGSTGSPKLVRLS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 190 HQNLYSNANDVAGYLGMDERDNVVCALPMFHVFCLTVcMNAPLMSGATVLIEPQFS-PASVFKLVKQQQVTIFAGVPTMY 268
Cdd:cd05922 139 HQNLLANARSIAEYLGITADDRALTVLPLSYDYGLSV-LNTHLLRGATLVLTNDGVlDDAFWEDLREHGATGLAGVPSTY 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 269 NYLfqhENGKKDDFS--SIRLCISGGAAMPVALLTAFEEKF-GVTILEGYGLSEASPVTCFNPFDR-GRKPGSIGTSILH 344
Cdd:cd05922 218 AML---TRLGFDPAKlpSLRYLTQAGGRLPQETIARLRELLpGAQVYVMYGQTEATRRMTYLPPERiLEKPGSIGLAIPG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 345 VENKVVDPLGRELPAHQVGELIVKGPNVMKGYYKMP-METEHALKDGWLYTGDLARRDEDGYFYIVDRKKDMIIVGGYNV 423
Cdd:cd05922 295 GEFEILDDDGTPTPPGEPGEIVHRGPNVMKGYWNDPpYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRI 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 424 YPREVEEVLYSHPDVKEAVVVGVPDPqSGEAVKGYVVPKrSGVTEEDIMQHCETHLAKYKRPAAITFLDDIPKNATGKML 503
Cdd:cd05922 375 SPTEIEAAARSIGLIIEAAAVGLPDP-LGEKLALFVTAP-DKIDPKDVLRSLAERLPPYKVPATVRVVDELPLTASGKVD 452
|
....*
gi 1816047872 504 RRALR 508
Cdd:cd05922 453 YAALR 457
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
25-505 |
7.88e-98 |
|
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: 302.98 E-value: 7.88e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 25 HMMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYTPTEIGYMLTNGDVKAIVg 104
Cdd:cd05907 4 QPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALF- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 105 vsqllplyecmheslpkVElvilcqtgeaepeaadpevrmkmttfakilrptsaakqnqelVPDDTAVILYTSGTTGKPK 184
Cdd:cd05907 83 -----------------VE------------------------------------------DPDDLATIIYTSGTTGRPK 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 185 GAMLTHQNLYSNANDVAGYLGMDERDNVVCALPMFHVFCLTVCMNAPLMSGATVLIEPqfSPASVFKLVKQQQVTIFAGV 264
Cdd:cd05907 104 GVMLSHRNILSNALALAERLPATEGDRHLSFLPLAHVFERRAGLYVPLLAGARIYFAS--SAETLLDDLSEVRPTVFLAV 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 265 PTMYNYLFQHENGKKDD-----------FSSIRLCISGGAAMPVALLTaFEEKFGVTILEGYGLSEASPVTCFNPFDRGR 333
Cdd:cd05907 182 PRVWEKVYAAIKVKAVPglkrklfdlavGGRLRFAASGGAPLPAELLH-FFRALGIPVYEGYGLTETSAVVTLNPPGDNR 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 334 kPGSIGTSILHVENKVVDplgrelpahqVGELIVKGPNVMKGYYKMPMET-EHALKDGWLYTGDLARRDEDGYFYIVDRK 412
Cdd:cd05907 261 -IGTVGKPLPGVEVRIAD----------DGEILVRGPNVMLGYYKNPEATaEALDADGWLHTGDLGEIDEDGFLHITGRK 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 413 KDMIIV-GGYNVYPREVEEVLYSHPDVKEAVVVG----------VPDPqsgEAVKGYVVPK-------RSGVTEEDIMQH 474
Cdd:cd05907 330 KDLIITsGGKNISPEPIENALKASPLISQAVVIGdgrpflvaliVPDP---EALEAWAEEHgiaytdvAELAANPAVRAE 406
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1816047872 475 CETH-------LAKYKRPAAITFLDDIPKNATGKM-----LRR 505
Cdd:cd05907 407 IEAAveaanarLSRYEQIKKFLLLPEPFTIENGELtptlkLKR 449
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
27-508 |
1.51e-97 |
|
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: 301.70 E-value: 1.51e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 27 MTYQELNEHIQRFADGL-QEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYTPTEIGYMLTNGdvkaivgv 105
Cdd:cd05958 11 WTYRDLLALANRIANVLvGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDKA-------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 106 sqllplyecmheslpkvelvilcqtgeaepeaadpevrmkmttfakilRPTSAAKQNQELVPDDTAVILYTSGTTGKPKG 185
Cdd:cd05958 83 ------------------------------------------------RITVALCAHALTASDDICILAFTSGTTGAPKA 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 186 AMLTHQNLYSNANDVA-GYLGMDERDNVVCALPMFHVFCLTVCMNAPLMSGATVLIEPQFSPASVFKLVKQQQVTIFAGV 264
Cdd:cd05958 115 TMHFHRDPLASADRYAvNVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEEATPDLLLSAIARYKPTVLFTA 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 265 PTMYNYLFQHENGKKDDFSSIRLCISGGAAMPVALLTAFEEKFGVTILEGYGLSEASPVTCFNPFDRGRkPGSIGTSILH 344
Cdd:cd05958 195 PTAYRAMLAHPDAAGPDLSSLRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEMFHIFISARPGDAR-PGATGKPVPG 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 345 VENKVVDPLGRELPAHQVGELIVKGPNVMKGYYKMPMETehALKDGWLYTGDLARRDEDGYFYIVDRKKDMIIVGGYNVY 424
Cdd:cd05958 274 YEAKVVDDEGNPVPDGTIGRLAVRGPTGCRYLADKRQRT--YVQGGWNITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIA 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 425 PREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVVPkRSGVTE-----EDIMQHCETHLAKYKRPAAITFLDDIPKNAT 499
Cdd:cd05958 352 PPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVL-RPGVIPgpvlaRELQDHAKAHIAPYKYPRAIEFVTELPRTAT 430
|
....*....
gi 1816047872 500 GKMLRRALR 508
Cdd:cd05958 431 GKLQRFALR 439
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
28-509 |
1.72e-97 |
|
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: 301.18 E-value: 1.72e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 28 TYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYTPTEIGYMLTNGDVKAIVgvsq 107
Cdd:cd05972 2 SFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIV---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 108 llplyecmheslpkvelvilcqtgeaepeaadpevrmkmttfakilrpTSAakqnqelvpDDTAVILYTSGTTGKPKGAM 187
Cdd:cd05972 78 ------------------------------------------------TDA---------EDPALIYFTSGTTGLPKGVL 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 188 LTHQNLYSNANDVAGYLGMDERDNVVCALPMFHVFCLTVCMNAPLMSGATVLI--EPQFSPASVFKLVKQQQVTIFAGVP 265
Cdd:cd05972 101 HTHSYPLGHIPTAAYWLGLRPDDIHWNIADPGWAKGAWSSFFGPWLLGATVFVyeGPRFDAERILELLERYGVTSFCGPP 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 266 TMYNYLFQhENGKKDDFSSIRLCISGGAAMPVALLTAFEEKFGVTILEGYGLSEaSPVTCFNPFDRGRKPGSIGTSILHV 345
Cdd:cd05972 181 TAYRMLIK-QDLSSYKFSHLRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTE-TGLTVGNFPDMPVKPGSMGRPTPGY 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 346 ENKVVDPLGRELPAHQVGELIVK-GPNVM-KGYYKMPMETEHALKDGWLYTGDLARRDEDGYFYIVDRKKDMIIVGGYNV 423
Cdd:cd05972 259 DVAIIDDDGRELPPGEEGDIAIKlPPPGLfLGYVGDPEKTEASIRGDYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRI 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 424 YPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVVPK----RSGVTEEDIMQHCETHLAKYKRPAAITFLDDIPKNAT 499
Cdd:cd05972 339 GPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTsgyePSEELAEELQGHVKKVLAPYKYPREIEFVEELPKTIS 418
|
490
....*....|
gi 1816047872 500 GKMLRRALRD 509
Cdd:cd05972 419 GKIRRVELRD 428
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
28-507 |
8.10e-96 |
|
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: 297.44 E-value: 8.10e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 28 TYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYTPTEIGYMLTNGDVKAIVGVSQ 107
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 108 LlplyecmheSLPKVELVILCQTGEAEPEAADPEVRMKMttfakilrptsaakqnqelvpDDTAVILYTSGTTGKPKGAM 187
Cdd:TIGR01923 81 L---------EEKDFQADSLDRIEAAGRYETSLSASFNM---------------------DQIATLMFTSGTTGKPKAVP 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 188 LTHQNLYSNANDVAGYLGMDERDNVVCALPMFHVFCLTVCMNApLMSGATVLIEPQFspASVFKLVKQQQVTIFAGVPTM 267
Cdd:TIGR01923 131 HTFRNHYASAVGSKENLGFTEDDNWLLSLPLYHISGLSILFRW-LIEGATLRIVDKF--NQLLEMIANERVTHISLVPTQ 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 268 YNYLFQHENGKkddfSSIRLCISGGAAMPVALLTAFEEKfGVTILEGYGLSE-ASPVTCFNPFDRGRKPGSiGTSILHVE 346
Cdd:TIGR01923 208 LNRLLDEGGHN----ENLRKILLGGSAIPAPLIEEAQQY-GLPIYLSYGMTEtCSQVTTATPEMLHARPDV-GRPLAGRE 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 347 NKVVDPLGRElpahqVGELIVKGPNVMKGYYKMPMETEHALKDGWLYTGDLARRDEDGYFYIVDRKKDMIIVGGYNVYPR 426
Cdd:TIGR01923 282 IKIKVDNKEG-----HGEIMVKGANLMKGYLYQGELTPAFEQQGWFNTGDIGELDGEGFLYVLGRRDDLIISGGENIYPE 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 427 EVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVVpKRSGVTEEDIMQHCETHLAKYKRPAAITFLDDIPKNATGKMLRRA 506
Cdd:TIGR01923 357 EIETVLYQHPGIQEAVVVPKPDAEWGQVPVAYIV-SESDISQAKLIAYLTEKLAKYKVPIAFEKLDELPYNASGKILRNQ 435
|
.
gi 1816047872 507 L 507
Cdd:TIGR01923 436 L 436
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
28-508 |
4.56e-94 |
|
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: 292.75 E-value: 4.56e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 28 TYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYTPTEIGYMLTNGDVKAIVgvsq 107
Cdd:cd05903 3 TYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFV---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 108 llplyecmheslpkvelvilcqtgeaepeaadpevrmkmttfakilRPTSAAKQNQELVPDDTAVILYTSGTTGKPKGAM 187
Cdd:cd05903 79 ----------------------------------------------VPERFRQFDPAAMPDAVALLLFTSGTTGEPKGVM 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 188 LTHQNLYSNANDVAGYLGMDERDNVVCALPMFHVFCLTVCMNAPLMSGATVLIEPQFSPASVFKLVKQQQVTIFAGVPTM 267
Cdd:cd05903 113 HSHNTLSASIRQYAERLGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQDIWDPDKALALMREHGVTFMMGATPF 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 268 YNYLFQHENGKKDDFSSIRLCISGGAAMPVALLTAFEEKFGVTILEGYGLSE-ASPVTCFNPFDRGRKPGSIGTSILHVE 346
Cdd:cd05903 193 LTDLLNAVEEAGEPLSRLRTFVCGGATVPRSLARRAAELLGAKVCSAYGSTEcPGAVTSITPAPEDRRLYTDGRPLPGVE 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 347 NKVVDPLGRELPAHQVGELIVKGPNVMKGYYKMPMETEHALKDGWLYTGDLARRDEDGYFYIVDRKKDMIIVGGYNVYPR 426
Cdd:cd05903 273 IKVVDDTGATLAPGVEGELLSRGPSVFLGYLDRPDLTADAAPEGWFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVL 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 427 EVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVVPKrSG--VTEEDIMQHCETH-LAKYKRPAAITFLDDIPKNATGKML 503
Cdd:cd05903 353 EVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTK-SGalLTFDELVAYLDRQgVAKQYWPERLVHVDDLPRTPSGKVQ 431
|
....*
gi 1816047872 504 RRALR 508
Cdd:cd05903 432 KFRLR 436
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
27-509 |
1.30e-93 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 293.73 E-value: 1.30e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 27 MTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYTPTEIGYMLTNGDVKAIVGVS 106
Cdd:PRK08276 12 VTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVLIVSA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 107 QLLPLYECMHESLPKVELVILCQTGEAEPEAADPEVRmkmttfakilrptsaAKQNQELVPDDTA--VILYTSGTTGKPK 184
Cdd:PRK08276 92 ALADTAAELAAELPAGVPLLLVVAGPVPGFRSYEEAL---------------AAQPDTPIADETAgaDMLYSSGTTGRPK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 185 GAM--LTHQNLYSNANDVAGYLGMD---ERDNV--VCAlPMFHVFCLTVCMNAPLMSGaTVLIEPQFSPASVFKLVKQQQ 257
Cdd:PRK08276 157 GIKrpLPGLDPDEAPGMMLALLGFGmygGPDSVylSPA-PLYHTAPLRFGMSALALGG-TVVVMEKFDAEEALALIERYR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 258 VTIFAGVPTMYNYLFQ--HENGKKDDFSSIRLCISGGAAMPVALLTAFEEKFGVTILEGYGLSEASPVTCFNPFDRGRKP 335
Cdd:PRK08276 235 VTHSQLVPTMFVRMLKlpEEVRARYDVSSLRVAIHAAAPCPVEVKRAMIDWWGPIIHEYYASSEGGGVTVITSEDWLAHP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 336 GSIGTSILHvENKVVDPLGRELPAHQVGELIVKGPNVMKGYYKMPMETEHA-LKDGWLYTGDLARRDEDGYFYIVDRKKD 414
Cdd:PRK08276 315 GSVGKAVLG-EVRILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAArNPHGWVTVGDVGYLDEDGYLYLTDRKSD 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 415 MIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGyVVPKRSGVT-----EEDIMQHCETHLAKYKRPAAIT 489
Cdd:PRK08276 394 MIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKA-VVQPADGADagdalAAELIAWLRGRLAHYKCPRSID 472
|
490 500
....*....|....*....|
gi 1816047872 490 FLDDIPKNATGKMLRRALRD 509
Cdd:PRK08276 473 FEDELPRTPTGKLYKRRLRD 492
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
15-507 |
5.04e-92 |
|
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: 287.89 E-value: 5.04e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 15 PDSIACRFKDHMMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYTPTEIGYML 94
Cdd:cd05930 1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 95 tnGDVKAivgvsqllplyecmheslpkvELVILCqtgeaepeaadpevrmkmttfakilrptsaakqnqelvPDDTAVIL 174
Cdd:cd05930 81 --EDSGA---------------------KLVLTD--------------------------------------PDDLAYVI 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 175 YTSGTTGKPKGAMLTHQNLYSNANDVAGYLGMDERDNVvcALPMFHVFCLTVC-MNAPLMSGATVLIEPQ---FSPASVF 250
Cdd:cd05930 100 YTSGSTGKPKGVMVEHRGLVNLLLWMQEAYPLTPGDRV--LQFTSFSFDVSVWeIFGALLAGATLVVLPEevrKDPEALA 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 251 KLVKQQQVTIFAGVPTMYNYLFQHenGKKDDFSSIRLCISGGAAMPVALLTAFEEKF-GVTILEGYGLSEASPVTCFNPF 329
Cdd:cd05930 178 DLLAEEGITVLHLTPSLLRLLLQE--LELAALPSLRLVLVGGEALPPDLVRRWRELLpGARLVNLYGPTEATVDATYYRV 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 330 DRGRKPGS---IGTSILHVENKVVDPLGRELPAHQVGELIVKGPNVMKGYYKMPMETEHAL------KDGWLY-TGDLAR 399
Cdd:cd05930 256 PPDDEEDGrvpIGRPIPNTRVYVLDENLRPVPPGVPGELYIGGAGLARGYLNRPELTAERFvpnpfgPGERMYrTGDLVR 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 400 RDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVVPK-RSGVTEEDIMQHCETH 478
Cdd:cd05930 336 WLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDeGGELDEEELRAHLAER 415
|
490 500
....*....|....*....|....*....
gi 1816047872 479 LAKYKRPAAITFLDDIPKNATGKMLRRAL 507
Cdd:cd05930 416 LPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
27-509 |
1.98e-91 |
|
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ligase, 4-hydroxybenzoate-CoA ligase, 2-aminobenzoate-CoA ligase, etc. Members are related to fatty acid and acetate CoA ligases.
Pssm-ID: 274059 [Multi-domain] Cd Length: 505 Bit Score: 288.28 E-value: 1.98e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 27 MTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYTPTEIGYMLTNGDVKAIVGVS 106
Cdd:TIGR02262 31 LSYGELEAQVRRLAAALRRLGVKREERVLLLMLDGVDFPIAFLGAIRAGIVPVALNTLLTADDYAYMLEDSRARVVFVSG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 107 QLLPLYECMHESLPKVELVILcqTGEAEPeaadPEVRmkmttFAKILRPTSAAKQNQELVPDDTAVILYTSGTTGKPKGA 186
Cdd:TIGR02262 111 ALLPVIKAALGKSPHLEHRVV--VGRPEA----GEVQ-----LAELLATESEQFKPAATQADDPAFWLYSSGSTGMPKGV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 187 MLTHQNLYSNANDVAG-YLGMDERDNVVCALPMFHVFCLTVCMNAPLMSGATVLIEPQF-SPASVFKLVKQQQVTIFAGV 264
Cdd:TIGR02262 180 VHTHSNPYWTAELYARnTLGIREDDVCFSAAKLFFAYGLGNALTFPMSVGATTVLMGERpTPDAVFDRLRRHQPTIFYGV 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 265 PTMYNYLFQHENGKKDDFSSIRLCISGGAAMPVALLTAFEEKFGVTILEGYGLSEASPVTCFNPFDRGRKpGSIGTSILH 344
Cdd:TIGR02262 260 PTLYAAMLADPNLPSEDQVRLRLCTSAGEALPAEVGQRWQARFGVDIVDGIGSTEMLHIFLSNLPGDVRY-GTSGKPVPG 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 345 VENKVVDPLGRELPAHQVGELIVKGPNVMKGYYKMPMETEHALKDGWLYTGDLARRDEDGYFYIVDRKKDMIIVGGYNVY 424
Cdd:TIGR02262 339 YRLRLVGDGGQDVADGEPGELLISGPSSATMYWNNRAKSRDTFQGEWTRSGDKYVRNDDGSYTYAGRTDDMLKVSGIYVS 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 425 PREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVVPK-RSGVTEEDIMQHCETHLAKYKRPAAITFLDDIPKNATGKML 503
Cdd:TIGR02262 419 PFEIESALIQHPAVLEAAVVGVADEDGLIKPKAFVVLRpGQTALETELKEHVKDRLAPYKYPRWIVFVDDLPKTATGKIQ 498
|
....*.
gi 1816047872 504 RRALRD 509
Cdd:TIGR02262 499 RFKLRE 504
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
7-510 |
2.08e-91 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 289.35 E-value: 2.08e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 7 LEETASEKPDSIACRFKDHMMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYT 86
Cdd:PRK06155 27 LARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 87 PTEIGYMLTNGDVKAIVGVSQLLPLYECMHES-LPKVELVILcqtGEAEPEAADPEVRmkmttfAKILRPTSAAKQNQEL 165
Cdd:PRK06155 107 GPQLEHILRNSGARLLVVEAALLAALEAADPGdLPLPAVWLL---DAPASVSVPAGWS------TAPLPPLDAPAPAAAV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 166 VPDDTAVILYTSGTTGKPKGAMLTHQNLYSNANDVAGYLGMDERDNVVCALPMFHVFCLTVCMNApLMSGATVLIEPQFS 245
Cdd:PRK06155 178 QPGDTAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADDVLYTTLPLFHTNALNAFFQA-LLAGATYVLEPRFS 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 246 PASVFKLVKQQQVTIFAGVPTMYNYLFQHENGKKDDFSSIRLCISGGaaMPVALLTAFEEKFGVTILEGYGLSEASPVTC 325
Cdd:PRK06155 257 ASGFWPAVRRHGATVTYLLGAMVSILLSQPARESDRAHRVRVALGPG--VPAALHAAFRERFGVDLLDGYGSTETNFVIA 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 326 FNPfdRGRKPGSIGTSILHVENKVVDPLGRELPAHQVGELIVKGPN---VMKGYYKMPMETEHALKDGWLYTGDLARRDE 402
Cdd:PRK06155 335 VTH--GSQRPGSMGRLAPGFEARVVDEHDQELPDGEPGELLLRADEpfaFATGYFGMPEKTVEAWRNLWFHTGDRVVRDA 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 403 DGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVVPkRSGVTEE--DIMQHCETHLA 480
Cdd:PRK06155 413 DGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVL-RDGTALEpvALVRHCEPRLA 491
|
490 500 510
....*....|....*....|....*....|
gi 1816047872 481 KYKRPAAITFLDDIPKNATGKMLRRALRDI 510
Cdd:PRK06155 492 YFAVPRYVEFVAALPKTENGKVQKFVLREQ 521
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
11-510 |
8.99e-90 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 285.28 E-value: 8.99e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 11 ASEKPDSIACRFKDHMMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYTPTEI 90
Cdd:PRK07788 59 ARRAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 91 GYMLTNGDVKAIVGVSQLLPLYECMHESLPKVELVILCQTGEAEPEAADPevrmkmtTFAKILRPTSAAKQnqELVPDDT 170
Cdd:PRK07788 139 AEVAAREGVKALVYDDEFTDLLSALPPDLGRLRAWGGNPDDDEPSGSTDE-------TLDDLIAGSSTAPL--PKPPKPG 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 171 AVILYTSGTTGKPKGAMLTHQNLYSNandVAGYLG---MDERDNVVCALPMFHVFCLtVCMNAPLMSGATVLIEPQFSPA 247
Cdd:PRK07788 210 GIVILTSGTTGTPKGAPRPEPSPLAP---LAGLLSrvpFRAGETTLLPAPMFHATGW-AHLTLAMALGSTVVLRRRFDPE 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 248 SVFKLVKQQQVTIFAGVPTMYNYLFQH--ENGKKDDFSSIRLCISGGAAMPVALLTAFEEKFGVTILEGYGLSEASPVTC 325
Cdd:PRK07788 286 ATLEDIAKHKATALVVVPVMLSRILDLgpEVLAKYDTSSLKIIFVSGSALSPELATRALEAFGPVLYNLYGSTEVAFATI 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 326 FNPFDRGRKPGSIGTSILHVENKVVDPLGRELPAHQVGELIVKGPNVMKGYykmpmeTEHALK---DGWLYTGDLARRDE 402
Cdd:PRK07788 366 ATPEDLAEAPGTVGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFPFEGY------TDGRDKqiiDGLLSSGDVGYFDE 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 403 DGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVVPKR-SGVTEEDIMQHCETHLAK 481
Cdd:PRK07788 440 DGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKAPgAALDEDAIKDYVRDNLAR 519
|
490 500
....*....|....*....|....*....
gi 1816047872 482 YKRPAAITFLDDIPKNATGKMLRRALRDI 510
Cdd:PRK07788 520 YKVPRDVVFLDELPRNPTGKVLKRELREM 548
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
1-509 |
1.79e-89 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 282.93 E-value: 1.79e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 1 MNLVSKLEETASEKPDSIACRFKDHMMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVP 80
Cdd:PRK06145 2 FNLSASIAFHARRTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 81 INPLYTPTEIGYMLTNGDVKaivgvsqlLPLYECMHESLPKVELVILCQTgeaepEAADPEVRmkmttfaKILRPTSAAK 160
Cdd:PRK06145 82 INYRLAADEVAYILGDAGAK--------LLLVDEEFDAIVALETPKIVID-----AAAQADSR-------RLAQGGLEIP 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 161 QNQELVPDDTAVILYTSGTTGKPKGAMLTHQNLYSNANDVAGYLGMDERDNVVCALPMFHVFCLTVCMNAPLMSGATVLI 240
Cdd:PRK06145 142 PQAAVAPTDLVRLMYTSGTTDRPKGVMHSYGNLHWKSIDHVIALGLTASERLLVVGPLYHVGAFDLPGIAVLWVGGTLRI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 241 EPQFSPASVFKLVKQQQVTIFAGVPTMYNYLFQHENGKKDDFSSIRLCISGGAAMPVALLTAFEEKF-GVTILEGYGLSE 319
Cdd:PRK06145 222 HREFDPEAVLAAIERHRLTCAWMAPVMLSRVLTVPDRDRFDLDSLAWCIGGGEKTPESRIRDFTRVFtRARYIDAYGLTE 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 320 ASPVTCFnpFDRGR---KPGSIGTSILHVENKVVDPLGRELPAHQVGELIVKGPNVMKGYYKMPMETEHALKDGWLYTGD 396
Cdd:PRK06145 302 TCSGDTL--MEAGReieKIGSTGRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGDWFRSGD 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 397 LARRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVVPKR-SGVTEEDIMQHC 475
Cdd:PRK06145 380 VGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPgATLTLEALDRHC 459
|
490 500 510
....*....|....*....|....*....|....
gi 1816047872 476 ETHLAKYKRPAAITFLDDIPKNATGKMLRRALRD 509
Cdd:PRK06145 460 RQRLASFKVPRQLKVRDELPRNPSGKVLKRVLRD 493
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
1-511 |
3.35e-89 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 283.09 E-value: 3.35e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 1 MNLVSKLEETASEKPDSIACRFKDHMMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVP 80
Cdd:PRK07470 7 MNLAHFLRQAARRFPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 81 INPLYTPTEIGYMLTNGDVKAIVGVSQLLPLYECMHESLPKVELVILCQTGEAEPEAAdpevrmkmttfAKILRPTSAAK 160
Cdd:PRK07470 87 TNFRQTPDEVAYLAEASGARAMICHADFPEHAAAVRAASPDLTHVVAIGGARAGLDYE-----------ALVARHLGARV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 161 QNQELVPDDTAVILYTSGTTGKPKGAMLTH-QNLYSNANDVAGYL-GMDERDnvvCALPMfhvfcltvcmnAPLMSGA-- 236
Cdd:PRK07470 156 ANAAVDHDDPCWFFFTSGTTGRPKAAVLTHgQMAFVITNHLADLMpGTTEQD---ASLVV-----------APLSHGAgi 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 237 -----------TVLI-EPQFSPASVFKLVKQQQVTIFAGVPTMYNYLFQHENGKKDDFSSIRLCISGGAAMPVALLTAFE 304
Cdd:PRK07470 222 hqlcqvargaaTVLLpSERFDPAEVWALVERHRVTNLFTVPTILKMLVEHPAVDRYDHSSLRYVIYAGAPMYRADQKRAL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 305 EKFGVTILEGYGLSEAS-PVTCFNPFDRGRKPG---SIGTSILH---VENKVVDPLGRELPAHQVGELIVKGPNVMKGYY 377
Cdd:PRK07470 302 AKLGKVLVQYFGLGEVTgNITVLPPALHDAEDGpdaRIGTCGFErtgMEVQIQDDEGRELPPGETGEICVIGPAVFAGYY 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 378 KMPMETEHALKDGWLYTGDLARRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKG 457
Cdd:PRK07470 382 NNPEANAKAFRDGWFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVA 461
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1816047872 458 YVVPKRSG-VTEEDIMQHCETHLAKYKRPAAITFLDDIPKNATGKMLRRALRDIL 511
Cdd:PRK07470 462 VCVARDGApVDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMVREEL 516
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
169-504 |
1.44e-88 |
|
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: 275.15 E-value: 1.44e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 169 DTAVILYTSGTTGKPKGAMLTHQNLYSNANDVAGYLGMDERDNVVCALPMFHVFCLTVCMNAPLMSGATVLIEPQFSPAS 248
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIINPFFHTFGYKAGIVACLLTGATVVPVAVFDVDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 249 VFKLVKQQQVTIFAGVPTMYNYLFQHENGKKDDFSSIRLCISGGAAMPVALLTAFEEKFGV-TILEGYGLSEASPVTCFN 327
Cdd:cd17638 81 ILEAIERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFeTVLTAYGLTEAGVATMCR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 328 PFDRGRKPGS-IGTSILHVENKVVDPlgrelpahqvGELIVKGPNVMKGYYKMPMETEHAL-KDGWLYTGDLARRDEDGY 405
Cdd:cd17638 161 PGDDAETVATtCGRACPGFEVRIADD----------GEVLVRGYNVMQGYLDDPEATAEAIdADGWLHTGDVGELDERGY 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 406 FYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVVPKR-SGVTEEDIMQHCETHLAKYKR 484
Cdd:cd17638 231 LRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPgVTLTEEDVIAWCRERLANYKV 310
|
330 340
....*....|....*....|
gi 1816047872 485 PAAITFLDDIPKNATGKMLR 504
Cdd:cd17638 311 PRFVRFLDELPRNASGKVMK 330
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
169-504 |
3.44e-88 |
|
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: 274.15 E-value: 3.44e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 169 DTAVILYTSGTTGKPKGAMLTHQNLYSNANDVAGYLGMDERDNVVCALPMFHV--FCLTVCMnapLMSGATVLIEPQFSP 246
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPLFHIagLNLALAT---FHAGGANVVMEKFDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 247 ASVFKLVKQQQVTIFAGVPTMYNYLFQHENGKKDDFSSIRLCisGGAAMPvALLTAFEEKFGVTILEGYGLSEASPVTCF 326
Cdd:cd17637 78 AEALELIEEEKVTLMGSFPPILSNLLDAAEKSGVDLSSLRHV--LGLDAP-ETIQRFEETTGATFWSLYGQTETSGLVTL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 327 NPFDRgrKPGSIGTSILHVENKVVDPLGRELPAHQVGELIVKGPNVMKGYYKMPMETEHALKDGWLYTGDLARRDEDGYF 406
Cdd:cd17637 155 SPYRE--RPGSAGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTFRNGWHHTGDLGRFDEDGYL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 407 YIVDRK--KDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVV--PKRSgVTEEDIMQHCETHLAKY 482
Cdd:cd17637 233 WYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVlkPGAT-LTADELIEFVGSRIARY 311
|
330 340
....*....|....*....|..
gi 1816047872 483 KRPAAITFLDDIPKNATGKMLR 504
Cdd:cd17637 312 KKPRYVVFVEALPKTADGSIDR 333
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
11-507 |
3.69e-87 |
|
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: 276.70 E-value: 3.69e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 11 ASEKPDSIACRF--KDHMMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYTPT 88
Cdd:cd05923 11 ASRAPDACAIADpaRGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 89 EIGYMLTNGDVKAIVGVSQLLPLYECMHESLPKVELVILCQTGEAE---PEAADPEVRmkmttfakilrptsaakqnqel 165
Cdd:cd05923 91 ELAELIERGEMTAAVIAVDAQVMDAIFQSGVRVLALSDLVGLGEPEsagPLIEDPPRE---------------------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 166 vPDDTAVILYTSGTTGKPKGAMLTHQNLYSNA---NDVAGYL-GmdeRDNVVCAL-PMFHVFCLTVCMNAPLMSGATVLI 240
Cdd:cd05923 149 -PEQPAFVFYTSGTTGLPKGAVIPQRAAESRVlfmSTQAGLRhG---RHNVVLGLmPLYHVIGFFAVLVAALALDGTYVV 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 241 EPQFSPASVFKLVKQQQVTIFAGVPTMYNYLFQHENGKKDDFSSIRLCISGGAAMPVALLTAFEEKFGVTILEGYGLSEA 320
Cdd:cd05923 225 VEEFDPADALKLIEQERVTSLFATPTHLDALAAAAEFAGLKLSSLRHVTFAGATMPDAVLERVNQHLPGEKVNIYGTTEA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 321 SPVTcfnpFDRGRKPGSIGTSILHVENKVVDPLGRE---LPAHQVGELIVK--GPNVMKGYYKMPMETEHALKDGWLYTG 395
Cdd:cd05923 305 MNSL----YMRDARTGTEMRPGFFSEVRIVRIGGSPdeaLANGEEGELIVAaaADAAFTGYLNQPEATAKKLQDGWYRTG 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 396 DLARRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVVPKRSGVTEEDIMQHC 475
Cdd:cd05923 381 DVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREGTLSADELDQFC 460
|
490 500 510
....*....|....*....|....*....|...
gi 1816047872 476 ET-HLAKYKRPAAITFLDDIPKNATGKMLRRAL 507
Cdd:cd05923 461 RAsELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
1-508 |
1.24e-86 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 274.56 E-value: 1.24e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 1 MNLVSKLEETASEKPDsiACRFKDHMMTYQELNEHIQRFADGLQEAgmekgDHLALLLGNSPDFIIAFFGALKAGIVVVP 80
Cdd:PRK07787 2 ASLNPAAVAAAADIAD--AVRIGGRVLSRSDLAGAATAVAERVAGA-----RRVAVLATPTLATVLAVVGALIAGVPVVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 81 INPLYTPTEIGYMLTNGDVKAIVGVSQLLPlyecmhESLPKVELVILCQTGEAEPEAAdpevrmkmttfakilrptsaak 160
Cdd:PRK07787 75 VPPDSGVAERRHILADSGAQAWLGPAPDDP------AGLPHVPVRLHARSWHRYPEPD---------------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 161 qnqelvPDDTAVILYTSGTTGKPKGAMLTHQNLYSNANDVAGYLGMDERDNVVCALPMFHVFCLTVCMNAPLMSGATVLI 240
Cdd:PRK07787 127 ------PDAPALIVYTSGTTGPPKGVVLSRRAIAADLDALAEAWQWTADDVLVHGLPLFHVHGLVLGVLGPLRIGNRFVH 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 241 EPQFSPASVFKLVkQQQVTIFAGVPTMYNYLFQHENGKKdDFSSIRLCISGGAAMPVALLTAFEEKFGVTILEGYGLSEa 320
Cdd:PRK07787 201 TGRPTPEAYAQAL-SEGGTLYFGVPTVWSRIAADPEAAR-ALRGARLLVSGSAALPVPVFDRLAALTGHRPVERYGMTE- 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 321 SPVTCFNPFDRGRKPGSIGTSILHVENKVVDPLGRELPA--HQVGELIVKGPNVMKGYYKMPMETEHAL-KDGWLYTGDL 397
Cdd:PRK07787 278 TLITLSTRADGERRPGWVGLPLAGVETRLVDEDGGPVPHdgETVGELQVRGPTLFDGYLNRPDATAAAFtADGWFRTGDV 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 398 ARRDEDGYFYIVDRKK-DMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVVPKRsGVTEEDIMQHCE 476
Cdd:PRK07787 358 AVVDPDGMHRIVGREStDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVGAD-DVAADELIDFVA 436
|
490 500 510
....*....|....*....|....*....|..
gi 1816047872 477 THLAKYKRPAAITFLDDIPKNATGKMLRRALR 508
Cdd:PRK07787 437 QQLSVHKRPREVRFVDALPRNAMGKVLKKQLL 468
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
3-513 |
3.80e-86 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 276.15 E-value: 3.80e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 3 LVSKLEETASEKPDSIACRFKDHMMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPIN 82
Cdd:PRK06178 35 LTEYLRAWARERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 83 PLYTPTEIGYMLTNGDVKAIVGVSQLLPLYECMHESLPkVELVILCQTGE---AEPEAADPEV----RMKMTTFAKILRP 155
Cdd:PRK06178 115 PLFREHELSYELNDAGAEVLLALDQLAPVVEQVRAETS-LRHVIVTSLADvlpAEPTLPLPDSlrapRLAAAGAIDLLPA 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 156 TSAAKQNQELVP---DDTAVILYTSGTTGKPKGAMLTHQNL-YSNANDVAGYLGMDERDNVVCALPMFHV----FCLTVc 227
Cdd:PRK06178 194 LRACTAPVPLPPpalDALAALNYTGGTTGMPKGCEHTQRDMvYTAAAAYAVAVVGGEDSVFLSFLPEFWIagenFGLLF- 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 228 mnaPLMSGATVLIEPQFSPASVFKLVKQQQVTIFAGVPTMYNYLFQHENGKKDDFSSIR--LCISGGAAMPVALLTAFEE 305
Cdd:PRK06178 273 ---PLFSGATLVLLARWDAVAFMAAVERYRVTRTVMLVDNAVELMDHPRFAEYDLSSLRqvRVVSFVKKLNPDYRQRWRA 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 306 KFGVTILEG-YGLSEASPVTCF------NPFDRGRKPGSIGTSILHVENKVVD-PLGRELPAHQVGELIVKGPNVMKGYY 377
Cdd:PRK06178 350 LTGSVLAEAaWGMTETHTCDTFtagfqdDDFDLLSQPVFVGLPVPGTEFKICDfETGELLPLGAEGEIVVRTPSLLKGYW 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 378 KMPMETEHALKDGWLYTGDLARRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKG 457
Cdd:PRK06178 430 NKPEATAEALRDGWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVA 509
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1816047872 458 YVVPK-RSGVTEEDIMQHCETHLAKYKRPaAITFLDDIPKNATGKMLRRALRDILPQ 513
Cdd:PRK06178 510 FVQLKpGADLTAAALQAWCRENMAVYKVP-EIRIVDALPMTATGKVRKQDLQALAEE 565
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
167-508 |
5.72e-86 |
|
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: 269.35 E-value: 5.72e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 167 PDDTAVILYTSGTTGKPKGAMLTHQNLYSNANDVAGYLGMDERDNVVCALPMFHVFCLTVCMNAPLMSGATVLIEpqfSP 246
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVVLA---GP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 247 A---------SVFKLVKQQQVTIFAGVPTMYNYLFQHENGKkdDFSSIRLCISGGAAMPVALLTAFEEKFGVTILEGYGL 317
Cdd:cd05944 78 AgyrnpglfdNFWKLVERYRITSLSTVPTVYAALLQVPVNA--DISSLRFAMSGAAPLPVELRARFEDATGLPVVEGYGL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 318 SEASPVTCFNPFDRGRKPGSIGTSI--LHVENKVVDPLG---RELPAHQVGELIVKGPNVMKGYYKMPMETEHALKDGWL 392
Cdd:cd05944 156 TEATCLVAVNPPDGPKRPGSVGLRLpyARVRIKVLDGVGrllRDCAPDEVGEICVAGPGVFGGYLYTEGNKNAFVADGWL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 393 YTGDLARRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVVPKR-SGVTEEDI 471
Cdd:cd05944 236 NTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPgAVVEEEEL 315
|
330 340 350
....*....|....*....|....*....|....*...
gi 1816047872 472 MQHCETHLA-KYKRPAAITFLDDIPKNATGKMLRRALR 508
Cdd:cd05944 316 LAWARDHVPeRAAVPKHIEVLEELPVTAVGKVFKPALR 353
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
7-513 |
2.75e-85 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 273.47 E-value: 2.75e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 7 LEETASEKPDSIAC------RFKDHMMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVP 80
Cdd:PRK13295 30 LDACVASCPDKTAVtavrlgTGAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNP 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 81 INPLYTPTEIGYMLTNGDVKAIVgVSQLLPLY--ECM----HESLPKVELVI-------------LCQTG-EAEPEAADP 140
Cdd:PRK13295 110 LMPIFRERELSFMLKHAESKVLV-VPKTFRGFdhAAMarrlRPELPALRHVVvvggdgadsfealLITPAwEQEPDAPAI 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 141 EVRmkmttfakiLRPTsaakqnqelvPDDTAVILYTSGTTGKPKGAMLTHQNLYSNANDVAGYLGMDERDNVVCALPMFH 220
Cdd:PRK13295 189 LAR---------LRPG----------PDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILMASPMAH 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 221 VFCLTVCMNAPLMSGATVLIEPQFSPASVFKLVKQQQVTIFAGVPTMYNYLFQHENGKKDDFSSIRLCISGGAAMPVALL 300
Cdd:PRK13295 250 QTGFMYGLMMPVMLGATAVLQDIWDPARAAELIRTEGVTFTMASTPFLTDLTRAVKESGRPVSSLRTFLCAGAPIPGALV 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 301 TAFEEKFGVTILEGYGLSEASPVTCFNPFDRGRKPG-SIGTSILHVENKVVDPLGRELPAHQVGELIVKGPNVMKGYYKM 379
Cdd:PRK13295 330 ERARAALGAKIVSAWGMTENGAVTLTKLDDPDERAStTDGCPLPGVEVRVVDADGAPLPAGQIGRLQVRGCSNFGGYLKR 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 380 PMETEHAlKDGWLYTGDLARRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYV 459
Cdd:PRK13295 410 PQLNGTD-ADGWFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFV 488
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1816047872 460 VPKR-SGVTEEDIMQHCETH-LAKYKRPAAITFLDDIPKNATGKMLRRALRDILPQ 513
Cdd:PRK13295 489 VPRPgQSLDFEEMVEFLKAQkVAKQYIPERLVVRDALPRTPSGKIQKFRLREMLRG 544
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
28-510 |
1.04e-84 |
|
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: 271.71 E-value: 1.04e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 28 TYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYTPTEIGYMLTNGDVKAIVGVSQ 107
Cdd:cd17642 46 SYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFCSKK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 108 LLPLYECMHESLPKVELVILCQTGEaepeaaDPEVRMKMTTFakILRPTSAAKQNQELVP------DDTAVILYTSGTTG 181
Cdd:cd17642 126 GLQKVLNVQKKLKIIKTIIILDSKE------DYKGYQCLYTF--ITQNLPPGFNEYDFKPpsfdrdEQVALIMNSSGSTG 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 182 KPKGAMLTHQNL---YSNANDVAGYLGMDERDNVVCALPMFHVF-CLTVCmnAPLMSGATVLIEPQFSPASVFKLVKQQQ 257
Cdd:cd17642 198 LPKGVQLTHKNIvarFSHARDPIFGNQIIPDTAILTVIPFHHGFgMFTTL--GYLICGFRVVLMYKFEEELFLRSLQDYK 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 258 VTIFAGVPTMYNYLFQHENGKKDDFSSIRLCISGGAAMPVALLTAFEEKFGVT-ILEGYGLSEASPVTCFNPfDRGRKPG 336
Cdd:cd17642 276 VQSALLVPTLFAFFAKSTLVDKYDLSNLHEIASGGAPLSKEVGEAVAKRFKLPgIRQGYGLTETTSAILITP-EGDDKPG 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 337 SIGTSILHVENKVVDP-LGRELPAHQVGELIVKGPNVMKGYYKMPMETEHAL-KDGWLYTGDLARRDEDGYFYIVDRKKD 414
Cdd:cd17642 355 AVGKVVPFFYAKVVDLdTGKTLGPNERGELCVKGPMIMKGYVNNPEATKALIdKDGWLHSGDIAYYDEDGHFFIVDRLKS 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 415 MIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEaVKGYVVPKRSGV--TEEDIMQHCETHLAKYKR-PAAITFL 491
Cdd:cd17642 435 LIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGE-LPAAVVVLEAGKtmTEKEVMDYVASQVSTAKRlRGGVKFV 513
|
490
....*....|....*....
