|
Name |
Accession |
Description |
Interval |
E-value |
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
57-615 |
0e+00 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 809.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 57 GLSYIQGHTDSHLVNTTVGECLDATAQRFPDREALVILHENIRLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYA 136
Cdd:PRK08315 1 GLSYVRGPTDVPLLEQTIGQLLDRTAARYPDREALVYRDQGLRWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 137 WVLIQLATAQAGIILVSVNPAYQSSELEYVLRKVGCKGIVFPKQFKTQQYYDILKQVCPELEKAQPGALKSERLPDLTTV 216
Cdd:PRK08315 81 WVLTQFATAKIGAILVTINPAYRLSELEYALNQSGCKALIAADGFKDSDYVAMLYELAPELATCEPGQLQSARLPELRRV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 217 ISVDA-PLPGTLLLDDIvAAGGKEQNLAQLRYNQRFLSCYDPINIQFTSGTTGNPKGATLSHHNIVNNSMLIGQRLKMpt 295
Cdd:PRK08315 161 IFLGDeKHPGMLNFDEL-LALGRAVDDAELAARQATLDPDDPINIQYTSGTTGFPKGATLTHRNILNNGYFIGEAMKL-- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 296 kTAEElRLVLPSPLYHCLGSVGGTMVSMMHGATLLLSSPSFNGKKALEAISREKGTLLYGTPTMFVDILNQPDFSSYDFT 375
Cdd:PRK08315 238 -TEED-RLCIPVPLYHCFGMVLGNLACVTHGATMVYPGEGFDPLATLAAVEEERCTALYGVPTMFIAELDHPDFARFDLS 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 376 SIRGGVIAGSPAPPELIRAIINKMNMKELVVVYGTTENSPVTFMNFPEDTLEQKAGSVGRIMPHTEAQIVNVETGELTNL 455
Cdd:PRK08315 316 SLRTGIMAGSPCPIEVMKRVIDKMHMSEVTIAYGMTETSPVSTQTRTDDPLEKRVTTVGRALPHLEVKIVDPETGETVPR 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 456 NVPGELYIRGYCVMQGYWGEPQKTFETVGQDKWYRTGDIALMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQV 535
Cdd:PRK08315 396 GEQGELCTRGYSVMKGYWNDPEKTAEAIDADGWMHTGDLAVMDEEGYVNIVGRIKDMIIRGGENIYPREIEEFLYTHPKI 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 536 QEAQVVGVKDERMGEEICACIRLKSGETTTAEEIKAFCKGKISHFKIPRYIVFVEGYPLTISGKIQKFKLREQMEQHLKL 615
Cdd:PRK08315 476 QDVQVVGVPDEKYGEEVCAWIILRPGATLTEEDVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGKIQKFKMREMMIEELGL 555
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
57-615 |
0e+00 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 666.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 57 GLSYIQGHTDSHLVNTTVGECLDATAQRFPDREALVILHENIRLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYA 136
Cdd:PRK12583 3 QPSYYQGGGDKPLLTQTIGDAFDATVARFPDREALVVRHQALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 137 WVLIQLATAQAGIILVSVNPAYQSSELEYVLRKVGCKGIVFPKQFKTQQYYDILKQVCPELEKAQPGALKSERLPDLTTV 216
Cdd:PRK12583 83 WLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWVICADAFKTSDYHAMLQELLPGLAEGQPGALACERLPELRGV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 217 ISVD-APLPGTLLLDDIVAAGgKEQNLAQLRYNQRFLSCYDPINIQFTSGTTGNPKGATLSHHNIVNNSMLIGQRLKMpt 295
Cdd:PRK12583 163 VSLApAPPPGFLAWHELQARG-ETVSREALAERQASLDRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGL-- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 296 ktAEELRLVLPSPLYHCLGSVGGTMVSMMHGATLLLSSPSFNGKKALEAISREKGTLLYGTPTMFVDILNQPDFSSYDFT 375
Cdd:PRK12583 240 --TEHDRLCVPVPLYHCFGMVLANLGCMTVGACLVYPNEAFDPLATLQAVEEERCTALYGVPTMFIAELDHPQRGNFDLS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 376 SIRGGVIAGSPAPPELIRAIINKMNMKELVVVYGTTENSPVTFMNFPEDTLEQKAGSVGRIMPHTEAQIVNVEtGELTNL 455
Cdd:PRK12583 318 SLRTGIMAGAPCPIEVMRRVMDEMHMAEVQIAYGMTETSPVSLQTTAADDLERRVETVGRTQPHLEVKVVDPD-GATVPR 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 456 NVPGELYIRGYCVMQGYWGEPQKTFETVGQDKWYRTGDIALMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQV 535
Cdd:PRK12583 397 GEIGELCTRGYSVMKGYWNNPEATAESIDEDGWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAV 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 536 QEAQVVGVKDERMGEEICACIRLKSGETTTAEEIKAFCKGKISHFKIPRYIVFVEGYPLTISGKIQKFKLREQMEQHLKL 615
Cdd:PRK12583 477 ADVQVFGVPDEKYGEEIVAWVRLHPGHAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMREISIEELAL 556
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
254-606 |
0e+00 |
|
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: 619.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 254 CYDPINIQFTSGTTGNPKGATLSHHNIVNNSMLIGQRLKMPtktaEELRLVLPSPLYHCLGSVGGTMVSMMHGATLLLSS 333
Cdd:cd05917 1 PDDVINIQFTSGTTGSPKGATLTHHNIVNNGYFIGERLGLT----EQDRLCIPVPLFHCFGSVLGVLACLTHGATMVFPS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 334 PSFNGKKALEAISREKGTLLYGTPTMFVDILNQPDFSSYDFTSIRGGVIAGSPAPPELIRAIINKMNMKELVVVYGTTEN 413
Cdd:cd05917 77 PSFDPLAVLEAIEKEKCTALHGVPTMFIAELEHPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEVMNMKDVTIAYGMTET 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 414 SPVTFMNFPEDTLEQKAGSVGRIMPHTEAQIVNVETGELTNLNVPGELYIRGYCVMQGYWGEPQKTFETVGQDKWYRTGD 493
Cdd:cd05917 157 SPVSTQTRTDDSIEKRVNTVGRIMPHTEAKIVDPEGGIVPPVGVPGELCIRGYSVMKGYWNDPEKTAEAIDGDGWLHTGD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 494 IALMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQEAQVVGVKDERMGEEICACIRLKSGETTTAEEIKAFC 573
Cdd:cd05917 237 LAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLKEGAELTEEDIKAYC 316
|
330 340 350
....*....|....*....|....*....|...
gi 24418933 574 KGKISHFKIPRYIVFVEGYPLTISGKIQKFKLR 606
Cdd:cd05917 317 KGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
74-612 |
1.07e-174 |
|
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440087 [Multi-domain] Cd Length: 452 Bit Score: 503.57 E-value: 1.07e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 74 VGECLDATAQRFPDREALVilHENIRLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVS 153
Cdd:COG0318 1 LADLLRRAAARHPDRPALV--FGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 154 VNPAYQSSELEYVLRKVGCKGIVFpkqfktqqyydilkqvcpelekaqpgalkserlpdlttvisvdaplpgtlllddiv 233
Cdd:COG0318 79 LNPRLTAEELAYILEDSGARALVT-------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 234 aaggkeqnlaqlrynqrflscydpINIQFTSGTTGNPKGATLSHHNIVNNSMLIGQRLKMptkTAEElRLVLPSPLYHCL 313
Cdd:COG0318 103 ------------------------ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGL---TPGD-VVLVALPLFHVF 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 314 GSVGGTMVSMMHGATLLLSsPSFNGKKALEAISREKGTLLYGTPTMFVDILNQPDFSSYDFTSIRGGVIAGSPAPPELIR 393
Cdd:COG0318 155 GLTVGLLAPLLAGATLVLL-PRFDPERVLELIERERVTVLFGVPTMLARLLRHPEFARYDLSSLRLVVSGGAPLPPELLE 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 394 AIINKMNMkELVVVYGTTENSPVTFMNfPEDTLEQKAGSVGRIMPHTEAQIVNVETGELTNlNVPGELYIRGYCVMQGYW 473
Cdd:COG0318 234 RFEERFGV-RIVEGYGLTETSPVVTVN-PEDPGERRPGSVGRPLPGVEVRIVDEDGRELPP-GEVGEIVVRGPNVMKGYW 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 474 GEPQKTFETVgQDKWYRTGDIALMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQEAQVVGVKDERMGEEIC 553
Cdd:COG0318 311 NDPEATAEAF-RDGWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVV 389
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 24418933 554 ACIRLKSGETTTAEEIKAFCKGKISHFKIPRYIVFVEGYPLTISGKIQKFKLREQMEQH 612
Cdd:COG0318 390 AFVVLRPGAELDAEELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRERYAAG 448
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
73-608 |
1.99e-142 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 423.16 E-value: 1.99e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 73 TVGECLDATAQRFPDREALVILHEniRLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILV 152
Cdd:PRK07656 6 TLPELLARAARRFGDKEAYVFGDQ--RLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 153 SVNPAYQSSELEYVLRKVGCKGIVFPKQFktqqyydilkqvCPELEKAqpgalkSERLPDLTTVISV-----DAPLPGTL 227
Cdd:PRK07656 84 PLNTRYTADEAAYILARGDAKALFVLGLF------------LGVDYSA------TTRLPALEHVVICeteedDPHTEKMK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 228 LLDDIVAAGGKEQNLAQLRYNqrflscyDPINIQFTSGTTGNPKGATLSHHNIVNNSMLIGQRLKMptktAEELRLVLPS 307
Cdd:PRK07656 146 TFTDFLAAGDPAERAPEVDPD-------DVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGL----TEGDRYLAAN 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 308 PLYHCLGSVGGTMVSMMHGATLLLSsPSFNGKKALEAISREKGTLLYGTPTMFVDILNQPDFSSYDFTSIRGGVIAGSPA 387
Cdd:PRK07656 215 PFFHVFGYKAGVNAPLMRGATILPL-PVFDPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSAEDLSSLRLAVTGAASM 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 388 PPELIRAIINKMNMKELVVVYGTTENSPVTFMNFPEDTLEQKAGSVGRIMPHTEAQIVNvETGELTNLNVPGELYIRGYC 467
Cdd:PRK07656 294 PVALLERFESELGVDIVLTGYGLSEASGVTTFNRLDDDRKTVAGTIGTAIAGVENKIVN-ELGEEVPVGEVGELLVRGPN 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 468 VMQGYWGEPQKTFETVGQDKWYRTGDIALMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQEAQVVGVKDER 547
Cdd:PRK07656 373 VMKGYYDDPEATAAAIDADGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDER 452
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24418933 548 MGEEICACIRLKSGETTTAEEIKAFCKGKISHFKIPRYIVFVEGYPLTISGKIQKFKLREQ 608
Cdd:PRK07656 453 LGEVGKAYVVLKPGAELTEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRALREK 513
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
73-608 |
1.93e-133 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 400.33 E-value: 1.93e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 73 TVGECLDATAQRFPDREALVIlhENIRLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILV 152
Cdd:PRK06187 7 TIGRILRHGARKHPDKEAVYF--DGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 153 SVNPAYQSSELEYVLRKVGCKGIVFPKQFKtqqyydilkqvcPELEKAQPgalkseRLPDLTTVISV-DAPLPGT----L 227
Cdd:PRK06187 85 PINIRLKPEEIAYILNDAEDRVVLVDSEFV------------PLLAAILP------QLPTVRTVIVEgDGPAAPLapevG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 228 LLDDIVAAGGKEQNLAQLRYNQRFLSCYdpiniqfTSGTTGNPKGATLSHHNIVNNSMLIGQRLKMptkTAEELRLVLpS 307
Cdd:PRK06187 147 EYEELLAAASDTFDFPDIDENDAAAMLY-------TSGTTGHPKGVVLSHRNLFLHSLAVCAWLKL---SRDDVYLVI-V 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 308 PLYHClGSVGGTMVSMMHGATLLLssP-SFNGKKALEAISREKGTLLYGTPTMFVDILNQPDFSSYDFTSIRGGVIAGSP 386
Cdd:PRK06187 216 PMFHV-HAWGLPYLALMAGAKQVI--PrRFDPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYFVDFSSLRLVIYGGAA 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 387 APPELIRAIINKMNMKeLVVVYGTTENSPVTFMNFPEDTLE---QKAGSVGRIMPHTEAQIVNVETGEL-TNLNVPGELY 462
Cdd:PRK06187 293 LPPALLREFKEKFGID-LVQGYGMTETSPVVSVLPPEDQLPgqwTKRRSAGRPLPGVEARIVDDDGDELpPDGGEVGEII 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 463 IRGYCVMQGYWGEPQKTFETVgQDKWYRTGDIALMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQEAQVVG 542
Cdd:PRK06187 372 VRGPWLMQGYWNRPEATAETI-DGGWLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIG 450
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24418933 543 VKDERMGEEICACIRLKSGETTTAEEIKAFCKGKISHFKIPRYIVFVEGYPLTISGKIQKFKLREQ 608
Cdd:PRK06187 451 VPDEKWGERPVAVVVLKPGATLDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVLREQ 516
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
78-606 |
2.70e-127 |
|
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: 382.68 E-value: 2.70e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 78 LDATAQRFPDREALVILHEniRLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVSVNPA 157
Cdd:cd05936 5 LEEAARRFPDKTALIFMGR--KLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 158 YQSSELEYVLRKVGCKGIVFPKQFKTqqyydilkqvcpelekaqpgALKSERLPDLTTVISvdaplpgtllLDDIVAagg 237
Cdd:cd05936 83 YTPRELEHILNDSGAKALIVAVSFTD--------------------LLAAGAPLGERVALT----------PEDVAV--- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 238 keqnlaqlrynqrflscydpinIQFTSGTTGNPKGATLSHHNIVNNSMLIGQRLKMPTKtaEELRLVLPSPLYHCLG-SV 316
Cdd:cd05936 130 ----------------------LQYTSGTTGVPKGAMLTHRNLVANALQIKAWLEDLLE--GDDVVLAALPLFHVFGlTV 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 317 GGtMVSMMHGATLLLSsPSFNGKKALEAISREKGTLLYGTPTMFVDILNQPDFSSYDFTSIRGGVIAGSPAPPELIRAII 396
Cdd:cd05936 186 AL-LLPLALGATIVLI-PRFRPIGVLKEIRKHRVTIFPGVPTMYIALLNAPEFKKRDFSSLRLCISGGAPLPVEVAERFE 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 397 NKMNMKeLVVVYGTTENSPVTFMNFPEDtlEQKAGSVGRIMPHTEAQIVNVETGELTNLNVpGELYIRGYCVMQGYWGEP 476
Cdd:cd05936 264 ELTGVP-IVEGYGLTETSPVVAVNPLDG--PRKPGSIGIPLPGTEVKIVDDDGEELPPGEV-GELWVRGPQVMKGYWNRP 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 477 QKTFETVgQDKWYRTGDIALMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQEAQVVGVKDERMGEEICACI 556
Cdd:cd05936 340 EETAEAF-VDGWLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFV 418
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 24418933 557 RLKSGETTTAEEIKAFCKGKISHFKIPRYIVFVEGYPLTISGKIQKFKLR 606
Cdd:cd05936 419 VLKEGASLTEEEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
78-602 |
1.18e-125 |
|
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: 377.34 E-value: 1.18e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 78 LDATAQRFPDREALVilHENIRLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVSVNPA 157
Cdd:cd17631 1 LRRRARRHPDRTALV--FGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 158 YQSSELEYVLrkvgckgivfpkqfktqqyydilkqvcpelekAQPGAlkserlpdlttvisvdaplpgTLLLDDIVAagg 237
Cdd:cd17631 79 LTPPEVAYIL--------------------------------ADSGA---------------------KVLFDDLAL--- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 238 keqnlaqlrynqrflscydpinIQFTSGTTGNPKGATLSHHNIVNNSMLIGQRLKMPTKTaeelRLVLPSPLYHCLGSVG 317
Cdd:cd17631 103 ----------------------LMYTSGTTGRPKGAMLTHRNLLWNAVNALAALDLGPDD----VLLVVAPLFHIGGLGV 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 318 GTMVSMMHGATLLLSsPSFNGKKALEAISREKGTLLYGTPTMFVDILNQPDFSSYDFTSIRGGVIAGSPAPPELIRAIIN 397
Cdd:cd17631 157 FTLPTLLRGGTVVIL-RKFDPETVLDLIERHRVTSFFLVPTMIQALLQHPRFATTDLSSLRAVIYGGAPMPERLLRALQA 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 398 KMnmKELVVVYGTTENSPVTFMNFPEDTLEqKAGSVGRIMPHTEAQIVN-----VETGEltnlnvPGELYIRGYCVMQGY 472
Cdd:cd17631 236 RG--VKFVQGYGMTETSPGVTFLSPEDHRR-KLGSAGRPVFFVEVRIVDpdgreVPPGE------VGEIVVRGPHVMAGY 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 473 WGEPQKTFETVgQDKWYRTGDIALMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQEAQVVGVKDERMGEEI 552
Cdd:cd17631 307 WNRPEATAAAF-RDGWFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAV 385
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 24418933 553 CACIRLKSGETTTAEEIKAFCKGKISHFKIPRYIVFVEGYPLTISGKIQK 602
Cdd:cd17631 386 VAVVVPRPGAELDEDELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
78-516 |
5.02e-125 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 375.11 E-value: 5.02e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 78 LDATAQRFPDREALVIlHENIRLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVSVNPA 157
Cdd:pfam00501 1 LERQAARTPDKTALEV-GEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 158 YQSSELEYVLRKVGCKGIVFPKQFKtqqyydiLKQVCPELEKaqpgalksERLPDLTTVISVDAPLPGTLLLDDIVAAGG 237
Cdd:pfam00501 80 LPAEELAYILEDSGAKVLITDDALK-------LEELLEALGK--------LEVVKLVLVLDRDPVLKEEPLPEEAKPADV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 238 KEQNLAQLRYNqrflscyDPINIQFTSGTTGNPKGATLSHHNIVNNSMLIGQRLKMPTKTAEELRLVLPSPLYHCLGSVG 317
Cdd:pfam00501 145 PPPPPPPPDPD-------DLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPRGFGLGPDDRVLSTLPLFHDFGLSL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 318 GTMVSMMHGATLLLSSPS--FNGKKALEAISREKGTLLYGTPTMFVDILNQPDFSSYDFTSIRGGVIAGSPAPPELIRAI 395
Cdd:pfam00501 218 GLLGPLLAGATVVLPPGFpaLDPAALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSSLRLVLSGGAPLPPELARRF 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 396 INKMNMkELVVVYGTTENSPVTFMNFPEDTLEQKAGSVGRIMPHTEAQIVNVETGELTNLNVPGELYIRGYCVMQGYWGE 475
Cdd:pfam00501 298 RELFGG-ALVNGYGLTETTGVVTTPLPLDEDLRSLGSVGRPLPGTEVKIVDDETGEPVPPGEPGELCVRGPGVMKGYLND 376
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 24418933 476 PQKTFETVGQDKWYRTGDIALMDEQGFCKIVGRSKDMIIRG 516
Cdd:pfam00501 377 PELTAEAFDEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
256-601 |
5.34e-122 |
|
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341228 [Multi-domain] Cd Length: 336 Bit Score: 364.30 E-value: 5.34e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 256 DPINIQFTSGTTGNPKGATLSHHNIVNNSMLIGQRLKMPtktaEELRLVLPSPLYHcLGSVGGTMVSMMHGATLLLSsPS 335
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLT----EGDVFLSTLPLFH-IGGLFGLLGALLAGGTVVLL-PK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 336 FNGKKALEAISREKGTLLYGTPTMFVDILNQPDFSSYDFTSIRGGVIAGSPAPPELIRAIINKMNMKeLVVVYGTTENSP 415
Cdd:cd04433 75 FDPEAALELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGAPLPPELLERFEEAPGIK-LVNGYGLTETGG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 416 VTFMNFPEDtLEQKAGSVGRIMPHTEAQIVNVETGELtNLNVPGELYIRGYCVMQGYWGEPQKTFEtVGQDKWYRTGDIA 495
Cdd:cd04433 154 TVATGPPDD-DARKPGSVGRPVPGVEVRIVDPDGGEL-PPGEIGELVVRGPSVMKGYWNNPEATAA-VDEDGWYRTGDLG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 496 LMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQEAQVVGVKDERMGEEICACIRLKSGETTTAEEIKAFCKG 575
Cdd:cd04433 231 RLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLDAEELRAHVRE 310
|
330 340
....*....|....*....|....*.
gi 24418933 576 KISHFKIPRYIVFVEGYPLTISGKIQ 601
Cdd:cd04433 311 RLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
100-601 |
2.38e-108 |
|
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: 334.57 E-value: 2.38e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 100 LNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVSVNPAYQSSELEYVLRKVGCKGIvfpk 179
Cdd:cd05911 11 LTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVI---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 180 qFKTQQYYDILKQVCpelekaqpgalksERLPDLTTVISVDAPLPGTLLLDDIVAAGGKEQnlAQLRYNQRFLSCYDPIN 259
Cdd:cd05911 87 -FTDPDGLEKVKEAA-------------KELGPKDKIIVLDDKPDGVLSIEDLLSPTLGEE--DEDLPPPLKDGKDDTAA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 260 IQFTSGTTGNPKGATLSHHNIVNNSMLIGQRLKMPTKTAEelRLVLPSPLYHCLGsVGGTMVSMMHGATLLLSsPSFNGK 339
Cdd:cd05911 151 ILYSSGTTGLPKGVCLSHRNLIANLSQVQTFLYGNDGSND--VILGFLPLYHIYG-LFTTLASLLNGATVIIM-PKFDSE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 340 KALEAISREKGTLLYGTPTMFVDILNQPDFSSYDFTSIRGGVIAGSPAPPELIRAIINKMNMKELVVVYGTTENSPVTFM 419
Cdd:cd05911 227 LFLDLIEKYKITFLYLVPPIAAALAKSPLLDKYDLSSLRVILSGGAPLSKELQELLAKRFPNATIKQGYGMTETGGILTV 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 420 NFPEDtleQKAGSVGRIMPHTEAQIVNVETGELTNLNVPGELYIRGYCVMQGYWGEPQKTFETVGQDKWYRTGDIALMDE 499
Cdd:cd05911 307 NPDGD---DKPGSVGRLLPNVEAKIVDDDGKDSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGWLHTGDIGYFDE 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 500 QGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQEAQVVGVKDERMGEEICACIRLKSGETTTAEEIKAFCKGKISH 579
Cdd:cd05911 384 DGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGEKLTEKEVKDYVAKKVAS 463
|
490 500
....*....|....*....|...
gi 24418933 580 FKIPRY-IVFVEGYPLTISGKIQ 601
Cdd:cd05911 464 YKQLRGgVVFVDEIPKSASGKIL 486
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
73-611 |
2.10e-103 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 323.04 E-value: 2.10e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 73 TVGECLDATAQRFPDREALVilHENIRLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILV 152
Cdd:PRK08316 12 TIGDILRRSARRYPDKTALV--FGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 153 SVNPAYQSSELEYVLRKVGCKGIVfpkqfktqqyydilkqVCPEL-EKAQPGALKSERLPDLTTVISVDAPLPGTLL-LD 230
Cdd:PRK08316 90 PVNFMLTGEELAYILDHSGARAFL----------------VDPALaPTAEAALALLPVDTLILSLVLGGREAPGGWLdFA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 231 DIVAAGGKEQNLAQLRYNqrflscyDPINIQFTSGTTGNPKGATLSHHNIVNN--SMLIGQRLKmptktaEELRLVLPSP 308
Cdd:PRK08316 154 DWAEAGSVAEPDVELADD-------DLAQILYTSGTESLPKGAMLTHRALIAEyvSCIVAGDMS------ADDIPLHALP 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 309 LYHCLGSVGGTMVSMMHGAT-LLLSSPsfNGKKALEAISREKGTLLYGTPTMFVDILNQPDFSSYDFTSIRGGVIAGSPA 387
Cdd:PRK08316 221 LYHCAQLDVFLGPYLYVGATnVILDAP--DPELILRTIEAERITSFFAPPTVWISLLRHPDFDTRDLSSLRKGYYGASIM 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 388 PPELIRAIINKMNMKELVVVYGTTENSPVTFMNFPEDTLEqKAGSVGRIMPHTEAQIVNvETGELTNLNVPGELYIRGYC 467
Cdd:PRK08316 299 PVEVLKELRERLPGLRFYNCYGQTEIAPLATVLGPEEHLR-RPGSAGRPVLNVETRVVD-DDGNDVAPGEVGEIVHRSPQ 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 468 VMQGYWGEPQKTFETVgQDKWYRTGDIALMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQEAQVVGVKDER 547
Cdd:PRK08316 377 LMLGYWDDPEKTAEAF-RGGWFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPK 455
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24418933 548 MGEEICACIRLKSGETTTAEEIKAFCKGKISHFKIPRYIVFVEGYPLTISGKIQKFKLREQMEQ 611
Cdd:PRK08316 456 WIEAVTAVVVPKAGATVTEDELIAHCRARLAGFKVPKRVIFVDELPRNPSGKILKRELRERYAG 519
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
76-611 |
3.33e-102 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 321.29 E-value: 3.33e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 76 ECLDATAQRFPDREALVILHEN---IRLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILV 152
Cdd:COG0365 13 NCLDRHAEGRGDKVALIWEGEDgeeRTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 153 SVNPAYQSSELEYVLRKVGCKGIVFpkqfkTQQYYDILKQVC--PELEKAQpgalksERLPDLTTVISV-----DAPLPG 225
Cdd:COG0365 93 PVFPGFGAEALADRIEDAEAKVLIT-----ADGGLRGGKVIDlkEKVDEAL------EELPSLEHVIVVgrtgaDVPMEG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 226 TLLLDDIVAAGGKEQNLAQLRYNqrflscyDPINIQFTSGTTGNPKGATLSHHNIVnnsmligqrLKMPTktaeELRLVL 305
Cdd:COG0365 162 DLDWDELLAAASAEFEPEPTDAD-------DPLFILYTSGTTGKPKGVVHTHGGYL---------VHAAT----TAKYVL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 306 ---PSPLYHCLGSVGGTMV-------SMMHGATLLL--SSPSF-NGKKALEAISREKGTLLYGTPTMFVDILNQPDF--S 370
Cdd:COG0365 222 dlkPGDVFWCTADIGWATGhsyivygPLLNGATVVLyeGRPDFpDPGRLWELIEKYGVTVFFTAPTAIRALMKAGDEplK 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 371 SYDFTSIRGGVIAGSPAPPELIRAIINKMNmKELVVVYGTTENSpVTFMNFPeDTLEQKAGSVGRIMPHTEAQIVNvETG 450
Cdd:COG0365 302 KYDLSSLRLLGSAGEPLNPEVWEWWYEAVG-VPIVDGWGQTETG-GIFISNL-PGLPVKPGSMGKPVPGYDVAVVD-EDG 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 451 ELTNLNVPGELYIRGYC--VMQGYWGEPQKTFETV--GQDKWYRTGDIALMDEQGFCKIVGRSKDMIIRGGENIYPAELE 526
Cdd:COG0365 378 NPVPPGEEGELVIKGPWpgMFRGYWNDPERYRETYfgRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIE 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 527 DFFLKHPQVQEAQVVGVKDERMGEEICACIRLKSGETTTAE---EIKAFCKGKISHFKIPRYIVFVEGYPLTISGKIQKF 603
Cdd:COG0365 458 SALVSHPAVAEAAVVGVPDEIRGQVVKAFVVLKPGVEPSDElakELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRR 537
|
....*...
gi 24418933 604 KLREQMEQ 611
Cdd:COG0365 538 LLRKIAEG 545
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
99-607 |
8.29e-93 |
|
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: 8.29e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 99 RLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVSVNPAYQSSELEYVLRKVGCKGIVFP 178
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 179 KQFKTQQYydilkqvcpelekaqpgalkserlpdlttvisvdAPLPGtlllddivaaggkeqnlaqlrynqrflscyDPI 258
Cdd:cd05903 81 ERFRQFDP----------------------------------AAMPD------------------------------AVA 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 259 NIQFTSGTTGNPKGATLSHHNIVNNSMLIGQRLKMPtktaEELRLVLPSPLYHCLGSVGGTMVSMMHGATLLLSSpSFNG 338
Cdd:cd05903 97 LLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLG----PGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQD-IWDP 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 339 KKALEAISREKGTLLYGTPTMFVDILNQPDFSSYDFTSIRGGVIAGSPAPPELIRAIINKMNMKeLVVVYGTTENSpvTF 418
Cdd:cd05903 172 DKALALMREHGVTFMMGATPFLTDLLNAVEEAGEPLSRLRTFVCGGATVPRSLARRAAELLGAK-VCSAYGSTECP--GA 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 419 MNFPEDTLEQKA-GSVGRIMPHTEAQIVNvETGELTNLNVPGELYIRGYCVMQGYWGEPQKTFETVgQDKWYRTGDIALM 497
Cdd:cd05903 249 VTSITPAPEDRRlYTDGRPLPGVEIKVVD-DTGATLAPGVEGELLSRGPSVFLGYLDRPDLTADAA-PEGWFRTGDLARL 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 498 DEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQEAQVVGVKDERMGEEICACIRLKSGETTTAEEIKAFCKGK- 576
Cdd:cd05903 327 DEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGALLTFDELVAYLDRQg 406
|
490 500 510
....*....|....*....|....*....|.
gi 24418933 577 ISHFKIPRYIVFVEGYPLTISGKIQKFKLRE 607
Cdd:cd05903 407 VAKQYWPERLVHVDDLPRTPSGKVQKFRLRE 437
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
82-608 |
9.79e-93 |
|
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: 294.91 E-value: 9.79e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 82 AQRFPDREALVILHENIRLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVSVNPAYQSS 161
Cdd:cd05904 15 ASAHPSRPALIDAATGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 162 ELEYVLRKVGCKGIVfpkqfktqqyydilkQVCPELEKAQPGALKserlpdltTVISVDAPLPGTLLLDDIVAAGgkEQN 241
Cdd:cd05904 95 EIAKQVKDSGAKLAF---------------TTAELAEKLASLALP--------VVLLDSAEFDSLSFSDLLFEAD--EAE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 242 LAQLRYNQRflscyDPINIQFTSGTTGNPKGATLSHHNIVnnSMLIGQRLKMPTKTAEELRLVLPSPLYHCLGSVGGTMV 321
Cdd:cd05904 150 PPVVVIKQD-----DVAALLYSSGTTGRSKGVMLTHRNLI--AMVAQFVAGEGSNSDSEDVFLCVLPMFHIYGLSSFALG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 322 SMMHGATLLLSsPSFNGKKALEAISREKGTLLYGTPTMFVDILNQPDFSSYDFTSIRGGVIAGSPAPPELIRAIINKMNM 401
Cdd:cd05904 223 LLRLGATVVVM-PRFDLEELLAAIERYKVTHLPVVPPIVLALVKSPIVDKYDLSSLRQIMSGAAPLGKELIEAFRAKFPN 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 402 KELVVVYGTTENSPVTFMNFPEDTLEQKAGSVGRIMPHTEAQIVNVETGELTNLNVPGELYIRGYCVMQGYWGEPQKTFE 481
Cdd:cd05904 302 VDLGQGYGMTESTGVVAMCFAPEKDRAKYGSVGRLVPNVEAKIVDPETGESLPPNQTGELWIRGPSIMKGYLNNPEATAA 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 482 TVGQDKWYRTGDIALMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQEAQVVGVKDERMGEEICACIRLKSG 561
Cdd:cd05904 382 TIDKEGWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKPG 461
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 24418933 562 ETTTAEEIKAFCKGKISHFKIPRYIVFVEGYPLTISGKIqkfkLREQ 608
Cdd:cd05904 462 SSLTEDEIMDFVAKQVAPYKKVRKVAFVDAIPKSPSGKI----LRKE 504
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
71-611 |
1.44e-92 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 295.81 E-value: 1.44e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 71 NTTVGECLDATAQRFPDREALVILH----ENIRLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQ 146
Cdd:PRK13295 23 DRTINDDLDACVASCPDKTAVTAVRlgtgAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 147 AGIILVSVNPAYQSSELEYVLRKVGCKGIVFPKQFKTQQYYDILKQVCPELekaqpgalkserlPDLTTVISVDAPLPG- 225
Cdd:PRK13295 103 IGAVLNPLMPIFRERELSFMLKHAESKVLVVPKTFRGFDHAAMARRLRPEL-------------PALRHVVVVGGDGADs 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 226 --TLLLDdivAAGGKEQNLAQLRYNQRfLSCYDPINIQFTSGTTGNPKGATLSHHNIVNNSMLIGQRLKMptkTAEELRL 303
Cdd:PRK13295 170 feALLIT---PAWEQEPDAPAILARLR-PGPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGL---GADDVIL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 304 vLPSPLYHCLGSVGGTMVSMMHGATLLLSSpSFNGKKALEAISREKGTLLYGTPTMFVDILNQPDFSSYDFTSIRGGVIA 383
Cdd:PRK13295 243 -MASPMAHQTGFMYGLMMPVMLGATAVLQD-IWDPARAAELIRTEGVTFTMASTPFLTDLTRAVKESGRPVSSLRTFLCA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 384 GSPAPPELIRAIINKMNMKeLVVVYGTTENSPVTFMNfPEDTLEQKAGSVGRIMPHTEAQIVNVETGELTnLNVPGELYI 463
Cdd:PRK13295 321 GAPIPGALVERARAALGAK-IVSAWGMTENGAVTLTK-LDDPDERASTTDGCPLPGVEVRVVDADGAPLP-AGQIGRLQV 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 464 RGYCVMQGYWGEPQKTfeTVGQDKWYRTGDIALMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQEAQVVGV 543
Cdd:PRK13295 398 RGCSNFGGYLKRPQLN--GTDADGWFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAY 475
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24418933 544 KDERMGEEICACIRLKSGETTTAEEIKAFCKG-KISHFKIPRYIVFVEGYPLTISGKIQKFKLREQMEQ 611
Cdd:PRK13295 476 PDERLGERACAFVVPRPGQSLDFEEMVEFLKAqKVAKQYIPERLVVRDALPRTPSGKIQKFRLREMLRG 544
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
78-611 |
9.72e-90 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 288.86 E-value: 9.72e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 78 LDATAQRFPDREALVILHENIrlNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVSVNPA 157
Cdd:PRK06710 30 VEQMASRYPEKKALHFLGKDI--TFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 158 YQSSELEYVLRKVG-----CKGIVFPKQFKTQQyydilkqvcpelekaqpgALKSERLpdLTTVISVDAPLPGTLLL--- 229
Cdd:PRK06710 108 YTERELEYQLHDSGakvilCLDLVFPRVTNVQS------------------ATKIEHV--IVTRIADFLPFPKNLLYpfv 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 230 -----DDIVAAGGKEQ----NLAQLRYNQRFLSCYDPIN----IQFTSGTTGNPKGATLSHHNIVNNSmLIGQRLKMPTK 296
Cdd:PRK06710 168 qkkqsNLVVKVSESETihlwNSVEKEVNTGVEVPCDPENdlalLQYTGGTTGFPKGVMLTHKNLVSNT-LMGVQWLYNCK 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 297 TAEELRL-VLPspLYHCLGSVGGTMVSMMHGATLLLSsPSFNGKKALEAISREKGTLLYGTPTMFVDILNQPDFSSYDFT 375
Cdd:PRK06710 247 EGEEVVLgVLP--FFHVYGMTAVMNLSIMQGYKMVLI-PKFDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLLKEYDIS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 376 SIRGGVIAGSPAPPElIRAIINKMNMKELVVVYGTTENSPVTFMNFPEDtlEQKAGSVGRIMPHTEAQIVNVETGELTNL 455
Cdd:PRK06710 324 SIRACISGSAPLPVE-VQEKFETVTGGKLVEGYGLTESSPVTHSNFLWE--KRVPGSIGVPWPDTEAMIMSLETGEALPP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 456 NVPGELYIRGYCVMQGYWGEPQKTfETVGQDKWYRTGDIALMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQV 535
Cdd:PRK06710 401 GEIGEIVVKGPQIMKGYWNKPEET-AAVLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKV 479
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24418933 536 QEAQVVGVKDERMGEEICACIRLKSGETTTAEEIKAFCKGKISHFKIPRYIVFVEGYPLTISGKIQKFKLREQMEQ 611
Cdd:PRK06710 480 QEVVTIGVPDPYRGETVKAFVVLKEGTECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVLIEEEKR 555
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
71-614 |
1.09e-89 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 288.18 E-value: 1.09e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 71 NTTVGECLDATAQRFPDREAlVILHENIRLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGII 150
Cdd:PRK06087 22 DASLADYWQQTARAMPDKIA-VVDNHGASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 151 LVSVNPAYQSSELEYVLRKVGCKGIVFPKQFKTQQYYDILKQVcpelekaqpgalkSERLPDLTTVISVDAPLPGTllld 230
Cdd:PRK06087 101 SVPLLPSWREAELVWVLNKCQAKMFFAPTLFKQTRPVDLILPL-------------QNQLPQLQQIVGVDKLAPAT---- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 231 divaaggKEQNLAQLrynqrfLSCYDPIN------------IQFTSGTTGNPKGATLSHHNIVNNSMLIGQRLKMptkTA 298
Cdd:PRK06087 164 -------SSLSLSQI------IADYEPLTtaitthgdelaaVLFTSGTEGLPKGVMLTHNNILASERAYCARLNL---TW 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 299 EELrLVLPSPLYHCLGSVGGTMVSMMHGATLLLSSpSFNGKKALEAISREKGTLLYG-TPTMFvDILNQPDFSSYDFTSI 377
Cdd:PRK06087 228 QDV-FMMPAPLGHATGFLHGVTAPFLIGARSVLLD-IFTPDACLALLEQQRCTCMLGaTPFIY-DLLNLLEKQPADLSAL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 378 RGGVIAGSPAPPELIRAIINKmNMKeLVVVYGTTENSPVTFMNfPEDTLEQKAGSVGRIMPHTEAQIVNVETGELTnLNV 457
Cdd:PRK06087 305 RFFLCGGTTIPKKVARECQQR-GIK-LLSVYGSTESSPHAVVN-LDDPLSRFMHTDGYAAAGVEIKVVDEARKTLP-PGC 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 458 PGELYIRGYCVMQGYWGEPQKTFETVGQDKWYRTGDIALMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQE 537
Cdd:PRK06087 381 EGEEASRGPNVFMGYLDEPELTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHD 460
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24418933 538 AQVVGVKDERMGEEICACIRLKSGETT-TAEEIKAF-CKGKISHFKIPRYIVFVEGYPLTISGKIQKFKLREQMEQHLK 614
Cdd:PRK06087 461 ACVVAMPDERLGERSCAYVVLKAPHHSlTLEEVVAFfSRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRKDIMRRLT 539
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
78-608 |
5.98e-88 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 282.13 E-value: 5.98e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 78 LDATAQRFPDREALVILHENirLNFAQLKEEVDKAASGLL-SIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVSVNP 156
Cdd:PRK06839 8 IEKRAYLHPDRIAIITEEEE--MTYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 157 AYQSSELEYVLRKVGCKGIVFPKQFktqqyydilkQVCPELEKAQPGALKSERLPDLTTVISVDaplpgtllLDDIVAAG 236
Cdd:PRK06839 86 RLTENELIFQLKDSGTTVLFVEKTF----------QNMALSMQKVSYVQRVISITSLKEIEDRK--------IDNFVEKN 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 237 GKeqnlaqlrynqrflscyDPINIQFTSGTTGNPKGATLSHHNIVNNSMligQRLKMPTKTAEELRLVLpSPLYHcLGSV 316
Cdd:PRK06839 148 ES-----------------ASFIICYTSGTTGKPKGAVLTQENMFWNAL---NNTFAIDLTMHDRSIVL-LPLFH-IGGI 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 317 GGTMVSMMHGATLLLSSPSFNGKKALEAISREKGTLLYGTPTMFVDILNQPDFSSYDFTSIRGGVIAGSPAPPELIRAII 396
Cdd:PRK06839 206 GLFAFPTLFAGGVIIVPRKFEPTKALSMIEKHKVTVVMGVPTIHQALINCSKFETTNLQSVRWFYNGGAPCPEELMREFI 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 397 NKMNMkeLVVVYGTTENSPVTFMnFPEDTLEQKAGSVGRIMPHTEAQIVNVETGELTNLNVpGELYIRGYCVMQGYWGEP 476
Cdd:PRK06839 286 DRGFL--FGQGFGMTETSPTVFM-LSEEDARRKVGSIGKPVLFCDYELIDENKNKVEVGEV-GELLIRGPNVMKEYWNRP 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 477 QKTFETVgQDKWYRTGDIALMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQEAQVVGVKDERMGEEICACI 556
Cdd:PRK06839 362 DATEETI-QDGWLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFI 440
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 24418933 557 RLKSGETTTAEEIKAFCKGKISHFKIPRYIVFVEGYPLTISGKIQKFKLREQ 608
Cdd:PRK06839 441 VKKSSSVLIEKDVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQLVNQ 492
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
102-606 |
2.07e-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. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 275.71 E-value: 2.07e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 102 FAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVSVNPAYQSSELEYVLRKVGCKGIVFpkqf 181
Cdd:cd05934 6 YAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 182 ktqqyydilkqvcpelekaqpgalkserlpdlttvisvdaplpgtlllddivaaggkeqnlaqlrynqrflscyDPINIQ 261
Cdd:cd05934 82 --------------------------------------------------------------------------DPASIL 87
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 262 FTSGTTGNPKGATLSHHNIVNNSMLIGQRLKMPtktaEELRLVLPSPLYHCLGSVGGTMVSMMHGATLLLSsPSFNGKKA 341
Cdd:cd05934 88 YTSGTTGPPKGVVITHANLTFAGYYSARRFGLG----EDDVYLTVLPLFHINAQAVSVLAALSVGATLVLL-PRFSASRF 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 342 LEAISREKGTLLYGTPTMFVDILNQPDfsSYDFTSIRGGVIAGSPAPPELIRAIINKMNMKeLVVVYGTTENSPVTFMNF 421
Cdd:cd05934 163 WSDVRRYGATVTNYLGAMLSYLLAQPP--SPDDRAHRLRAAYGAPNPPELHEEFEERFGVR-LLEGYGMTETIVGVIGPR 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 422 PEDTleqKAGSVGRIMPHTEAQIVNVETGELTNlNVPGELYIR---GYCVMQGYWGEPQKTFETVgQDKWYRTGDIALMD 498
Cdd:cd05934 240 DEPR---RPGSIGRPAPGYEVRIVDDDGQELPA-GEPGELVIRglrGWGFFKGYYNMPEATAEAM-RNGWFHTGDLGYRD 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 499 EQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQEAQVVGVKDERMGEEICACIRLKSGETTTAEEIKAFCKGKIS 578
Cdd:cd05934 315 ADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLDPEELFAFCEGQLA 394
|
490 500
....*....|....*....|....*...