gi 1816047872 492 DDIPKNATGKMLRRALRDI 510
Cdd:cd17642 514 DEVPKGLTGKIDRRKIREI 532
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
9-511 |
1.19e-84 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 272.01 E-value: 1.19e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 9 ETASEKPDSIAcrFKDHM---MTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLY 85
Cdd:PRK06087 31 QTARAMPDKIA--VVDNHgasYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 86 TPTEIGYMLTNGDVKAIVG---------VSQLLPLyecmHESLPKVELVILCQtgEAEPEAADPevrmkmtTFAKILRPT 156
Cdd:PRK06087 109 REAELVWVLNKCQAKMFFAptlfkqtrpVDLILPL----QNQLPQLQQIVGVD--KLAPATSSL-------SLSQIIADY 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 157 SAAKQNQELVPDDTAVILYTSGTTGKPKGAMLTHQNLYSNANDVAGYLGMDERDNVVCALPMFHVFCLTVCMNAPLMSGA 236
Cdd:PRK06087 176 EPLTTAITTHGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGA 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 237 TVLIEPQFSPASVFKLVKQQQVTIFAG-VPTMYNyLFQHENGKKDDFSSIRLCISGGAAMPVALLTAFEEKfGVTILEGY 315
Cdd:PRK06087 256 RSVLLDIFTPDACLALLEQQRCTCMLGaTPFIYD-LLNLLEKQPADLSALRFFLCGGTTIPKKVARECQQR-GIKLLSVY 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 316 GLSEASPVTCFNPFD-RGRKPGSIGTSILHVENKVVDPLGRELPAHQVGELIVKGPNVMKGYYKMPMETEHAL-KDGWLY 393
Cdd:PRK06087 334 GSTESSPHAVVNLDDpLSRFMHTDGYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYLDEPELTARALdEEGWYY 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 394 TGDLARRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVVPKRS--GVTEEDI 471
Cdd:PRK06087 414 SGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVVLKAPhhSLTLEEV 493
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1816047872 472 MQH-CETHLAKYKRPAAITFLDDIPKNATGKMLRRALR-DIL 511
Cdd:PRK06087 494 VAFfSRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRkDIM 535
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
25-511 |
3.68e-82 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 265.03 E-value: 3.68e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 25 HMMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYTPTEIGYMLTNGDVKAIVG 104
Cdd:PRK07008 38 HRYTYRDCERRAKQLAQALAALGVEPGDRVGTLAWNGYRHLEAYYGVSGSGAVCHTINPRLFPEQIAYIVNHAEDRYVLF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 105 VSQLLPLYECMHESLPKVE-LVILCQtgeaepEAADPEVRMKMTTFAKILRPTSAAKQNQELVPDDTAVILYTSGTTGKP 183
Cdd:PRK07008 118 DLTFLPLVDALAPQCPNVKgWVAMTD------AAHLPAGSTPLLCYETLVGAQDGDYDWPRFDENQASSLCYTSGTTGNP 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 184 KGAMLTHQN--LYSNANDVAGYLGMDERDNVVCALPMFHVFCLTVCMNAPLMSGATVLIEPQFSPASVFKLVKQQQVTIF 261
Cdd:PRK07008 192 KGALYSHRStvLHAYGAALPDAMGLSARDAVLPVVPMFHVNAWGLPYSAPLTGAKLVLPGPDLDGKSLYELIEAERVTFS 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 262 AGVPTMYNYLFQH--ENGKKddFSSIRLCISGGAAMPVALLTAFEEKFGVTILEGYGLSEASPV--TC--------FNPF 329
Cdd:PRK07008 272 AGVPTVWLGLLNHmrEAGLR--FSTLRRTVIGGSACPPAMIRTFEDEYGVEVIHAWGMTEMSPLgtLCklkwkhsqLPLD 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 330 DRGRKPGSIGTSILHVENKVVDPLGRELPAHQV--GELIVKGPNVMKGYYKmpmETEHALKDGWLYTGDLARRDEDGYFY 407
Cdd:PRK07008 350 EQRKLLEKQGRVIYGVDMKIVGDDGRELPWDGKafGDLQVRGPWVIDRYFR---GDASPLVDGWFPTGDVATIDADGFMQ 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 408 IVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVVPKRSG-VTEEDIMQHCETHLAKYKRPA 486
Cdd:PRK07008 427 ITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLVVVKRPGAeVTREELLAFYEGKVAKWWIPD 506
|
490 500
....*....|....*....|....*
gi 1816047872 487 AITFLDDIPKNATGKMLRRALRDIL 511
Cdd:PRK07008 507 DVVFVDAIPHTATGKLQKLKLREQF 531
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
51-509 |
1.19e-81 |
|
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: 262.27 E-value: 1.19e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 51 GDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYTPTEIGYMLTNGDVKAIVGVSQLLPLYECMH--ESLPKVELVILc 128
Cdd:cd05909 31 GENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVLTSKQFIEKLKLHHlfDVEYDARIVYL- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 129 qtgeaEPEAADPEVRMKMTTFAKILRPTSAAKQNQELV---PDDTAVILYTSGTTGKPKGAMLTHQNLYSNANDVAGYLG 205
Cdd:cd05909 110 -----EDLRAKISKADKCKAFLAGKFPPKWLLRIFGVApvqPDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFD 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 206 MDERDNVVCALPMFHVFCLTVCMNAPLMSGATVLIEPQ-FSPASVFKLVKQQQVTIFAGVPTMYNYLFQheNGKKDDFSS 284
Cdd:cd05909 185 PNPEDVVFGALPFFHSFGLTGCLWLPLLSGIKVVFHPNpLDYKKIPELIYDKKATILLGTPTFLRGYAR--AAHPEDFSS 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 285 IRLCISGGAAMPVALLTAFEEKFGVTILEGYGLSEASPVTCFNPFDRGRKPGSIGTSILHVENKVVDPLGR-ELPAHQVG 363
Cdd:cd05909 263 LRLVVAGAEKLKDTLRQEFQEKFGIRILEGYGTTECSPVISVNTPQSPNKEGTVGRPLPGMEVKIVSVETHeEVPIGEGG 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 364 ELIVKGPNVMKGYYKMPMETEHALKDGWLYTGDLARRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSH-PDVKEAV 442
Cdd:cd05909 343 LLLVRGPNVMLGYLNEPELTSFAFGDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEIlPEDNEVA 422
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1816047872 443 VVGVPDPQSGEAVKGYVVPKRSGVTE-EDIMQHCET-HLAKykrPAAITFLDDIPKNATGKMLRRALRD 509
Cdd:cd05909 423 VVSVPDGRKGEKIVLLTTTTDTDPSSlNDILKNAGIsNLAK---PSYIHQVEEIPLLGTGKPDYVTLKA 488
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
22-504 |
1.44e-81 |
|
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: 261.22 E-value: 1.44e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 22 FKDHMMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYTPTEIGYMLTNGDVKA 101
Cdd:cd05914 3 YGGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 102 IVgVSQllplyecmheslpkvelvilcqtgeaepeaadpevrmkmttfakilrptsaakqnqelvPDDTAVILYTSGTTG 181
Cdd:cd05914 83 IF-VSD-----------------------------------------------------------EDDVALINYTSGTTG 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 182 KPKGAMLTHQNLYSNANDVAGYLGMDERDNVVCALPMFHVFCLTVCMNAPLMSGATVLIEPQFSPASVFKLvKQQQVTIF 261
Cdd:cd05914 103 NSKGVMLTYRNIVSNVDGVKEVVLLGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFLDKIPSAKIIAL-AFAQVTPT 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 262 AGVPTMY----------------------------NYLFQHENGKK--DDFS-SIRLCISGGAAMPvALLTAFEEKFGVT 310
Cdd:cd05914 182 LGVPVPLviekifkmdiipkltlkkfkfklakkinNRKIRKLAFKKvhEAFGgNIKEFVIGGAKIN-PDVEEFLRTIGFP 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 311 ILEGYGLSEASPVTCFNPFDRGRKpGSIGTSILHVENKVVDPLgrelPAHQVGELIVKGPNVMKGYYKMPMETEHAL-KD 389
Cdd:cd05914 261 YTIGYGMTETAPIISYSPPNRIRL-GSAGKVIDGVEVRIDSPD----PATGEGEIIVRGPNVMKGYYKNPEATAEAFdKD 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 390 GWLYTGDLARRDEDGYFYIVDRKKDMIIVG-GYNVYPREVEEVLYSHPDVKEAVVV---------GVPDPQSGEAVKGYV 459
Cdd:cd05914 336 GWFHTGDLGKIDAEGYLYIRGRKKEMIVLSsGKNIYPEEIEAKINNMPFVLESLVVvqekklvalAYIDPDFLDVKALKQ 415
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1816047872 460 VPKRSGVTEEDIMQHcETHLAKYKRPAAITFL-DDIPKNATGKMLR 504
Cdd:cd05914 416 RNIIDAIKWEVRDKV-NQKVPNYKKISKVKIVkEEFEKTPKGKIKR 460
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
7-507 |
5.71e-81 |
|
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: 260.34 E-value: 5.71e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 7 LEETASEKPDSIACRFKDHMMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYT 86
Cdd:cd05920 21 LARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPVLALPSHR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 87 PTEIGYMLTNGDVKAIVGVSQL-----LPLYECMHESLPkvelvilcqtgeaepeaadpevrmkmttfakilrptsaakq 161
Cdd:cd05920 101 RSELSAFCAHAEAVAYIVPDRHagfdhRALARELAESIP----------------------------------------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 162 nqelvpdDTAVILYTSGTTGKPKGAMLTHQNLYSNANDVAGYLGMDERDNVVCALPMFHVFCLTvC--MNAPLMSGATVL 239
Cdd:cd05920 140 -------EVALFLLSGGTTGTPKLIPRTHNDYAYNVRASAEVCGLDQDTVYLAVLPAAHNFPLA-CpgVLGTLLAGGRVV 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 240 IEPQFSPASVFKLVKQQQVTIFAGVPTMYNYLFQHENGKKDDFSSIRLCISGGAAMPVALLTAFEEKFGVTILEGYGLSE 319
Cdd:cd05920 212 LAPDPSPDAAFPLIEREGVTVTALVPALVSLWLDAAASRRADLSSLRLLQVGGARLSPALARRVPPVLGCTLQQVFGMAE 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 320 AspVTCFNPFDrgrKPGSIgtsILHV---------ENKVVDPLGRELPAHQVGELIVKGPNVMKGYYKMPMETEHAL-KD 389
Cdd:cd05920 292 G--LLNYTRLD---DPDEV---IIHTqgrpmspddEIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFtPD 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 390 GWLYTGDLARRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVVPKRSGVTEE 469
Cdd:cd05920 364 GFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVLRDPPPSAA 443
|
490 500 510
....*....|....*....|....*....|....*....
gi 1816047872 470 DIMQHC-ETHLAKYKRPAAITFLDDIPKNATGKMLRRAL 507
Cdd:cd05920 444 QLRRFLrERGLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
28-508 |
1.75e-80 |
|
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: 257.82 E-value: 1.75e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 28 TYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYTPTEIGYMLTNGDVKAIVgvsq 107
Cdd:cd05969 2 TFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLI---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 108 llplyecmheslpkvelvilcqtgeaepeaADPEVRMKMTtfakilrptsaakqnqelvPDDTAVILYTSGTTGKPKGAM 187
Cdd:cd05969 78 ------------------------------TTEELYERTD-------------------PEDPTLLHYTSGTTGTPKGVL 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 188 LTHQNLYSNANDVAGYLGMDERDNVVCALPMFHVFCLTVCMNAPLMSGATVLI-EPQFSPASVFKLVKQQQVTIFAGVPT 266
Cdd:cd05969 109 HVHDAMIFYYFTGKYVLDLHPDDIYWCTADPGWVTGTVYGIWAPWLNGVTNVVyEGRFDAESWYGIIERVKVTVWYTAPT 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 267 MYNYLFQH--ENGKKDDFSSIRLCISGGAAMPVALLTAFEEKFGVTILEGYGLSEASPVTCFNPFDRGRKPGSIGTSILH 344
Cdd:cd05969 189 AIRMLMKEgdELARKYDLSSLRFIHSVGEPLNPEAIRWGMEVFGVPIHDTWWQTETGSIMIANYPCMPIKPGSMGKPLPG 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 345 VENKVVDPLGRELPAHQVGELIVKG--PNVMKGYYKMPMETEHALKDGWLYTGDLARRDEDGYFYIVDRKKDMIIVGGYN 422
Cdd:cd05969 269 VKAAVVDENGNELPPGTKGILALKPgwPSMFRGIWNDEERYKNSFIDGWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHR 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 423 VYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVVPKR----SGVTEEDIMQHCETHLAKYKRPAAITFLDDIPKNA 498
Cdd:cd05969 349 VGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEgfepSDELKEEIINFVRQKLGAHVAPREIEFVDNLPKTR 428
|
490
....*....|
gi 1816047872 499 TGKMLRRALR 508
Cdd:cd05969 429 SGKIMRRVLK 438
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
5-509 |
2.52e-80 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 260.26 E-value: 2.52e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 5 SKLEETASEKPDSIACRFKDHMMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPL 84
Cdd:PRK08162 22 SFLERAAEVYPDRPAVIHGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 85 YTPTEIGYMLTNGDVKAIVGVSQLLPLyecMHESL-----PKVeLVI---LCQTGEAEP------EAA----DPEvrmkm 146
Cdd:PRK08162 102 LDAASIAFMLRHGEAKVLIVDTEFAEV---AREALallpgPKP-LVIdvdDPEYPGGRFigaldyEAFlasgDPD----- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 147 ttFAKILrptsaakqnqelvPDDT--AVIL-YTSGTTGKPKGAMLTHQNLYSNA--NDVAGylGMDERDNVVCALPMFHV 221
Cdd:PRK08162 173 --FAWTL-------------PADEwdAIALnYTSGTTGNPKGVVYHHRGAYLNAlsNILAW--GMPKHPVYLWTLPMFHC 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 222 ----FCLTVCMNAplmsGATVLIEpQFSPASVFKLVKQQQVTIFAGVPTMYNYLFqheNGKKDDFSSIRLCISG---GAA 294
Cdd:PRK08162 236 ngwcFPWTVAARA----GTNVCLR-KVDPKLIFDLIREHGVTHYCGAPIVLSALI---NAPAEWRAGIDHPVHAmvaGAA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 295 MPVALLTAFEEkFGVTILEGYGLSEA-SPVT-C--------FNPFDRGRKPGSIGTSILHVEN-KVVDP-LGRELPA--H 360
Cdd:PRK08162 308 PPAAVIAKMEE-IGFDLTHVYGLTETyGPATvCawqpewdaLPLDERAQLKARQGVRYPLQEGvTVLDPdTMQPVPAdgE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 361 QVGELIVKGPNVMKGYYKMPMETEHALKDGWLYTGDLARRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKE 440
Cdd:PRK08162 387 TIGEIMFRGNIVMKGYLKNPKATEEAFAGGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLV 466
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 441 AVVVGVPDPQSGEAVKGYVVPKR-SGVTEEDIMQHCETHLAKYKRPAAITFlDDIPKNATGKMLRRALRD 509
Cdd:PRK08162 467 AAVVAKPDPKWGEVPCAFVELKDgASATEEEIIAHCREHLAGFKVPKAVVF-GELPKTSTGKIQKFVLRE 535
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
28-509 |
3.49e-80 |
|
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: 256.98 E-value: 3.49e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 28 TYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYTPTEIGYMLTNGDVKAIVgvsq 107
Cdd:cd05971 8 TFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALV---- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 108 llplyecmheslpkvelvilcqTGEAepeaadpevrmkmttfakilrptsaakqnqelvpDDTAVILYTSGTTGKPKGAM 187
Cdd:cd05971 84 ----------------------TDGS----------------------------------DDPALIIYTSGTTGPPKGAL 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 188 LTHQNLYSNANDVAGYLGMDERDNVVCALP--------MFHVFCltvcmnAPLMSGATVLIE--PQFSPASVFKLVKQQQ 257
Cdd:cd05971 108 HAHRVLLGHLPGVQFPFNLFPRDGDLYWTPadwawiggLLDVLL------PSLYFGVPVLAHrmTKFDPKAALDLMSRYG 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 258 VTIFAGVPTMYNYLFQHENGKKDDFSSIRLCISGGAAMPVALLTAFEEKFGVTILEGYGLSEASPVT--CFNPFDRgrKP 335
Cdd:cd05971 182 VTTAFLPPTALKMMRQQGEQLKHAQVKLRAIATGGESLGEELLGWAREQFGVEVNEFYGQTECNLVIgnCSALFPI--KP 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 336 GSIGTSILHVENKVVDPLGRELPAHQVGELIVKGPN--VMKGYYKMPMETEHALKDGWLYTGDLARRDEDGYFYIVDRKK 413
Cdd:cd05971 260 GSMGKPIPGHRVAIVDDNGTPLPPGEVGEIAVELPDpvAFLGYWNNPSATEKKMAGDWLLTGDLGRKDSDGYFWYVGRDD 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 414 DMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVVPKRSGVTEE----DIMQHCETHLAKYKRPAAIT 489
Cdd:cd05971 340 DVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGETPSDalarEIQELVKTRLAAHEYPREIE 419
|
490 500
....*....|....*....|
gi 1816047872 490 FLDDIPKNATGKMLRRALRD 509
Cdd:cd05971 420 FVNELPRTATGKIRRRELRA 439
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
24-509 |
8.81e-80 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 258.09 E-value: 8.81e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 24 DHMMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYTPTEIGYMLTNGDVKAIV 103
Cdd:PRK12406 9 DRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 104 GVSQLLplyECMHESLPKVELVILCQT------------GEAEPEAADPEVRMKMTTFAKILRPTSAAKQNqelvpddta 171
Cdd:PRK12406 89 AHADLL---HGLASALPAGVTVLSVPTppeiaaayrispALLTPPAGAIDWEGWLAQQEPYDGPPVPQPQS--------- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 172 vILYTSGTTGKPKG---AMLTHQNLYSNANDVAGYLGMDERDNVVCALPMFHvfcltvcmNAP----LMS---GATVLIE 241
Cdd:PRK12406 157 -MIYTSGTTGHPKGvrrAAPTPEQAAAAEQMRALIYGLKPGIRALLTGPLYH--------SAPnaygLRAgrlGGVLVLQ 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 242 PQFSPASVFKLVKQQQVTIFAGVPTMYNYLFQ--HENGKKDDFSSIRLCISGGAAMPVALLTAFEEKFGVTILEGYGLSE 319
Cdd:PRK12406 228 PRFDPEELLQLIERHRITHMHMVPTMFIRLLKlpEEVRAKYDVSSLRHVIHAAAPCPADVKRAMIEWWGPVIYEYYGSTE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 320 ASPVTCFNPFDRGRKPGSIGTSILHVENKVVDPLGRELPAHQVGELIVKGP-NVMKGYYKMPMETEHALKDGWLYTGDLA 398
Cdd:PRK12406 308 SGAVTFATSEDALSHPGTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAgNPDFTYHNKPEKRAEIDRGGFITSGDVG 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 399 RRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVVPKrSGVT--EEDIMQHCE 476
Cdd:PRK12406 388 YLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQ-PGATldEADIRAQLK 466
|
490 500 510
....*....|....*....|....*....|...
gi 1816047872 477 THLAKYKRPAAITFLDDIPKNATGKMLRRALRD 509
Cdd:PRK12406 467 ARLAGYKVPKHIEIMAELPREDSGKIFKRRLRD 499
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
11-508 |
1.76e-79 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 259.06 E-value: 1.76e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 11 ASEKPDSIACRFKD----HMMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYT 86
Cdd:PRK04319 54 DGGRKDKVALRYLDasrkEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFM 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 87 PTEIGYMLTNGDVKAIVGVSQLLPlyECMHESLPKVELVILC-QTGEAEPEAADpevrmkmttFAKILRPTSAAKQNQEL 165
Cdd:PRK04319 134 EEAVRDRLEDSEAKVLITTPALLE--RKPADDLPSLKHVLLVgEDVEEGPGTLD---------FNALMEQASDEFDIEWT 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 166 VPDDTAVILYTSGTTGKPKGAMLTHQNLYsnANDVAGYLGMDERDNVV--C-ALP------MFHVFcltvcmnAPLMSGA 236
Cdd:PRK04319 203 DREDGAILHYTSGSTGKPKGVLHVHNAML--QHYQTGKYVLDLHEDDVywCtADPgwvtgtSYGIF-------APWLNGA 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 237 TVLI-EPQFSPASVFKLVKQQQVTIFAGVPTMYNYLFQH--ENGKKDDFSSIRLCISGGAAM-PVALLTAfEEKFGVTIL 312
Cdd:PRK04319 274 TNVIdGGRFSPERWYRILEDYKVTVWYTAPTAIRMLMGAgdDLVKKYDLSSLRHILSVGEPLnPEVVRWG-MKVFGLPIH 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 313 EGYGLSEASPVTCFNPFDRGRKPGSIGTSILHVENKVVDPLGRELPAHQVGEL-IVKG-PNVMKGYYKMPMETEHALKDG 390
Cdd:PRK04319 353 DNWWMTETGGIMIANYPAMDIKPGSMGKPLPGIEAAIVDDQGNELPPNRMGNLaIKKGwPSMMRGIWNNPEKYESYFAGD 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 391 WLYTGDLARRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVVpKRSGV--TE 468
Cdd:PRK04319 433 WYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVA-LRPGYepSE 511
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1816047872 469 E---DIMQHCETHLAKYKRPAAITFLDDIPKNATGKMLRRALR 508
Cdd:PRK04319 512 ElkeEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKIMRRVLK 554
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
8-507 |
3.75e-79 |
|
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: 255.59 E-value: 3.75e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 8 EETASEKPDSIACRFKDHMMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYTP 87
Cdd:cd12117 4 EEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 88 TEIGYMLTNGDVKAIV---GVSQLLPLYECmheslpkveLVILCQTGEAEPEAADPEVrmkmttfakilrptsaakqnqe 164
Cdd:cd12117 84 ERLAFMLADAGAKVLLtdrSLAGRAGGLEV---------AVVIDEALDAGPAGNPAVP---------------------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 165 LVPDDTAVILYTSGTTGKPKGAMLTHQN---LYSNANdvagYLGMDERDNVVCALPM-FHVFCLTVCmnAPLMSGAT-VL 239
Cdd:cd12117 133 VSPDDLAYVMYTSGSTGRPKGVAVTHRGvvrLVKNTN----YVTLGPDDRVLQTSPLaFDASTFEIW--GALLNGARlVL 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 240 IEPQF--SPASVFKLVKQQQVTIFAGVPTMYNYLFQHEngkKDDFSSIRLCISGGAAMPVALLTAFEEKF-GVTILEGYG 316
Cdd:cd12117 207 APKGTllDPDALGALIAEEGVTVLWLTAALFNQLADED---PECFAGLRELLTGGEVVSPPHVRRVLAACpGLRLVNGYG 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 317 LSEASPVTCFNPFDRGRKPGS---IGTSILHVENKVVDPLGRELPAHQVGELIVKGPNVMKGYYKMPMET-----EHALK 388
Cdd:cd12117 284 PTENTTFTTSHVVTELDEVAGsipIGRPIANTRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTaerfvADPFG 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 389 DG-WLY-TGDLARRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVVPKRsGV 466
Cdd:cd12117 364 PGeRLYrTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVVAEG-AL 442
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1816047872 467 TEEDIMQHCETHLAKYKRPAAITFLDDIPKNATGKMLRRAL 507
Cdd:cd12117 443 DAAELRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
11-509 |
3.76e-79 |
|
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: 257.04 E-value: 3.76e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 11 ASEKPDSIACRFKD-----HMMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLY 85
Cdd:cd05970 27 AKEYPDKLALVWCDdageeRIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 86 TPTEIGYMLTNGDVKAIVGVSQ--LLPLYECMHESLPKVELVILCqtGEAEPEA---ADPEVrMKMTTFakILRPTSaak 160
Cdd:cd05970 107 TAKDIVYRIESADIKMIVAIAEdnIPEEIEKAAPECPSKPKLVWV--GDPVPEGwidFRKLI-KNASPD--FERPTA--- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 161 qNQELVPDDTAVILYTSGTTGKPKgaMLTHQNLYSNANDVAGYLGMDERDNVVcalpmfHvfcLTV-------CMNAPL- 232
Cdd:cd05970 179 -NSYPCGEDILLVYFSSGTTGMPK--MVEHDFTYPLGHIVTAKYWQNVREGGL------H---LTVadtgwgkAVWGKIy 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 233 ---MSGATVLI--EPQFSPASVFKLVKQQQVTIFAGVPTMYNYLFqHENGKKDDFSSIRLCISGGAAMPVALLTAFEEKF 307
Cdd:cd05970 247 gqwIAGAAVFVydYDKFDPKALLEKLSKYGVTTFCAPPTIYRFLI-REDLSRYDLSSLRYCTTAGEALNPEVFNTFKEKT 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 308 GVTILEGYGLSEASPVT----CFNPfdrgrKPGSIGTSILHVENKVVDPLGRELPAHQVGELIV---KGPNV--MKGYYK 378
Cdd:cd05970 326 GIKLMEGFGQTETTLTIatfpWMEP-----KPGSMGKPAPGYEIDLIDREGRSCEAGEEGEIVIrtsKGKPVglFGGYYK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 379 MPMETEHALKDGWLYTGDLARRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGY 458
Cdd:cd05970 401 DAEKTAEVWHDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKAT 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1816047872 459 VVPKR----SGVTEEDIMQHCETHLAKYKRPAAITFLDDIPKNATGKMLRRALRD 509
Cdd:cd05970 481 IVLAKgyepSEELKKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEIRE 535
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
28-443 |
3.59e-78 |
|
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: 250.65 E-value: 3.59e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 28 TYQELNEHIQRFADGLQEA-GMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYtPTE-IGYMLTNGDVKAIVGV 105
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAY-PAErLAFILEDAGARLLLTD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 106 SQLLPLYECMhesLPKVELVILCQTGEAEPEAADPEVRMKMttfakilrptsaakqnqelVPDDTAVILYTSGTTGKPKG 185
Cdd:TIGR01733 80 SALASRLAGL---VLPVILLDPLELAALDDAPAPPPPDAPS-------------------GPDDLAYVIYTSGSTGRPKG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 186 AMLTHQNLYSNANDVAGYLGMDERDNVVCALPmfHVFCLTVC-MNAPLMSGATVLI----EPQFSPASVFKLVKQQQVTI 260
Cdd:TIGR01733 138 VVVTHRSLVNLLAWLARRYGLDPDDRVLQFAS--LSFDASVEeIFGALLAGATLVVppedEERDDAALLAALIAEHPVTV 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 261 FAGVPTMYNYLFQHENGkkdDFSSIRLCISGGAAMPVALLTAFEEKFG-VTILEGYGLSEASPVTCFNPFD----RGRKP 335
Cdd:TIGR01733 216 LNLTPSLLALLAAALPP---ALASLRLVILGGEALTPALVDRWRARGPgARLINLYGPTETTVWSTATLVDpddaPRESP 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 336 GSIGTSILHVENKVVDPLGRELPAHQVGELIVKGPNVMKGYYKMPMETE-------HALKDG-WLY-TGDLARRDEDGYF 406
Cdd:TIGR01733 293 VPIGRPLANTRLYVLDDDLRPVPVGVVGELYIGGPGVARGYLNRPELTAerfvpdpFAGGDGaRLYrTGDLVRYLPDGNL 372
|
410 420 430
....*....|....*....|....*....|....*..
gi 1816047872 407 YIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVV 443
Cdd:TIGR01733 373 EFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
7-501 |
7.16e-78 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 253.65 E-value: 7.16e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 7 LEETASEKPDSIACRFKDHMMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYT 86
Cdd:PRK07798 9 FEAVADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 87 PTEIGYMLTNGDVKAIVGVSQLLPLYECMHESLPKVELVILCQTGEAEPEAADPEvrmkmtTFAKILRPTSAAKQNQELV 166
Cdd:PRK07798 89 EDELRYLLDDSDAVALVYEREFAPRVAEVLPRLPKLRTLVVVEDGSGNDLLPGAV------DYEDALAAGSPERDFGERS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 167 PDDTaVILYTSGTTGKPKGAMLTHQNLY-SNANDVAGYLG---MDERDNVV-----------CALPMFHVFCLTVCMNAp 231
Cdd:PRK07798 163 PDDL-YLLYTGGTTGMPKGVMWRQEDIFrVLLGGRDFATGepiEDEEELAKraaagpgmrrfPAPPLMHGAGQWAAFAA- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 232 LMSGATVLIEPQ--FSPASVFKLVKQQQVTIFAGV-PTMYNYLFQH-ENGKKDDFSSIRLCISGGAAMPVALLTAFEEKF 307
Cdd:PRK07798 241 LFSGQTVVLLPDvrFDADEVWRTIEREKVNVITIVgDAMARPLLDAlEARGPYDLSSLFAIASGGALFSPSVKEALLELL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 308 -GVTILEGYGLSEaspvTCFNPFDRgRKPGSIGTSILHVE----NKVVDPLGREL-PAHQVGELIVKGPNVMKGYYKMPM 381
Cdd:PRK07798 321 pNVVLTDSIGSSE----TGFGGSGT-VAKGAVHTGGPRFTigprTVVLDEDGNPVePGSGEIGWIARRGHIPLGYYKDPE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 382 ETEHALK--DG--WLYTGDLARRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKG 457
Cdd:PRK07798 396 KTAETFPtiDGvrYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVPDERWGQEVVA 475
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1816047872 458 yVVPKRSGV--TEEDIMQHCETHLAKYKRPAAITFLDDIPKNATGK 501
Cdd:PRK07798 476 -VVQLREGArpDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
26-509 |
7.27e-78 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 253.91 E-value: 7.27e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 26 MMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYTPTEIGYMLTNGDVKAIVGV 105
Cdd:PRK13382 68 TLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPALAEVVTREGVDTVIYD 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 106 SQLLPLYECMHESLPKVELVilcqtgEAEPEAADPEVRMKMTTFAKILRPTSAAKQNQelvpddtaVILYTSGTTGKPKG 185
Cdd:PRK13382 148 EEFSATVDRALADCPQATRI------VAWTDEDHDLTVEVLIAAHAGQRPEPTGRKGR--------VILLTSGTTGTPKG 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 186 AMLTHQNLYSNANDVAGYLGMDERDNVVCALPMFHVFCLTVCMNAPLMSgATVLIEPQFSPASVFKLVKQQQVTIFAGVP 265
Cdd:PRK13382 214 ARRSGPGGIGTLKAILDRTPWRAEEPTVIVAPMFHAWGFSQLVLAASLA-CTIVTRRRFDPEATLDLIDRHRATGLAVVP 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 266 TMYNYLFQ--HENGKKDDFSSIRLCISGGAAMPVALLTAFEEKFGVTILEGYGLSEASPVTCFNPFDRGRKPGSIGTSIL 343
Cdd:PRK13382 293 VMFDRIMDlpAEVRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFGDVIYNNYNATEAGMIATATPADLRAAPDTAGRPAE 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 344 HVENKVVDPLGRELPAHQVGELIVKGPNVMKGYYKMPMETEHalkDGWLYTGDLARRDEDGYFYIVDRKKDMIIVGGYNV 423
Cdd:PRK13382 373 GTEIRILDQDFREVPTGEVGTIFVRNDTQFDGYTSGSTKDFH---DGFMASGDVGYLDENGRLFVVGRDDEMIVSGGENV 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 424 YPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVVPK-RSGVTEEDIMQHCETHLAKYKRPAAITFLDDIPKNATGKM 502
Cdd:PRK13382 450 YPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKpGASATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKI 529
|
....*..
gi 1816047872 503 LRRALRD 509
Cdd:PRK13382 530 LRRELQA 536
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
25-509 |
1.29e-77 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 253.14 E-value: 1.29e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 25 HMMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYTPTEIGYMLTNGDVKAIVG 104
Cdd:PRK06018 38 VRTTYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVIT 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 105 VSQLLPLYECMHESLPKVELVILCQTGEAEPEAADPevrmKMTTFAKILRPTSAAKQNQELVPDDTAVILYTSGTTGKPK 184
Cdd:PRK06018 118 DLTFVPILEKIADKLPSVERYVVLTDAAHMPQTTLK----NAVAYEEWIAEADGDFAWKTFDENTAAGMCYTSGTTGDPK 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 185 GAMLTHQN--LYSNANDVAGYLGMDERDNVVCALPMFHVFCLTVCMNAPLMSGATVLIEPQFSPASVFKLVKQQQVTIFA 262
Cdd:PRK06018 194 GVLYSHRSnvLHALMANNGDALGTSAADTMLPVVPLFHANSWGIAFSAPSMGTKLVMPGAKLDGASVYELLDTEKVTFTA 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 263 GVPTMYNYLFQHENGKKDDFSSIRLCISGGAAMPVALLTAFEEkFGVTILEGYGLSEASPV----TCFNPFDRGRKPGSI 338
Cdd:PRK06018 274 GVPTVWLMLLQYMEKEGLKLPHLKMVVCGGSAMPRSMIKAFED-MGVEVRHAWGMTEMSPLgtlaALKPPFSKLPGDARL 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 339 ------GTSILHVENKVVDPLGRELP--AHQVGELIVKGPNVMKGYYKmpMETEHALKDGWLYTGDLARRDEDGYFYIVD 410
Cdd:PRK06018 353 dvlqkqGYPPFGVEMKITDDAGKELPwdGKTFGRLKVRGPAVAAAYYR--VDGEILDDDGFFDTGDVATIDAYGYMRITD 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 411 RKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVVPKR-SGVTEEDIMQHCETHLAKYKRPAAIT 489
Cdd:PRK06018 431 RSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQLKPgETATREEILKYMDGKIAKWWMPDDVA 510
|
490 500
....*....|....*....|
gi 1816047872 490 FLDDIPKNATGKMLRRALRD 509
Cdd:PRK06018 511 FVDAIPHTATGKILKTALRE 530
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
28-509 |
6.17e-77 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 250.76 E-value: 6.17e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 28 TYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYTPTEIGYMLTNGDVKAIVGVSQ 107
Cdd:PRK13391 26 TYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAAYIVDDSGARALITSAA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 108 LLPLYECMHESLPKVEL-VILCQTGEAEPeaadpevrmkMTTFAKILRPTSAAKQNQELVPDDtavILYTSGTTGKPKG- 185
Cdd:PRK13391 106 KLDVARALLKQCPGVRHrLVLDGDGELEG----------FVGYAEAVAGLPATPIADESLGTD---MLYSSGTTGRPKGi 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 186 -AMLTHQNLySNANDVAGYL----GMDERDNVVCALPMFHVFCLTVCMNAPLMSGATVLIEpQFSPASVFKLVKQQQVTI 260
Cdd:PRK13391 173 kRPLPEQPP-DTPLPLTAFLqrlwGFRSDMVYLSPAPLYHSAPQRAVMLVIRLGGTVIVME-HFDAEQYLALIEEYGVTH 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 261 FAGVPTMYNYLFQ--HENGKKDDFSSIRLCISGGAAMPVALLTAFEEKFGVTILEGYGLSEASPVTCFNPFDRGRKPGSI 338
Cdd:PRK13391 251 TQLVPTMFSRMLKlpEEVRDKYDLSSLEVAIHAAAPCPPQVKEQMIDWWGPIIHEYYAATEGLGFTACDSEEWLAHPGTV 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 339 GTSI---LHVenkvVDPLGRELPAHQVGELIVKGPNVMKgYYKMPMETEHALKD--GWLYTGDLARRDEDGYFYIVDRKK 413
Cdd:PRK13391 331 GRAMfgdLHI----LDDDGAELPPGEPGTIWFEGGRPFE-YLNDPAKTAEARHPdgTWSTVGDIGYVDEDGYLYLTDRAA 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 414 DMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVVPKRSGVTEEDIMQ----HCETHLAKYKRPAAIT 489
Cdd:PRK13391 406 FMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPVDGVDPGPALAAeliaFCRQRLSRQKCPRSID 485
|
490 500
....*....|....*....|
gi 1816047872 490 FLDDIPKNATGKMLRRALRD 509
Cdd:PRK13391 486 FEDELPRLPTGKLYKRLLRD 505
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
27-511 |
2.90e-75 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 247.45 E-value: 2.90e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 27 MTYQELNEHIQRFADGL-QEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYTPTEIGymltngdvKAIVGV 105
Cdd:PLN02574 67 ISYSELQPLVKSMAAGLyHVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIK--------KRVVDC 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 106 SQLLPLYECMH-ESLPKVEL-VILCqtgeaePEAAD-PEVRMKMTTFAKILRPTSAAKQNQELVPDDTAVILYTSGTTGK 182
Cdd:PLN02574 139 SVGLAFTSPENvEKLSPLGVpVIGV------PENYDfDSKRIEFPKFYELIKEDFDFVPKPVIKQDDVAAIMYSSGTTGA 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 183 PKGAMLTHQNLYSNANDV----AGYLGMDERDNV-VCALPMFHVFCLTVCMNAPLMSGATVLIEPQFSPASVFKLVKQQQ 257
Cdd:PLN02574 213 SKGVVLTHRNLIAMVELFvrfeASQYEYPGSDNVyLAALPMFHIYGLSLFVVGLLSLGSTIVVMRRFDASDMVKVIDRFK 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 258 VTIFAGVPTMYNYLFQHENGK-KDDFSSIRLCISGGAAMPVALLTAFEEKFG-VTILEGYGLSEASPVTC--FNPfDRGR 333
Cdd:PLN02574 293 VTHFPVVPPILMALTKKAKGVcGEVLKSLKQVSCGAAPLSGKFIQDFVQTLPhVDFIQGYGMTESTAVGTrgFNT-EKLS 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 334 KPGSIGTSILHVENKVVD-PLGRELPAHQVGELIVKGPNVMKGYYKMPMETE-HALKDGWLYTGDLARRDEDGYFYIVDR 411
Cdd:PLN02574 372 KYSSVGLLAPNMQAKVVDwSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQsTIDKDGWLRTGDIAYFDEDGYLYIVDR 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 412 KKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVVPKR-SGVTEEDIMQHCETHLAKYKRPAAITF 490
Cdd:PLN02574 452 LKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQgSTLSQEAVINYVAKQVAPYKKVRKVVF 531
|
490 500
....*....|....*....|.
gi 1816047872 491 LDDIPKNATGKMLRRALRDIL 511
Cdd:PLN02574 532 VQSIPKSPAGKILRRELKRSL 552
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
28-509 |
5.31e-73 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 241.42 E-value: 5.31e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 28 TYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYTPTEIGYMLTNGDVKAIVgvsq 107
Cdd:PLN02330 57 TYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIV---- 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 108 llpLYECMHESLPKVELVILCqTGEAEPEAAdpevrMKMTTFAKILRPTSAAKQNQELVPDDTAVILYTSGTTGKPKGAM 187
Cdd:PLN02330 133 ---TNDTNYGKVKGLGLPVIV-LGEEKIEGA-----VNWKELLEAADRAGDTSDNEEILQTDLCALPFSSGTTGISKGVM 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 188 LTHQNLYSNANDVAGYLGMDERDNVVCA--LPMFHVFCLTVCMNAPLMSGATVLIEPQFSPASVFKLVKQQQVTIFAGVP 265
Cdd:PLN02330 204 LTHRNLVANLCSSLFSVGPEMIGQVVTLglIPFFHIYGITGICCATLRNKGKVVVMSRFELRTFLNALITQEVSFAPIVP 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 266 TMYNYLFQHENGKKDDFSSIRLCISGGAAMPVA--LLTAFEEKF-GVTILEGYGLSEASPVTCF--NPfDRGR---KPGS 337
Cdd:PLN02330 284 PIILNLVKNPIVEEFDLSKLKLQAIMTAAAPLApeLLTAFEAKFpGVQVQEAYGLTEHSCITLThgDP-EKGHgiaKKNS 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 338 IGTSILHVENKVVDP-LGRELPAHQVGELIVKGPNVMKGYYKMPMETEHAL-KDGWLYTGDLARRDEDGYFYIVDRKKDM 415
Cdd:PLN02330 363 VGFILPNLEVKFIDPdTGRSLPKNTPGELCVRSQCVMQGYYNNKEETDRTIdEDGWLHTGDIGYIDDDGDIFIVDRIKEL 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 416 IIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVV-PKRSGVTEEDIMQHCETHLAKYKRPAAITFLDDI 494
Cdd:PLN02330 443 IKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVViNPKAKESEEDILNFVAANVAHYKKVRVVQFVDSI 522
|
490
....*....|....*
gi 1816047872 495 PKNATGKMLRRALRD 509
Cdd:PLN02330 523 PKSLSGKIMRRLLKE 537
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
9-508 |
5.39e-73 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 239.91 E-value: 5.39e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 9 ETASEKPDSIACRFKDHMmTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYTPT 88
Cdd:PRK13390 8 QIAPDRPAVIVAETGEQV-SYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 89 EIGYMLTNGDVKAIVGVSQLlplyecmheslpkvelvilcqTGEAEPEAADPEVRM----KMTTFAKILRPTSAAKQNQE 164
Cdd:PRK13390 87 EADYIVGDSGARVLVASAAL---------------------DGLAAKVGADLPLRLsfggEIDGFGSFEAALAGAGPRLT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 165 LVPDDtAVILYTSGTTGKPKGAM--LTHQNLYSNANDVA----GYLGMDERDNVVCALPMFHVFCLTVCMNAPLMsGATV 238
Cdd:PRK13390 146 EQPCG-AVMLYSSGTTGFPKGIQpdLPGRDVDAPGDPIVaiarAFYDISESDIYYSSAPIYHAAPLRWCSMVHAL-GGTV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 239 LIEPQFSPASVFKLVKQQQVTIFAGVPTMYNYLFQ--HENGKKDDFSSIRLCISGGAAMPVALLTAFEEKFGVTILEGYG 316
Cdd:PRK13390 224 VLAKRFDAQATLGHVERYRITVTQMVPTMFVRLLKldADVRTRYDVSSLRAVIHAAAPCPVDVKHAMIDWLGPIVYEYYS 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 317 LSEASPVTCFNPFDRGRKPGSIGTSILHVENkVVDPLGRELPAHQVGELIVKGPNVMKGYYKMPMET---EHALKDGWLY 393
Cdd:PRK13390 304 STEAHGMTFIDSPDWLAHPGSVGRSVLGDLH-ICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKTaaaQHPAHPFWTT 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 394 TGDLARRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGyVVPKRSGV--TEE-- 469
Cdd:PRK13390 383 VGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKA-VIQLVEGIrgSDEla 461
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1816047872 470 -DIMQHCETHLAKYKRPAAITFLDDIPKNATGKMLRRALR 508
Cdd:PRK13390 462 rELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
1-511 |
1.12e-72 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 238.91 E-value: 1.12e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 1 MNLVSKLEETASEKPDSIACRFKDHMMTYQELNEHIQRFADGLQE-AGMEKgdHLALLLGNSPDFIIAFFGALKAGIVVV 79
Cdd:PRK07638 1 MGITKEYKKHASLQPNKIAIKENDRVLTYKDWFESVCKVANWLNEkESKNK--TIAILLENRIEFLQLFAGAAMAGWTCV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 80 PINPLYTPTEIGYMLTNGDVKAIVGVSQLLPLYECmhESLPKVELvilcqtgeaepeaadPEVRMKMTTFAkilrPTSAA 159
Cdd:PRK07638 79 PLDIKWKQDELKERLAISNADMIVTERYKLNDLPD--EEGRVIEI---------------DEWKRMIEKYL----PTYAP 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 160 KQNQELVPDDTAvilYTSGTTGKPKGAMLTHQNLYSNANDVAGYLGMDERDNVVCALPMFHVFCLTVCMNApLMSGATVL 239
Cdd:PRK07638 138 IENVQNAPFYMG---FTSGSTGKPKAFLRAQQSWLHSFDCNVHDFHMKREDSVLIAGTLVHSLFLYGAIST-LYVGQTVH 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 240 IEPQFSPASVFKLVKQQQVTIFAGVPTMYNYLFQhENGKKDDFSSIrlcISGGAAMPVALLTAFEEKF-GVTILEGYGLS 318
Cdd:PRK07638 214 LMRKFIPNQVLDKLETENISVMYTVPTMLESLYK-ENRVIENKMKI---ISSGAKWEAEAKEKIKNIFpYAKLYEFYGAS 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 319 EASPVTCFNPFDRGRKPGSIGTSILHVENKVVDPLGRELPAHQVGELIVKGPNVMKGYYKMPMETEHALKDGWLYTGDLA 398
Cdd:PRK07638 290 ELSFVTALVDEESERRPNSVGRPFHNVQVRICNEAGEEVQKGEIGTVYVKSPQFFMGYIIGGVLARELNADGWMTVRDVG 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 399 RRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVvpkRSGVTEEDIMQHCETH 478
Cdd:PRK07638 370 YEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAII---KGSATKQQLKSFCLQR 446
|
490 500 510
....*....|....*....|....*....|...
gi 1816047872 479 LAKYKRPAAITFLDDIPKNATGKMLRRALRDIL 511
Cdd:PRK07638 447 LSSFKIPKEWHFVDEIPYTNSGKIARMEAKSWI 479
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
33-509 |
1.63e-72 |
|
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: 238.05 E-value: 1.63e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 33 NEHIQRFADGLQEAGmekgDHLALLLGNSPDFIIAFFGALKAGIVvvPINPLYTPTEIGYMLTNGDVKAIVGVSQLLPLY 112
Cdd:cd05929 8 RAQVFHQRRLLLLDV----YSIALNRNARAAAAEGVWIADGVYIY--LINSILTVFAAAAAWKCGACPAYKSSRAPRAEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 113 ECMHESLPKVELVILcqtgeaepeAADPEVRMKMTTFAKilrptSAAKQNQELVPDDTA--VILYTSGTTGKPKGAMlth 190
Cdd:cd05929 82 CAIIEIKAAALVCGL---------FTGGGALDGLEDYEA-----AEGGSPETPIEDEAAgwKMLYSGGTTGRPKGIK--- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 191 QNLYSNANDV------AGYLGMDERDNVVCALPMFHVFCLTVCMNAPLMsGATVLIEPQFSPASVFKLVKQQQVTIFAGV 264
Cdd:cd05929 145 RGLPGGPPDNdtlmaaALGFGPGADSVYLSPAPLYHAAPFRWSMTALFM-GGTLVLMEKFDPEEFLRLIERYRVTFAQFV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 265 PTMYNYLFQ--HENGKKDDFSSIRLCISGGAAMPVALLTAFEEKFGVTILEGYGLSEASPVTCFNPFDRGRKPGSIGTSI 342
Cdd:cd05929 224 PTMFVRLLKlpEAVRNAYDLSSLKRVIHAAAPCPPWVKEQWIDWGGPIIWEYYGGTEGQGLTIINGEEWLTHPGSVGRAV 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 343 LHvENKVVDPLGRELPAHQVGELIVKGPNVmKGYYKMPMETEHAL-KDGWLYTGDLARRDEDGYFYIVDRKKDMIIVGGY 421
Cdd:cd05929 304 LG-KVHILDEDGNEVPPGEIGEVYFANGPG-FEYTNDPEKTAAARnEGGWSTLGDVGYLDEDGYLYLTDRRSDMIISGGV 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 422 NVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVVPKRSGVT----EEDIMQHCETHLAKYKRPAAITFLDDIPKN 497
Cdd:cd05929 382 NIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVQPAPGADAgtalAEELIAFLRDRLSRYKCPRSIEFVAELPRD 461
|
490
....*....|..
gi 1816047872 498 ATGKMLRRALRD 509
Cdd:cd05929 462 DTGKLYRRLLRD 473
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
7-513 |
2.48e-72 |
|
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: 250.16 E-value: 2.48e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 7 LEETASEKPDSIACRFKDHMMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYt 86
Cdd:COG1020 482 FEAQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAY- 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 87 PTE-IGYMLTNGDVKAIVGVSQLLplyecmhESLPKVELVILC--QTGEAEPEAADPEVrmkmttfakilrptsaakqnq 163
Cdd:COG1020 561 PAErLAYMLEDAGARLVLTQSALA-------ARLPELGVPVLAldALALAAEPATNPPV--------------------- 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 164 ELVPDDTAVILYTSGTTGKPKGAMLTHQNLYSNANDVAGYLGMDERDNVVcalpMFHVFC--LTVC-MNAPLMSGAT-VL 239
Cdd:COG1020 613 PVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVL----QFASLSfdASVWeIFGALLSGATlVL 688
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 240 IEPQ--FSPASVFKLVKQQQVTIFAGVPTMYNYLFQHENgkkDDFSSIRLCISGGAAMPVALLTAFEEKF-GVTILEGYG 316
Cdd:COG1020 689 APPEarRDPAALAELLARHRVTVLNLTPSLLRALLDAAP---EALPSLRLVLVGGEALPPELVRRWRARLpGARLVNLYG 765
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 317 LSEASPVTCF---NPFDRGRKPGSIGTSILHVENKVVDPLGRELPAHQVGELIVKGPNVMKGYYKMPMETE-------HA 386
Cdd:COG1020 766 PTETTVDSTYyevTPPDADGGSVPIGRPIANTRVYVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAerfvadpFG 845
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 387 LKDGWLY-TGDLARRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVVPKRSG 465
Cdd:COG1020 846 FPGARLYrTGDLARWLPDGNLEFLGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGA 925
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1816047872 466 VTEEDIMQHCETHLAKYKRPAAITFLDDIPKNATGKMLRRALRDILPQ 513
Cdd:COG1020 926 AAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALPAPAA 973
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
3-507 |
3.09e-72 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 239.02 E-value: 3.09e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 3 LVSKLEETASEKPDSIACRFKDH--MMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVP 80
Cdd:PRK05852 18 IADLVEVAATRLPEAPALVVTADriAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 81 INPLYTPTEigymltNGDVKAIVGVSQLLPLYECMHESLP---KVELVILCQTGEAEPEAADPEVRMKMTTfakilRPTS 157
Cdd:PRK05852 98 LDPALPIAE------QRVRSQAAGARVVLIDADGPHDRAEpttRWWPLTVNVGGDSGPSGGTLSVHLDAAT-----EPTP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 158 AAKQNQELVPDDtAVILYTSGTTGKPKGAMLTHQNLYSNAND-VAGYlGMDERDNVVCALPMFHVFCLTVCMNAPLMSGA 236
Cdd:PRK05852 167 ATSTPEGLRPDD-AMIMFTGGTTGLPKMVPWTHANIASSVRAiITGY-RLSPRDATVAVMPLYHGHGLIAALLATLASGG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 237 TVLIEP--QFSPASVFKLVKQQQVTIFAGVPTMYNYLFQH--ENGKKDDFSSIRLCISGGAAMPVALLTAFEEKFGVTIL 312
Cdd:PRK05852 245 AVLLPArgRFSAHTFWDDIKAVGATWYTAVPTIHQILLERaaTEPSGRKPAALRFIRSCSAPLTAETAQALQTEFAAPVV 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 313 EGYGLSEAS---PVTCFNPFDRGRKP----GSIGTSIlHVENKVVDPLGRELPAHQVGELIVKGPNVMKGYYKMPMETEH 385
Cdd:PRK05852 325 CAFGMTEAThqvTTTQIEGIGQTENPvvstGLVGRST-GAQIRIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDPTITAA 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 386 ALKDGWLYTGDLARRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVVPKRSG 465
Cdd:PRK05852 404 NFTDGWLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIVPRESA 483
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1816047872 466 -VTEEDIMQHCETHLAKYKRPAAITFLDDIPKNATGKMLRRAL 507
Cdd:PRK05852 484 pPTAEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRRAV 526
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
7-507 |
5.66e-70 |
|
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: 231.78 E-value: 5.66e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 7 LEETASEKPDSIACRFKDHMMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYT 86
Cdd:cd17646 4 VAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 87 PTEIGYMLTNGDVKAIVGVSQLLPLYEcmheslPKVELVILCQTGEAEPEAADPEVrmkmttfakilrptsaakqnqELV 166
Cdd:cd17646 84 ADRLAYMLADAGPAVVLTTADLAARLP------AGGDVALLGDEALAAPPATPPLV---------------------PPR 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 167 PDDTAVILYTSGTTGKPKGAMLTHQNLysnANDVAGY-----LGMDERdnVVCALP------MFHVFcltvcmnAPLMSG 235
Cdd:cd17646 137 PDNLAYVIYTSGSTGRPKGVMVTHAGI---VNRLLWMqdeypLGPGDR--VLQKTPlsfdvsVWELF-------WPLVAG 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 236 AT-VLIEP--QFSPASVFKLVKQQQVTIFAGVPTMYNYLFqhENGKKDDFSSIRLCISGGAAMPVALLTAFEEKFGVTIL 312
Cdd:cd17646 205 ARlVVARPggHRDPAYLAALIREHGVTTCHFVPSMLRVFL--AEPAAGSCASLRRVFCSGEALPPELAARFLALPGAELH 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 313 EGYGLSEA----SPVTCFNPFDRGRKPgsIGTSILHVENKVVDPLGRELPAHQVGELIVKGPNVMKGYYKMPMETEHALK 388
Cdd:cd17646 283 NLYGPTEAaidvTHWPVRGPAETPSVP--IGRPVPNTRLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFV 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 389 DGW------LY-TGDLARRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVVP 461
Cdd:cd17646 361 PDPfgpgsrMYrTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVP 440
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1816047872 462 KR--SGVTEEDIMQHCETHLAKYKRPAAITFLDDIPKNATGKMLRRAL 507
Cdd:cd17646 441 AAgaAGPDTAALRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
50-510 |
9.54e-70 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 241.75 E-value: 9.54e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 50 KGDHLALLLGNSPDFIIAFFGALKAGIVVVPINplYTPTE--IGYMLTNGDVKAIVGVSQL---LPLYECMHESLPKVEL 124
Cdd:PRK08633 664 DEENVGILLPPSVAGALANLALLLAGKVPVNLN--YTASEaaLKSAIEQAQIKTVITSRKFlekLKNKGFDLELPENVKV 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 125 VILcqtgeaEPEAADPEVRMKMTTFAKI-LRPTS--AAKQNQELVPDDTAVILYTSGTTGKPKGAMLTHQNLYSNANDVA 201
Cdd:PRK08633 742 IYL------EDLKAKISKVDKLTALLAArLLPARllKRLYGPTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQIS 815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 202 GYLGMDERDNVVCALPMFHVFCLTVCMNAPLMSGATVLIEPqfSP---ASVFKLVKQQQVTIFAGVPTMYNYLFQHENGK 278
Cdd:PRK08633 816 DVFNLRNDDVILSSLPFFHSFGLTVTLWLPLLEGIKVVYHP--DPtdaLGIAKLVAKHRATILLGTPTFLRLYLRNKKLH 893
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 279 KDDFSSIRLCISGGAAMPVALLTAFEEKFGVTILEGYGLSEASPVTCFN---------PFDRGRKPGSIGTSILHVENKV 349
Cdd:PRK08633 894 PLMFASLRLVVAGAEKLKPEVADAFEEKFGIRILEGYGATETSPVASVNlpdvlaadfKRQTGSKEGSVGMPLPGVAVRI 973
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 350 VDPL-GRELPAHQVGELIVKGPNVMKGYYKMPMETEHALKD----GWLYTGDLARRDEDGYFYIVDRKKDMIIVGGYNVY 424
Cdd:PRK08633 974 VDPEtFEELPPGEDGLILIGGPQVMKGYLGDPEKTAEVIKDidgiGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVP 1053
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 425 PREVEE----VLYShpDVKEAVVVGVPDPQSGEAVkgYVVPKRSGVTEEDIMQHC-ETHLAKYKRPAAITFLDDIPKNAT 499
Cdd:PRK08633 1054 LGAVEEelakALGG--EEVVFAVTAVPDEKKGEKL--VVLHTCGAEDVEELKRAIkESGLPNLWKPSRYFKVEALPLLGS 1129
|
490
....*....|.
gi 1816047872 500 GKMLRRALRDI 510
Cdd:PRK08633 1130 GKLDLKGLKEL 1140
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
11-509 |
1.42e-69 |
|
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: 232.13 E-value: 1.42e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 11 ASEKPDSIACRF------KDHMMTYQELNEHIQRFADGLQEAGMEkGDHLALLLGNSPDFIIAFFGALKAGIVVVPinpL 84
Cdd:cd05931 3 AAARPDRPAYTFlddeggREETLTYAELDRRARAIAARLQAVGKP-GDRVLLLAPPGLDFVAAFLGCLYAGAIAVP---L 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 85 YTPTEIGYMltnGDVKAIV---GVSQLLplyeCMHESLPKVElvilcQTGEAEPEAADPEVRmkmttFAKILRPTSAAK- 160
Cdd:cd05931 79 PPPTPGRHA---ERLAAILadaGPRVVL----TTAAALAAVR-----AFAASRPAAGTPRLL-----VVDLLPDTSAADw 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 161 QNQELVPDDTAVILYTSGTTGKPKGAMLTHQNLYSNANDVAGYLGMDERDNVVCALPMFHVFCLTVCMNAPLMSGAT-VL 239
Cdd:cd05931 142 PPPSPDPDDIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGPsVL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 240 IEPQ-F--SPASVFKLVKQQQVTIfAGVPTM-YNYL---FQHENGKKDDFSSIRLCISGgaAMPV--ALLTAFEEKFG-- 308
Cdd:cd05931 222 MSPAaFlrRPLRWLRLISRYRATI-SAAPNFaYDLCvrrVRDEDLEGLDLSSWRVALNG--AEPVrpATLRRFAEAFApf 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 309 ----VTILEGYGLSEAspvTCF---------------------NPFDRGRKPG-------SIGTSILHVENKVVDP-LGR 355
Cdd:cd05931 299 gfrpEAFRPSYGLAEA---TLFvsggppgtgpvvlrvdrdalaGRAVAVAADDpaarelvSCGRPLPDQEVRIVDPeTGR 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 356 ELPAHQVGELIVKGPNVMKGYYKMPMETEHALK-------DGWLYTGDLARRDeDGYFYIVDRKKDMIIVGGYNVYPREV 428
Cdd:cd05931 376 ELPDGEVGEIWVRGPSVASGYWGRPEATAETFGalaatdeGGWLRTGDLGFLH-DGELYITGRLKDLIIVRGRNHYPQDI 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 429 E-EVLYSHPDVKE--AVVVGVPDPQSGEAVkgYVVPKRSGVTEED---IMQHCETHLAKYK--RPAAITFL--DDIPKNA 498
Cdd:cd05931 455 EaTAEEAHPALRPgcVAAFSVPDDGEERLV--VVAEVERGADPADlaaIAAAIRAAVAREHgvAPADVVLVrpGSIPRTS 532
|
570
....*....|.
gi 1816047872 499 TGKMLRRALRD 509
Cdd:cd05931 533 SGKIQRRACRA 543
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
169-500 |
2.98e-69 |
|
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: 224.87 E-value: 2.98e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 169 DTAVILYTSGTTGKPKGAMLTHQNLYSNANDVAGYLGMDERDNVVCALPMFHVFCLTVCMNAPLMSGATVLIePQFSPAS 248
Cdd:cd17636 1 DPVLAIYTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTVFLNSGPLFHIGTLMFTLATFHAGGTNVFV-RRVDAEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 249 VFKLVKQQQVTIFAGVPTMYNYLFQHENGKKDDFSSIRlcisGGAAMP--VALLTAFEEKFGVTiLEGYGLSEASPVTCF 326
Cdd:cd17636 80 VLELIEAERCTHAFLLPPTIDQIVELNADGLYDLSSLR----SSPAAPewNDMATVDTSPWGRK-PGGYGQTEVMGLATF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 327 NPFDRGRKPGSIGTSILhVENKVVDPLGRELPAHQVGELIVKGPNVMKGYYKMPMETEHALKDGWLYTGDLARRDEDGYF 406
Cdd:cd17636 155 AALGGGAIGGAGRPSPL-VQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRTRGGWHHTNDLGRREPDGSL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 407 YIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVVPKR-SGVTEEDIMQHCETHLAKYKRP 485
Cdd:cd17636 234 SFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPgASVTEAELIEHCRARIASYKKP 313
|
330
....*....|....*
gi 1816047872 486 AAITFLDDIPKNATG 500
Cdd:cd17636 314 KSVEFADALPRTAGG 328
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
15-507 |
4.14e-69 |
|
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: 228.71 E-value: 4.14e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 15 PDSIACRFKDHMMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYTPTEIGYML 94
Cdd:cd12116 1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 95 tnGDVKAIvgvsqllplyecmheslpkvelVILCQTGEAEPEAADPevrmkMTTFAKILRPTSAAKQNQELV-PDDTAVI 173
Cdd:cd12116 81 --EDAEPA----------------------LVLTDDALPDRLPAGL-----PVLLLALAAAAAAPAAPRTPVsPDDLAYV 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 174 LYTSGTTGKPKGAMLTHQNLYSNANDVAGYLGMDERDNVVcAL--PMFHVFCLTVCMnaPLMSGATVLIEP---QFSPAS 248
Cdd:cd12116 132 IYTSGSTGRPKGVVVSHRNLVNFLHSMRERLGLGPGDRLL-AVttYAFDISLLELLL--PLLAGARVVIAPretQRDPEA 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 249 VFKLVKQQQVTIFAGVPTMYNYLFQHENGKKDDFSSirLCisGGAAMPVALLTAFEEKFG-VTILegYGLSEASPVTCFN 327
Cdd:cd12116 209 LARLIEAHSITVMQATPATWRMLLDAGWQGRAGLTA--LC--GGEALPPDLAARLLSRVGsLWNL--YGPTETTIWSTAA 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 328 PFDRGRKPGSIGTSILHVENKVVDPLGRELPAHQVGELIVKGPNVMKGYYKMPMETE-------HALKDGWLY-TGDLAR 399
Cdd:cd12116 283 RVTAAAGPIPIGRPLANTQVYVLDAALRPVPPGVPGELYIGGDGVAQGYLGRPALTAerfvpdpFAGPGSRLYrTGDLVR 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 400 RDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVkGYVVPK-RSGVTEEDIMQHCETH 478
Cdd:cd12116 363 RRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGGDRRLV-AYVVLKaGAAPDAAALRAHLRAT 441
|
490 500
....*....|....*....|....*....
gi 1816047872 479 LAKYKRPAAITFLDDIPKNATGKMLRRAL 507
Cdd:cd12116 442 LPAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
1-509 |
1.16e-67 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 226.93 E-value: 1.16e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 1 MNLVSKLEETASEKPDSIACRFKDHMMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVP 80
Cdd:PRK06164 10 DTLASLLDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 81 INPLYTPTEIGYMLTNGDVKAIV------GVSQLLPLYECMHESLPKVELVILcqTGEAEPEAADPEVRMKMTTFAKILR 154
Cdd:PRK06164 90 VNTRYRSHEVAHILGRGRARWLVvwpgfkGIDFAAILAAVPPDALPPLRAIAV--VDDAADATPAPAPGARVQLFALPDP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 155 PTSAAKQNQELVPDDTAVILYTSGTTGKPKGAMLTHQNLYSNANDVAGYLGMDERDNVVCALPMFHVFCLTVCMNApLMS 234
Cdd:PRK06164 168 APPAAAGERAADPDAGALLFTTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFGFSTLLGA-LAG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 235 GATVLIEPQFSPASVFKLVKQQQVTIFAGVPTMYNYLFQhENGKKDDFSSIRLCisGGAAMPVAL--LTAFEEKFGVTIL 312
Cdd:PRK06164 247 GAPLVCEPVFDAARTARALRRHRVTHTFGNDEMLRRILD-TAGERADFPSARLF--GFASFAPALgeLAALARARGVPLT 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 313 EGYGLSEASPVTCFNPFD---RGRKPGsiGTSILHVENKV--VDPL-GRELPAHQVGELIVKGPNVMKGYYKMPMETEHA 386
Cdd:PRK06164 324 GLYGSSEVQALVALQPATdpvSVRIEG--GGRPASPEARVraRDPQdGALLPDGESGEIEIRAPSLMRGYLDNPDATARA 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 387 LK-DGWLYTGDLARRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVkGYVVPKrSG 465
Cdd:PRK06164 402 LTdDGYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGATRDGKTVPV-AFVIPT-DG 479
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1816047872 466 VT--EEDIMQHCETHLAKYKRPAAITFLDDIPKNATG---KMLRRALRD 509
Cdd:PRK06164 480 ASpdEAGLMAACREALAGFKVPARVQVVEAFPVTESAngaKIQKHRLRE 528
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
169-511 |
4.67e-67 |
|
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: 219.12 E-value: 4.67e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 169 DTAVILYTSGTTGKPKGAMLTHQNLYSNANDVAGYLGMDERDNVVCALPMFHVFCLTVcMNAPLMSGATvLIEPQFSPAS 248
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLYHVGGLAI-LVRSLLAGAE-LVLLERNQAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 249 VFKLVkQQQVTIFAGVPTMYNYLFqHENGKKDDFSSIRLCISGGAAMPVALLTAFEEKfGVTILEGYGLSE-ASPVTCFN 327
Cdd:cd17630 79 AEDLA-PPGVTHVSLVPTQLQRLL-DSGQGPAALKSLRAVLLGGAPIPPELLERAADR-GIPLYTTYGMTEtASQVATKR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 328 PFDRGRkpGSIGTSILHVENKVVDPlgrelpahqvGELIVKGPNVMKGYYKMPMETEhALKDGWLYTGDLARRDEDGYFY 407
Cdd:cd17630 156 PDGFGR--GGVGVLLPGRELRIVED----------GEIWVGGASLAMGYLRGQLVPE-FNEDGWFTTKDLGELHADGRLT 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 408 IVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVVPkRSGVTEEDIMQHCETHLAKYKRPAA 487
Cdd:cd17630 223 VLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVG-RGPADPAELRAWLKDKLARFKLPKR 301
|
330 340
....*....|....*....|....
gi 1816047872 488 ITFLDDIPKNATGKMLRRALRDIL 511
Cdd:cd17630 302 IYPVPELPRTGGGKVDRRALRAWL 325
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
26-509 |
3.02e-66 |
|
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: 223.11 E-value: 3.02e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 26 MMTYQELNEHIQRFADGLQEA-GMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYTPTEIGYMLTNGDVKAIVG 104
Cdd:cd05928 41 KWSFRELGSLSRKAANVLSGAcGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 105 VSQLLPLYECMHESLPKVELVILcqtgeaepeaADPEVRMKMTTFAKILRPTSAAKQNQELVPDDTAVILYTSGTTGKPK 184
Cdd:cd05928 121 SDELAPEVDSVASECPSLKTKLL----------VSEKSRDGWLNFKELLNEASTEHHCVETGSQEPMAIYFTSGTTGSPK 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 185 GAMLTHQNLYSNANDVAGY-LGMDERDNVVCALPMFHVFCLTVCMNAPLMSGATVLIE--PQFSPASVFKLVKQQQVTIF 261
Cdd:cd05928 191 MAEHSHSSLGLGLKVNGRYwLDLTASDIMWNTSDTGWIKSAWSSLFEPWIQGACVFVHhlPRFDPLVILKTLSSYPITTF 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 262 AGVPTMYNYLFQhENGKKDDFSSIRLCISGGAAMPVALLTAFEEKFGVTILEGYGLSEASpVTCFNPFDRGRKPGSIGTS 341
Cdd:cd05928 271 CGAPTVYRMLVQ-QDLSSYKFPSLQHCVTGGEPLNPEVLEKWKAQTGLDIYEGYGQTETG-LICANFKGMKIKPGSMGKA 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 342 ILHVENKVVDPLGRELPAHQVGELIVK-GPN----VMKGYYKMPMETEHALKDGWLYTGDLARRDEDGYFYIVDRKKDMI 416
Cdd:cd05928 349 SPPYDVQIIDDNGNVLPPGTEGDIGIRvKPIrpfgLFSGYVDNPEKTAATIRGDFYLTGDRGIMDEDGYFWFMGRADDVI 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 417 IVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVV---PKRSGVTEE---DIMQHCETHLAKYKRPAAITF 490
Cdd:cd05928 429 NSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVlapQFLSHDPEQltkELQQHVKSVTAPYKYPRKVEF 508
|
490
....*....|....*....
gi 1816047872 491 LDDIPKNATGKMLRRALRD 509
Cdd:cd05928 509 VQELPKTVTGKIQRNELRD 527
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
15-508 |
2.37e-65 |
|
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: 218.39 E-value: 2.37e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 15 PDSIACRFKDHMMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYTPTEIGYML 94
Cdd:cd17649 1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 95 TNGDVKaivgvsqllplyecmheslpkvelVILCQTgeaepeaadpevrmkmttfakilrptsaakqnqelvPDDTAVIL 174
Cdd:cd17649 81 EDSGAG------------------------LLLTHH------------------------------------PRQLAYVI 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 175 YTSGTTGKPKGAMLTHQNLYSNANDVAGYLGMDERDNVVCALPM-FHVFclTVCMNAPLMSGATVLIEPQ---FSPASVF 250
Cdd:cd17649 101 YTSGSTGTPKGVAVSHGPLAAHCQATAERYGLTPGDRELQFASFnFDGA--HEQLLPPLICGACVVLRPDelwASADELA 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 251 KLVKQQQVTIfAGVPTMYNYLFQHE--NGKKDDFSSIRLCISGGAAMPVALLTAFEeKFGVTILEGYGLSEA--SPVTCF 326
Cdd:cd17649 179 EMVRELGVTV-LDLPPAYLQQLAEEadRTGDGRPPSLRLYIFGGEALSPELLRRWL-KAPVRLFNAYGPTEAtvTPLVWK 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 327 NPFDRGRKPGS--IGTSILHVENKVVDPLGRELPAHQVGELIVKGPNVMKGYYKMPMET-EHALKD------GWLY-TGD 396
Cdd:cd17649 257 CEAGAARAGASmpIGRPLGGRSAYILDADLNPVPVGVTGELYIGGEGLARGYLGRPELTaERFVPDpfgapgSRLYrTGD 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 397 LARRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPqSGEAVKGYVVPkRSGVTEEDIMQHCE 476
Cdd:cd17649 337 LARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGA-GGKQLVAYVVL-RAAAAQPELRAQLR 414
|
490 500 510
....*....|....*....|....*....|....*.
gi 1816047872 477 THLAK----YKRPAAITFLDDIPKNATGKMLRRALR 508
Cdd:cd17649 415 TALRAslpdYMVPAHLVFLARLPLTPNGKLDRKALP 450
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
7-508 |
4.21e-65 |
|
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: 218.75 E-value: 4.21e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 7 LEETASEKPDSIACRFKDHMMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYT 86
Cdd:cd17651 1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 87 PTEIGYMLTNGDVKAIVGvsqllplyecmHESLpkvelvilcqTGEAEPEAADPEVRMKMTTFAKILRPTSAAKQnqelv 166
Cdd:cd17651 81 AERLAFMLADAGPVLVLT-----------HPAL----------AGELAVELVAVTLLDQPGAAAGADAEPDPALD----- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 167 PDDTAVILYTSGTTGKPKGAMLTHQNLysnANDVA---GYLGMDERDNVV-CALPMFHVFCLTVCmnAPLMSGATVLIEP 242
Cdd:cd17651 135 ADDLAYVIYTSGSTGRPKGVVMPHRSL---ANLVAwqaRASSLGPGARTLqFAGLGFDVSVQEIF--STLCAGATLVLPP 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 243 ---QFSPASVFKLVKQQQVTIfAGVPT-MYNYLFQHENGKKDDFSSIRLCISGGAAMPVALLTA--FEEKFGVTILEGYG 316
Cdd:cd17651 210 eevRTDPPALAAWLDEQRISR-VFLPTvALRALAEHGRPLGVRLAALRYLLTGGEQLVLTEDLRefCAGLPGLRLHNHYG 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 317 LSEASPVTCF----NPFDRGRKPgSIGTSILHVENKVVDPLGRELPAHQVGELIVKGPNVMKGYYKMP-METEHALKDGW 391
Cdd:cd17651 289 PTETHVVTALslpgDPAAWPAPP-PIGRPIDNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPeLTAERFVPDPF 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 392 -----LY-TGDLARRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVVPKR-S 464
Cdd:cd17651 368 vpgarMYrTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPeA 447
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1816047872 465 GVTEEDIMQHCETHLAKYKRPAAITFLDDIPKNATGKMLRRALR 508
Cdd:cd17651 448 PVDAAELRAALATHLPEYMVPSAFVLLDALPLTPNGKLDRRALP 491
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
15-507 |
1.46e-64 |
|
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: 216.41 E-value: 1.46e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 15 PDSIACRFKDHMMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYTPTEIGYML 94
Cdd:cd17643 1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 95 tngdvkaivgvsqllplyecmheslpkvelvilcqtgeaepeaADPEVRMKMTTfakilrptsaakqnqelvPDDTAVIL 174
Cdd:cd17643 81 -------------------------------------------ADSGPSLLLTD------------------PDDLAYVI 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 175 YTSGTTGKPKGAMLTHQN---LYSNANDVagyLGMDERDNVVcalpMFHVFCLTVC---MNAPLMSGATVLIEPQF---S 245
Cdd:cd17643 100 YTSGSTGRPKGVVVSHANvlaLFAATQRW---FGFNEDDVWT----LFHSYAFDFSvweIWGALLHGGRLVVVPYEvarS 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 246 PASVFKLVKQQQVTIFAGVPTMYNYLFQHENGKKDDFSSIRLCISGGAAMPVALLTAFEEKFGV---TILEGYGLSEASP 322
Cdd:cd17643 173 PEDFARLLRDEGVTVLNQTPSAFYQLVEAADRDGRDPLALRYVIFGGEALEAAMLRPWAGRFGLdrpQLVNMYGITETTV 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 323 VTCFNPFDRGRKPGS----IGTSILHVENKVVDPLGRELPAHQVGELIVKGPNVMKGYYKMPMET-------EHALKDGW 391
Cdd:cd17643 253 HVTFRPLDAADLPAAaaspIGRPLPGLRVYVLDADGRPVPPGVVGELYVSGAGVARGYLGRPELTaerfvanPFGGPGSR 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 392 LY-TGDLARRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVVPK-RSGVTEE 469
Cdd:cd17643 333 MYrTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVADdGAAADIA 412
|
490 500 510
....*....|....*....|....*....|....*...
gi 1816047872 470 DIMQHCETHLAKYKRPAAITFLDDIPKNATGKMLRRAL 507
Cdd:cd17643 413 ELRALLKELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
8-507 |
1.51e-64 |
|
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: 217.58 E-value: 1.51e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 8 EETASEKPDSIACRFKDHMMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYTP 87
Cdd:cd17655 4 EEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 88 TEIGYMLTNGDVKAIVGVSQLLPLyecmhesLPKVELVILCQTGEAEPEAAdpevrmkmttfakilrpTSAAKQNQelvP 167
Cdd:cd17655 84 ERIQYILEDSGADILLTQSHLQPP-------IAFIGLIDLLDEDTIYHEES-----------------ENLEPVSK---S 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 168 DDTAVILYTSGTTGKPKGAMLTHQNL--YSNANDVAGYLGmdERDNVvcalPMF--HVFCLTVC-MNAPLMSGATVLIEP 242
Cdd:cd17655 137 DDLAYVIYTSGSTGKPKGVMIEHRGVvnLVEWANKVIYQG--EHLRV----ALFasISFDASVTeIFASLLSGNTLYIVR 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 243 QFSPASVFKLVK---QQQVTIFAGVPTMYNYLfqhENGKKDDFSSIRLCISGGAAMPVALLTAFEEKFG--VTILEGYGL 317
Cdd:cd17655 211 KETVLDGQALTQyirQNRITIIDLTPAHLKLL---DAADDSEGLSLKHLIVGGEALSTELAKKIIELFGtnPTITNAYGP 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 318 SE----ASPVTCFNPFDRGRKPgSIGTSILHVENKVVDPLGRELPAHQVGELIVKGPNVMKGYYKMPMETEHALKD---- 389
Cdd:cd17655 288 TEttvdASIYQYEPETDQQVSV-PIGKPLGNTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDdpfv 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 390 --GWLY-TGDLARRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVVPKRSgV 466
Cdd:cd17655 367 pgERMYrTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEKE-L 445
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1816047872 467 TEEDIMQHCETHLAKYKRPAAITFLDDIPKNATGKMLRRAL 507
Cdd:cd17655 446 PVAQLREFLARELPDYMIPSYFIKLDEIPLTPNGKVDRKAL 486
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
28-445 |
1.70e-64 |
|
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: 216.84 E-value: 1.70e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 28 TYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYTPTEIGYMLTNGDVKAIVgvsq 107
Cdd:cd17640 7 TYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALV---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 108 llplyecmheslpkVElvilcqtgeaepeaadpevrmkmttfakilrptsaakqNQelvPDDTAVILYTSGTTGKPKGAM 187
Cdd:cd17640 83 --------------VE--------------------------------------ND---SDDLATIIYTSGTTGNPKGVM 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 188 LTHQNLYSNANDVAGYLGMDERDNVVCALPMFHVF---CLTVCmnapLMSGATVLiepqFSPASVFKL-VKQQQVTIFAG 263
Cdd:cd17640 108 LTHANLLHQIRSLSDIVPPQPGDRFLSILPIWHSYersAEYFI----FACGCSQA----YTSIRTLKDdLKRVKPHYIVS 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 264 VPTMYNYLFQ--HENGKKDDFSS------------IRLCISGGAAMPVALLTAFeEKFGVTILEGYGLSEASPVTCFNPF 329
Cdd:cd17640 180 VPRLWESLYSgiQKQVSKSSPIKqflflfflsggiFKFGISGGGALPPHVDTFF-EAIGIEVLNGYGLTETSPVVSARRL 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 330 DRgRKPGSIGTSILHVENKVVDPLGRE-LPAHQVGELIVKGPNVMKGYYKMPMETEHAL-KDGWLYTGDLARRDEDGYFY 407
Cdd:cd17640 259 KC-NVRGSVGRPLPGTEIKIVDPEGNVvLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLdSDGWFNTGDLGWLTCGGELV 337
|
410 420 430
....*....|....*....|....*....|....*....
gi 1816047872 408 IVDRKKDMIIV-GGYNVYPREVEEVLYSHPDVKEAVVVG 445
Cdd:cd17640 338 LTGRAKDTIVLsNGENVEPQPIEEALMRSPFIEQIMVVG 376
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
15-507 |
5.46e-62 |
|
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: 210.21 E-value: 5.46e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 15 PDSIACRFKDHMMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYTPTEIGYML 94
Cdd:cd12114 1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 95 TNGDVKAIvgVSQllplyecmHESLPKVELVILCQTGEAEPEAADPEvrmkmttfakilrPTSAAKQnqelvPDDTAVIL 174
Cdd:cd12114 81 ADAGARLV--LTD--------GPDAQLDVAVFDVLILDLDALAAPAP-------------PPPVDVA-----PDDLAYVI 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 175 YTSGTTGKPKGAMLTHQNLYSNANDVAGYLGMDERDNVVCA------LPMFHVFcltvcmnAPLMSGATVLIEPQ---FS 245
Cdd:cd12114 133 FTSGSTGTPKGVMISHRAALNTILDINRRFAVGPDDRVLALsslsfdLSVYDIF-------GALSAGATLVLPDEarrRD 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 246 PASVFKLVKQQQVTIFAGVPTMYNYLFQHENGKKDDFSSIRLCISGGAAMPVALLTAFEEKF-GVTILEGYGLSEAS--- 321
Cdd:cd12114 206 PAHWAELIERHGVTLWNSVPALLEMLLDVLEAAQALLPSLRLVLLSGDWIPLDLPARLRALApDARLISLGGATEASiws 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 322 ---PVTCFNPFDRgrkpgSI--GTSILHVENKVVDPLGRELPAHQVGELIVKGPNVMKGYYKMPMETE-----HALKDGW 391
Cdd:cd12114 286 iyhPIDEVPPDWR-----SIpyGRPLANQRYRVLDPRGRDCPDWVPGELWIGGRGVALGYLGDPELTAarfvtHPDGERL 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 392 LYTGDLARRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPqSGEAVKGYVVPKR--SGVTEE 469
Cdd:cd12114 361 YRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDP-GGKRLAAFVVPDNdgTPIAPD 439
|
490 500 510
....*....|....*....|....*....|....*...
gi 1816047872 470 DIMQHCETHLAKYKRPAAITFLDDIPKNATGKMLRRAL 507
Cdd:cd12114 440 ALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
11-507 |
6.96e-62 |
|
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: 209.41 E-value: 6.96e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 11 ASEKPDSIACRFKDHMMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPlYTPTEi 90
Cdd:cd05945 1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDA-SSPAE- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 91 gymltngdvkaivgvsqllplyecmheslpKVELVIlcqtgeaepEAADPEVRMKmttfakilrptsaakqnqelVPDDT 170
Cdd:cd05945 79 ------------------------------RIREIL---------DAAKPALLIA--------------------DGDDN 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 171 AVILYTSGTTGKPKGAMLTHQNLYSNANDVAGYLGMDERDNVVCALP------MFHVFCltvcmnaPLMSGATVLIEP-- 242
Cdd:cd05945 100 AYIIFTSGSTGRPKGVQISHDNLVSFTNWMLSDFPLGPGDVFLNQAPfsfdlsVMDLYP-------ALASGATLVPVPrd 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 243 -QFSPASVFKLVKQQQVTIFAGVPTMYNYLFQHENGKKDDFSSIRLCISGGAAMPVALLTAFEEKF-GVTILEGYGLSEA 320
Cdd:cd05945 173 aTADPKQLFRFLAEHGITVWVSTPSFAAMCLLSPTFTPESLPSLRHFLFCGEVLPHKTARALQQRFpDARIYNTYGPTEA 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 321 SpVTC-FNPFDR----GRKPGSIGTSILHVENKVVDPLGRELPAHQVGELIVKGPNVMKGYYKMPMETEHAL----KDGW 391
Cdd:cd05945 253 T-VAVtYIEVTPevldGYDRLPIGYAKPGAKLVILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFfpdeGQRA 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 392 LYTGDLARRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVVPKRSG--VTEE 469
Cdd:cd05945 332 YRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPGAeaGLTK 411
|
490 500 510
....*....|....*....|....*....|....*...