gi 24418933 579 HFKIPRYIVFVEGYPLTISGKIQKFKLR 606
Cdd:cd05934 395 YFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
256-602 |
1.23e-85 |
|
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: 270.53 E-value: 1.23e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 256 DPINIQFTSGTTGNPKGATLSHHNivnnSMLIGQRLKMPTKTAEELRLVLPSPLYHCLGSVGGTMVSMMHGATLLlSSPS 335
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQ----TLRAAAAWADCADLTEDDRYLIINPFFHTFGYKAGIVACLLTGATVV-PVAV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 336 FNGKKALEAISREKGTLLYGTPTMFVDILNQPDFSSYDFTSIRGGVIAGSPAPPELIRAIINKMNMKELVVVYGTTENSP 415
Cdd:cd17638 76 FDVDAILEAIERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFETVLTAYGLTEAGV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 416 VTfMNFPEDTLEQKAGSVGRIMPHTEAQIVNvetgeltnlnvPGELYIRGYCVMQGYWGEPQKTFETVGQDKWYRTGDIA 495
Cdd:cd17638 156 AT-MCRPGDDAETVATTCGRACPGFEVRIAD-----------DGEVLVRGYNVMQGYLDDPEATAEAIDADGWLHTGDVG 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 496 LMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQEAQVVGVKDERMGEEICACIRLKSGETTTAEEIKAFCKG 575
Cdd:cd17638 224 ELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGVTLTEEDVIAWCRE 303
|
330 340
....*....|....*....|....*..
gi 24418933 576 KISHFKIPRYIVFVEGYPLTISGKIQK 602
Cdd:cd17638 304 RLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
69-614 |
2.22e-85 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 277.65 E-value: 2.22e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 69 LVNTTVGECLDATAQRFPDREALVILHEniRLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAG 148
Cdd:PRK05605 29 YGDTTLVDLYDNAVARFGDRPALDFFGA--TTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 149 IILVSVNPAYQSSELEYVLRKVGCKGIVFpkqfktqqyYDilkqvcpeleKAQPGAlksERLPD---LTTVISVD----- 220
Cdd:PRK05605 107 AVVVEHNPLYTAHELEHPFEDHGARVAIV---------WD----------KVAPTV---ERLRRttpLETIVSVNmiaam 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 221 -----------------------APLPGTLLLDDIVAAGGkeqNLAQLRYNQRFLSCYDPINIQFTSGTTGNPKGATLSH 277
Cdd:PRK05605 165 pllqrlalrlpipalrkaraaltGPAPGTVPWETLVDAAI---GGDGSDVSHPRPTPDDVALILYTSGTTGKPKGAQLTH 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 278 HNIVNNsMLIGqRLKMPT--KTAEELRLVLPspLYHCLGSVGGTMVSMMHGATLLLSsPSFNGKKALEAISREKGTLLYG 355
Cdd:PRK05605 242 RNLFAN-AAQG-KAWVPGlgDGPERVLAALP--MFHAYGLTLCLTLAVSIGGELVLL-PAPDIDLILDAMKKHPPTWLPG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 356 TPTMFVDILNQPDFSSYDFTSIRGGVIAGSPAPPELIRAIINKMNMKeLVVVYGTTENSPVTFMNFPEDTleQKAGSVGR 435
Cdd:PRK05605 317 VPPLYEKIAEAAEERGVDLSGVRNAFSGAMALPVSTVELWEKLTGGL-LVEGYGLTETSPIIVGNPMSDD--RRPGYVGV 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 436 IMPHTEAQIVNVET-------GEltnlnvPGELYIRGYCVMQGYWGEPQKTFETVgQDKWYRTGDIALMDEQGFCKIVGR 508
Cdd:PRK05605 394 PFPDTEVRIVDPEDpdetmpdGE------EGELLVRGPQVFKGYWNRPEETAKSF-LDGWFRTGDVVVMEEDGFIRIVDR 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 509 SKDMIIRGGENIYPAELEDFFLKHPQVQEAQVVGVKDERMGEEICACIRLKSGETTTAEEIKAFCKGKISHFKIPRYIVF 588
Cdd:PRK05605 467 IKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEPGAALDPEGLRAYCREHLTRYKVPRRFYH 546
|
570 580
....*....|....*....|....*.
gi 24418933 589 VEGYPLTISGKIQKFKLREQMEQHLK 614
Cdd:PRK05605 547 VDELPRDQLGKVRRREVREELLEKLG 572
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
68-613 |
1.23e-84 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 274.92 E-value: 1.23e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 68 HLVNTTVGECLDATAQRFPDREALVILHEniRLNFAQLKEEVDKAAsGLLS--IGLRKGDRLGMWGPNSYAWVLIQLATA 145
Cdd:PRK08314 6 TLPETSLFHNLEVSARRYPDKTAIVFYGR--AISYRELLEEAERLA-GYLQqeCGVRKGDRVLLYMQNSPQFVIAYYAIL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 146 QAGIILVSVNPAYQSSELEYVLRKVGCKGIVFpkqfkTQQYYDILKQVCPELEKAQ------PGALKSE---RLPDLttv 216
Cdd:PRK08314 83 RANAVVVPVNPMNREEELAHYVTDSGARVAIV-----GSELAPKVAPAVGNLRLRHvivaqySDYLPAEpeiAVPAW--- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 217 ISVDAPLP-----GTLLLDDIVAAG-------GKEQNLAQLRYnqrflscydpiniqfTSGTTGNPKGATLSH----HNI 280
Cdd:PRK08314 155 LRAEPPLQalapgGVVAWKEALAAGlappphtAGPDDLAVLPY---------------TSGTTGVPKGCMHTHrtvmANA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 281 VNNSMLIGQrlkmptkTAEELRL-VLpsPLYHCLGsvggtMVSMMH-----GATLLLsSPSFNGKKALEAISREKGTLLY 354
Cdd:PRK08314 220 VGSVLWSNS-------TPESVVLaVL--PLFHVTG-----MVHSMNapiyaGATVVL-MPRWDREAAARLIERYRVTHWT 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 355 GTPTMFVDILNQPDFSSYDFTSIRggVIAGSPAP-PElirAIINKmnMKELVVV-----YGTTENSPVTFMNFPEDTLEQ 428
Cdd:PRK08314 285 NIPTMVVDFLASPGLAERDLSSLR--YIGGGGAAmPE---AVAER--LKELTGLdyvegYGLTETMAQTHSNPPDRPKLQ 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 429 KAGsvgriMPH--TEAQIVNVETGELTNLNVPGELYIRGYCVMQGYWGEPQKT---FETVGQDKWYRTGDIALMDEQGFC 503
Cdd:PRK08314 358 CLG-----IPTfgVDARVIDPETLEELPPGEVGEIVVHGPQVFKGYWNRPEATaeaFIEIDGKRFFRTGDLGRMDEEGYF 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 504 KIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQEAQVVGVKDERMGEEICACIRLKSGE--TTTAEEIKAFCKGKISHFK 581
Cdd:PRK08314 433 FITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPDPRRGETVKAVVVLRPEArgKTTEEEIIAWAREHMAAYK 512
|
570 580 590
....*....|....*....|....*....|..
gi 24418933 582 IPRYIVFVEGYPLTISGKIQKFKLREQMEQHL 613
Cdd:PRK08314 513 YPRIVEFVDSLPKSGSGKILWRQLQEQEKARA 544
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
78-607 |
2.77e-84 |
|
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: 272.25 E-value: 2.77e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 78 LDATAQRFPDREALVilHENIRLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVSVNPA 157
Cdd:cd12118 10 LERAAAVYPDRTSIV--YGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 158 YQSSELEYVLRKVGCKGIVFPKQFktqQYYDILKQVCPELEKAQPgalKSErlpdlttvisvdaplpgtlllddivaagg 237
Cdd:cd12118 88 LDAEEIAFILRHSEAKVLFVDREF---EYEDLLAEGDPDFEWIPP---ADE----------------------------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 238 keqnlaqlrynqrflscYDPINIQFTSGTTGNPKGATLSHHNIVNNSMLIGQRLKMPTKTAEELRLvlpsPLYHCLG--- 314
Cdd:cd12118 133 -----------------WDPIALNYTSGTTGRPKGVVYHHRGAYLNALANILEWEMKQHPVYLWTL----PMFHCNGwcf 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 315 -----SVGGTMVSMmhgatlllssPSFNGKKALEAISREKGTLLYGTPTMFVDILNQPDFSSYDFTSIRGGVIAGSPAPP 389
Cdd:cd12118 192 pwtvaAVGGTNVCL----------RKVDAKAIYDLIEKHKVTHFCGAPTVLNMLANAPPSDARPLPHRVHVMTAGAPPPA 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 390 elirAIINKMNMKELVV--VYGTTENS-PVTFMNF-PE-DTL--EQKAGSVGR----IMPHTEAQIVNVETGEltnlNVP 458
Cdd:cd12118 262 ----AVLAKMEELGFDVthVYGLTETYgPATVCAWkPEwDELptEERARLKARqgvrYVGLEEVDVLDPETMK----PVP 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 459 ------GELYIRGYCVMQGYWGEPQKTFETVgQDKWYRTGDIALMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKH 532
Cdd:cd12118 334 rdgktiGEIVFRGNIVMKGYLKNPEATAEAF-RGGWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKH 412
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24418933 533 PQVQEAQVVGVKDERMGEEICACIRLKSGETTTAEEIKAFCKGKISHFKIPRYIVFVEgYPLTISGKIQKFKLRE 607
Cdd:cd12118 413 PAVLEAAVVARPDEKWGEVPCAFVELKEGAKVTEEEIIAFCREHLAGFMVPKTVVFGE-LPKTSTGKIQKFVLRD 486
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
86-607 |
3.50e-84 |
|
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: 271.88 E-value: 3.50e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 86 PDREALVILHENIRLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVSVNPAYQSSELEY 165
Cdd:cd05926 1 PDAPALVVPGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 166 VLRKVGCKGIVFPKQfktqqyydilkqvcpELEKAQPGALKSE-RLPDLT--TVISVDAPLPGTLLLDDIVAAGGKEQNL 242
Cdd:cd05926 81 YLADLGSKLVLTPKG---------------ELGPASRAASKLGlAILELAldVGVLIRAPSAESLSNLLADKKNAKSEGV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 243 AQLRynqrflscyDPINIQFTSGTTGNPKGATLSHHNIVNNSMLIGQRLKMptkTAEElRLVLPSPLYHCLGSVGGTMVS 322
Cdd:cd05926 146 PLPD---------DLALILHTSGTTGRPKGVPLTHRNLAASATNITNTYKL---TPDD-RTLVVMPLFHVHGLVASLLST 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 323 MMHGATLLLSsPSFNGKKALEAISREKGTLLYGTPTMFVDILNQPDFSSYD-FTSIRggVI--AGSPAPPELIRAIINKM 399
Cdd:cd05926 213 LAAGGSVVLP-PRFSASTFWPDVRDYNATWYTAVPTIHQILLNRPEPNPESpPPKLR--FIrsCSASLPPAVLEALEATF 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 400 NMKeLVVVYGTTENSPVTFMNfPEDTLEQKAGSVGRimPH-TEAQIVNvETGELTNLNVPGELYIRGYCVMQGYWGEPQK 478
Cdd:cd05926 290 GAP-VLEAYGMTEAAHQMTSN-PLPPGPRKPGSVGK--PVgVEVRILD-EDGEILPPGVVGEICLRGPNVTRGYLNNPEA 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 479 TFETVGQDKWYRTGDIALMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQEAQVVGVKDERMGEEICACIRL 558
Cdd:cd05926 365 NAEAAFKDGWFRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVL 444
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 24418933 559 KSGETTTAEEIKAFCKGKISHFKIPRYIVFVEGYPLTISGKIQKFKLRE 607
Cdd:cd05926 445 REGASVTEEELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKVAE 493
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
73-611 |
9.79e-84 |
|
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: 272.02 E-value: 9.79e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 73 TVGECLDATAQRFPDREALVilHENIRLNFAQLKEEVDKAASGLLSIGLRKGDR----LgmwgPNSYAWVLIQLATAQAG 148
Cdd:COG1021 26 TLGDLLRRRAERHPDRIAVV--DGERRLSYAELDRRADRLAAGLLALGLRPGDRvvvqL----PNVAEFVIVFFALFRAG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 149 IILVSVNPAYQSSELEYVLRKVGCKGIVFPKQFKTQQYYDILKQVCpelekaqpgalksERLPDLTTVISVDAPLPGTLL 228
Cdd:COG1021 100 AIPVFALPAHRRAEISHFAEQSEAVAYIIPDRHRGFDYRALARELQ-------------AEVPSLRHVLVVGDAGEFTSL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 229 lDDIVAAGGKE-------QNLAQLrynqrflscydpiniQFTSGTTGNPKGATLSHHNIVNNSmligqrlkmpTKTAEEL 301
Cdd:COG1021 167 -DALLAAPADLseprpdpDDVAFF---------------QLSGGTTGLPKLIPRTHDDYLYSV----------RASAEIC 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 302 RL--------VLP--------SPLYhcLG--SVGGTMVsmmhgatlLLSSPSFNGkkALEAISREKGTLLYGTPTMFVDI 363
Cdd:COG1021 221 GLdadtvylaALPaahnfplsSPGV--LGvlYAGGTVV--------LAPDPSPDT--AFPLIERERVTVTALVPPLALLW 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 364 LNQPDFSSYDFTSIRGGVIAGSPAPPELIRAIINKMNMKeLVVVYGTTEnSPVtfmNF--PEDTLEQKAGSVGR-IMPHT 440
Cdd:COG1021 289 LDAAERSRYDLSSLRVLQVGGAKLSPELARRVRPALGCT-LQQVFGMAE-GLV---NYtrLDDPEEVILTTQGRpISPDD 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 441 EAQIVN-----VETGEltnlnvPGELYIRGYCVMQGYWGEP---QKTFEtvgQDKWYRTGDIALMDEQGFCKIVGRSKDM 512
Cdd:COG1021 364 EVRIVDedgnpVPPGE------VGELLTRGPYTIRGYYRAPehnARAFT---PDGFYRTGDLVRRTPDGYLVVEGRAKDQ 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 513 IIRGGENIYPAELEDFFLKHPQVQEAQVVGVKDERMGEEICACIRLKsGETTTAEEIKAFCKGK-ISHFKIPRYIVFVEG 591
Cdd:COG1021 435 INRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGERSCAFVVPR-GEPLTLAELRRFLRERgLAAFKLPDRLEFVDA 513
|
570 580
....*....|....*....|
gi 24418933 592 YPLTISGKIQKFKLREQMEQ 611
Cdd:COG1021 514 LPLTAVGKIDKKALRAALAA 533
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
78-607 |
4.68e-83 |
|
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: 269.89 E-value: 4.68e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 78 LDATAQRFPDREALVILHEN--IRLNFAQLKEEVDKAASGLLSIGLRKGDRLG--MWgpNSYAWVLIQLATAQAGIILVS 153
Cdd:cd12119 2 LEHAARLHGDREIVSRTHEGevHRYTYAEVAERARRLANALRRLGVKPGDRVAtlAW--NTHRHLELYYAVPGMGAVLHT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 154 VNPAYQSSELEYVLRKVGCKGIVFPKQFKtqqyydilkqvcPELEKAQPgalkseRLPDLTTVI----SVDAPLPGTLLL 229
Cdd:cd12119 80 INPRLFPEQIAYIINHAEDRVVFVDRDFL------------PLLEAIAP------RLPTVEHVVvmtdDAAMPEPAGVGV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 230 ---DDIVAAGGKEQNLAQLRYNQRFLSCYdpiniqfTSGTTGNPKGATLSHHNIVNNSMLIGQRLKMPTktaEELRLVLP 306
Cdd:cd12119 142 layEELLAAESPEYDWPDFDENTAAAICY-------TSGTTGNPKGVVYSHRSLVLHAMAALLTDGLGL---SESDVVLP 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 307 -SPLYHcLGSVGGTMVSMMHGATLLLSSPSFNGKKALEAISREKGTLLYGTPTMFVDILNQPDFSSYDFTSIRGGVIAGS 385
Cdd:cd12119 212 vVPMFH-VNAWGLPYAAAMVGAKLVLPGPYLDPASLAELIEREGVTFAAGVPTVWQGLLDHLEANGRDLSSLRRVVIGGS 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 386 PAPPELIRAIiNKMNMkELVVVYGTTENSPVTFMNFP-----EDTLEQKAG---SVGRIMPHTEAQIVNVETGELtnlnv 457
Cdd:cd12119 291 AVPRSLIEAF-EERGV-RVIHAWGMTETSPLGTVARPpsehsNLSEDEQLAlraKQGRPVPGVELRIVDDDGREL----- 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 458 P------GELYIRGYCVMQGYWGEPQKTfETVGQDKWYRTGDIALMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLK 531
Cdd:cd12119 364 PwdgkavGELQVRGPWVTKSYYKNDEES-EALTEDGWLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMA 442
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24418933 532 HPQVQEAQVVGVKDERMGEEICACIRLKSGETTTAEEIKAFCKGKISHFKIPRYIVFVEGYPLTISGKIQKFKLRE 607
Cdd:cd12119 443 HPAVAEAAVIGVPHPKWGERPLAVVVLKEGATVTAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKALRE 518
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
99-600 |
1.24e-80 |
|
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: 260.87 E-value: 1.24e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 99 RLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVSVNPAYQSSELEYVLRKVGCKGIVfp 178
Cdd:cd05935 1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAV-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 179 kqfktqqyydilkqvcpelekaqpgaLKSErlpdlttvisvdaplpgtllLDDIVAaggkeqnlaqlrynqrflscydpi 258
Cdd:cd05935 79 --------------------------VGSE--------------------LDDLAL------------------------ 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 259 nIQFTSGTTGNPKGATLSHHNIVNNSMLigqrLKMPTKTAEELRLVLPSPLYHCLGSVGGTMVSMMHGATLLLSSpSFNG 338
Cdd:cd05935 89 -IPYTSGTTGLPKGCMHTHFSAAANALQ----SAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMA-RWDR 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 339 KKALEAISREKGTLLYGTPTMFVDILNQPDFSSYDFTSIRGGVIAGSPAPPELIRAIINKMNMKeLVVVYGTTENSPVTF 418
Cdd:cd05935 163 ETALELIEKYKVTFWTNIPTMLVDLLATPEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTGLR-FVEGYGLTETMSQTH 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 419 MNFPedtLEQKAGSVGRIMPHTEAQIVNVETGELTNLNVPGELYIRGYCVMQGYWGEPQKT---FETVGQDKWYRTGDIA 495
Cdd:cd05935 242 TNPP---LRPKLQCLGIP*FGVDARVIDIETGRELPPNEVGEIVVRGPQIFKGYWNRPEETeesFIEIKGRRFFRTGDLG 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 496 LMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQEAQVVGVKDERMGEEICACIRLKSGE--TTTAEEIKAFC 573
Cdd:cd05935 319 YMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEYrgKVTEEDIIEWA 398
|
490 500
....*....|....*....|....*..
gi 24418933 574 KGKISHFKIPRYIVFVEGYPLTISGKI 600
Cdd:cd05935 399 REQMAAYKYPREVEFVDELPRSASGKI 425
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
99-606 |
1.40e-77 |
|
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: 254.99 E-value: 1.40e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 99 RLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVSVNPAYQSSELEYVLRKVGCKGIVFP 178
Cdd:cd05959 29 SLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVVS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 179 KQFktqqyydiLKQVCPELEKAQPgalkserlpDLTTVISVDA--PLPGTLLLDDIVAAGGKEQNLAQLRynqrflsCYD 256
Cdd:cd05959 109 GEL--------APVLAAALTKSEH---------TLVVLIVSGGagPEAGALLLAELVAAEAEQLKPAATH-------ADD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 257 PINIQFTSGTTGNPKGATLSHHNIVNNSMLIGQRLkmpTKTAEELRLVLPSPLYHCLGSVGGTMVSMMHGATLLLSSPSF 336
Cdd:cd05959 165 PAFWLYSSGSTGRPKGVVHLHADIYWTAELYARNV---LGIREDDVCFSAAKLFFAYGLGNSLTFPLSVGATTVLMPERP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 337 NGKKALEAISREKGTLLYGTPTMFVDILNQPDFSSYDFTSIRGGVIAGSPAPPELIRAIINKMNMkELVVVYGTTENSPV 416
Cdd:cd05959 242 TPAAVFKRIRRYRPTVFFGVPTLYAAMLAAPNLPSRDLSSLRLCVSAGEALPAEVGERWKARFGL-DILDGIGSTEMLHI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 417 TFMNFPEDTleqKAGSVGRIMPHTEAQIVNvETGELTNLNVPGELYIRGYCVMQGYWGEPQKTFETVgQDKWYRTGDIAL 496
Cdd:cd05959 321 FLSNRPGRV---RYGTTGKPVPGYEVELRD-EDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTF-QGEWTRTGDKYV 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 497 MDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQEAQVVGVKDERMGEEICACIRLKSGETTTA---EEIKAFC 573
Cdd:cd05959 396 RDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPGYEDSEaleEELKEFV 475
|
490 500 510
....*....|....*....|....*....|...
gi 24418933 574 KGKISHFKIPRYIVFVEGYPLTISGKIQKFKLR 606
Cdd:cd05959 476 KDRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
72-547 |
4.30e-77 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 256.57 E-value: 4.30e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 72 TTVGECLDATAQRFPDREALVILHENI--RLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGi 149
Cdd:COG1022 11 DTLPDLLRRRAARFPDRVALREKEDGIwqSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAG- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 150 iLVSVnPAYQSS---ELEYVLRKVGCKGIVFpkqfKTQQYYDILKQVcpelekaqpgalkSERLPDLTTVISVDAP---- 222
Cdd:COG1022 90 -AVTV-PIYPTSsaeEVAYILNDSGAKVLFV----EDQEQLDKLLEV-------------RDELPSLRHIVVLDPRglrd 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 223 LPGTLLLDDIVAAGGKEQNLAQLRYNQRFLSCYDPINIQFTSGTTGNPKGATLSHHNIVNNSMLIGQRLKMpTKTAEELr 302
Cdd:COG1022 151 DPRLLSLDELLALGREVADPAELEARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPL-GPGDRTL- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 303 LVLPspLYHCLGSVGGTMVsMMHGA--------------------TLLLSSPS-----------------------FN-- 337
Cdd:COG1022 229 SFLP--LAHVFERTVSYYA-LAAGAtvafaespdtlaedlrevkpTFMLAVPRvwekvyagiqakaeeagglkrklFRwa 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 338 ---GKKALEAISREKG-TLLYGTPTMFVDILNqpdfssydFTSIR---GG-----VIAGSPAPPELIR---AIinKMNMK 402
Cdd:COG1022 306 lavGRRYARARLAGKSpSLLLRLKHALADKLV--------FSKLRealGGrlrfaVSGGAALGPELARffrAL--GIPVL 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 403 ElvvVYGTTENSPVTFMNFPEDtleQKAGSVGRIMPHTEAQIvnvetGEltnlnvPGELYIRGYCVMQGYWGEPQKTFET 482
Cdd:COG1022 376 E---GYGLTETSPVITVNRPGD---NRIGTVGPPLPGVEVKI-----AE------DGEILVRGPNVMKGYYKNPEATAEA 438
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24418933 483 VGQDKWYRTGDIALMDEQGFCKIVGRSKDMII-RGGENIYPAELEDFFLKHPQVQEAQVVGvkDER 547
Cdd:COG1022 439 FDADGWLHTGDIGELDEDGFLRITGRKKDLIVtSGGKNVAPQPIENALKASPLIEQAVVVG--DGR 502
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
82-609 |
9.13e-76 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 249.72 E-value: 9.13e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 82 AQRFPDREALVILHENIRLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVSVNPAYQSS 161
Cdd:PRK09088 5 ARLQPQRLAAVDLALGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSAS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 162 ELEYVLrkvgckgivfpkqfktqqyydilkqvcpelEKAQPgalkseRLpdlttvisvdaplpgtLLLDDIVAAGGKE-Q 240
Cdd:PRK09088 85 ELDALL------------------------------QDAEP------RL----------------LLGDDAVAAGRTDvE 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 241 NLAQLRYNqrfLSCYDPIN-----------IQFTSGTTGNPKGATLSHHNI----VNNSMLigqrlkmpTKTAEELRLVL 305
Cdd:PRK09088 113 DLAAFIAS---ADALEPADtpsippervslILFTSGTSGQPKGVMLSERNLqqtaHNFGVL--------GRVDAHSSFLC 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 306 PSPLYHCLGSVGGTMVSMMHGATLLLSsPSFNGKKALEAISREK--GTLLYGTPTMFVDILNQPDFSSYDFTSIRGGVIA 383
Cdd:PRK09088 182 DAPMFHIIGLITSVRPVLAVGGSILVS-NGFEPKRTLGRLGDPAlgITHYFCVPQMAQAFRAQPGFDAAALRHLTALFTG 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 384 GSPAPPELIRAIINkmNMKELVVVYGTTENSPVTFMNFPEDTLEQKAGSVGRIMPHTEAQIVNvETGELTNLNVPGELYI 463
Cdd:PRK09088 261 GAPHAAEDILGWLD--DGIPMVDGFGMSEAGTVFGMSVDCDVIRAKAGAAGIPTPTVQTRVVD-DQGNDCPAGVPGELLL 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 464 RGYCVMQGYWGEPQKTFETVGQDKWYRTGDIALMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQEAQVVGV 543
Cdd:PRK09088 338 RGPNLSPGYWRRPQATARAFTGDGWFRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGM 417
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24418933 544 KDERMGEEICACIRLKSGETTTAEEIKAFCKGKISHFKIPRYIVFVEGYPLTISGKIQKFKLREQM 609
Cdd:PRK09088 418 ADAQWGEVGYLAIVPADGAPLDLERIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARLRDAL 483
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
82-610 |
1.33e-75 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 249.80 E-value: 1.33e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 82 AQRFPDREALVILHENIrlNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVSVNPAYQSS 161
Cdd:PRK06145 12 ARRTPDRAALVYRDQEI--SYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAAD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 162 ELEYVLRKVGCKGIVFPKQFktqqyydilkQVCPELEKAQpgalkserlpdltTVISVDAPLPGTLLlddivAAGGKEQN 241
Cdd:PRK06145 90 EVAYILGDAGAKLLLVDEEF----------DAIVALETPK-------------IVIDAAAQADSRRL-----AQGGLEIP 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 242 LAQLRYNQrflscyDPINIQFTSGTTGNPKGATLSHHNIVNNSMLIGQRLKMptkTAEElRLVLPSPLYHclgsVGGT-- 319
Cdd:PRK06145 142 PQAAVAPT------DLVRLMYTSGTTDRPKGVMHSYGNLHWKSIDHVIALGL---TASE-RLLVVGPLYH----VGAFdl 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 320 --MVSMMHGATLLLSSpSFNGKKALEAISREKGTLLYGTPTMFVDILNQPDFSSYDFTSIRGGVIAGSPAPPELIRAIIN 397
Cdd:PRK06145 208 pgIAVLWVGGTLRIHR-EFDPEAVLAAIERHRLTCAWMAPVMLSRVLTVPDRDRFDLDSLAWCIGGGEKTPESRIRDFTR 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 398 KMNMKELVVVYGTTEN-SPVTFMNFPEDTleQKAGSVGRIMPHTEAQIVNvETGELTNLNVPGELYIRGYCVMQGYWGEP 476
Cdd:PRK06145 287 VFTRARYIDAYGLTETcSGDTLMEAGREI--EKIGSTGRALAHVEIRIAD-GAGRWLPPNMKGEICMRGPKVTKGYWKDP 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 477 QKTFETVGQDkWYRTGDIALMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQEAQVVGVKDERMGEEICACI 556
Cdd:PRK06145 364 EKTAEAFYGD-WFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVV 442
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 24418933 557 RLKSGETTTAEEIKAFCKGKISHFKIPRYIVFVEGYPLTISGKIQKFKLREQME 610
Cdd:PRK06145 443 VLNPGATLTLEALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVLRDELN 496
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
72-608 |
1.91e-73 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 244.51 E-value: 1.91e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 72 TTVGECLDATAQRFPDREALVIlhENIRLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSyAWVLIQLATAQ-AGII 150
Cdd:PRK06188 12 ATYGHLLVSALKRYPDRPALVL--GDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNR-PEVLMAIGAAQlAGLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 151 LVSVNPAYQSSELEYVLRKVGCKGIVF-PKQFktqqyydilkqvcpeLEKAqpGALKsERLPDLTTVISVDaPLPGTLll 229
Cdd:PRK06188 89 RTALHPLGSLDDHAYVLEDAGISTLIVdPAPF---------------VERA--LALL-ARVPSLKHVLTLG-PVPDGV-- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 230 dDIVAAGGKEQNlAQLRynqRFLSCYDPINIQFTSGTTGNPKGATLSHHNIVNNSMLIGQRLKMPtktaEELRLVLPSPL 309
Cdd:PRK06188 148 -DLLAAAAKFGP-APLV---AAALPPDIAGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWP----ADPRFLMCTPL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 310 YHclgsVGGTMV--SMMHGATLLLSsPSFNGKKALEAISREKGTLLYGTPTMFVDILNQPDFSSYDFTSIRGGVIAGSPA 387
Cdd:PRK06188 219 SH----AGGAFFlpTLLRGGTVIVL-AKFDPAEVLRAIEEQRITATFLVPTMIYALLDHPDLRTRDLSSLETVYYGASPM 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 388 PPELIRAIINKMNmKELVVVYGTTE-NSPVTFM----NFPEDtlEQKAGSVGRIMPHTEAQIVN-----VETGEltnlnv 457
Cdd:PRK06188 294 SPVRLAEAIERFG-PIFAQYYGQTEaPMVITYLrkrdHDPDD--PKRLTSCGRPTPGLRVALLDedgreVAQGE------ 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 458 PGELYIRGYCVMQGYWGEPQKTFETVgQDKWYRTGDIALMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQE 537
Cdd:PRK06188 365 VGEICVRGPLVMDGYWNRPEETAEAF-RDGWLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQ 443
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24418933 538 AQVVGVKDERMGEEICACIRLKSGETTTAEEIKAFCKGKISHFKIPRYIVFVEGYPLTISGKIQKFKLREQ 608
Cdd:PRK06188 444 VAVIGVPDEKWGEAVTAVVVLRPGAAVDAAELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKALRAR 514
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
73-607 |
3.45e-73 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 245.17 E-value: 3.45e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 73 TVGECLDATAQRFPDREALVILHENIrlNFAQLKEEVDKAASGLLS-IGLRKGDRLGMWGPNSYAWVLIQLATAQAGIIL 151
Cdd:PRK08751 26 TVAEVFATSVAKFADRPAYHSFGKTI--TYREADQLVEQFAAYLLGeLQLKKGDRVALMMPNCLQYPIATFGVLRAGLTV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 152 VSVNPAYQSSELEYVLRKVGCKGIVFPKQFKT---QQYYDI-LKQVCP----ELEKAQPGALKSERLPDLTTVISvDAPL 223
Cdd:PRK08751 104 VNVNPLYTPRELKHQLIDSGASVLVVIDNFGTtvqQVIADTpVKQVITtglgDMLGFPKAALVNFVVKYVKKLVP-EYRI 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 224 PGTLLLDDIVAAGGKEqnlaqlRYNQRFLSCYDPINIQFTSGTTGNPKGATLSHHNIVNNSMLIGQRLKMPTKTAEELRL 303
Cdd:PRK08751 183 NGAIRFREALALGRKH------SMPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQWLAGTGKLEEGCEV 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 304 VLPS-PLYHCLGSVGGTMVSM-MHGATLLLSSPSfNGKKALEAISREKGTLLYGTPTMFVDILNQPDFSSYDFTSIR--- 378
Cdd:PRK08751 257 VITAlPLYHIFALTANGLVFMkIGGCNHLISNPR-DMPGFVKELKKTRFTAFTGVNTLFNGLLNTPGFDQIDFSSLKmtl 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 379 GGVIAGSPAPPELIRaiinKMNMKELVVVYGTTENSPVTFMNfpEDTLEQKAGSVGRIMPHTEAQIVNvETGELTNLNVP 458
Cdd:PRK08751 336 GGGMAVQRSVAERWK----QVTGLTLVEAYGLTETSPAACIN--PLTLKEYNGSIGLPIPSTDACIKD-DAGTVLAIGEI 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 459 GELYIRGYCVMQGYWGEPQKTFETVGQDKWYRTGDIALMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQEA 538
Cdd:PRK08751 409 GELCIKGPQVMKGYWKRPEETAKVMDADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEV 488
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24418933 539 QVVGVKDERMGEEICACIrLKSGETTTAEEIKAFCKGKISHFKIPRYIVFVEGYPLTISGKIQKFKLRE 607
Cdd:PRK08751 489 AAVGVPDEKSGEIVKVVI-VKKDPALTAEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRRELRD 556
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
73-606 |
4.05e-73 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 244.54 E-value: 4.05e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 73 TVGECLDATAQRFPDREALVILHENIRlnFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILV 152
Cdd:PRK07059 24 SLADLLEESFRQYADRPAFICMGKAIT--YGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 153 SVNPAYQSSELEYVLRKVGCKGIVFPKQFKTqqyydILKQVCPELE-----KAQPGALKSERLPDLTTVIS-----VDA- 221
Cdd:PRK07059 102 NVNPLYTPRELEHQLKDSGAEAIVVLENFAT-----TVQQVLAKTAvkhvvVASMGDLLGFKGHIVNFVVRrvkkmVPAw 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 222 PLPGTLLLDDIVAAGGKeqnlaqLRYNQRFLSCYDPINIQFTSGTTGNPKGATLSHHNIVNNSMLIGQRLKmPTKTA--- 298
Cdd:PRK07059 177 SLPGHVRFNDALAEGAR------QTFKPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVLQMEAWLQ-PAFEKkpr 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 299 -EELRLVLPSPLYHCLGSVGGTMVSMMHGATLLL-----SSPSFngkkaLEAISREKGTLLYGTPTMFVDILNQPDFSSY 372
Cdd:PRK07059 250 pDQLNFVCALPLYHIFALTVCGLLGMRTGGRNILipnprDIPGF-----IKELKKYQVHIFPAVNTLYNALLNNPDFDKL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 373 DFTSIR---GGVIAgspappeLIRAIIN---KMNMKELVVVYGTTENSPVTFMNfPEDTLEQkAGSVGRIMPHTEAQIVN 446
Cdd:PRK07059 325 DFSKLIvanGGGMA-------VQRPVAErwlEMTGCPITEGYGLSETSPVATCN-PVDATEF-SGTIGLPLPSTEVSIRD 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 447 vETGELTNLNVPGELYIRGYCVMQGYWGEPQKTFETVGQDKWYRTGDIALMDEQGFCKIVGRSKDMIIRGGENIYPAELE 526
Cdd:PRK07059 396 -DDGNDLPLGEPGEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIE 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 527 DFFLKHPQVQEAQVVGVKDERMGEEICACIrLKSGETTTAEEIKAFCKGKISHFKIPRYIVFVEGYPLTISGKIQKFKLR 606
Cdd:PRK07059 475 EVVASHPGVLEVAAVGVPDEHSGEAVKLFV-VKKDPALTEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRRELR 553
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
87-607 |
8.58e-73 |
|
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: 240.65 E-value: 8.58e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 87 DREALVILHENIrlNFAQLKEEVDKAASGLLSIG-LRKGDRLGMWGPNSYAWVLIQLATAQAGIILVSVNPAYQSSELEY 165
Cdd:cd05941 1 DRIAIVDDGDSI--TYADLVARAARLANRLLALGkDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 166 VLRKvgckgivfpkqfktqqyydilkqvcpelekAQPgalkserlpdlttvisvdaplpgTLLLDDIVaaggkeqnlaql 245
Cdd:cd05941 79 VITD------------------------------SEP-----------------------SLVLDPAL------------ 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 246 rynqrflscydpinIQFTSGTTGNPKGATLSHHNIVNNSmligQRLKMPTKTAEELRLVLPSPLYHCLGSVGGTMVSMMH 325
Cdd:cd05941 94 --------------ILYTSGTTGRPKGVVLTHANLAANV----RALVDAWRWTEDDVLLHVLPLHHVHGLVNALLCPLFA 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 326 GATLLLSsPSFNGKKALEAISREKGTLLYGTPTMFVDILNQPDFSSYDFTSIRGG-------VIAGSPAPPELIRAIINK 398
Cdd:cd05941 156 GASVEFL-PKFDPKEVAISRLMPSITVFMGVPTIYTRLLQYYEAHFTDPQFARAAaaerlrlMVSGSAALPVPTLEEWEA 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 399 MNMKELVVVYGTTEnspvTFMNF--PEDTlEQKAGSVGRIMPHTEAQIVNVETGELTNLNVPGELYIRGYCVMQGYWGEP 476
Cdd:cd05941 235 ITGHTLLERYGMTE----IGMALsnPLDG-ERRPGTVGMPLPGVQARIVDEETGEPLPRGEVGEIQVRGPSVFKEYWNKP 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 477 QKTFETVGQDKWYRTGDIALMDEQGFCKIVGRSKDMII-RGGENIYPAELEDFFLKHPQVQEAQVVGVKDERMGEEICAC 555
Cdd:cd05941 310 EATKEEFTDDGWFKTGDLGVVDEDGYYWILGRSSVDIIkSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAV 389
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 24418933 556 IRLKSGETT-TAEEIKAFCKGKISHFKIPRYIVFVEGYPLTISGKIQKFKLRE 607
Cdd:cd05941 390 VVLRAGAAAlSLEELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
72-607 |
1.11e-72 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 243.58 E-value: 1.11e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 72 TTVGECLDATAQRFPDREALVILheNIRLNFAQLkEEVDKAASGLLS--IGLRKGDRLGMWGPNSYAWVLIQLATAQAGI 149
Cdd:PRK12492 24 KSVVEVFERSCKKFADRPAFSNL--GVTLSYAEL-ERHSAAFAAYLQqhTDLVPGDRIAVQMPNVLQYPIAVFGALRAGL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 150 ILVSVNPAYQSSELEYVLRKVGCKGIVFPKQFKTQqyydiLKQVCPE-----LEKAQPGALkserLPDL------TTVIS 218
Cdd:PRK12492 101 IVVNTNPLYTAREMRHQFKDSGARALVYLNMFGKL-----VQEVLPDtgieyLIEAKMGDL----LPAAkgwlvnTVVDK 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 219 VDAPLPGTLLLDDI----VAAGGKEQNLAQLRynqrfLSCYDPINIQFTSGTTGNPKGATLSHHNIVNNSMLI------- 287
Cdd:PRK12492 172 VKKMVPAYHLPQAVpfkqALRQGRGLSLKPVP-----VGLDDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVraclsql 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 288 ---GQRLkmpTKTAEELrLVLPSPLYHCLGSVGGTMVSMMHGA-TLLLSSP-SFNGkkALEAISREKGTLLYGTPTMFVD 362
Cdd:PRK12492 247 gpdGQPL---MKEGQEV-MIAPLPLYHIYAFTANCMCMMVSGNhNVLITNPrDIPG--FIKELGKWRFSALLGLNTLFVA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 363 ILNQPDFSSYDFTSIRGGVIAGSPappeLIRAIINK---MNMKELVVVYGTTENSPVTFMNfPEDTLeQKAGSVGRIMPH 439
Cdd:PRK12492 321 LMDHPGFKDLDFSALKLTNSGGTA----LVKATAERweqLTGCTIVEGYGLTETSPVASTN-PYGEL-ARLGTVGIPVPG 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 440 TEAQIVNVETGELTnLNVPGELYIRGYCVMQGYWGEPQKTFETVGQDKWYRTGDIALMDEQGFCKIVGRSKDMIIRGGEN 519
Cdd:PRK12492 395 TALKVIDDDGNELP-LGERGELCIKGPQVMKGYWQQPEATAEALDAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFN 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 520 IYPAELEDFFLKHPQVQEAQVVGVKDERMGEEICACIRLKSGeTTTAEEIKAFCKGKISHFKIPRYIVFVEGYPLTISGK 599
Cdd:PRK12492 474 VYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVKLFVVARDP-GLSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGK 552
|
....*...