gi 1816047872 470 DIMQHCETHLAKYKRPAAITFLDDIPKNATGKMLRRAL 507
Cdd:cd05945 412 AIKAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
7-509 |
2.52e-61 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 210.86 E-value: 2.52e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 7 LEETASEKPDSIACRFKDHMMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYT 86
Cdd:PLN02479 26 LERAAVVHPTRKSVVHGSVRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRLN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 87 PTEIGYMLTNGDVKAIVGVSQLLPLYEcmhESLP----------KVELVILCQTGEAEPEAADPEVRMKMTTFAKILR-- 154
Cdd:PLN02479 106 APTIAFLLEHSKSEVVMVDQEFFTLAE---EALKilaekkkssfKPPLLIVIGDPTCDPKSLQYALGKGAIEYEKFLEtg 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 155 -PTSAAKQnqelvPDD---TAVILYTSGTTGKPKGAMLTHQNLYSNANDVAGYLGMDERDNVVCALPMFHV--FCLTVCM 228
Cdd:PLN02479 183 dPEFAWKP-----PADewqSIALGYTSGTTASPKGVVLHHRGAYLMALSNALIWGMNEGAVYLWTLPMFHCngWCFTWTL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 229 NAplMSGATVLIEpQFSPASVFKLVKQQQVTIFAGVPTMYNYLFqheNGKKDD----FSSIRLCISGGAAMPVALLTAFE 304
Cdd:PLN02479 258 AA--LCGTNICLR-QVTAKAIYSAIANYGVTHFCAAPVVLNTIV---NAPKSEtilpLPRVVHVMTAGAAPPPSVLFAMS 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 305 EKfGVTILEGYGLSEA---SPVTCFNP-------FDRGRKPGSIGTSILHVEN-KVVDP-LGRELPA--HQVGELIVKGP 370
Cdd:PLN02479 332 EK-GFRVTHTYGLSETygpSTVCAWKPewdslppEEQARLNARQGVRYIGLEGlDVVDTkTMKPVPAdgKTMGEIVMRGN 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 371 NVMKGYYKMPMETEHALKDGWLYTGDLARRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQ 450
Cdd:PLN02479 411 MVMKGYLKNPKANEEAFANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDER 490
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1816047872 451 SGEAVKGYVVPK------RSGVTEEDIMQHCETHLAKYKRPAAITFlDDIPKNATGKMLRRALRD 509
Cdd:PLN02479 491 WGESPCAFVTLKpgvdksDEAALAEDIMKFCRERLPAYWVPKSVVF-GPLPKTATGKIQKHVLRA 554
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
7-449 |
2.92e-60 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 208.57 E-value: 2.92e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 7 LEETASEKPDSIACRFKDHMMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYT 86
Cdd:PRK08279 43 FEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLNTQQR 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 87 PTEIGYMLTNGDVKAIVGVSQLLPLYECMHESLPKVELVILCQTGEAEPEAADPEVRMKMTTFAKILRPTSAAkqnqeLV 166
Cdd:PRK08279 123 GAVLAHSLNLVDAKHLIVGEELVEAFEEARADLARPPRLWVAGGDTLDDPEGYEDLAAAAAGAPTTNPASRSG-----VT 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 167 PDDTAVILYTSGTTGKPKGAMLTHQNLYSNANDVAGYLGMDERDNVVCALPMFHVFCLTVCMNAPLMSGATVLIEPQFSp 246
Cdd:PRK08279 198 AKDTAFYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLTPDDVLYCCLPLYHNTGGTVAWSSVLAAGATLALRRKFS- 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 247 ASVF-KLVKQQQVTIFAGVPTMYNYLFQHENGKKDDFSSIRLCIsgGAAMPVALLTAFEEKFGVT-ILEGYGLSEASpVT 324
Cdd:PRK08279 277 ASRFwDDVRRYRATAFQYIGELCRYLLNQPPKPTDRDHRLRLMI--GNGLRPDIWDEFQQRFGIPrILEFYAASEGN-VG 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 325 CFNPFDR----GRKPGSIGTSILHVE-----NKVV-DPLGR--ELPAHQVGELIVK----GPnvMKGYYKmPMETE---- 384
Cdd:PRK08279 354 FINVFNFdgtvGRVPLWLAHPYAIVKydvdtGEPVrDADGRciKVKPGEVGLLIGRitdrGP--FDGYTD-PEASEkkil 430
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1816047872 385 -HALKDG--WLYTGDLARRDEDGYFYIVDRkkdmiiVG------GYNVYPREVEEVLYSHPDVKEAVVVGVPDP 449
Cdd:PRK08279 431 rDVFKKGdaWFNTGDLMRDDGFGHAQFVDR------LGdtfrwkGENVATTEVENALSGFPGVEEAVVYGVEVP 498
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
8-507 |
3.38e-58 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 209.25 E-value: 3.38e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 8 EETASEKPDSIACRFKDHMMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYTP 87
Cdd:PRK12467 519 EAQARQHPERPALVFGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQ 598
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 88 TEIGYMLTNGDVKAIVGVSQLLPLYEcMHESLPKVELVILCQTGEAEPEAaDPEVRmkmttfakilrptsaakqnqeLVP 167
Cdd:PRK12467 599 DRLAYMLDDSGVRLLLTQSHLLAQLP-VPAGLRSLCLDEPADLLCGYSGH-NPEVA---------------------LDP 655
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 168 DDTAVILYTSGTTGKPKGAMLTHQNLYSNANDVAGYLGMDERDNVVcalpMFHVFCLTVC---MNAPLMSGATVLIEPQ- 243
Cdd:PRK12467 656 DNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSML----MVSTFAFDLGvteLFGALASGATLHLLPPd 731
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 244 --FSPASVFKLVKQQQVTIFAGVPTMYNYLFQheNGKKDDFSSIRLCISGGAAMPVALLTA-FEEKFGVTILEGYGLSEA 320
Cdd:PRK12467 732 caRDAEAFAALMADQGVTVLKIVPSHLQALLQ--ASRVALPRPQRALVCGGEALQVDLLARvRALGPGARLINHYGPTET 809
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 321 S-PVTCFNPFDRGRKPGS--IGTSILHVENKVVDPLGRELPAHQVGELIVKGPNVMKGYYKMPMET-EHALKD------G 390
Cdd:PRK12467 810 TvGVSTYELSDEERDFGNvpIGQPLANLGLYILDHYLNPVPVGVVGELYIGGAGLARGYHRRPALTaERFVPDpfgadgG 889
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 391 WLY-TGDLARRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVkGYVVPK------R 463
Cdd:PRK12467 890 RLYrTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAGLQLV-AYLVPAavadgaE 968
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1816047872 464 SGVTEEDIMQHCETHLAKYKRPAAITFLDDIPKNATGKMLRRAL 507
Cdd:PRK12467 969 HQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKAL 1012
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
8-507 |
3.53e-58 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 209.43 E-value: 3.53e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 8 EETASEKPDSIACRFKDHMMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYTP 87
Cdd:PRK12316 518 EEQVERTPEAPALAFGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPA 597
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 88 TEIGYMLTNGDVKAIVGVSQLLPLYecmheSLPKVELVILCQTGEAEPEAadpevrmkmttfakilrpTSAAKQNQELVP 167
Cdd:PRK12316 598 ERLAYMLEDSGVQLLLSQSHLGRKL-----PLAAGVQVLDLDRPAAWLEG------------------YSEENPGTELNP 654
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 168 DDTAVILYTSGTTGKPKGAMLTHQNLYSNANDVAGYLGMDERDNVVCALPMfhVFCLTVCM-NAPLMSGATVLIEPQ--- 243
Cdd:PRK12316 655 ENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPF--SFDVSVWEfFWPLMSGARLVVAAPgdh 732
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 244 FSPASVFKLVKQQQVTIFAGVPTMYNYLFQHENgkKDDFSSIRLCISGGAAMPVALLTAFEEKFGVT-ILEGYGLSEAS- 321
Cdd:PRK12316 733 RDPAKLVELINREGVDTLHFVPSMLQAFLQDED--VASCTSLRRIVCSGEALPADAQEQVFAKLPQAgLYNLYGPTEAAi 810
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 322 PVTCFNPFDRGRKPGSIGTSILHVENKVVDPLGRELPAHQVGELIVKGPNVMKGYYKMP-METEHALKDGW-----LY-T 394
Cdd:PRK12316 811 DVTHWTCVEEGGDSVPIGRPIANLACYILDANLEPVPVGVLGELYLAGRGLARGYHGRPgLTAERFVPSPFvagerMYrT 890
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 395 GDLARRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGvpdpQSGEAVKGYVVPK-RSGVTEEDIMQ 473
Cdd:PRK12316 891 GDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLA----VDGKQLVGYVVLEsEGGDWREALKA 966
|
490 500 510
....*....|....*....|....*....|....
gi 1816047872 474 HCETHLAKYKRPAAITFLDDIPKNATGKMLRRAL 507
Cdd:PRK12316 967 HLAASLPEYMVPAQWLALERLPLTPNGKLDRKAL 1000
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
11-510 |
7.94e-58 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 201.79 E-value: 7.94e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 11 ASE-KPDSIACRFKDHMMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYTPTE 89
Cdd:PLN03102 23 ASEcYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 90 IGYMLTNGDVKAIVGVSQLLPLY-ECMH-----ESLPKVELVILCQ---TGEAEPEAADPEVRMKMTtfakilRPTSAAK 160
Cdd:PLN03102 103 IAAILRHAKPKILFVDRSFEPLArEVLHllsseDSNLNLPVIFIHEidfPKRPSSEELDYECLIQRG------EPTPSLV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 161 QNQELVPD--DTAVILYTSGTTGKPKGAMLTHQNLY-SNANDVAGYlGMDERDNVVCALPMFHVFCLTVCMNAPLMSGAT 237
Cdd:PLN03102 177 ARMFRIQDehDPISLNYTSGTTADPKGVVISHRGAYlSTLSAIIGW-EMGTCPVYLWTLPMFHCNGWTFTWGTAARGGTS 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 238 VLIEPQFSPaSVFKLVKQQQVTIFAGVPTMYNYLFQHENGKKDDFSSIRLCISGGAAMPVALLTAFEeKFGVTILEGYGL 317
Cdd:PLN03102 256 VCMRHVTAP-EIYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSPRSGPVHVLTGGSPPPAALVKKVQ-RLGFQVMHAYGL 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 318 SEAS-PVT-CFNPFDRGRKP--------GSIGTSIL-----HVEN-KVVDPLGRElpAHQVGELIVKGPNVMKGYYKMPM 381
Cdd:PLN03102 334 TEATgPVLfCEWQDEWNRLPenqqmelkARQGVSILgladvDVKNkETQESVPRD--GKTMGEIVIKGSSIMKGYLKNPK 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 382 ETEHALKDGWLYTGDLARRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVVP 461
Cdd:PLN03102 412 ATSEAFKHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVL 491
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 462 KRSGVT-----------EEDIMQHCETHLAKYKRPAAITFLDDIPKNATGKMLRRALRDI 510
Cdd:PLN03102 492 EKGETTkedrvdklvtrERDLIEYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKLRDI 551
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
175-504 |
1.92e-57 |
|
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: 193.78 E-value: 1.92e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 175 YTSGTTGKPKGAMLTHQN-LYSNANDVAGYLgMDERDNVVCALPMFHVFCLTVCMNApLMSGATVLIEPQFSPASVFKLV 253
Cdd:cd17633 7 FTSGTTGLPKAYYRSERSwIESFVCNEDLFN-ISGEDAILAPGPLSHSLFLYGAISA-LYLGGTFIGQRKFNPKSWIRKI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 254 KQQQVTIFAGVPTMYNYLFQHENGKkddfSSIRLCISGGAAMPVALLTAFEEKF-GVTILEGYGLSEASPVTcFNPFDRG 332
Cdd:cd17633 85 NQYNATVIYLVPTMLQALARTLEPE----SKIKSIFSSGQKLFESTKKKLKNIFpKANLIEFYGTSELSFIT-YNFNQES 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 333 RKPGSIGTSILHVENKVVDPLGRElpahqVGELIVKGPNVMKGYYKMPMETehalKDGWLYTGDLARRDEDGYFYIVDRK 412
Cdd:cd17633 160 RPPNSVGRPFPNVEIEIRNADGGE-----IGKIFVKSEMVFSGYVRGGFSN----PDGWMSVGDIGYVDEEGYLYLVGRE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 413 KDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEavKGYVVPKRSGVTEEDIMQHCETHLAKYKRPAAITFLD 492
Cdd:cd17633 231 SDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGE--IAVALYSGDKLTYKQLKRFLKQKLSRYEIPKKIIFVD 308
|
330
....*....|..
gi 1816047872 493 DIPKNATGKMLR 504
Cdd:cd17633 309 SLPYTSSGKIAR 320
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
27-508 |
4.68e-57 |
|
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: 196.20 E-value: 4.68e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 27 MTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYTPTEIGYMLTNGDVKAIVgvs 106
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVV--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 107 qllplyecmheslpkvelvilcqtgeaepeaADPEVRMKMTtfakilrptsaakqnqelvpDDTAVILYTSGTTGKPKGA 186
Cdd:cd05973 78 -------------------------------TDAANRHKLD--------------------SDPFVMMFTSGTTGLPKGV 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 187 MLTHQNLYSNANDVAGYLGMDERDNVVCALPMFHVFCLTVCMNAPLMSG-ATVLIEPQFSPASVFKLVKQQQVTIFAGVP 265
Cdd:cd05973 107 PVPLRALAAFGAYLRDAVDLRPEDSFWNAADPGWAYGLYYAITGPLALGhPTILLEGGFSVESTWRVIERLGVTNLAGSP 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 266 TMYNYLFQHENGKKDDFS-SIRLCISGGAAMPVALLTAFEEKFGVTILEGYGLSEASPVTCfNPFDRGR--KPGSIGTSI 342
Cdd:cd05973 187 TAYRLLMAAGAEVPARPKgRLRRVSSAGEPLTPEVIRWFDAALGVPIHDHYGQTELGMVLA-NHHALEHpvHAGSAGRAM 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 343 LHVENKVVDPLGRELPAHQVGELIVKGPNV----MKGYYKMPmetEHALKDGWLYTGDLARRDEDGYFYIVDRKKDMIIV 418
Cdd:cd05973 266 PGWRVAVLDDDGDELGPGEPGRLAIDIANSplmwFRGYQLPD---TPAIDGGYYLTGDTVEFDPDGSFSFIGRADDVITM 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 419 GGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVV--PKRSGVTE--EDIMQHCETHLAKYKRPAAITFLDDI 494
Cdd:cd05973 343 SGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVlrGGHEGTPAlaDELQLHVKKRLSAHAYPRTIHFVDEL 422
|
490
....*....|....
gi 1816047872 495 PKNATGKMLRRALR 508
Cdd:cd05973 423 PKTPSGKIQRFLLR 436
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
169-504 |
5.63e-57 |
|
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: 193.25 E-value: 5.63e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 169 DTAVILYTSGTTGKPKGAMLTHQNLYSNA-NDVAGYLGMDERDNVVCALPMFHVFCLTVCMNAPLMSGATVLIEPQFSPA 247
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANKTFFAVPdILQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGENTTYK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 248 SVFKLVKQQQVTIFAGVPTMYNYLFQHENGKKDDFSSIRlCISGGAAMPVALLTAFEEKFGVT-ILEGYGLSEASPVTCF 326
Cdd:cd17635 82 SLFKILTTNAVTTTCLVPTLLSKLVSELKSANATVPSLR-LIGYGGSRAIAADVRFIEATGLTnTAQVYGLSETGTALCL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 327 nPFDRGRKP-GSIGTSILHVENKVVDPLGRELPAHQVGELIVKGPNVMKGYYKMPMETEHALKDGWLYTGDLARRDEDGY 405
Cdd:cd17635 161 -PTDDDSIEiNAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLIDGWVNTGDLGERREDGF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 406 FYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVVpkRSGVTEED----IMQHCETHLAK 481
Cdd:cd17635 240 LFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVV--ASAELDENairaLKHTIRRELEP 317
|
330 340
....*....|....*....|...
gi 1816047872 482 YKRPAAITFLDDIPKNATGKMLR 504
Cdd:cd17635 318 YARPSTIVIVTDIPRTQSGKVKR 340
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
15-507 |
1.39e-56 |
|
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: 194.78 E-value: 1.39e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 15 PDSIACRFKDHMMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYTPTEIGYML 94
Cdd:cd17652 1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 95 tnGDVKAIVGVSQllplyecmheslpkvelvilcqtgeaepeaadpevrmkmttfakilrptsaakqnqelvPDDTAVIL 174
Cdd:cd17652 81 --ADARPALLLTT-----------------------------------------------------------PDNLAYVI 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 175 YTSGTTGKPKGAMLTHQNLYSNANDVAGYLGMDERDNVV-CALPMFHVFCLTVCMNapLMSGATVLIEPQ---FSPASVF 250
Cdd:cd17652 100 YTSGSTGRPKGVVVTHRGLANLAAAQIAAFDVGPGSRVLqFASPSFDASVWELLMA--LLAGATLVLAPAeelLPGEPLA 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 251 KLVKQQQVTIFAGVPTMYNYLfqhengKKDDFSSIRLCISGGAAMPVALLtafeEKFGVT--ILEGYGLSEASPVTCFNP 328
Cdd:cd17652 178 DLLREHRITHVTLPPAALAAL------PPDDLPDLRTLVVAGEACPAELV----DRWAPGrrMINAYGPTETTVCATMAG 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 329 FDRGRKPGSIGTSILHVENKVVDPLGRELPAHQVGELIVKGPNVMKGYYKMPMET-EHALKD------GWLY-TGDLARR 400
Cdd:cd17652 248 PLPGGGVPPIGRPVPGTRVYVLDARLRPVPPGVPGELYIAGAGLARGYLNRPGLTaERFVADpfgapgSRMYrTGDLARW 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 401 DEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVVPKRSG-VTEEDIMQHCETHL 479
Cdd:cd17652 328 RADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAPGAaPTAAELRAHLAERL 407
|
490 500
....*....|....*....|....*...
gi 1816047872 480 AKYKRPAAITFLDDIPKNATGKMLRRAL 507
Cdd:cd17652 408 PGYMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
53-509 |
4.08e-56 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 196.05 E-value: 4.08e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 53 HLALLLGNSPDFIIAFFGALKAGIVVVPINPLYTPTEIGYMLTNGDVKAIVGVSQLLPLYECMhesLPKVELVILCQTGE 132
Cdd:PRK07867 56 HVGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARDIAHADCQLVLTESAHAELLDGL---DPGVRVINVDSPAW 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 133 AEPEAADPEVRmkmttfakiLRPTSAAkqnqelvPDDTAVILYTSGTTGKPKGAMLTHQNLYSNANDVAGYLGMDERDNV 212
Cdd:PRK07867 133 ADELAAHRDAE---------PPFRVAD-------PDDLFMLIFTSGTSGDPKAVRCTHRKVASAGVMLAQRFGLGPDDVC 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 213 VCALPMFHVFCLTVCMNAPLMSGATVLIEPQFSpASVF-KLVKQQQVTIFAGVPTMYNYLFQHENGKKDDFSSIRLcISG 291
Cdd:PRK07867 197 YVSMPLFHSNAVMAGWAVALAAGASIALRRKFS-ASGFlPDVRRYGATYANYVGKPLSYVLATPERPDDADNPLRI-VYG 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 292 GAAMPVALlTAFEEKFGVTILEGYGLSEASPVTCFNPfdrGRKPGSIG-----TSILHVENK------VVDPLGRELPAH 360
Cdd:PRK07867 275 NEGAPGDI-ARFARRFGCVVVDGFGSTEGGVAITRTP---DTPPGALGplppgVAIVDPDTGtecppaEDADGRLLNADE 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 361 QVGELI-VKGPNVMKGYYKMPMETEHALKDGWLYTGDLARRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVK 439
Cdd:PRK07867 351 AIGELVnTAGPGGFEGYYNDPEADAERMRGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDAT 430
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1816047872 440 EAVVVGVPDPQSGEAVKGYVVPKRSGVTEEDIMQ---HCETHLAKYKRPAAITFLDDIPKNATGKMLRRALRD 509
Cdd:PRK07867 431 EVAVYAVPDPVVGDQVMAALVLAPGAKFDPDAFAeflAAQPDLGPKQWPSYVRVCAELPRTATFKVLKRQLSA 503
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
15-507 |
1.43e-55 |
|
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: 192.30 E-value: 1.43e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 15 PDSIACRFKDHMMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYTPTEIGYML 94
Cdd:cd17650 1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 95 TNGDVKAIVgvsqllplyecmheslpkvelvilcqtgeaepeaadpevrmkmttfakilrptsaakqnqeLVPDDTAVIL 174
Cdd:cd17650 81 EDSGAKLLL-------------------------------------------------------------TQPEDLAYVI 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 175 YTSGTTGKPKGAMLTHQNLYSNANDVAGYLGMDERDnvVCALPM----FHVFCLTVCMNapLMSGATVLIEPQ---FSPA 247
Cdd:cd17650 100 YTSGTTGKPKGVMVEHRNVAHAAHAWRREYELDSFP--VRLLQMasfsFDVFAGDFARS--LLNGGTLVICPDevkLDPA 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 248 SVFKLVKQQQVTIFAGVPTMYNYLFQHENGKKDDFSSIRLCISGGAAMPVALLTAFEEKFG--VTILEGYGLSEASPVTC 325
Cdd:cd17650 176 ALYDLILKSRITLMESTPALIRPVMAYVYRNGLDLSAMRLLIVGSDGCKAQDFKTLAARFGqgMRIINSYGVTEATIDST 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 326 FNPFDRGRKPGS----IGTSILHVENKVVDPLGRELPAHQVGELIVKGPNVMKGYYKMPMETEHALKD------GWLY-T 394
Cdd:cd17650 256 YYEEGRDPLGDSanvpIGRPLPNTAMYVLDERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVEnpfapgERMYrT 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 395 GDLARRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVVPKRSGVTEEdIMQH 474
Cdd:cd17650 336 GDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVREDKGGEARLCAYVVAAATLNTAE-LRAF 414
|
490 500 510
....*....|....*....|....*....|...
gi 1816047872 475 CETHLAKYKRPAAITFLDDIPKNATGKMLRRAL 507
Cdd:cd17650 415 LAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
28-511 |
2.39e-55 |
|
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: 194.04 E-value: 2.39e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 28 TYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYTPTEIgymltNGDVKAIVGVSQ 107
Cdd:cd05906 41 SYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLTVPPTYDEP-----NARLRKLRHIWQ 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 108 LL--PLYECMHESLPKVelvilcqtgeaEPEAADPEVRMKMTTFAKILRPTSAAKQNQELVPDDTAVILYTSGTTGKPKG 185
Cdd:cd05906 116 LLgsPVVLTDAELVAEF-----------AGLETLSGLPGIRVLSIEELLDTAADHDLPQSRPDDLALLMLTSGSTGFPKA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 186 AMLTHQNLYSNANDVAGYLGMDERDNVVCALPMFHVFCLTVCMNAPLMSGA--------TVLIEP-QFspasvFKLVKQQ 256
Cdd:cd05906 185 VPLTHRNILARSAGKIQHNGLTPQDVFLNWVPLDHVGGLVELHLRAVYLGCqqvhvpteEILADPlRW-----LDLIDRY 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 257 QVTI-FAgvPtmyNYLFQH-------ENGKKDDFSSIRLCISGG----AAMPVALLTAFeEKFGV---TILEGYGLSE-A 320
Cdd:cd05906 260 RVTItWA--P---NFAFALlndlleeIEDGTWDLSSLRYLVNAGeavvAKTIRRLLRLL-EPYGLppdAIRPAFGMTEtC 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 321 SPVTCFNPFDRGRKPG-----SIGTSILHVENKVVDPLGRELPAHQVGELIVKGPNVMKGYYKMPMETEHAL-KDGWLYT 394
Cdd:cd05906 334 SGVIYSRSFPTYDHSQalefvSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFtEDGWFRT 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 395 GDLARRDeDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKE--AVVVGVPDPQSGEA------VKGYVVPKRSGV 466
Cdd:cd05906 414 GDLGFLD-NGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPsfTAAFAVRDPGAETEelaiffVPEYDLQDALSE 492
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1816047872 467 TEEDIMQHC--ETHLakykRPAAITFL--DDIPKNATGKMLRRALRDIL 511
Cdd:cd05906 493 TLRAIRSVVsrEVGV----SPAYLIPLpkEEIPKTSLGKIQRSKLKAAF 537
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
7-507 |
3.11e-55 |
|
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: 191.38 E-value: 3.11e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 7 LEETASEKPDSIACRFKDHMMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYT 86
Cdd:cd12115 5 VEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 87 PTEIGYMLTngdvkaivgvsqllplyecmheslpkvelvilcqtgeaepeaaDPEVRMKMTTfakilrptsaakqnqelv 166
Cdd:cd12115 85 PERLRFILE-------------------------------------------DAQARLVLTD------------------ 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 167 PDDTAVILYTSGTTGKPKGAMLTHQNLYSNANDVAGYLGMDERDNVVCA------LPMFHVFCltvcmnaPLMSGATV-L 239
Cdd:cd12115 104 PDDLAYVIYTSGSTGRPKGVAIEHRNAAAFLQWAAAAFSAEELAGVLAStsicfdLSVFELFG-------PLATGGKVvL 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 240 IEPQFSPasvFKLVKQQQVTIFAGVPTMYNYLFQHengkkDDF-SSIRLCISGGAAMPVALLTAFEEKFGVT-ILEGYGL 317
Cdd:cd12115 177 ADNVLAL---PDLPAAAEVTLINTVPSAAAELLRH-----DALpASVRVVNLAGEPLPRDLVQRLYARLQVErVVNLYGP 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 318 SEASPVTCFNPFDRG-RKPGSIGTSILHVENKVVDPLGRELPAHQVGELIVKGPNVMKGYYKMPMET-EHALKDGW---- 391
Cdd:cd12115 249 SEDTTYSTVAPVPPGaSGEVSIGRPLANTQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTaERFLPDPFgpga 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 392 -LY-TGDLARRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVVPKR-SGVTE 468
Cdd:cd12115 329 rLYrTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEPgAAGLV 408
|
490 500 510
....*....|....*....|....*....|....*....
gi 1816047872 469 EDIMQHCETHLAKYKRPAAITFLDDIPKNATGKMLRRAL 507
Cdd:cd12115 409 EDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
16-509 |
6.99e-55 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 192.93 E-value: 6.99e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 16 DSIACRFKDHMMTYQELNEHIQRFADGLQEAGMEKGD-HLALLLGNSPDFIIAFFGALKAGIVVVPINPLYTPTEIGYML 94
Cdd:PRK13388 16 DTIAVRYGDRTWTWREVLAEAAARAAALIALADPDRPlHVGVLLGNTPEMLFWLAAAALGGYVLVGLNTTRRGAALAADI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 95 TNGDVKAIVGVSQLLPLYECMheSLPKVELVIlcqtgeaepeAADPEvrmkmttFAKILRPTSAAKQNQELVPDDTAVIL 174
Cdd:PRK13388 96 RRADCQLLVTDAEHRPLLDGL--DLPGVRVLD----------VDTPA-------YAELVAAAGALTPHREVDAMDPFMLI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 175 YTSGTTGKPKGAMLTHQNLYSNANDVAGYLGMDERDNVVCALPMFHVFCLTVCMNAPLMSGATVLIEPQFSPASVFKLVK 254
Cdd:PRK13388 157 FTSGTTGAPKAVRCSHGRLAFAGRALTERFGLTRDDVCYVSMPLFHSNAVMAGWAPAVASGAAVALPAKFSASGFLDDVR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 255 QQQVTIFAGVPTMYNYLFQHENGKKDDFSSIRLCIsGGAAMPVALlTAFEEKFGVTILEGYGLSE-ASPVTcfnpFDRGR 333
Cdd:PRK13388 237 RYGATYFNYVGKPLAYILATPERPDDADNPLRVAF-GNEASPRDI-AEFSRRFGCQVEDGYGSSEgAVIVV----REPGT 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 334 KPGSIG-----TSILHVENKVV------DPLGREL-PAHQVGELIVK-GPNVMKGYYKMPMETEHALKDGWLYTGDLARR 400
Cdd:PRK13388 311 PPGSIGrgapgVAIYNPETLTEcavarfDAHGALLnADEAIGELVNTaGAGFFEGYYNNPEATAERMRHGMYWSGDLAYR 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 401 DEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVVPKRSGVTEEDIMQ---HCET 477
Cdd:PRK13388 391 DADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVGDQVMAALVLRDGATFDPDAFAaflAAQP 470
|
490 500 510
....*....|....*....|....*....|..
gi 1816047872 478 HLAKYKRPAAITFLDDIPKNATGKMLRRALRD 509
Cdd:PRK13388 471 DLGTKAWPRYVRIAADLPSTATNKVLKRELIA 502
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
7-507 |
1.01e-54 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 199.23 E-value: 1.01e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 7 LEETASEKPDSIACRFKDHMMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYT 86
Cdd:PRK12467 1580 IEDQAAATPEAVALVFGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYP 1659
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 87 PTEIGYMLTNGDVKAIVGVSQLLPlyecmheSLP---KVELVILCQTG---EAEPEaADPEVRmkmttfakilrptsaak 160
Cdd:PRK12467 1660 RERLAYMIEDSGIELLLTQSHLQA-------RLPlpdGLRSLVLDQEDdwlEGYSD-SNPAVN----------------- 1714
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 161 qnqeLVPDDTAVILYTSGTTGKPKGAMLTHQNLYSNANDVAGYLGMDERDNVVcalpMFHVFCLTVCMNA---PLMSGAT 237
Cdd:PRK12467 1715 ----LAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVVL----QFTSFAFDVSVWElfwPLINGAR 1786
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 238 VLIEP---QFSPASVFKLVKQQQVTIFAGVPTMYNYLFQHEnGKKDDFSSIRLCISGGAAMPVALLTAFEEKFGVT-ILE 313
Cdd:PRK12467 1787 LVIAPpgaHRDPEQLIQLIERQQVTTLHFVPSMLQQLLQMD-EQVEHPLSLRRVVCGGEALEVEALRPWLERLPDTgLFN 1865
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 314 GYGLSEAS-PVT---CFNPFDRGRKPGSIGTSILHVENKVVDPLGRELPAHQVGELIVKGPNVMKGYYKMPMETEH---- 385
Cdd:PRK12467 1866 LYGPTETAvDVThwtCRRKDLEGRDSVPIGQPIANLSTYILDASLNPVPIGVAGELYLGGVGLARGYLNRPALTAErfva 1945
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 386 ---ALKDGWLY-TGDLARRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVpDPQSGEAVKGYVVP 461
Cdd:PRK12467 1946 dpfGTVGSRLYrTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIAQ-DGANGKQLVAYVVP 2024
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1816047872 462 KRSGVTEEDIMQ---------HCETHLAKYKRPAAITFLDDIPKNATGKMLRRAL 507
Cdd:PRK12467 2025 TDPGLVDDDEAQvalrailknHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKAL 2079
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
1-455 |
2.02e-54 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 191.65 E-value: 2.02e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 1 MNLVSKLEETASEKPDSIACRFKDHM----------MTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFG 70
Cdd:PRK09274 6 ANIARHLPRAAQERPDQLAVAVPGGRgadgklaydeLSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 71 ALKAGIVVVPINPlytpteigymltnGdvkaiVGVSQLLplyECMHESLPKVELVIlcqtgeaePEA---------ADPE 141
Cdd:PRK09274 86 LFKAGAVPVLVDP-------------G-----MGIKNLK---QCLAEAQPDAFIGI--------PKAhlarrlfgwGKPS 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 142 VR----------MKMTTFAKILRPTSAAK-QNQELVPDDTAVILYTSGTTGKPKGAMLTHQNLYSNANDVAGYLGM--DE 208
Cdd:PRK09274 137 VRrlvtvggrllWGGTTLATLLRDGAAAPfPMADLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIepGE 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 209 RDnvvcaLPMFHVFCLTvcmnAPLMSGATVLIEPQFS------PASVFKLVKQQQVTIFAGVPTMYNYLFQHENGKKDDF 282
Cdd:PRK09274 217 ID-----LPTFPLFALF----GPALGMTSVIPDMDPTrpatvdPAKLFAAIERYGVTNLFGSPALLERLGRYGEANGIKL 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 283 SSIRLCISGGAAMPVALLTAFEEKF--GVTILEGYGLSEASPVTC-------FNPFDRGRKPGSI--GTSILHVENKVV- 350
Cdd:PRK09274 288 PSLRRVISAGAPVPIAVIERFRAMLppDAEILTPYGATEALPISSiesreilFATRAATDNGAGIcvGRPVDGVEVRIIa 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 351 ---DPL-----GRELPAHQVGELIVKGPNVMKGYYKMPMETEHA-LKDG----WLYTGDLARRDEDGYFYIVDRKKDMII 417
Cdd:PRK09274 368 isdAPIpewddALRLATGEIGEIVVAGPMVTRSYYNRPEATRLAkIPDGqgdvWHRMGDLGYLDAQGRLWFCGRKAHRVE 447
|
490 500 510
....*....|....*....|....*....|....*...
gi 1816047872 418 VGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAV 455
Cdd:PRK09274 448 TAGGTLYTIPCERIFNTHPGVKRSALVGVGVPGAQRPV 485
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
28-509 |
3.85e-54 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 191.53 E-value: 3.85e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 28 TYQELNEHIQRFADGLQ-EAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYTPTEIGYMLTNGDVKAIVGVS 106
Cdd:PRK05620 40 TFAAIGARAAALAHALHdELGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIVADP 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 107 QLLPLYECMHESLPKVELVILCQTGEA-EPEAADPEvRMKMTTFAKILRPTSAAKQNQELVPDDTAVILYTSGTTGKPKG 185
Cdd:PRK05620 120 RLAEQLGEILKECPCVRAVVFIGPSDAdSAAAHMPE-GIKVYSYEALLDGRSTVYDWPELDETTAAAICYSTGTTGAPKG 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 186 AMLTHQNLYSNANDV--AGYLGMDERDNVVCALPMFHVFCLTVCMnAPLMSGA-TVLIEPQFSPASVFKLVKQQQVTIFA 262
Cdd:PRK05620 199 VVYSHRSLYLQSLSLrtTDSLAVTHGESFLCCVPIYHVLSWGVPL-AAFMSGTpLVFPGPDLSAPTLAKIIATAMPRVAH 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 263 GVPTMYNYLFQHENGKKDDFSSIRLCISGGAAMPVALLTAFEEKFGVTILEGYGLSEASPV-TCFNP------------- 328
Cdd:PRK05620 278 GVPTLWIQLMVHYLKNPPERMSLQEIYVGGSAVPPILIKAWEERYGVDVVHVWGMTETSPVgTVARPpsgvsgearwayr 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 329 FDRGRKPGSIgtsilhvENKVVDPlGRELPAH--QVGELIVKGPNVMKGYYKMPMETEHAL-----------------KD 389
Cdd:PRK05620 358 VSQGRFPASL-------EYRIVND-GQVMESTdrNEGEIQVRGNWVTASYYHSPTEEGGGAastfrgedvedandrftAD 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 390 GWLYTGDLARRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVV----PKRSG 465
Cdd:PRK05620 430 GWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLAVTVlapgIEPTR 509
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1816047872 466 VTEEDIMQHCETHLAKYKRPAAITFLDDIPKNATGKM----LRRALRD 509
Cdd:PRK05620 510 ETAERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFdkkdLRQHLAD 557
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
7-507 |
5.72e-54 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 197.10 E-value: 5.72e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 7 LEETASEKPDSIACRFKDHMMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYT 86
Cdd:PRK12316 4557 VAERARMTPDAVAVVFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYP 4636
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 87 PTEIGYMLTNGDVKAIVGVSQLLPlyecmheSLP---KVELVILCQTGEAEP-EAADPEVRmkmttfakilrptsaakqn 162
Cdd:PRK12316 4637 RERLAYMMEDSGAALLLTQSHLLQ-------RLPipdGLASLALDRDEDWEGfPAHDPAVR------------------- 4690
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 163 qeLVPDDTAVILYTSGTTGKPKGAMLTHQNLYSNANDVAGYLGMDERDNVVCALPM-FHVFCLTvcMNAPLMSGATVLIE 241
Cdd:PRK12316 4691 --LHPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSFsFDGSHEG--LYHPLINGASVVIR 4766
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 242 P--QFSPASVFKLVKQQQVTIFAGVPTMYNYLFQHENgKKDDFSSIRLCISGGAAMPVALLT-AFEEKFGVTILEGYGLS 318
Cdd:PRK12316 4767 DdsLWDPERLYAEIHEHRVTVLVFPPVYLQQLAEHAE-RDGEPPSLRVYCFGGEAVAQASYDlAWRALKPVYLFNGYGPT 4845
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 319 EASPV----TCFNPFDRGRKPGSIGTSILHVENKVVDPLGRELPAHQVGELIVKGPNVMKGYYKMPMET-EHALKD---- 389
Cdd:PRK12316 4846 ETTVTvllwKARDGDACGAAYMPIGTPLGNRSGYVLDGQLNPLPVGVAGELYLGGEGVARGYLERPALTaERFVPDpfga 4925
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 390 --GWLY-TGDLARRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPqSGEAVKGYVVPKRSGV 466
Cdd:PRK12316 4926 pgGRLYrTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGA-VGKQLVGYVVPQDPAL 5004
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1816047872 467 TEEDIMQ---------HCETHLAKYKRPAAITFLDDIPKNATGKMLRRAL 507
Cdd:PRK12316 5005 ADADEAQaelrdelkaALRERLPEYMVPAHLVFLARMPLTPNGKLDRKAL 5054
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
7-511 |
8.46e-54 |
|
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: 188.52 E-value: 8.46e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 7 LEETASEKPDSIACRFKDHMMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYT 86
Cdd:cd05918 5 IEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLDPSHP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 87 PTEIGYMLTngDVKAIVgvsqllplyecmheslpkvelvILCQTgeaepeaadpevrmkmttfakilrptsaakqnqelv 166
Cdd:cd05918 85 LQRLQEILQ--DTGAKV----------------------VLTSS------------------------------------ 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 167 PDDTAVILYTSGTTGKPKGAMLTHQNLYSNANDVAGYLGMDERDNVVC-ALPMFHVFCLTVCMnaPLMSGATVLIEPQFS 245
Cdd:cd05918 105 PSDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRALGLTSESRVLQfASYTFDVSILEIFT--TLAAGGCLCIPSEED 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 246 -PASVFKLVKQQQVTiFAG-VPTMYNYLfqhengKKDDFSSIRLCISGGAAMPVALLTAFEEKfgVTILEGYGLSEASPV 323
Cdd:cd05918 183 rLNDLAGFINRLRVT-WAFlTPSVARLL------DPEDVPSLRTLVLGGEALTQSDVDTWADR--VRLINAYGPAECTIA 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 324 TCFNPFDRGRKPGSIGTSI---LHVenkvVDPL--GRELPAHQVGELIVKGPNVMKGYYKMPMET-------------EH 385
Cdd:cd05918 254 ATVSPVVPSTDPRNIGRPLgatCWV----VDPDnhDRLVPIGAVGELLIEGPILARGYLNDPEKTaaafiedpawlkqEG 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 386 ALKDGWLY-TGDLARRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVK---GYVVP 461
Cdd:cd05918 330 SGRGRRLYrTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSLPGAKEVVVEVVKPKDGSSSPqlvAFVVL 409
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1816047872 462 KRSGVTEED------------------IMQHCETHLAKYKRPAAITFLDDIPKNATGKMLRRALRDIL 511
Cdd:cd05918 410 DGSSSGSGDgdslflepsdefralvaeLRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRALRELA 477
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
7-508 |
1.11e-53 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 190.01 E-value: 1.11e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 7 LEETASEKPDSIACRFKDHMMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYT 86
Cdd:PLN02860 13 LTRLATLRGNAVVTISGNRRRTGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 87 PTEIGY-MLTNGDVKAIV--GVSQLLPlyECMHESLPKVELVILCQ--TGEAEPEAAD---PEVRMKMTTFAKILRPTSA 158
Cdd:PLN02860 93 FEEAKSaMLLVRPVMLVTdeTCSSWYE--ELQNDRLPSLMWQVFLEspSSSVFIFLNSfltTEMLKQRALGTTELDYAWA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 159 akqnqelvPDDTAVILYTSGTTGKPKGAMLTH-----QNLYSNAndVAGYlgmDERDNVVCALPMFHVFCLTVCMnAPLM 233
Cdd:PLN02860 171 --------PDDAVLICFTSGTTGRPKGVTISHsalivQSLAKIA--IVGY---GEDDVYLHTAPLCHIGGLSSAL-AMLM 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 234 SGATVLIEPQFSPASVFKLVKQQQVTIFAGVPTMYNYLFQHENGKKDD--FSSIRLCISGGAAMPVALLTAFEEKF-GVT 310
Cdd:PLN02860 237 VGACHVLLPKFDAKAALQAIKQHNVTSMITVPAMMADLISLTRKSMTWkvFPSVRKILNGGGSLSSRLLPDAKKLFpNAK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 311 ILEGYGLSEA---------------SPVTCFNPFDRgRKPGS--------IGTSILHVENKVvdplGRELPAHqVGELIV 367
Cdd:PLN02860 317 LFSAYGMTEAcssltfmtlhdptleSPKQTLQTVNQ-TKSSSvhqpqgvcVGKPAPHVELKI----GLDESSR-VGRILT 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 368 KGPNVMKGYYKMPMETEHAL-KDGWLYTGDLARRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGV 446
Cdd:PLN02860 391 RGPHVMLGYWGQNSETASVLsNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGV 470
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1816047872 447 PDPQSGEAVKGYV------------VPKRSG---VTEEDIMQHC-ETHLAKYKRPAAIT-FLDDIPKNATGKMLRRALR 508
Cdd:PLN02860 471 PDSRLTEMVVACVrlrdgwiwsdneKENAKKnltLSSETLRHHCrEKNLSRFKIPKLFVqWRKPFPLTTTGKIRRDEVR 549
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
8-509 |
2.21e-53 |
|
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: 186.36 E-value: 2.21e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 8 EETASEKPDSIACRFKDHMMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYTP 87
Cdd:cd17653 4 ERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 88 TEIGYMLTngdvkaivgvsqllplyecmheslpkvelvilcqtgeaepeaadpevrmkmTTFAKILRPTSAakqnqelvP 167
Cdd:cd17653 84 ARIQAILR---------------------------------------------------TSGATLLLTTDS--------P 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 168 DDTAVILYTSGTTGKPKGAMLTHQNL-----YSNANDVAGY---------LGMDerdnvVCALPMFhvfcltvcmnAPLM 233
Cdd:cd17653 105 DDLAYIIFTSGSTGIPKGVMVPHRGVlnyvsQPPARLDVGPgsrvaqvlsIAFD-----ACIGEIF----------STLC 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 234 SGAT-VLIEPQFSPASVFKlvkqqQVTIFAGVPTMYNYLfqhengKKDDFSSIRLCISGGAAMPVALLTAFeeKFGVTIL 312
Cdd:cd17653 170 NGGTlVLADPSDPFAHVAR-----TVDALMSTPSILSTL------SPQDFPNLKTIFLGGEAVPPSLLDRW--SPGRRLY 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 313 EGYGLSEASpVTCFNPFDRGRKPGSIGTSILHVENKVVDPLGRELPAHQVGELIVKGPNVMKGYYKMPMET-----EHAL 387
Cdd:cd17653 237 NAYGPTECT-ISSTMTELLPGQPVTIGKPIPNSTCYILDADLQPVPEGVVGEICISGVQVARGYLGNPALTaskfvPDPF 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 388 KDGW-LY-TGDLARRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLY-SHPDVKEAVVVgvpdpQSGEAVKGYVVPkrS 464
Cdd:cd17653 316 WPGSrMYrTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEVVLqSQPEVTQAAAI-----VVNGRLVAFVTP--E 388
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1816047872 465 GVTEEDIMQHCETHLAKYKRPAAITFLDDIPKNATGKMLRRALRD 509
Cdd:cd17653 389 TVDVDGLRSELAKHLPSYAVPDRIIALDSFPLTANGKVDRKALRE 433
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
6-507 |
2.78e-53 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 194.79 E-value: 2.78e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 6 KLEETASEKPDSIACRFKDHMMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLY 85
Cdd:PRK12316 2008 RIAEQAARAPEAIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNY 2087
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 86 tPTE-IGYMLTNGDVKAIV---GVSQLLPLyecmHESLPKVELvilcqtgEAEPEAADpevrmkmttfakilRPTSAAkQ 161
Cdd:PRK12316 2088 -PAErLAYMLEDSGAALLLtqrHLLERLPL----PAGVARLPL-------DRDAEWAD--------------YPDTAP-A 2140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 162 NQeLVPDDTAVILYTSGTTGKPKGAMLTHQNLYSNANDVAGYLGMDERDNVVCALPM----FHVFCLTvcmnaPLMSGAT 237
Cdd:PRK12316 2141 VQ-LAGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPADCELQFMSFsfdgAHEQWFH-----PLLNGAR 2214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 238 VLIEP--QFSPASVFKLVKQQQVTIFAGVPTMYNYLFQHE--NGKKddfSSIRLCISGGAAMPVALLTAFEEKF-GVTIL 312
Cdd:PRK12316 2215 VLIRDdeLWDPEQLYDEMERHGVTILDFPPVYLQQLAEHAerDGRP---PAVRVYCFGGEAVPAASLRLAWEALrPVYLF 2291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 313 EGYGLSEASPV----TCFNPFDRGRKPGSIGTSILHVENKVVDPLGRELPAHQVGELIVKGPNVMKGYYKMPMET-EHAL 387
Cdd:PRK12316 2292 NGYGPTEAVVTpllwKCRPQDPCGAAYVPIGRALGNRRAYILDADLNLLAPGMAGELYLGGEGLARGYLNRPGLTaERFV 2371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 388 KD------GWLY-TGDLARRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVpDPQSGEAVKGYVV 460
Cdd:PRK12316 2372 PDpfsasgERLYrTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQ-DGASGKQLVAYVV 2450
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1816047872 461 PKRSGVTE-EDIMQHCETHLAKYKRPAAITFLDDIPKNATGKMLRRAL 507
Cdd:PRK12316 2451 PDDAAEDLlAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKAL 2498
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
1-508 |
6.08e-53 |
|
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: 188.85 E-value: 6.08e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 1 MNLVSKLEET-ASEKPDSIACRFKDH-----MMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKA 74
Cdd:cd05968 60 MNIVEQLLDKwLADTRTRPALRWEGEdgtsrTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARI 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 75 GIVVVPINPLYTPTEIGYMLTNGDVKAIV---GVSQ------LLPLYECMHESLPKVELVILCQTGEAEPEAAdpEVRMK 145
Cdd:cd05968 140 GGIVVPIFSGFGKEAAATRLQDAEAKALItadGFTRrgrevnLKEEADKACAQCPTVEKVVVVRHLGNDFTPA--KGRDL 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 146 MTTFAKILRPTSAAKQNqelvPDDTAVILYTSGTTGKPKGAMLTHQNL-YSNANDVagYLGMDERdnvvcalPMFHVFCL 224
Cdd:cd05968 218 SYDEEKETAGDGAERTE----SEDPLMIIYTSGTTGKPKGTVHVHAGFpLKAAQDM--YFQFDLK-------PGDLLTWF 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 225 TVC--MNAP------LMSGATVLI---EPQF-SPASVFKLVKQQQVTIFAGVPTMYNYLFQH--ENGKKDDFSSIRLCIS 290
Cdd:cd05968 285 TDLgwMMGPwlifggLILGATMVLydgAPDHpKADRLWRMVEDHEITHLGLSPTLIRALKPRgdAPVNAHDLSSLRVLGS 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 291 GGAAM-PVALLTAFEEKFG--VTILEGYGLSEASPVTCFNPFDRGRKPGSIGTSILHVENKVVDPLGRELPAhQVGELIV 367
Cdd:cd05968 365 TGEPWnPEPWNWLFETVGKgrNPIINYSGGTEISGGILGNVLIKPIKPSSFNGPVPGMKADVLDESGKPARP-EVGELVL 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 368 KGP--NVMKGYYKMP---METEHALKDGWLYTGDLARRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAV 442
Cdd:cd05968 444 LAPwpGMTRGFWRDEdryLETYWSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESA 523
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 443 VVGVPDPQSGEAVKGYVVPK----RSGVTEEDIMQHCETHLAKYKRPAAITFLDDIPKNATGKMLRRALR 508
Cdd:cd05968 524 AIGVPHPVKGEAIVCFVVLKpgvtPTEALAEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIR 593
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
7-510 |
1.10e-50 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 187.29 E-value: 1.10e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 7 LEETASEKPDSIACRFKDHMMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYT 86
Cdd:PRK12467 3101 IEAQVARTPEAPALVFGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYP 3180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 87 PTEIGYMLTNGDVKAIVGVSQLLPlyecmHESLPKVELVILCQTGEAEPEA-ADPEVRmkmttfakilrptsaakqnqeL 165
Cdd:PRK12467 3181 RERLAYMIEDSGVKLLLTQAHLLE-----QLPAPAGDTALTLDRLDLNGYSeNNPSTR---------------------V 3234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 166 VPDDTAVILYTSGTTGKPKGAMLTHQNLYSNANDVAGYLGMDERDNVVcaLPMFHVFCLTVC-MNAPLMSGATVLIEP-- 242
Cdd:PRK12467 3235 MGENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDRVL--LFMSFSFDGAQErFLWTLICGGCLVVRDnd 3312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 243 QFSPASVFKLVKQQQVTIFAGVPTMYNYLFQHENGKkdDFSSIRLCISGGAAMPVALLTAFEEKFG-VTILEGYGLSEAS 321
Cdd:PRK12467 3313 LWDPEELWQAIHAHRISIACFPPAYLQQFAEDAGGA--DCASLDIYVFGGEAVPPAAFEQVKRKLKpRGLTNGYGPTEAV 3390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 322 PVTCFNPFDRGRKPGS----IGTSILHVENKVVDPLGRELPAHQVGELIVKGPNVMKGYYKMPMET-EHALKD------G 390
Cdd:PRK12467 3391 VTVTLWKCGGDAVCEApyapIGRPVAGRSIYVLDGQLNPVPVGVAGELYIGGVGLARGYHQRPSLTaERFVADpfsgsgG 3470
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 391 WLY-TGDLARRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVpDPQSGEAVKGYVVPK-RSGVTE 468
Cdd:PRK12467 3471 RLYrTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLAR-DGAGGKQLVAYVVPAdPQGDWR 3549
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1816047872 469 EDIMQHCETHLAKYKRPAAITFLDDIPKNATGKMLRRALRDI 510
Cdd:PRK12467 3550 ETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKALPDP 3591
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
141-501 |
1.75e-50 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 185.94 E-value: 1.75e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 141 EVRMKMTTFAKIL------RPTSAAKQNQelvPDDTAVILYTSGTTGKPKGAMLTHQNLYSNANDVAGYLGMDERDNVVC 214
Cdd:PRK06814 763 DVRAQIGLADKIKgllagrFPLVYFCNRD---PDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARIDFSPEDKVFN 839
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 215 ALPMFHVFCLTVCMNAPLMSGATVLIEPqfSP---ASVFKLVKQQQVTIFAGVPTMYN--------YlfqhengkkdDFS 283
Cdd:PRK06814 840 ALPVFHSFGLTGGLVLPLLSGVKVFLYP--SPlhyRIIPELIYDTNATILFGTDTFLNgyaryahpY----------DFR 907
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 284 SIRLCISGGAAMPVALLTAFEEKFGVTILEGYGLSEASPVTCFN-P-FDRgrkPGSIGTSILHVENKVVDPLGRElpahQ 361
Cdd:PRK06814 908 SLRYVFAGAEKVKEETRQTWMEKFGIRILEGYGVTETAPVIALNtPmHNK---AGTVGRLLPGIEYRLEPVPGID----E 980
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 362 VGELIVKGPNVMKGYYKmpMETEHALK---DGWLYTGDLARRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEvLYSH--P 436
Cdd:PRK06814 981 GGRLFVRGPNVMLGYLR--AENPGVLEppaDGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEE-LAAElwP 1057
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1816047872 437 DVKEAvVVGVPDPQSGEAVkgYVVPKRSGVTEEDIMQHCETH-LAKYKRPAAITFLDDIPKNATGK 501
Cdd:PRK06814 1058 DALHA-AVSIPDARKGERI--ILLTTASDATRAAFLAHAKAAgASELMVPAEIITIDEIPLLGTGK 1120
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
28-510 |
2.10e-50 |
|
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: 182.13 E-value: 2.10e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 28 TYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYTPTEIGYMLTNGDVKAIVGVS- 106
Cdd:cd05967 84 TYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGFAAKELASRIDDAKPKLIVTASc 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 107 -----QLLPLYECMHESLP----KVELVILCQTGEAEPEAADPEVRMKMTTFAKILRPTsaakqnqELVP---DDTAVIL 174
Cdd:cd05967 164 giepgKVVPYKPLLDKALElsghKPHHVLVLNRPQVPADLTKPGRDLDWSELLAKAEPV-------DCVPvaaTDPLYIL 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 175 YTSGTTGKPKGAMlthqnlysnaNDVAGYL-----------GMDERDNVVCALPMFHVFCLTVCMNAPLMSGAT-VLIE- 241
Cdd:cd05967 237 YTSGTTGKPKGVV----------RDNGGHAvalnwsmrniyGIKPGDVWWAASDVGWVVGHSYIVYGPLLHGATtVLYEg 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 242 -PQFSP-ASVF-KLVKQQQVTIFAGVPTMYNYLFQH----ENGKKDDFSSIRLCISGGAAMPVALLTAFEEKFGVTILEG 314
Cdd:cd05967 307 kPVGTPdPGAFwRVIEKYQVNALFTAPTAIRAIRKEdpdgKYIKKYDLSSLRTLFLAGERLDPPTLEWAENTLGVPVIDH 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 315 YGLSEA-SPVTCfNPF---DRGRKPGSIGTSILHVENKVVDPLGRELPAHQVGELIVKGP---NVMKGYYKMPMETEH-- 385
Cdd:cd05967 387 WWQTETgWPITA-NPVglePLPIKAGSPGKPVPGYQVQVLDEDGEPVGPNELGNIVIKLPlppGCLLTLWKNDERFKKly 465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 386 -ALKDGWLYTGDLARRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVVPKRS 464
Cdd:cd05967 466 lSKFPGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELKGQVPLGLVVLKEG 545
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1816047872 465 G-VTEED----IMQHCETHLAKYKRPAAITFLDDIPKNATGKMLRRALRDI 510
Cdd:cd05967 546 VkITAEElekeLVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTLRKI 596
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
2-512 |
3.96e-50 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 182.92 E-value: 3.96e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 2 NLVSKLEETASE-----KPdsiaCRFKDHMMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGI 76
Cdd:PRK06060 5 NLAGLLAEQASEagwydRP----AFYAADVVTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 77 VVVPINP-LYTP--------TEIGYMLTNGDVKAIVGVSQLLPLYEcmheslpkvelvILCQTGEAEPeaADPEVrmkmt 147
Cdd:PRK06060 81 MAFLANPeLHRDdhalaarnTEPALVVTSDALRDRFQPSRVAEAAE------------LMSEAARVAP--GGYEP----- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 148 tfakilrptsaakqnqeLVPDDTAVILYTSGTTGKPKGAMLTHQNLYSNANDVA-GYLGMDERDNVVCALPMFHVFCLTV 226
Cdd:PRK06060 142 -----------------MGGDALAYATYTSGTTGPPKAAIHRHADPLTFVDAMCrKALRLTPEDTGLCSARMYFAYGLGN 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 227 CMNAPLMSGATVLIEP-QFSPASVFKLVKQQQVTIFAGVPTMYNYLFqhENGKKDDFSSIRLCISGGAAMPVALLTAFEE 305
Cdd:PRK06060 205 SVWFPLATGGSAVINSaPVTPEAAAILSARFGPSVLYGVPNFFARVI--DSCSPDSFRSLRCVVSAGEALELGLAERLME 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 306 KFG-VTILEGYGLSEASPVTCFNPFDRGRkPGSIGTSILHVENKVVDPLGRELPAHQVGELIVKGPNVMKGYYKMPmetE 384
Cdd:PRK06060 283 FFGgIPILDGIGSTEVGQTFVSNRVDEWR-LGTLGRVLPPYEIRVVAPDGTTAGPGVEGDLWVRGPAIAKGYWNRP---D 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 385 HALKD-GWLYTGDLARRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVVPKR 463
Cdd:PRK06060 359 SPVANeGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATS 438
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1816047872 464 SGVTEEDIMQHCE----THLAKYKRPAAITFLDDIPKNATGKMLRRALRDILP 512
Cdd:PRK06060 439 GATIDGSVMRDLHrgllNRLSAFKVPHRFAVVDRLPRTPNGKLVRGALRKQSP 491
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
15-507 |
5.95e-50 |
|
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: 177.59 E-value: 5.95e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 15 PDSIACRFKDHMMTYQELNEHIQRFADGLQEAGMEKGDHL-ALLLGNSPDFIIAFFGALKAGIVVVPINPLYTPTEIGYM 93
Cdd:cd17648 1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAEIRPDDLvGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 94 LtnGDVKAivgvsqllplyecmheslpkvelvilcqtgeaepeaadpevRMKMTTfakilrptsaakqnqelvPDDTAVI 173
Cdd:cd17648 81 L--EDTGA-----------------------------------------RVVITN------------------STDLAYA 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 174 LYTSGTTGKPKGAMLTHQNLYSNANDVAG-YLGMDERDNVVCALP--MFHVFCLTVCMNapLMSGATVLIEPQ---FSPA 247
Cdd:cd17648 100 IYTSGTTGKPKGVLVEHGSVVNLRTSLSErYFGRDNGDEAVLFFSnyVFDFFVEQMTLA--LLNGQKLVVPPDemrFDPD 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 248 SVFKLVKQQQVTIFAGVPTMynyLFQHENGKKDdfsSIRLCISGGAAMPVALLTAFEEKFGVTILEGYGLSEASpVTC-- 325
Cdd:cd17648 178 RFYAYINREKVTYLSGTPSV---LQQYDLARLP---HLKRVDAAGEEFTAPVFEKLRSRFAGLIINAYGPTETT-VTNhk 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 326 -FNPFDRgRKPGSIGTSILHVENKVVDPLGRELPAHQVGELIVKGPNVMKGYYKM-----------PMETEHALKDG--- 390
Cdd:cd17648 251 rFFPGDQ-RFDKSLGRPVRNTKCYVLNDAMKRVPVGAVGELYLGGDGVARGYLNRpeltaerflpnPFQTEQERARGrna 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 391 WLY-TGDLARRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVK-----GYVVPKRS 464
Cdd:cd17648 330 RLYkTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAKEDASQAQSRIqkylvGYYLPEPG 409
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1816047872 465 GVTEEDIMQHCETHLAKYKRPAAITFLDDIPKNATGKMLRRAL 507
Cdd:cd17648 410 HVPESDLLSFLRAKLPRYMVPARLVRLEGIPVTINGKLDVRAL 452
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
28-510 |
1.32e-49 |
|
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: 179.68 E-value: 1.32e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 28 TYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYTPTEIGYMLTNGDVKAIVGVSQ 107
Cdd:cd05966 86 TYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFAGFSAESLADRINDAQCKLVITADG 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 108 ------LLPLYECMHESL---PKVELVILC-----------------------QTGEAEPEAADPEvrmkmttfakilrp 155
Cdd:cd05966 166 gyrggkVIPLKEIVDEALekcPSVEKVLVVkrtggevpmtegrdlwwhdlmakQSPECEPEWMDSE-------------- 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 156 tsaakqnqelvpdDTAVILYTSGTTGKPKGAMLTHqnlysnandvAGYLgmderdnVVCALPMFHVFCLT-----VCMN- 229
Cdd:cd05966 232 -------------DPLFILYTSGSTGKPKGVVHTT----------GGYL-------LYAATTFKYVFDYHpddiyWCTAd 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 230 ------------APLMSGATVLI-E--PQFSPASVF-KLVKQQQVTIFAGVPTMYNYLFQHENG--KKDDFSSIRLCISG 291
Cdd:cd05966 282 igwitghsyivyGPLANGATTVMfEgtPTYPDPGRYwDIVEKHKVTIFYTAPTAIRALMKFGDEwvKKHDLSSLRVLGSV 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 292 GAAM-PVALLTaFEEKFG---VTILEGYGLSEA-----SPVtcfnPFDRGRKPGSIGTSILHVENKVVDPLGRELPAHQV 362
Cdd:cd05966 362 GEPInPEAWMW-YYEVIGkerCPIVDTWWQTETggimiTPL----PGATPLKPGSATRPFFGIEPAILDEEGNEVEGEVE 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 363 GELIVKG--PNVMKGYYKMP---METEHALKDGWLYTGDLARRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPD 437
Cdd:cd05966 437 GYLVIKRpwPGMARTIYGDHeryEDTYFSKFPGYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPA 516
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1816047872 438 VKEAVVVGVPDPQSGEAVKGYVVPK----RSGVTEEDIMQHCETHLAKYKRPAAITFLDDIPKNATGKMLRRALRDI 510
Cdd:cd05966 517 VAEAAVVGRPHDIKGEAIYAFVTLKdgeePSDELRKELRKHVRKEIGPIATPDKIQFVPGLPKTRSGKIMRRILRKI 593
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
2-507 |
1.79e-49 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 177.88 E-value: 1.79e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 2 NLVSKLEETASEKPDSIACRFKDHMMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPI 81
Cdd:PRK13383 36 NPYTLLAVTAARWPGRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPI 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 82 NPLYTPTEIGYMLTNGDVKAIVGVSQLLPLYECMHESLpkveLVILCQTGEAEPEAAdpevrmkmttfakilRPTSAAKQ 161
Cdd:PRK13383 116 STEFRSDALAAALRAHHISTVVADNEFAERIAGADDAV----AVIDPATAGAEESGG---------------RPAVAAPG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 162 NqelvpddtaVILYTSGTTGKPKGAMLTHQNlysnANDVAGYLGMDER------DNVVCALPMFHVFCLTVCMnAPLMSG 235
Cdd:PRK13383 177 R---------IVLLTSGTTGKPKGVPRAPQL----RSAVGVWVTILDRtrlrtgSRISVAMPMFHGLGLGMLM-LTIALG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 236 ATVLIEPQFSPASVFKLVKQQQVTIFAGVPTMYNYLFQ--HENGKKDDFSSIRLCISGGAAMPVALLTAFEEKFGVTILE 313
Cdd:PRK13383 243 GTVLTHRHFDAEAALAQASLHRADAFTAVPVVLARILElpPRVRARNPLPQLRVVMSSGDRLDPTLGQRFMDTYGDILYN 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 314 GYGLSEASPVTCFNPFDRGRKPGSIGTSILHVENKVVDPLGRELPAHQVGELIVKGPNVMKGYYKmpmETEHALKDGWLY 393
Cdd:PRK13383 323 GYGSTEVGIGALATPADLRDAPETVGKPVAGCPVRILDRNNRPVGPRVTGRIFVGGELAGTRYTD---GGGKAVVDGMTS 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 394 TGDLARRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVVPKR-SGVTEEDIM 472
Cdd:PRK13383 400 TGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPgSGVDAAQLR 479
|
490 500 510
....*....|....*....|....*....|....*
gi 1816047872 473 QHCETHLAKYKRPAAITFLDDIPKNATGKMLRRAL 507
Cdd:PRK13383 480 DYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
15-507 |
2.98e-49 |
|
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: 176.13 E-value: 2.98e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 15 PDSIACRFKDHMMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYTPTEIGYML 94
Cdd:cd17656 2 PDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 95 TNGDVKAIVgvsqllplyECMHESLPkvelviLCQTGEAE-PEaaDPEVRMKmttfakilrptSAAKQNQELVPDDTAVI 173
Cdd:cd17656 82 LDSGVRVVL---------TQRHLKSK------LSFNKSTIlLE--DPSISQE-----------DTSNIDYINNSDDLLYI 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 174 LYTSGTTGKPKGAMLTHQNLYSNANDVAGYLGMDERDNVVcalpMFHVFCLTVCMN---APLMSGATVLIEPQFSPASV- 249
Cdd:cd17656 134 IYTSGTTGKPKGVQLEHKNMVNLLHFEREKTNINFSDKVL----QFATCSFDVCYQeifSTLLSGGTLYIIREETKRDVe 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 250 --FKLVKQQQVTIfAGVPTMYNYLFQHENGKKDDF-SSIRLCISGGAAMPVA-LLTAFEEKFGVTILEGYGLSEASPVTC 325
Cdd:cd17656 210 qlFDLVKRHNIEV-VFLPVAFLKFIFSEREFINRFpTCVKHIITAGEQLVITnEFKEMLHEHNVHLHNHYGPSETHVVTT 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 326 --FNPFDRGRKPGSIGTSILHVENKVVDPLGRELPAHQVGELIVKGPNVMKGYYKMP-METEHALKDGW-----LY-TGD 396
Cdd:cd17656 289 ytINPEAEIPELPPIGKPISNTWIYILDQEQQLQPQGIVGELYISGASVARGYLNRQeLTAEKFFPDPFdpnerMYrTGD 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 397 LARRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVVPKRSgVTEEDIMQHCE 476
Cdd:cd17656 369 LARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFVMEQE-LNISQLREYLA 447
|
490 500 510
....*....|....*....|....*....|.
gi 1816047872 477 THLAKYKRPAAITFLDDIPKNATGKMLRRAL 507
Cdd:cd17656 448 KQLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
3-507 |
6.91e-49 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 176.74 E-value: 6.91e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 3 LVSKLEETASEKPDSIACRFKD--HMMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVP 80
Cdd:PRK05857 16 VLDRVFEQARQQPEAIALRRCDgtSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 81 INPLYTPTEIGYMLTNGDVKAIvgvsqlLPLYECM--HESLPkvelvilcqtgeaEPEAADPEVRMKMTTFAKILRP--- 155
Cdd:PRK05857 96 ADGNLPIAAIERFCQITDPAAA------LVAPGSKmaSSAVP-------------EALHSIPVIAVDIAAVTRESEHsld 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 156 TSAAKQNQELVPDDTAVILYTSGTTGKPKGAMLTHQNLYSnANDVAGYLGMDERDNVV-----CALPMFHVFCLTVCMNA 230
Cdd:PRK05857 157 AASLAGNADQGSEDPLAMIFTSGTTGEPKAVLLANRTFFA-VPDILQKEGLNWVTWVVgettySPLPATHIGGLWWILTC 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 231 pLMSGATVLIEPQFSpASVFKLVKQQQVTIFAGVPTMYNYLFQHENGKKDDFSSIRLCISGGAAMpVALLTAFEEKFGVT 310
Cdd:PRK05857 236 -LMHGGLCVTGGENT-TSLLEILTTNAVATTCLVPTLLSKLVSELKSANATVPSLRLVGYGGSRA-IAADVRFIEATGVR 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 311 ILEGYGLSEASPVTCFNPFDRGR----KPGSIGTSILHVENKVVDPLG------RELPAHQVGELIVKGPNVMKGYYKMP 380
Cdd:PRK05857 313 TAQVYGLSETGCTALCLPTDDGSivkiEAGAVGRPYPGVDVYLAATDGigptapGAGPSASFGTLWIKSPANMLGYWNNP 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 381 METEHALKDGWLYTGDLARRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVV 460
Cdd:PRK05857 393 ERTAEVLIDGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGALVGLAVV 472
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1816047872 461 PKrSGVTEEDIMQHCETHLAKYK-------RPAAITFLDDIPKNATGKMLRRAL 507
Cdd:PRK05857 473 AS-AELDESAARALKHTIAARFRresepmaRPSTIVIVTDIPRTQSGKVMRASL 525
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
14-513 |
1.76e-48 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 175.18 E-value: 1.76e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 14 KPDSIACRFKDHMMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGivVVPINPLYT--PTEIG 91
Cdd:PRK10946 36 ASDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLG--VAPVNALFShqRSELN 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 92 YMLTNGDVKAIVGVSQLlPLY------ECMHESLPKVELVILcqTGEAEPEAADPEVRMKMTTFakILRPTSAakqnqel 165
Cdd:PRK10946 114 AYASQIEPALLIADRQH-ALFsdddflNTLVAEHSSLRVVLL--LNDDGEHSLDDAINHPAEDF--TATPSPA------- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 166 vpDDTAVILYTSGTTGKPKGAMLTHQNLYSNANDVAGYLGMDERDNVVCALPMFHVFCltvcMNAP-----LMSGATVLI 240
Cdd:PRK10946 182 --DEVAFFQLSGGSTGTPKLIPRTHNDYYYSVRRSVEICGFTPQTRYLCALPAAHNYP----MSSPgalgvFLAGGTVVL 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 241 EPQFSPASVFKLVKQQQVTIFAGVPTMYNYLFQH--ENGKKDDFSSIRLCISGGAAMPVALLTAFEEKFGVTILEGYGLS 318
Cdd:PRK10946 256 APDPSATLCFPLIEKHQVNVTALVPPAVSLWLQAiaEGGSRAQLASLKLLQVGGARLSETLARRIPAELGCQLQQVFGMA 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 319 EA---------SPVTCFNPFDRGRKPGSigtsilhvENKVVDPLGRELPAHQVGELIVKGPNVMKGYYKMPMETEHAL-K 388
Cdd:PRK10946 336 EGlvnytrlddSDERIFTTQGRPMSPDD--------EVWVADADGNPLPQGEVGRLMTRGPYTFRGYYKSPQHNASAFdA 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 389 DGWLYTGDLARRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVVPkRSGVTE 468
Cdd:PRK10946 408 NGFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAFLVV-KEPLKA 486
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1816047872 469 EDIMQHC-ETHLAKYKRPAAITFLDDIPKNATGKMLRRALRDILPQ 513
Cdd:PRK10946 487 VQLRRFLrEQGIAEFKLPDRVECVDSLPLTAVGKVDKKQLRQWLAS 532
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
1-503 |
3.81e-48 |
|
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: 175.46 E-value: 3.81e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 1 MNLVSK-LEETASEKPDSIACRFKDHM------MTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALK 73
Cdd:cd17634 52 LNLAANaLDRHLRENGDRTAIIYEGDDtsqsrtISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACAR 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 74 AGIVVVPINPLYTPTEIGYMLTNGDVKAIVGVS------QLLPLYECMHESL----PKVELVILCQTGEAE---PEAADP 140
Cdd:cd17634 132 IGAVHSVIFGGFAPEAVAGRIIDSSSRLLITADggvragRSVPLKKNVDDALnpnvTSVEHVIVLKRTGSDidwQEGRDL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 141 EVRMKMTTfakilrpTSAAKQNQELVPDDTAVILYTSGTTGKPKGAMLTHQN-LYSNANDVAGYLGMDERDNVVCALPMF 219
Cdd:cd17634 212 WWRDLIAK-------ASPEHQPEAMNAEDPLFILYTSGTTGKPKGVLHTTGGyLVYAATTMKYVFDYGPGDIYWCTADVG 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 220 HVFCLTVCMNAPLMSGATVLI---EPQF-SPASVFKLVKQQQVTIFAGVPTMYNYLFQHENG--KKDDFSSIRLCISGGA 293
Cdd:cd17634 285 WVTGHSYLLYGPLACGATTLLyegVPNWpTPARMWQVVDKHGVNILYTAPTAIRALMAAGDDaiEGTDRSSLRILGSVGE 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 294 AM---PVALLTAFEEKFGVTILEGYGLSEASPVTCFN-PFDRGRKPGSIGTSILHVENKVVDPLGRELPAHQVGELIVKG 369
Cdd:cd17634 365 PInpeAYEWYWKKIGKEKCPVVDTWWQTETGGFMITPlPGAIELKAGSATRPVFGVQPAVVDNEGHPQPGGTEGNLVITD 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 370 --PNVMKGYYKMP---METEHALKDGWLYTGDLARRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVV 444
Cdd:cd17634 445 pwPGQTRTLFGDHerfEQTYFSTFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVV 524
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1816047872 445 GVPDPQSGEAVKGYVVpKRSGVTEED-----IMQHCETHLAKYKRPAAITFLDDIPKNATGKML 503
Cdd:cd17634 525 GIPHAIKGQAPYAYVV-LNHGVEPSPelyaeLRNWVRKEIGPLATPDVVHWVDSLPKTRSGKIM 587
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
24-508 |
5.79e-48 |
|
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: 172.15 E-value: 5.79e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 24 DHMMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINplytpteigYMLTngdvkaiv 103
Cdd:cd05940 1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALIN---------YNLR-------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 104 gvsqLLPLYECMHESLPKVELVilcqtgeaepeaadpevrmkmttfakilrptsaakqnqelvpdDTAVILYTSGTTGKP 183
Cdd:cd05940 64 ----GESLAHCLNVSSAKHLVV-------------------------------------------DAALYIYTSGTTGLP 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 184 KGAMLTHQNLYSNANDVAGYLGMDERDNVVCALPMFHVFCLTVCMNAPLMSGATVLIEPQFSPASVFKLVKQQQVTIFAG 263
Cdd:cd05940 97 KAAIISHRRAWRGGAFFAGSGGALPSDVLYTCLPLYHSTALIVGWSACLASGATLVIRKKFSASNFWDDIRKYQATIFQY 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 264 VPTMYNYLF---QHENGKKddfSSIRlCISGGAAMPvALLTAFEEKFGV-TILEGYGLSEASpvtcFNPFDRGRKPGSIG 339
Cdd:cd05940 177 IGELCRYLLnqpPKPTERK---HKVR-MIFGNGLRP-DIWEEFKERFGVpRIAEFYAATEGN----SGFINFFGKPGAIG 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 340 ----TSILHVENKVV-----------DPLGR--ELPAHQVGELI--VKGPNVMKGYYKmPMETEH-----ALKDG--WLY 393
Cdd:cd05940 248 rnpsLLRKVAPLALVkydlesgepirDAEGRciKVPRGEPGLLIsrINPLEPFDGYTD-PAATEKkilrdVFKKGdaWFN 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 394 TGDLARRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQS-GEA-VKGYVVPKRSGVTEEDI 471
Cdd:cd05940 327 TGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQVPGTdGRAgMAAIVLQPNEEFDLSAL 406
|
490 500 510
....*....|....*....|....*....|....*..
gi 1816047872 472 MQHCETHLAKYKRPAAITFLDDIPKNATGKMLRRALR 508
Cdd:cd05940 407 AAHLEKNLPGYARPLFLRLQPEMEITGTFKQQKVDLR 443
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
29-455 |
6.33e-48 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 174.81 E-value: 6.33e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 29 YQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPInPLYTP--------TEIGYMLTNGDVK 100
Cdd:PRK09192 52 YQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPL-PLPMGfggresyiAQLRGMLASAQPA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 101 AIVGVSQLLPLYECMHESLPkvelviLCQTGEAEPEAADPEVRMKMttfakilrptsaakqnQELVPDDTAVILYTSGTT 180
Cdd:PRK09192 131 AIITPDELLPWVNEATHGNP------LLHVLSHAWFKALPEADVAL----------------PRPTPDDIAYLQYSSGST 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 181 GKPKGAMLTHQNLYSNANDVAgYLGMDERDNVVCA--LPMFHVFCLTVCMNAPLMSGATV--LIEPQFS--PASVFKLVK 254
Cdd:PRK09192 189 RFPRGVIITHRALMANLRAIS-HDGLKVRPGDRCVswLPFYHDMGLVGFLLTPVATQLSVdyLPTRDFArrPLQWLDLIS 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 255 QQQVTIfAGVPTMYNYLFQHENGKKD----DFSSIRLCISGGAAMPVALLTAFEEKFGV------TILEGYGLSEASPVT 324
Cdd:PRK09192 268 RNRGTI-SYSPPFGYELCARRVNSKDlaelDLSCWRVAGIGADMIRPDVLHQFAEAFAPagfddkAFMPSYGLAEATLAV 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 325 CFNPFDRGRKPGSIGTSIL----------------------------HvENKVVDPLGRELPAHQVGELIVKGPNVMKGY 376
Cdd:PRK09192 347 SFSPLGSGIVVEEVDRDRLeyqgkavapgaetrrvrtfvncgkalpgH-EIEIRNEAGMPLPERVVGHICVRGPSLMSGY 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 377 YKMPmETEHALK-DGWLYTGDLARRdEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVK--EAVVVGVPDPqSGE 453
Cdd:PRK09192 426 FRDE-ESQDVLAaDGWLDTGDLGYL-LDGYLYITGRAKDLIIINGRNIWPQDIEWIAEQEPELRsgDAAAFSIAQE-NGE 502
|
..
gi 1816047872 454 AV 455
Cdd:PRK09192 503 KI 504
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
27-474 |
9.63e-48 |
|
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: 173.56 E-value: 9.63e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 27 MTYQELNEHIQRFADGLQEAGME--KGDHLALLLGNSPDFIIAFFGALKAGIVVVPinpLY---TPTEIGYMLTNGDVKa 101
Cdd:cd05927 6 ISYKEVAERADNIGSALRSLGGKpaPASFVGIYSINRPEWIISELACYAYSLVTVP---LYdtlGPEAIEYILNHAEIS- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 102 ivgvsqllplyecmheslpkvelVILCQTGeaepeaadpevrMKMTTFAKILRPTSAAKQNQEL-VPDDTAVILYTSGTT 180
Cdd:cd05927 82 -----------------------IVFCDAG------------VKVYSLEEFEKLGKKNKVPPPPpKPEDLATICYTSGTT 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 181 GKPKGAMLTHQNLYSNandVAG-------YLGMDERDNVVCALPMFHVFcLTVCMNAPLMSGATVliepQFSPASVFKLV 253
Cdd:cd05927 127 GNPKGVMLTHGNIVSN---VAGvfkileiLNKINPTDVYISYLPLAHIF-ERVVEALFLYHGAKI----GFYSGDIRLLL 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 254 KQQQV---TIFAGVPTMYNYLF-----------------------------QHENGKKDDF--------------SSIRL 287
Cdd:cd05927 199 DDIKAlkpTVFPGVPRVLNRIYdkifnkvqakgplkrklfnfalnyklaelRSGVVRASPFwdklvfnkikqalgGNVRL 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 288 CISGGAAMPVALLTAFEEKFGVTILEGYGLSEASPVTCFN-PFDRGrkPGSIGTSILHVENKVVD-PlgrEL-----PAH 360
Cdd:cd05927 279 MLTGSAPLSPEVLEFLRVALGCPVLEGYGQTECTAGATLTlPGDTS--VGHVGGPLPCAEVKLVDvP---EMnydakDPN 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 361 QVGELIVKGPNVMKGYYKMPMETEHAL-KDGWLYTGDLARRDEDGYFYIVDRKKDMI-IVGGYNVYPREVEEVL------ 432
Cdd:cd05927 354 PRGEVCIRGPNVFSGYYKDPEKTAEALdEDGWLHTGDIGEWLPNGTLKIIDRKKNIFkLSQGEYVAPEKIENIYarspfv 433
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1816047872 433 ---YSHPDVKEAVVVG--VPDPqsgEAVKGYVVPKRSGV-TEEDIMQH 474
Cdd:cd05927 434 aqiFVYGDSLKSFLVAivVPDP---DVLKEWAASKGGGTgSFEELCKN 478
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
28-510 |
1.65e-47 |
|
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: 174.36 E-value: 1.65e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 28 TYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYTPTEIGYMLTNGDVKAIVGVSQ 107
Cdd:TIGR02188 90 TYRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLACARIGAIHSVVFGGFSAEALADRINDAGAKLVITADE 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 108 L------LPLYECMHESL----PKVELVILCQ-TGEaepeaadPEVRMK----------MttfakilrptsaAKQNQELV 166
Cdd:TIGR02188 170 GlrggkvIPLKAIVDEALekcpVSVEHVLVVRrTGN-------PVVPWVegrdvwwhdlM------------AKASAYCE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 167 PD-----DTAVILYTSGTTGKPKGAMLThqnlysnandVAGYLgmderdnVVCALPMFHVF---------CL-------- 224
Cdd:TIGR02188 231 PEpmdseDPLFILYTSGSTGKPKGVLHT----------TGGYL-------LYAAMTMKYVFdikdgdifwCTadvgwitg 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 225 -TVCMNAPLMSGATVLI---EPQFSPASVF-KLVKQQQVTIFAGVPTMYNYL--FQHENGKKDDFSSIRLCISGGAAM-P 296
Cdd:TIGR02188 294 hSYIVYGPLANGATTVMfegVPTYPDPGRFwEIIEKHKVTIFYTAPTAIRALmrLGDEWVKKHDLSSLRLLGSVGEPInP 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 297 VALLTAFeEKFG---VTILEGYGLSEA-----SPVTCFNPFdrgrKPGSIGTSILHVENKVVDPLGRELP-AHQVGELIV 367
Cdd:TIGR02188 374 EAWMWYY-KVVGkerCPIVDTWWQTETggimiTPLPGATPT----KPGSATLPFFGIEPAVVDEEGNPVEgPGEGGYLVI 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 368 KG--PNVMKGYYKMP---METEHALKDGWLYTGDLARRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAV 442
Cdd:TIGR02188 449 KQpwPGMLRTIYGDHerfVDTYFSPFPGYYFTGDGARRDKDGYIWITGRVDDVINVSGHRLGTAEIESALVSHPAVAEAA 528
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1816047872 443 VVGVPDPQSGEAVKGYVVPKRSG----VTEEDIMQHCETHLAKYKRPAAITFLDDIPKNATGKMLRRALRDI 510
Cdd:TIGR02188 529 VVGIPDDIKGQAIYAFVTLKDGYepddELRKELRKHVRKEIGPIAKPDKIRFVPGLPKTRSGKIMRRLLRKI 600
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
8-507 |
6.30e-47 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 176.30 E-value: 6.30e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 8 EETASEKPDSIACRFKDHMMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYTP 87
Cdd:PRK12316 3064 EEQVERTPDAVALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPE 3143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 88 TEIGYMLtnGDVKAIVGVSQllplyecMHESLPKVELV--ILCQTGEAEPEAADPEVRmkmttfakilrptsaakqnqeL 165
Cdd:PRK12316 3144 ERLAYML--EDSGAQLLLSQ-------SHLRLPLAQGVqvLDLDRGDENYAEANPAIR---------------------T 3193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 166 VPDDTAVILYTSGTTGKPKGAMLTHQNLYSNANDVAGYLGMDERDNVVCALPM-FHVFCLTvcMNAPLMSGATVLI---E 241
Cdd:PRK12316 3194 MPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFsFDVFVEE--LFWPLMSGARVVLagpE 3271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 242 PQFSPASVFKLVKQQQVTIFAGVPTMYNYLFQHENGKkdDFSSIRLCISGGAAMPVALLTAFEEkfGVTILEGYGLSEAS 321
Cdd:PRK12316 3272 DWRDPALLVELINSEGVDVLHAYPSMLQAFLEEEDAH--RCTSLKRIVCGGEALPADLQQQVFA--GLPLYNLYGPTEAT 3347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 322 -PVTCFNPFDRGRKPGSIGTSILHVENKVVDPLGRELPAHQVGELIVKGPNVMKGYYKMPMET-EHALKD-----GWLY- 393
Cdd:PRK12316 3348 iTVTHWQCVEEGKDAVPIGRPIANRACYILDGSLEPVPVGALGELYLGGEGLARGYHNRPGLTaERFVPDpfvpgERLYr 3427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 394 TGDLARRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVpdpqSGEAVKGYVVPK-RSGVTEEDIM 472
Cdd:PRK12316 3428 TGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLAV----DGRQLVAYVVPEdEAGDLREALK 3503
|
490 500 510
....*....|....*....|....*....|....*
gi 1816047872 473 QHCETHLAKYKRPAAITFLDDIPKNATGKMLRRAL 507
Cdd:PRK12316 3504 AHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKAL 3538
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
22-508 |
9.14e-47 |
|
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: 170.30 E-value: 9.14e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 22 FKDHMMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYTPTEIGYMLTNGDVKA 101
Cdd:cd05915 20 GEVHRTTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 102 IVGVSQLLPLYEcmhESLPKVELVILCQTGEAEPEAADPEVRMKMTTFaKILRPTSAAkqnqelvpdDTAVILYTSGTTG 181
Cdd:cd05915 100 LLFDPNLLPLVE---AIRGELKTVQHFVVMDEKAPEGYLAYEEALGEE-ADPVRVPER---------AACGMAYTTGTTG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 182 KPKGAMLTHQNLYSNANDVAGYLGMDERDNVV--CALPMFHVFCLTVCMNAPLMSGATVLIEPQFSPASVFKLVKQQQVT 259
Cdd:cd05915 167 LPKGVVYSHRALVLHSLAASLVDGTALSEKDVvlPVVPMFHVNAWCLPYAATLVGAKQVLPGPRLDPASLVELFDGEGVT 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 260 IFAGVPTMYNYLFQHENGKKDDFSSIRLCISGGAAMPVALLT-----AFEEKFGVTILEGYGLSEAS---PVTCFNPFDR 331
Cdd:cd05915 247 FTAGVPTVWLALADYLESTGHRLKTLRRLVVGGSAAPRSLIArfermGVEVRQGYGLTETSPVVVQNfvkSHLESLSEEE 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 332 G-RKPGSIGTSILHVENKVVDPLGRELP--AHQVGELIVKGPNVMKGYYKMPMETE-HALKDGWLYTGDLARRDEDGYFY 407
Cdd:cd05915 327 KlTLKAKTGLPIPLVRLRVADEEGRPVPkdGKALGEVQLKGPWITGGYYGNEEATRsALTPDGFFRTGDIAVWDEEGYVE 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 408 IVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVVPKRSGVTEEDIMQHCETHLAKYKR-PA 486
Cdd:cd05915 407 IKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVVVPRGEKPTPEELNEHLLKAGFAKWQlPD 486
|
490 500
....*....|....*....|..