gi 24418933 600 IQKFKLRE 607
Cdd:PRK12492 553 ILRRELRD 560
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
76-608 |
7.60e-72 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 241.50 E-value: 7.60e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 76 ECLDATAQRFPDREALVILHENirLNFAQLkEEVDKAASGLLS--IGLRKGDRLGMWGPNsyawvLIQLATA-----QAG 148
Cdd:PRK08974 27 DMFEQAVARYADQPAFINMGEV--MTFRKL-EERSRAFAAYLQngLGLKKGDRVALMMPN-----LLQYPIAlfgilRAG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 149 IILVSVNPAYQSSELEYVLRKVGCKGIVFPKQF---------KTQQYYDILKQVCPELEKAQpGALKS------ERLpdl 213
Cdd:PRK08974 99 MIVVNVNPLYTPRELEHQLNDSGAKAIVIVSNFahtlekvvfKTPVKHVILTRMGDQLSTAK-GTLVNfvvkyiKRL--- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 214 ttVISVDapLPGTLLLDDIVAAGGKEQnlaqlrYNQRFLSCYDPINIQFTSGTTGNPKGATLSHHNIVNNSMLIGQRLKM 293
Cdd:PRK08974 175 --VPKYH--LPDAISFRSALHKGRRMQ------YVKPELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQAKAAYGP 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 294 PTKTAEELrLVLPSPLYHCLG-SVGGTMVSMMHGATLLLSSPsfngkKALEAISREKG----TLLYGTPTMFVDILNQPD 368
Cdd:PRK08974 245 LLHPGKEL-VVTALPLYHIFAlTVNCLLFIELGGQNLLITNP-----RDIPGFVKELKkypfTAITGVNTLFNALLNNEE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 369 FSSYDFTSIRGGVIAGSPAPpeliRAIINK---MNMKELVVVYGTTENSPVTFMNfPEDtLEQKAGSVGRIMPHTEAQIV 445
Cdd:PRK08974 319 FQELDFSSLKLSVGGGMAVQ----QAVAERwvkLTGQYLLEGYGLTECSPLVSVN-PYD-LDYYSGSIGLPVPSTEIKLV 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 446 NvETGELTNLNVPGELYIRGYCVMQGYWGEPQKTFEtVGQDKWYRTGDIALMDEQGFCKIVGRSKDMIIRGGENIYPAEL 525
Cdd:PRK08974 393 D-DDGNEVPPGEPGELWVKGPQVMLGYWQRPEATDE-VIKDGWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEI 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 526 EDFFLKHPQVQEAQVVGVKDERMGEEICACIrLKSGETTTAEEIKAFCKGKISHFKIPRYIVFVEGYPLTISGKIQKFKL 605
Cdd:PRK08974 471 EDVVMLHPKVLEVAAVGVPSEVSGEAVKIFV-VKKDPSLTEEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRREL 549
|
...
gi 24418933 606 REQ 608
Cdd:PRK08974 550 RDE 552
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
80-607 |
3.37e-71 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 239.44 E-value: 3.37e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 80 ATAQRFPDREALVilHENIRLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVSVNPAYQ 159
Cdd:PRK07788 57 HAARRAPDRAALI--DERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFS 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 160 SSELEYVLRKVGCKGIVFPKQFKtqqyyDILKQVCPELEKAqpgalkserlpdLTTVISVDA---PLPGTLLLDDIVAAG 236
Cdd:PRK07788 135 GPQLAEVAAREGVKALVYDDEFT-----DLLSALPPDLGRL------------RAWGGNPDDdepSGSTDETLDDLIAGS 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 237 GKEqNLAQLRYNQRFlscydpinIQFTSGTTGNPKGATLSHhniVNNSMLIGQRL-KMPTKTAEELrlVLPSPLYHCLGS 315
Cdd:PRK07788 198 STA-PLPKPPKPGGI--------VILTSGTTGTPKGAPRPE---PSPLAPLAGLLsRVPFRAGETT--LLPAPMFHATGW 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 316 VGGTmVSMMHGATLLLSSpSFNGKKALEAISREKGTLLYGTPTMFVDILNQPD--FSSYDFTSIRGGVIAGSPAPPELIR 393
Cdd:PRK07788 264 AHLT-LAMALGSTVVLRR-RFDPEATLEDIAKHKATALVVVPVMLSRILDLGPevLAKYDTSSLKIIFVSGSALSPELAT 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 394 AIINKMNmKELVVVYGTTENSPVTFMNfPEDtLEQKAGSVGRIMPHTEAQIVNVETGELTNlNVPGELYIRGYCVMQGYW 473
Cdd:PRK07788 342 RALEAFG-PVLYNLYGSTEVAFATIAT-PED-LAEAPGTVGRPPKGVTVKILDENGNEVPR-GVVGRIFVGNGFPFEGYT 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 474 GEPQKtfETVgqDKWYRTGDIALMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQEAQVVGVKDERMGEEIC 553
Cdd:PRK07788 418 DGRDK--QII--DGLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLR 493
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 24418933 554 ACIRLKSGETTTAEEIKAFCKGKISHFKIPRYIVFVEGYPLTISGKIQKFKLRE 607
Cdd:PRK07788 494 AFVVKAPGAALDEDAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELRE 547
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
76-607 |
1.17e-70 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 239.86 E-value: 1.17e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 76 ECLDATAQRFPDREALVILH------ENIRLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGI 149
Cdd:PRK07529 29 ELLSRAAARHPDAPALSFLLdadpldRPETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGEAAGI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 150 IlVSVNPAYQSSELEYVLRKVGCKGIV----FPKQfktqqyyDILKQVCPELEkaqpgalkseRLPDLTTVISVDAPLPG 225
Cdd:PRK07529 109 A-NPINPLLEPEQIAELLRAAGAKVLVtlgpFPGT-------DIWQKVAEVLA----------ALPELRTVVEVDLARYL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 226 TLLLDDIVAAGGKEQNLAQLRYNQRFLSCYD-------PINIQ-----F-TSGTTGNPKGATLSHHNIVNNSMLIGQRLK 292
Cdd:PRK07529 171 PGPKRLAVPLIRRKAHARILDFDAELARQPGdrlfsgrPIGPDdvaayFhTGGTTGMPKLAQHTHGNEVANAWLGALLLG 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 293 M-PTKTaeelrLVLPSPLYHCLGSVGGTMVSMMHGATLLLSSPS-FNGKKAL----EAISREKGTLLYGTPTMFVDILNQ 366
Cdd:PRK07529 251 LgPGDT-----VFCGLPLFHVNALLVTGLAPLARGAHVVLATPQgYRGPGVIanfwKIVERYRINFLSGVPTVYAALLQV 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 367 PdFSSYDFTSIRGGVIAGSPAPPELIRAIINKMNMKeLVVVYGTTENSPVTFMNFPEDtlEQKAGSVGRIMPHTEAQIVN 446
Cdd:PRK07529 326 P-VDGHDISSLRYALCGAAPLPVEVFRRFEAATGVR-IVEGYGLTEATCVSSVNPPDG--ERRIGSVGLRLPYQRVRVVI 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 447 VE----------TGEltnlnvPGELYIRGYCVMQGYWgEPQKTFETVGQDKWYRTGDIALMDEQGFCKIVGRSKDMIIRG 516
Cdd:PRK07529 402 LDdagrylrdcaVDE------VGVLCIAGPNVFSGYL-EAAHNKGLWLEDGWLNTGDLGRIDADGYFWLTGRAKDLIIRG 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 517 GENIYPAELEDFFLKHPQVQEAQVVGVKDERMGEEICACIRLKSGETTTAEEIKAFCKGKISH-FKIPRYIVFVEGYPLT 595
Cdd:PRK07529 475 GHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGELPVAYVQLKPGASATEAELLAFARDHIAErAAVPKHVRILDALPKT 554
|
570
....*....|..
gi 24418933 596 ISGKIQKFKLRE 607
Cdd:PRK07529 555 AVGKIFKPALRR 566
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
77-611 |
1.71e-70 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 236.86 E-value: 1.71e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 77 CLDATAQRFPDREALVilHENIRLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVSVNP 156
Cdd:PRK07470 12 FLRQAARRFPDRIALV--WGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 157 AYQSSELEYVLRKVGCKGIVFPKQFktQQYYDILKQVCPelekaqpgalkserlpDLTTVISVDAPlPGTLLLDDIVA-- 234
Cdd:PRK07470 90 RQTPDEVAYLAEASGARAMICHADF--PEHAAAVRAASP----------------DLTHVVAIGGA-RAGLDYEALVArh 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 235 AGGKEQNlAQLRYNqrflscyDPINIQFTSGTTGNPKGATLSHHN---IVNNsmligqRLK--MPTKTAEELRLVLpSPL 309
Cdd:PRK07470 151 LGARVAN-AAVDHD-------DPCWFFFTSGTTGRPKAAVLTHGQmafVITN------HLAdlMPGTTEQDASLVV-APL 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 310 YHCLGSVGGTMVSmmHGA-TLLLSSPSFNGKKALEAISREKGTLLYGTPTMFVDILNQPDFSSYDFTSIRGGVIAGSP-- 386
Cdd:PRK07470 216 SHGAGIHQLCQVA--RGAaTVLLPSERFDPAEVWALVERHRVTNLFTVPTILKMLVEHPAVDRYDHSSLRYVIYAGAPmy 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 387 -APPELIRAIINKMnmkeLVVVYGTTEnspVT--------FMNFPEDTLEQKAGSVGRIMPHTEAQIVNVEtGELTNLNV 457
Cdd:PRK07470 294 rADQKRALAKLGKV----LVQYFGLGE---VTgnitvlppALHDAEDGPDARIGTCGFERTGMEVQIQDDE-GRELPPGE 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 458 PGELYIRGYCVMQGYWGEPQ---KTFetvgQDKWYRTGDIALMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQ 534
Cdd:PRK07470 366 TGEICVIGPAVFAGYYNNPEanaKAF----RDGWFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPA 441
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24418933 535 VQEAQVVGVKDERMGEEICACIRLKSGETTTAEEIKAFCKGKISHFKIPRYIVFVEGYPLTISGKIQKFKLREQMEQ 611
Cdd:PRK07470 442 VSEVAVLGVPDPVWGEVGVAVCVARDGAPVDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMVREELEE 518
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
82-610 |
2.16e-70 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 235.24 E-value: 2.16e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 82 AQRFPDREALVIlhENIRLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVSVNPAYQSS 161
Cdd:PRK03640 12 AFLTPDRTAIEF--EEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSRE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 162 ELEYVLRKVGCKGIVFPKQFKTQQYYDIlkqvcpelekaqpgalkSERLPDLTTVISVDAPLPGTLLLDDIVAaggkeqn 241
Cdd:PRK03640 90 ELLWQLDDAEVKCLITDDDFEAKLIPGI-----------------SVKFAELMNGPKEEAEIQEEFDLDEVAT------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 242 laqlrynqrflscydpinIQFTSGTTGNPKGATLSHHN----IVNNSMLIGQRlkmptktaEELRLVLPSPLYHclgsVG 317
Cdd:PRK03640 146 ------------------IMYTSGTTGKPKGVIQTYGNhwwsAVGSALNLGLT--------EDDCWLAAVPIFH----IS 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 318 G---TMVSMMHGATLLLSsPSFNGKKALEAISREKGTLLYGTPTMFVDILNQPDFSSYDfTSIRGGVIAGSPAPPELIRa 394
Cdd:PRK03640 196 GlsiLMRSVIYGMRVVLV-EKFDAEKINKLLQTGGVTIISVVSTMLQRLLERLGEGTYP-SSFRCMLLGGGPAPKPLLE- 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 395 iinKMNMKELVVV--YGTTENSP--VTFMnfPEDTLEqKAGSVGRimPHTEAQIVNVETGELTNLNVPGELYIRGYCVMQ 470
Cdd:PRK03640 273 ---QCKEKGIPVYqsYGMTETASqiVTLS--PEDALT-KLGSAGK--PLFPCELKIEKDGVVVPPFEEGEIVVKGPNVTK 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 471 GYWGEPQKTFETVgQDKWYRTGDIALMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQEAQVVGVKDERMGE 550
Cdd:PRK03640 345 GYLNREDATRETF-QDGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQ 423
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 551 EICACIrlKSGETTTAEEIKAFCKGKISHFKIPRYIVFVEGYPLTISGKIQKFKLREQME 610
Cdd:PRK03640 424 VPVAFV--VKSGEVTEEELRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHELKQLVE 481
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
99-608 |
6.91e-70 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 234.98 E-value: 6.91e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 99 RLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVSVNPAYQSSELEYVLRKVGCKGIVfp 178
Cdd:PRK12406 11 RRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLI-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 179 kqfktqQYYDILKQVCPELEKAQPgALKSERLPDLTTVISVDA----PLPGTLLLDDIVAAggkEQNLAQLRYNQrflsc 254
Cdd:PRK12406 89 ------AHADLLHGLASALPAGVT-VLSVPTPPEIAAAYRISPalltPPAGAIDWEGWLAQ---QEPYDGPPVPQ----- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 255 ydPINIQFTSGTTGNPKG-----ATLSHhnivnnSMLIGQRLKMPTKTAEELRLVLPSPLYHCLGSVGGtMVSMMHGATL 329
Cdd:PRK12406 154 --PQSMIYTSGTTGHPKGvrraaPTPEQ------AAAAEQMRALIYGLKPGIRALLTGPLYHSAPNAYG-LRAGRLGGVL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 330 LLSsPSFNGKKALEAISREKGTLLYGTPTMFVDILNQPDF--SSYDFTSIRGGVIAGSPAPPELIRAIINKMNMkelVVV 407
Cdd:PRK12406 225 VLQ-PRFDPEELLQLIERHRITHMHMVPTMFIRLLKLPEEvrAKYDVSSLRHVIHAAAPCPADVKRAMIEWWGP---VIY 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 408 --YGTTENSPVTFMNfPEDTLeQKAGSVGRIMPHTEAQIVN-----VETGEltnlnvPGELYIRgycvMQG-----YWGE 475
Cdd:PRK12406 301 eyYGSTESGAVTFAT-SEDAL-SHPGTVGKAAPGAELRFVDedgrpLPQGE------IGEIYSR----IAGnpdftYHNK 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 476 PQKTFEtVGQDKWYRTGDIALMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQEAQVVGVKDERMGEEICAC 555
Cdd:PRK12406 369 PEKRAE-IDRGGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAV 447
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 24418933 556 IRLKSGETTTAEEIKAFCKGKISHFKIPRYIVFVEGYPLTISGKIQKFKLREQ 608
Cdd:PRK12406 448 VEPQPGATLDEADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLRDP 500
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
100-608 |
1.65e-69 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 233.64 E-value: 1.65e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 100 LNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVSVNPAYQSSELEYVLRKVGCKGIVFpk 179
Cdd:PRK08276 12 VTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVLIV-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 180 qfktqqyydilkqvcpelekaqpgalkSERLPDLTTVISVDAPLPGTLLLddiVAAGGKE--QNLAQLRYNQrflSCYDP 257
Cdd:PRK08276 90 ---------------------------SAALADTAAELAAELPAGVPLLL---VVAGPVPgfRSYEEALAAQ---PDTPI 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 258 IN------IQFTSGTTGNPKG--ATLSHHNI-VNNSMLIGQRLKMPTKTAEELRLVlPSPLYHCLGSVGGTMVSMMHGAT 328
Cdd:PRK08276 137 ADetagadMLYSSGTTGRPKGikRPLPGLDPdEAPGMMLALLGFGMYGGPDSVYLS-PAPLYHTAPLRFGMSALALGGTV 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 329 LLLssPSFNGKKALEAISREKGTLLYGTPTMFVDILNQPDF--SSYDFTSIRGGVIAGSPAPPELIRAIINKMNMkelVV 406
Cdd:PRK08276 216 VVM--EKFDAEEALALIERYRVTHSQLVPTMFVRMLKLPEEvrARYDVSSLRVAIHAAAPCPVEVKRAMIDWWGP---II 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 407 V--YGTTENSPVTFMNfPEDTLEqKAGSVGRIMpHTEAQIVN-----VETGEltnlnvPGELYIRgycvMQG----YWGE 475
Cdd:PRK08276 291 HeyYASSEGGGVTVIT-SEDWLA-HPGSVGKAV-LGEVRILDedgneLPPGE------IGTVYFE----MDGypfeYHND 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 476 PQKTFETVGQDKWYRTGDIALMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQEAQVVGVKDERMGEEICAC 555
Cdd:PRK08276 358 PEKTAAARNPHGWVTVGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKAV 437
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 24418933 556 IRLKSGETTT---AEEIKAFCKGKISHFKIPRYIVFVEGYPLTISGKIQKFKLREQ 608
Cdd:PRK08276 438 VQPADGADAGdalAAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLRDR 493
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
82-608 |
1.18e-68 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 232.36 E-value: 1.18e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 82 AQRFPDREALVILHENIrlNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVSVNPAYQSS 161
Cdd:PRK07786 27 ALMQPDAPALRFLGNTT--TWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 162 ELEYVLRKVGCKGIVfpkqfkTQqyyDILKQVCPELEKAQPGalkserlpdLTTVISV-DAPLPGTLLLDDIVAAGGKEQ 240
Cdd:PRK07786 105 EIAFLVSDCGAHVVV------TE---AALAPVATAVRDIVPL---------LSTVVVAgGSSDDSVLGYEDLLAEAGPAH 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 241 NLAQLRYNQrflscydPINIQFTSGTTGNPKGATLSHHNIVNNSM--LIGQRLKmptkTAEELRLVlPSPLYHCLGsVGG 318
Cdd:PRK07786 167 APVDIPNDS-------PALIMYTSGTTGRPKGAVLTHANLTGQAMtcLRTNGAD----INSDVGFV-GVPLFHIAG-IGS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 319 TMVSMMHGA-TLLLSSPSFNGKKALEAISREKGTLLYGTPTMFVDILNQPDFSSYDFtSIRGGVIAGSPAPPELIRAIIN 397
Cdd:PRK07786 234 MLPGLLLGApTVIYPLGAFDPGQLLDVLEAEKVTGIFLVPAQWQAVCAEQQARPRDL-ALRVLSWGAAPASDTLLRQMAA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 398 KMNMKELVVVYGTTENSPVTFMNFPEDTLeQKAGSVGRIMPHTEAQIVN-----VETGELtnlnvpGELYIRGYCVMQGY 472
Cdd:PRK07786 313 TFPEAQILAAFGQTEMSPVTCMLLGEDAI-RKLGSVGKVIPTVAARVVDenmndVPVGEV------GEIVYRAPTLMSGY 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 473 WGEPQKTFETVgQDKWYRTGDIALMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQEAQVVGVKDERMGEEI 552
Cdd:PRK07786 386 WNNPEATAEAF-AGGWFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVP 464
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 24418933 553 CACIRLKSGETT-TAEEIKAFCKGKISHFKIPRYIVFVEGYPLTISGKIQKFKLREQ 608
Cdd:PRK07786 465 VAVAAVRNDDAAlTLEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKVLKTELRER 521
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
73-611 |
1.70e-68 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 232.62 E-value: 1.70e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 73 TVGECLDATAQRFPDREALVILHEniRLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILV 152
Cdd:PRK06178 34 PLTEYLRAWARERPQRPAIIFYGH--VITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 153 SVNPAYQSSELEYVLRKVGCKGIVFPKQFktqqyYDILKQVCPE--LEKAQPGALkSERLPDLTTVisvdaPLPGtLLLD 230
Cdd:PRK06178 112 PVSPLFREHELSYELNDAGAEVLLALDQL-----APVVEQVRAEtsLRHVIVTSL-ADVLPAEPTL-----PLPD-SLRA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 231 DIVAAGGKEQNLAQLRYNQRFLSCY-----DPINIQFTSGTTGNPKGATLSHHNIVNN---SMLIGQRLKMPTktaeelr 302
Cdd:PRK06178 180 PRLAAAGAIDLLPALRACTAPVPLPppaldALAALNYTGGTTGMPKGCEHTQRDMVYTaaaAYAVAVVGGEDS------- 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 303 lVLPS--PLYHCLGSVGGTMVSMMHGATLLLSSpSFNGKKALEAISREKGTLLYGTPTMFVDILNQPDFSSYDFTSIRGg 380
Cdd:PRK06178 253 -VFLSflPEFWIAGENFGLLFPLFSGATLVLLA-RWDAVAFMAAVERYRVTRTVMLVDNAVELMDHPRFAEYDLSSLRQ- 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 381 viagspappelIRAI--INKMNM------KELV------VVYGTTE-NSPVTF-MNFPEDTLEQKAGS--VGRIMPHTEA 442
Cdd:PRK06178 330 -----------VRVVsfVKKLNPdyrqrwRALTgsvlaeAAWGMTEtHTCDTFtAGFQDDDFDLLSQPvfVGLPVPGTEF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 443 QIVNVETGELTNLNVPGELYIRGYCVMQGYWGEPQKTFETVgQDKWYRTGDIALMDEQGFCKIVGRSKDMIIRGGENIYP 522
Cdd:PRK06178 399 KICDFETGELLPLGAEGEIVVRTPSLLKGYWNKPEATAEAL-RDGWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFP 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 523 AELEDFFLKHPQVQEAQVVGVKDERMGEEICACIRLKSGETTTAEEIKAFCKGKISHFKIPRyIVFVEGYPLTISGKIQK 602
Cdd:PRK06178 478 SEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPGADLTAAALQAWCRENMAVYKVPE-IRIVDALPMTATGKVRK 556
|
....*....
gi 24418933 603 FKLREQMEQ 611
Cdd:PRK06178 557 QDLQALAEE 565
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
74-608 |
4.02e-68 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 231.58 E-value: 4.02e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 74 VGECLDATAQRFPDREALVILHENIRlnFAQLkEEVDKAASGLLS--IGLRKGDRLGMWGPNSYAWVLIQLATAQAGIIL 151
Cdd:PRK05677 26 IQAVLKQSCQRFADKPAFSNLGKTLT--YGEL-YKLSGAFAAWLQqhTDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 152 VSVNPAYQSSELEYVLRKVGCKGI------------VFPKqfkTQQYYDILKQVCPELekaqpGALKSERLPDLTTVISV 219
Cdd:PRK05677 103 VNTNPLYTAREMEHQFNDSGAKALvclanmahlaekVLPK---TGVKHVIVTEVADML-----PPLKRLLINAVVKHVKK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 220 DAP---LPGTLLLDDIVAAGgKEQNLAQLRYNQRflscyDPINIQFTSGTTGNPKGATLSHHNIVNNSM----LIGQRLK 292
Cdd:PRK05677 175 MVPayhLPQAVKFNDALAKG-AGQPVTEANPQAD-----DVAVLQYTGGTTGVAKGAMLTHRNLVANMLqcraLMGSNLN 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 293 MPTKTaeelrLVLPSPLYHCLGSVGGTMVSMMHGA-TLLLSSPsfngkKALEAISRE----KGTLLYGTPTMFVDILNQP 367
Cdd:PRK05677 249 EGCEI-----LIAPLPLYHIYAFTFHCMAMMLIGNhNILISNP-----RDLPAMVKElgkwKFSGFVGLNTLFVALCNNE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 368 DFSSYDFTSIR---GGVIAGSPAPPELIRAIINKmnmkELVVVYGTTENSPVTFMNFPEDTleqKAGSVGRIMPHTEAQI 444
Cdd:PRK05677 319 AFRKLDFSALKltlSGGMALQLATAERWKEVTGC----AICEGYGMTETSPVVSVNPSQAI---QVGTIGIPVPSTLCKV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 445 VNVETGELTnLNVPGELYIRGYCVMQGYWGEPQKTFETVGQDKWYRTGDIALMDEQGFCKIVGRSKDMIIRGGENIYPAE 524
Cdd:PRK05677 392 IDDDGNELP-LGEVGELCVKGPQVMKGYWQRPEATDEILDSDGWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNE 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 525 LEDFFLKHPQVQEAQVVGVKDERMGEEICACIRLKSGETTTAEEIKAFCKGKISHFKIPRYIVFVEGYPLTISGKIQKFK 604
Cdd:PRK05677 471 LEDVLAALPGVLQCAAIGVPDEKSGEAIKVFVVVKPGETLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRRE 550
|
....
gi 24418933 605 LREQ 608
Cdd:PRK05677 551 LRDE 554
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
100-542 |
5.78e-68 |
|
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: 228.25 E-value: 5.78e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 100 LNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVsvnPAYQSS---ELEYVLRKVGCKGIV 176
Cdd:cd05907 6 ITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPV---PIYPTSsaeQIAYILNDSEAKALF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 177 fpkqfktqqyydilkqvCPELEkaqpgalkserlpDLTTVIsvdaplpgtlllddivaaggkeqnlaqlrynqrflscyd 256
Cdd:cd05907 83 -----------------VEDPD-------------DLATII--------------------------------------- 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 257 piniqFTSGTTGNPKGATLSHHNIVNNSMLIGQRLkmpTKTAEElRLVLPSPLYHCLGSVGGTMVSMMHGATLLLSSPSf 336
Cdd:cd05907 94 -----YTSGTTGRPKGVMLSHRNILSNALALAERL---PATEGD-RHLSFLPLAHVFERRAGLYVPLLAGARIYFASSA- 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 337 ngKKALEAISREKGTLLYGTPTMFVDILN------QPDFSSYDFTSIRGG-----VIAGSPAPPELIR--AIINkMNMKE 403
Cdd:cd05907 164 --ETLLDDLSEVRPTVFLAVPRVWEKVYAaikvkaVPGLKRKLFDLAVGGrlrfaASGGAPLPAELLHffRALG-IPVYE 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 404 lvvVYGTTENSPVTFMNFPEDtleQKAGSVGRIMPHTEAQIVNVetgeltnlnvpGELYIRGYCVMQGYWGEPQKTFETV 483
Cdd:cd05907 241 ---GYGLTETSAVVTLNPPGD---NRIGTVGKPLPGVEVRIADD-----------GEILVRGPNVMLGYYKNPEATAEAL 303
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 484 GQDKWYRTGDIALMDEQGFCKIVGRSKDMII-RGGENIYPAELEDFFLKHPQVQEAQVVG 542
Cdd:cd05907 304 DADGWLHTGDLGEIDEDGFLHITGRKKDLIItSGGKNISPEPIENALKASPLISQAVVIG 363
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
78-611 |
6.68e-68 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 230.60 E-value: 6.68e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 78 LDATAQRFPDREALVilHENIRLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVSVNPA 157
Cdd:PRK08162 24 LERAAEVYPDRPAVI--HGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 158 YQSSELEYVLRKVGCKGIVFPKQFKtqqyyDILKQVCPELEKAQPgalkserlpdltTVISVD------APLPGTLLLDD 231
Cdd:PRK08162 102 LDAASIAFMLRHGEAKVLIVDTEFA-----EVAREALALLPGPKP------------LVIDVDdpeypgGRFIGALDYEA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 232 IVAAGGKEQnLAQLRYNQrflscYDPINIQFTSGTTGNPKGaTLSHH-----NIVNNSMLIGqrlkMPtKTAEELRLVlp 306
Cdd:PRK08162 165 FLASGDPDF-AWTLPADE-----WDAIALNYTSGTTGNPKG-VVYHHrgaylNALSNILAWG----MP-KHPVYLWTL-- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 307 sPLYHCLG--------SVGGTMVSMMhgatlllsspSFNGKKALEAISREKGTLLYGTPTMFVDILNQPDFSSYDFTSIR 378
Cdd:PRK08162 231 -PMFHCNGwcfpwtvaARAGTNVCLR----------KVDPKLIFDLIREHGVTHYCGAPIVLSALINAPAEWRAGIDHPV 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 379 GGVIAGSPAPPelirAIINKM-NMK-ELVVVYGTTEN-SPVTFMNFPED----TLEQKAGSVGR--IMPHTEAQI--VNV 447
Cdd:PRK08162 300 HAMVAGAAPPA----AVIAKMeEIGfDLTHVYGLTETyGPATVCAWQPEwdalPLDERAQLKARqgVRYPLQEGVtvLDP 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 448 ETGEltnlNVP------GELYIRGYCVMQGYWGEPQKTFETVgQDKWYRTGDIALMDEQGFCKIVGRSKDMIIRGGENIY 521
Cdd:PRK08162 376 DTMQ----PVPadgetiGEIMFRGNIVMKGYLKNPKATEEAF-AGGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENIS 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 522 PAELEDFFLKHPQVQEAQVVGVKDERMGEEICACIRLKSGETTTAEEIKAFCKGKISHFKIPRYIVFVEgYPLTISGKIQ 601
Cdd:PRK08162 451 SIEVEDVLYRHPAVLVAAVVAKPDPKWGEVPCAFVELKDGASATEEEIIAHCREHLAGFKVPKAVVFGE-LPKTSTGKIQ 529
|
570
....*....|
gi 24418933 602 KFKLREQMEQ 611
Cdd:PRK08162 530 KFVLREQAKS 539
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
100-606 |
1.53e-67 |
|
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: 226.06 E-value: 1.53e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 100 LNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVSVNPAYQSSELEYVLRKVGCKGIVfpk 179
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIV--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 180 qfktqqyydilkqvcpelekaqpgalkserlpdlttvisVDAPlpgtlllddivaaggkeqnlaqlrynqrflscyDPIN 259
Cdd:cd05972 78 ---------------------------------------TDAE---------------------------------DPAL 85
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 260 IQFTSGTTGNPKGATLSHhnivnnSMLIGQrlkMPT-KTAEELRlvlPSPLYHCLGSVG-------GTMVSMMHGATLLL 331
Cdd:cd05972 86 IYFTSGTTGLPKGVLHTH------SYPLGH---IPTaAYWLGLR---PDDIHWNIADPGwakgawsSFFGPWLLGATVFV 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 332 -SSPSFNGKKALEAISREKGTLLYGTPTMFvDILNQPDFSSYDFTSIRGGVIAGSPAPPELIRAIINKMNMKeLVVVYGT 410
Cdd:cd05972 154 yEGPRFDAERILELLERYGVTSFCGPPTAY-RMLIKQDLSSYKFSHLRLVVSAGEPLNPEVIEWWRAATGLP-IRDGYGQ 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 411 TEnSPVTFMNFPedTLEQKAGSVGRIMPHTEAQIVNvETGELTNLNVPGELYIRGYCV--MQGYWGEPQKTFETVGQDkW 488
Cdd:cd05972 232 TE-TGLTVGNFP--DMPVKPGSMGRPTPGYDVAIID-DDGRELPPGEEGDIAIKLPPPglFLGYVGDPEKTEASIRGD-Y 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 489 YRTGDIALMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQEAQVVGVKDERMGEEICACIRLKSGETTT--- 565
Cdd:cd05972 307 YLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYEPSeel 386
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 24418933 566 AEEIKAFCKGKISHFKIPRYIVFVEGYPLTISGKIQKFKLR 606
Cdd:cd05972 387 AEELQGHVKKVLAPYKYPREIEFVEELPKTISGKIRRVELR 427
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
102-607 |
4.85e-67 |
|
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: 224.53 E-value: 4.85e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 102 FAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVSVNPAYQSSELEYVLRKVGCKgivfpkqf 181
Cdd:cd05912 4 FAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVK-------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 182 ktqqyydilkqvcpelekaqpgalkserlpdlttvisvdaplpgtllLDDIVAaggkeqnlaqlrynqrflscydpinIQ 261
Cdd:cd05912 76 -----------------------------------------------LDDIAT-------------------------IM 83
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 262 FTSGTTGNPKGATLSHHNIVNNSmlIGQRLKMptKTAEELRLVLPSPLYHclgsVGG---TMVSMMHGATLLLSsPSFNG 338
Cdd:cd05912 84 YTSGTTGKPKGVQQTFGNHWWSA--IGSALNL--GLTEDDNWLCALPLFH----ISGlsiLMRSVIYGMTVYLV-DKFDA 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 339 KKALEAISREKGTLLYGTPTMFVDILNQ-PDFSSYDFtsiRGGVIAGSPAPPELIRaiinKMNMKELVVV--YGTTENSP 415
Cdd:cd05912 155 EQVLHLINSGKVTIISVVPTMLQRLLEIlGEGYPNNL---RCILLGGGPAPKPLLE----QCKEKGIPVYqsYGMTETCS 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 416 --VTFMnfPEDTLEqKAGSVGRIMPHTEAQIVNvetgELTNLNVPGELYIRGYCVMQGYWGEPQKTfETVGQDKWYRTGD 493
Cdd:cd05912 228 qiVTLS--PEDALN-KIGSAGKPLFPVELKIED----DGQPPYEVGEILLKGPNVTKGYLNRPDAT-EESFENGWFKTGD 299
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 494 IALMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQEAQVVGVKDERMGEEICACIrlKSGETTTAEEIKAFC 573
Cdd:cd05912 300 IGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFV--VSERPISEEELIAYC 377
|
490 500 510
....*....|....*....|....*....|....
gi 24418933 574 KGKISHFKIPRYIVFVEGYPLTISGKIQKFKLRE 607
Cdd:cd05912 378 SEKLAKYKVPKKIYFVDELPRTASGKLLRHELKQ 411
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
74-613 |
7.88e-66 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 225.45 E-value: 7.88e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 74 VGECLDATAQRFPDreALVILHENIRLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVS 153
Cdd:PLN02860 9 ICQCLTRLATLRGN--AVVTISGNRRRTGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 154 VNPAYQSSELEYVLRKVGCKGIVFPKQfkTQQYYDilkqvcpelekaqpgALKSERLPDLTTVISVDAP-------LPGT 226
Cdd:PLN02860 87 LNYRWSFEEAKSAMLLVRPVMLVTDET--CSSWYE---------------ELQNDRLPSLMWQVFLESPsssvfifLNSF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 227 LLLDDIVAAGGKEQNLAQlrynqrflsCYDPIN---IQFTSGTTGNPKGATLSHhnivnnSMLIGQRL-KMPTKTAEELR 302
Cdd:PLN02860 150 LTTEMLKQRALGTTELDY---------AWAPDDavlICFTSGTTGRPKGVTISH------SALIVQSLaKIAIVGYGEDD 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 303 LVL-PSPLYHcLGSVGGTMVSMMHGATLLLSsPSFNGKKALEAISREKGTLLYGTPTMFVDIL--NQPDFSSYDFTSIRG 379
Cdd:PLN02860 215 VYLhTAPLCH-IGGLSSALAMLMVGACHVLL-PKFDAKAALQAIKQHNVTSMITVPAMMADLIslTRKSMTWKVFPSVRK 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 380 GVIAGSPAPPELIRAIINKMNMKELVVVYGTTEN-SPVTFMNFPEDTLE------------------QKAGS-VGRIMPH 439
Cdd:PLN02860 293 ILNGGGSLSSRLLPDAKKLFPNAKLFSAYGMTEAcSSLTFMTLHDPTLEspkqtlqtvnqtksssvhQPQGVcVGKPAPH 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 440 TEAQIVNVETGELtnlnvpGELYIRGYCVMQGYWGEPQKTFETVGQDKWYRTGDIALMDEQGFCKIVGRSKDMIIRGGEN 519
Cdd:PLN02860 373 VELKIGLDESSRV------GRILTRGPHVMLGYWGQNSETASVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGEN 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 520 IYPAELEDFFLKHPQVQEAQVVGVKDERMGEEICACIRLKSG--------------ETTTAEEIKAFCKGK-ISHFKIPR 584
Cdd:PLN02860 447 VYPEEVEAVLSQHPGVASVVVVGVPDSRLTEMVVACVRLRDGwiwsdnekenakknLTLSSETLRHHCREKnLSRFKIPK 526
|
570 580 590
....*....|....*....|....*....|
gi 24418933 585 -YIVFVEGYPLTISGKIQKFKLREQMEQHL 613
Cdd:PLN02860 527 lFVQWRKPFPLTTTGKIRRDEVRREVLSHL 556
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
73-609 |
9.24e-66 |
|
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: 223.54 E-value: 9.24e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 73 TVGECLDATAQRFPDREALVILHENIRLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILV 152
Cdd:cd05923 2 TVFEMLRRAASRAPDACAIADPARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 153 SVNPAYQSSELEYVLRKVG-CKGIVFPKQFKTQQyyDILKQVCPELEKAQPGALKSERLPDLttvISVDAPLPGtllldd 231
Cdd:cd05923 82 LINPRLKAAELAELIERGEmTAAVIAVDAQVMDA--IFQSGVRVLALSDLVGLGEPESAGPL---IEDPPREPE------ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 232 ivaaggkeqnlaqlrynqrflscyDPINIQFTSGTTGNPKGATLSHHNIVNNSMLIGQRLKMPTKTAEELRLVLPspLYH 311
Cdd:cd05923 151 ------------------------QPAFVFYTSGTTGLPKGAVIPQRAAESRVLFMSTQAGLRHGRHNVVLGLMP--LYH 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 312 CLGSVGGTMVSMMHGATLLLSSpSFNGKKALEAISREKGTLLYGTPTMFVDILNQPDFSSYDFTSIRGGVIAGSPAPPEL 391
Cdd:cd05923 205 VIGFFAVLVAALALDGTYVVVE-EFDPADALKLIEQERVTSLFATPTHLDALAAAAEFAGLKLSSLRHVTFAGATMPDAV 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 392 IRAIiNKMNMKELVVVYGTTENSPVTFMNFPedtleqKAGSVGRIMPHTEAQIVNVETG--ELTNLNVPGELYIR--GYC 467
Cdd:cd05923 284 LERV-NQHLPGEKVNIYGTTEAMNSLYMRDA------RTGTEMRPGFFSEVRIVRIGGSpdEALANGEEGELIVAaaADA 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 468 VMQGYWGEPQKTFETVgQDKWYRTGDIALMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQEAQVVGVKDER 547
Cdd:cd05923 357 AFTGYLNQPEATAKKL-QDGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADER 435
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24418933 548 MGEEICACIRLKSGeTTTAEEIKAFCK-GKISHFKIPRYIVFVEGYPLTISGKIqkfkLREQM 609
Cdd:cd05923 436 WGQSVTACVVPREG-TLSADELDQFCRaSELADFKRPRRYFFLDELPKNAMNKV----LRRQL 493
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
82-611 |
5.32e-65 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 222.55 E-value: 5.32e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 82 AQRFPDREALVILHENIRLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVSVNPAYQSS 161
Cdd:PLN02246 33 LSEFSDRPCLIDGATGRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 162 ELEYVLRKVGCKGIVfpkqfkTQ-QYYDILKQVCPElekaqpgalkserlpDLTTVISVDAPLPGTLLLDDIVAAggKEQ 240
Cdd:PLN02246 113 EIAKQAKASGAKLII------TQsCYVDKLKGLAED---------------DGVTVVTIDDPPEGCLHFSELTQA--DEN 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 241 NLAQLRYNQRflscyDPINIQFTSGTTGNPKGATLSHHNIVNNsmlIGQR-------LKMptkTAEELRL-VLPspLYH- 311
Cdd:PLN02246 170 ELPEVEISPD-----DVVALPYSSGTTGLPKGVMLTHKGLVTS---VAQQvdgenpnLYF---HSDDVILcVLP--MFHi 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 312 -CLGSVggTMVSMMHGATLLLSsPSFNGKKALEAISREKGTLLYGTPTMFVDILNQPDFSSYDFTSIRGgVIAG-SPAPP 389
Cdd:PLN02246 237 ySLNSV--LLCGLRVGAAILIM-PKFEIGALLELIQRHKVTIAPFVPPIVLAIAKSPVVEKYDLSSIRM-VLSGaAPLGK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 390 ELIRAIINKMNMKELVVVYGTTENSPVTFMN--FPEDTLEQKAGSVGRIMPHTEAQIVNVETGELTNLNVPGELYIRGYC 467
Cdd:PLN02246 313 ELEDAFRAKLPNAVLGQGYGMTEAGPVLAMClaFAKEPFPVKSGSCGTVVRNAELKIVDPETGASLPRNQPGEICIRGPQ 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 468 VMQGYWGEPQKTFETVGQDKWYRTGDIALMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQEAQVVGVKDER 547
Cdd:PLN02246 393 IMKGYLNDPEATANTIDKDGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEV 472
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24418933 548 MGEEICACIRLKSGETTTAEEIKAFCKGKISHFKIPRYIVFVEGYPLTISGKIQKFKLREQMEQ 611
Cdd:PLN02246 473 AGEVPVAFVVRSNGSEITEDEIKQFVAKQVVFYKRIHKVFFVDSIPKAPSGKILRKDLRAKLAA 536
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
256-600 |
6.39e-65 |
|
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: 216.37 E-value: 6.39e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 256 DPINIQFTSGTTGNPKGATLSHHNIVNNSMligqRLKMPTKTAEELRLVLPSPLYHCLGSvgGTMVSMMH--GATLLLSS 333
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLIAANL----QLIHAMGLTEADVYLNMLPLFHIAGL--NLALATFHagGANVVMEK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 334 psFNGKKALEAISREKGTLLYGTPTMFVDILNQPDFSSYDFTSIRggVIAGSPAPpELIRAIINKMNMKeLVVVYGTTEN 413
Cdd:cd17637 75 --FDPAEALELIEEEKVTLMGSFPPILSNLLDAAEKSGVDLSSLR--HVLGLDAP-ETIQRFEETTGAT-FWSLYGQTET 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 414 S-PVTFMNFPEdtleqKAGSVGRIMPHTEAQIVN-----VETGEltnlnvPGELYIRGYCVMQGYWGEPQKTFETVgQDK 487
Cdd:cd17637 149 SgLVTLSPYRE-----RPGSAGRPGPLVRVRIVDdndrpVPAGE------TGEIVVRGPLVFQGYWNLPELTAYTF-RNG 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 488 WYRTGDIALMDEQGFCKIVGRS--KDMIIRGGENIYPAELEDFFLKHPQVQEAQVVGVKDERMGEEICACIRLKSGETTT 565
Cdd:cd17637 217 WHHTGDLGRFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKPGATLT 296
|
330 340 350
....*....|....*....|....*....|....*
gi 24418933 566 AEEIKAFCKGKISHFKIPRYIVFVEGYPLTISGKI 600
Cdd:cd17637 297 ADELIEFVGSRIARYKKPRYVVFVEALPKTADGSI 331
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
79-608 |
2.11e-64 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 220.13 E-value: 2.11e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 79 DATAQRFPDREALVI-LHENIRLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVSVNPA 157
Cdd:PRK07514 7 DALRAAFADRDAPFIeTPDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 158 YQSSELEYVLRKVGCKGIVF-PKQFktqqyydilkqvcPELEK--AQPGAlkserlpdlTTVISVDAPLPGTLLL----- 229
Cdd:PRK07514 87 YTLAELDYFIGDAEPALVVCdPANF-------------AWLSKiaAAAGA---------PHVETLDADGTGSLLEaaaaa 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 230 -DDIVAAGGKEQNLAQLRYnqrflscydpiniqfTSGTTGNPKGATLSHHNIVNNSmligQRLKMPTKTAEELRLVLPSP 308
Cdd:PRK07514 145 pDDFETVPRGADDLAAILY---------------TSGTTGRSKGAMLSHGNLLSNA----LTLVDYWRFTPDDVLIHALP 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 309 LYHCLGSVGGTMVSMMHGATLLLSsPSFNGKKALEAISRekGTLLYGTPTMFVDILNQPDFSSYDFTSIRGgVIAGSpAP 388
Cdd:PRK07514 206 IFHTHGLFVATNVALLAGASMIFL-PKFDPDAVLALMPR--ATVMMGVPTFYTRLLQEPRLTREAAAHMRL-FISGS-AP 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 389 --PELIR--------AIINKmnmkelvvvYGTTEnspvTFMNF--PEDTlEQKAGSVGRIMPHTEAQIVNVETGELTNLN 456
Cdd:PRK07514 281 llAETHRefqertghAILER---------YGMTE----TNMNTsnPYDG-ERRAGTVGFPLPGVSLRVTDPETGAELPPG 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 457 VPGELYIRGYCVMQGYWGEPQKTFETVGQDKWYRTGDIALMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQ 536
Cdd:PRK07514 347 EIGMIEVKGPNVFKGYWRMPEKTAEEFRADGFFITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVV 426
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24418933 537 EAQVVGVKDERMGEEICACIRLKSGETTTAEEIKAFCKGKISHFKIPRYIVFVEGYPLTISGKIQKFKLREQ 608
Cdd:PRK07514 427 ESAVIGVPHPDFGEGVTAVVVPKPGAALDEAAILAALKGRLARFKQPKRVFFVDELPRNTMGKVQKNLLREQ 498
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
78-613 |
1.68e-63 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 218.46 E-value: 1.68e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 78 LDATAQRFPDREALviLHENIRLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVSVNPA 157
Cdd:PRK06164 16 LDAHARARPDAVAL--IDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 158 YQSSELEYVLRKVGCKGIVFPKQFKTQQYYDILKQVCPELekaqpgalkserLPDLTTVISVD---APLPGTLLLDDIVA 234
Cdd:PRK06164 94 YRSHEVAHILGRGRARWLVVWPGFKGIDFAAILAAVPPDA------------LPPLRAIAVVDdaaDATPAPAPGARVQL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 235 AGGKEQnlAQLRYNQRFLSCYDPINIQF-TSGTTGNPKGATLSHHNIVNNSMLIGQRLKMptktAEELRLVLPSPLyhCl 313
Cdd:PRK06164 162 FALPDP--APPAAAGERAADPDAGALLFtTSGTTSGPKLVLHRQATLLRHARAIARAYGY----DPGAVLLAALPF--C- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 314 GSVG-GTMVSMMHGATLLLSSPSFNGKKALEAISREKGTLLYGTPTMFVDILNQPDfSSYDFTSIRG-GVIAGSPAPPEL 391
Cdd:PRK06164 233 GVFGfSTLLGALAGGAPLVCEPVFDAARTARALRRHRVTHTFGNDEMLRRILDTAG-ERADFPSARLfGFASFAPALGEL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 392 I-RAIINKMnmkELVVVYGTTENSPVTFMNFPEDTLEQKAGSVGRIM-PHTEAQIVNVETGELTNLNVPGELYIRGYCVM 469
Cdd:PRK06164 312 AaLARARGV---PLTGLYGSSEVQALVALQPATDPVSVRIEGGGRPAsPEARVRARDPQDGALLPDGESGEIEIRAPSLM 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 470 QGYWGEPQKTFETVGQDKWYRTGDIALMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQEAQVVGVkdERMG 549
Cdd:PRK06164 389 RGYLDNPDATARALTDDGYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGA--TRDG 466
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24418933 550 EEIC-ACIRLKSGETTTAEEIKAFCKGKISHFKIPRYIVFVEGYPLTISG---KIQKFKLREQMEQHL 613
Cdd:PRK06164 467 KTVPvAFVIPTDGASPDEAGLMAACREALAGFKVPARVQVVEAFPVTESAngaKIQKHRLREMAQARL 534
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
102-605 |
3.51e-63 |
|
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: 215.01 E-value: 3.51e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 102 FAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVSVNPAYQSSELEYVLRKVgckgivfPKQF 181
Cdd:TIGR01923 2 WQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDL-------DVQL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 182 ktqqyydILKQVCPELEkaqpgalkserlpDLTTVIsvdaplpgtllLDDIVAAGGKEQNLAQlrynqrFLSCYDPINIQ 261
Cdd:TIGR01923 75 -------LLTDSLLEEK-------------DFQADS-----------LDRIEAAGRYETSLSA------SFNMDQIATLM 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 262 FTSGTTGNPKGATLSHHNIVNNSMliGQRLKMPTKTAEELRLVLPspLYHcLGSVGGTMVSMMHGATLLLSSPsFNgkKA 341
Cdd:TIGR01923 118 FTSGTTGKPKAVPHTFRNHYASAV--GSKENLGFTEDDNWLLSLP--LYH-ISGLSILFRWLIEGATLRIVDK-FN--QL 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 342 LEAISREKGTLLYGTPTMFVDILNQpDFSSYDFTSIRGGviaGSPAPPELIRAIINKMnmKELVVVYGTTENSPvTFMNF 421
Cdd:TIGR01923 190 LEMIANERVTHISLVPTQLNRLLDE-GGHNENLRKILLG---GSAIPAPLIEEAQQYG--LPIYLSYGMTETCS-QVTTA 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 422 PEDTLEQKaGSVGRIMPHTEAQIvnvetgELTNLNVPGELYIRGYCVMQGYWGEPQKTfETVGQDKWYRTGDIALMDEQG 501
Cdd:TIGR01923 263 TPEMLHAR-PDVGRPLAGREIKI------KVDNKEGHGEIMVKGANLMKGYLYQGELT-PAFEQQGWFNTGDIGELDGEG 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 502 FCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQEAQVVGVKDERMGEEICACIRLKSgeTTTAEEIKAFCKGKISHFK 581
Cdd:TIGR01923 335 FLYVLGRRDDLIISGGENIYPEEIETVLYQHPGIQEAVVVPKPDAEWGQVPVAYIVSES--DISQAKLIAYLTEKLAKYK 412
|
490 500
....*....|....*....|....