gi 1816047872 487 AITFLDDIPKNATGKMLRRALR 508
Cdd:cd05915 487 AYVFAEEIPRTSAGKFLKRALR 508
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
28-493 |
1.68e-46 |
|
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: 169.57 E-value: 1.68e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 28 TYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYTPTEIGYMLTNGDVKAIV---- 103
Cdd:cd05932 8 TWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFvgkl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 104 --------GVSQLLPLYECMHESLPKvelvilCQTGEAEPEAADPEVRMKMTTFakilrptsaakqnqelvPDDTAVILY 175
Cdd:cd05932 88 ddwkamapGVPEGLISISLPPPSAAN------CQYQWDDLIAQHPPLEERPTRF-----------------PEQLATLIY 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 176 TSGTTGKPKGAMLTHQNLYSNANDVAGYLGMDERDNVVCALPMFHVFCLTVCMNAPLMSGATVliepqFSPASVFKLV-- 253
Cdd:cd05932 145 TSGTTGQPKGVMLTFGSFAWAAQAGIEHIGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLV-----AFAESLDTFVed 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 254 -KQQQVTIFAGVPTMYNyLFQHE------NGKKDDFSSI--------------------RLCISGGAAMPVALLTAFEeK 306
Cdd:cd05932 220 vQRARPTLFFSVPRLWT-KFQQGvqdkipQQKLNLLLKIpvvnslvkrkvlkglgldqcRLAGCGSAPVPPALLEWYR-S 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 307 FGVTILEGYGLSEASPVTCFN-PFDRgrKPGSIGTSILHVENKVVDPlgrelpahqvGELIVKGPNVMKGYYKMPMETEH 385
Cdd:cd05932 298 LGLNILEAYGMTENFAYSHLNyPGRD--KIGTVGNAGPGVEVRISED----------GEILVRSPALMMGYYKDPEATAE 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 386 AL-KDGWLYTGDLARRDEDGYFYIVDRKKDMIIVG-GYNVYPREVEEVLYSHPDVKEAVVVGVPDPQ-------SGEAVK 456
Cdd:cd05932 366 AFtADGFLRTGDKGELDADGNLTITGRVKDIFKTSkGKYVAPAPIENKLAEHDRVEMVCVIGSGLPAplalvvlSEEARL 445
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1816047872 457 GYVVPKRSGVtEEDIMQHCE---THLAKYKRPAAITFLDD 493
Cdd:cd05932 446 RADAFARAEL-EASLRAHLArvnSTLDSHEQLAGIVVVKD 484
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
27-508 |
1.85e-46 |
|
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: 167.74 E-value: 1.85e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 27 MTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYTPTEIGYMLTNGdvKAIVgvs 106
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRDRVDRG--GAVY--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 107 qllplyecmheslpkvelvilcqtgeaepeaadpevrmkmttfakilrptsaAKQNQELVPDDTAVILYTSGTTGKPKGA 186
Cdd:cd05974 76 ----------------------------------------------------AAVDENTHADDPMLLYFTSGTTSKPKLV 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 187 MLTHQNLYSNANDVAGYLGMDERD---NVVCALPMFHVFCltvCMNAPLMSGATVLI--EPQFSPASVFKLVKQQQVTIF 261
Cdd:cd05974 104 EHTHRSYPVGHLSTMYWIGLKPGDvhwNISSPGWAKHAWS---CFFAPWNAGATVFLfnYARFDAKRVLAALVRYGVTTL 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 262 AGVPTMYNYLFQHENGKKDdfSSIRLCISGGAAMPVALLTAFEEKFGVTILEGYGLSEASPVTCFNPfDRGRKPGSIGTS 341
Cdd:cd05974 181 CAPPTVWRMLIQQDLASFD--VKLREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETTALVGNSP-GQPVKAGSMGRP 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 342 ILHVENKVVDPLGRelPAHQvGEL-IVKGPN----VMKGYYKMPMETEHALKDGWLYTGDLARRDEDGYFYIVDRKKDMI 416
Cdd:cd05974 258 LPGYRVALLDPDGA--PATE-GEVaLDLGDTrpvgLMKGYAGDPDKTAHAMRGGYYRTGDIAMRDEDGYLTYVGRADDVF 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 417 IVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVV----PKRSGVTEEDIMQHCETHLAKYKRPAAITFLd 492
Cdd:cd05974 335 KSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVlragYEPSPETALEIFRFSRERLAPYKRIRRLEFA- 413
|
490
....*....|....*.
gi 1816047872 493 DIPKNATGKMLRRALR 508
Cdd:cd05974 414 ELPKTISGKIRRVELR 429
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
8-507 |
2.49e-46 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 174.20 E-value: 2.49e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 8 EETASEKPDSIACRFKDHMMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYTP 87
Cdd:PRK05691 2195 AAQAARTPQAPALTFAGQTLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPL 2274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 88 TEIGYMLTNGdvkaivGVSQLLPlYECMHESLpkvelvilcqtGEAEPEAAdpevRMKMTTFAKILRPTSAAKQNQELVP 167
Cdd:PRK05691 2275 ERLHYMIEDS------GIGLLLS-DRALFEAL-----------GELPAGVA----RWCLEDDAAALAAYSDAPLPFLSLP 2332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 168 DDTAVILYTSGTTGKPKGAMLTHQNLYSNANDVAGYLGMDERDnvvCALpmfHVFCL-----TVCMNAPLMSGATVLI-- 240
Cdd:PRK05691 2333 QHQAYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIERFGMRADD---CEL---HFYSInfdaaSERLLVPLLCGARVVLra 2406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 241 EPQFSPASVFKLVKQQQVTIFAGVPTMYNYLFQHEnGKKDDFSSIRLCISGGAAMPVALLTAFEEKFGVTIL-EGYGLSE 319
Cdd:PRK05691 2407 QGQWGAEEICQLIREQQVSILGFTPSYGSQLAQWL-AGQGEQLPVRMCITGGEALTGEHLQRIRQAFAPQLFfNAYGPTE 2485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 320 A--SPVTCFNP--FDRGRKPGSIGTSILHVENKVVDPLGRELPAHQVGELIVKGPNVMKGYYKMP-METEHALKD----- 389
Cdd:PRK05691 2486 TvvMPLACLAPeqLEEGAASVPIGRVVGARVAYILDADLALVPQGATGELYVGGAGLAQGYHDRPgLTAERFVADpfaad 2565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 390 -GWLY-TGDLARRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPqSGEAVKGYVVPKRSGVT 467
Cdd:PRK05691 2566 gGRLYrTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLALDTP-SGKQLAGYLVSAVAGQD 2644
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1816047872 468 EEDIMQ-------HCETHLAKYKRPAAITFLDDIPKNATGKMLRRAL 507
Cdd:PRK05691 2645 DEAQAAlrealkaHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRAL 2691
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
8-507 |
1.84e-45 |
|
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: 165.69 E-value: 1.84e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 8 EETASEKPDSIACRFKDHMMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYTP 87
Cdd:cd17644 7 EEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLDPNYPQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 88 TEIGYMLTNGDVKaivgvsqllplyecmheslpkvelVILCQtgeaepeaadpevrmkmttfakilrptsaakqnqelvP 167
Cdd:cd17644 87 ERLTYILEDAQIS------------------------VLLTQ-------------------------------------P 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 168 DDTAVILYTSGTTGKPKGAMLTHQNLYSNANDVAGYLGMDERDNVVcalpMFHVFCLTVCMN---APLMSGATVLIEPQ- 243
Cdd:cd17644 106 ENLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEYGITSSDRVL----QFASIAFDVAAEeiyVTLLSGATLVLRPEe 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 244 --FSPASVFKLVKQQQVTIFAgVPTMYNYLFQHE--NGKKDDFSSIRLCISGGAAMPVALLTAFEEKFG--VTILEGYGL 317
Cdd:cd17644 182 mrSSLEDFVQYIQQWQLTVLS-LPPAYWHLLVLEllLSTIDLPSSLRLVIVGGEAVQPELVRQWQKNVGnfIQLINVYGP 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 318 SEAS-PVTCFNPFD---RGRKPGSIGTSILHVENKVVDPLGRELPAHQVGELIVKGPNVMKGYYKMPMETE--------H 385
Cdd:cd17644 261 TEATiAATVCRLTQlteRNITSVPIGRPIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAekfishpfN 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 386 ALKDGWLY-TGDLARRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVVPK-- 462
Cdd:cd17644 341 SSESERLYkTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIVPHye 420
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1816047872 463 RSGVTEEdIMQHCETHLAKYKRPAAITFLDDIPKNATGKMLRRAL 507
Cdd:cd17644 421 ESPSTVE-LRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
49-501 |
1.99e-45 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 169.51 E-value: 1.99e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 49 EKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINplYTPTEIGYM--LTNGDVKAIVGVSQLLPLYECMH--ESLPKVEL 124
Cdd:PRK08043 253 VEGERIGLMLPNATISAAVIFGASLRRRIPAMMN--YTAGVKGLTsaITAAEIKTIFTSRQFLDKGKLWHlpEQLTQVRW 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 125 VILcqtgeaEPEAADPEVRMKMTTFAKILRPTSAAKQNQelvPDDTAVILYTSGTTGKPKGAMLTHQNLYSNANDVAGYL 204
Cdd:PRK08043 331 VYL------EDLKDDVTTADKLWIFAHLLMPRLAQVKQQ---PEDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIA 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 205 GMDERDNVVCALPMFHVFCLTVCMNAPLMSGATVLIEPqfSPAS---VFKLVKQQQVTIFAGVPT-MYNYL-FQHENgkk 279
Cdd:PRK08043 402 DFTPNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYP--SPLHyriVPELVYDRNCTVLFGTSTfLGNYArFANPY--- 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 280 dDFSSIRLCISGGAAMPVALLTAFEEKFGVTILEGYGLSEASPVTCFN-PFdrGRKPGSIGTSILHVENKVVDPLGrelp 358
Cdd:PRK08043 477 -DFARLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINvPM--AAKPGTVGRILPGMDARLLSVPG---- 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 359 AHQVGELIVKGPNVMKGYYKMP----METEHA------LKDGWLYTGDLARRDEDGYFYIVDRKKDMIIVGGYNVYPREV 428
Cdd:PRK08043 550 IEQGGRLQLKGPNIMNGYLRVEkpgvLEVPTAenargeMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMV 629
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1816047872 429 EEV-LYSHPDVKEAVVVgVPDPQSGEAVKGYVVPkrSGVTEEDIMQHCETH-LAKYKRPAAITFLDDIPKNATGK 501
Cdd:PRK08043 630 EQLaLGVSPDKQHATAI-KSDASKGEALVLFTTD--SELTREKLQQYAREHgVPELAVPRDIRYLKQLPLLGSGK 701
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
28-508 |
7.09e-45 |
|
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: 164.58 E-value: 7.09e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 28 TYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINplytpteIGymltngdvkaivgvsq 107
Cdd:cd05908 17 SYRHLREEALGYLGALQELGIKPGQEVVFQITHNNKFLYLFWACLLGGMIAVPVS-------IG---------------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 108 llplyecmheslpkvelvilcqtgeaepeaADPEVRMKMTTFAKIL-RPTSAAKQN-QELVPDDTAVILYTSGTTGKPKG 185
Cdd:cd05908 74 ------------------------------SNEEHKLKLNKVWNTLkNPYLITEEEvLCELADELAFIQFSSGSTGDPKG 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 186 AMLTHQNLYSNANDVAGYLGMDERDNVVCALPMFHVFCLTVCMNAPLMSGATVLIEP--QF--SPASVFKLVKQQQVTIF 261
Cdd:cd05908 124 VMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGMNQYLMPtrLFirRPILWLKKASEHKATIV 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 262 AGVPTMYNYLFQHENGKKD---DFSSIRLCISGGAAMPVALLTAFEE---KFGV---TILEGYGLSEASPVTCFNPFD-- 330
Cdd:cd05908 204 SSPNFGYKYFLKTLKPEKAndwDLSSIRMILNGAEPIDYELCHEFLDhmsKYGLkrnAILPVYGLAEASVGASLPKAQsp 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 331 --------RGRKPG-----------------SIGTSILHVENKVVDPLGRELPAHQVGELIVKGPNVMKGYYKMPMETEH 385
Cdd:cd05908 284 fktitlgrRHVTHGepepevdkkdsecltfvEVGKPIDETDIRICDEDNKILPDGYIGHIQIRGKNVTPGYYNNPEATAK 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 386 AL-KDGWLYTGDLARRdEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVK--EAVVVGVPDPQS-GEAVKGYVVP 461
Cdd:cd05908 364 VFtDDGWLKTGDLGFI-RNGRLVITGREKDIIFVNGQNVYPHDIERIAEELEGVElgRVVACGVNNSNTrNEEIFCFIEH 442
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1816047872 462 KRSgvtEEDIM---QHCETHLAKYK--RPAAITFLDDIPKNATGKMLRRALR 508
Cdd:cd05908 443 RKS---EDDFYplgKKIKKHLNKRGgwQINEVLPIRRIPKTTSGKVKRYELA 491
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
167-501 |
1.54e-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: 341248 [Multi-domain] Cd Length: 364 Bit Score: 160.63 E-value: 1.54e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 167 PDDTaVILYTSGTTGKPKGAMLTHQNLYS---------NANDVAGYLGMDERDN-----VVCALPMFHVFCLTVCMNAPL 232
Cdd:cd05924 3 ADDL-YILYTGGTTGMPKGVMWRQEDIFRmlmggadfgTGEFTPSEDAHKAAAAaagtvMFPAPPLMHGTGSWTAFGGLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 233 MSGATVLIEPQFSPASVFKLVKQQQVTIFAGV-PTMYNYLFQHENGKKD-DFSSIRLCISGGAAMPVALLTAF-EEKFGV 309
Cdd:cd05924 82 GGQTVVLPDDRFDPEEVWRTIEKHKVTSMTIVgDAMARPLIDALRDAGPyDLSSLFAISSGGALLSPEVKQGLlELVPNI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 310 TILEGYGLSEAS-----------PVTcfNPFDRgRKPGSIgtsilhvenkVVDPLGREL-PAHQVGELIVKGPNVMKGYY 377
Cdd:cd05924 162 TLVDAFGSSETGftgsghsagsgPET--GPFTR-ANPDTV----------VLDDDGRVVpPGSGGVGWIARRGHIPLGYY 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 378 KMPMETEHALK--DG--WLYTGDLARRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGE 453
Cdd:cd05924 229 GDEAKTAETFPevDGvrYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQ 308
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1816047872 454 AVKGyVVPKRSG--VTEEDIMQHCETHLAKYKRPAAITFLDDIPKNATGK 501
Cdd:cd05924 309 EVVA-VVQLREGagVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
8-507 |
2.05e-44 |
|
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: 162.34 E-value: 2.05e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 8 EETASEKPDSIACRFKDHMMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYTP 87
Cdd:cd17645 5 EEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 88 TEIGYMLTNGDVKaivgvsqllplyecmheslpkvelVILCQtgeaepeaadpevrmkmttfakilrptsaakqnqelvP 167
Cdd:cd17645 85 ERIAYMLADSSAK------------------------ILLTN-------------------------------------P 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 168 DDTAVILYTSGTTGKPKGAMLTHQNLYSNANDVAGYLGMDERDN-VVCALPMFHVFCLTvcMNAPLMSGATVLIEPQFSP 246
Cdd:cd17645 104 DDLAYVIYTSGSTGLPKGVMIEHHNLVNLCEWHRPYFGVTPADKsLVYASFSFDASAWE--IFPHLTAGAALHVVPSERR 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 247 ASVFKL---VKQQQVTIfAGVPTMYNYLF-QHENgkkddfSSIRLCISGGAAMPVAlltafeEKFGVTILEGYGLSEASP 322
Cdd:cd17645 182 LDLDALndyFNQEGITI-SFLPTGAAEQFmQLDN------QSLRVLLTGGDKLKKI------ERKGYKLVNNYGPTENTV 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 323 VTCFNPFDRGRKPGSIGTSILHVENKVVDPLGRELPAHQVGELIVKGPNVMKGYYKMPMETE-----HALKDG-WLY-TG 395
Cdd:cd17645 249 VATSFEIDKPYANIPIGKPIDNTRVYILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAekfivHPFVPGeRMYrTG 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 396 DLARRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVVPKRSgVTEEDIMQHC 475
Cdd:cd17645 329 DLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTAPEE-IPHEELREWL 407
|
490 500 510
....*....|....*....|....*....|..
gi 1816047872 476 ETHLAKYKRPAAITFLDDIPKNATGKMLRRAL 507
Cdd:cd17645 408 KNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
28-445 |
4.85e-44 |
|
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: 163.75 E-value: 4.85e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 28 TYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYTPTEIGYMLTNGDVKAIVG--V 105
Cdd:cd17641 13 TWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIAedE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 106 SQLLPLYECMHEsLPKVELVILCqtgeaEPEAADPEVRMKMTTFAKIL-RPTSAAKQNQELV--------PDDTAVILYT 176
Cdd:cd17641 93 EQVDKLLEIADR-IPSVRYVIYC-----DPRGMRKYDDPRLISFEDVVaLGRALDRRDPGLYerevaagkGEDVAVLCTT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 177 SGTTGKPKGAMLTHQNLYSNAndvAGYLGMDER---DNVVCALPMFHVFCLTVCMNAPLMSGATV--------------L 239
Cdd:cd17641 167 SGTTGKPKLAMLSHGNFLGHC---AAYLAADPLgpgDEYVSVLPLPWIGEQMYSVGQALVCGFIVnfpeepetmmedlrE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 240 IEPQF--SPASVFK------LVKQQQVTIF------AGVPTMYNYLFQHENGKKDD-----------------------F 282
Cdd:cd17641 244 IGPTFvlLPPRVWEgiaadvRARMMDATPFkrfmfeLGMKLGLRALDRGKRGRPVSlwlrlaswladallfrplrdrlgF 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 283 SSIRLCISGGAAMPVALLTaFEEKFGVTILEGYGLSEASPVTCFNPfDRGRKPGSIGTSILHVENKVVDplgrelpahqV 362
Cdd:cd17641 324 SRLRSAATGGAALGPDTFR-FFHAIGVPLKQLYGQTELAGAYTVHR-DGDVDPDTVGVPFPGTEVRIDE----------V 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 363 GELIVKGPNVMKGYYKMPMET-EHALKDGWLYTGDLARRDEDGYFYIVDRKKD-MIIVGGYNVYPREVEEVLYSHPDVKE 440
Cdd:cd17641 392 GEILVRSPGVFVGYYKNPEATaEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDvGTTSDGTRFSPQFIENKLKFSPYIAE 471
|
....*
gi 1816047872 441 AVVVG 445
Cdd:cd17641 472 AVVLG 476
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
25-445 |
1.59e-43 |
|
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: 162.53 E-value: 1.59e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 25 HMMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYTPTEIGYMLTNGDVKAIV- 103
Cdd:cd05933 7 HTLTYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSEANILVv 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 104 -GVSQLLPLYEcMHESLPKVELVIlcQTGEaEPEAADPevrmKMTTFAKILRPTSAAKQNQELV------PDDTAVILYT 176
Cdd:cd05933 87 eNQKQLQKILQ-IQDKLPHLKAII--QYKE-PLKEKEP----NLYSWDEFMELGRSIPDEQLDAiissqkPNQCCTLIYT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 177 SGTTGKPKGAMLTHQNLYSNANDVAGYLGMDERDN----VVCALPMFHVFCLTVCMNAPLMSGATV-LIEPQFSPASVFK 251
Cdd:cd05933 159 SGTTGMPKGVMLSHDNITWTAKAASQHMDLRPATVgqesVVSYLPLSHIAAQILDIWLPIKVGGQVyFAQPDALKGTLVK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 252 LVKQQQVTIFAGVPTMYNYL--------------------------FQHE----NGKKDDFSSIRL-------------- 287
Cdd:cd05933 239 TLREVRPTAFMGVPRVWEKIqekmkavgaksgtlkrkiaswakgvgLETNlklmGGESPSPLFYRLakklvfkkvrkalg 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 288 ------CISGGAAMPVALLTAFEeKFGVTILEGYGLSEAS-PVTCFNPFDRGRkpGSIGTSILHVENKVVDPlgrelPAH 360
Cdd:cd05933 319 ldrcqkFFTGAAPISRETLEFFL-SLNIPIMELYGMSETSgPHTISNPQAYRL--LSCGKALPGCKTKIHNP-----DAD 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 361 QVGELIVKGPNVMKGYYKMPMETEHALK-DGWLYTGDLARRDEDGYFYIVDRKKDMIIV-GGYNVYPREVEE-VLYSHPD 437
Cdd:cd05933 391 GIGEICFWGRHVFMGYLNMEDKTEEAIDeDGWLHSGDLGKLDEDGFLYITGRIKELIITaGGENVPPVPIEDaVKKELPI 470
|
....*...
gi 1816047872 438 VKEAVVVG 445
Cdd:cd05933 471 ISNAMLIG 478
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
25-507 |
5.57e-43 |
|
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: 159.69 E-value: 5.57e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 25 HMMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPInplY-TPTEIGymltngdvkaiv 103
Cdd:cd17639 4 KYMSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTV---YaTLGEDA------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 104 gvsqllpLYECMHESlpKVElVILCqtgeaepeaaDPEvrmkmttfakilrptsaakqnqelvPDDTAVILYTSGTTGKP 183
Cdd:cd17639 69 -------LIHSLNET--ECS-AIFT----------DGK-------------------------PDDLACIMYTSGSTGNP 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 184 KGAMLTHQNLysnandVAGYLGMDER-------DNVVCA-LPMFHVFCLTVCMNApLMSGATV-------LIEPQFS--- 245
Cdd:cd17639 104 KGVMLTHGNL------VAGIAGLGDRvpellgpDDRYLAyLPLAHIFELAAENVC-LYRGGTIgygsprtLTDKSKRgck 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 246 -PASVFKlvkqqqVTIFAGVP--------------------------TMYNY-LFQHENGKKDDF--------------S 283
Cdd:cd17639 177 gDLTEFK------PTLMVGVPaiwdtirkgvlaklnpmgglkrtlfwTAYQSkLKALKEGPGTPLldelvfkkvraalgG 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 284 SIRLCISGGAamPVALLT-AFEEKFGVTILEGYGLSEASPVTCF-NPFDRgrKPGSIGTSILHVENKVVD-PLGR---EL 357
Cdd:cd17639 251 RLRYMLSGGA--PLSADTqEFLNIVLCPVIQGYGLTETCAGGTVqDPGDL--ETGRVGPPLPCCEIKLVDwEEGGystDK 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 358 PAHQvGELIVKGPNVMKGYYKMPMETEHALK-DGWLYTGDLARRDEDGYFYIVDRKKDMI-IVGGYNVYPREVEEVLYSH 435
Cdd:cd17639 327 PPPR-GEILIRGPNVFKGYYKNPEKTKEAFDgDGWFHTGDIGEFHPDGTLKIIDRKKDLVkLQNGEYIALEKLESIYRSN 405
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 436 PDVKEAVVVGVPDPQSgeaVKGYVVP---------KRSGVTEEDIMQHCE------------------THLAKYKRPAAI 488
Cdd:cd17639 406 PLVNNICVYADPDKSY---PVAIVVPnekhltklaEKHGVINSEWEELCEdkklqkavlkslaetaraAGLEKFEIPQGV 482
|
570 580
....*....|....*....|....*
gi 1816047872 489 TFLDDI--PKN----ATGKMLRRAL 507
Cdd:cd17639 483 VLLDEEwtPENglvtAAQKLKRKEI 507
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
4-507 |
9.04e-43 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 163.80 E-value: 9.04e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 4 VSKLEETASEKPDSIACRFKDHMMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINP 83
Cdd:PRK05691 3723 VRLFEAQVAAHPQRIAASCLDQQWSYAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDP 3802
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 84 lytpteigyMLTNGDVKAIVGVSQLlPLYECMHESLPKVELVIlcqtgEAEPEAADPEVRMKMTTFAKilrptSAAKQNQ 163
Cdd:PRK05691 3803 ---------GLPAQRLQRIIELSRT-PVLVCSAACREQARALL-----DELGCANRPRLLVWEEVQAG-----EVASHNP 3862
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 164 ELV--PDDTAVILYTSGTTGKPKGAMLTHQNLYSNANDVAGYLGMDERDnvVCALPMFHVFCLTVC--MNAPLMsGATVL 239
Cdd:PRK05691 3863 GIYsgPDNLAYVIYTSGSTGLPKGVMVEQRGMLNNQLSKVPYLALSEAD--VIAQTASQSFDISVWqfLAAPLF-GARVE 3939
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 240 IEPQ---FSPASVFKLVKQQQVTIFAGVPTMYNYLFQHEngkKDDFSSIRLCISGGAAMPVALLTAFEEKF-GVTILEGY 315
Cdd:PRK05691 3940 IVPNaiaHDPQGLLAHVQAQGITVLESVPSLIQGMLAED---RQALDGLRWMLPTGEAMPPELARQWLQRYpQIGLVNAY 4016
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 316 GLSEASPVTCFNPFDRGRKPGS---IGTSilhVENKVVDPLGREL---PAHQVGELIVKGPNVMKGYYKMPMETEHAL-- 387
Cdd:PRK05691 4017 GPAECSDDVAFFRVDLASTRGSylpIGSP---TDNNRLYLLDEALelvPLGAVGELCVAGTGVGRGYVGDPLRTALAFvp 4093
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 388 -----KDGWLY-TGDLARRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAvVVGVPDPQSGEAVKGYVVP 461
Cdd:PRK05691 4094 hpfgaPGERLYrTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREA-AVAVQEGVNGKHLVGYLVP 4172
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1816047872 462 KRSGVTE----EDIMQHCETHLAKYKRPAAITFLDDIPKNATGKMLRRAL 507
Cdd:PRK05691 4173 HQTVLAQgallERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKAL 4222
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
28-509 |
2.63e-41 |
|
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: 154.13 E-value: 2.63e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 28 TYQELNEHIQRFADGLQEA-GMEKGDHLALLLGNSPDFIIAFFGALKAGIVvvpinplytPTEIGYMLTnGDvkaivgvs 106
Cdd:cd05937 7 TYSETYDLVLRYAHWLHDDlGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAA---------PAFINYNLS-GD-------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 107 qllPLYECMHESLPKveLVIlcqtgeaepeaADPevrmkmttfakilrptsaakqnqelvpDDTAVILYTSGTTGKPKGA 186
Cdd:cd05937 69 ---PLIHCLKLSGSR--FVI-----------VDP---------------------------DDPAILIYTSGTTGLPKAA 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 187 MLTHQNLYSNANDVAGYLGMDERDNVVCALPMFHVFCLTVCMNAPLMSGATVLIEPQFSPASVFKLVKQQQVTIFAGVPT 266
Cdd:cd05937 106 AISWRRTLVTSNLLSHDLNLKNGDRTYTCMPLYHGTAAFLGACNCLMSGGTLALSRKFSASQFWKDVRDSGATIIQYVGE 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 267 MYNYLFQHENGKKDDFSSIRLCISGGaaMPVALLTAFEEKFGV-TILEGYGLSEAsPVTCFN----PFDRG--RKPGSIG 339
Cdd:cd05937 186 LCRYLLSTPPSPYDRDHKVRVAWGNG--LRPDIWERFRERFNVpEIGEFYAATEG-VFALTNhnvgDFGAGaiGHHGLIR 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 340 TSILHVENKVV-------DPLGR-------ELPAHQVGELIVKGPNVMK----GYYKMPMETEHAL-------KDGWLYT 394
Cdd:cd05937 263 RWKFENQVVLVkmdpetdDPIRDpktgfcvRAPVGEPGEMLGRVPFKNReafqGYLHNEDATESKLvrdvfrkGDIYFRT 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 395 GDLARRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQ-SGEAVKGYVVPKRSGVTEEDIM- 472
Cdd:cd05937 343 GDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGVKVPGhDGRAGCAAITLEESSAVPTEFTk 422
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1816047872 473 ----QHCETHLAKYKRPAAITFLDDIPKNATGKMLRRALRD 509
Cdd:cd05937 423 sllaSLARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVLRD 463
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
28-506 |
3.93e-41 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 155.15 E-value: 3.93e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 28 TYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVvpiNPLYTPTE----IGYMLTNGDVKAIV 103
Cdd:PRK07768 31 TWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASL---TMLHQPTPrtdlAVWAEDTLRVIGMI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 104 GVSqllplyecmheslpkveLVILcqtgeAEP-EAADPEVRMKMTTFAKI--LRPTSAAKQnQELVPDDTAVILYTSGTT 180
Cdd:PRK07768 108 GAK-----------------AVVV-----GEPfLAAAPVLEEKGIRVLTVadLLAADPIDP-VETGEDDLALMQLTSGST 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 181 GKPKGAMLTHQNLYSNANDVAGYLGMD-ERDNVVCALPMFH----VFCLTVcmnaPLMSGAT-VLIEP-QF--SPASVFK 251
Cdd:PRK07768 165 GSPKAVQITHGNLYANAEAMFVAAEFDvETDVMVSWLPLFHdmgmVGFLTV----PMYFGAElVKVTPmDFlrDPLLWAE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 252 LVKQQQVTIFAGVPTMYNYLFQH-ENGKKD---DFSSIRLCISGGAAMPVALLTAFEE---KFGV---TILEGYGLSEAS 321
Cdd:PRK07768 241 LISKYRGTMTAAPNFAYALLARRlRRQAKPgafDLSSLRFALNGAEPIDPADVEDLLDagaRFGLrpeAILPAYGMAEAT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 322 PVTCFNPFDRG-------------------------RKPGSIGTSILHVENKVVDPLGRELPAHQVGELIVKGPNVMKGY 376
Cdd:PRK07768 321 LAVSFSPCGAGlvvdevdadllaalrravpatkgntRRLATLGPPLPGLEVRVVDEDGQVLPPRGVGVIELRGESVTPGY 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 377 YKM--PMETEHAlkDGWLYTGDLARRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKE--AVVVGVPDPQSG 452
Cdd:PRK07768 401 LTMdgFIPAQDA--DGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVRPgnAVAVRLDAGHSR 478
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1816047872 453 E--AVkgyVVPKRSGVTEEDI--MQHCETH---LAKYKRPAAITFLD--DIPKNATGKmLRRA 506
Cdd:PRK07768 479 EgfAV---AVESNAFEDPAEVrrIRHQVAHevvAEVGVRPRNVVVLGpgSIPKTPSGK-LRRA 537
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
27-498 |
3.83e-40 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 153.72 E-value: 3.83e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 27 MTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYTPTEIGYMLTNGDVKAIVGVS 106
Cdd:PLN02736 79 MTYGEAGTARTAIGSGLVQHGIPKGACVGLYFINRPEWLIVDHACSAYSYVSVPLYDTLGPDAVKFIVNHAEVAAIFCVP 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 107 QLLP-LYECMHEsLPKVELVILCQTGEAEPEAADPEVRMKMTTFAKIL-------RPTSAAKqnqelvPDDTAVILYTSG 178
Cdd:PLN02736 159 QTLNtLLSCLSE-IPSVRLIVVVGGADEPLPSLPSGTGVEIVTYSKLLaqgrsspQPFRPPK------PEDVATICYTSG 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 179 TTGKPKGAMLTHQNLYSNandVAGY---LGMDERDNVVCALPMFHVFcLTVCMNAPLMSGATVliepQFSPASVFKLVKQ 255
Cdd:PLN02736 232 TTGTPKGVVLTHGNLIAN---VAGSslsTKFYPSDVHISYLPLAHIY-ERVNQIVMLHYGVAV----GFYQGDNLKLMDD 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 256 QQV---TIFAGVPTMYN--Y----------------LFQH---------ENGK-------KDDFSSI--------RLCIS 290
Cdd:PLN02736 304 LAAlrpTIFCSVPRLYNriYdgitnavkesgglkerLFNAaynakkqalENGKnpspmwdRLVFNKIkaklggrvRFMSS 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 291 GGAAMPVALLTAFEEKFGVTILEGYGLSEAS-PVTCFNPFDrgRKPGSIGTSILHVENKVVD-----------PLGRelp 358
Cdd:PLN02736 384 GASPLSPDVMEFLRICFGGRVLEGYGMTETScVISGMDEGD--NLSGHVGSPNPACEVKLVDvpemnytsedqPYPR--- 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 359 ahqvGELIVKGPNVMKGYYKMPMETEHAL-KDGWLYTGDLARRDEDGYFYIVDRKKDMI-IVGGYNVYPREVEEVLYSHP 436
Cdd:PLN02736 459 ----GEICVRGPIIFKGYYKDEVQTREVIdEDGWLHTGDIGLWLPGGRLKIIDRKKNIFkLAQGEYIAPEKIENVYAKCK 534
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1816047872 437 DVKEAVVVG-----------VPDPqsgEAVKGYVvpKRSGVTEEDIMQHCETHLAkykRPAAITFLDDIPKNA 498
Cdd:PLN02736 535 FVAQCFVYGdslnsslvavvVVDP---EVLKAWA--ASEGIKYEDLKQLCNDPRV---RAAVLADMDAVGREA 599
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
28-510 |
1.81e-39 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 151.64 E-value: 1.81e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 28 TYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAF-------------FGALKAGIVVVPINplytpteigyml 94
Cdd:PRK10524 86 TFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMlacarigaihsvvFGGFASHSLAARID------------ 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 95 tngDVKAIVGVS--------QLLP----LYECMHESLPKVELVILCQTGEAEpeaadpevrMKMTTFAKILRPTSAAKQN 162
Cdd:PRK10524 154 ---DAKPVLIVSadagsrggKVVPykplLDEAIALAQHKPRHVLLVDRGLAP---------MARVAGRDVDYATLRAQHL 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 163 QELVP------DDTAVILYTSGTTGKPKGAMlthqnlysnaNDVAGYlgmderdNVVCALPMFHVFC-----LTVCMN-- 229
Cdd:PRK10524 222 GARVPvewlesNEPSYILYTSGTTGKPKGVQ----------RDTGGY-------AVALATSMDTIFGgkageTFFCASdi 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 230 -----------APLMSG-ATVLIE--PQFSPASV-FKLVKQQQVTIFAGVPTMYNYLFQHENG--KKDDFSSIRLCISGG 292
Cdd:PRK10524 285 gwvvghsyivyAPLLAGmATIMYEglPTRPDAGIwWRIVEKYKVNRMFSAPTAIRVLKKQDPAllRKHDLSSLRALFLAG 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 293 AamPVALLTA--FEEKFGVTILEGYGLSEAS-PV-TCFNPF-DRGRKPGSIGTSILHVENKVVDPL-GRELPAHQVGELI 366
Cdd:PRK10524 365 E--PLDEPTAswISEALGVPVIDNYWQTETGwPIlAIARGVeDRPTRLGSPGVPMYGYNVKLLNEVtGEPCGPNEKGVLV 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 367 VKGPnvmkgyykMP---MET-----EHALKDGW------LY-TGDLARRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEV 431
Cdd:PRK10524 443 IEGP--------LPpgcMQTvwgddDRFVKTYWslfgrqVYsTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEES 514
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 432 LYSHPDVKEAVVVGVPDPQSGEAVKGYVVPKRSGVT---------EEDIMQHCETHLAKYKRPAAITFLDDIPKNATGKM 502
Cdd:PRK10524 515 ISSHPAVAEVAVVGVKDALKGQVAVAFVVPKDSDSLadrearlalEKEIMALVDSQLGAVARPARVWFVSALPKTRSGKL 594
|
....*...
gi 1816047872 503 LRRALRDI 510
Cdd:PRK10524 595 LRRAIQAI 602
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
28-510 |
4.94e-39 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 150.29 E-value: 4.94e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 28 TYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAF-------------FG-----ALKAGIVvvpinplytpte 89
Cdd:PRK00174 100 TYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMlacarigavhsvvFGgfsaeALADRII------------ 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 90 igymltNGDVKAIV----GV--SQLLPLYECMHESL---PKVELVILCQ-TGEA----------------------EPEA 137
Cdd:PRK00174 168 ------DAGAKLVItadeGVrgGKPIPLKANVDEALancPSVEKVIVVRrTGGDvdwvegrdlwwhelvagasdecEPEP 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 138 ADPEvrmkmttfakilrptsaakqnqelvpdDTAVILYTSGTTGKPKGAMltHqnlysnanDVAGYLgmderdnVVCALP 217
Cdd:PRK00174 242 MDAE---------------------------DPLFILYTSGSTGKPKGVL--H--------TTGGYL-------VYAAMT 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 218 MFHVF---------CltvcmNA--------------PLMSGATVLI-E--PQFSPASVF-KLVKQQQVTIFAGVPTMYNY 270
Cdd:PRK00174 278 MKYVFdykdgdvywC-----TAdvgwvtghsyivygPLANGATTLMfEgvPNYPDPGRFwEVIDKHKVTIFYTAPTAIRA 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 271 LFQH--ENGKKDDFSSIRLCISGGAAM-PVALLTAFE----------------EKFGVTI--LEGyglseASPVtcfnpf 329
Cdd:PRK00174 353 LMKEgdEHPKKYDLSSLRLLGSVGEPInPEAWEWYYKvvggercpivdtwwqtETGGIMItpLPG-----ATPL------ 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 330 drgrKPGSIGTSILHVENKVVDPLGRELPAHQVGELIVKG--PNVMKGYYKMP---METEHALKDGWLYTGDLARRDEDG 404
Cdd:PRK00174 422 ----KPGSATRPLPGIQPAVVDEEGNPLEGGEGGNLVIKDpwPGMMRTIYGDHerfVKTYFSTFKGMYFTGDGARRDEDG 497
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 405 YFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVVPKRSGVTEEDIMQHCETHLAK--- 481
Cdd:PRK00174 498 YYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLKGGEEPSDELRKELRNWVRKeig 577
|
570 580 590
....*....|....*....|....*....|
gi 1816047872 482 -YKRPAAITFLDDIPKNATGKMLRRALRDI 510
Cdd:PRK00174 578 pIAKPDVIQFAPGLPKTRSGKIMRRILRKI 607
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
3-507 |
1.40e-38 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 150.96 E-value: 1.40e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 3 LVSKLEETASEKPDSIACRFKDHMMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPIN 82
Cdd:PRK10252 460 LSALVAQQAAKTPDAPALADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLD 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 83 PLYTPTEIGYMLTNGDVKAIVGVSQLLPLYecmhESLPKVELviLCQTGEAEPEAADPEVRMKmttfakilrptsaakqn 162
Cdd:PRK10252 540 TGYPDDRLKMMLEDARPSLLITTADQLPRF----ADVPDLTS--LCYNAPLAPQGAAPLQLSQ----------------- 596
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 163 qelvPDDTAVILYTSGTTGKPKGAMLTH----------QNLYsnandvagylGMDERDNVVCALPM-FHV----FCLtvc 227
Cdd:PRK10252 597 ----PHHTAYIIFTSGSTGRPKGVMVGQtaivnrllwmQNHY----------PLTADDVVLQKTPCsFDVsvweFFW--- 659
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 228 mnaPLMSGAT-VLIEPQF--SPASVFKLVKQQQVTIFAGVPTMYNYLFQH--ENGKKDDFSSIRLCISGGAAMPVALLTA 302
Cdd:PRK10252 660 ---PFIAGAKlVMAEPEAhrDPLAMQQFFAEYGVTTTHFVPSMLAAFVASltPEGARQSCASLRQVFCSGEALPADLCRE 736
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 303 FEEKFGVTILEGYGLSEAS-PVTCFNPF--DRGRKPGS---IGTSILHVENKVVDPLGRELPAHQVGELIVKGPNVMKGY 376
Cdd:PRK10252 737 WQQLTGAPLHNLYGPTEAAvDVSWYPAFgeELAAVRGSsvpIGYPVWNTGLRILDARMRPVPPGVAGDLYLTGIQLAQGY 816
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 377 YKMP-METEHALKD-----GWLY-TGDLARRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGV--- 446
Cdd:PRK10252 817 LGRPdLTASRFIADpfapgERMYrTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAVTHACvin 896
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1816047872 447 -PDPQSGEAVK--GYVVPkRSGVT--EEDIMQHCETHLAKYKRPAAITFLDDIPKNATGKMLRRAL 507
Cdd:PRK10252 897 qAAATGGDARQlvGYLVS-QSGLPldTSALQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKAL 961
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
3-507 |
3.01e-37 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 147.24 E-value: 3.01e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 3 LVSKLEETASEKPDSIACRFKDHMMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPIN 82
Cdd:PRK05691 1133 LPELLNEQARQTPERIALVWDGGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLD 1212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 83 PLYTPTEIGYMLTNGDVKAIVGVSQLLplyecmhESLPKVELVILcqtgeaepeaadpevrMKMTTFAKILRPTSAAKQN 162
Cdd:PRK05691 1213 PDYPAERLAYMLADSGVELLLTQSHLL-------ERLPQAEGVSA----------------IALDSLHLDSWPSQAPGLH 1269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 163 qeLVPDDTAVILYTSGTTGKPKGAMLTHQNLYSNANDVAGYLGMDERDNVVCALPMfhVFCLTV--CMnAPLMSGATVLI 240
Cdd:PRK05691 1270 --LHGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKAPI--SFDVSVweCF-WPLITGCRLVL 1344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 241 E---PQFSPASVFKLVKQQQVTIFAGVPTMYNyLFQHENGKKDdFSSIRLCISGGAAMPVALLTAFEEKF-GVTILEGYG 316
Cdd:PRK05691 1345 AgpgEHRDPQRIAELVQQYGVTTLHFVPPLLQ-LFIDEPLAAA-CTSLRRLFSGGEALPAELRNRVLQRLpQVQLHNRYG 1422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 317 LSE-ASPVT---CfNPFDRGRKPgsIGTSILHVENKVVDPLGRELPAHQVGELIVKGPNVMKGYYKMPMET-EHALKDGW 391
Cdd:PRK05691 1423 PTEtAINVThwqC-QAEDGERSP--IGRPLGNVLCRVLDAELNLLPPGVAGELCIGGAGLARGYLGRPALTaERFVPDPL 1499
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 392 ------LY-TGDLARRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVgVPDPQSGEAVKGY-VVPKR 463
Cdd:PRK05691 1500 gedgarLYrTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVL-VREGAAGAQLVGYyTGEAG 1578
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1816047872 464 SGVTEEDIMQHCETHLAKYKRPAAITFLDDIPKNATGKMLRRAL 507
Cdd:PRK05691 1579 QEAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRAL 1622
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
24-508 |
4.08e-37 |
|
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: 142.56 E-value: 4.08e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 24 DHMMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYTPTEIGYMLTNGDVKAIV 103
Cdd:cd05939 1 DRHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 104 gVSQLLPLYECMHESLPKvelvilCQTGEAepeaadpevrmkmttfakilrptsaakqnqelvpDDTAVILYTSGTTGKP 183
Cdd:cd05939 81 -FNLLDPLLTQSSTEPPS------QDDVNF----------------------------------RDKLFYIYTSGTTGLP 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 184 KGAMLTHQNLYSNANDVAGYLGMDERDNVVCALPMFHVFCLTVCMNAPLMSGATVLIEPQFSPASVFKLVKQQQVTIFAG 263
Cdd:cd05939 120 KAAVIVHSRYYRIAAGAYYAFGMRPEDVVYDCLPLYHSAGGIMGVGQALLHGSTVVIRKKFSASNFWDDCVKYNCTIVQY 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 264 VPTMYNYLFQHENGKKDDFSSIRLCISGGaaMPVALLTAFEEKFGVT-ILEGYGLSEAspvTCfNPFDRGRKPGSIG--T 340
Cdd:cd05939 200 IGEICRYLLAQPPSEEEQKHNVRLAVGNG--LRPQIWEQFVRRFGIPqIGEFYGATEG---NS-SLVNIDNHVGACGfnS 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 341 SILHVENKV----VDPLGREL---------------PAHQVGELIVKGP-NVMKGYYKmpmETEHALK---------DGW 391
Cdd:cd05939 274 RILPSVYPIrlikVDEDTGELirdsdglcipcqpgePGLLVGKIIQNDPlRRFDGYVN---EGATNKKiardvfkkgDSA 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 392 LYTGDLARRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQS-GEAVKGYVVPKRSGVTEED 470
Cdd:cd05939 351 FLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVYGVEVPGVeGRAGMAAIVDPERKVDLDR 430
|
490 500 510
....*....|....*....|....*....|....*...
gi 1816047872 471 IMQHCETHLAKYKRPAAITFLDDIPKNATGKMLRRALR 508
Cdd:cd05939 431 FSAVLAKSLPPYARPQFIRLLPEVDKTGTFKLQKTDLQ 468
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
3-508 |
4.72e-37 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 146.47 E-value: 4.72e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 3 LVSKLEETASEKPDSIACRF----KDH--MMTYQELNEHIQRFADGLQEAGmEKGDHLALLLGNSPDFIIAFFGALKAGI 76
Cdd:PRK05691 11 LVQALQRRAAQTPDRLALRFladdPGEgvVLSYRDLDLRARTIAAALQARA-SFGDRAVLLFPSGPDYVAAFFGCLYAGV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 77 VVVPInplyTPTEIGYMLTNGDVKAIVGVSQ--LLPLYECMHESLpkvelvilcQTGEAEPEAADPEVRMKMTtfakiLR 154
Cdd:PRK05691 90 IAVPA----YPPESARRHHQERLLSIIADAEprLLLTVADLRDSL---------LQMEELAAANAPELLCVDT-----LD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 155 PTSAAK-QNQELVPDDTAVILYTSGTTGKPKGAMLTHQNLYSNANDVAGYLGMDERDN--VVCALPMFHVFCLTVCMNAP 231
Cdd:PRK05691 152 PALAEAwQEPALQPDDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGIDLNPDdvIVSWLPLYHDMGLIGGLLQP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 232 LMSGA-TVLIEPQF---SPASVFKLVKQQQVTIfAGVPTmYNYLFQHE-----NGKKDDFSSIRLCISGGAAMPVALLTA 302
Cdd:PRK05691 232 IFSGVpCVLMSPAYfleRPLRWLEAISEYGGTI-SGGPD-FAYRLCSErvsesALERLDLSRWRVAYSGSEPIRQDSLER 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 303 FEEKFGV------TILEGYGLSEAspvTCF-----------------NPFDRGR-KPG------SIGTSILHVENKVVDP 352
Cdd:PRK05691 310 FAEKFAAcgfdpdSFFASYGLAEA---TLFvsggrrgqgipaleldaEALARNRaEPGtgsvlmSCGRSQPGHAVLIVDP 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 353 L-GRELPAHQVGELIVKGPNVMKGYYKMPMETEHAL--KDG--WLYTGDLARRdEDGYFYIVDRKKDMIIVGGYNVYPRE 427
Cdd:PRK05691 387 QsLEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTFveHDGrtWLRTGDLGFL-RDGELFVTGRLKDMLIVRGHNLYPQD 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 428 VEEVLYSHPDV--KEAVVVGVPDPQSGEAVKGYVVPKRS---GVTEEDIMQHCETHLAKYKR--PAAITFLDD--IPKNA 498
Cdd:PRK05691 466 IEKTVEREVEVvrKGRVAAFAVNHQGEEGIGIAAEISRSvqkILPPQALIKSIRQAVAEACQeaPSVVLLLNPgaLPKTS 545
|
570
....*....|
gi 1816047872 499 TGKMLRRALR 508
Cdd:PRK05691 546 SGKLQRSACR 555
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
155-513 |
7.75e-37 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 141.67 E-value: 7.75e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 155 PTSAAKQNQELVPDDTAVILY-TSGTTGKPKGAMLTHQNLYSNANDVAGYLGMDeRDNVVCALPMFHVFCLTVCMNApLM 233
Cdd:PRK07445 106 HPPPLPSQGILPNLETGWIMIpTGGSSGQIRFAIHTWETLTASVQGFQRYFQLQ-QVNSFCVLPLYHVSGLMQFMRS-FL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 234 SGATVLIEPqfspasvFKLVKQQQVT-IFAG------VPTMYNYLFQHENGKKDDFSSIRLciSGGAAMPVALLTAfeEK 306
Cdd:PRK07445 184 TGGKLVILP-------YKRLKSGQELpPNPSdfflslVPTQLQRLLQLRPQWLAQFRTILL--GGAPAWPSLLEQA--RQ 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 307 FGVTILEGYGLSE-ASPVTCFNPFDRGRKPGSIGTSILHVenKVvdplgrELPAHQVGELIVKGPNVMKGYYkmPmetEH 385
Cdd:PRK07445 253 LQLRLAPTYGMTEtASQIATLKPDDFLAGNNSSGQVLPHA--QI------TIPANQTGNITIQAQSLALGYY--P---QI 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 386 ALKDGWLYTGDLARRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVVPKRSG 465
Cdd:PRK07445 320 LDSQGIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYVPKDPS 399
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1816047872 466 VTEEDIMQHCETHLAKYKRPAAITFLDDIPKNATGKMLRRALRDILPQ 513
Cdd:PRK07445 400 ISLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQQIAVQ 447
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
27-449 |
1.17e-36 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 141.06 E-value: 1.17e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 27 MTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPlytpteigymltNGDVKAIVGVS 106
Cdd:cd05910 3 LSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDP------------GMGRKNLKQCL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 107 QllplyecmheslpkvelvilcqtgEAEPEAadpevrmkmttFAKILRPtsaakqnqelvpDDTAVILYTSGTTGKPKGA 186
Cdd:cd05910 71 Q------------------------EAEPDA-----------FIGIPKA------------DEPAAILFTSGSTGTPKGV 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 187 MLTHQNLYSNANDVAGYLGMDERDNVVCALPMFHVFcltvcmnAPLMSGATVL--IEP----QFSPASVFKLVKQQQVTI 260
Cdd:cd05910 104 VYRHGTFAAQIDALRQLYGIRPGEVDLATFPLFALF-------GPALGLTSVIpdMDPtrpaRADPQKLVGAIRQYGVSI 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 261 FAGVPTMYNYLFQH--ENGKKddFSSIRLCISGGAAMPVALLTAFEEKF--GVTILEGYGLSEASPVTCF---------- 326
Cdd:cd05910 177 VFGSPALLERVARYcaQHGIT--LPSLRRVLSAGAPVPIALAARLRKMLsdEAEILTPYGATEALPVSSIgsrellattt 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 327 NPFDRGRK-------PGsIGTSILHVENKVVDPLG--RELPAHQVGELIVKGPNVMKGYYKMPMETE-HALKDG----WL 392
Cdd:cd05910 255 AATSGGAGtcvgrpiPG-VRVRIIEIDDEPIAEWDdtLELPRGEIGEITVTGPTVTPTYVNRPVATAlAKIDDNsegfWH 333
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1816047872 393 YTGDLARRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDP 449
Cdd:cd05910 334 RMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVGVGKP 390
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
28-507 |
7.67e-36 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 137.86 E-value: 7.67e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 28 TYQELNEHIQRFA--DGLQEAgmeKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPlYTPTEIGYMLTngdVKAivgv 105
Cdd:PRK08308 10 SKSDFDLRLQRYEemEQFQEA---AGNRFAVCLKDPFDIITLVFFLKEKGASVLPIHP-DTPKEAAIRMA---KRA---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 106 sqllplyECMHeslpkvelvILCQTGEaepeaadpevrmkmttFAKILRPTSAAKQNqelvpddtAVILYTSGTTGKPKg 185
Cdd:PRK08308 79 -------GCHG---------LLYGESD----------------FTKLEAVNYLAEEP--------SLLQYSSGTTGEPK- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 186 amLTHQNLYSNANDVAGY---LGMDERDNVVCALPMFHVFCLTVCMNAPLMSGATVLIEPQFSPASVFKLVKQQQVTIFA 262
Cdd:PRK08308 118 --LIRRSWTEIDREIEAYneaLNCEQDETPIVACPVTHSYGLICGVLAALTRGSKPVIITNKNPKFALNILRNTPQHILY 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 263 GVPTMYNYLFQHENGKKDdFSSIrlcISGGAAMPVALLTAFEEKfGVTILEGYGLSEASPVTCFNPFdrgRKPGSIGTSI 342
Cdd:PRK08308 196 AVPLMLHILGRLLPGTFQ-FHAV---MTSGTPLPEAWFYKLRER-TTYMMQQYGCSEAGCVSICPDM---KSHLDLGNPL 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 343 LHVenKVVDPLGRELPahqvGELIVKgpnvmkgyykmpmetehaLKDGWLYTGDLARRDEDGYFYIVDRKKDMIIVGGYN 422
Cdd:PRK08308 268 PHV--SVSAGSDENAP----EEIVVK------------------MGDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLN 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 423 VYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVVpKRSGVTEEDIMQHCETHLAKYKRPAAITFLDDIPKNATGKM 502
Cdd:PRK08308 324 VYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVI-SHEEIDPVQLREWCIQHLAPYQVPHEIESVTEIPKNANGKV 402
|
....*
gi 1816047872 503 LRRAL 507
Cdd:PRK08308 403 SRKLL 407
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
11-513 |
8.55e-36 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 138.85 E-value: 8.55e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 11 ASEKPDSIACRFKDHMMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYTPTEI 90
Cdd:PRK09029 13 AQVRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 91 gymltngdvkaivgvSQLLPLYECMHeslpkvelvILCQTGEAEPEAADPevrmkmTTFAKILRPTSAAKQNQELvpddt 170
Cdd:PRK09029 93 ---------------EELLPSLTLDF---------ALVLEGENTFSALTS------LHLQLVEGAHAVAWQPQRL----- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 171 AVILYTSGTTGKPKGAMLTHQNLYSNANDVAGYLGMDERDNVVCALPMFHVFCLTVcMNAPLMSGAT-VLIEPQFSPASV 249
Cdd:PRK09029 138 ATMTLTSGSTGLPKAAVHTAQAHLASAEGVLSLMPFTAQDSWLLSLPLFHVSGQGI-VWRWLYAGATlVVRDKQPLEQAL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 250 fklvkqQQVTIFAGVPTMYNYLFQHENGKkddfSSIRLCISGGAAMPVALlTAFEEKFGVTILEGYGLSE-ASPVtCFNP 328
Cdd:PRK09029 217 ------AGCTHASLVPTQLWRLLDNRSEP----LSLKAVLLGGAAIPVEL-TEQAEQQGIRCWCGYGLTEmASTV-CAKR 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 329 FDRgrKPGsIGTSILHVENKVVDplgrelpahqvGELIVKGPNVMKGYYK----MPMETEhalkDGWLYTGDLARRDeDG 404
Cdd:PRK09029 285 ADG--LAG-VGSPLPGREVKLVD-----------GEIWLRGASLALGYWRqgqlVPLVND----EGWFATRDRGEWQ-NG 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 405 YFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGE---AvkgyVVPKRSGVTEEDIMQHCETHLAK 481
Cdd:PRK09029 346 ELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVPVADAEFGQrpvA----VVESDSEAAVVNLAEWLQDKLAR 421
|
490 500 510
....*....|....*....|....*....|..
gi 1816047872 482 YKRPAAITFLDDIPKNATGKMLRRALRDILPQ 513
Cdd:PRK09029 422 FQQPVAYYLLPPELKNGGIKISRQALKEWVAQ 453
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
2-455 |
3.64e-35 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 139.09 E-value: 3.64e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 2 NLVSKLEETASEKPDSIACRFKD---------HMMTYQELNEHIQRFADGLQEAGmEKGDHLALLLGNSPDFIIAFFGAL 72
Cdd:PRK07769 22 NLVRHVERWAKVRGDKLAYRFLDfsterdgvaRDLTWSQFGARNRAVGARLQQVT-KPGDRVAILAPQNLDYLIAFFGAL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 73 KAGIVVVpinPLYTPTEIGYMltnGDVKAIVGvsqllplyECMheslPKvelVILCQTGEAE---------PEAADPEVr 143
Cdd:PRK07769 101 YAGRIAV---PLFDPAEPGHV---GRLHAVLD--------DCT----PS---AILTTTDSAEgvrkffrarPAKERPRV- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 144 mkmttFAKILRPTSAAK--QNQELVPDDTAVILYTSGTTGKPKGAMLTHQNLYSNANDVAGYLGMDERDNVVCALPMFHV 221
Cdd:PRK07769 159 -----IAVDAVPDEVGAtwVPPEANEDTIAYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALEGQEGDRGVSWLPFFHD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 222 FCLTVCMNAPLMSGATVLIEPQFSPASVFKLVKQQQVT------IFAGVPtmyNYLFQH-------ENGKKD-DFSSIRL 287
Cdd:PRK07769 234 MGLITVLLPALLGHYITFMSPAAFVRRPGRWIRELARKpggtggTFSAAP---NFAFEHaaarglpKDGEPPlDLSNVKG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 288 CISGGAAMPVALLTAFEEKFG------VTILEGYGLSEASPVTCFNPF---------DR-----GR-------------- 333
Cdd:PRK07769 311 LLNGSEPVSPASMRKFNEAFApyglppTAIKPSYGMAEATLFVSTTPMdeeptviyvDRdelnaGRfvevpadapnavaq 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 334 -KPGSIGTSILHVenkVVDP-LGRELPAHQVGELIVKGPNVMKGYYKMPMETE--------------HAL----KDGWLY 393
Cdd:PRK07769 391 vSAGKVGVSEWAV---IVDPeTASELPDGQIGEIWLHGNNIGTGYWGKPEETAatfqnilksrlsesHAEgapdDALWVR 467
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1816047872 394 TGDLARRdEDGYFYIVDRKKDMIIVGGYNVYPREVEevlYSHPDVKEAVVVG------VPDPQSGEAV 455
Cdd:PRK07769 468 TGDYGVY-FDGELYITGRVKDLVIIDGRNHYPQDLE---YTAQEATKALRTGyvaafsVPANQLPQVV 531
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
22-504 |
1.45e-34 |
|
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: 136.27 E-value: 1.45e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 22 FKDHMMTYQELNEHIQRFADGL-QEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYTPTEIGYMLTNGDVK 100
Cdd:cd05938 1 FEGETYTYRDVDRRSNQAARALlAHAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 101 AIVGVSQLLPLYECMHESLPKVELVILCQTGEAEPEAadpevrmkMTTFAKILRPTSA----AKQNQELVPDDTAVILYT 176
Cdd:cd05938 81 VLVVAPELQEAVEEVLPALRADGVSVWYLSHTSNTEG--------VISLLDKVDAASDepvpASLRAHVTIKSPALYIYT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 177 SGTTGKPKGAMLTHQNLYSNANdVAGYLGMDERDNVVCALPMFHVFCLTVCMNAPLMSGATVLIEPQFSPASVFKLVKQQ 256
Cdd:cd05938 153 SGTTGLPKAARISHLRVLQCSG-FLSLCGVTADDVIYITLPLYHSSGFLLGIGGCIELGATCVLKPKFSASQFWDDCRKH 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 257 QVTIFAGVPTMYNYLFQHENGKKDDFSSIRLCISGGAAMPValLTAFEEKFG-VTILEGYGLSEASpVTCFNpfdRGRKP 335
Cdd:cd05938 232 NVTVIQYIGELLRYLCNQPQSPNDRDHKVRLAIGNGLRADV--WREFLRRFGpIRIREFYGSTEGN-IGFFN---YTGKI 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 336 GSIG-TSILH--------------VENKVVDPLGR--ELPAHQVGELIVK----GPNVmkGYYKMPMETEHAL-----KD 389
Cdd:cd05938 306 GAVGrVSYLYkllfpfelikfdveKEEPVRDAQGFciPVAKGEPGLLVAKitqqSPFL--GYAGDKEQTEKKLlrdvfKK 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 390 GWLY--TGDLARRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDP-QSGEAVKGYVVPKRSGV 466
Cdd:cd05938 384 GDVYfnTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVYGVTVPgHEGRIGMAAVKLKPGHE 463
|
490 500 510
....*....|....*....|....*....|....*....
gi 1816047872 467 TE-EDIMQHCETHLAKYKRPAAITFLDDIPKNATGKMLR 504
Cdd:cd05938 464 FDgKKLYQHVREYLPAYARPRFLRIQDSLEITGTFKQQK 502
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
1-507 |
7.86e-34 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 133.87 E-value: 7.86e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 1 MNLVSKLEETASEKPDSIACRFKDHMMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVP 80
Cdd:PRK04813 2 MDIIETIEEFAQTQPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 81 INpLYTPTEigymltngDVKAIVGVSQllplyecmheslPkvELVIlcQTGEAEPEAADPEVrMKMTTFAKILRPTSAAK 160
Cdd:PRK04813 82 VD-VSSPAE--------RIEMIIEVAK------------P--SLII--ATEELPLEILGIPV-ITLDELKDIFATGNPYD 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 161 QNQELVPDDTAVILYTSGTTGKPKGAMLTHQNLYSNANDVAGYLGMDERdNVVCALPMFHvFCLTVCMNAP-LMSGATVL 239
Cdd:PRK04813 136 FDHAVKGDDNYYIIFTSGTTGKPKGVQISHDNLVSFTNWMLEDFALPEG-PQFLNQAPYS-FDLSVMDLYPtLASGGTLV 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 240 IEPQ---FSPASVFKLVKQQQVTIFAGVPT-----MYNYLFQHENgkKDDFSSIRLCisgGAAMPV----ALLTAFEEkf 307
Cdd:PRK04813 214 ALPKdmtANFKQLFETLPQLPINVWVSTPSfadmcLLDPSFNEEH--LPNLTHFLFC---GEELPHktakKLLERFPS-- 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 308 gVTILEGYGLSEAS------PVT--CFNPFDR---GR-KPGSigtsilhvENKVVDPLGRELPAHQVGELIVKGPNVMKG 375
Cdd:PRK04813 287 -ATIYNTYGPTEATvavtsiEITdeMLDQYKRlpiGYaKPDS--------PLLIIDEEGTKLPDGEQGEIVISGPSVSKG 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 376 YYKMPMETEHALK--DG-WLY-TGDLARRDeDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQS 451
Cdd:PRK04813 358 YLNNPEKTAEAFFtfDGqPAYhTGDAGYLE-DGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVVPYNKDHK 436
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1816047872 452 GEAVKGYVVPKRSGVTEE-----DIMQHCETHLAKYKRPAAITFLDDIPKNATGKMLRRAL 507
Cdd:PRK04813 437 VQYLIAYVVPKEEDFEREfeltkAIKKELKERLMEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
2-399 |
2.18e-31 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 127.85 E-value: 2.18e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 2 NLVSKLEETASEKPDS--IACRFKDH----MMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAG 75
Cdd:PRK12582 50 SIPHLLAKWAAEAPDRpwLAQREPGHgqwrKVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAG 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 76 IVVVPINPLYTpteigyMLTNGDVK----------AIVGVSQLLPLYECMHE-SLPKVELVILcqTGEAEPEAADPEVRM 144
Cdd:PRK12582 130 VPAAPVSPAYS------LMSHDHAKlkhlfdlvkpRVVFAQSGAPFARALAAlDLLDVTVVHV--TGPGEGIASIAFADL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 145 KMTTfakilrPTSAAKQNQE-LVPDDTAVILYTSGTTGKPKGAMLTHQNLYSNANDVAGyLGMDERD----NVVCALPMF 219
Cdd:PRK12582 202 AATP------PTAAVAAAIAaITPDTVAKYLFTSGSTGMPKAVINTQRMMCANIAMQEQ-LRPREPDppppVSLDWMPWN 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 220 HVFCLTVCMNAPLMSGATVLIEP------QFSPasVFKLVKQQQVTIFAGVPTMYNYLFQHEngKKDD------FSSIRL 287
Cdd:PRK12582 275 HTMGGNANFNGLLWGGGTLYIDDgkplpgMFEE--TIRNLREISPTVYGNVPAGYAMLAEAM--EKDDalrrsfFKNLRL 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 288 CISGGAAMPVAL------LTAFEEKFGVTILEGYGLSEASPVTCFNPFDRGRkPGSIGTSILHVENKVVdPLGRELpahq 361
Cdd:PRK12582 351 MAYGGATLSDDLyermqaLAVRTTGHRIPFYTGYGATETAPTTTGTHWDTER-VGLIGLPLPGVELKLA-PVGDKY---- 424
|
410 420 430
....*....|....*....|....*....|....*....
gi 1816047872 362 vgELIVKGPNVMKGYYKMPMETEHAL-KDGWLYTGDLAR 399
Cdd:PRK12582 425 --EVRVKGPNVTPGYHKDPELTAAAFdEEGFYRLGDAAR 461
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
1-429 |
1.37e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 125.44 E-value: 1.37e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 1 MNLVSKLEETASEKPDSIACRFKD---------HMMTYQELNEHIQRFADGLQEAGmEKGDHLALLLGNSPDFIIAFFGA 71
Cdd:PRK05850 1 SSVPSLLRERASLQPDDAAFTFIDyeqdpagvaETLTWSQLYRRTLNVAEELRRHG-STGDRAVILAPQGLEYIVAFLGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 72 LKAGIVVVPIN-PLY--------------TPTEIgymLTN----GDVKAIVGVSQLlplyecmhESLPKVelvilcqtge 132
Cdd:PRK05850 80 LQAGLIAVPLSvPQGgahdervsavlrdtSPSVV---LTTsavvDDVTEYVAPQPG--------QSAPPV---------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 133 AEPEAADPEVRmkmttfakilRPTSAAKQNqelvPDDTAVILYTSGTTGKPKGAMLTHQNLYSNANDV-AGYLGMDER-- 209
Cdd:PRK05850 139 IEVDLLDLDSP----------RGSDARPRD----LPSTAYLQYTSGSTRTPAGVMVSHRNVIANFEQLmSDYFGDTGGvp 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 210 ---DNVVCALPMFHVFCLTVCMNAPLMSG-ATVLIEP-QF--SPASVFKLVKQQQVTIFAGvPtmyNYLFQHENGK-KD- 280
Cdd:PRK05850 205 ppdTTVVSWLPFYHDMGLVLGVCAPILGGcPAVLTSPvAFlqRPARWMQLLASNPHAFSAA-P---NFAFELAVRKtSDd 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 281 -----DFSSIRLCISGGAAMPVALLTAFEEKFG------VTILEGYGLSEA------------SPVTCFNP--FDRG--- 332
Cdd:PRK05850 281 dmaglDLGGVLGIISGSERVHPATLKRFADRFApfnlreTAIRPSYGLAEAtvyvatrepgqpPESVRFDYekLSAGhak 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 333 RKPGSIGTSIL--HVEN----KVVDP-LGRELPAHQVGELIVKGPNVMKGYYKMPMETEHALK-----------DG-WLY 393
Cdd:PRK05850 361 RCETGGGTPLVsyGSPRsptvRIVDPdTCIECPAGTVGEIWVHGDNVAAGYWQKPEETERTFGatlvdpspgtpEGpWLR 440
|
490 500 510
....*....|....*....|....*....|....*.
gi 1816047872 394 TGDLARRDeDGYFYIVDRKKDMIIVGGYNVYPREVE 429
Cdd:PRK05850 441 TGDLGFIS-EGELFIVGRIKDLLIVDGRNHYPDDIE 475
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
7-410 |
7.87e-30 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 123.45 E-value: 7.87e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 7 LEETASEKPDS--IACRFKDH---MMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPI 81
Cdd:PRK08180 45 LVHWAQEAPDRvfLAERGADGgwrRLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALAAMYAGVPYAPV 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 82 NPlytpteiGYMLTNGDVKAIVGVSQLLPlyecmheslPKVelvILCQTGEA------EPEAADPEV--------RMKMT 147
Cdd:PRK08180 125 SP-------AYSLVSQDFGKLRHVLELLT---------PGL---VFADDGAAfaralaAVVPADVEVvavrgavpGRAAT 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 148 TFAKIL---RPTSAAKQNQELVPDDTAVILYTSGTTGKPKGAMLTHQNLYSNA---NDVAGYLGmDERDNVVCALPMFHV 221
Cdd:PRK08180 186 PFAALLatpPTAAVDAAHAAVGPDTIAKFLFTSGSTGLPKAVINTHRMLCANQqmlAQTFPFLA-EEPPVLVDWLPWNHT 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 222 FCLTVCMNAPLMSGATVLIEP-QFSPASVFKLV---KQQQVTIFAGVPTMYNYLFQHEngKKDD------FSSIRLCISG 291
Cdd:PRK08180 265 FGGNHNLGIVLYNGGTLYIDDgKPTPGGFDETLrnlREISPTVYFNVPKGWEMLVPAL--ERDAalrrrfFSRLKLLFYA 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 292 GAAMPVALLTAFE--------EKfgVTILEGYGLSEASPVTCF--NPFDRgrkPGSIGTSILHVENKVVdPLGRELpahq 361
Cdd:PRK08180 343 GAALSQDVWDRLDrvaeatcgER--IRMMTGLGMTETAPSATFttGPLSR---AGNIGLPAPGCEVKLV-PVGGKL---- 412
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1816047872 362 vgELIVKGPNVMKGYYKMPMETEHALkdgwlytgdlarrDEDGYFYIVD 410
Cdd:PRK08180 413 --EVRVKGPNVTPGYWRAPELTAEAF-------------DEEGYYRSGD 446
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
168-508 |
3.61e-29 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 118.22 E-value: 3.61e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 168 DDTAVILYTSGTTGKPKGAMLTHQNLYSNANDVAGYLGMDERdnVVCALPMFHVFCLTVCMNApLMSGATVLI------- 240
Cdd:PRK07824 35 DDVALVVATSGTTGTPKGAMLTAAALTASADATHDRLGGPGQ--WLLALPAHHIAGLQVLVRS-VIAGSEPVEldvsagf 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 241 EPQFSPASVFKLVKQQQVTIFagVPTMYNYLFQHENGKKD--DFSSIRLcisGGAAMPVALLTAFEEkFGVTILEGYGLS 318
Cdd:PRK07824 112 DPTALPRAVAELGGGRRYTSL--VPMQLAKALDDPAATAAlaELDAVLV---GGGPAPAPVLDAAAA-AGINVVRTYGMS 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 319 EASPvTCfnpfdrgrkpgsigtsilhvenkVVDplGRELPAHQV----GELIVKGPNVMKGYYKMPMETEHAlKDGWLYT 394
Cdd:PRK07824 186 ETSG-GC-----------------------VYD--GVPLDGVRVrvedGRIALGGPTLAKGYRNPVDPDPFA-EPGWFRT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 395 GDLARRDeDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVVPK-RSGVTEEDIMQ 473
Cdd:PRK07824 239 DDLGALD-DGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAVVGDgGPAPTLEALRA 317
|
330 340 350
....*....|....*....|....*....|....*
gi 1816047872 474 HCETHLAKYKRPAAITFLDDIPKNATGKMLRRALR 508
Cdd:PRK07824 318 HVARTLDRTAAPRELHVVDELPRRGIGKVDRRALV 352
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
2-508 |
7.58e-29 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 120.23 E-value: 7.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 2 NLVSKLEETASEKPDSIACRFKDHM---------MTYQELN-------EHIQRFAdglqeagmEKGDHLALLLGNSPDFI 65
Cdd:PRK12476 35 TLISLIERNIANVGDTVAYRYLDHShsaagcaveLTWTQLGvrlravgARLQQVA--------GPGDRVAILAPQGIDYV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 66 IAFFGALKAGIVVVPinpLYTPTEIGYMltngdvkaivgvsqllplyECMHESLPKVE-LVILCQTGEAEPE----AADP 140
Cdd:PRK12476 107 AGFFAAIKAGTIAVP---LFAPELPGHA-------------------ERLDTALRDAEpTVVLTTTAAAEAVegflRNLP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 141 EV-RMKMTTFAKIlrPTSAAK--QNQELVPDDTAVILYTSGTTGKPKGAMLTHQNLYSNANDVAGYLGMDERD-NVVCAL 216
Cdd:PRK12476 165 RLrRPRVIAIDAI--PDSAGEsfVPVELDTDDVSHLQYTSGSTRPPVGVEITHRAVGTNLVQMILSIDLLDRNtHGVSWL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 217 PMFHVFCLTVCMNAPLMSGATVLIEPQFSPASVFKLVKQ-----QQVTIFAGVPTM-YNYLFQH---ENGKKDDFSSIRL 287
Cdd:PRK12476 243 PLYHDMGLSMIGFPAVYGGHSTLMSPTAFVRRPQRWIKAlsegsRTGRVVTAAPNFaYEWAAQRglpAEGDDIDLSNVVL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 288 cISGGAAMPVALLTAFEEKFG------VTILEGYGLSEASP-VTCFNP--------FDR-----GRK---PGSIGTSILH 344
Cdd:PRK12476 323 -IIGSEPVSIDAVTTFNKAFApyglprTAFKPSYGIAEATLfVATIAPdaepsvvyLDReqlgaGRAvrvAADAPNAVAH 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 345 VE---------NKVVDP-LGRELPAHQVGELIVKGPNVMKGYYKMPMETE---HA-----LKDG-----------WLYTG 395
Cdd:PRK12476 402 VScgqvarsqwAVIVDPdTGAELPDGEVGEIWLHGDNIGRGYWGRPEETErtfGAklqsrLAEGshadgaaddgtWLRTG 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 396 DLARRdEDGYFYIVDRKKDMIIVGGYNVYPREVE-EVLYSHPDVKEAVVVG--VPDPQSGEAVkgyVVPKR-SGVTEEDI 471
Cdd:PRK12476 482 DLGVY-LDGELYITGRIADLIVIDGRNHYPQDIEaTVAEASPMVRRGYVTAftVPAEDNERLV---IVAERaAGTSRADP 557
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 1816047872 472 MQHCETHLAKYKRPAAITFLD-------DIPKNATGKMLRRALR 508
Cdd:PRK12476 558 APAIDAIRAAVSRRHGLAVADvrlvpagAIPRTTSGKLARRACR 601
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
51-456 |
8.11e-29 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 119.92 E-value: 8.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 51 GDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYTPTEIGYMLTNGDVKAIVGVSQLLP-LYECMHESLPKVELVILCQ 129
Cdd:PRK06334 67 DQHIGIMMPASAGAYIAYFATLLSGKIPVMINWSQGLREVTACANLVGVTHVLTSKQLMQhLAQTHGEDAEYPFSLIYME 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 130 tgeaepeaadpEVRMKMTTFAKI-------------LRPTSAAKQNqelvPDDTAVILYTSGTTGKPKGAMLTHQNLYSN 196
Cdd:PRK06334 147 -----------EVRKELSFWEKCrigiymsipfewlMRWFGVSDKD----PEDVAVILFTSGTEKLPKGVPLTHANLLAN 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 197 ANDVAGYLGMDERDNVVCALPMFHVFCLTVCMNAPLMSGATVLIEPQ-FSPASVFKLVKQQQVTIFAGVPTMYNYLFQHE 275
Cdd:PRK06334 212 QRACLKFFSPKEDDVMMSFLPPFHAYGFNSCTLFPLLSGVPVVFAYNpLYPKKIVEMIDEAKVTFLGSTPVFFDYILKTA 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 276 NGKKDDFSSIRLCISGGAAMPVALLTAFEEKF-GVTILEGYGLSEASPVTCFNPFDRGRKPGSIGTSILHVENKVVDPLG 354
Cdd:PRK06334 292 KKQESCLPSLRFVVIGGDAFKDSLYQEALKTFpHIQLRQGYGTTECSPVITINTVNSPKHESCVGMPIRGMDVLIVSEET 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 355 R-ELPAHQVGELIVKGPNVMKGYykMPMETEHAL----KDGWLYTGDLARRDEDGYFYIVDRKKDMIIVGGYNVYPREVE 429
Cdd:PRK06334 372 KvPVSSGETGLVLTRGTSLFSGY--LGEDFGQGFvelgGETWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALE 449
|
410 420 430
....*....|....*....|....*....|...
gi 1816047872 430 EVLYSH------PDVKEAVVVGVPdpqsGEAVK 456
Cdd:PRK06334 450 SILMEGfgqnaaDHAGPLVVCGLP----GEKVR 478
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
28-444 |
3.91e-28 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 118.38 E-value: 3.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 28 TYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYTPTEIGYMLTNGDVKAI-VGVS 106
Cdd:PLN02430 78 TYKEVYEEVLQIGSALRASGAEPGSRVGIYGSNCPQWIVAMEACAAHSLICVPLYDTLGPGAVDYIVDHAEIDFVfVQDK 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 107 QLLPLYECMHESLPKVELVILCQTGEAEPEAADPEVRMKMTTFAKILRptsAAKQNQELV----PDDTAVILYTSGTTGK 182
Cdd:PLN02430 158 KIKELLEPDCKSAKRLKAIVSFTSVTEEESDKASQIGVKTYSWIDFLH---MGKENPSETnppkPLDICTIMYTSGTSGD 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 183 PKGAMLTHQNLYSNANDVAGYL-----GMDERDNVVCALPMFHVFcltvcmnaplmsgaTVLIEPQF--SPASVFKL--- 252
Cdd:PLN02430 235 PKGVVLTHEAVATFVRGVDLFMeqfedKMTHDDVYLSFLPLAHIL--------------DRMIEEYFfrKGASVGYYhgd 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 253 -------VKQQQVTIFAGVPTMY----------------------NYLFQHE-----NGKKDDFSS-------------- 284
Cdd:PLN02430 301 lnalrddLMELKPTLLAGVPRVFerihegiqkalqelnprrrlifNALYKYKlawmnRGYSHKKASpmadflafrkvkak 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 285 ----IRLCISGGAAmpvaLLTAFEEKFGVT----ILEGYGLSEA-SPVTCFNPfDRGRKPGSIGTSILHVENKV------ 349
Cdd:PLN02430 381 lggrLRLLISGGAP----LSTEIEEFLRVTscafVVQGYGLTETlGPTTLGFP-DEMCMLGTVGAPAVYNELRLeevpem 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 350 -VDPLGrELPAhqvGELIVKGPNVMKGYYKMPMETEHALKDGWLYTGDLARRDEDGYFYIVDRKKDMIIVGGYNVYPREV 428
Cdd:PLN02430 456 gYDPLG-EPPR---GEICVRGKCLFSGYYKNPELTEEVMKDGWFHTGDIGEILPNGVLKIIDRKKNLIKLSQGEYVALEY 531
|
490
....*....|....*.
gi 1816047872 429 EEVLYSHPDVKEAVVV 444
Cdd:PLN02430 532 LENVYGQNPIVEDIWV 547
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
27-435 |
5.10e-28 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 118.15 E-value: 5.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 27 MTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYTPTEIGYMLTNGDVKAIV--- 103
Cdd:PTZ00216 122 ITYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAIVcng 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 104 -GVSQLLPLyecMHES-LPKVELVILcqtgEAEPEAADPEvRMKMTTFAKILRpTSAAKQNQELVP-----DDTAVILYT 176
Cdd:PTZ00216 202 kNVPNLLRL---MKSGgMPNTTIIYL----DSLPASVDTE-GCRLVAWTDVVA-KGHSAGSHHPLNipennDDLALIMYT 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 177 SGTTGKPKGAMLTHQNLYSNANDVAGYL----GMDERDNVVCA-LPMFHVFCLTVcMNAPLMSGATV------------- 238
Cdd:PTZ00216 273 SGTTGDPKGVMHTHGSLTAGILALEDRLndliGPPEEDETYCSyLPLAHIMEFGV-TNIFLARGALIgfgsprtltdtfa 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 239 -----LIEpqFSPasvfklvkqqqvTIFAGVP------------------TMYNYLFQH---------ENGKKDDF---- 282
Cdd:PTZ00216 352 rphgdLTE--FRP------------VFLIGVPrifdtikkaveaklppvgSLKRRVFDHayqsrlralKEGKDTPYwnek 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 283 ----------SSIRLCISGGAAMPVALLTAFEEKFGVTIlEGYGLSEAspvTCFNPFDR-GR-KPGSIGTSILHVENKVV 350
Cdd:PTZ00216 418 vfsapravlgGRVRAMLSGGGPLSAATQEFVNVVFGMVI-QGWGLTET---VCCGGIQRtGDlEPNAVGQLLKGVEMKLL 493
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 351 D---------PLGRelpahqvGELIVKGPNVMKGYYKMPMETEHAL-KDGWLYTGDLARRDEDGYFYIVDRKKDMI--IV 418
Cdd:PTZ00216 494 DteeykhtdtPEPR-------GEILLRGPFLFKGYYKQEELTREVLdEDGWFHTGDVGSIAANGTLRIIGRVKALAknCL 566
|
490
....*....|....*..
gi 1816047872 419 GGYnvYPREVEEVLYSH 435
Cdd:PTZ00216 567 GEY--IALEALEALYGQ 581
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
7-410 |
9.51e-27 |
|
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.