gi 24418933 582 IPRYIVFVEGYPLTISGKIQKFKL 605
Cdd:TIGR01923 413 VPIAFEKLDELPYNASGKILRNQL 436
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
82-614 |
1.25e-62 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 216.38 E-value: 1.25e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 82 AQRFPDREALVILHENIRLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVSVNPAYQSS 161
Cdd:PLN02330 38 AELYADKVAFVEAVTGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALES 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 162 ELEYVLRKVGCKGIVfpkqfktqqyydilkqvcpeLEKAQPGALKSERLPdltTVISVDAPLPGTLLLDDIVAAGGKEQN 241
Cdd:PLN02330 118 EIKKQAEAAGAKLIV--------------------TNDTNYGKVKGLGLP---VIVLGEEKIEGAVNWKELLEAADRAGD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 242 LAQlryNQRFLSCyDPINIQFTSGTTGNPKGATLSHHNIVNN--SMLIGQRLKMPTKTAEeLRLVlpsPLYHCLGSVGGT 319
Cdd:PLN02330 175 TSD---NEEILQT-DLCALPFSSGTTGISKGVMLTHRNLVANlcSSLFSVGPEMIGQVVT-LGLI---PFFHIYGITGIC 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 320 MVSMMHGATLLLSSpSFNGKKALEAISREKGTLLYGTPTMFVDILNQPDFSSYDFTSI--RGGVIAGSPAPPELIRAIIN 397
Cdd:PLN02330 247 CATLRNKGKVVVMS-RFELRTFLNALITQEVSFAPIVPPIILNLVKNPIVEEFDLSKLklQAIMTAAAPLAPELLTAFEA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 398 KMNMKELVVVYGTTENSPVTFMNFPEDTLE--QKAGSVGRIMPHTEAQIVNVETGELTNLNVPGELYIRGYCVMQGYWGE 475
Cdd:PLN02330 326 KFPGVQVQEAYGLTEHSCITLTHGDPEKGHgiAKKNSVGFILPNLEVKFIDPDTGRSLPKNTPGELCVRSQCVMQGYYNN 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 476 PQKTFETVGQDKWYRTGDIALMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQEAQVVGVKDERMGEEICAC 555
Cdd:PLN02330 406 KEETDRTIDEDGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAAC 485
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 24418933 556 IRLKSGETTTAEEIKAFCKGKISHFKIPRYIVFVEGYPLTISGKIQKFKLREQMEQHLK 614
Cdd:PLN02330 486 VVINPKAKESEEDILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLKEKMLSINK 544
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
82-608 |
1.44e-62 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 215.33 E-value: 1.44e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 82 AQRFPDREALVILHENIRLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVSVNPAYQSS 161
Cdd:PRK13391 7 AQTTPDKPAVIMASTGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 162 ELEYVLRKVGCKGIVfpkqfKTQQYYDilkqVCPELEKAQPGALksERLpdlttVISVDAPLPGTLLLDDIVAA----GG 237
Cdd:PRK13391 87 EAAYIVDDSGARALI-----TSAAKLD----VARALLKQCPGVR--HRL-----VLDGDGELEGFVGYAEAVAGlpatPI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 238 KEQNLAQLrynqrflscydpinIQFTSGTTGNPKG--ATLSHHNIVNNSMLIGQrLKMPTKTAEELRLVLPSPLYHC--- 312
Cdd:PRK13391 151 ADESLGTD--------------MLYSSGTTGRPKGikRPLPEQPPDTPLPLTAF-LQRLWGFRSDMVYLSPAPLYHSapq 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 313 -----LGSVGGTMVSMMHgatlllsspsFNGKKALEAISREKGTLLYGTPTMFVDILNQPD--FSSYDFTSIRGGVIAGS 385
Cdd:PRK13391 216 ravmlVIRLGGTVIVMEH----------FDAEQYLALIEEYGVTHTQLVPTMFSRMLKLPEevRDKYDLSSLEVAIHAAA 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 386 PAPPELIRAIINKMNmkelVVV---YGTTENSPVTFMNfPEDTLEQKaGSVGRIM---PHteaqIVNvETGELTNLNVPG 459
Cdd:PRK13391 286 PCPPQVKEQMIDWWG----PIIheyYAATEGLGFTACD-SEEWLAHP-GTVGRAMfgdLH----ILD-DDGAELPPGEPG 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 460 ELYIRGYCVMQgYWGEPQKTFETVGQDK-WYRTGDIALMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQEA 538
Cdd:PRK13391 355 TIWFEGGRPFE-YLNDPAKTAEARHPDGtWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADA 433
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24418933 539 QVVGVKDERMGEEICACIRLKSGETTT---AEEIKAFCKGKISHFKIPRYIVFVEGYPLTISGKIQKFKLREQ 608
Cdd:PRK13391 434 AVFGVPNEDLGEEVKAVVQPVDGVDPGpalAAELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLLRDR 506
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
93-606 |
2.69e-62 |
|
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.
Pssm-ID: 341243 [Multi-domain] Cd Length: 436 Bit Score: 212.71 E-value: 2.69e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 93 ILHENIRLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVSVNPAYQSSELEYVLRKVGC 172
Cdd:cd05919 4 FYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 173 KGIVfpkqfktqqyydilkqvcpelekaqpgalkserlpdlttvisVDAplpgtlllDDIvaaggkeqnlaqlrynqrfl 252
Cdd:cd05919 84 RLVV------------------------------------------TSA--------DDI-------------------- 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 253 sCYdpinIQFTSGTTGNPKGATLSHhnivNNSMLIGQRLKMPT-KTAEELRLVLPSPLYHCLGSVGGTMVSMMHGATLLL 331
Cdd:cd05919 94 -AY----LLYSSGTTGPPKGVMHAH----RDPLLFADAMAREAlGLTPGDRVFSSAKMFFGYGLGNSLWFPLAVGASAVL 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 332 SSPSFNGKKALEAISREKGTLLYGTPTMFVDILNQPDFSSYDFTSIRGGVIAGSPAPPELIRAIINKMNMkELVVVYGTT 411
Cdd:cd05919 165 NPGWPTAERVLATLARFRPTVLYGVPTFYANLLDSCAGSPDALRSLRLCVSAGEALPRGLGERWMEHFGG-PILDGIGAT 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 412 ENSPVTFMNFPEDTleqKAGSVGRIMPHTEAQIVNvETGELTNLNVPGELYIRGYCVMQGYWGEPQKTFETVgQDKWYRT 491
Cdd:cd05919 244 EVGHIFLSNRPGAW---RLGSTGRPVPGYEIRLVD-EEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATF-NGGWYRT 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 492 GDIALMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQEAQVVGVKDERMGEEICACIRLKSGETTT---AEE 568
Cdd:cd05919 319 GDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPQeslARD 398
|
490 500 510
....*....|....*....|....*....|....*...
gi 24418933 569 IKAFCKGKISHFKIPRYIVFVEGYPLTISGKIQKFKLR 606
Cdd:cd05919 399 IHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKLR 436
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
78-608 |
1.63e-61 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 213.47 E-value: 1.63e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 78 LDATAQRFPDREALVIlhENIRLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVSVNPA 157
Cdd:PRK06155 27 LARQAERYPDRPLLVF--GGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 158 YQSSELEYVLRKVGCKGIVFPKQFktqqyydilkqvCPELEKAQPGALKSER--LPDLTTVISVDA-----PLPGtllLD 230
Cdd:PRK06155 105 LRGPQLEHILRNSGARLLVVEAAL------------LAALEAADPGDLPLPAvwLLDAPASVSVPAgwstaPLPP---LD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 231 DIVAAGGkeqnlaqlrynqrfLSCYDPINIQFTSGTTGNPKGATLSHhnivnnsmliGQRLKMPTKTAEELRLVLPSPLY 310
Cdd:PRK06155 170 APAPAAA--------------VQPGDTAAILYTSGTTGPSKGVCCPH----------AQFYWWGRNSAEDLEIGADDVLY 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 311 HCL-----GSVGGTMVSMMHGATLLLSsPSFNGKKALEAISREKGTLLYGTPTMFVDILNQPDFSSYDFTSIRggvIAGS 385
Cdd:PRK06155 226 TTLplfhtNALNAFFQALLAGATYVLE-PRFSASGFWPAVRRHGATVTYLLGAMVSILLSQPARESDRAHRVR---VALG 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 386 PA-PPELIRAIINKMNMkELVVVYGTTENspvtfmNFP--EDTLEQKAGSVGRIMPHTEAQIVNVETGELTNlNVPGELY 462
Cdd:PRK06155 302 PGvPAALHAAFRERFGV-DLLDGYGSTET------NFViaVTHGSQRPGSMGRLAPGFEARVVDEHDQELPD-GEPGELL 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 463 IRG---YCVMQGYWGEPQKTFETvGQDKWYRTGDIALMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQEAQ 539
Cdd:PRK06155 374 LRAdepFAFATGYFGMPEKTVEA-WRNLWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAA 452
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24418933 540 VVGVKDERMGEEICACIRLKSGETTTAEEIKAFCKGKISHFKIPRYIVFVEGYPLTISGKIQKFKLREQ 608
Cdd:PRK06155 453 VFPVPSELGEDEVMAAVVLRDGTALEPVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVLREQ 521
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
79-606 |
2.87e-61 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 211.85 E-value: 2.87e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 79 DATAQRFPDREALVilHENI-----RLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVS 153
Cdd:PRK08008 14 DDLADVYGHKTALI--FESSggvvrRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 154 VNPAYQSSELEYVLRKVGCKGIVFPKQF-----KTQQYYDI-LKQVCpelekaqpgaLKSERLPDLTTVISVDaplpgTL 227
Cdd:PRK08008 92 INARLLREESAWILQNSQASLLVTSAQFypmyrQIQQEDATpLRHIC----------LTRVALPADDGVSSFT-----QL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 228 llddivaaggKEQNLAQLRYnQRFLSCYDPINIQFTSGTTGNPKGATLSHHNIvnnsMLIGQRLKMPTKTAEELRLVLPS 307
Cdd:PRK08008 157 ----------KAQQPATLCY-APPLSTDDTAEILFTSGTTSRPKGVVITHYNL----RFAGYYSAWQCALRDDDVYLTVM 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 308 PLYHCLGSVGGTMVSMMHGATLLL----SSPSFNGKkaleaISREKGTLLYGTPTMFVDILNQPdfssydftsirggvia 383
Cdd:PRK08008 222 PAFHIDCQCTAAMAAFSAGATFVLlekySARAFWGQ-----VCKYRATITECIPMMIRTLMVQP---------------- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 384 gsPAPPE---LIRAIINKMNMKE-------------LVVVYGTTENSPVTFMNFPEDtlEQKAGSVGRIMPHTEAQIVNV 447
Cdd:PRK08008 281 --PSANDrqhCLREVMFYLNLSDqekdafeerfgvrLLTSYGMTETIVGIIGDRPGD--KRRWPSIGRPGFCYEAEIRDD 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 448 ETGELTNlNVPGELYIRGY---CVMQGYWGEPQKTFETVGQDKWYRTGDIALMDEQGFCKIVGRSKDMIIRGGENIYPAE 524
Cdd:PRK08008 357 HNRPLPA-GEIGEICIKGVpgkTIFKEYYLDPKATAKVLEADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVE 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 525 LEDFFLKHPQVQEAQVVGVKDERMGEEICACIRLKSGETTTAEEIKAFCKGKISHFKIPRYIVFVEGYPLTISGKIQKFK 604
Cdd:PRK08008 436 LENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKN 515
|
..
gi 24418933 605 LR 606
Cdd:PRK08008 516 LK 517
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
256-600 |
4.97e-61 |
|
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: 205.72 E-value: 4.97e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 256 DPINIQFTSGTTGNPKGATLSHHNIVNnSMLIGQRLkMPTKTAEelRLVLPSPLYHCLgSVGGTMVSMMHGATLLLSSpS 335
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRSERSWIE-SFVCNEDL-FNISGED--AILAPGPLSHSL-FLYGAISALYLGGTFIGQR-K 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 336 FNGKKALEAISREKGTLLYGTPTMfVDILNQPDFSSYDFTSIRGGviaGSPAPPELIRAIINKMNMKELVVVYGTTENSP 415
Cdd:cd17633 75 FNPKSWIRKINQYNATVIYLVPTM-LQALARTLEPESKIKSIFSS---GQKLFESTKKKLKNIFPKANLIEFYGTSELSF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 416 VTFmNFPEDtlEQKAGSVGRIMPHTEAQIVNVETGELTNLNVPGELYIRGYCVMQGYwgepqktfetvGQDKWYRTGDIA 495
Cdd:cd17633 151 ITY-NFNQE--SRPPNSVGRPFPNVEIEIRNADGGEIGKIFVKSEMVFSGYVRGGFS-----------NPDGWMSVGDIG 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 496 LMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQEAQVVGVKDERMGEEICACIrlkSGETTTAEEIKAFCKG 575
Cdd:cd17633 217 YVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALY---SGDKLTYKQLKRFLKQ 293
|
330 340
....*....|....*....|....*
gi 24418933 576 KISHFKIPRYIVFVEGYPLTISGKI 600
Cdd:cd17633 294 KLSRYEIPKKIIFVDSLPYTSSGKI 318
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
113-600 |
1.31e-60 |
|
C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.
Pssm-ID: 341235 [Multi-domain] Cd Length: 490 Bit Score: 209.49 E-value: 1.31e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 113 ASGLLSIGLRK----GDRLGMWGPNSYAWVLIQLATAQAGIILVSVNPAYQSSELEYVLRKVGCKGIVFPKQFktqqyyd 188
Cdd:cd05909 16 GAIALARKLAKmtkeGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVLTSKQF------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 189 ilkqvcpeLEKaqpgaLKSERLPDLTTVISVdaplpgtLLLDDI-----------VAAGGKEQNLAQLRynQRFLSCY-- 255
Cdd:cd05909 89 --------IEK-----LKLHHLFDVEYDARI-------VYLEDLrakiskadkckAFLAGKFPPKWLLR--IFGVAPVqp 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 256 -DPINIQFTSGTTGNPKGATLSHHNIVNNSMLIgqRLKMPTKTAEELRLVLPspLYHCLGSVGGTMVSMMHGATLLLSSP 334
Cdd:cd05909 147 dDPAVILFTSGSEGLPKGVVLSHKNLLANVEQI--TAIFDPNPEDVVFGALP--FFHSFGLTGCLWLPLLSGIKVVFHPN 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 335 SFNGKKALEAISREKGTLLYGTPTMFVDILNQPdfSSYDFTSIRGgVIAGSPAPPELIRAIINKMNMKELVVVYGTTENS 414
Cdd:cd05909 223 PLDYKKIPELIYDKKATILLGTPTFLRGYARAA--HPEDFSSLRL-VVAGAEKLKDTLRQEFQEKFGIRILEGYGTTECS 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 415 PVTFMNFPEdtLEQKAGSVGRIMPHTEAQIVNVETGELTNLNVPGELYIRGYCVMQGYWGEPQKTfETVGQDKWYRTGDI 494
Cdd:cd05909 300 PVISVNTPQ--SPNKEGTVGRPLPGMEVKIVSVETHEEVPIGEGGLLLVRGPNVMLGYLNEPELT-SFAFGDGWYDTGDI 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 495 ALMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKH-PQVQEAQVVGVKDERMGEEICACIrlkSGETTTAEEIKAFC 573
Cdd:cd05909 377 GKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVPDGRKGEKIVLLT---TTTDTDPSSLNDIL 453
|
490 500
....*....|....*....|....*...
gi 24418933 574 K-GKISHFKIPRYIVFVEGYPLTISGKI 600
Cdd:cd05909 454 KnAGISNLAKPSYIHQVEEIPLLGTGKP 481
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
73-599 |
3.54e-60 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 209.36 E-value: 3.54e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 73 TVGECLDATAQRFPDREALVilHENIRLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILV 152
Cdd:PRK07798 4 NIADLFEAVADAVPDRVALV--CGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 153 SVNPAYQSSELEYVLRKVGCKGIVFPKQFktqqyydilkqvCPELEKAQPgalkseRLPDLTTVISVD-----APLPGTL 227
Cdd:PRK07798 82 NVNYRYVEDELRYLLDDSDAVALVYEREF------------APRVAEVLP------RLPKLRTLVVVEdgsgnDLLPGAV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 228 LLDDIVAAGGKEQNLAQlrynqrflSCYDPINIQFTSGTTGNPKGATLSHHNIVNNSMliGQRLKM---PTKTAEEL--- 301
Cdd:PRK07798 144 DYEDALAAGSPERDFGE--------RSPDDLYLLYTGGTTGMPKGVMWRQEDIFRVLL--GGRDFAtgePIEDEEELakr 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 302 --------RLVLPsPLYHCLGSVGGTMVSMMHGATLLLSSPSFNGKKALEAISREKGTLL------YGTPtmFVDILNQP 367
Cdd:PRK07798 214 aaagpgmrRFPAP-PLMHGAGQWAAFAALFSGQTVVLLPDVRFDADEVWRTIEREKVNVItivgdaMARP--LLDALEAR 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 368 DfsSYDFTSIRggVIAGSPAP--PELIRAIINKMNMKELVVVYGTTENSpvtFMNFPEDTLEQKAGSVGRIMPHTEAQIV 445
Cdd:PRK07798 291 G--PYDLSSLF--AIASGGALfsPSVKEALLELLPNVVLTDSIGSSETG---FGGSGTVAKGAVHTGGPRFTIGPRTVVL 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 446 NVETGELTnlnvPGE-----LYIRGYcVMQGYWGEPQK---TFETVGQDKWYRTGDIALMDEQGFCKIVGRSKDMIIRGG 517
Cdd:PRK07798 364 DEDGNPVE----PGSgeigwIARRGH-IPLGYYKDPEKtaeTFPTIDGVRYAIPGDRARVEADGTITLLGRGSVCINTGG 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 518 ENIYPAELEDFFLKHPQVQEAQVVGVKDERMGEEICACIRLKSGETTTAEEIKAFCKGKISHFKIPRYIVFVEGYPLTIS 597
Cdd:PRK07798 439 EKVFPEEVEEALKAHPDVADALVVGVPDERWGQEVVAVVQLREGARPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPA 518
|
..
gi 24418933 598 GK 599
Cdd:PRK07798 519 GK 520
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
80-606 |
5.42e-59 |
|
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: 203.86 E-value: 5.42e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 80 ATAQRFPDREalvilhenirLNFAQLKEEVDKAASGLLS-IGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVSVNPAY 158
Cdd:cd05958 1 RTCLRSPERE----------WTYRDLLALANRIANVLVGeLGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 159 QSSELEYVLRKVgckgivfpkqfktqqyyDILKQVCPElekaqpgalkserlpDLTTVisvdaplpgtlllDDIVAaggk 238
Cdd:cd05958 71 RPKELAYILDKA-----------------RITVALCAH---------------ALTAS-------------DDICI---- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 239 eqnlaqlrynqrflscydpinIQFTSGTTGNPKGATLSHHNIVNNSMLIGQRLKMPTktaEELRLVLPSPLYHCLGsVGG 318
Cdd:cd05958 102 ---------------------LAFTSGTTGAPKATMHFHRDPLASADRYAVNVLRLR---EDDRFVGSPPLAFTFG-LGG 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 319 TMVSMMH-GATLLL---SSPSfngkKALEAISREKGTLLYGTPTMFVDILNQPDFSSYDFTSIRGGVIAGSPAPPELIRA 394
Cdd:cd05958 157 VLLFPFGvGASGVLleeATPD----LLLSAIARYKPTVLFTAPTAYRAMLAHPDAAGPDLSSLRKCVSAGEALPAALHRA 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 395 IINKMNMkELVVVYGTTENSPVTFMNFPEDTleqKAGSVGRIMPHTEAQIVN-----VETGELTNLNVPGElyirgycvm 469
Cdd:cd05958 233 WKEATGI-PIIDGIGSTEMFHIFISARPGDA---RPGATGKPVPGYEAKVVDdegnpVPDGTIGRLAVRGP--------- 299
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 470 QGYWGEPQKTFETVGQDKWYRTGDIALMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQEAQVVGVKDERMG 549
Cdd:cd05958 300 TGCRYLADKRQRTYVQGGWNITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRG 379
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 550 EEICACIRLKSGETTT---AEEIKAFCKGKISHFKIPRYIVFVEGYPLTISGKIQKFKLR 606
Cdd:cd05958 380 VVVKAFVVLRPGVIPGpvlARELQDHAKAHIAPYKYPRAIEFVTELPRTATGKLQRFALR 439
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
86-600 |
2.12e-58 |
|
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: 202.37 E-value: 2.12e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 86 PDREALVilHENIRLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVSVNPAYQSSELEY 165
Cdd:cd05930 1 PDAVAVV--DGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 166 VLRKVGCKgivfpkqfktqqyydilkqvcpelekaqpgalkserlpdlttvisvdaplpgtLLLDDivaaggkEQNLAql 245
Cdd:cd05930 79 ILEDSGAK-----------------------------------------------------LVLTD-------PDDLA-- 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 246 rynqrflscYdpinIQFTSGTTGNPKGATLSHHNIVNnsMLIGQRLKMPtKTAEELRLVLPSPLYHclGSVGGTMVSMMH 325
Cdd:cd05930 97 ---------Y----VIYTSGSTGKPKGVMVEHRGLVN--LLLWMQEAYP-LTPGDRVLQFTSFSFD--VSVWEIFGALLA 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 326 GATLLLSSPS--FNGKKALEAISREKGTLLYGTPTMFVDILNQPDFSsyDFTSIRGGVIAGSPAPPELIRAIINKMNMKE 403
Cdd:cd05930 159 GATLVVLPEEvrKDPEALADLLAEEGITVLHLTPSLLRLLLQELELA--ALPSLRLVLVGGEALPPDLVRRWRELLPGAR 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 404 LVVVYGTTENS-PVTFMNFPEDTLEQKAGSVGRIMPHTEAQIVNvETGELTNLNVPGELYIRGYCVMQGYWGEPQKTFET 482
Cdd:cd05930 237 LVNLYGPTEATvDATYYRVPPDDEEDGRVPIGRPIPNTRVYVLD-ENLRPVPPGVPGELYIGGAGLARGYLNRPELTAER 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 483 VGQDKW------YRTGDIALMDEQGFCKIVGRSKDMI-IRGgeniY---PAELEDFFLKHPQVQEAQVVGVKDERMGEEI 552
Cdd:cd05930 316 FVPNPFgpgermYRTGDLVRWLPDGNLEFLGRIDDQVkIRG----YrieLGEIEAALLAHPGVREAAVVAREDGDGEKRL 391
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 24418933 553 CACIRLKSGETTTAEEIKAFCKGKISHFKIPRYIVFVEGYPLTISGKI 600
Cdd:cd05930 392 VAYVVPDEGGELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKV 439
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
260-607 |
1.07e-56 |
|
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: 198.37 E-value: 1.07e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 260 IQFTSGTTGNPKGATLSH-HNIVNNSMLIGQRLKMPTktAEELRLVLPSPLYHCLGSVGgTMVSMMHGATLLLSsPSFNG 338
Cdd:cd05929 130 MLYSGGTTGRPKGIKRGLpGGPPDNDTLMAAALGFGP--GADSVYLSPAPLYHAAPFRW-SMTALFMGGTLVLM-EKFDP 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 339 KKALEAISREKGTLLYGTPTMFVDILNQPD--FSSYDFTSIRGGVIAGSPAPPELIRAIINKMNMKeLVVVYGTTENSPV 416
Cdd:cd05929 206 EEFLRLIERYRVTFAQFVPTMFVRLLKLPEavRNAYDLSSLKRVIHAAAPCPPWVKEQWIDWGGPI-IWEYYGGTEGQGL 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 417 TFMNfPEDTLEQKaGSVGRIMpHTEAQIVNvETGELTNLNVPGELYIRGYCVMQgYWGEPQKTFETVGQDKWYRTGDIAL 496
Cdd:cd05929 285 TIIN-GEEWLTHP-GSVGRAV-LGKVHILD-EDGNEVPPGEIGEVYFANGPGFE-YTNDPEKTAAARNEGGWSTLGDVGY 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 497 MDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQEAQVVGVKDERMGEEICACIRLKSGE---TTTAEEIKAFC 573
Cdd:cd05929 360 LDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVQPAPGAdagTALAEELIAFL 439
|
330 340 350
....*....|....*....|....*....|....
gi 24418933 574 KGKISHFKIPRYIVFVEGYPLTISGKIQKFKLRE 607
Cdd:cd05929 440 RDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLRD 473
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
263-606 |
1.20e-56 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 195.01 E-value: 1.20e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 263 TSGTTGNPKGATLSHHNIVNNSMlIGQRLKMPTKTAEelrLVLPSPLYHCLGSVGGTMVSMMHGATLLLSSPS-FNGKKA 341
Cdd:cd05944 10 TGGTTGTPKLAQHTHSNEVYNAW-MLALNSLFDPDDV---LLCGLPLFHVNGSVVTLLTPLASGAHVVLAGPAgYRNPGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 342 LEA----ISREKGTLLYGTPTMFVDILNQPDfsSYDFTSIRGGVIAGSPAPPELIRAIINKMNMKeLVVVYGTTENSPVT 417
Cdd:cd05944 86 FDNfwklVERYRITSLSTVPTVYAALLQVPV--NADISSLRFAMSGAAPLPVELRARFEDATGLP-VVEGYGLTEATCLV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 418 FMNFPEDtlEQKAGSVGRIMPHTEAQIV--NVETGELTNLNVP--GELYIRGYCVMQGY-WGEPQKtfETVGQDKWYRTG 492
Cdd:cd05944 163 AVNPPDG--PKRPGSVGLRLPYARVRIKvlDGVGRLLRDCAPDevGEICVAGPGVFGGYlYTEGNK--NAFVADGWLNTG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 493 DIALMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQEAQVVGVKDERMGEEICACIRLKSGETTTAEEIKAF 572
Cdd:cd05944 239 DLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPGAVVEEEELLAW 318
|
330 340 350
....*....|....*....|....*....|....*
gi 24418933 573 CKGKI-SHFKIPRYIVFVEGYPLTISGKIQKFKLR 606
Cdd:cd05944 319 ARDHVpERAAVPKHIEVLEELPVTAVGKVFKPALR 353
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
80-607 |
1.70e-56 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 199.60 E-value: 1.70e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 80 ATAQRFPDREALVilHENIRLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVSVNPAYQ 159
Cdd:PRK13382 51 IAAQRCPDRPGLI--DELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 160 SSELEYVLRKVGCKGIVFPKQFktqqyydilkqvCPELEKA---QPGALKSERLPDLttvisvdaplPGTLLLDDIVAAG 236
Cdd:PRK13382 129 GPALAEVVTREGVDTVIYDEEF------------SATVDRAladCPQATRIVAWTDE----------DHDLTVEVLIAAH 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 237 GKEQNLAQLRYNQRFLscydpiniqFTSGTTGNPKGATLSHHNIVNNSMLIGQRLKMptkTAEELrLVLPSPLYHCLGSV 316
Cdd:PRK13382 187 AGQRPEPTGRKGRVIL---------LTSGTTGTPKGARRSGPGGIGTLKAILDRTPW---RAEEP-TVIVAPMFHAWGFS 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 317 GGTMVSMMhgATLLLSSPSFNGKKALEAISREKGTLLYGTPTMFVDILNQPD--FSSYDFTSIRGGVIAGSPAPPELIRA 394
Cdd:PRK13382 254 QLVLAASL--ACTIVTRRRFDPEATLDLIDRHRATGLAVVPVMFDRIMDLPAevRNRYSGRSLRFAAASGSRMRPDVVIA 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 395 IINKMNmKELVVVYGTTENSPVTFMNfPEDtLEQKAGSVGRIMPHTEAQIVNVETGELTNLNVpGELYIRGYCVMQGYWG 474
Cdd:PRK13382 332 FMDQFG-DVIYNNYNATEAGMIATAT-PAD-LRAAPDTAGRPAEGTEIRILDQDFREVPTGEV-GTIFVRNDTQFDGYTS 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 475 EPQKTFetvgQDKWYRTGDIALMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQEAQVVGVKDERMGEEICA 554
Cdd:PRK13382 408 GSTKDF----HDGFMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAA 483
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 24418933 555 CIRLKSGETTTAEEIKAFCKGKISHFKIPRYIVFVEGYPLTISGKIQKFKLRE 607
Cdd:PRK13382 484 FVVLKPGASATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQA 536
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
256-607 |
7.88e-55 |
|
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: 189.08 E-value: 7.88e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 256 DPINIQFTSGTTGNPKGATLSHHNIVNNSMLIGQRLKMptkTAEELRLVLpSPLYHclgsVGGTMV---SMMHGATLLLS 332
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGF---GGGDSWLLS-LPLYH----VGGLAIlvrSLLAGAELVLL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 333 SPsfngkKALEAISREKGTLLYG--TPTMFVDILnQPDFSSYDFTSIRGGVIAGSPAPPELIRAIINKMnmKELVVVYGT 410
Cdd:cd17630 73 ER-----NQALAEDLAPPGVTHVslVPTQLQRLL-DSGQGPAALKSLRAVLLGGAPIPPELLERAADRG--IPLYTTYGM 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 411 TENSPVTFMNFPEDTleqKAGSVGRIMPHTEAQIVNvetgeltnlnvPGELYIRGYCVMQGYW--GEPQKTFEtvgqDKW 488
Cdd:cd17630 145 TETASQVATKRPDGF---GRGGVGVLLPGRELRIVE-----------DGEIWVGGASLAMGYLrgQLVPEFNE----DGW 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 489 YRTGDIALMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQEAQVVGVKDERMGEEICACIRlkSGETTTAEE 568
Cdd:cd17630 207 FTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIV--GRGPADPAE 284
|
330 340 350
....*....|....*....|....*....|....*....
gi 24418933 569 IKAFCKGKISHFKIPRYIVFVEGYPLTISGKIQKFKLRE 607
Cdd:cd17630 285 LRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRA 323
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
73-602 |
1.45e-54 |
|
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: 192.93 E-value: 1.45e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 73 TVGECLDATAQRFPDREALVilHENIRLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILV 152
Cdd:cd05920 16 PLGDLLARSAARHPDRIAVV--DGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 153 SVNPAYQSSELEYVLRKVGCKGIVFPKQFktqqyydilkqvcpelekaqpgalkserlpdlttvisvdaplpgtlllddi 232
Cdd:cd05920 94 LALPSHRRSELSAFCAHAEAVAYIVPDRH--------------------------------------------------- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 233 vaAGGKEQNLAQlrynQRFLSCYDPINIQFTSGTTGNPKGATLSHHNIVNNSmligqrlkmpTKTAEELRL--------V 304
Cdd:cd05920 123 --AGFDHRALAR----ELAESIPEVALFLLSGGTTGTPKLIPRTHNDYAYNV----------RASAEVCGLdqdtvylaV 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 305 LPSPlyH-----CLGSVGgtmvSMMHGATLLLSsPSFNGKKALEAISREKGTLLYGTPTMFVDILNQPDFSSYDFTSIRG 379
Cdd:cd05920 187 LPAA--HnfplaCPGVLG----TLLAGGRVVLA-PDPSPDAAFPLIEREGVTVTALVPALVSLWLDAAASRRADLSSLRL 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 380 GVIAGSPAPPELIRAIINKMNMKeLVVVYGTTENspvtFMNF--PEDTLEQKAGSVGRIM-PHTEAQIVN-----VETGE 451
Cdd:cd05920 260 LQVGGARLSPALARRVPPVLGCT-LQQVFGMAEG----LLNYtrLDDPDEVIIHTQGRPMsPDDEIRVVDeegnpVPPGE 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 452 ltnlnvPGELYIRGYCVMQGYWGEPQKTFETVGQDKWYRTGDIALMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLK 531
Cdd:cd05920 335 ------EGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLR 408
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24418933 532 HPQVQEAQVVGVKDERMGEEICACIRLKsGETTTAEEIKAFCKGK-ISHFKIPRYIVFVEGYPLTISGKIQK 602
Cdd:cd05920 409 HPAVHDAAVVAMPDELLGERSCAFVVLR-DPPPSAAQLRRFLRERgLAAYKLPDRIEFVDSLPLTAVGKIDK 479
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
98-608 |
3.22e-54 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 193.43 E-value: 3.22e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 98 IRLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSY----AWVLIQlataQAGIILVSVNPAYQSSELEYVLRKVGCK 173
Cdd:PRK06018 38 VRTTYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWrhleAWYGIM----GIGAICHTVNPRLFPEQIAWIINHAEDR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 174 GIVFPKQFktqqyydilkqvCPELEKAQPGALKSERLPDLTTVISVDAP-LPGTLLLDDIVAAGGKEQNLAQLRYNQRFL 252
Cdd:PRK06018 114 VVITDLTF------------VPILEKIADKLPSVERYVVLTDAAHMPQTtLKNAVAYEEWIAEADGDFAWKTFDENTAAG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 253 SCYdpiniqfTSGTTGNPKGATLSHHNIVNNSMLIGQRLKMPTKTAEelrLVLPS-PLYHClGSVGGTMVSMMHGATLLL 331
Cdd:PRK06018 182 MCY-------TSGTTGDPKGVLYSHRSNVLHALMANNGDALGTSAAD---TMLPVvPLFHA-NSWGIAFSAPSMGTKLVM 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 332 SSPSFNGKKALEAISREKGTLLYGTPTMFVDILNQPDFSSYDFTSIRGGVIAGSPAPPELIRAIiNKMNMkELVVVYGTT 411
Cdd:PRK06018 251 PGAKLDGASVYELLDTEKVTFTAGVPTVWLMLLQYMEKEGLKLPHLKMVVCGGSAMPRSMIKAF-EDMGV-EVRHAWGMT 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 412 ENSPV--------TFMNFPEDT-LEQKAGSvGRIMPHTEAQIVNVETGELT-NLNVPGELYIRGYCVMQGYWGEPQKTFE 481
Cdd:PRK06018 329 EMSPLgtlaalkpPFSKLPGDArLDVLQKQ-GYPPFGVEMKITDDAGKELPwDGKTFGRLKVRGPAVAAAYYRVDGEILD 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 482 tvgQDKWYRTGDIALMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQEAQVVGVKDERMGEEICACIRLKSG 561
Cdd:PRK06018 408 ---DDGFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQLKPG 484
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 24418933 562 ETTTAEEIKAFCKGKISHFKIPRYIVFVEGYPLTISGKIQKFKLREQ 608
Cdd:PRK06018 485 ETATREEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALREQ 531
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
112-606 |
3.36e-53 |
|
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: 188.80 E-value: 3.36e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 112 AASGLLSIGLRKGDR--LGMWGPNSYAWVLIQLATAQA--GIILVSVNPAYQSSELEYVLRKVGCKgIVFPkqfktqqyy 187
Cdd:cd05922 6 AASALLEAGGVRGERvvLILPNRFTYIELSFAVAYAGGrlGLVFVPLNPTLKESVLRYLVADAGGR-IVLA--------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 188 dilkqvcpelekaqpgalkSERLPDLTTVISVDAPLPGT-LLLDDIVAAGgkeQNLAQLRynqrfLSCYDPINIQFTSGT 266
Cdd:cd05922 76 -------------------DAGAADRLRDALPASPDPGTvLDADGIRAAR---ASAPAHE-----VSHEDLALLLYTSGS 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 267 TGNPKGATLSHHNIVNNSMLIGQRLKMptkTAEElRLVLPSPLYHCLG-SVGGTmvSMMHGATLLLSSPSFNGKKALEAI 345
Cdd:cd05922 129 TGSPKLVRLSHQNLLANARSIAEYLGI---TADD-RALTVLPLSYDYGlSVLNT--HLLRGATLVLTNDGVLDDAFWEDL 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 346 SREKGTLLYGTPTMFvDILNQPDFSSYDFTSIRGGVIAGSPAPPELIRAIINKMNMKELVVVYGTTENSP-VTFMnfPED 424
Cdd:cd05922 203 REHGATGLAGVPSTY-AMLTRLGFDPAKLPSLRYLTQAGGRLPQETIARLRELLPGAQVYVMYGQTEATRrMTYL--PPE 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 425 TLEQKAGSVGRIMPHTEAQIVNvETGELTNLNVPGELYIRGYCVMQGYWGEPQKTFETVGQDKWYRTGDIALMDEQGFCK 504
Cdd:cd05922 280 RILEKPGSIGLAIPGGEFEILD-DDGTPTPPGEPGEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDEDGFLF 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 505 IVGRSKDMIIRGGENIYPAELEDFFLKHPQVQEAQVVGVKDErMGEEICACIRLKSGetTTAEEIKAFCKGKISHFKIPR 584
Cdd:cd05922 359 IVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDP-LGEKLALFVTAPDK--IDPKDVLRSLAERLPPYKVPA 435
|
490 500
....*....|....*....|..