Pssm-ID: 341245 [Multi-domain] Cd Length: 561 Bit Score: 113.68 E-value: 9.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 7 LEETASEKPDSI--ACRFKDH---MMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPI 81
Cdd:cd05921 1 LAHWARQAPDRTwlAEREGNGgwrRVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 82 NPLYTpteigymLTNGDVKAIVGVSQLLPLYECMHESLPKVELVIlcqtgeAEPEAADPEV--------RMKMTTFAKIL 153
Cdd:cd05921 81 SPAYS-------LMSQDLAKLKHLFELLKPGLVFAQDAAPFARAL------AAIFPLGTPLvvsrnavaGRGAISFAELA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 154 R--PTSAAKQNQELV-PDDTAVILYTSGTTGKPKGAMLTHQNLYSNANDVAGYLGM--DERDNVVCALPMFHVFCLTVCM 228
Cdd:cd05921 148 AtpPTAAVDAAFAAVgPDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFfgEEPPVLVDWLPWNHTFGGNHNF 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 229 NAPLMSGATVLIE-----PQFSPASVFKLvKQQQVTIFAGVPTMYNYLFQHEngKKDD------FSSIRLCISGGAAMPV 297
Cdd:cd05921 228 NLVLYNGGTLYIDdgkpmPGGFEETLRNL-REISPTVYFNVPAGWEMLVAAL--EKDEalrrrfFKRLKLMFYAGAGLSQ 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 298 ALLTAFEE------KFGVTILEGYGLSEASPVTCFNPFDRGRkPGSIGTSILHVENKVVdPLGRELpahqvgELIVKGPN 371
Cdd:cd05921 305 DVWDRLQAlavatvGERIPMMAGLGATETAPTATFTHWPTER-SGLIGLPAPGTELKLV-PSGGKY------EVRVKGPN 376
|
410 420 430
....*....|....*....|....*....|....*....
gi 1816047872 372 VMKGYYKMPMETEHALkdgwlytgdlarrDEDGYFYIVD 410
Cdd:cd05921 377 VTPGYWRQPELTAQAF-------------DEEGFYCLGD 402
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
28-438 |
1.45e-26 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 113.67 E-value: 1.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 28 TYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYTPTEIGYMLTNGDVKA-IVGVS 106
Cdd:PLN02387 108 TYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTvICDSK 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 107 QLLPLYEcMHESLPKVELVILCQTGEAEPEAADPEV-RMKMTTFAKI--LRPTSAAKQNQELvPDDTAVILYTSGTTGKP 183
Cdd:PLN02387 188 QLKKLID-ISSQLETVKRVIYMDDEGVDSDSSLSGSsNWTVSSFSEVekLGKENPVDPDLPS-PNDIAVIMYTSGSTGLP 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 184 KGAMLTHQNLYSNANDVAGYL-GMDERDNVVCALPMFHVFCLTVcmnAPLMSGATVLIEpQFSP---------------- 246
Cdd:PLN02387 266 KGVMMTHGNIVATVAGVMTVVpKLGKNDVYLAYLPLAHILELAA---ESVMAAVGAAIG-YGSPltltdtsnkikkgtkg 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 247 -ASVFKlvkqqqVTIFAGVPTMYNYLFQHENGKKD----------DFS-------------------------------- 283
Cdd:PLN02387 342 dASALK------PTLMTAVPAILDRVRDGVRKKVDakgglakklfDIAykrrlaaiegswfgawglekllwdalvfkkir 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 284 -----SIRLCISGGAAmpvalLTAFEEKF-----GVTILEGYGLSEaspvTC----FNPFDrGRKPGSIGTSILHVENKV 349
Cdd:PLN02387 416 avlggRIRFMLSGGAP-----LSGDTQRFiniclGAPIGQGYGLTE----TCagatFSEWD-DTSVGRVGPPLPCCYVKL 485
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 350 VD-----------PLGRelpahqvGELIVKGPNVMKGYYKMPMETEHALKDG-----WLYTGDLARRDEDGYFYIVDRKK 413
Cdd:PLN02387 486 VSweeggylisdkPMPR-------GEIVIGGPSVTLGYFKNQEKTDEVYKVDergmrWFYTGDIGQFHPDGCLEIIDRKK 558
|
490 500
....*....|....*....|....*..
gi 1816047872 414 DMIIV--GGYnVYPREVEEVLYSHPDV 438
Cdd:PLN02387 559 DIVKLqhGEY-VSLGKVEAALSVSPYV 584
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
24-510 |
2.74e-26 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 113.07 E-value: 2.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 24 DHMMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYTPTEIGYMLTNGDVKAIV 103
Cdd:PLN02654 118 DASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQRIVDCKPKVVI 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 104 GVS------QLLPLYECMHESLPKVEL----VILCQTGEAEP--EAADPEVRMKMTTFAKILRPTSAAKQNQELV-PDDT 170
Cdd:PLN02654 198 TCNavkrgpKTINLKDIVDAALDESAKngvsVGICLTYENQLamKREDTKWQEGRDVWWQDVVPNYPTKCEVEWVdAEDP 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 171 AVILYTSGTTGKPKGAMLThqnlysnandVAGYLgmderdnVVCALPMFHVF---------CLTVC---------MNAPL 232
Cdd:PLN02654 278 LFLLYTSGSTGKPKGVLHT----------TGGYM-------VYTATTFKYAFdykptdvywCTADCgwitghsyvTYGPM 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 233 MSGATVLI---EPQF-SPASVFKLVKQQQVTIFAGVPTMYNYLFQHENGKKDDFSSIRLCISGGAAMPVALlTAFEEKFG 308
Cdd:PLN02654 341 LNGATVLVfegAPNYpDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGDEYVTRHSRKSLRVLGSVGEPINP-SAWRWFFN 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 309 VT------ILEGYGLSEA-----SPVTCFNPfdrgRKPGSIGTSILHVENKVVDPLGRELPAHQVGELIVKG--PNVMKG 375
Cdd:PLN02654 420 VVgdsrcpISDTWWQTETggfmiTPLPGAWP----QKPGSATFPFFGVQPVIVDEKGKEIEGECSGYLCVKKswPGAFRT 495
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 376 YY--KMPMETEH-ALKDGWLYTGDLARRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSG 452
Cdd:PLN02654 496 LYgdHERYETTYfKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEVKG 575
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1816047872 453 EAVKGYV-----VPKRSGVTEEDIMQhCETHLAKYKRPAAITFLDDIPKNATGKMLRRALRDI 510
Cdd:PLN02654 576 QGIYAFVtlvegVPYSEELRKSLILT-VRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRKI 637
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
427-501 |
7.19e-26 |
|
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: 100.70 E-value: 7.19e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1816047872 427 EVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVVPKR-SGVTEEDIMQHCETHLAKYKRPAAITFLDDIPKNATGK 501
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPgVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
27-415 |
3.13e-25 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 109.55 E-value: 3.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 27 MTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYTPTEIGYMLTNGDVK-AIVGV 105
Cdd:PLN02861 78 LTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVSiAFVQE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 106 SQLLPLYECmhesLPKVE--LVILCQTGEAEPEAADPEVRMKMTTFAKILRPtSAAKQNQELVP---DDTAVILYTSGTT 180
Cdd:PLN02861 158 SKISSILSC----LPKCSsnLKTIVSFGDVSSEQKEEAEELGVSCFSWEEFS-LMGSLDCELPPkqkTDICTIMYTSGTT 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 181 GKPKGAMLThqnlysNANDVAGYLGMD-----------ERDNVVCALPMFHVFClTVCMNAPLMSGATVliepQFSPASV 249
Cdd:PLN02861 233 GEPKGVILT------NRAIIAEVLSTDhllkvtdrvatEEDSYFSYLPLAHVYD-QVIETYCISKGASI----GFWQGDI 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 250 FKLVKQQQV---TIFAGVPTMYN------------------YLFQH---------ENGKKDDFSS--------------- 284
Cdd:PLN02861 302 RYLMEDVQAlkpTIFCGVPRVYDriytgimqkissggmlrkKLFDFaynyklgnlRKGLKQEEASprldrlvfdkikegl 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 285 ---IRLCISGGAAMPVALltafEEKFGVT----ILEGYGLSEaSPVTCFNPF-DRGRKPGSIGTSILHVENKV--VDPLG 354
Cdd:PLN02861 382 ggrVRLLLSGAAPLPRHV----EEFLRVTscsvLSQGYGLTE-SCGGCFTSIaNVFSMVGTVGVPMTTIEARLesVPEMG 456
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1816047872 355 RE-LPAHQVGELIVKGPNVMKGYYKMPMETEHALKDGWLYTGDLARRDEDGYFYIVDRKKDM 415
Cdd:PLN02861 457 YDaLSDVPRGEICLRGNTLFSGYHKRQDLTEEVLIDGWFHTGDIGEWQPNGAMKIIDRKKNI 518
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
28-449 |
5.91e-24 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 105.87 E-value: 5.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 28 TYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYTPTEIGYMLTNGDVK-AIVGVS 106
Cdd:PLN02614 81 TYQEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSiVFVEEK 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 107 QLLPLYECMHESLPKVELVIlcQTGEAEPEAADPEVRMKMTTFA--KILRpTSAAKQNQELV--PDDTAVILYTSGTTGK 182
Cdd:PLN02614 161 KISELFKTCPNSTEYMKTVV--SFGGVSREQKEEAETFGLVIYAwdEFLK-LGEGKQYDLPIkkKSDICTIMYTSGTTGD 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 183 PKGAMLTHQNLYSNANDVAGYLG-----MDERDNVVCALPMFHVF--CLTVCMnapLMSGATVliepQFSPASVFKLVK- 254
Cdd:PLN02614 238 PKGVMISNESIVTLIAGVIRLLKsanaaLTVKDVYLSYLPLAHIFdrVIEECF---IQHGAAI----GFWRGDVKLLIEd 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 255 --QQQVTIFAGVP----TMYNYLFQHENG----KKDDFSS-------------------------------------IRL 287
Cdd:PLN02614 311 lgELKPTIFCAVPrvldRVYSGLQKKLSDggflKKFVFDSafsykfgnmkkgqshveasplcdklvfnkvkqglggnVRI 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 288 CISGGAAMPVALLTAFEEKFGVTILEGYGLSEASPVTCFNPFDRGRKPGSIGTSILHVENKV-------VDPLGrelpAH 360
Cdd:PLN02614 391 ILSGAAPLASHVESFLRVVACCHVLQGYGLTESCAGTFVSLPDELDMLGTVGPPVPNVDIRLesvpemeYDALA----ST 466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 361 QVGELIVKGPNVMKGYYKMPMETEHALKDGWLYTGDLARRDEDGYFYIVDRKKDMIIV--GGY-------NVYPR-EVEE 430
Cdd:PLN02614 467 PRGEICIRGKTLFSGYYKREDLTKEVLIDGWLHTGDVGEWQPNGSMKIIDRKKNIFKLsqGEYvavenieNIYGEvQAVD 546
|
490
....*....|....*....
gi 1816047872 431 VLYSHPDVKEAVVVGVPDP 449
Cdd:PLN02614 547 SVWVYGNSFESFLVAIANP 565
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
137-511 |
1.64e-22 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 100.61 E-value: 1.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 137 AADPEVRMK-MTTFAKILRPTSAAKQNqelvPDDTAVILYTSGTTGKPKGAMLTHQNLYSNANDVAGYLGMDERDNVVCA 215
Cdd:PRK05851 124 AVDSSVTVHdLATAAHTNRSASLTPPD----SGGPAVLQGTAGSTGTPRTAILSPGAVLSNLRGLNARVGLDAATDVGCS 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 216 -LPMFHVFCLTVCMNApLMSGATVLIEPQ--FSpASVFKLVK---QQQVTIFAGvPTM-YNYLFQHENGKKD-DFSSIRL 287
Cdd:PRK05851 200 wLPLYHDMGLAFLLTA-ALAGAPLWLAPTtaFS-ASPFRWLSwlsDSRATLTAA-PNFaYNLIGKYARRVSDvDLGALRV 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 288 CISGGAAMPVALLTAFEE---KFGV---TILEGYGLSEAS-PVTCFNP-----FDR--------GRKPGSIGTSILHVEN 347
Cdd:PRK05851 277 ALNGGEPVDCDGFERFATamaPFGFdagAAAPSYGLAESTcAVTVPVPgiglrVDEvttddgsgARRHAVLGNPIPGMEV 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 348 KVVDPLG-RELPAHQVGELIVKGPNVMKGYY-KMPMEtehalKDGWLYTGDLARRDEDGyFYIVDRKKDMIIVGGYNVYP 425
Cdd:PRK05851 357 RISPGDGaAGVAGREIGEIEIRGASMMSGYLgQAPID-----PDDWFPTGDLGYLVDGG-LVVCGRAKELITVAGRNIFP 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 426 REVEEVLYSHPDVKEAVVVGVpDPQSGEAVKGYVV------PKRSGVTEEDIMQ---HCEThlakykRPAAITFLD--DI 494
Cdd:PRK05851 431 TEIERVAAQVRGVREGAVVAV-GTGEGSARPGLVIaaefrgPDEAGARSEVVQRvasECGV------VPSDVVFVApgSL 503
|
410
....*....|....*..
gi 1816047872 495 PKNATGKMLRRALRDIL 511
Cdd:PRK05851 504 PRTSSGKLRRLAVKRSL 520
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
28-443 |
3.31e-22 |
|
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: 100.12 E-value: 3.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 28 TYQELNEHIQRFADGLQEAGMEK-GDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYTPTEIGYMLTNgdVKAIVGVS 106
Cdd:cd05905 16 TWGKLLSRAEKIAAVLQKKVGLKpGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLGFLLGT--CKVRVALT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 107 QllplyECMHESLPKVELVILCQTgeaepEAADPEVRMKMTTFAKILRPTSAAKQNQELVP----DDTAVILYTSGTTGK 182
Cdd:cd05905 94 V-----EACLKGLPKKLLKSKTAA-----EIAKKKGWPKILDFVKIPKSKRSKLKKWGPHPptrdGDTAYIEYSFSSDGS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 183 PKGAMLTHQNLYSNANDVAGYLGMDERDNVVCALP------MFHVFCLTVcmnaplMSGATVLIEPQF----SPASVFKL 252
Cdd:cd05905 164 LSGVAVSHSSLLAHCRALKEACELYESRPLVTVLDfksglgLWHGCLLSV------YSGHHTILIPPElmktNPLLWLQT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 253 VKQQQV-TIFAGVPTMYNYL----FQHENGKK--DDFSSIRLCISGGAAMP-VALLTAFEEKFGvTIlegyGLSE--ASP 322
Cdd:cd05905 238 LSQYKVrDAYVKLRTLHWCLkdlsSTLASLKNrdVNLSSLRMCMVPCENRPrISSCDSFLKLFQ-TL----GLSPraVST 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 323 V--TCFNPF-DRGRKPGSI--------------------------------GTSILHVENKVVDPLGREL-PAHQVGELI 366
Cdd:cd05905 313 EfgTRVNPFiCWQGTSGPEpsrvyldmralrhgvvrlderdkpnslplqdsGKVLPGAQVAIVNPETKGLcKDGEIGEIW 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 367 VKGPNVMKGYYKMPMETEH-------------ALKDGWLYTGDL----------ARRDEDGYFYIVDRKKDMIIVGGYNV 423
Cdd:cd05905 393 VNSPANASGYFLLDGETNDtfkvfpstrlstgITNNSYARTGLLgflrptkctdLNVEEHDLLFVVGSIDETLEVRGLRH 472
|
490 500
....*....|....*....|.
gi 1816047872 424 YPREVEE-VLYSHPDVKEAVV 443
Cdd:cd05905 473 HPSDIEAtVMRVHPYRGRCAV 493
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
27-453 |
3.26e-21 |
|
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: 97.14 E-value: 3.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 27 MTYQELNEHIQRFADGLQ-EAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYTPTEIGYMLTNGDVKAIVGV 105
Cdd:cd17632 68 ITYAELWERVGAVAAAHDpEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLAVS 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 106 SQLLPL-YECMHESLPKVELVILCQTGE-----------AEPEAADPEVRMKMTTFAKILRPTSAAKQNQELVPDDT-AV 172
Cdd:cd17632 148 AEHLDLaVEAVLEGGTPPRLVVFDHRPEvdahraalesaRERLAAVGIPVTTLTLIAVRGRDLPPAPLFRPEPDDDPlAL 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 173 ILYTSGTTGKPKGAMLTHQNLYSNANDVAGYLGMDERDNVVCA-LPMFHVFCLTVcMNAPLMSGATVLIEPQFSPASVFK 251
Cdd:cd17632 228 LIYTSGSTGTPKGAMYTERLVATFWLKVSSIQDIRPPASITLNfMPMSHIAGRIS-LYGTLARGGTAYFAAASDMSTLFD 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 252 LVKQQQVTIFAGVPTMYNYLFQHENGKKDDFSS------------------------IRLCISGGAAMPVALLTAFEEKF 307
Cdd:cd17632 307 DLALVRPTELFLVPRVCDMLFQRYQAELDRRSVagadaetlaervkaelrervlggrLLAAVCGSAPLSAEMKAFMESLL 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 308 GVTILEGYGLSEASPVTCFNpfdRGRKPGSIgtsilhvENKVVD--PLG---RELPaHQVGELIVKGPNVMKGYYKMPME 382
Cdd:cd17632 387 DLDLHDGYGSTEAGAVILDG---VIVRPPVL-------DYKLVDvpELGyfrTDRP-HPRGELLVKTDTLFPGYYKRPEV 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 383 TEHAL-KDGWLYTGD-LARRDEDGYFYiVDRKKDMI-IVGGYNVYPREVEEVLYSHPDVKE-------------AVVVGV 446
Cdd:cd17632 456 TAEVFdEDGFYRTGDvMAELGPDRLVY-VDRRNNVLkLSQGEFVTVARLEAVFAASPLVRQifvygnserayllAVVVPT 534
|
....*..
gi 1816047872 447 PDPQSGE 453
Cdd:cd17632 535 QDALAGE 541
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
166-438 |
1.17e-20 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 94.06 E-value: 1.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 166 VPDDTAVILY-TSGTTGKPKGAMLTHQNLYSNANDVAGYL---GMDERDNVVCALPMfHVFcltvcmNAPLM-------S 234
Cdd:COG1541 80 VPLEEIVRIHaSSGTTGKPTVVGYTRKDLDRWAELFARSLraaGVRPGDRVQNAFGY-GLF------TGGLGlhygaerL 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 235 GATVLiepqfsPASV------FKLVKQQQVTIFAGVPTMYNYL--FQHENGKKDDFSSIRLCISGGAAMPVALLTAFEEK 306
Cdd:COG1541 153 GATVI------PAGGgnterqLRLMQDFGPTVLVGTPSYLLYLaeVAEEEGIDPRDLSLKKGIFGGEPWSEEMRKEIEER 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 307 FGVTILEGYGLSEASPVTCFN-PFDRGrkpGSIGTSILHVEnkVVDPL-GRELPAHQVGELIV-----KGpnvmkgyykM 379
Cdd:COG1541 227 WGIKAYDIYGLTEVGPGVAYEcEAQDG---LHIWEDHFLVE--IIDPEtGEPVPEGEEGELVVttltkEA---------M 292
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 380 PMetehalkdgwL-Y-TGDLARRDED----GYFY-----IVDRKKDMIIVGGYNVYPREVEEVLYSHPDV 438
Cdd:COG1541 293 PL----------IrYrTGDLTRLLPEpcpcGRTHprigrILGRADDMLIIRGVNVFPSQIEEVLLRIPEV 352
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
7-513 |
1.66e-18 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 88.98 E-value: 1.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 7 LEETASEKPDSIACRFKD--------HMMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVV 78
Cdd:PLN03052 181 LTPKPSKTDDSIAIIWRDegsddlpvNRMTLSELRSQVSRVANALDALGFEKGDAIAIDMPMNVHAVIIYLAIILAGCVV 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 79 VPINPLYTPTEIGYMLTNGDVKA------IVGVSQLLPLYECMHESLPKVELVIlcqtgEAEPEAADPEVRMKMTTFAKI 152
Cdd:PLN03052 261 VSIADSFAPSEIATRLKISKAKAiftqdvIVRGGKSIPLYSRVVEAKAPKAIVL-----PADGKSVRVKLREGDMSWDDF 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 153 LRPTSAAKQNQELVP-----DDTAVILYTSGTTGKPKGAMLTHQNLYSNANDvaGYLGMDERDNVVCALP------MFHV 221
Cdd:PLN03052 336 LARANGLRRPDEYKAveqpvEAFTNILFSSGTTGEPKAIPWTQLTPLRAAAD--AWAHLDIRKGDIVCWPtnlgwmMGPW 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 222 FcltvcMNAPLMSGATVLIEpQFSP-ASVF-KLVKQQQVTIFAGVPTMYNYlFQHENGKKD-DFSSIRLCISGGAA---- 294
Cdd:PLN03052 414 L-----VYASLLNGATLALY-NGSPlGRGFaKFVQDAKVTMLGTVPSIVKT-WKNTNCMAGlDWSSIRCFGSTGEAssvd 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 295 -----MPVALLTAFEEKFGVTILeGYGLSEASPV--TCFNPFdrgrKPGSIGTSILhvenkVVDPLGRELPAHQ--VGEL 365
Cdd:PLN03052 487 dylwlMSRAGYKPIIEYCGGTEL-GGGFVTGSLLqpQAFAAF----STPAMGCKLF-----ILDDSGNPYPDDApcTGEL 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 366 IVkGPNVM------------KGYYK-MPMETEHALKDgwlyTGDLARRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVL 432
Cdd:PLN03052 557 AL-FPLMFgasstllnadhyKVYFKgMPVFNGKILRR----HGDIFERTSGGYYRAHGRADDTMNLGGIKVSSVEIERVC 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 433 YS-HPDVKEAVVVGVPDPQSG-EAVKGYVVPKRSGVTEEDIMQ-------HCETHLAKYKRPAAITFLDDIPKNATGKML 503
Cdd:PLN03052 632 NAaDESVLETAAIGVPPPGGGpEQLVIAAVLKDPPGSNPDLNElkkifnsAIQKKLNPLFKVSAVVIVPSFPRTASNKVM 711
|
570
....*....|
gi 1816047872 504 RRALRDILPQ 513
Cdd:PLN03052 712 RRVLRQQLAQ 721
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
28-511 |
2.51e-18 |
|
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.
Pssm-ID: 341265 [Multi-domain] Cd Length: 629 Bit Score: 88.10 E-value: 2.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 28 TYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAF----------------FGAlkAGIV--VVPINP--LYTP 87
Cdd:cd05943 100 TWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMlatasigaiwsscspdFGV--PGVLdrFGQIEPkvLFAV 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 88 TEIGYmltNG---DVKAivGVSQLLplyecmhESLPKVELVILCQTGEAEPEaADPEVRMKMTTFAKILRPTSAAKQNQE 164
Cdd:cd05943 178 DAYTY---NGkrhDVRE--KVAELV-------KGLPSLLAVVVVPYTVAAGQ-PDLSKIAKALTLEDFLATGAAGELEFE 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 165 LVP-DDTAVILYTSGTTGKPK-------GAMLTHQNLYSNANDvagyLGMDERdnvvcalpmfhVFCLTVCM----N--- 229
Cdd:cd05943 245 PLPfDHPLYILYSSGTTGLPKcivhgagGTLLQHLKEHILHCD----LRPGDR-----------LFYYTTCGwmmwNwlv 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 230 APLMSGATVLI---EPQF-SPASVFKLVKQQQVTIFAGVPTmynYLFQHENGKKD-----DFSSIRLCISGGAAMPVALL 300
Cdd:cd05943 310 SGLAVGATIVLydgSPFYpDTNALWDLADEEGITVFGTSAK---YLDALEKAGLKpaethDLSSLRTILSTGSPLKPESF 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 301 TAFEEKFGVTILEGYGLSEASPVTCF---NPFDRGRkPGSIGTSILHVENKVVDPLGRELPAhQVGELIVKGPnvmkgyy 377
Cdd:cd05943 387 DYVYDHIKPDVLLASISGGTDIISCFvggNPLLPVY-RGEIQCRGLGMAVEAFDEEGKPVWG-EKGELVCTKP------- 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 378 kMPMETEHALKDG----------------WlYTGDLARRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEA 441
Cdd:cd05943 458 -FPSMPVGFWNDPdgsryraayfakypgvW-AHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDS 535
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1816047872 442 VVVGVPDPQSGEAVKGYVVpKRSGVT-----EEDIMQHCETHLAKYKRPAAITFLDDIPKNATGKMLRRALRDIL 511
Cdd:cd05943 536 LVVGQEWKDGDERVILFVK-LREGVElddelRKRIRSTIRSALSPRHVPAKIIAVPDIPRTLSGKKVEVAVKKII 609
|
|
| PRK07868 |
PRK07868 |
acyl-CoA synthetase; Validated |
7-508 |
1.12e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236121 [Multi-domain] Cd Length: 994 Bit Score: 86.69 E-value: 1.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 7 LEETASEKPDSIACRFKDHMMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFfGAL-KAGIVVVPINPly 85
Cdd:PRK07868 453 IAEQARDAPKGEFLLFDGRVHTYEAVNRRINNVVRGLIAVGVRQGDRVGVLMETRPSALVAI-AALsRLGAVAVLMPP-- 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 86 tPTEIGYMLTNGDVKAIVGVSQLLPlyecMHESLPKVELVIlcqtGEAEPEAADPEVRMKMTTFAKI----------LRP 155
Cdd:PRK07868 530 -DTDLAAAVRLGGVTEIITDPTNLE----AARQLPGRVLVL----GGGESRDLDLPDDADVIDMEKIdpdavelpgwYRP 600
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 156 TSAakqnqelVPDDTAVILYtSGTTGKPKGAMLTHQNLYSNANDVAGYLGMDERDNVVCALPMFHVFCLTVCMNAPLMSG 235
Cdd:PRK07868 601 NPG-------LARDLAFIAF-STAGGELVAKQITNYRWALSAFGTASAAALDRRDTVYCLTPLHHESGLLVSLGGAVVGG 672
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 236 ATVLIEPQFSPASVFKLVKQQQVTIFAGVPTMYNYLFQHENGKKDDFSSIRLCIsgGAAMPVALLTAFEEKFG-VTILEG 314
Cdd:PRK07868 673 SRIALSRGLDPDRFVQEVRQYGVTVVSYTWAMLREVVDDPAFVLHGNHPVRLFI--GSGMPTGLWERVVEAFApAHVVEF 750
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 315 YGLSEASPVTCfNPfdRGRKPGSIGTSI---LHVENKVVDPLG-----------RELPAHQVGELIVK--GP-----NVM 373
Cdd:PRK07868 751 FATTDGQAVLA-NV--SGAKIGSKGRPLpgaGRVELAAYDPEHdlileddrgfvRRAEVNEVGVLLARarGPidptaSVK 827
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 374 KGYYkmpmetehALKDGWLYTGDLARRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGE 453
Cdd:PRK07868 828 RGVF--------APADTWISTEYLFRRDDDGDYWLVDRRGSVIRTARGPVYTEPVTDALGRIGGVDLAVTYGVEVGGRQL 899
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1816047872 454 AVKGYVVPKRSGVTEEDIMQHCEThLAKYKRPAAITFLDDIPKNATGKMLRRALR 508
Cdd:PRK07868 900 AVAAVTLRPGAAITAADLTEALAS-LPVGLGPDIVHVVPEIPLSATYRPTVSALR 953
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
160-511 |
1.38e-17 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 85.95 E-value: 1.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 160 KQNQ-----ELVPDDTA---VILYTSGTTGKPKGAmlthqnLYSNANDVAG----YLGMDERDNVVCALP-------MFH 220
Cdd:PTZ00237 238 KENNqspfyEYVPVESShplYILYTSGTTGNSKAV------VRSNGPHLVGlkyyWRSIIEKDIPTVVFShssigwvSFH 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 221 VFcltvcMNAPLMSGATV------LIEPQFSPASVFKLVKQQQVTIFAGVPTMYNYLFQHE-NGK----KDDFSSIRLCI 289
Cdd:PTZ00237 312 GF-----LYGSLSLGNTFvmfeggIIKNKHIEDDLWNTIEKHKVTHTLTLPKTIRYLIKTDpEATiirsKYDLSNLKEIW 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 290 SGGAAMPVALLTAFEEKFGVTILEGYGLSEaSPVTCFNPFDRGRKP-GSIGTSILHVENKVVDPLGRELPAHQVGELIVK 368
Cdd:PTZ00237 387 CGGEVIEESIPEYIENKLKIKSSRGYGQTE-IGITYLYCYGHINIPyNATGVPSIFIKPSILSEDGKELNVNEIGEVAFK 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 369 ---GPNVMKGYYKMPMETEHALKD--GWLYTGDLARRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVV 443
Cdd:PTZ00237 466 lpmPPSFATTFYKNDEKFKQLFSKfpGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCS 545
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1816047872 444 VGVPDPQSGEAVKGYVVPKRSGVTEEDIMQHCETHL--------AKYKRPAAITFLDDIPKNATGKMLRRALRDIL 511
Cdd:PTZ00237 546 IGIYDPDCYNVPIGLLVLKQDQSNQSIDLNKLKNEInniitqdiESLAVLRKIIIVNQLPKTKTGKIPRQIISKFL 621
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
27-511 |
2.48e-17 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 85.23 E-value: 2.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 27 MTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGA--LKA---------GIVVV-----PINP--LYTPT 88
Cdd:PRK03584 115 LSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLATasLGAiwsscspdfGVQGVldrfgQIEPkvLIAVD 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 89 EIGYmltNG-------DVKAIVgvsqllplyecmhESLPKVELVILC-QTGEAEPEAADPEVrmkmTTFAKILRPTSAAK 160
Cdd:PRK03584 195 GYRY---GGkafdrraKVAELR-------------AALPSLEHVVVVpYLGPAAAAAALPGA----LLWEDFLAPAEAAE 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 161 QNQELVP-DDTAVILYTSGTTGKPK-------GAMLTHqnLYSNA--NDvagyLGMDERdnvvcalpmfhVFCLTVC--- 227
Cdd:PRK03584 255 LEFEPVPfDHPLWILYSSGTTGLPKcivhghgGILLEH--LKELGlhCD----LGPGDR-----------FFWYTTCgwm 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 228 M-N---APLMSGATVLI---EPQF-SPASVFKLVKQQQVTIFAGVPTmynYL-----FQHENGKKDDFSSIRLCISGGAA 294
Cdd:PRK03584 318 MwNwlvSGLLVGATLVLydgSPFYpDPNVLWDLAAEEGVTVFGTSAK---YLdacekAGLVPGETHDLSALRTIGSTGSP 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 295 MPVAlltAFE---EKFGVTILegygLSEASP----VTCF---NPFDRGRkPGSIGTSILHVENKVVDPLGRELpAHQVGE 364
Cdd:PRK03584 395 LPPE---GFDwvyEHVKADVW----LASISGgtdiCSCFvggNPLLPVY-RGEIQCRGLGMAVEAWDEDGRPV-VGEVGE 465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 365 LIVKGPnvmkgyykMP-M-------ETEHALKDGWLYT-------GDLARRDEDGYFYIVDRKKDMIIVGG--------Y 421
Cdd:PRK03584 466 LVCTKP--------FPsMplgfwndPDGSRYRDAYFDTfpgvwrhGDWIEITEHGGVVIYGRSDATLNRGGvrigtaeiY 537
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 422 NVypreVEEVlyshPDVKEAVVVGVPDPQSGEAVKGYVVPkRSGVTEED-----IMQHCETHLAKYKRPAAITFLDDIPK 496
Cdd:PRK03584 538 RQ----VEAL----PEVLDSLVIGQEWPDGDVRMPLFVVL-AEGVTLDDalrarIRTTIRTNLSPRHVPDKIIAVPDIPR 608
|
570
....*....|....*
gi 1816047872 497 NATGKMLRRALRDIL 511
Cdd:PRK03584 609 TLSGKKVELPVKKLL 623
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
28-501 |
1.15e-16 |
|
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: 82.13 E-value: 1.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 28 TYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYTPTEIGYMLTNGDVKAIVgvsq 107
Cdd:cd17654 18 SYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKCHVSYLL---- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 108 llplYECMHESLPKVelvilcqtgeaepeAADPEVRMKMTTfakilrptsaakqnqelvPDDTAVILYTSGTTGKPKGAM 187
Cdd:cd17654 94 ----QNKELDNAPLS--------------FTPEHRHFNIRT------------------DECLAYVIHTSGTTGTPKIVA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 188 LTHQNLYSNANDVAGYLGMDERDNVVCALPM-FHVFCLTVCMNapLMSGATVLI-------EPQFSPASVFKLvkqQQVT 259
Cdd:cd17654 138 VPHKCILPNIQHFRSLFNITSEDILFLTSPLtFDPSVVEIFLS--LSSGATLLIvptsvkvLPSKLADILFKR---HRIT 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 260 IFAGVPTMYN----YLFQHENGKKDdfSSIRLCISGGAAMP--VALLTAFEEKFGVTILEGYGLSEASPVTCFNPFDRGR 333
Cdd:cd17654 213 VLQATPTLFRrfgsQSIKSTVLSAT--SSLRVLALGGEPFPslVILSSWRGKGNRTRIFNIYGITEVSCWALAYKVPEED 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 334 KPGSIGTSILHVENKVVDPLGRElpahQVGELIVKGPN---VMKGYYKMPMETEHAlkdgwlyTGDLARRdEDGYFYIVD 410
Cdd:cd17654 291 SPVQLGSPLLGTVIEVRDQNGSE----GTGQVFLGGLNrvcILDDEVTVPKGTMRA-------TGDFVTV-KDGELFFLG 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 411 RKKDMIIVGGYNVYPREVEEVLYSHPDVkEAVVVGVPDPQsgEAVKGYVVPKRSGVTEEDIMQHcetHLAKYKRPAAITF 490
Cdd:cd17654 359 RKDSQIKRRGKRINLDLIQQVIESCLGV-ESCAVTLSDQQ--RLIAFIVGESSSSRIHKELQLT---LLSSHAIPDTFVQ 432
|
490
....*....|.
gi 1816047872 491 LDDIPKNATGK 501
Cdd:cd17654 433 IDKLPLTSHGK 443
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
61-513 |
9.63e-15 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 76.39 E-value: 9.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 61 SPDFIIAFFGALKAGIVVVPINPLYTPTEIGYMLtngDVKAIVGV---------SQLLPLYECMHESLPKVELVIlcqtg 131
Cdd:PLN03051 4 TVDAVIIYLAIVLAGCVVVSVADSFSAKEIATRL---DISGAKGVftqdvvlrgGRALPLYSKVVEAAPAKAIVL----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 132 EAEPEAADPEVRMKMTTFAKILRptSAAKQNQ----ELVP-----DDTAVILYTSGTTGKPKGAMLTHQNLYSNANDvaG 202
Cdd:PLN03051 76 PAAGEPVAVPLREQDLSWCDFLG--VAAAQGSvggnEYSPvyapvESVTNILFSSGTTGEPKAIPWTHLSPLRCASD--G 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 203 YLGMDERDNvvcalpmfHVFCLTVcmNAPLMSGATVLIEPQFSPASV------------FKLVKQQQVTIFAGVPTMYNy 270
Cdd:PLN03051 152 WAHMDIQPG--------DVVCWPT--NLGWMMGPWLLYSAFLNGATLalyggaplgrgfGKFVQDAGVTVLGLVPSIVK- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 271 LFQHENG---KKDDFSSIR-LCISGGAAMP--VALLTAFEEKF--------GVTILEGYGLSEASPVTCFNPFdrgrKPG 336
Cdd:PLN03051 221 AWRHTGAfamEGLDWSKLRvFASTGEASAVddVLWLSSVRGYYkpvieycgGTELASGYISSTLLQPQAPGAF----STA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 337 SIGTS-ILHVENKVvdPLGRELPAhqVGELIVKGP-----------NVMKGYYK-MPM--ETEHALKDgwlyTGDLARRD 401
Cdd:PLN03051 297 SLGTRfVLLNDNGV--PYPDDQPC--VGEVALAPPmlgasdrllnaDHDKVYYKgMPMygSKGMPLRR----HGDIMKRT 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 402 EDGYFYIVDRKKDMIIVGGYNVYPREVEEVL-YSHPDVKEAVVVGVPDPQSGEAVkgYVVPKRSGVTEEDIMQHCETHLA 480
Cdd:PLN03051 369 PGGYFCVQGRADDTMNLGGIKTSSVEIERACdRAVAGIAETAAVGVAPPDGGPEL--LVIFLVLGEEKKGFDQARPEALQ 446
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1816047872 481 KYKRPAAITFLD------------DIPKNATGKMLRRALRDILPQ 513
Cdd:PLN03051 447 KKFQEAIQTNLNplfkvsrvkivpELPRNASNKLLRRVLRDQLKK 491
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
161-416 |
7.83e-14 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 74.37 E-value: 7.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 161 QNQElvPDDTAVILYTSGTTGKPKGAMLTHQNLY------SNANDVAGYlgmdERDNVVCALPMFHVFCLTVCMNApLMS 234
Cdd:PTZ00342 299 QNED--PDFITSIVYTSGTSGKPKGVMLSNKNLYntvvplCKHSIFKKY----NPKTHLSYLPISHIYERVIAYLS-FML 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 235 GATVLIEPQ----FSpasvfKLVKQQQVTIFAGVPTMYNYLF--------------------------QHENGKKDDF-- 282
Cdd:PTZ00342 372 GGTINIWSKdinyFS-----KDIYNSKGNILAGVPKVFNRIYtnimteinnlpplkrflvkkilslrkSNNNGGFSKFle 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 283 ------SSIRLCI--------SGGAAMPVALLTAFEEKFGVTILEGYGLSEAS-PVtcFNPFDRGRKPGSIGTSIL-HVE 346
Cdd:PTZ00342 447 githisSKIKDKVnpnlevilNGGGKLSPKIAEELSVLLNVNYYQGYGLTETTgPI--FVQHADDNNTESIGGPISpNTK 524
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1816047872 347 NKVV--------DPLGRelpahqvGELIVKGPNVMKGYYKMPMETEHAL-KDGWLYTGDLARRDEDGYFYIVDRKKDMI 416
Cdd:PTZ00342 525 YKVRtwetykatDTLPK-------GELLIKSDSIFSGYFLEKEQTKNAFtEDGYFKTGDIVQINKNGSLTFLDRSKGLV 596
|
|
| PaaK |
cd05913 |
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic ... |
176-439 |
2.08e-09 |
|
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic degradation pathway, by converting phenylacetic acid (PA) into phenylacetyl-CoA (PA-CoA). Phenylacetate-CoA ligase has been found in proteobacteria as well as gram positive prokaryotes. The enzyme is specifically induced after aerobic growth in a chemically defined medium containing PA or phenylalanine (Phe) as the sole carbon source. PaaKs are members of the adenylate-forming enzyme (AFE) family. However, sequence comparison reveals divergent features of PaaK with respect to the superfamily, including a novel N-terminal sequence.
Pssm-ID: 341239 [Multi-domain] Cd Length: 425 Bit Score: 59.56 E-value: 2.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 176 TSGTTGKPKGAMLTHQNLYSNANDVAGYLGMD--ERDNVVCALPMFHVF--------------CLTVCMNAplmsGATvl 239
Cdd:cd05913 86 SSGTTGKPTVVGYTKNDLDVWAELVARCLDAAgvTPGDRVQNAYGYGLFtgglgfhygaerlgALVIPAGG----GNT-- 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 240 iEPQFspasvfKLVKQQQVTIFAGVPTMYNYLFQ--HENGKKDDFSSIRLCISGGAAMPVALLTAFEEKFGVTILEGYGL 317
Cdd:cd05913 160 -ERQL------QLIKDFGPTVLCCTPSYALYLAEeaEEEGIDPRELSLKVGIFGAEPWTEEMRKRIERRLGIKAYDIYGL 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 318 SE----ASPVTCfnpfdrGRKPGsigtsiLHV-------EnkVVDPL-GRELPAHQVGELIVKgpNVMKGYykMPMeteh 385
Cdd:cd05913 233 TEiigpGVAFEC------EEKDG------LHIwedhfipE--IIDPEtGEPVPPGEVGELVFT--TLTKEA--MPL---- 290
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1816047872 386 aLKdgwlY-TGDLARRDED----GYFY-----IVDRKKDMIIVGGYNVYPREVEEVLYSHPDVK 439
Cdd:cd05913 291 -IR----YrTRDITRLLPGpcpcGRTHrridrITGRSDDMLIIRGVNVFPSQIEDVLLKIPGLG 349
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
28-507 |
1.17e-07 |
|
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Pssm-ID: 341302 [Multi-domain] Cd Length: 520 Bit Score: 54.06 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 28 TYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYTPTEIGYMLtngdvkaivGVSQ 107
Cdd:cd17647 22 TYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQNIYL---------GVAK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 108 llplyecmheslPKVELVIlcqtgeaepEAADPEVRmkmttfakilrptsaakqnqelvPDDTAVILYTSGTTGKPKGAM 187
Cdd:cd17647 93 ------------PRGLIVI---------RAAGVVVG-----------------------PDSNPTLSFTSGSEGIPKGVL 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 188 LTHQNLYSNANDVAGYLGMDERDNVVCALPMFHVfCLTVCMNAPLMSGATVLIEPQ---FSPASVFKLVKQQQVTIFAGV 264
Cdd:cd17647 129 GRHFSLAYYFPWMAKRFNLSENDKFTMLSGIAHD-PIQRDMFTPLFLGAQLLVPTQddiGTPGRLAEWMAKYGATVTHLT 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 265 PTMYNYLfqhengkkddfssirlciSGGAAMPV-ALLTAFeekF------------------GVTILEGYGLSEAS-PVT 324
Cdd:cd17647 208 PAMGQLL------------------TAQATTPFpKLHHAF---FvgdiltkrdclrlqtlaeNVRIVNMYGTTETQrAVS 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 325 CFNPFDRGRKPGSI---------GTSILHVENKVVDPLGRE--LPAHQVGELIVKGPNVMKGYYKMPMETEHALKDGW-- 391
Cdd:cd17647 267 YFEVPSRSSDPTFLknlkdvmpaGRGMLNVQLLVVNRNDRTqiCGIGEVGEIYVRAGGLAEGYRGLPELNKEKFVNNWfv 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 392 --------------------------LY-TGDLARRDEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVV 444
Cdd:cd17647 347 epdhwnyldkdnnepwrqfwlgprdrLYrTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITL 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 445 GVPDPQSGEAVKGYVVPKRSGVTEE----------------------------DIMQHCETHLAKYKRPAAITFLDDIPK 496
Cdd:cd17647 427 VRRDKDEEPTLVSYIVPRFDKPDDEsfaqedvpkevstdpivkgligyrklikDIREFLKKRLASYAIPSLIVVLDKLPL 506
|
570
....*....|.
gi 1816047872 497 NATGKMLRRAL 507
Cdd:cd17647 507 NPNGKVDKPKL 517
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
9-507 |
3.53e-07 |
|
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.
Pssm-ID: 274582 [Multi-domain] Cd Length: 1389 Bit Score: 53.14 E-value: 3.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 9 ETAS-EKPDSiacrfKDHMMTYQELNEHIQRFADGLQEAGMEKGDHLALLLGNSPDFIIAFFGALKAGIVVVPINPLYTP 87
Cdd:TIGR03443 257 ETPSfLDPSS-----KTRSFTYKQINEASNILAHYLLKTGIKRGDVVMIYAYRGVDLVVAVMGVLKAGATFSVIDPAYPP 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 88 TEIGYMLTNGDVKAIVGVS---QLLPLYE-CMHESLpkvELVILC-----------QTGEAEPEAADpevrmkmttfakI 152
Cdd:TIGR03443 332 ARQTIYLSVAKPRALIVIEkagTLDQLVRdYIDKEL---ELRTEIpalalqddgslVGGSLEGGETD------------V 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 153 LRPTSAAKQNQELV---PDDTAVILYTSGTTGKPKGAMLTHQNLYSNANDVAGYLGMDERDNVVCALPMFH------VFc 223
Cdd:TIGR03443 397 LAPYQALKDTPTGVvvgPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFGLSENDKFTMLSGIAHdpiqrdMF- 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 224 ltvcmnAPLMSGATVLIEPQ----------------------FSPAsVFKLVKQQQVTIFagvPTMYNYLFQhengkkDD 281
Cdd:TIGR03443 476 ------TPLFLGAQLLVPTAddigtpgrlaewmakygatvthLTPA-MGQLLSAQATTPI---PSLHHAFFV------GD 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 282 FSSIRLCISggaampvalLTAFEEKfgVTILEGYGLSEAS-PVTCFNPFDRGRKPGSI---------GTSILHVENKVVD 351
Cdd:TIGR03443 540 ILTKRDCLR---------LQTLAEN--VCIVNMYGTTETQrAVSYFEIPSRSSDSTFLknlkdvmpaGKGMKNVQLLVVN 608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 352 PLGRELPAH--QVGELIVKGPNVMKGYYKMP------------------METEHALKDGW----------LY-TGDLARR 400
Cdd:TIGR03443 609 RNDRTQTCGvgEVGEIYVRAGGLAEGYLGLPelnaekfvnnwfvdpshwIDLDKENNKPErefwlgprdrLYrTGDLGRY 688
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816047872 401 DEDGYFYIVDRKKDMIIVGGYNVYPREVEEVLYSHPDVKEAVVVGVPDPQSGEAVKGYVVPK---------RSGVTEE-- 469
Cdd:TIGR03443 689 LPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTLVRRDKDEEPTLVSYIVPQdksdeleefKSEVDDEes 768
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 1816047872 470 ----------------DIMQHCETHLAKYKRPAAITFLDDIPKNATGKMLRRAL 507
Cdd:TIGR03443 769 sdpvvkglikyrklikDIREYLKKKLPSYAIPTVIVPLKKLPLNPNGKVDKPAL 822
|
|
| |