gi 24418933 585 YIVFVEGYPLTISGKIQKFKLR 606
Cdd:cd05922 436 TVRVVDELPLTASGKVDYAALR 457
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
99-612 |
7.20e-53 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 189.53 E-value: 7.20e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 99 RLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVSVNPAYQSSELEYVLRKVGCKGIVFP 178
Cdd:PRK07008 39 RYTYRDCERRAKQLAQALAALGVEPGDRVGTLAWNGYRHLEAYYGVSGSGAVCHTINPRLFPEQIAYIVNHAEDRYVLFD 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 179 KQFktqqyYDILKQVCPELEKAQPGALKSER--LPDLTTvisvdaPLpgtLLLDDIVAAGGKEQNLAQLRYNQRFLSCYd 256
Cdd:PRK07008 119 LTF-----LPLVDALAPQCPNVKGWVAMTDAahLPAGST------PL---LCYETLVGAQDGDYDWPRFDENQASSLCY- 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 257 piniqfTSGTTGNPKGATLSHHNivnnSMLIGQRLKMPTKTAEELR-LVLP-SPLYHcLGSVGGTMVSMMHGATLLLSSP 334
Cdd:PRK07008 184 ------TSGTTGNPKGALYSHRS----TVLHAYGAALPDAMGLSARdAVLPvVPMFH-VNAWGLPYSAPLTGAKLVLPGP 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 335 SFNGKKALEAISREKGTLLYGTPTMFVDILNQPDFSSYDFTSIRGGVIAGSPAPPELIRAIINKMNMkELVVVYGTTENS 414
Cdd:PRK07008 253 DLDGKSLYELIEAERVTFSAGVPTVWLGLLNHMREAGLRFSTLRRTVIGGSACPPAMIRTFEDEYGV-EVIHAWGMTEMS 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 415 PV----TFMN----FPEDTLEQKAGSVGRIMPHTEAQIVNVETGELTNLNVP-GELYIRGYCVMQGYWGEPQKTFEtvgq 485
Cdd:PRK07008 332 PLgtlcKLKWkhsqLPLDEQRKLLEKQGRVIYGVDMKIVGDDGRELPWDGKAfGDLQVRGPWVIDRYFRGDASPLV---- 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 486 DKWYRTGDIALMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQEAQVVGVK----DERmgeEICACIRlKSG 561
Cdd:PRK07008 408 DGWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAhpkwDER---PLLVVVK-RPG 483
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 24418933 562 ETTTAEEIKAFCKGKISHFKIPRYIVFVEGYPLTISGKIQKFKLREQMEQH 612
Cdd:PRK07008 484 AEVTREELLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKLREQFRDY 534
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
100-606 |
5.28e-52 |
|
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: 185.01 E-value: 5.28e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 100 LNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVSVNPAYQSSELEYVLRKVGCKGIVfpk 179
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLI--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 180 qfktqqyydilkqVCPEL-EKAQPGalkserlpdlttvisvdaplpgtlllddivaaggkeqnlaqlrynqrflscyDPI 258
Cdd:cd05969 78 -------------TTEELyERTDPE----------------------------------------------------DPT 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 259 NIQFTSGTTGNPKGATLSHHNIVNNSMLIGQRLKMptktaeelrlvLPSPLYHCL-------GSVGGTMVSMMHGATLLL 331
Cdd:cd05969 93 LLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLDL-----------HPDDIYWCTadpgwvtGTVYGIWAPWLNGVTNVV 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 332 SSPSFNGKKALEAISREKGTLLYGTPTMFVDILNQPDF--SSYDFTSIRGGVIAGSPAPPELIRAIINKMNMKeLVVVYG 409
Cdd:cd05969 162 YEGRFDAESWYGIIERVKVTVWYTAPTAIRMLMKEGDElaRKYDLSSLRFIHSVGEPLNPEAIRWGMEVFGVP-IHDTWW 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 410 TTENSPVTFMNFPedTLEQKAGSVGRIMPHTEAQIVNVETGELTNlNVPGELYIR-GYCVM-QGYWGEPQKtFETVGQDK 487
Cdd:cd05969 241 QTETGSIMIANYP--CMPIKPGSMGKPLPGVKAAVVDENGNELPP-GTKGILALKpGWPSMfRGIWNDEER-YKNSFIDG 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 488 WYRTGDIALMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQEAQVVGVKDERMGEEICACIRLKSG-ETTTA 566
Cdd:cd05969 317 WYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGfEPSDE 396
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 24418933 567 --EEIKAFCKGKISHFKIPRYIVFVEGYPLTISGKIQKFKLR 606
Cdd:cd05969 397 lkEEIINFVRQKLGAHVAPREIEFVDNLPKTRSGKIMRRVLK 438
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
79-605 |
3.03e-51 |
|
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: 183.94 E-value: 3.03e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 79 DATAQRFPDREALVilHENIRLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVSVNPAY 158
Cdd:cd12117 4 EEQAARTPDAVAVV--YGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 159 QSSELEYVLRKVGCKGIVfpkqfktqqyydilkqVCPELEKAQPGalkserlpDLTTVISVDAPLPGTLLLDDIVAAGGk 238
Cdd:cd12117 82 PAERLAFMLADAGAKVLL----------------TDRSLAGRAGG--------LEVAVVIDEALDAGPAGNPAVPVSPD- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 239 eqnlaqlrynqrflscyDPINIQFTSGTTGNPKGATLSHHNIVnnsmligqRLKMPTK---TAEELRLVLPSPlyhcLGS 315
Cdd:cd12117 137 -----------------DLAYVMYTSGSTGRPKGVAVTHRGVV--------RLVKNTNyvtLGPDDRVLQTSP----LAF 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 316 VGGTM---VSMMHGATLLLSSPSF--NGKKALEAISREKGTLLYGTPTMF---VDIlnQPDFssydFTSIRGGVIAGSPA 387
Cdd:cd12117 188 DASTFeiwGALLNGARLVLAPKGTllDPDALGALIAEEGVTVLWLTAALFnqlADE--DPEC----FAGLRELLTGGEVV 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 388 PPELIRAIINKMNMKELVVVYGTTENSpvTF-MNFPEDTLEQKAGSV--GRIMPHTEAQIVNvETGELTNLNVPGELYIR 464
Cdd:cd12117 262 SPPHVRRVLAACPGLRLVNGYGPTENT--TFtTSHVVTELDEVAGSIpiGRPIANTRVYVLD-EDGRPVPPGVPGELYVG 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 465 GYCVMQGYWGEPQKTFETVGQD------KWYRTGDIALMDEQGFCKIVGRSKDMI-IRgGENIYPAELEDFFLKHPQVQE 537
Cdd:cd12117 339 GDGLALGYLNRPALTAERFVADpfgpgeRLYRTGDLARWLPDGRLEFLGRIDDQVkIR-GFRIELGEIEAALRAHPGVRE 417
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24418933 538 AqVVGVKDERMGE-EICACIRLKsgETTTAEEIKAFCKGKISHFKIPRYIVFVEGYPLTISGKIQKFKL 605
Cdd:cd12117 418 A-VVVVREDAGGDkRLVAYVVAE--GALDAAELRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
80-614 |
2.73e-50 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 181.52 E-value: 2.73e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 80 ATAQRFPDREALVilHENIRLNFAQLKEEVDKAASGLLSIGlRKGDRLGMWGPNSYAWVLIQLATAQAGIILVSVNPAYQ 159
Cdd:PRK07638 9 KHASLQPNKIAIK--ENDRVLTYKDWFESVCKVANWLNEKE-SKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 160 SSELEYVLrKVGCKGIVFPKQFKTQqyyDILKQVCPELEKAQPGALKSERLPDLTTVISVDaplpgtlllddivaaggke 239
Cdd:PRK07638 86 QDELKERL-AISNADMIVTERYKLN---DLPDEEGRVIEIDEWKRMIEKYLPTYAPIENVQ------------------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 240 qnlaqlrynqrflscYDPINIQFTSGTTGNPKGATLSHHNIVNNSMLIGQRLKMptktAEELRLVLPSPLYHCLGSVGGt 319
Cdd:PRK07638 143 ---------------NAPFYMGFTSGSTGKPKAFLRAQQSWLHSFDCNVHDFHM----KREDSVLIAGTLVHSLFLYGA- 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 320 mVSMMH-GATLLLSsPSFNGKKALEAISREKGTLLYGTPTMFVDILNQPDFSSYDFTSIrggvIAGSPAPPELIRAIINK 398
Cdd:PRK07638 203 -ISTLYvGQTVHLM-RKFIPNQVLDKLETENISVMYTVPTMLESLYKENRVIENKMKII----SSGAKWEAEAKEKIKNI 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 399 MNMKELVVVYGTTENSPVTFMNfPEDTlEQKAGSVGRIMPHTEAQIVNvETGELTNLNVPGELYIRGYCVMQGYWGEPQK 478
Cdd:PRK07638 277 FPYAKLYEFYGASELSFVTALV-DEES-ERRPNSVGRPFHNVQVRICN-EAGEEVQKGEIGTVYVKSPQFFMGYIIGGVL 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 479 TFEtVGQDKWYRTGDIALMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQEAQVVGVKDERMGEEICACIRl 558
Cdd:PRK07638 354 ARE-LNADGWMTVRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAIIK- 431
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 24418933 559 ksgETTTAEEIKAFCKGKISHFKIPRYIVFVEGYPLTISGKIQKFKLREQMEQHLK 614
Cdd:PRK07638 432 ---GSATKQQLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEAKSWIENQEK 484
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
85-607 |
3.89e-50 |
|
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: 181.96 E-value: 3.89e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 85 FPDREALVILHENIRLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVSVNPAYQSSELE 164
Cdd:cd17642 30 VPGTIAFTDAHTGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 165 YVL-----RKVGCKGIVFPKQFKTQQYYDILKQVCPELEKAQPGALKSerlpdLTTVISVDAPlPGTLLLDDIVAAGGKE 239
Cdd:cd17642 110 HSLniskpTIVFCSKKGLQKVLNVQKKLKIIKTIIILDSKEDYKGYQC-----LYTFITQNLP-PGFNEYDFKPPSFDRD 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 240 QNLAQlrynqrflscydpinIQFTSGTTGNPKGATLSHHNIVnnSMLIGQRlkMPT---KTAEELRLVLPSPLYHCLGSV 316
Cdd:cd17642 184 EQVAL---------------IMNSSGSTGLPKGVQLTHKNIV--ARFSHAR--DPIfgnQIIPDTAILTVIPFHHGFGMF 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 317 GgTMVSMMHGATLLLSsPSFNGKKALEAISREKGTLLYGTPTMFVDILNQPDFSSYDFTSIRGGVIAGSPAPPELIRAII 396
Cdd:cd17642 245 T-TLGYLICGFRVVLM-YKFEEELFLRSLQDYKVQSALLVPTLFAFFAKSTLVDKYDLSNLHEIASGGAPLSKEVGEAVA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 397 NKMNMKELVVVYGTTENSPVTFMNFPEDTleqKAGSVGRIMPHTEAQIVNVETGELTNLNVPGELYIRGYCVMQGYWGEP 476
Cdd:cd17642 323 KRFKLPGIRQGYGLTETTSAILITPEGDD---KPGAVGKVVPFFYAKVVDLDTGKTLGPNERGELCVKGPMIMKGYVNNP 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 477 QKTFETVGQDKWYRTGDIALMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQEAQVVGVKDERMGEEICACI 556
Cdd:cd17642 400 EATKALIDKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVV 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 24418933 557 RLKSGETTTAEEIKAFCKGKISHFKIPR-YIVFVEGYPLTISGKIQKFKLRE 607
Cdd:cd17642 480 VLEAGKTMTEKEVMDYVASQVSTAKRLRgGVKFVDEVPKGLTGKIDRRKIRE 531
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
96-608 |
5.19e-50 |
|
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: 181.51 E-value: 5.19e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 96 ENIRLNFAQLKEEVDKAASGLL-SIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVSVNPAYQSSELEYVLRKVGCKG 174
Cdd:cd05928 38 DEVKWSFRELGSLSRKAANVLSgACGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKC 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 175 IVfpkqfktqqyydILKQVCPELEkaqpgALKSErLPDLTTVISV-DAPLPGTLLLDDIVAAGGKEQNLAQLRYNqrfls 253
Cdd:cd05928 118 IV------------TSDELAPEVD-----SVASE-CPSLKTKLLVsEKSRDGWLNFKELLNEASTEHHCVETGSQ----- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 254 cyDPINIQFTSGTTGNPKGATLSHHnivnnsmLIGQRLKMPTKTAEELRlvlPSPLYHCLGSVG------GTMVS-MMHG 326
Cdd:cd05928 175 --EPMAIYFTSGTTGSPKMAEHSHS-------SLGLGLKVNGRYWLDLT---ASDIMWNTSDTGwiksawSSLFEpWIQG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 327 ATLLLSS-PSFNGKKALEAISREKGTLLYGTPTMFvDILNQPDFSSYDFTSIRGGVIAGSPAPPELIRAIINKMNMkELV 405
Cdd:cd05928 243 ACVFVHHlPRFDPLVILKTLSSYPITTFCGAPTVY-RMLVQQDLSSYKFPSLQHCVTGGEPLNPEVLEKWKAQTGL-DIY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 406 VVYGTTEnSPVTFMNFpeDTLEQKAGSVGRIMPHTEAQIVNvETGELTNLNVPGELYIR-----GYCVMQGYWGEPQKTF 480
Cdd:cd05928 321 EGYGQTE-TGLICANF--KGMKIKPGSMGKASPPYDVQIID-DNGNVLPPGTEGDIGIRvkpirPFGLFSGYVDNPEKTA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 481 ETVGQDkWYRTGDIALMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQEAQVVGVKDERMGEEICACIRLKS 560
Cdd:cd05928 397 ATIRGD-FYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLAP 475
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 24418933 561 G------ETTTAeEIKAFCKGKISHFKIPRYIVFVEGYPLTISGKIQKFKLREQ 608
Cdd:cd05928 476 QflshdpEQLTK-ELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNELRDK 528
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
78-608 |
6.89e-50 |
|
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: 181.54 E-value: 6.89e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 78 LDATAQRFPDREALVILH---ENIRLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVSV 154
Cdd:cd05970 23 VDAMAKEYPDKLALVWCDdagEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 155 NPAYQSSELEYVLRKVGCKGIVFPKQFKTQQYYDILKQVCPELEK-AQPGALKSERLPDLTTVI---SVDAPLPgtlllD 230
Cdd:cd05970 103 THQLTAKDIVYRIESADIKMIVAIAEDNIPEEIEKAAPECPSKPKlVWVGDPVPEGWIDFRKLIknaSPDFERP-----T 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 231 DIVAAGGKeqnlaqlrynqrflscyDPINIQFTSGTTGNPKgaTLSHhnivNNSMLIGQRLkmptkTAEELRLVLPSPLY 310
Cdd:cd05970 178 ANSYPCGE-----------------DILLVYFSSGTTGMPK--MVEH----DFTYPLGHIV-----TAKYWQNVREGGLH 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 311 HCLGSVG--GTMVSMMHG------ATLLLSSPSFNGKKALEAISREKGTLLYGTPTMFvDILNQPDFSSYDFTSIRGGVI 382
Cdd:cd05970 230 LTVADTGwgKAVWGKIYGqwiagaAVFVYDYDKFDPKALLEKLSKYGVTTFCAPPTIY-RFLIREDLSRYDLSSLRYCTT 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 383 AGSPAPPELIRAIINKMNMKeLVVVYGTTENSpVTFMNFPedTLEQKAGSVGRIMPHTEAQIVN-----VETGEltnlnv 457
Cdd:cd05970 309 AGEALNPEVFNTFKEKTGIK-LMEGFGQTETT-LTIATFP--WMEPKPGSMGKPAPGYEIDLIDregrsCEAGE------ 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 458 PGELYIR-----GYCVMQGYWGEPQKTFEtVGQDKWYRTGDIALMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKH 532
Cdd:cd05970 379 EGEIVIRtskgkPVGLFGGYYKDAEKTAE-VWHDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQH 457
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24418933 533 PQVQEAQVVGVKDERMGEEICACIRLKSGETTTAE---EIKAFCKGKISHFKIPRYIVFVEGYPLTISGKIQKFKLREQ 608
Cdd:cd05970 458 PAVLECAVTGVPDPIRGQVVKATIVLAKGYEPSEElkkELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEIRER 536
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
114-600 |
8.42e-50 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 186.67 E-value: 8.42e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 114 SGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVSVNpaYQSSE--LEYVLRKVGCKGIVFPKQFktqqyydilk 191
Cdd:PRK08633 655 ARLLKRELKDEENVGILLPPSVAGALANLALLLAGKVPVNLN--YTASEaaLKSAIEQAQIKTVITSRKF---------- 722
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 192 qvcpeLEKaqpgalkserLPDLTTVISVDaPLPGTLLLDDIVAAGGKEQNLAQL-------------RYNQRFlSCYDPI 258
Cdd:PRK08633 723 -----LEK----------LKNKGFDLELP-ENVKVIYLEDLKAKISKVDKLTALlaarllparllkrLYGPTF-KPDDTA 785
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 259 NIQFTSGTTGNPKGATLSHHNIVNNSmligQRLKMPTKTAEELRLVLPSPLYHCLGSVGGTMVSMMHGATLLLSSPSFNG 338
Cdd:PRK08633 786 TIIFSSGSEGEPKGVMLSHHNILSNI----EQISDVFNLRNDDVILSSLPFFHSFGLTVTLWLPLLEGIKVVYHPDPTDA 861
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 339 KKALEAISREKGTLLYGTPTMFVDILNQPDFSSYDFTSIRGgVIAGSPA-PPELIRAIINKMNmKELVVVYGTTENSPVT 417
Cdd:PRK08633 862 LGIAKLVAKHRATILLGTPTFLRLYLRNKKLHPLMFASLRL-VVAGAEKlKPEVADAFEEKFG-IRILEGYGATETSPVA 939
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 418 FMNFP----EDTLEQ---KAGSVGRIMPHTEAQIVNVETGELTNLNVPGELYIRGYCVMQGYWGEPQKTFE---TVGQDK 487
Cdd:PRK08633 940 SVNLPdvlaADFKRQtgsKEGSVGMPLPGVAVRIVDPETFEELPPGEDGLILIGGPQVMKGYLGDPEKTAEvikDIDGIG 1019
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 488 WYRTGDIALMDEQGFCKIVGR----SKdmIirGGENIYPAELEDF---FLKHPQVQEAqVVGVKDERMGEEIcacIRLKS 560
Cdd:PRK08633 1020 WYVTGDKGHLDEDGFLTITDRysrfAK--I--GGEMVPLGAVEEElakALGGEEVVFA-VTAVPDEKKGEKL---VVLHT 1091
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 24418933 561 GETTTAEEIKAFCK-GKISHFKIPRYIVFVEGYPLTISGKI 600
Cdd:PRK08633 1092 CGAEDVEELKRAIKeSGLPNLWKPSRYFKVEALPLLGSGKL 1132
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
78-608 |
3.06e-49 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 179.70 E-value: 3.06e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 78 LDATAQRFPDREALVILHENIRLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVSVNPA 157
Cdd:PRK05852 22 VEVAATRLPEAPALVVTADRIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 158 YQSSELEYVLRKVGCKGIVFPKQFKTQQyydilkqvcpelekaqpgALKSERL-PDLTTVISVDAPLPGTLL--LDDIVA 234
Cdd:PRK05852 102 LPIAEQRVRSQAAGARVVLIDADGPHDR------------------AEPTTRWwPLTVNVGGDSGPSGGTLSvhLDAATE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 235 AGGKEQNLAQLRYnqrflscyDPINIQFTSGTTGNPKGATLSHHNIVNN--SMLIGQRLKMPTKTaeelrlVLPSPLYHC 312
Cdd:PRK05852 164 PTPATSTPEGLRP--------DDAMIMFTGGTTGLPKMVPWTHANIASSvrAIITGYRLSPRDAT------VAVMPLYHG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 313 LGSVGGTMVSMMHGATLLLSSPS-FNGKKALEAISREKGTLLYGTPTMFVDILNQPDFSSYDFTSIRGGVIAGSPAP--P 389
Cdd:PRK05852 230 HGLIAALLATLASGGAVLLPARGrFSAHTFWDDIKAVGATWYTAVPTIHQILLERAATEPSGRKPAALRFIRSCSAPltA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 390 ELIRAIINKMnMKELVVVYGTTENS-PVTFMNFP-EDTLEQKAGSVGRIMPHTEAQ--IVNVETGELTNLNVpGELYIRG 465
Cdd:PRK05852 310 ETAQALQTEF-AAPVVCAFGMTEAThQVTTTQIEgIGQTENPVVSTGLVGRSTGAQirIVGSDGLPLPAGAV-GEVWLRG 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 466 YCVMQGYWGEPQKTFETVgQDKWYRTGDIALMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQEAQVVGVKD 545
Cdd:PRK05852 388 TTVVRGYLGDPTITAANF-TDGWLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPD 466
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24418933 546 ERMGEEICACIRLKSGETTTAEEIKAFCKGKISHFKIPRYIVFVEGYPLTISGKIQKFKLREQ 608
Cdd:PRK05852 467 QLYGEAVAAVIVPRESAPPTAEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRRAVAEQ 529
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
79-607 |
5.87e-48 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 176.62 E-value: 5.87e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 79 DATAQRFPDRealvilHENIRLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNS---YAWVLiqlataqaGIIlvsvn 155
Cdd:PRK04319 59 DKVALRYLDA------SRKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIpelYFALL--------GAL----- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 156 payqsseleyvlrKVGCkgIVFP--KQFKTQQYYDILKQ-------VCPELEKAQPgalkSERLPDLTTVISVDAP---L 223
Cdd:PRK04319 120 -------------KNGA--IVGPlfEAFMEEAVRDRLEDseakvliTTPALLERKP----ADDLPSLKHVLLVGEDveeG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 224 PGTLLLDDIVAAGGKEqnlaqlrYNQRFLSCYDPINIQFTSGTTGNPKGATlshHniVNNSMLIGqrlKMPTKTAEELRl 303
Cdd:PRK04319 181 PGTLDFNALMEQASDE-------FDIEWTDREDGAILHYTSGSTGKPKGVL---H--VHNAMLQH---YQTGKYVLDLH- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 304 vlPSPLYHCL---GSVGGT----MVSMMHGATLLLSSPSFNGKKALEAISREKGTLLYGTPTMF-------VDILNQpdf 369
Cdd:PRK04319 245 --EDDVYWCTadpGWVTGTsygiFAPWLNGATNVIDGGRFSPERWYRILEDYKVTVWYTAPTAIrmlmgagDDLVKK--- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 370 ssYDFTSIRGGVIAGSPAPPELIRaiinkMNMKelvvVYG--------TTENSPVTFMNFPedTLEQKAGSVGRIMPHTE 441
Cdd:PRK04319 320 --YDLSSLRHILSVGEPLNPEVVR-----WGMK----VFGlpihdnwwMTETGGIMIANYP--AMDIKPGSMGKPLPGIE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 442 AQIVNVETGELTNlNVPGELYIR-GY-CVMQGYWGEPQKtFETVGQDKWYRTGDIALMDEQGFCKIVGRSKDMIIRGGEN 519
Cdd:PRK04319 387 AAIVDDQGNELPP-NRMGNLAIKkGWpSMMRGIWNNPEK-YESYFAGDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGER 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 520 IYPAELEDFFLKHPQVQEAQVVGVKDERMGEEICACIRLKSGETTTAE---EIKAFCKGKISHFKIPRYIVFVEGYPLTI 596
Cdd:PRK04319 465 VGPFEVESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVALRPGYEPSEElkeEIRGFVKKGLGAHAAPREIEFKDKLPKTR 544
|
570
....*....|...
gi 24418933 597 SGKIQK--FKLRE 607
Cdd:PRK04319 545 SGKIMRrvLKAWE 557
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
78-607 |
1.13e-47 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 175.98 E-value: 1.13e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 78 LDATAQRFPDREAlvILHENIRLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVSVNPA 157
Cdd:PLN03102 20 LKRASECYPNRTS--IIYGKTRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 158 YQSSELEYVLRKVGCKGIVFPKQFK--TQQYYDILKQvcpelEKAQPGalkserlPDLTTVISVDAPL-PGTLLLD--DI 232
Cdd:PLN03102 98 LDATSIAAILRHAKPKILFVDRSFEplAREVLHLLSS-----EDSNLN-------LPVIFIHEIDFPKrPSSEELDyeCL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 233 VAAGGKEQNLAQLRYnqRFLSCYDPINIQFTSGTTGNPKGATLSHHN--IVNNSMLIGQRLKMPTKTAEELrlvlpsPLY 310
Cdd:PLN03102 166 IQRGEPTPSLVARMF--RIQDEHDPISLNYTSGTTADPKGVVISHRGayLSTLSAIIGWEMGTCPVYLWTL------PMF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 311 HCLG--------SVGGTMVSMMHgatllLSSPSFNGKKALEAIsrekgTLLYGTPTMFVDILNQpdfSSYDFTSIRGGV- 381
Cdd:PLN03102 238 HCNGwtftwgtaARGGTSVCMRH-----VTAPEIYKNIEMHNV-----THMCCVPTVFNILLKG---NSLDLSPRSGPVh 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 382 --IAGSPAPPELIRAIiNKMNMkELVVVYGTTENS-PVTFMNF-------PEDT-LEQKAGSVGRIMPHTEAQIVNVETG 450
Cdd:PLN03102 305 vlTGGSPPPAALVKKV-QRLGF-QVMHAYGLTEATgPVLFCEWqdewnrlPENQqMELKARQGVSILGLADVDVKNKETQ 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 451 EltnlNVP------GELYIRGYCVMQGYWGEPQKTFETVgQDKWYRTGDIALMDEQGFCKIVGRSKDMIIRGGENIYPAE 524
Cdd:PLN03102 383 E----SVPrdgktmGEIVIKGSSIMKGYLKNPKATSEAF-KHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVE 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 525 LEDFFLKHPQVQEAQVVGVKDERMGEEICACIRLKSGETTTAEEIKAF----------CKGKISHFKIPRYIVFVEGYPL 594
Cdd:PLN03102 458 VENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGETTKEDRVDKLvtrerdlieyCRENLPHFMCPRKVVFLQELPK 537
|
570
....*....|...
gi 24418933 595 TISGKIQKFKLRE 607
Cdd:PLN03102 538 NGNGKILKPKLRD 550
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
82-606 |
8.89e-46 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 169.42 E-value: 8.89e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 82 AQRFPDREALVILHENIRLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVSVNPAYQSS 161
Cdd:PRK13390 7 AQIAPDRPAVIVAETGEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 162 ELEYVLRKVGCKGIVfpkqfktqqyydilkqvcpelEKAQPGALKSERLPDLTTVISVDAPLPGTLLLDDIVAAGG---K 238
Cdd:PRK13390 87 EADYIVGDSGARVLV---------------------ASAALDGLAAKVGADLPLRLSFGGEIDGFGSFEAALAGAGprlT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 239 EQNLAQLrynqrflscydpinIQFTSGTTGNPKGATLShhnivnnsmLIGQRLKMP----TKTAEELRLVLPS------- 307
Cdd:PRK13390 146 EQPCGAV--------------MLYSSGTTGFPKGIQPD---------LPGRDVDAPgdpiVAIARAFYDISESdiyyssa 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 308 PLYHCLGSVGGTMVSMMHGATLLlsSPSFNGKKALEAISREKGTLLYGTPTMFVDILNQPD--FSSYDFTSIRGGVIAGS 385
Cdd:PRK13390 203 PIYHAAPLRWCSMVHALGGTVVL--AKRFDAQATLGHVERYRITVTQMVPTMFVRLLKLDAdvRTRYDVSSLRAVIHAAA 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 386 PAPPELIRAIINKMNmKELVVVYGTTENSPVTFMNFPEDTLEQkaGSVGRIMPHTeAQIVNVETGELTNLNVpGELYIRG 465
Cdd:PRK13390 281 PCPVDVKHAMIDWLG-PIVYEYYSSTEAHGMTFIDSPDWLAHP--GSVGRSVLGD-LHICDDDGNELPAGRI-GTVYFER 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 466 YCVMQGYWGEPQKTFETV--GQDKWYRTGDIALMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQEAQVVGV 543
Cdd:PRK13390 356 DRLPFRYLNDPEKTAAAQhpAHPFWTTVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGV 435
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24418933 544 KDERMGEEICACIRLKSG---ETTTAEEIKAFCKGKISHFKIPRYIVFVEGYPLTISGKIQKFKLR 606
Cdd:PRK13390 436 PDPEMGEQVKAVIQLVEGirgSDELARELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
82-611 |
8.12e-45 |
|
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.
Pssm-ID: 341254 [Multi-domain] Cd Length: 547 Bit Score: 167.42 E-value: 8.12e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 82 AQRFPDREALVILH----ENIRLNFAQLKEEVDKAASGLLSIGLRkGDRLGMWGPNSYAWVLIQLATAQAGIILVsvnPA 157
Cdd:cd05931 3 AAARPDRPAYTFLDdeggREETLTYAELDRRARAIAARLQAVGKP-GDRVLLLAPPGLDFVAAFLGCLYAGAIAV---PL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 158 YQSSELEYVLRKVG----CK-GIVFPkqfkTQQYYDILKQVCPELEKAQPGALkseRLPDLTTVISVDAPLPGTLLLDDI 232
Cdd:cd05931 79 PPPTPGRHAERLAAiladAGpRVVLT----TAAALAAVRAFAASRPAAGTPRL---LVVDLLPDTSAADWPPPSPDPDDI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 233 VaaggkeqnlaqlrynqrFLscydpiniQFTSGTTGNPKGATLSHHNIVNNSMLIGQRLKMPTKTaeelRLVLPSPLYHC 312
Cdd:cd05931 152 A-----------------YL--------QYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGD----VVVSWLPLYHD 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 313 LGSVGGTMVSMMHGATLLLSSP-SFNGKKA--LEAISREKGTLLYGtPTmF-----VDILNQPDFSSYDFTSIRGGVIAG 384
Cdd:cd05931 203 MGLIGGLLTPLYSGGPSVLMSPaAFLRRPLrwLRLISRYRATISAA-PN-FaydlcVRRVRDEDLEGLDLSSWRVALNGA 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 385 SPAPPELIRAIINKM--------------NMKELVV-VYGTTENSPVTFMNFPEDTLEQKAG-------------SVGRI 436
Cdd:cd05931 281 EPVRPATLRRFAEAFapfgfrpeafrpsyGLAEATLfVSGGPPGTGPVVLRVDRDALAGRAVavaaddpaarelvSCGRP 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 437 MPHTEAQIVNVETGELTNLNVPGELYIRGYCVMQGYWGEPQKTFETVGQ------DKWYRTGDIA-LMDEQGFckIVGRS 509
Cdd:cd05931 361 LPDQEVRIVDPETGRELPDGEVGEIWVRGPSVASGYWGRPEATAETFGAlaatdeGGWLRTGDLGfLHDGELY--ITGRL 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 510 KDMIIRGGENIYPAELEDF-FLKHPQVQEAQVV--GVKDERMGEEICACIRLKSGETTTAEEIKAFCKGKIS-HFKI-PR 584
Cdd:cd05931 439 KDLIIVRGRNHYPQDIEATaEEAHPALRPGCVAafSVPDDGEERLVVVAEVERGADPADLAAIAAAIRAAVArEHGVaPA 518
|
570 580
....*....|....*....|....*....
gi 24418933 585 YIVFVE--GYPLTISGKIQKFKLREQMEQ 611
Cdd:cd05931 519 DVVLVRpgSIPRTSSGKIQRRACRAAYLD 547
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
103-540 |
3.13e-44 |
|
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: 162.82 E-value: 3.13e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 103 AQLKEEVDKAASGLLSI-GLRKGDRLGMWGPNSyAWVLI-QLATAQAGIILVSVNPAYQSSELEYVLRKVGCKGIVfpkq 180
Cdd:TIGR01733 3 RELDERANRLARHLRAAgGVGPGDRVAVLLERS-AELVVaILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLL---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 181 fktqqyydilkqVCPELEKAQPGALKSERLPDLTTVISVDAPLPGTLllddiVAAGGKEQNLAqlrynqrflscYdpinI 260
Cdd:TIGR01733 78 ------------TDSALASRLAGLVLPVILLDPLELAALDDAPAPPP-----PDAPSGPDDLA-----------Y----V 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 261 QFTSGTTGNPKGATLSHHNIVNnsmLIGQRLKMPTKTAEELRLVLPSplYHCLGSVGGTMVSMMHGATLLLSSPS---FN 337
Cdd:TIGR01733 126 IYTSGSTGRPKGVVVTHRSLVN---LLAWLARRYGLDPDDRVLQFAS--LSFDASVEEIFGALLAGATLVVPPEDeerDD 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 338 GKKALEAISREKGTLLYGTPTMFVDILNQPDFSsydFTSIRGGVIAGSPAPPELIRAIINKMNMKELVVVYGTTENSPVT 417
Cdd:TIGR01733 201 AALLAALIAEHPVTVLNLTPSLLALLAAALPPA---LASLRLVILGGEALTPALVDRWRARGPGARLINLYGPTETTVWS 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 418 FMNFPEDTLEQKAGSV--GRIMPHTEAQIVNvETGELTNLNVPGELYIRGYCVMQGYWGEPQKT--------FETVGQDK 487
Cdd:TIGR01733 278 TATLVDPDDAPRESPVpiGRPLANTRLYVLD-DDLRPVPVGVVGELYIGGPGVARGYLNRPELTaerfvpdpFAGGDGAR 356
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 24418933 488 WYRTGDIALMDEQGFCKIVGRSKDMI-IRgGENIYPAELEDFFLKHPQVQEAQV 540
Cdd:TIGR01733 357 LYRTGDLVRYLPDGNLEFLGRIDDQVkIR-GYRIELGEIEAALLRHPGVREAVV 409
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
78-606 |
8.69e-44 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 165.02 E-value: 8.69e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 78 LDATAQRFPDREALVilHENIRLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVSVNPA 157
Cdd:PLN02479 26 LERAAVVHPTRKSVV--HGSVRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 158 YQSSELEYVLRKVGCKGIVFpkqfkTQQYYDILKQVCPELEKAQPGALKserlPDLTTVISVDAPLPGTLllDDIVAAGG 237
Cdd:PLN02479 104 LNAPTIAFLLEHSKSEVVMV-----DQEFFTLAEEALKILAEKKKSSFK----PPLLIVIGDPTCDPKSL--QYALGKGA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 238 KEQnlaqlrynQRFLSCYDP-------------INIQFTSGTTGNPKGATLSHHNI----VNNSMLIGqrlkMPTKTAEE 300
Cdd:PLN02479 173 IEY--------EKFLETGDPefawkppadewqsIALGYTSGTTASPKGVVLHHRGAylmaLSNALIWG----MNEGAVYL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 301 LRLvlpsPLYHCLGSVGGTMVSMMHGATLLLSSPSfnGKKALEAISREKGTLLYGTPTMFVDILNQPDFSSY-DFTSIRG 379
Cdd:PLN02479 241 WTL----PMFHCNGWCFTWTLAALCGTNICLRQVT--AKAIYSAIANYGVTHFCAAPVVLNTIVNAPKSETIlPLPRVVH 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 380 GVIAGSPAPPELIRAiinkMNMKELVVV--YGTTEN-SPVTFMNFPEDTLEQKAGSVGRIMPHTEAQIVNVETGEL---- 452
Cdd:PLN02479 315 VMTAGAAPPPSVLFA----MSEKGFRVThtYGLSETyGPSTVCAWKPEWDSLPPEEQARLNARQGVRYIGLEGLDVvdtk 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 453 TNLNVP------GELYIRGYCVMQGYWGEPQKTFETVgQDKWYRTGDIALMDEQGFCKIVGRSKDMIIRGGENIYPAELE 526
Cdd:PLN02479 391 TMKPVPadgktmGEIVMRGNMVMKGYLKNPKANEEAF-ANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVE 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 527 DFFLKHPQVQEAQVVGVKDERMGEEICACIRLKSG-----ETTTAEEIKAFCKGKISHFKIPRYIVFvEGYPLTISGKIQ 601
Cdd:PLN02479 470 NVVYTHPAVLEASVVARPDERWGESPCAFVTLKPGvdksdEAALAEDIMKFCRERLPAYWVPKSVVF-GPLPKTATGKIQ 548
|
....*
gi 24418933 602 KFKLR 606
Cdd:PLN02479 549 KHVLR 553
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
99-549 |
1.03e-43 |
|
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: 162.91 E-value: 1.03e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 99 RLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVSVNPAYQSSELEYVLRKVGCKGIVfp 178
Cdd:cd17640 5 RITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALV-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 179 kqfktqqyydilkqvcpeLEKAQPgalkserlpDLTTVIsvdaplpgtlllddivaaggkeqnlaqlrynqrflscydpi 258
Cdd:cd17640 83 ------------------VENDSD---------DLATII----------------------------------------- 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 259 niqFTSGTTGNPKGATLSHHNIVNNsmlIGQRLKM-PTKTAEELRLVLPSplYHCLGSVGGTmVSMMHGATLLLSSPSFn 337
Cdd:cd17640 95 ---YTSGTTGNPKGVMLTHANLLHQ---IRSLSDIvPPQPGDRFLSILPI--WHSYERSAEY-FIFACGCSQAYTSIRT- 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 338 gkkALEAISREKGTLLYGTPTMFVDILN--QPDFSSYDFTS-------IRGG----VIAGSPAPPELIRAIINKMNMkEL 404
Cdd:cd17640 165 ---LKDDLKRVKPHYIVSVPRLWESLYSgiQKQVSKSSPIKqflflffLSGGifkfGISGGGALPPHVDTFFEAIGI-EV 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 405 VVVYGTTENSPVTFMNFPEdtlEQKAGSVGRIMPHTEAQIVNVETGELTNLNVPGELYIRGYCVMQGYWGEPQKTFETVG 484
Cdd:cd17640 241 LNGYGLTETSPVVSARRLK---CNVRGSVGRPLPGTEIKIVDPEGNVVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLD 317
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24418933 485 QDKWYRTGDIALMDEQGFCKIVGRSKDMII-RGGENIYPAELEDFFLKHPQVQEAQVVGVKDERMG 549
Cdd:cd17640 318 SDGWFNTGDLGWLTCGGELVLTGRAKDTIVlSNGENVEPQPIEEALMRSPFIEQIMVVGQDQKRLG 383
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
260-606 |
1.16e-43 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 162.85 E-value: 1.16e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 260 IQFTSGTTGNPKGATLSHHNIVNNSMLIGQRLKMptkTAEELrLVLPSPLYHCLGSVGGTMVSMMHGATLLlsspsFNGK 339
Cdd:PRK07787 133 IVYTSGTTGPPKGVVLSRRAIAADLDALAEAWQW---TADDV-LVHGLPLFHVHGLVLGVLGPLRIGNRFV-----HTGR 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 340 KALEAISRE---KGTLLYGTPTMFVDILNQPDfSSYDFTSIRGGViAGSPAPPELIRAIINKMNMKELVVVYGTTEnspv 416
Cdd:PRK07787 204 PTPEAYAQAlseGGTLYFGVPTVWSRIAADPE-AARALRGARLLV-SGSAALPVPVFDRLAALTGHRPVERYGMTE---- 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 417 TFMNFpeDTL---EQKAGSVGRIMPHTEAQIVNvETGEltnlNVP------GELYIRGYCVMQGYWGEPQKTFETVGQDK 487
Cdd:PRK07787 278 TLITL--STRadgERRPGWVGLPLAGVETRLVD-EDGG----PVPhdgetvGELQVRGPTLFDGYLNRPDATAAAFTADG 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 488 WYRTGDIALMDEQGFCKIVGR-SKDMIIRGGENIYPAELEDFFLKHPQVQEAQVVGVKDERMGEEICACIrlKSGETTTA 566
Cdd:PRK07787 351 WFRTGDVAVVDPDGMHRIVGReSTDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYV--VGADDVAA 428
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 24418933 567 EEIKAFCKGKISHFKIPRYIVFVEGYPLTISGKIQKFKLR 606
Cdd:PRK07787 429 DELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLL 468
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
86-606 |
1.37e-43 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 164.24 E-value: 1.37e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 86 PDREALVILHENIRLNFAQLKEEVDKAASGLL-SIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVSVNPAyqSSELE 164
Cdd:PLN02574 53 NGDTALIDSSTGFSISYSELQPLVKSMAAGLYhVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPS--SSLGE 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 165 YVLRKVGCK-GIVFpkqfktqqyydilkqVCPElekaqpgalKSERLPDL-TTVISVdaplPGTLLLDDIVAAGGKEQNL 242
Cdd:PLN02574 131 IKKRVVDCSvGLAF---------------TSPE---------NVEKLSPLgVPVIGV----PENYDFDSKRIEFPKFYEL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 243 AQLRYN---QRFLSCYDPINIQFTSGTTGNPKGATLSHHNIVNNSMLI----GQRLKMPTKTAEELRLVlpsPLYHCLG- 314
Cdd:PLN02574 183 IKEDFDfvpKPVIKQDDVAAIMYSSGTTGASKGVVLTHRNLIAMVELFvrfeASQYEYPGSDNVYLAAL---PMFHIYGl 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 315 --------SVGGTMVSMMhgatlllsspSFNGKKALEAISREKGTLLYGTPTMFVDILNQPD-FSSYDFTSIRGGVIAGS 385
Cdd:PLN02574 260 slfvvgllSLGSTIVVMR----------RFDASDMVKVIDRFKVTHFPVVPPILMALTKKAKgVCGEVLKSLKQVSCGAA 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 386 PAPPELIRAIINKMNMKELVVVYGTTENSPVTFMNFPEDTLeQKAGSVGRIMPHTEAQIVNVETGELTNLNVPGELYIRG 465
Cdd:PLN02574 330 PLSGKFIQDFVQTLPHVDFIQGYGMTESTAVGTRGFNTEKL-SKYSSVGLLAPNMQAKVVDWSTGCLLPPGNCGELWIQG 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 466 YCVMQGYWGEPQKTFETVGQDKWYRTGDIALMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQEAQVVGVKD 545
Cdd:PLN02574 409 PGVMKGYLNNPKATQSTIDKDGWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPD 488
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24418933 546 ERMGEEICACIRLKSGETTTAEEIKAFCKGKISHFKIPRYIVFVEGYPLTISGKIQKFKLR 606
Cdd:PLN02574 489 KECGEIPVAFVVRRQGSTLSQEAVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRRELK 549
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
86-600 |
1.88e-43 |
|
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: 162.08 E-value: 1.88e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 86 PDREALVILHEniRLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVSVNPAYQSSELEY 165
Cdd:cd12116 1 PDATAVRDDDR--SLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 166 VLrkvgckgivfpkqfktqqyydilkqvcpelEKAQPGA-LKSERLPDlttviSVDAPLPGTLLLDDIVAAGGKEQnlaq 244
Cdd:cd12116 79 IL------------------------------EDAEPALvLTDDALPD-----RLPAGLPVLLLALAAAAAAPAAP---- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 245 lrynQRFLSCYDPINIQFTSGTTGNPKGATLSHHNIVNNSMLIGQRLKMptkTAEE--------------LRLVLPsply 310
Cdd:cd12116 120 ----RTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSMRERLGL---GPGDrllavttyafdislLELLLP---- 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 311 hclgsvggtmvsMMHGATLLLSSPSFN--GKKALEAISREKGTLLYGTPT---MFVDILNQPdfssydftsiRGGVIA-- 383
Cdd:cd12116 189 ------------LLAGARVVIAPRETQrdPEALARLIEAHSITVMQATPAtwrMLLDAGWQG----------RAGLTAlc 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 384 -GSPAPPELIRAIINKMnmKELVVVYGTTEN---SPVTFMnfpedTLEQKAGSVGRIMPHTEAQIVN-----VETGeltn 454
Cdd:cd12116 247 gGEALPPDLAARLLSRV--GSLWNLYGPTETtiwSTAARV-----TAAAGPIPIGRPLANTQVYVLDaalrpVPPG---- 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 455 lnVPGELYIRGYCVMQGYWGEPQKTFETVGQD-------KWYRTGDIALMDEQGFCKIVGRSKDMI-IRgGENIYPAELE 526
Cdd:cd12116 316 --VPGELYIGGDGVAQGYLGRPALTAERFVPDpfagpgsRLYRTGDLVRRRADGRLEYLGRADGQVkIR-GHRIELGEIE 392
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24418933 527 DFFLKHPQVQEAQVVgVKDERMGEEICACIRLKSGETTTAEEIKAFCKGKISHFKIPRYIVFVEGYPLTISGKI 600
Cdd:cd12116 393 AALAAHPGVAQAAVV-VREDGGDRRLVAYVVLKAGAAPDAAALRAHLRATLPAYMVPSAFVRLDALPLTANGKL 465
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
99-606 |
3.34e-43 |
|
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: 160.68 E-value: 3.34e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 99 RLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVSVNPAYQSSELEYVLRKVGckgivfp 178
Cdd:cd05971 6 KVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSG------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 179 kqfktqqyydilkqvcpelekaqpgalkserlpdlTTVISVDAPlpgtlllddivaaggkeqnlaqlrynqrflscYDPI 258
Cdd:cd05971 79 -----------------------------------ASALVTDGS--------------------------------DDPA 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 259 NIQFTSGTTGNPKGATLSHHnivnnsMLIGQR--LKMPTKTAEELRLVLPSPL-YHCLGSVGGTMV-SMMHGATLLLSSP 334
Cdd:cd05971 92 LIIYTSGTTGPPKGALHAHR------VLLGHLpgVQFPFNLFPRDGDLYWTPAdWAWIGGLLDVLLpSLYFGVPVLAHRM 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 335 S-FNGKKALEAISREKGTLLYGTPTMFVDILNQPDFSSYDFTSIRGGVIAGSPAPPELIRAIINKMNMkELVVVYGTTEN 413
Cdd:cd05971 166 TkFDPKAALDLMSRYGVTTAFLPPTALKMMRQQGEQLKHAQVKLRAIATGGESLGEELLGWAREQFGV-EVNEFYGQTEC 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 414 SPVTFMN---FPedtleQKAGSVGRIMPHTEAQIVNvETGELTNLNVPGELYIRGYC--VMQGYWGEPQKTFETVGQDkW 488
Cdd:cd05971 245 NLVIGNCsalFP-----IKPGSMGKPIPGHRVAIVD-DNGTPLPPGEVGEIAVELPDpvAFLGYWNNPSATEKKMAGD-W 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 489 YRTGDIALMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQEAQVVGVKDERMGEEICACIRLKSGETTT--- 565
Cdd:cd05971 318 LLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGETPSdal 397
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 24418933 566 AEEIKAFCKGKISHFKIPRYIVFVEGYPLTISGKIQKFKLR 606
Cdd:cd05971 398 AREIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRRELR 438
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
82-605 |
5.50e-43 |
|
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: 160.11 E-value: 5.50e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 82 AQRFPDREALVilHENIRLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVSVNPAYQSS 161
Cdd:cd05945 1 AAANPDRPAVV--EGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 162 ELEYVLRKVGCKGIVfpkQFKTQQYYdilkqvcpelekaqpgalkserlpdlttvisvdaplpgtlllddivaaggkeqn 241
Cdd:cd05945 79 RIREILDAAKPALLI---ADGDDNAY------------------------------------------------------ 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 242 laqlrynqrflscydpinIQFTSGTTGNPKGATLSHHNIVNNSMLIGQRLKMPtktaEELRlVLPSPLYHCLGSVGGTMV 321
Cdd:cd05945 102 ------------------IIFTSGSTGRPKGVQISHDNLVSFTNWMLSDFPLG----PGDV-FLNQAPFSFDLSVMDLYP 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 322 SMMHGATLLLSSP--SFNGKKALEAISREKGTLLYGTPTmFVDILNQ-PDFSSYDFTSIRGGVIAGSPAPPELIRAIINK 398
Cdd:cd05945 159 ALASGATLVPVPRdaTADPKQLFRFLAEHGITVWVSTPS-FAAMCLLsPTFTPESLPSLRHFLFCGEVLPHKTARALQQR 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 399 MNMKELVVVYGTTE-NSPVTFMNFPEDTLEQkAGSV--GRIMPHTEAQIVNvETGELTNLNVPGELYIRGYCVMQGYWGE 475
Cdd:cd05945 238 FPDARIYNTYGPTEaTVAVTYIEVTPEVLDG-YDRLpiGYAKPGAKLVILD-EDGRPVPPGEKGELVISGPSVSKGYLNN 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 476 PQKT----FETVGQdKWYRTGDIALMDEQGFCKIVGRSKDMI-IRGgeniYPAELED--FFL-KHPQVQEAQVVGVKDER 547
Cdd:cd05945 316 PEKTaaafFPDEGQ-RAYRTGDLVRLEADGLLFYRGRLDFQVkLNG----YRIELEEieAALrQVPGVKEAVVVPKYKGE 390
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24418933 548 MGEEICACIRLKSGET---TTaeEIKAFCKGKISHFKIPRYIVFVEGYPLTISGKIQKFKL 605
Cdd:cd05945 391 KVTELIAFVVPKPGAEaglTK--AIKAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
85-607 |
1.99e-42 |
|
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: 159.90 E-value: 1.99e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 85 FPDREALVI---LHENIRLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVSVNPAYQSS 161
Cdd:cd05915 7 LFGRKEVVSrlhTGEVHRTTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 162 ELEYVLRKVGCKgiVFpkqFKTQQYYDILKQVCPELEKAQPGALKSERLPDLTTVISVDAPlpgtlllddivaaggkeqN 241
Cdd:cd05915 87 EIAYILNHAEDK--VL---LFDPNLLPLVEAIRGELKTVQHFVVMDEKAPEGYLAYEEALG------------------E 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 242 LAQLRYNQRflsCyDPINIQFTSGTTGNPKGATLSHHNIVNNSMLIGQRLKMPTKTAEELRLVLPspLYHCLGSVGGTMV 321
Cdd:cd05915 144 EADPVRVPE---R-AACGMAYTTGTTGLPKGVVYSHRALVLHSLAASLVDGTALSEKDVVLPVVP--MFHVNAWCLPYAA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 322 SMMHGATLLLSSpSFNGKKALEAISREKGTLLYGTPTMFVDILNQPDFSSYDFT-SIRggVIAGSPAPPELIRAIiNKMN 400
Cdd:cd05915 218 TLVGAKQVLPGP-RLDPASLVELFDGEGVTFTAGVPTVWLALADYLESTGHRLKtLRR--LVVGGSAAPRSLIAR-FERM 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 401 MKELVVVYGTTE----NSPVTFM----NFPED-TLEQKAgsvgRIMPHTEAQIVNVEtgELTNLNVPGE------LYIRG 465
Cdd:cd05915 294 GVEVRQGYGLTEtspvVVQNFVKshleSLSEEeKLTLKA----KTGLPIPLVRLRVA--DEEGRPVPKDgkalgeVQLKG 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 466 YCVMQGYWGEPQKTFETVGQDKWYRTGDIALMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQEAQVVGVKD 545
Cdd:cd05915 368 PWITGGYYGNEEATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPH 447
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24418933 546 ERMGEEICACIRLKSGEtTTAEEIKAFCKGKISHFK-IPRYIVFVEGYPLTISGKIQKFKLRE 607
Cdd:cd05915 448 PKWQERPLAVVVPRGEK-PTPEELNEHLLKAGFAKWqLPDAYVFAEEIPRTSAGKFLKRALRE 509
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
95-541 |
1.33e-41 |
|
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: 156.83 E-value: 1.33e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 95 HENIRLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVSVNPAYQSSELEYVLRKVGCKg 174
Cdd:cd05914 3 YGGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAK- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 175 IVFPkqfktqqyydilkqvcpelekaqpgalkserlpdlttvisvdaplpgtlllddivaagGKEQNLAQLRYnqrflsc 254
Cdd:cd05914 82 AIFV----------------------------------------------------------SDEDDVALINY------- 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 255 ydpiniqfTSGTTGNPKGATLSHHNIVNNsMLIGQRLKMPTKTAEELRLVlpsPLYHCLGSVGGTMVSMMHGATL-LLSS 333
Cdd:cd05914 97 --------TSGTTGNSKGVMLTYRNIVSN-VDGVKEVVLLGKGDKILSIL---PLHHIYPLTFTLLLPLLNGAHVvFLDK 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 334 PSfngKKALEAISREKGTLLYGTPTMFV-------DILNQPDFSSYDF--------TSIR-----------GG-----VI 382
Cdd:cd05914 165 IP---SAKIIALAFAQVTPTLGVPVPLViekifkmDIIPKLTLKKFKFklakkinnRKIRklafkkvheafGGnikefVI 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 383 AGSPAPPElIRAIINKMNMKeLVVVYGTTENSPVTFMNFPEDTleqKAGSVGRIMPHTEAQI--VNVETGEltnlnvpGE 460
Cdd:cd05914 242 GGAKINPD-VEEFLRTIGFP-YTIGYGMTETAPIISYSPPNRI---RLGSAGKVIDGVEVRIdsPDPATGE-------GE 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 461 LYIRGYCVMQGYWGEPQKTFETVGQDKWYRTGDIALMDEQGFCKIVGRSKDMIIRG-GENIYPAELEDFFLKHPQVQEAQ 539
Cdd:cd05914 310 IIVRGPNVMKGYYKNPEATAEAFDKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSsGKNIYPEEIEAKINNMPFVLESL 389
|
..
gi 24418933 540 VV 541
Cdd:cd05914 390 VV 391
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
26-609 |
1.37e-40 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 155.15 E-value: 1.37e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 26 LLSRPRPNSKLQSVRALSSGMVNCTNPLPIgglsyiqghtdshlvnttvgecldaTAQRFPDREAlvILHENIRLNFAQL 105
Cdd:PRK13383 14 LLNPPSPRAVLRLLREASRGGTNPYTLLAV-------------------------TAARWPGRTA--IIDDDGALSYREL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 106 KEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVSVNPAYQSSELEYVLRKVGCKGIVFPKQFKTQQ 185
Cdd:PRK13383 67 QRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAALRAHHISTVVADNEFAERI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 186 yydilkqvcpelekaqPGALKSERLPDLTTVISVDAplpgtlllddivaaGGKEQNLAQLRYnqrflscydpinIQFTSG 265
Cdd:PRK13383 147 ----------------AGADDAVAVIDPATAGAEES--------------GGRPAVAAPGRI------------VLLTSG 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 266 TTGNPKGATLSHH--NIVNNSMLIGQRLKMPTKTaeelRLVLPSPLYHCLGsVGGTMVSMMHGATLLlSSPSFNGKKALE 343
Cdd:PRK13383 185 TTGKPKGVPRAPQlrSAVGVWVTILDRTRLRTGS----RISVAMPMFHGLG-LGMLMLTIALGGTVL-THRHFDAEAALA 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 344 AISREKGTLLYGTPTMFVDILNQPD--FSSYDFTSIRGGVIAGSPAPPELIRAIINKMNmKELVVVYGTTE------NSP 415
Cdd:PRK13383 259 QASLHRADAFTAVPVVLARILELPPrvRARNPLPQLRVVMSSGDRLDPTLGQRFMDTYG-DILYNGYGSTEvgigalATP 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 416 VTFMNFPEdtleqkagSVGRIMPHTEAQIVNvETGELTNLNVPGELYIRGYCVMQGYWGEPQKTFetvgQDKWYRTGDIA 495
Cdd:PRK13383 338 ADLRDAPE--------TVGKPVAGCPVRILD-RNNRPVGPRVTGRIFVGGELAGTRYTDGGGKAV----VDGMTSTGDMG 404
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 496 LMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQEAQVVGVKDERMGEEICACIRLKSGETTTAEEIKAFCKG 575
Cdd:PRK13383 405 YLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPGSGVDAAQLRDYLKD 484
|
570 580 590
....*....|....*....|....*....|....
gi 24418933 576 KISHFKIPRYIVFVEGYPLTISGKIqkfkLREQM 609
Cdd:PRK13383 485 RVSRFEQPRDINIVSSIPRNPTGKV----LRKEL 514
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
80-605 |
1.18e-39 |
|
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: 150.93 E-value: 1.18e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 80 ATAQRFPDREALVILHEniRLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVSVNPAYQ 159
Cdd:cd12115 7 AQAARTPDAIALVCGDE--SLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 160 SSELEYVLRKVGCKgivfpkqfktqqyydilkqvcpelekaqpgalkserlpdlttvisvdaplpgtLLLDDivaaggke 239
Cdd:cd12115 85 PERLRFILEDAQAR-----------------------------------------------------LVLTD-------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 240 qnLAQLRYnqrflscydpinIQFTSGTTGNPKGATLSHHNIVNnsmLIgqRLKMPTKTAEELRLVLPS------------ 307
Cdd:cd12115 104 --PDDLAY------------VIYTSGSTGRPKGVAIEHRNAAA---FL--QWAAAAFSAEELAGVLAStsicfdlsvfel 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 308 --PLyhclgSVGGTMVsMMHGATLLLSSPSfngkkaleaisREKGTLLYGTPTMFVDILNQPDFSsydfTSIRGGVIAGS 385
Cdd:cd12115 165 fgPL-----ATGGKVV-LADNVLALPDLPA-----------AAEVTLINTVPSAAAELLRHDALP----ASVRVVNLAGE 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 386 PAPPELIRAIINKMNMKELVVVYGTTENSpvTFMNF-PEDTLEQKAGSVGRIMPHTEAQIVNvETGELTNLNVPGELYIR 464
Cdd:cd12115 224 PLPRDLVQRLYARLQVERVVNLYGPSEDT--TYSTVaPVPPGASGEVSIGRPLANTQAYVLD-RALQPVPLGVPGELYIG 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 465 GYCVMQGYWGEPQKTFETVGQD------KWYRTGDIALMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQEA 538
Cdd:cd12115 301 GAGVARGYLGRPGLTAERFLPDpfgpgaRLYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREA 380
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24418933 539 QVVGVKDERMGEEICACIRLKSGETTTAEEIKAFCKGKISHFKIPRYIVFVEGYPLTISGKIQKFKL 605
Cdd:cd12115 381 VVVAIGDAAGERRLVAYIVAEPGAAGLVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
256-598 |
1.60e-39 |
|
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: 147.83 E-value: 1.60e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 256 DPINIQFTSGTTGNPKGATLSHHNIVNNSMLIGQRLKMptktAEELRLVLPSPLYHcLGSVGGTMVSMMHGATLLLSsPS 335
Cdd:cd17636 1 DPVLAIYTAAFSGRPNGALLSHQALLAQALVLAVLQAI----DEGTVFLNSGPLFH-IGTLMFTLATFHAGGTNVFV-RR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 336 FNGKKALEAISREKGTLLYGTPTMFVDILNQPDFSSYDFTSIRGGVIA------GSPAPPELIRAIINkmnmkelvvvYG 409
Cdd:cd17636 75 VDAEEVLELIEAERCTHAFLLPPTIDQIVELNADGLYDLSSLRSSPAApewndmATVDTSPWGRKPGG----------YG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 410 TTENS-PVTFMNFPEDTleqkAGSVGRIMPHTEAQIVN-----VETGEltnlnvPGELYIRGYCVMQGYWGEPQKTFETV 483
Cdd:cd17636 145 QTEVMgLATFAALGGGA----IGGAGRPSPLVQVRILDedgreVPDGE------VGEIVARGPTVMAGYWNRPEVNARRT 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 484 gQDKWYRTGDIALMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQEAQVVGVKDERMGEEICACIRLKSGET 563
Cdd:cd17636 215 -RGGWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPGAS 293
|
330 340 350
....*....|....*....|....*....|....*
gi 24418933 564 TTAEEIKAFCKGKISHFKIPRYIVFVEGYPLTISG 598
Cdd:cd17636 294 VTEAELIEHCRARIASYKKPKSVEFADALPRTAGG 328
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
254-599 |
4.50e-39 |
|
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: 147.14 E-value: 4.50e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 254 CYDPINIQFTSGTTGNPKGATLSHHNIVnnSMLIGQRLKM-PTKT-----------AEELRLVLPSPLYHCLGSVGGtMV 321
Cdd:cd05924 2 SADDLYILYTGGTTGMPKGVMWRQEDIF--RMLMGGADFGtGEFTpsedahkaaaaAAGTVMFPAPPLMHGTGSWTA-FG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 322 SMMHGATLLLSSPSFNGKKALEAISREKGTLLygtpTMFVDILNQP------DFSSYDFTSIRGGVIAGSPAPPELIRAI 395
Cdd:cd05924 79 GLLGGQTVVLPDDRFDPEEVWRTIEKHKVTSM----TIVGDAMARPlidalrDAGPYDLSSLFAISSGGALLSPEVKQGL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 396 INKMNMKELVVVYGTTENSpvtFMNFPEDTlEQKAGSVGRIMPHTEAQIVNVETGELT-NLNVPGELYIRGYcVMQGYWG 474
Cdd:cd05924 155 LELVPNITLVDAFGSSETG---FTGSGHSA-GSGPETGPFTRANPDTVVLDDDGRVVPpGSGGVGWIARRGH-IPLGYYG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 475 EPQK---TFETVGQDKWYRTGDIALMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQEAQVVGVKDERMGEE 551
Cdd:cd05924 230 DEAKtaeTFPEVDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQE 309
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 24418933 552 ICACIRLKSGETTTAEEIKAFCKGKISHFKIPRYIVFVEGYPLTISGK 599
Cdd:cd05924 310 VVAVVQLREGAGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
82-600 |
6.38e-39 |
|
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: 149.80 E-value: 6.38e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 82 AQRFPDREALVilHENIRLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVSVNPAYQSS 161
Cdd:cd17651 5 AARTPDAPALV--AEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 162 ELEYvlrkvgckgivfpkqfktqqyydILKQVCPELEKAQPGALkserlPDLTTVISVDAPLPGTLLLDDIVAAGGKEQN 241
Cdd:cd17651 83 RLAF-----------------------MLADAGPVLVLTHPALA-----GELAVELVAVTLLDQPGAAAGADAEPDPALD 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 242 LAQLRYnqrflscydpinIQFTSGTTGNPKGATLSHHNIVNnsmLIG---QRLKMPTktaeELRLVLPSPLyhclG---S 315
Cdd:cd17651 135 ADDLAY------------VIYTSGSTGRPKGVVMPHRSLAN---LVAwqaRASSLGP----GARTLQFAGL----GfdvS 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 316 VGGTMVSMMHGATLLLSSPSF-NGKKALEAISREKG-TLLYGTPTMFVDILNQPDFSSYDFTSIRGGVIAGSPAPP-ELI 392
Cdd:cd17651 192 VQEIFSTLCAGATLVLPPEEVrTDPPALAAWLDEQRiSRVFLPTVALRALAEHGRPLGVRLAALRYLLTGGEQLVLtEDL 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 393 RAIINKMNMKELVVVYGTTENSPVTFMNFPEDTLEQKA-GSVGRIMPHTEAQIVNvETGELTNLNVPGELYIRGYCVMQG 471
Cdd:cd17651 272 REFCAGLPGLRLHNHYGPTETHVVTALSLPGDPAAWPApPPIGRPIDNTRVYVLD-AALRPVPPGVPGELYIGGAGLARG 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 472 YWGEPQKTFET------VGQDKWYRTGDIALMDEQGFCKIVGRSKDMI-IRGgENIYPAELEDFFLKHPQVQEAQVVGVK 544
Cdd:cd17651 351 YLNRPELTAERfvpdpfVPGARMYRTGDLARWLPDGELEFLGRADDQVkIRG-FRIELGEIEAALARHPGVREAVVLARE 429
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 24418933 545 DERMGEEICACIRLKSGETTTAEEIKAFCKGKISHFKIPRYIVFVEGYPLTISGKI 600
Cdd:cd17651 430 DRPGEKRLVAYVVGDPEAPVDAAELRAALATHLPEYMVPSAFVLLDALPLTPNGKL 485
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
82-607 |
3.54e-38 |
|
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: 147.47 E-value: 3.54e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 82 AQRFPDREALVIlhENIRLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVSVNPAYQSS 161
Cdd:cd17655 7 AEKTPDHTAVVF--EDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 162 ELEYVLRKVGCKGIVFPKQFKtqqyydilkqvcpelekaqpgalksERLPDLTTVISVDaplpgtlllDDIVAAGGKEQ- 240
Cdd:cd17655 85 RIQYILEDSGADILLTQSHLQ-------------------------PPIAFIGLIDLLD---------EDTIYHEESENl 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 241 ----NLAQLRYnqrflscydpinIQFTSGTTGNPKGATLSHHNIVNNSMLIGQRLKMptktAEELRLVLPSPLYHCLgSV 316
Cdd:cd17655 131 epvsKSDDLAY------------VIYTSGSTGKPKGVMIEHRGVVNLVEWANKVIYQ----GEHLRVALFASISFDA-SV 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 317 GGTMVSMMHGATLLLS--SPSFNGKKALEAISREKGTLLYGTPTmFVDILNQPDFSsyDFTSIRGGVIAGSPAPPELIRA 394
Cdd:cd17655 194 TEIFASLLSGNTLYIVrkETVLDGQALTQYIRQNRITIIDLTPA-HLKLLDAADDS--EGLSLKHLIVGGEALSTELAKK 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 395 IINKMNMK-ELVVVYGTTENSpVTFMNFPEDTLEQKAGSV--GRIMPHTEAQIVNvETGELTNLNVPGELYIRGYCVMQG 471
Cdd:cd17655 271 IIELFGTNpTITNAYGPTETT-VDASIYQYEPETDQQVSVpiGKPLGNTRIYILD-QYGRPQPVGVAGELYIGGEGVARG 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 472 YWGEPQKTFET------VGQDKWYRTGDIALMDEQGFCKIVGRSKDMI-IRgGENIYPAELEDFFLKHPQVQEAQVVGVK 544
Cdd:cd17655 349 YLNRPELTAEKfvddpfVPGERMYRTGDLARWLPDGNIEFLGRIDHQVkIR-GYRIELGEIEARLLQHPDIKEAVVIARK 427
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24418933 545 DERMGEEICACIrlKSGETTTAEEIKAFCKGKISHFKIPRYIVFVEGYPLTISGKIQKFKLRE 607
Cdd:cd17655 428 DEQGQNYLCAYI--VSEKELPVAQLREFLARELPDYMIPSYFIKLDEIPLTPNGKVDRKALPE 488
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
256-602 |
3.94e-38 |
|
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: 143.94 E-value: 3.94e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 256 DPINIQFTSGTTGNPKGATLSHHNIVNNSMLIGQRLKmpTKTAEELrLVLPSPLYHCLGSVGGTMvSMMHGATLLLSSPS 335
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGL--NWVVGDV-TYLPLPATHIGGLWWILT-CLIHGGLCVTGGEN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 336 FNGKKALEAISREKGTLLYGTPTMFVDILNQPDFSSYDFTSIRGgVIAGSPAPPELIRAIINKMNMKELVVVYGTTENSP 415
Cdd:cd17635 78 TTYKSLFKILTTNAVTTTCLVPTLLSKLVSELKSANATVPSLRL-IGYGGSRAIAADVRFIEATGLTNTAQVYGLSETGT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 416 VTFMNFPEDTLEqkAGSVGRIMPHTEAQIVNVETGELTNlNVPGELYIRGYCVMQGYWGEPQKTFEtVGQDKWYRTGDIA 495
Cdd:cd17635 157 ALCLPTDDDSIE--INAVGRPYPGVDVYLAATDGIAGPS-ASFGTIWIKSPANMLGYWNNPERTAE-VLIDGWVNTGDLG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 496 LMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQEAQVVGVKDERMGEEICACIrLKSGE--TTTAEEIKAFC 573
Cdd:cd17635 233 ERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAV-VASAEldENAIRALKHTI 311
|
330 340
....*....|....*....|....*....
gi 24418933 574 KGKISHFKIPRYIVFVEGYPLTISGKIQK 602
Cdd:cd17635 312 RRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
70-599 |
5.23e-38 |
|
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: 151.16 E-value: 5.23e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 70 VNTTVGECLDATAQRFPDREALVilHENIRLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGI 149
Cdd:COG1020 474 ADATLHELFEAQAARTPDAVAVV--FGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGA 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 150 ILVSVNPAYQSSELEYVLRKVGCKGIVfpkqfkTQQyydilkqvcpelekaqpgALKsERLPDLT-TVISVDAPLPGTLL 228
Cdd:COG1020 552 AYVPLDPAYPAERLAYMLEDAGARLVL------TQS------------------ALA-ARLPELGvPVLALDALALAAEP 606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 229 LDDIVAAGGkEQNLAqlrynqrflscYdpinIQFTSGTTGNPKGATLSHHNIVNNSMLIGQRLKMptktAEELRLVLPSP 308
Cdd:COG1020 607 ATNPPVPVT-PDDLA-----------Y----VIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGL----GPGDRVLQFAS 666
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 309 lyhcLG---SVGGTMVSMMHGATLLLSSPS--FNGKKALEAISREKGTLLYGTPTMF---VDILNQpdfssyDFTSIRGG 380
Cdd:COG1020 667 ----LSfdaSVWEIFGALLSGATLVLAPPEarRDPAALAELLARHRVTVLNLTPSLLralLDAAPE------ALPSLRLV 736
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 381 VIAGSPAPPELIRAIINKMNMKELVVVYGTTENS-PVTFMNFPEDTLEQKAGSVGRIMPHTEAQIVNvETGELTNLNVPG 459
Cdd:COG1020 737 LVGGEALPPELVRRWRARLPGARLVNLYGPTETTvDSTYYEVTPPDADGGSVPIGRPIANTRVYVLD-AHLQPVPVGVPG 815
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 460 ELYIRGYCVMQGYWGEPQKT--------FETVGQdKWYRTGDIALMDEQG---FckiVGRSKDMI-IRGgeniY---PAE 524
Cdd:COG1020 816 ELYIGGAGLARGYLNRPELTaerfvadpFGFPGA-RLYRTGDLARWLPDGnleF---LGRADDQVkIRG----FrieLGE 887
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24418933 525 LEDFFLKHPQVQEAQVVGVKDERMGEEICACIRLKSGETTTAEEIKAFCKGKISHFKIPRYIVFVEGYPLTISGK 599
Cdd:COG1020 888 IEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGK 962
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
256-600 |
7.12e-38 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 150.50 E-value: 7.12e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 256 DPINIQFTSGTTGNPKGATLSHHNIVNNSMLIGQRLkmPTKTAEELRLVLpsPLYHCLGSVGGTMVSMMHGA-TLLLSSP 334
Cdd:PRK06814 794 DPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARI--DFSPEDKVFNAL--PVFHSFGLTGGLVLPLLSGVkVFLYPSP 869
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 335 sFNGKKALEAISREKGTLLYGTPTMFVDILNQPDfsSYDFTSIRgGVIAGSpappELIRAIINKMNMKELVV----VYGT 410
Cdd:PRK06814 870 -LHYRIIPELIYDTNATILFGTDTFLNGYARYAH--PYDFRSLR-YVFAGA----EKVKEETRQTWMEKFGIrileGYGV 941
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 411 TENSPVTFMNFPedtLEQKAGSVGRIMPHTEAQIVNVEtgeltNLNVPGELYIRGYCVMQGYW-GEPQKTFEtVGQDKWY 489
Cdd:PRK06814 942 TETAPVIALNTP---MHNKAGTVGRLLPGIEYRLEPVP-----GIDEGGRLFVRGPNVMLGYLrAENPGVLE-PPADGWY 1012
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 490 RTGDIALMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFF-LKHPQVQEAqVVGVKDERMGEEIcacIRLKSGETTTAEE 568
Cdd:PRK06814 1013 DTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAaELWPDALHA-AVSIPDARKGERI---ILLTTASDATRAA 1088
|
330 340 350
....*....|....*....|....*....|...
gi 24418933 569 IKAFCKGK-ISHFKIPRYIVFVEGYPLTISGKI 600
Cdd:PRK06814 1089 FLAHAKAAgASELMVPAEIITIDEIPLLGTGKI 1121
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
73-600 |
1.33e-37 |
|
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: 147.34 E-value: 1.33e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 73 TVGECLDATAQRFPDREALVILHENI----RLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAG 148
Cdd:cd17634 54 LAANALDRHLRENGDRTAIIYEGDDTsqsrTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIG 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 149 IILVSVNPAYQSSELEYVLRKVGCKGIVFPKQF-KTQQYYDILKQVCpelEKAQPGAlkserlPDLTTVISVD---APLP 224
Cdd:cd17634 134 AVHSVIFGGFAPEAVAGRIIDSSSRLLITADGGvRAGRSVPLKKNVD---DALNPNV------TSVEHVIVLKrtgSDID 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 225 GT----LLLDDIVAAGGKEQNLAQLrynqrflSCYDPINIQFTSGTTGNPKGATLSHHNivnnsmligqrlkMPTKTAEE 300
Cdd:cd17634 205 WQegrdLWWRDLIAKASPEHQPEAM-------NAEDPLFILYTSGTTGKPKGVLHTTGG-------------YLVYAATT 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 301 LRLVL---PSPLYHCLGSVGGTMV-------SMMHGATLLLSSPSFNGKKA---LEAISREKGTLLYGTPTMFVDILNQP 367
Cdd:cd17634 265 MKYVFdygPGDIYWCTADVGWVTGhsyllygPLACGATTLLYEGVPNWPTParmWQVVDKHGVNILYTAPTAIRALMAAG 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 368 D--FSSYDFTSIRGGVIAGSPAPPELIRAIINKMNMKELVVV--YGTTENSPVTFMNFPeDTLEQKAGSVGRIMPHTEAQ 443
Cdd:cd17634 345 DdaIEGTDRSSLRILGSVGEPINPEAYEWYWKKIGKEKCPVVdtWWQTETGGFMITPLP-GAIELKAGSATRPVFGVQPA 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 444 IVN-----VETGELTNLNV----PGElyirgycvMQGYWGEPQKTFETVGQ--DKWYRTGDIALMDEQGFCKIVGRSKDM 512
Cdd:cd17634 424 VVDneghpQPGGTEGNLVItdpwPGQ--------TRTLFGDHERFEQTYFStfKGMYFSGDGARRDEDGYYWITGRSDDV 495
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 513 IIRGGENIYPAELEDFFLKHPQVQEAQVVGVKDERMGEEICACIRLKSGET---TTAEEIKAFCKGKISHFKIPRYIVFV 589
Cdd:cd17634 496 INVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLNHGVEpspELYAELRNWVRKEIGPLATPDVVHWV 575
|
570
....*....|.
gi 24418933 590 EGYPLTISGKI 600
Cdd:cd17634 576 DSLPKTRSGKI 586
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
75-600 |
1.47e-37 |
|
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: 145.88 E-value: 1.47e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 75 GECLDATAQRFPDREALVilHENIRLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVSV 154
Cdd:cd17646 1 HALVAEQAARTPDAPAVV--DEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 155 NPAYQSSELEYVLRKVGckgivfpkqfktqqyydilkqvcPELEKAQPGAlkSERLPDLTTVISVDAPLPGTLLLDD-IV 233
Cdd:cd17646 79 DPGYPADRLAYMLADAG-----------------------PAVVLTTADL--AARLPAGGDVALLGDEALAAPPATPpLV 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 234 AAGGkeQNLAQLRYnqrflscydpiniqfTSGTTGNPKGATLSHHNIVNNsmLIGQRLKMPTkTAEElRLVLPSPlyhcL 313
Cdd:cd17646 134 PPRP--DNLAYVIY---------------TSGSTGRPKGVMVTHAGIVNR--LLWMQDEYPL-GPGD-RVLQKTP----L 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 314 G---SVGGTMVSMMHGATLLLSSPSFNGKKA--LEAISREKGTLLYGTPTMFVDILNQPDFSSYdfTSIRGGVIAGSPAP 388
Cdd:cd17646 189 SfdvSVWELFWPLVAGARLVVARPGGHRDPAylAALIREHGVTTCHFVPSMLRVFLAEPAAGSC--ASLRRVFCSGEALP 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 389 PELIRAIINKMNMkELVVVYGTTENSpVTFMNFPEDTlEQKAGSV--GRIMPHTEAQIVNvETGELTNLNVPGELYIRGY 466
Cdd:cd17646 267 PELAARFLALPGA-ELHNLYGPTEAA-IDVTHWPVRG-PAETPSVpiGRPVPNTRLYVLD-DALRPVPVGVPGELYLGGV 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 467 CVMQGYWGEPQKTFETVGQD------KWYRTGDIALMDEQGFCKIVGRSKDMI-IRgGENIYPAELEDFFLKHPQVQEAQ 539
Cdd:cd17646 343 QLARGYLGRPALTAERFVPDpfgpgsRMYRTGDLARWRPDGALEFLGRSDDQVkIR-GFRVEPGEIEAALAAHPAVTHAV 421
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24418933 540 VVGVKDERMGEEICACIRLKSGETT-TAEEIKAFCKGKISHFKIPRYIVFVEGYPLTISGKI 600
Cdd:cd17646 422 VVARAAPAGAARLVGYVVPAAGAAGpDTAALRAHLAERLPEYMVPAAFVVLDALPLTANGKL 483
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
65-602 |
2.85e-36 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 146.07 E-value: 2.85e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 65 TDSHLVNTTVGECLDATAQRFPDREALVIlhENIRLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLAT 144
Cdd:PRK12467 505 PATEYAPDCVHQLIEAQARQHPERPALVF--GEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAV 582
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 145 AQAGIILVSVNPAYQSSELEYVLRKVGCKgivfpkqfktqqyydilkqvcpeLEKAQPGALKSERLPDLTTVISVDAPLP 224
Cdd:PRK12467 583 LKAGGAYVPLDPEYPQDRLAYMLDDSGVR-----------------------LLLTQSHLLAQLPVPAGLRSLCLDEPAD 639
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 225 gtlllddiVAAGGKEQNlAQLRYNQRFLsCYdpinIQFTSGTTGNPKGATLSHHNIVNNSMLIGQRLKMptkTAEELRLV 304
Cdd:PRK12467 640 --------LLCGYSGHN-PEVALDPDNL-AY----VIYTSGSTGQPKGVAISHGALANYVCVIAERLQL---AADDSMLM 702
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 305 LPSPLYhclgSVGGTM--VSMMHGATLLLSSP--SFNGKKALEAISREKGTLLYGTPTMFVDILNQPdfSSYDFTSIRGG 380
Cdd:PRK12467 703 VSTFAF----DLGVTElfGALASGATLHLLPPdcARDAEAFAALMADQGVTVLKIVPSHLQALLQAS--RVALPRPQRAL 776
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 381 VIAGSPAPPELIRAIINKMNMKELVVVYGTTENS-PVTFMNFPEDTLEQKAGSVGRIMPHTEAQIVNVETGELTnLNVPG 459
Cdd:PRK12467 777 VCGGEALQVDLLARVRALGPGARLINHYGPTETTvGVSTYELSDEERDFGNVPIGQPLANLGLYILDHYLNPVP-VGVVG 855
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 460 ELYIRGYCVMQGYWGEPQKT--------FETVGQdKWYRTGDIALMDEQGFCKIVGRSKDMI-IRgGENIYPAELEDFFL 530
Cdd:PRK12467 856 ELYIGGAGLARGYHRRPALTaerfvpdpFGADGG-RLYRTGDLARYRADGVIEYLGRMDHQVkIR-GFRIELGEIEARLL 933
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24418933 531 KHPQVQEAQVVGVKDERMGEEICACIRLKSGETT----TAEEIKAFCKGKISHFKIPRYIVFVEGYPLTISGKIQK 602
Cdd:PRK12467 934 AQPGVREAVVLAQPGDAGLQLVAYLVPAAVADGAehqaTRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDR 1009
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
74-606 |
3.05e-34 |
|
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: 137.62 E-value: 3.05e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 74 VGECLDATAQRFPDREALVilHENIR-----LNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAG 148
Cdd:cd05968 63 VEQLLDKWLADTRTRPALR--WEGEDgtsrtLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIG 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 149 IILVSVNPAYQSSELEYVLRKVGCKGIVFPKQFKTQqyyDILKQVCPELEKAqpgalkSERLPDLTTVISV---DAPLPG 225
Cdd:cd05968 141 GIVVPIFSGFGKEAAATRLQDAEAKALITADGFTRR---GREVNLKEEADKA------CAQCPTVEKVVVVrhlGNDFTP 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 226 TLLlDDIVAAGGKEQNLAQLRYnqrfLSCYDPINIQFTSGTTGNPKGATLSHhnivnnsmligqrLKMPTKTAEELrlvl 305
Cdd:cd05968 212 AKG-RDLSYDEEKETAGDGAER----TESEDPLMIIYTSGTTGKPKGTVHVH-------------AGFPLKAAQDM---- 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 306 psplYHCLGSVGGTMVS-------MM----------HGATLLL--SSPSFNGKKAL-EAISREKGTLLYGTPTMFVDILN 365
Cdd:cd05968 270 ----YFQFDLKPGDLLTwftdlgwMMgpwlifggliLGATMVLydGAPDHPKADRLwRMVEDHEITHLGLSPTLIRALKP 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 366 QPD--FSSYDFTSIRGGVIAGSPAPPELIRAIINKMNMKELVVV-Y-GTTENSPVTFMNFPEDTLeqKAGSVGRIMPHTE 441
Cdd:cd05968 346 RGDapVNAHDLSSLRVLGSTGEPWNPEPWNWLFETVGKGRNPIInYsGGTEISGGILGNVLIKPI--KPSSFNGPVPGMK 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 442 AQIVNvETGELTNLNVpGELYIRGYCV--MQGYWGEPQKTFETVGQ---DKWYRtGDIALMDEQGFCKIVGRSKDMIIRG 516
Cdd:cd05968 424 ADVLD-ESGKPARPEV-GELVLLAPWPgmTRGFWRDEDRYLETYWSrfdNVWVH-GDFAYYDEEGYFYILGRSDDTINVA 500
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 517 GENIYPAELEDFFLKHPQVQEAQVVGVKDERMGEEICACIRLKSGETTT---AEEIKAFCKGKISHFKIPRYIVFVEGYP 593
Cdd:cd05968 501 GKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVLKPGVTPTealAEELMERVADELGKPLSPERILFVKDLP 580
|
570
....*....|...
gi 24418933 594 LTISGKIQKFKLR 606
Cdd:cd05968 581 KTRNAKVMRRVIR 593
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
79-602 |
4.51e-34 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 139.71 E-value: 4.51e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 79 DATAQRFPdrEALVILHENIRLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVSVNPAY 158
Cdd:PRK12316 518 EEQVERTP--EAPALAFGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEY 595
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 159 QSSELEYVLRKVGCKGIVfpkqfkTQQYydilkqVCPELEkaqpgalkserLPDLTTVISVDAPlpgTLLLDdivaaGGK 238
Cdd:PRK12316 596 PAERLAYMLEDSGVQLLL------SQSH------LGRKLP-----------LAAGVQVLDLDRP---AAWLE-----GYS 644
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 239 EQNLAQlrynqrflsCYDPIN---IQFTSGTTGNPKGATLSHHNIVNNSMLIGQRLKMPTKTAeelrlVLPSPLYHCLGS 315
Cdd:PRK12316 645 EENPGT---------ELNPENlayVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDT-----VLQKTPFSFDVS 710
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 316 VGGTMVSMMHGATLLLSSPS--FNGKKALEAISREKGTLLYGTPTMFVDILNQPDFSSydFTSIRGGVIAGSPAPPELIR 393
Cdd:PRK12316 711 VWEFFWPLMSGARLVVAAPGdhRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVAS--CTSLRRIVCSGEALPADAQE 788
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 394 AIINKMNMKELVVVYGTTENS-PVTFmnfpEDTLEQKAGSV--GRIMPHTEAQIVNVEtGELTNLNVPGELYIRGYCVMQ 470
Cdd:PRK12316 789 QVFAKLPQAGLYNLYGPTEAAiDVTH----WTCVEEGGDSVpiGRPIANLACYILDAN-LEPVPVGVLGELYLAGRGLAR 863
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 471 GYWGEPQKTFET------VGQDKWYRTGDIALMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQEAQVVGVK 544
Cdd:PRK12316 864 GYHGRPGLTAERfvpspfVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD 943
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 24418933 545 dermGEEICACIRLKSGETTTAEEIKAFCKGKISHFKIPRYIVFVEGYPLTISGKIQK 602
Cdd:PRK12316 944 ----GKQLVGYVVLESEGGDWREALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDR 997
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
256-606 |
1.59e-33 |
|
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: 133.41 E-value: 1.59e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 256 DPINIQFTSGTTGNPKGAtlshhnIVNNSMLIGQRLKMptKTAEELRlvlPSPLYHCLGSVG---GTMVSMMhgATLLLS 332
Cdd:cd05973 89 DPFVMMFTSGTTGLPKGV------PVPLRALAAFGAYL--RDAVDLR---PEDSFWNAADPGwayGLYYAIT--GPLALG 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 333 SPS------FNGKKALEAISREKGTLLYGTPTMFVDILNQPDFSSYDFT-SIRGGVIAGSPAPPELIRAIINKMNmkelV 405
Cdd:cd05973 156 HPTilleggFSVESTWRVIERLGVTNLAGSPTAYRLLMAAGAEVPARPKgRLRRVSSAGEPLTPEVIRWFDAALG----V 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 406 VV---YGTTE-NSPVTFMNFPEDTLeqKAGSVGRIMPHTEAQIVNVETGELTNlNVPGELYI--RGYCVM--QGYWGEPQ 477
Cdd:cd05973 232 PIhdhYGQTElGMVLANHHALEHPV--HAGSAGRAMPGWRVAVLDDDGDELGP-GEPGRLAIdiANSPLMwfRGYQLPDT 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 478 KTFEtvgqDKWYRTGDIALMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQEAQVVGVKDERMGEEICACIR 557
Cdd:cd05973 309 PAID----GGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVV 384
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 24418933 558 LKSGETTT---AEEIKAFCKGKISHFKIPRYIVFVEGYPLTISGKIQKFKLR 606
Cdd:cd05973 385 LRGGHEGTpalADELQLHVKKRLSAHAYPRTIHFVDELPKTPSGKIQRFLLR 436
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
100-542 |
2.07e-33 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.
Pssm-ID: 341250 [Multi-domain] Cd Length: 545 Bit Score: 134.65 E-value: 2.07e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 100 LNFAQLKEEVDKAASGLLSIGLR--KGDRLGMWGPNSYAWVLIQLATAQAGIILVsvnPAYQSSELE---YVLRKVGCKG 174
Cdd:cd05927 6 ISYKEVAERADNIGSALRSLGGKpaPASFVGIYSINRPEWIISELACYAYSLVTV---PLYDTLGPEaieYILNHAEISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 175 IVFPKQFKTQQYYDILKQVCPELEKAQPGALKserlpDLTTVisvdaplpgtlllddivaaggkeqnlaqlrynqrflsC 254
Cdd:cd05927 83 VFCDAGVKVYSLEEFEKLGKKNKVPPPPPKPE-----DLATI-------------------------------------C 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 255 YdpiniqfTSGTTGNPKGATLSHHNIVNNSMLIGQRLKMPTKTAEELRLVLPSPLYHCLGSVGgTMVSMMHGATLLLSSP 334
Cdd:cd05927 121 Y-------TSGTTGNPKGVMLTHGNIVSNVAGVFKILEILNKINPTDVYISYLPLAHIFERVV-EALFLYHGAKIGFYSG 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 335 sfNGKKALEAISREKGTLLYGTPTMFVDIlnqpdfssydFTSIRGGVIAGSPappeLIRAIINK-MNMKE---------- 403
Cdd:cd05927 193 --DIRLLLDDIKALKPTVFPGVPRVLNRI----------YDKIFNKVQAKGP----LKRKLFNFaLNYKLaelrsgvvra 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 404 ---------------------LVVV------------------------YGTTENSPVTFMNFPEDTLeqkAGSVGRIMP 438
Cdd:cd05927 257 spfwdklvfnkikqalggnvrLMLTgsaplspevleflrvalgcpvlegYGQTECTAGATLTLPGDTS---VGHVGGPLP 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 439 HTEAQIVNV-ETGELTNLNVP-GELYIRGYCVMQGYWGEPQKTFETVGQDKWYRTGDIALMDEQGFCKIVGRSKDMI-IR 515
Cdd:cd05927 334 CAEVKLVDVpEMNYDAKDPNPrGEVCIRGPNVFSGYYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIFkLS 413
|
490 500
....*....|....*....|....*..
gi 24418933 516 GGENIYPAELEDFFLKHPQVQEAQVVG 542
Cdd:cd05927 414 QGEYVAPEKIENIYARSPFVAQIFVYG 440
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
256-609 |
2.07e-33 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 134.91 E-value: 2.07e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 256 DPINIQFTSGTTGNPKGATLSHHNIVNNSMLIgqrlkmptKTAEELRL------VLPSPLYHCLgSVGGTMVSMMHGATL 329
Cdd:PRK05620 182 TAAAICYSTGTTGAPKGVVYSHRSLYLQSLSL--------RTTDSLAVthgesfLCCVPIYHVL-SWGVPLAAFMSGTPL 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 330 LLSSPSFNGKKALEAISREKGTLLYGTPTMFVDILNQPDFSSYDFTSIRGGVIAGSPAPPELIRAIINKMNMkELVVVYG 409
Cdd:PRK05620 253 VFPGPDLSAPTLAKIIATAMPRVAHGVPTLWIQLMVHYLKNPPERMSLQEIYVGGSAVPPILIKAWEERYGV-DVVHVWG 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 410 TTENSPVTFMNFPEDTLEQKAG-----SVGRIMPHTEAQIVNV-ETGELTNLNvPGELYIRGYCVMQGYW-------GEP 476
Cdd:PRK05620 332 MTETSPVGTVARPPSGVSGEARwayrvSQGRFPASLEYRIVNDgQVMESTDRN-EGEIQVRGNWVTASYYhspteegGGA 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 477 QKTF---------ETVGQDKWYRTGDIALMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQEAQVVGVKDER 547
Cdd:PRK05620 411 ASTFrgedvedanDRFTADGWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDK 490
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24418933 548 MGEEICACIRLKSG---ETTTAEEIKAFCKGKISHFKIPRYIVFVEGYPLTISGKIQKFKLREQM 609
Cdd:PRK05620 491 WGERPLAVTVLAPGiepTRETAERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDLRQHL 555
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
86-606 |
2.88e-33 |
|
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: 132.88 E-value: 2.88e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 86 PDREALVilHENIRLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVSVNPAYQSSELEY 165
Cdd:cd17649 1 PDAVALV--FGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 166 VLRKVGCKgivfpkqfktqqyydilkqvcpelekaqpgalkserlpdlttvisvdaplpgtLLLddivAAGGKeqNLAQL 245
Cdd:cd17649 79 MLEDSGAG-----------------------------------------------------LLL----THHPR--QLAYV 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 246 RYnqrflscydpiniqfTSGTTGNPKGATLSHHNIVNNSMLIGQRLKMptkTAEELRLVLPSPLYHclGSVGGTMVSMMH 325
Cdd:cd17649 100 IY---------------TSGSTGTPKGVAVSHGPLAAHCQATAERYGL---TPGDRELQFASFNFD--GAHEQLLPPLIC 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 326 GATLLLSSPS-FNGKKAL-EAISREKGTLLYGTPT---MFVDILNqpDFSSYDFTSIRGGVIAGSPAPPELIRAIInkMN 400
Cdd:cd17649 160 GACVVLRPDElWASADELaEMVRELGVTVLDLPPAylqQLAEEAD--RTGDGRPPSLRLYIFGGEALSPELLRRWL--KA 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 401 MKELVVVYGTTENSpVTFMNFPEDTLEQKAGS---VGRIMPHTEAQIVNVETGELTNlNVPGELYIRGYCVMQGYWGEPQ 477
Cdd:cd17649 236 PVRLFNAYGPTEAT-VTPLVWKCEAGAARAGAsmpIGRPLGGRSAYILDADLNPVPV-GVTGELYIGGEGLARGYLGRPE 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 478 KTFETVGQD-------KWYRTGDIALMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQEAQVVGVkDERMGE 550
Cdd:cd17649 314 LTAERFVPDpfgapgsRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVAL-DGAGGK 392
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 24418933 551 EICACIRLKSGETTTA--EEIKAFCKGKISHFKIPRYIVFVEGYPLTISGKIQKFKLR 606
Cdd:cd17649 393 QLVAYVVLRAAAAQPElrAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKALP 450
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
86-600 |
5.11e-33 |
|
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: 132.39 E-value: 5.11e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 86 PDREALVilHENIRLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVSVNPAYQSSELEY 165
Cdd:cd12114 1 PDATAVI--CGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 166 VLRKVGCKGIVfpkqfktqqyydilkqVCpelekaQPGALKSERLPDLTTVISVDAPLPgtllldDIVAAGgkEQNLAQL 245
Cdd:cd12114 79 ILADAGARLVL----------------TD------GPDAQLDVAVFDVLILDLDALAAP------APPPPV--DVAPDDL 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 246 RYnqrflscydpinIQFTSGTTGNPKGATLSHHNIVNNSMLIGQRLKMptkTAEElRLVLPSPLYHCLgSVG---GTMVS 322
Cdd:cd12114 129 AY------------VIFTSGSTGTPKGVMISHRAALNTILDINRRFAV---GPDD-RVLALSSLSFDL-SVYdifGALSA 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 323 mmhGATLLLSSPSFNGKKA--LEAISREKGTLLYGTPTMFVDILNQPDFSSYDFTSIRGGVIAGSPAPPELIRAIINKMN 400
Cdd:cd12114 192 ---GATLVLPDEARRRDPAhwAELIERHGVTLWNSVPALLEMLLDVLEAAQALLPSLRLVLLSGDWIPLDLPARLRALAP 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 401 MKELVVVYGTTENSpVTFMNFPEDTLEQKAGSV--GRIMPHTEAQIVNvETGELTNLNVPGELYIRGYCVMQGYWGEPQK 478
Cdd:cd12114 269 DARLISLGGATEAS-IWSIYHPIDEVPPDWRSIpyGRPLANQRYRVLD-PRGRDCPDWVPGELWIGGRGVALGYLGDPEL 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 479 T---FETVGQD-KWYRTGDIALMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQEAQVVGVkDERMGEEICA 554
Cdd:cd12114 347 TaarFVTHPDGeRLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVL-GDPGGKRLAA 425
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 24418933 555 CIRLKSGETT-TAEEIKAFCKGKISHFKIPRYIVFVEGYPLTISGKI 600
Cdd:cd12114 426 FVVPDNDGTPiAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKV 472
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
67-611 |
3.01e-32 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 131.25 E-value: 3.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 67 SHLVNTTVGECLDATAQRFPDREALVILH--ENIRLNFAQLKEEVDKAASGLLSIGLRKGDRlgmwgpnsyawVLIQLAT 144
Cdd:cd05906 5 PEGAPRTLLELLLRAAERGPTKGITYIDAdgSEEFQSYQDLLEDARRLAAGLRQLGLRPGDS-----------VILQFDD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 145 AQ-----------AGIILVSVNPAYQSSELEYVLRKvgckgivfpkqfktqqyydiLKQVCPELEkaQPGALKSERL-PD 212
Cdd:cd05906 74 NEdfipafwacvlAGFVPAPLTVPPTYDEPNARLRK--------------------LRHIWQLLG--SPVVLTDAELvAE 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 213 LTTVISVDAPLPGTLLLDDIVAAGGKEQNLAQLRYNqrflscyDPINIQFTSGTTGNPKGATLSHHNIVnnSMLIG---- 288
Cdd:cd05906 132 FAGLETLSGLPGIRVLSIEELLDTAADHDLPQSRPD-------DLALLMLTSGSTGFPKAVPLTHRNIL--ARSAGkiqh 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 289 QRLkmptkTAEELRLVLpSPLYHclgsVGG----------TMVSMMHGAT-LLLSSPSfngkKALEAISREKGTLLYGtP 357
Cdd:cd05906 203 NGL-----TPQDVFLNW-VPLDH----VGGlvelhlravyLGCQQVHVPTeEILADPL----RWLDLIDRYRVTITWA-P 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 358 TMFVDILNQ----PDFSSYDFTSIRGGVIAGSPAPPELIRAIIN---KMNMKELVVV--YGTTEN-SPVTFMN-FPEDTL 426
Cdd:cd05906 268 NFAFALLNDlleeIEDGTWDLSSLRYLVNAGEAVVAKTIRRLLRllePYGLPPDAIRpaFGMTETcSGVIYSRsFPTYDH 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 427 EQKA--GSVGRIMPHTEAQIVNvETGELTNLNVPGELYIRGYCVMQGYWGEPQKTFETVGQDKWYRTGDIALMDEqGFCK 504
Cdd:cd05906 348 SQALefVSLGRPIPGVSMRIVD-DEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTEDGWFRTGDLGFLDN-GNLT 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 505 IVGRSKDMIIRGGENIYPAELEDFflkhpqVQEAQVV--------GVKDERMGEEICAC-----IRLKSGETTTAEEIka 571
Cdd:cd05906 426 ITGRTKDTIIVNGVNYYSHEIEAA------VEEVPGVepsftaafAVRDPGAETEELAIffvpeYDLQDALSETLRAI-- 497
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 24418933 572 fcKGKISH-FKI-PRYIVFV--EGYPLTISGKIQKFKLREQMEQ 611
Cdd:cd05906 498 --RSVVSReVGVsPAYLIPLpkEEIPKTSLGKIQRSKLKAAFEA 539
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
260-611 |
4.22e-32 |
|
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: 130.30 E-value: 4.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 260 IQFTSGTTGNPKGATLSHHNIVNNSMLIGQRLKMPTKTaeelRLVLPSPLYHCLGSVGGTMVSMMHGA-------TLLLS 332
Cdd:cd05908 111 IQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKD----RILSWMPLTHDMGLIAFHLAPLIAGMnqylmptRLFIR 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 333 SPSFNGKKAleaiSREKGTLLyGTPT----MFVDILNQPDFSSYDFTSIRGGVIAGSPAPPELIRAIINKM---NMKE-- 403
Cdd:cd05908 187 RPILWLKKA----SEHKATIV-SSPNfgykYFLKTLKPEKANDWDLSSIRMILNGAEPIDYELCHEFLDHMskyGLKRna 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 404 LVVVYGTTENS-------------PVTFMN--------FPEDTLEQKAG----SVGRIMPHTEAQIVNVETGELTNlNVP 458
Cdd:cd05908 262 ILPVYGLAEASvgaslpkaqspfkTITLGRrhvthgepEPEVDKKDSECltfvEVGKPIDETDIRICDEDNKILPD-GYI 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 459 GELYIRGYCVMQGYWGEPQKTFETVGQDKWYRTGDIALMdEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQEA 538
Cdd:cd05908 341 GHIQIRGKNVTPGYYNNPEATAKVFTDDGWLKTGDLGFI-RNGRLVITGREKDIIFVNGQNVYPHDIERIAEELEGVELG 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 539 QVV--GVKDERMGEEICACIRLKSgetTTAEEIKAFCKGKISH------FKIPRyIVFVEGYPLTISGKIQKFKLREQME 610
Cdd:cd05908 420 RVVacGVNNSNTRNEEIFCFIEHR---KSEDDFYPLGKKIKKHlnkrggWQINE-VLPIRRIPKTTSGKVKRYELAQRYQ 495
|
.
gi 24418933 611 Q 611
Cdd:cd05908 496 S 496
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
77-606 |
9.99e-32 |
|
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.
Pssm-ID: 341270 [Multi-domain] Cd Length: 608 Bit Score: 130.37 E-value: 9.99e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 77 CLDATAQRFPDREALVI----LHENIRLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILV 152
Cdd:cd05966 58 CLDRHLKERGDKVAIIWegdePDQSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHS 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 153 SVNPAYQSSELEYVLRKVGCKGIVFPKQFKTQQYYDILKQVCPElekaqpgALksERLPDLTTVISV-----DAPL-PG- 225
Cdd:cd05966 138 VVFAGFSAESLADRINDAQCKLVITADGGYRGGKVIPLKEIVDE-------AL--EKCPSVEKVLVVkrtggEVPMtEGr 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 226 TLLLDDIVAAggkeqnlaQLRYNQ-RFLSCYDPINIQFTSGTTGNPKGatlshhnIVNNS--MLIGqrlkmptkTAEELR 302
Cdd:cd05966 209 DLWWHDLMAK--------QSPECEpEWMDSEDPLFILYTSGSTGKPKG-------VVHTTggYLLY--------AATTFK 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 303 LVL---PSPLYHCLGSVG-------GTMVSMMHGATLLL--SSPSF-NGKKALEAISREKGTLLYGTPT---MFVDILNQ 366
Cdd:cd05966 266 YVFdyhPDDIYWCTADIGwitghsyIVYGPLANGATTVMfeGTPTYpDPGRYWDIVEKHKVTIFYTAPTairALMKFGDE 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 367 PdFSSYDFTSIR--GGViaGSPAPPELIRAIINKMNMKELVVV--YGTTENSPVTFMNFPEDTlEQKAGSVGRIMPHTEA 442
Cdd:cd05966 346 W-VKKHDLSSLRvlGSV--GEPINPEAWMWYYEVIGKERCPIVdtWWQTETGGIMITPLPGAT-PLKPGSATRPFFGIEP 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 443 QIVNVETGELTNlNVPGELYIR----GycVMQGYWGEPQKTFETVGQD--KWYRTGDIALMDEQGFCKIVGRSKDMIIRG 516
Cdd:cd05966 422 AILDEEGNEVEG-EVEGYLVIKrpwpG--MARTIYGDHERYEDTYFSKfpGYYFTGDGARRDEDGYYWITGRVDDVINVS 498
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 517 GENIYPAELEDFFLKHPQVQEAQVVGVKDERMGEEICACIRLKSGETTT---AEEIKAFCKGKISHFKIPRYIVFVEGYP 593
Cdd:cd05966 499 GHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGEEPSdelRKELRKHVRKEIGPIATPDKIQFVPGLP 578
|
570
....*....|...
gi 24418933 594 LTISGKIQKFKLR 606
Cdd:cd05966 579 KTRSGKIMRRILR 591
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
79-607 |
1.58e-31 |
|
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: 127.43 E-value: 1.58e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 79 DATAQRFPDreALVILHENIRLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVSVNPAY 158
Cdd:cd17653 4 ERIAAAHPD--AVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 159 QSSELEYVLRKVGCKGIVFPKqfktqqyydilkqvcpelekaqpgalkserlpdlttviSVDaplpgtlllddivaaggk 238
Cdd:cd17653 82 PSARIQAILRTSGATLLLTTD--------------------------------------SPD------------------ 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 239 eqnlaqlrynqrflscyDPINIQFTSGTTGNPKGATLSHHNIVNNSMLIGQRLKMptkTAEELRLVLPSPLYHClgSVGG 318
Cdd:cd17653 106 -----------------DLAYIIFTSGSTGIPKGVMVPHRGVLNYVSQPPARLDV---GPGSRVAQVLSIAFDA--CIGE 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 319 TMVSMMHGATLLLSSPSFNgkkaLEAISREKgTLLYGTPTmFVDILNqPDfssyDFTSIRGGVIAGSPAPPELI------ 392
Cdd:cd17653 164 IFSTLCNGGTLVLADPSDP----FAHVARTV-DALMSTPS-ILSTLS-PQ----DFPNLKTIFLGGEAVPPSLLdrwspg 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 393 RAIINkmnmkelvvVYGTTENSPVTFMnfpEDTLEQKAGSVGRIMPHTEAQIVNvETGELTNLNVPGELYIRGYCVMQGY 472
Cdd:cd17653 233 RRLYN---------AYGPTECTISSTM---TELLPGQPVTIGKPIPNSTCYILD-ADLQPVPEGVVGEICISGVQVARGY 299
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 473 WGEPQKTFETVGQDKW------YRTGDIALMDEQGFCKIVGRSKDMI-IRG-----GENIYPAELEDfflkhPQVQEAQV 540
Cdd:cd17653 300 LGNPALTASKFVPDPFwpgsrmYRTGDYGRWTEDGGLEFLGREDNQVkVRGfrinlEEIEEVVLQSQ-----PEVTQAAA 374
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24418933 541 VGVKDermgeEICACIrlkSGETTTAEEIKAFCKGKISHFKIPRYIVFVEGYPLTISGKIQKFKLRE 607
Cdd:cd17653 375 IVVNG-----RLVAFV---TPETVDVDGLRSELAKHLPSYAVPDRIIALDSFPLTANGKVDRKALRE 433
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
86-600 |
2.78e-31 |
|
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: 127.13 E-value: 2.78e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 86 PDREALVilHENIRLNFAQLKEEVDKAASGLLSIG-LRKGDRLGMWGPNSYAWVLIQLATAQAGIILVSVNPAYQSSELE 164
Cdd:cd17648 1 PDRVAVV--YGDKRLTYRELNERANRLAHYLLSVAeIRPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 165 YVLRKVGCKGIVfpkqfktqqyydilkqvcpelekaqpgalkserlpdlttvisvdaplpgtlllddivaaggkeQNLAQ 244
Cdd:cd17648 79 FILEDTGARVVI---------------------------------------------------------------TNSTD 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 245 LRYnqrflscydpinIQFTSGTTGNPKGATLSHHNIVNNSMLIGQRLKMPTKTAEELrLVLPSplYHCLGSVGGTMVSMM 324
Cdd:cd17648 96 LAY------------AIYTSGTTGKPKGVLVEHGSVVNLRTSLSERYFGRDNGDEAV-LFFSN--YVFDFFVEQMTLALL 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 325 HGATLLLSSPSFNGKKA--LEAISREKGTLLYGTPTmfvdILNQPDFSSydFTSIRGGVIAG---SPAPPELIRA----- 394
Cdd:cd17648 161 NGQKLVVPPDEMRFDPDrfYAYINREKVTYLSGTPS----VLQQYDLAR--LPHLKRVDAAGeefTAPVFEKLRSrfagl 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 395 IINKmnmkelvvvYGTTENSpVTFMNFPEDTLEQKAGSVGRIMPHTEAQIVNVETGELTnLNVPGELYIRGYCVMQGYWG 474
Cdd:cd17648 235 IINA---------YGPTETT-VTNHKRFFPGDQRFDKSLGRPVRNTKCYVLNDAMKRVP-VGAVGELYLGGDGVARGYLN 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 475 EPQKT--------FETVGQ------DKWYRTGDIALMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQEAQV 540
Cdd:cd17648 304 RPELTaerflpnpFQTEQErargrnARLYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAV 383
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24418933 541 VGVKDERMGEEICA----CIRLKSGETTTAEEIKAFCKGKISHFKIPRYIVFVEGYPLTISGKI 600
Cdd:cd17648 384 VAKEDASQAQSRIQkylvGYYLPEPGHVPESDLLSFLRAKLPRYMVPARLVRLEGIPVTINGKL 447
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
100-579 |
3.65e-31 |
|
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: 128.63 E-value: 3.65e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 100 LNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVSVNPAYQSSELEYVLRKvGCKGIVFpk 179
Cdd:cd05933 9 LTYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAET-SEANILV-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 180 qFKTQQYYDILKQVcpelekaqpgalkSERLPDLTTVISVDAPL----PGTLLLDDIVAaGGKEQNLAQLRY---NQRFL 252
Cdd:cd05933 86 -VENQKQLQKILQI-------------QDKLPHLKAIIQYKEPLkekePNLYSWDEFME-LGRSIPDEQLDAiisSQKPN 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 253 SCYDPIniqFTSGTTGNPKGATLSHHNIVNNSMLIGQRLKMptKTAEELRLVLPS--PLYHCLGSVGGTMVSMMHGATLL 330
Cdd:cd05933 151 QCCTLI---YTSGTTGMPKGVMLSHDNITWTAKAASQHMDL--RPATVGQESVVSylPLSHIAAQILDIWLPIKVGGQVY 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 331 LSSPSfNGKKALEAISRE-KGTLLYGTPTMFVDILNQPDFSSYDFTSIRGGVIA--------------GSPAPPELIRAI 395
Cdd:cd05933 226 FAQPD-ALKGTLVKTLREvRPTAFMGVPRVWEKIQEKMKAVGAKSGTLKRKIASwakgvgletnlklmGGESPSPLFYRL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 396 INKMNMKE----------------------------------LVVVYGTTENSPVTFMNFPEDTleqKAGSVGRIMPHTE 441
Cdd:cd05933 305 AKKLVFKKvrkalgldrcqkfftgaapisretlefflslnipIMELYGMSETSGPHTISNPQAY---RLLSCGKALPGCK 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 442 AQIVNvetgelTNLNVPGELYIRGYCVMQGYWGEPQKTFETVGQDKWYRTGDIALMDEQGFCKIVGRSKDMIIR-GGENI 520
Cdd:cd05933 382 TKIHN------PDADGIGEICFWGRHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKELIITaGGENV 455
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24418933 521 YPAELEDFFLKH-PQVQEAQVVGvkDERmgEEICACIRLK------SGETTTA--EEIKAFCKGKISH 579
Cdd:cd05933 456 PPVPIEDAVKKElPIISNAMLIG--DKR--KFLSMLLTLKcevnpeTGEPLDEltEEAIEFCRKLGSQ 519
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
256-607 |
1.19e-30 |
|
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: 124.99 E-value: 1.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 256 DPINIQFTSGTTGNPKGATLSHHNI----VNNSMLIGQRlkmptktAEELRLVLPSPLY--HCLGSVggtMVSMMHGATL 329
Cdd:cd05974 86 DPMLLYFTSGTTSKPKLVEHTHRSYpvghLSTMYWIGLK-------PGDVHWNISSPGWakHAWSCF---FAPWNAGATV 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 330 LL-SSPSFNGKKALEAISREKGTLLYGTPTMFvDILNQPDFSSYDfTSIRGGVIAGSPAPPELIRAIINKMNMKeLVVVY 408
Cdd:cd05974 156 FLfNYARFDAKRVLAALVRYGVTTLCAPPTVW-RMLIQQDLASFD-VKLREVVGAGEPLNPEVIEQVRRAWGLT-IRDGY 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 409 GTTENSpVTFMNFPEDTLeqKAGSVGRIMPHTEAQIVNVETGELTNlnvpGELYI-----RGYCVMQGYWGEPQKTFETV 483
Cdd:cd05974 233 GQTETT-ALVGNSPGQPV--KAGSMGRPLPGYRVALLDPDGAPATE----GEVALdlgdtRPVGLMKGYAGDPDKTAHAM 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 484 GqDKWYRTGDIALMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQEAQVVGVKDERMGEEICACIRLKSG-- 561
Cdd:cd05974 306 R-GGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGye 384
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 24418933 562 -ETTTAEEIKAFCKGKISHFKIPRYIVFVEgYPLTISGKIQKFKLRE 607
Cdd:cd05974 385 pSPETALEIFRFSRERLAPYKRIRRLEFAE-LPKTISGKIRRVELRR 430
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
100-542 |
2.85e-30 |
|
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: 124.89 E-value: 2.85e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 100 LNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVSVNPAYQSSELEYVLRKVGCKGIVFPK 179
Cdd:cd05932 7 FTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFVGK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 180 QfktqQYYDILKQVCPElekaqpgalkserlpdltTVISVDAPLPGTL----LLDDIVAAGGKEQNlAQLRYNQRFLScy 255
Cdd:cd05932 87 L----DDWKAMAPGVPE------------------GLISISLPPPSAAncqyQWDDLIAQHPPLEE-RPTRFPEQLAT-- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 256 dpinIQFTSGTTGNPKGATLSHhnivNNSMLIGQRLKMPTKTAEELRLVLPSPLYHCLGSVGGTMVSMMHGATLLL--SS 333
Cdd:cd05932 142 ----LIYTSGTTGQPKGVMLTF----GSFAWAAQAGIEHIGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVAFaeSL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 334 PSFngkkaLEAISREKGTLLYGTPTMFVD----------------ILNQPDFSSYDFTSIRGGV------IAGS---PAP 388
Cdd:cd05932 214 DTF-----VEDVQRARPTLFFSVPRLWTKfqqgvqdkipqqklnlLLKIPVVNSLVKRKVLKGLgldqcrLAGCgsaPVP 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 389 PELI---RAIinKMNMKElvvVYGTTENSPVTFMNFPEDtleQKAGSVGRIMPHTEAQIVNvetgeltnlnvPGELYIRG 465
Cdd:cd05932 289 PALLewyRSL--GLNILE---AYGMTENFAYSHLNYPGR---DKIGTVGNAGPGVEVRISE-----------DGEILVRS 349
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24418933 466 YCVMQGYWGEPQKTFETVGQDKWYRTGDIALMDEQGFCKIVGRSKDMI-IRGGENIYPAELEDFFLKHPQVQEAQVVG 542
Cdd:cd05932 350 PALMMGYYKDPEATAEAFTADGFLRTGDKGELDADGNLTITGRVKDIFkTSKGKYVAPAPIENKLAEHDRVEMVCVIG 427
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
81-605 |
5.17e-30 |
|
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: 123.05 E-value: 5.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 81 TAQRFPDREALVilHENIRLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVSVNPAYQS 160
Cdd:cd17645 7 QVERTPDHVAVV--DRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 161 SELEYVLRKVGCKGIVfpkqfktqqyydilkqvcpelekAQPGalkserlpDLTTVIsvdaplpgtlllddivaaggkeq 240
Cdd:cd17645 85 ERIAYMLADSSAKILL-----------------------TNPD--------DLAYVI----------------------- 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 241 nlaqlrynqrflscydpiniqFTSGTTGNPKGATLSHHNIVNNSMLIGQRLKMptkTAEELRLVLPSPLYHclGSVGGTM 320
Cdd:cd17645 111 ---------------------YTSGSTGLPKGVMIEHHNLVNLCEWHRPYFGV---TPADKSLVYASFSFD--ASAWEIF 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 321 VSMMHGATL-LLSSPSFNGKKALEAISREKGTLLYGTPTMFVDilnqpDFSSYDFTSIRGGVIAGSpappELIRAiinKM 399
Cdd:cd17645 165 PHLTAGAALhVVPSERRLDLDALNDYFNQEGITISFLPTGAAE-----QFMQLDNQSLRVLLTGGD----KLKKI---ER 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 400 NMKELVVVYGTTENSPVTFMnFPEDTLEQKAgSVGRIMPHTEAQIVNvETGELTNLNVPGELYIRGYCVMQGYWGEPQKT 479
Cdd:cd17645 233 KGYKLVNNYGPTENTVVATS-FEIDKPYANI-PIGKPIDNTRVYILD-EALQLQPIGVAGELCIAGEGLARGYLNRPELT 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 480 FET------VGQDKWYRTGDIALMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQEAQVVGVKDERMGEEIC 553
Cdd:cd17645 310 AEKfivhpfVPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLV 389
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 24418933 554 ACIRLKsgETTTAEEIKAFCKGKISHFKIPRYIVFVEGYPLTISGKIQKFKL 605
Cdd:cd17645 390 AYVTAP--EEIPHEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
112-608 |
1.23e-29 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 123.21 E-value: 1.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 112 AASGLLSIGLRKGDR---LGMWGPNSYAWVLIQLATAQAGIILVSVNPAYQSSELEYVLRKVGCKGIVfpkqfktqqyyd 188
Cdd:PRK13388 37 AARAAALIALADPDRplhVGVLLGNTPEMLFWLAAAALGGYVLVGLNTTRRGAALAADIRRADCQLLV------------ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 189 ilkqvcpeLEKAQPGALKSERLPDLTtVISVDAPLpgtllLDDIVAAGGKEQNLAQLRYNQRFLscydpinIQFTSGTTG 268
Cdd:PRK13388 105 --------TDAEHRPLLDGLDLPGVR-VLDVDTPA-----YAELVAAAGALTPHREVDAMDPFM-------LIFTSGTTG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 269 NPKGATLSHHNIVnnsmLIGQRLkmptktAEELRLV------LPSPLYHCLGSVGGTMVSMMHGATLLLSsPSFNGKKAL 342
Cdd:PRK13388 164 APKAVRCSHGRLA----FAGRAL------TERFGLTrddvcyVSMPLFHSNAVMAGWAPAVASGAAVALP-AKFSASGFL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 343 EAISREKGTLL-Y-GTPTMFvdILNQPDFSSYDFTSIRGGViaGSPAPPELIRAIINKMNMkELVVVYGTTENSPVTFM- 419
Cdd:PRK13388 233 DDVRRYGATYFnYvGKPLAY--ILATPERPDDADNPLRVAF--GNEASPRDIAEFSRRFGC-QVEDGYGSSEGAVIVVRe 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 420 -NFPEdtleqkaGSVGRimPHTEAQIVNVET------------GELTNLN-VPGELYIR-GYCVMQGYWGEPQKTFETVg 484
Cdd:PRK13388 308 pGTPP-------GSIGR--GAPGVAIYNPETltecavarfdahGALLNADeAIGELVNTaGAGFFEGYYNNPEATAERM- 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 485 QDKWYRTGDIALMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQEAQVVGVKDERMGEEICACIRLKSGETT 564
Cdd:PRK13388 378 RHGMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVGDQVMAALVLRDGATF 457
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 24418933 565 TAEEIKAFCKGK--ISHFKIPRYIVFVEGYPLTISGKIQKFKLREQ 608
Cdd:PRK13388 458 DPDAFAAFLAAQpdLGTKAWPRYVRIAADLPSTATNKVLKRELIAQ 503
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
81-613 |
1.24e-29 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 123.18 E-value: 1.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 81 TAQRFPDREAlVILHENiRLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIilVSVNPAY-- 158
Cdd:PRK10946 32 TRHAASDAIA-VICGER-QFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLGV--APVNALFsh 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 159 QSSELEYVLRKVGCKGIVFPKQ---FKTQQYYDILKQVCPELE----KAQPGALKSERLPDLTTVISVDAPLPGtllldD 231
Cdd:PRK10946 108 QRSELNAYASQIEPALLIADRQhalFSDDDFLNTLVAEHSSLRvvllLNDDGEHSLDDAINHPAEDFTATPSPA-----D 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 232 IVAaggkeqnlaqlrynqrFLscydpiniQFTSGTTGNPKGATLSHHNI---VNNSMLIGQrlkmptkTAEELRLV--LP 306
Cdd:PRK10946 183 EVA----------------FF--------QLSGGSTGTPKLIPRTHNDYyysVRRSVEICG-------FTPQTRYLcaLP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 307 SPLYHCLGSVGGTMVSMMHGATLLLSSPSFNGKKALeaISREKGTLLYGTP---TMFVDILNQPDfSSYDFTSIRGGVIA 383
Cdd:PRK10946 232 AAHNYPMSSPGALGVFLAGGTVVLAPDPSATLCFPL--IEKHQVNVTALVPpavSLWLQAIAEGG-SRAQLASLKLLQVG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 384 GSPAPPELIRAIINKMNMKeLVVVYGTTENspvtFMNFP--EDTLEQKAGSVGRIM-PHTEAQIVNvETGELTNLNVPGE 460
Cdd:PRK10946 309 GARLSETLARRIPAELGCQ-LQQVFGMAEG----LVNYTrlDDSDERIFTTQGRPMsPDDEVWVAD-ADGNPLPQGEVGR 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 461 LYIRGYCVMQGYWGEPQKTFETVGQDKWYRTGDIALMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQEAQV 540
Cdd:PRK10946 383 LMTRGPYTFRGYYKSPQHNASAFDANGFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAAL 462
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24418933 541 VGVKDERMGEEICACIrlksgetTTAEEIKA-----FCKGK-ISHFKIPRYIVFVEGYPLTISGKIQKFKLREQMEQHL 613
Cdd:PRK10946 463 VSMEDELMGEKSCAFL-------VVKEPLKAvqlrrFLREQgIAEFKLPDRVECVDSLPLTAVGKVDKKQLRQWLASRA 534
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
74-605 |
2.17e-29 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 125.07 E-value: 2.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 74 VGECLDATAQRFPDREALVILHEniRLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVS 153
Cdd:PRK12316 2005 VHQRIAEQAARAPEAIAVVFGDQ--HLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVP 2082
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 154 VNPAYQSSELEYVLRKVGCKGIVfpkqfkTQQyyDILKQVCPelekaqPGALksERLPdlttvISVDAPLPGTLLLDDIV 233
Cdd:PRK12316 2083 LDPNYPAERLAYMLEDSGAALLL------TQR--HLLERLPL------PAGV--ARLP-----LDRDAEWADYPDTAPAV 2141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 234 AAGGkeQNLAQLRYnqrflscydpiniqfTSGTTGNPKGATLSHHNIVNNSMLIGQRLKMPTKTAEelrlvLPSPLYHCL 313
Cdd:PRK12316 2142 QLAG--ENLAYVIY---------------TSGSTGLPKGVAVSHGALVAHCQAAGERYELSPADCE-----LQFMSFSFD 2199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 314 GSVGGTMVSMMHGATLLLSSPSFNGKKALEAISREKGTLLYGTPTMFVDILNQPDFSSYDFTSIRGGVIAGSPAPPELIR 393
Cdd:PRK12316 2200 GAHEQWFHPLLNGARVLIRDDELWDPEQLYDEMERHGVTILDFPPVYLQQLAEHAERDGRPPAVRVYCFGGEAVPAASLR 2279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 394 AIINKMNMKELVVVYGTTEN--SPVTFMNFPEDTLEQKAGSVGRIMPHTEAQIVNvETGELTNLNVPGELYIRGYCVMQG 471
Cdd:PRK12316 2280 LAWEALRPVYLFNGYGPTEAvvTPLLWKCRPQDPCGAAYVPIGRALGNRRAYILD-ADLNLLAPGMAGELYLGGEGLARG 2358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 472 YWGEPQKTFETVGQDKW-------YRTGDIALMDEQGFCKIVGRSKDMI-IRGGEnIYPAELEDFFLKHPQVQEAQVVGv 543
Cdd:PRK12316 2359 YLNRPGLTAERFVPDPFsasgerlYRTGDLARYRADGVVEYLGRIDHQVkIRGFR-IELGEIEARLQAHPAVREAVVVA- 2436
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24418933 544 KDERMGEEICACIRLKSGETTTAEEIKAFCKGKISHFKIPRYIVFVEGYPLTISGKIQKFKL 605
Cdd:PRK12316 2437 QDGASGKQLVAYVVPDDAAEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKAL 2498
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
74-602 |
2.85e-29 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 124.68 E-value: 2.85e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 74 VGECLDATAQRFPDREALVILHEniRLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVS 153
Cdd:PRK12316 4553 VHQLVAERARMTPDAVAVVFDEE--KLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVP 4630
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 154 VNPAYQSSELEYVLRKVGCKGIVfpkqfkTQQYydiLKQVCPELEKAQpgALKSERLPDLTTVISVDAPLPgtllLDdiv 233
Cdd:PRK12316 4631 LDPEYPRERLAYMMEDSGAALLL------TQSH---LLQRLPIPDGLA--SLALDRDEDWEGFPAHDPAVR----LH--- 4692
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 234 aaggkEQNLAQLRYnqrflscydpiniqfTSGTTGNPKGATLSHHNIVNNSMLIGQRLKMptkTAEELRLVLPSplYHCL 313
Cdd:PRK12316 4693 -----PDNLAYVIY---------------TSGSTGRPKGVAVSHGSLVNHLHATGERYEL---TPDDRVLQFMS--FSFD 4747
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 314 GSVGGTMVSMMHGATLLLSSPSFNGKKALEA-ISREKGTLLYGTPTMFVDILNQPDfSSYDFTSIRGGVIAGSPAPPELI 392
Cdd:PRK12316 4748 GSHEGLYHPLINGASVVIRDDSLWDPERLYAeIHEHRVTVLVFPPVYLQQLAEHAE-RDGEPPSLRVYCFGGEAVAQASY 4826
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 393 RAIINKMNMKELVVVYGTTENS--PVTFMNFPEDTLEQKAGSVGRIMPHTEAQIVNVEtGELTNLNVPGELYIRGYCVMQ 470
Cdd:PRK12316 4827 DLAWRALKPVYLFNGYGPTETTvtVLLWKARDGDACGAAYMPIGTPLGNRSGYVLDGQ-LNPLPVGVAGELYLGGEGVAR 4905
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 471 GYWGEPQKT--------FETVGQdKWYRTGDIALMDEQGFCKIVGRSKDMI-IRGGEnIYPAELEDFFLKHPQVQEAQVV 541
Cdd:PRK12316 4906 GYLERPALTaerfvpdpFGAPGG-RLYRTGDLARYRADGVIDYLGRVDHQVkIRGFR-IELGEIEARLREHPAVREAVVI 4983
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24418933 542 GVkDERMGEEICACI-----RLKSGETTTAE---EIKAFCKGKISHFKIPRYIVFVEGYPLTISGKIQK 602
Cdd:PRK12316 4984 AQ-EGAVGKQLVGYVvpqdpALADADEAQAElrdELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDR 5051
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
86-602 |
4.79e-29 |
|
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: 120.49 E-value: 4.79e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 86 PDREALVILHEniRLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVSVNPAYQSSELEY 165
Cdd:cd17643 1 PEAVAVVDEDR--RLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 166 VLrkvgckgivfpkqfktqqyydilkqvcpelEKAQPGALKSErlPDlttvisvdaplpgtlllddivaaggkeqnlaql 245
Cdd:cd17643 79 IL------------------------------ADSGPSLLLTD--PD--------------------------------- 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 246 rynqrflscyDPINIQFTSGTTGNPKGATLSHHNIVnnSMLIGQRLkmPTKTAEELRLVLpsplYHCLG---SVGGTMVS 322
Cdd:cd17643 94 ----------DLAYVIYTSGSTGRPKGVVVSHANVL--ALFAATQR--WFGFNEDDVWTL----FHSYAfdfSVWEIWGA 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 323 MMHGATLLLSSP--SFNGKKALEAISREKGTLLYGTPTMFVDILNQPDFSSYDFTSIRGGVIAGSPAPPELIRAIINKMN 400
Cdd:cd17643 156 LLHGGRLVVVPYevARSPEDFARLLRDEGVTVLNQTPSAFYQLVEAADRDGRDPLALRYVIFGGEALEAAMLRPWAGRFG 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 401 MK--ELVVVYGTTENSP-VTFMNFPEDTLEQKAGSV-GRIMPHTEAQIVNvETGELTNLNVPGELYIRGYCVMQGYWGEP 476
Cdd:cd17643 236 LDrpQLVNMYGITETTVhVTFRPLDAADLPAAAASPiGRPLPGLRVYVLD-ADGRPVPPGVVGELYVSGAGVARGYLGRP 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 477 QKTFETVGQD-------KWYRTGDIALMDEQGFCKIVGRSKDMI-IRGgENIYPAELEDFFLKHPQVQEAQVVGVKDERM 548
Cdd:cd17643 315 ELTAERFVANpfggpgsRMYRTGDLARRLPDGELEYLGRADEQVkIRG-FRIELGEIEAALATHPSVRDAAVIVREDEPG 393
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 24418933 549 GEEICACIRLKSGETTTAEEIKAFCKGKISHFKIPRYIVFVEGYPLTISGKIQK 602
Cdd:cd17643 394 DTRLVAYVVADDGAAADIAELRALLKELLPDYMVPARYVPLDALPLTVNGKLDR 447
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
382-615 |
3.17e-28 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 117.79 E-value: 3.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 382 IAGSPAPPELI----RAIINkmnmkeLVVVYGTTEN-SPVTFMnFPEDTLeQKAGSVGRIMPHTEAQIVNVETGELTnln 456
Cdd:PRK07445 237 LGGAPAWPSLLeqarQLQLR------LAPTYGMTETaSQIATL-KPDDFL-AGNNSSGQVLPHAQITIPANQTGNIT--- 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 457 vpgelyIRGYCVMQGYW---GEPQKTFETvgqdkwyrtGDIALMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHP 533
Cdd:PRK07445 306 ------IQAQSLALGYYpqiLDSQGIFET---------DDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATG 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 534 QVQEAQVVGVKDERMGEEICACIRLKSGETTTaEEIKAFCKGKISHFKIPRYIVFVEGYPLTISGKIQKFKLREQMEQHL 613
Cdd:PRK07445 371 LVQDVCVLGLPDPHWGEVVTAIYVPKDPSISL-EELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQQIAVQRL 449
|
..
gi 24418933 614 KL 615
Cdd:PRK07445 450 GL 451
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
86-605 |
4.61e-28 |
|
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: 117.35 E-value: 4.61e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 86 PDREALVilHENIRLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVSVNPAYQSSELEY 165
Cdd:cd17652 1 PDAPAVV--FGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 166 VLrkvgckgivfpkqfktqqyydilkqvcpelEKAQPGALkserlpdLTTVisvdaplpgtlllddivaaggkeQNLAQL 245
Cdd:cd17652 79 ML------------------------------ADARPALL-------LTTP-----------------------DNLAYV 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 246 RYnqrflscydpiniqfTSGTTGNPKGATLSHHNIVNNSMLIGQRLKmPTKTAEELRLVLPSplyhCLGSVGGTMVSMMH 325
Cdd:cd17652 99 IY---------------TSGSTGRPKGVVVTHRGLANLAAAQIAAFD-VGPGSRVLQFASPS----FDASVWELLMALLA 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 326 GATLLL--SSPSFNGKKALEAISREKGTLLYGTPTMfVDILnqpdfSSYDFTSIRGGVIAGSPAPPELI------RAIIN 397
Cdd:cd17652 159 GATLVLapAEELLPGEPLADLLREHRITHVTLPPAA-LAAL-----PPDDLPDLRTLVVAGEACPAELVdrwapgRRMIN 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 398 kmnmkelvvVYGTTE---NSPVTFMNFPEDTLeqkagSVGRIMPHTEAQIVN-----VETGeltnlnVPGELYIRGYCVM 469
Cdd:cd17652 233 ---------AYGPTEttvCATMAGPLPGGGVP-----PIGRPVPGTRVYVLDarlrpVPPG------VPGELYIAGAGLA 292
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 470 QGYWGEPQKT--------FETVGqDKWYRTGDIALMDEQGFCKIVGRSKDMI-IRGgENIYPAELEDFFLKHPQVQEAqV 540
Cdd:cd17652 293 RGYLNRPGLTaerfvadpFGAPG-SRMYRTGDLARWRADGQLEFLGRADDQVkIRG-FRIELGEVEAALTEHPGVAEA-V 369
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24418933 541 VGVKDERMGEE-ICACIRLKSGETTTAEEIKAFCKGKISHFKIPRYIVFVEGYPLTISGKIQKFKL 605
Cdd:cd17652 370 VVVRDDRPGDKrLVAYVVPAPGAAPTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
74-602 |
9.91e-28 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 119.68 E-value: 9.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 74 VGECLDATAQRFPDREALVILHEniRLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVS 153
Cdd:PRK12316 3059 VHRLFEEQVERTPDAVALAFGEQ--RLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVP 3136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 154 VNPAYQSSELEYVLRKVGCKGIVFPKQFKTQQyydiLKQVCPELEKAQPGALKSERLPDLTTvisvdaplpgtlllddiv 233
Cdd:PRK12316 3137 LDPEYPEERLAYMLEDSGAQLLLSQSHLRLPL----AQGVQVLDLDRGDENYAEANPAIRTM------------------ 3194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 234 aaggkEQNLAQLRYnqrflscydpiniqfTSGTTGNPKGATLSHHNIVNNSMLIGQRLKMPTKTAeelrlVLPSPLYHCL 313
Cdd:PRK12316 3195 -----PENLAYVIY---------------TSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDR-----VLQFTTFSFD 3249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 314 GSVGGTMVSMMHGATLLLSSPSF--NGKKALEAISREKGTLLYGTPTMFVDILNQPDFSSYdfTSIRGGVIAGSPAPPEL 391
Cdd:PRK12316 3250 VFVEELFWPLMSGARVVLAGPEDwrDPALLVELINSEGVDVLHAYPSMLQAFLEEEDAHRC--TSLKRIVCGGEALPADL 3327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 392 IRAIINKMNMKELvvvYGTTEnSPVTFMNFPEDTLEQKAGSVGRIMPHTEAQIVNVeTGELTNLNVPGELYIRGYCVMQG 471
Cdd:PRK12316 3328 QQQVFAGLPLYNL---YGPTE-ATITVTHWQCVEEGKDAVPIGRPIANRACYILDG-SLEPVPVGALGELYLGGEGLARG 3402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 472 YWGEPQKTFETVGQD------KWYRTGDIALMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQEAQVVGVKd 545
Cdd:PRK12316 3403 YHNRPGLTAERFVPDpfvpgeRLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLAVD- 3481
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 24418933 546 ermGEEICACIRLKSGETTTAEEIKAFCKGKISHFKIPRYIVFVEGYPLTISGKIQK 602
Cdd:PRK12316 3482 ---GRQLVAYVVPEDEAGDLREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDR 3535
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
260-611 |
1.02e-27 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 118.66 E-value: 1.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 260 IQFTSGTTGNPKGATLSHHNIVNNsmlIGQRLKMPTKTAEElRLVLPSPLYHCLGSVGGTMVSMMHGATLLLSSPSFNGK 339
Cdd:PRK08043 370 ILFTSGSEGHPKGVVHSHKSLLAN---VEQIKTIADFTPND-RFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPLHYR 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 340 KALEAISREKGTLLYGTPTMfvdILNQPDFSS-YDFTSIRGgVIAGSPAPPELIRAI-INKMNMKELVVvYGTTENSPVT 417
Cdd:PRK08043 446 IVPELVYDRNCTVLFGTSTF---LGNYARFANpYDFARLRY-VVAGAEKLQESTKQLwQDKFGLRILEG-YGVTECAPVV 520
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 418 FMNFPedtLEQKAGSVGRIMPHTEAQIVNV---ETGeltnlnvpGELYIRGYCVMQGYWG-------EPQKTFETVGQDK 487
Cdd:PRK08043 521 SINVP---MAAKPGTVGRILPGMDARLLSVpgiEQG--------GRLQLKGPNIMNGYLRvekpgvlEVPTAENARGEME 589
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 488 --WYRTGDIALMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLK-HPQVQEAQVVgVKDERMGEeicACIRLKSGETT 564
Cdd:PRK08043 590 rgWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGvSPDKQHATAI-KSDASKGE---ALVLFTTDSEL 665
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 24418933 565 TAEEIKAFCKGK-ISHFKIPRYIVFVEGYPLTISGKIQKFKLREQMEQ 611
Cdd:PRK08043 666 TREKLQQYAREHgVPELAVPRDIRYLKQLPLLGSGKPDFVTLKSMVDE 713
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
260-600 |
1.66e-27 |
|
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: 116.00 E-value: 1.66e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 260 IQFTSGTTGNPKGATLSHHNIVNNSMLIGQRLKMPTktaeELRLVLPSPLyhCLG-SVGGTMVSMMHGATLLL------- 331
Cdd:cd17644 111 VIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEYGITS----SDRVLQFASI--AFDvAAEEIYVTLLSGATLVLrpeemrs 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 332 SSPSFngkkaLEAISREKGTLLYGTPT---MFVDILNQPDFSSYDftSIRGGVIAGSPAPPELIRAII-NKMNMKELVVV 407
Cdd:cd17644 185 SLEDF-----VQYIQQWQLTVLSLPPAywhLLVLELLLSTIDLPS--SLRLVIVGGEAVQPELVRQWQkNVGNFIQLINV 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 408 YGTTENS-PVTFMNFPEDTLEQ-KAGSVGRIMPHTEAQIVNvETGELTNLNVPGELYIRGYCVMQGYWGEPQKT------ 479
Cdd:cd17644 258 YGPTEATiAATVCRLTQLTERNiTSVPIGRPIANTQVYILD-ENLQPVPVGVPGELHIGGVGLARGYLNRPELTaekfis 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 480 --FETVGQDKWYRTGDIALMDEQGFCKIVGRSKDMI-IRGGEnIYPAELEDFFLKHPQVQEAQVVGVKDERMGEEICACI 556
Cdd:cd17644 337 hpFNSSESERLYKTGDLARYLPDGNIEYLGRIDNQVkIRGFR-IELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYI 415
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 24418933 557 RLKSGETTTAEEIKAFCKGKISHFKIPRYIVFVEGYPLTISGKI 600
Cdd:cd17644 416 VPHYEESPSTVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKI 459
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
256-526 |
1.79e-27 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 116.63 E-value: 1.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 256 DPINIQFTSGTTGNPKGATLSHHNIVNN--SMLIGQRLkmptkTAEELRLVLPSPLYHCLGSVGGTMVSMMHGATLLLSS 333
Cdd:PRK07768 153 DLALMQLTSGSTGSPKAVQITHGNLYANaeAMFVAAEF-----DVETDVMVSWLPLFHDMGMVGFLTVPMYFGAELVKVT 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 334 PS-FNGKKAL--EAISREKGTLLYGtPTMFVDIL-----NQPDFSSYDFTSIRGGVIAGSPAPPELIRAIIN-----KMN 400
Cdd:PRK07768 228 PMdFLRDPLLwaELISKYRGTMTAA-PNFAYALLarrlrRQAKPGAFDLSSLRFALNGAEPIDPADVEDLLDagarfGLR 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 401 MKELVVVYGTTENS-PVTFMNFPE---------DTLEQKAGSV-------------GRIMPHTEAQIVNvETGELTNLNV 457
Cdd:PRK07768 307 PEAILPAYGMAEATlAVSFSPCGAglvvdevdaDLLAALRRAVpatkgntrrlatlGPPLPGLEVRVVD-EDGQVLPPRG 385
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24418933 458 PGELYIRGYCVMQGYWgEPQKTFETVGQDKWYRTGDIALMDEQGFCKIVGRSKDMIIRGGENIYPAELE 526
Cdd:PRK07768 386 VGVIELRGESVTPGYL-TMDGFIPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIE 453
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
102-553 |
2.27e-27 |
|
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341296 [Multi-domain] Cd Length: 569 Bit Score: 116.75 E-value: 2.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 102 FAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVSVnpaYQSS---ELEYVLRKVGCKGIVFP 178
Cdd:cd17641 14 WADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGI---YQDSmaeEVAYLLNYTGARVVIAE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 179 KQFKTQQYYDILKQVcPELEKA---QPGALKSERLPDLTTVISV-------DAPLPGtlLLDDIVAAGgKEQNLAQLRYn 248
Cdd:cd17641 91 DEEQVDKLLEIADRI-PSVRYViycDPRGMRKYDDPRLISFEDVvalgralDRRDPG--LYEREVAAG-KGEDVAVLCT- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 249 qrflscydpiniqfTSGTTGNPKGATLSHHNIVNNSmLIGQRLKmPTKTAEELRLVLPSP-----LYhclgSVGGTMVS- 322
Cdd:cd17641 166 --------------TSGTTGKPKLAMLSHGNFLGHC-AAYLAAD-PLGPGDEYVSVLPLPwigeqMY----SVGQALVCg 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 323 -----------MMH-----GATLLLSSPS------------------FN----------GKKALEAISREK--GTLLYGT 356
Cdd:cd17641 226 fivnfpeepetMMEdlreiGPTFVLLPPRvwegiaadvrarmmdatpFKrfmfelgmklGLRALDRGKRGRpvSLWLRLA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 357 PTMFVDILNQPDFSSYDFTSIRGGVIAGSPAPPELIR---AIinKMNMKElvvVYGTTENSPVTFMNFPEDTleqKAGSV 433
Cdd:cd17641 306 SWLADALLFRPLRDRLGFSRLRSAATGGAALGPDTFRffhAI--GVPLKQ---LYGQTELAGAYTVHRDGDV---DPDTV 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 434 GRIMPHTEAQIVNVetgeltnlnvpGELYIRGYCVMQGYWGEPQKTFETVGQDKWYRTGDIALMDEQGFCKIVGRSKD-M 512
Cdd:cd17641 378 GVPFPGTEVRIDEV-----------GEILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDvG 446
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 24418933 513 IIRGGENIYPAELEDFFLKHPQVQEAQVVGVKDERMGEEIC 553
Cdd:cd17641 447 TTSDGTRFSPQFIENKLKFSPYIAEAVVLGAGRPYLTAFIC 487
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
74-613 |
5.06e-27 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 117.57 E-value: 5.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 74 VGECLDATAQRFPDREALVILHEniRLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVS 153
Cdd:PRK12467 1576 VHQLIEDQAAATPEAVALVFGEQ--ELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVP 1653
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 154 VNPAYQSSELEYVLRKVGCKGIVfpkqfkTQqyydilKQVCPELEkaqpgalkserLPDLTTVISVDAP---LPGTLLLD 230
Cdd:PRK12467 1654 LDPEYPRERLAYMIEDSGIELLL------TQ------SHLQARLP-----------LPDGLRSLVLDQEddwLEGYSDSN 1710
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 231 DIVAAGGkeQNLAQLRYnqrflscydpiniqfTSGTTGNPKGATLSHHNIVNNSMLIGQRLKMPTKTAeelrlVLPSPLY 310
Cdd:PRK12467 1711 PAVNLAP--QNLAYVIY---------------TSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADV-----VLQFTSF 1768
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 311 HCLGSVGGTMVSMMHGATLLLSSP--SFNGKKALEAISREKGTLLYGTPTMFVDILnQPDFSSYDFTSIRGGVIAGSPAP 388
Cdd:PRK12467 1769 AFDVSVWELFWPLINGARLVIAPPgaHRDPEQLIQLIERQQVTTLHFVPSMLQQLL-QMDEQVEHPLSLRRVVCGGEALE 1847
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 389 PELIRAIINKMNMKELVVVYGTTENS-PVTFMNFPEDTLEQKAGS-VGRIMPHTEAQIVNvETGELTNLNVPGELYIRGY 466
Cdd:PRK12467 1848 VEALRPWLERLPDTGLFNLYGPTETAvDVTHWTCRRKDLEGRDSVpIGQPIANLSTYILD-ASLNPVPIGVAGELYLGGV 1926
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 467 CVMQGYWGEPQKT--------FETVGQdKWYRTGDIALMDEQGFCKIVGRSKDMI-IRGGEnIYPAELEDFFLKHPQVQE 537
Cdd:PRK12467 1927 GLARGYLNRPALTaerfvadpFGTVGS-RLYRTGDLARYRADGVIEYLGRIDHQVkIRGFR-IELGEIEARLREQGGVRE 2004
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 538 AQVVgVKDERMGEEICACIRLKSGE--------TTTAEEIKAFCKGKISHFKIPRYIVFVEGYPLTISGKIQKFKL---- 605
Cdd:PRK12467 2005 AVVI-AQDGANGKQLVAYVVPTDPGlvdddeaqVALRAILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKALpapd 2083
|
570
....*....|....*....
gi 24418933 606 -----------REQMEQHL 613
Cdd:PRK12467 2084 aselqqayvapQSELEQRL 2102
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
86-605 |
5.85e-27 |
|
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: 114.49 E-value: 5.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 86 PDREAlvILHENIRLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVSVNPAYQSSELEY 165
Cdd:cd17656 2 PDAVA--VVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 166 VLRKVGCKGIVfpkqfkTQQYYdilkQVCPELEKAqpgalkserlpdlttvisvdaplpgTLLLDDIVAAGGKEQNLaQL 245
Cdd:cd17656 80 IMLDSGVRVVL------TQRHL----KSKLSFNKS-------------------------TILLEDPSISQEDTSNI-DY 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 246 RYNQRFLscydpINIQFTSGTTGNPKGATLSHHNIVNnsMLIGQRLKMPTKTAEELrLVLPSPLYH-CLGSVGGTMVSmm 324
Cdd:cd17656 124 INNSDDL-----LYIIYTSGTTGKPKGVQLEHKNMVN--LLHFEREKTNINFSDKV-LQFATCSFDvCYQEIFSTLLS-- 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 325 hGATLLLSSPSF--NGKKALEAISREKGTLLYgTPTMFVD-ILNQPDFSSYDFTSIRGGVIAGSPAppeLIRAIINKMNM 401
Cdd:cd17656 194 -GGTLYIIREETkrDVEQLFDLVKRHNIEVVF-LPVAFLKfIFSEREFINRFPTCVKHIITAGEQL---VITNEFKEMLH 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 402 KELVVV---YGTTENSPVTFMNF-PEDTLeQKAGSVGRIMPHTEAQIVNvETGELTNLNVPGELYIRGYCVMQGYWGEPQ 477
Cdd:cd17656 269 EHNVHLhnhYGPSETHVVTTYTInPEAEI-PELPPIGKPISNTWIYILD-QEQQLQPQGIVGELYISGASVARGYLNRQE 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 478 KTFETVGQDKW------YRTGDIALMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQEAQVVGVKDERMGEE 551
Cdd:cd17656 347 LTAEKFFPDPFdpnermYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKY 426
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 24418933 552 ICAciRLKSGETTTAEEIKAFCKGKISHFKIPRYIVFVEGYPLTISGKIQKFKL 605
Cdd:cd17656 427 LCA--YFVMEQELNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
89-600 |
8.94e-27 |
|
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: 113.72 E-value: 8.94e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 89 EALVILHENIRLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVSVNPAYQSSELEYVLR 168
Cdd:cd17650 2 DAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYMLE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 169 KVGCKGIVfpkqfktqqyydilkqvcpelekAQPGalkserlpdlttvisvdaplpgtlllddivaaggkeqnlaqlryn 248
Cdd:cd17650 82 DSGAKLLL-----------------------TQPE--------------------------------------------- 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 249 qrflscyDPINIQFTSGTTGNPKGATLSHHNIVNNSMLIGQRLKMPTKTAEELRL------VLPSPLYHCLgSVGGTMVS 322
Cdd:cd17650 94 -------DLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAWRREYELDSFPVRLLQMasfsfdVFAGDFARSL-LNGGTLVI 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 323 MMHGATlllsspsFNGKKALEAISREKGTLLYGTPTMFVDILNQPDFSSYDFTSIRGgVIAGSPAPP-----ELIRAIIN 397
Cdd:cd17650 166 CPDEVK-------LDPAALYDLILKSRITLMESTPALIRPVMAYVYRNGLDLSAMRL-LIVGSDGCKaqdfkTLAARFGQ 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 398 KMnmkELVVVYGTTENS-PVTFMNFPEDTLEQKAGS-VGRIMPHTEAQIVNvETGELTNLNVPGELYIRGYCVMQGYWGE 475
Cdd:cd17650 238 GM---RIINSYGVTEATiDSTYYEEGRDPLGDSANVpIGRPLPNTAMYVLD-ERLQPQPVGVAGELYIGGAGVARGYLNR 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 476 PQKTFETVGQDKW------YRTGDIALMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQEAQVVGVKDERMG 549
Cdd:cd17650 314 PELTAERFVENPFapgermYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVREDKGGE 393
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 24418933 550 EEICACIrlKSGETTTAEEIKAFCKGKISHFKIPRYIVFVEGYPLTISGKI 600
Cdd:cd17650 394 ARLCAYV--VAAATLNTAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKV 442
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
67-605 |
1.33e-26 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 114.34 E-value: 1.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 67 SHLvNTTVGECLDATAQRFPDREALVILHENIRLNFAQLKEEVDKAASGLLSIGLRKGDR---LGMWGPNSYAWVLiqlA 143
Cdd:PRK05857 10 PQL-PSTVLDRVFEQARQQPEAIALRRCDGTSALRYRELVAEVGGLAADLRAQSVSRGSRvlvISDNGPETYLSVL---A 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 144 TAQAGIILVSVN---PAYQSSELEYVLRKVGckgiVFPkqfktqqyydilkqvcpelekAQPGALKSERLPDLTTVISVd 220
Cdd:PRK05857 86 CAKLGAIAVMADgnlPIAAIERFCQITDPAA----ALV---------------------APGSKMASSAVPEALHSIPV- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 221 aplpgtlLLDDIVAAGGKEQNLAQLRY--NQRFLSCYDPINIQFTSGTTGNPKGATLSHHNIVN-NSMLIGQRLKMPTKT 297
Cdd:PRK05857 140 -------IAVDIAAVTRESEHSLDAASlaGNADQGSEDPLAMIFTSGTTGEPKAVLLANRTFFAvPDILQKEGLNWVTWV 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 298 AEELRLVlPSPLYHcLGSVGGTMVSMMHGATLLLSSPsfNGKKALEAISREKGTLLYGTPTMFVDILNQPDFSSYDFTSI 377
Cdd:PRK05857 213 VGETTYS-PLPATH-IGGLWWILTCLMHGGLCVTGGE--NTTSLLEILTTNAVATTCLVPTLLSKLVSELKSANATVPSL 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 378 RGGVIAGSPAPPELIRAIinKMNMKELVVVYGTTENSpVTFMNFPEDT---LEQKAGSVGRIMPHTEAQIVNVETGELTN 454
Cdd:PRK05857 289 RLVGYGGSRAIAADVRFI--EATGVRTAQVYGLSETG-CTALCLPTDDgsiVKIEAGAVGRPYPGVDVYLAATDGIGPTA 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 455 LNVP-----GELYIRGYCVMQGYWGEPQKTFETVGqDKWYRTGDIALMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFF 529
Cdd:PRK05857 366 PGAGpsasfGTLWIKSPANMLGYWNNPERTAEVLI-DGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIA 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 530 LKHPQVQEAQVVGVKDERMGEEI-CACIRLKSGETTTAEEIK----AFCKGKISHFKIPRYIVFVEGYPLTISGKIQKFK 604
Cdd:PRK05857 445 EGVSGVREAACYEIPDEEFGALVgLAVVASAELDESAARALKhtiaARFRRESEPMARPSTIVIVTDIPRTQSGKVMRAS 524
|
.
gi 24418933 605 L 605
Cdd:PRK05857 525 L 525
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
74-602 |
3.05e-26 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 114.87 E-value: 3.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 74 VGECLDATAQRFPDREALVIlhENIRLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVS 153
Cdd:PRK12467 3097 VHQLIEAQVARTPEAPALVF--GDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVP 3174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 154 VNPAYQSSELEYVLRKVGCKGIVfpkqfkTQQYydILkqvcpelekaqpgalksERLPDLTTVIsvdaplpgTLLLDDIV 233
Cdd:PRK12467 3175 LDPEYPRERLAYMIEDSGVKLLL------TQAH--LL-----------------EQLPAPAGDT--------ALTLDRLD 3221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 234 AAGGKEQNLAQLRYNQRFlsCYdpinIQFTSGTTGNPKGATLSHHNIVNNSMLIGQRLKMPTKTaeelRLVLPSPlYHCL 313
Cdd:PRK12467 3222 LNGYSENNPSTRVMGENL--AY----VIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDAND----RVLLFMS-FSFD 3290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 314 GSVGGTMVSMMHGATLLLS-SPSFNGKKALEAISREKGTLLYGTPTMFVDILNQPDFSSYdfTSIRGGVIAGSPAPPELI 392
Cdd:PRK12467 3291 GAQERFLWTLICGGCLVVRdNDLWDPEELWQAIHAHRISIACFPPAYLQQFAEDAGGADC--ASLDIYVFGGEAVPPAAF 3368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 393 RAIINKMNMKELVVVYGTTENS-PVTFMNFPEDTL-EQKAGSVGRIMPHTEAQIVNvETGELTNLNVPGELYIRGYCVMQ 470
Cdd:PRK12467 3369 EQVKRKLKPRGLTNGYGPTEAVvTVTLWKCGGDAVcEAPYAPIGRPVAGRSIYVLD-GQLNPVPVGVAGELYIGGVGLAR 3447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 471 GYWGEPQKT--------FETVGQdKWYRTGDIALMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQEAQVVG 542
Cdd:PRK12467 3448 GYHQRPSLTaerfvadpFSGSGG-RLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLA 3526
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 543 VkDERMGEEICACIRLKSGETTTAEEIKAFCKGKISHFKIPRYIVFVEGYPLTISGKIQK 602
Cdd:PRK12467 3527 R-DGAGGKQLVAYVVPADPQGDWRETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDR 3585
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
82-544 |
5.53e-26 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 112.30 E-value: 5.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 82 AQRFPDREALVILH--------ENIRLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVS 153
Cdd:PRK09274 16 AQERPDQLAVAVPGgrgadgklAYDELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGAVPVL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 154 VNPAYqsseleyvlrkvgckGIvfpKQFKTqqyydILKQVCPELEKAQPGALKSERL-----PDLTTVISVDAPL-PGTL 227
Cdd:PRK09274 96 VDPGM---------------GI---KNLKQ-----CLAEAQPDAFIGIPKAHLARRLfgwgkPSVRRLVTVGGRLlWGGT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 228 LLDDIVAAGGKEQnlaqlrYNQRFLSCYDPINIQFTSGTTGNPKGATLSHhnivnnSMLIGQRlkmptktaEELRLV--- 304
Cdd:PRK09274 153 TLATLLRDGAAAP------FPMADLAPDDMAAILFTSGSTGTPKGVVYTH------GMFEAQI--------EALREDygi 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 305 ------LPS-PLYH----CLGsvGGTMVSMMHgatllLSSP-SFNGKKALEAISREKGTLLYGTPTMFVDILNQPDFSSY 372
Cdd:PRK09274 213 epgeidLPTfPLFAlfgpALG--MTSVIPDMD-----PTRPaTVDPAKLFAAIERYGVTNLFGSPALLERLGRYGEANGI 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 373 DFTSIRGGVIAGSPAPPELI---RAIINkmNMKELVVVYGTTENSPVTFMNFPE------DTLEQKAGS-VGRIMPHTEA 442
Cdd:PRK09274 286 KLPSLRRVISAGAPVPIAVIerfRAMLP--PDAEILTPYGATEALPISSIESREilfatrAATDNGAGIcVGRPVDGVEV 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 443 QIVNV---------ETGELTNLNVpGELYIRGYCVMQGYWGEPQKTFET----VGQDKWYRTGDIALMDEQG---FCkiv 506
Cdd:PRK09274 364 RIIAIsdapipewdDALRLATGEI-GEIVVAGPMVTRSYYNRPEATRLAkipdGQGDVWHRMGDLGYLDAQGrlwFC--- 439
|
490 500 510
....*....|....*....|....*....|....*...
gi 24418933 507 GRSKDMIIRGGENIYPAELEDFFLKHPQVQEAQVVGVK 544
Cdd:PRK09274 440 GRKAHRVETAGGTLYTIPCERIFNTHPGVKRSALVGVG 477
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
65-610 |
5.98e-26 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 114.11 E-value: 5.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 65 TDSHLVNTTVGECLDATAQRFPDREALVIL----HENIRLNFAQLKEEVDKAASGLLSIGlRKGDRLGMWGPNSYAWVLI 140
Cdd:PRK05691 2 MDAFELPLTLVQALQRRAAQTPDRLALRFLaddpGEGVVLSYRDLDLRARTIAAALQARA-SFGDRAVLLFPSGPDYVAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 141 QLATAQAGIILVsvnPAY--QSSELEYVLRKVGCKGIVFPKQFKTqqyydiLKQVCPELekAQPGALKSERLPDLttvIS 218
Cdd:PRK05691 81 FFGCLYAGVIAV---PAYppESARRHHQERLLSIIADAEPRLLLT------VADLRDSL--LQMEELAAANAPEL---LC 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 219 VDAplpgtllLDDIVAAGGKEQNLAQlrynqrflscyDPIN-IQFTSGTTGNPKGATLSHHNIVNNSMLIGQRLKMPTKT 297
Cdd:PRK05691 147 VDT-------LDPALAEAWQEPALQP-----------DDIAfLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGIDLNP 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 298 AEelrlVLPS--PLYHCLGSVGGTMVSMMHGATLLLSSPS-FNGK--KALEAISREKGTLLYGtptmfvdilnqPDFSsY 372
Cdd:PRK05691 209 DD----VIVSwlPLYHDMGLIGGLLQPIFSGVPCVLMSPAyFLERplRWLEAISEYGGTISGG-----------PDFA-Y 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 373 DFTSIR------------GGVIAGSPAPP---ELIRAIINKM-----NMKELVVVYGTTENS------------PVTFMN 420
Cdd:PRK05691 273 RLCSERvsesalerldlsRWRVAYSGSEPirqDSLERFAEKFaacgfDPDSFFASYGLAEATlfvsggrrgqgiPALELD 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 421 ---FPEDTLEQKAGSV----GRIMPHTEAQIVNVETGELTNLNVPGELYIRGYCVMQGYWGEPQ---KTF-ETVGQdKWY 489
Cdd:PRK05691 353 aeaLARNRAEPGTGSVlmscGRSQPGHAVLIVDPQSLEVLGDNRVGEIWASGPSIAHGYWRNPEasaKTFvEHDGR-TWL 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 490 RTGDIALMDEqGFCKIVGRSKDMIIRGGENIYPAELEDFFLKH-PQVQEAQVVGVKDERMGEE---ICACIRLKSGETTT 565
Cdd:PRK05691 432 RTGDLGFLRD-GELFVTGRLKDMLIVRGHNLYPQDIEKTVEREvEVVRKGRVAAFAVNHQGEEgigIAAEISRSVQKILP 510
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 24418933 566 AEE-IKAFCKGKISHFK-IPRYIVFVE--GYPLTISGKIQKFKLREQME 610
Cdd:PRK05691 511 PQAlIKSIRQAVAEACQeAPSVVLLLNpgALPKTSSGKLQRSACRLRLA 559
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
262-608 |
6.72e-26 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 112.82 E-value: 6.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 262 FTSGTTGNPKGATLSHHNI---VNNSMLIGQRLkmptkTAEELRLVlPSPLYHCLGSVGGTMVSMMHGATLLLSSPSFNG 338
Cdd:PRK06060 152 YTSGTTGPPKAAIHRHADPltfVDAMCRKALRL-----TPEDTGLC-SARMYFAYGLGNSVWFPLATGGSAVINSAPVTP 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 339 KKALEAISREKGTLLYGTPTMFVDILN--QPDfssyDFTSIRGGVIAGSPAPPELIRAIINKMNMKELVVVYGTTENSPv 416
Cdd:PRK06060 226 EAAAILSARFGPSVLYGVPNFFARVIDscSPD----SFRSLRCVVSAGEALELGLAERLMEFFGGIPILDGIGSTEVGQ- 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 417 TFMNFPEDtlEQKAGSVGRIMPHTEAQIVNVEtGELTNLNVPGELYIRGYCVMQGYWGEPQKTFETVGqdkWYRTGDIAL 496
Cdd:PRK06060 301 TFVSNRVD--EWRLGTLGRVLPPYEIRVVAPD-GTTAGPGVEGDLWVRGPAIAKGYWNRPDSPVANEG---WLDTRDRVC 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 497 MDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQEAQVVGVKDERMGEEICACIRLKSGE---TTTAEEIKAFC 573
Cdd:PRK06060 375 IDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSGAtidGSVMRDLHRGL 454
|
330 340 350
....*....|....*....|....*....|....*
gi 24418933 574 KGKISHFKIPRYIVFVEGYPLTISGKIQKFKLREQ 608
Cdd:PRK06060 455 LNRLSAFKVPHRFAVVDRLPRTPNGKLVRGALRKQ 489
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
99-611 |
9.54e-26 |
|
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: 112.02 E-value: 9.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 99 RLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVSVNPAYQSSELEYVLRKVGCKGIV-- 176
Cdd:cd05967 82 TYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGFAAKELASRIDDAKPKLIVta 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 177 -FPKQF-KTQQYYDILKQVCpELEKAQPgalkserlpdlTTVISVDAPLPGTLLLDdivaaGGKEQNLAQLRYNQRFLSC 254
Cdd:cd05967 162 sCGIEPgKVVPYKPLLDKAL-ELSGHKP-----------HHVLVLNRPQVPADLTK-----PGRDLDWSELLAKAEPVDC 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 255 Y-----DPINIQFTSGTTGNPKGA---TLSHHNIVNNSMLIGQRLKmptktaeelrlvlPSPLYHClGS-----VGGTMV 321
Cdd:cd05967 225 VpvaatDPLYILYTSGTTGKPKGVvrdNGGHAVALNWSMRNIYGIK-------------PGDVWWA-ASdvgwvVGHSYI 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 322 ---SMMHGATLLLsspsFNGKKA--------LEAISREKGTLLYGTPTMFVDILNQP----DFSSYDFTSIRGGVIAGSP 386
Cdd:cd05967 291 vygPLLHGATTVL----YEGKPVgtpdpgafWRVIEKYQVNALFTAPTAIRAIRKEDpdgkYIKKYDLSSLRTLFLAGER 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 387 APPELIRAIINKMNmKELVVVYGTTEN-SPVTFMNFPEDTLEQKAGSVGRIMPHTEAQIVNvETGELTNLNVPGELYIRG 465
Cdd:cd05967 367 LDPPTLEWAENTLG-VPVIDHWWQTETgWPITANPVGLEPLPIKAGSPGKPVPGYQVQVLD-EDGEPVGPNELGNIVIKL 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 466 YC---VMQGYWGEPQKTFET-VGQDK-WYRTGDIALMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQEAQV 540
Cdd:cd05967 445 PLppgCLLTLWKNDERFKKLyLSKFPgYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAV 524
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24418933 541 VGVKDERMGEEICACIRLKSGETTTAE----EIKAFCKGKISHFKIPRYIVFVEGYPLTISGKIqkfkLREQMEQ 611
Cdd:cd05967 525 VGVRDELKGQVPLGLVVLKEGVKITAEelekELVALVREQIGPVAAFRLVIFVKRLPKTRSGKI----LRRTLRK 595
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
260-607 |
1.23e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 109.74 E-value: 1.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 260 IQFTSGTTGNPKGATLSHHNIVNNSMLIGQRLKMPtktaEELRLVLPSPLYHCLGSVGGTMVSMMHGatlllSSPSF--- 336
Cdd:PRK08308 106 LQYSSGTTGEPKLIRRSWTEIDREIEAYNEALNCE----QDETPIVACPVTHSYGLICGVLAALTRG-----SKPVIitn 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 337 -NGKKALEAISREKGTLLYGTPTMfVDILNQpdFSSYDFTsIRGGVIAGSPAPPELIRAIINKMNMkeLVVVYGTTENSP 415
Cdd:PRK08308 177 kNPKFALNILRNTPQHILYAVPLM-LHILGR--LLPGTFQ-FHAVMTSGTPLPEAWFYKLRERTTY--MMQQYGCSEAGC 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 416 VTF---MNFPEDtleqkagsVGRIMPHteaqiVNVETGelTNLNVPGELYIRgycvmqgywgepqktfetVGqDKWYRTG 492
Cdd:PRK08308 251 VSIcpdMKSHLD--------LGNPLPH-----VSVSAG--SDENAPEEIVVK------------------MG-DKEIFTK 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 493 DIALMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQEAQVVGVKDERMGEEICAciRLKSGETTTAEEIKAF 572
Cdd:PRK08308 297 DLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKA--KVISHEEIDPVQLREW 374
|
330 340 350
....*....|....*....|....*....|....*
gi 24418933 573 CKGKISHFKIPRYIVFVEGYPLTISGKIQKfKLRE 607
Cdd:PRK08308 375 CIQHLAPYQVPHEIESVTEIPKNANGKVSR-KLLE 408
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
262-607 |
1.66e-25 |
|
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: 110.32 E-value: 1.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 262 FTSGTTGNPKGATLSHHNIVNNSMLIGQRLKMPTKTaeelRlVLPSPLYHCLGSVGGTMVSMMHGATllLSSPSfngKKA 341
Cdd:cd05918 113 FTSGSTGKPKGVVIEHRALSTSALAHGRALGLTSES----R-VLQFASYTFDVSILEIFTTLAAGGC--LCIPS---EED 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 342 L-----EAISREKGTLLYGTPTmFVDILnQPDfssyDFTSIRGGVIAGSPAPPELIRAIINKMNmkeLVVVYGTTENSPV 416
Cdd:cd05918 183 RlndlaGFINRLRVTWAFLTPS-VARLL-DPE----DVPSLRTLVLGGEALTQSDVDTWADRVR---LINAYGPAECTIA 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 417 TfmNFPEDTLEQKAGSVGRIMPHTeAQIVNVET-GELTNLNVPGELYIRGYCVMQGYWGEPQKTFETVGQD-KW------ 488
Cdd:cd05918 254 A--TVSPVVPSTDPRNIGRPLGAT-CWVVDPDNhDRLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDpAWlkqegs 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 489 ------YRTGDIALMDEQGFCKIVGRSKDMI-IRgGENIYPAELEDFFLKHPQVQEAQVVGV---KDERMGEEICACIRL 558
Cdd:cd05918 331 grgrrlYRTGDLVRYNPDGSLEYVGRKDTQVkIR-GQRVELGEIEHHLRQSLPGAKEVVVEVvkpKDGSSSPQLVAFVVL 409
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24418933 559 KSGETTT-----------------AEEIKAFCKGKISHFKIPRYIVFVEGYPLTISGKIQKFKLRE 607
Cdd:cd05918 410 DGSSSGSgdgdslflepsdefralVAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRALRE 475
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
100-607 |
5.54e-25 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 109.32 E-value: 5.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 100 LNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVSVN-PAYQSSELEYV------LRKVGC 172
Cdd:PRK09192 50 LPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPLPlPMGFGGRESYIaqlrgmLASAQP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 173 KGIVFPkqfktqqyyDILKQVCPELEKAQPGaLKSERLPDLTTVISVDAPLPgTLLLDDIvaaggkeqnlaqlrynqrfl 252
Cdd:PRK09192 130 AAIITP---------DELLPWVNEATHGNPL-LHVLSHAWFKALPEADVALP-RPTPDDI-------------------- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 253 sCYdpinIQFTSGTTGNPKGATLSHHNIVNNSMLIGQR-LKMptktAEELRLVLPSPLYHCLGSVGGTMVSMMHGATL-L 330
Cdd:PRK09192 179 -AY----LQYSSGSTRFPRGVIITHRALMANLRAISHDgLKV----RPGDRCVSWLPFYHDMGLVGFLLTPVATQLSVdY 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 331 LSSPSFNGKKA--LEAISREKGTLLYgTPTMFVDI----LNQPDFSSYDFTSIRGGVIAGSPAPPELIRAIINKM----- 399
Cdd:PRK09192 250 LPTRDFARRPLqwLDLISRNRGTISY-SPPFGYELcarrVNSKDLAELDLSCWRVAGIGADMIRPDVLHQFAEAFapagf 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 400 NMKELVVVYGTTENS-PVTFMnfP-----------EDTLEQKAGSV---------------GRIMPHTEAQIVNVETGEL 452
Cdd:PRK09192 329 DDKAFMPSYGLAEATlAVSFS--PlgsgivveevdRDRLEYQGKAVapgaetrrvrtfvncGKALPGHEIEIRNEAGMPL 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 453 TNLNVpGELYIRGYCVMQGYWGEpQKTFETVGQDKWYRTGDIALMDEqGFCKIVGRSKDMIIRGGENIYPAELEDFFLKH 532
Cdd:PRK09192 407 PERVV-GHICVRGPSLMSGYFRD-EESQDVLAADGWLDTGDLGYLLD-GYLYITGRAKDLIIINGRNIWPQDIEWIAEQE 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 533 PQVQ--EAQVVGVKDERmGEEICACIRLKSGETTTAEEIKAFCKGKI-SHFKIPRYIVFV--EGYPLTISGKIQKFKLRE 607
Cdd:PRK09192 484 PELRsgDAAAFSIAQEN-GEKIVLLVQCRISDEERRGQLIHALAALVrSEFGVEAAVELVppHSLPRTSSGKLSRAKAKK 562
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
100-536 |
2.36e-24 |
|
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: 106.92 E-value: 2.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 100 LNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVSVNPAYQSSELEYVLRKVGCKGIVfpk 179
Cdd:cd17639 6 MSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECSAIF--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 180 qfktqqyydilkqvcpelekaqpgalkserlpdlttvisvdaplpgtlllddivaAGGKEQNLAqlrynqrflsCydpin 259
Cdd:cd17639 83 -------------------------------------------------------TDGKPDDLA----------C----- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 260 IQFTSGTTGNPKGATLSHHNIVNNSMLIGQRLkmPTKTAEELRLVLPSPLYHCLgSVGGTMVSMMHGATLLLSSPsfngK 339
Cdd:cd17639 93 IMYTSGSTGNPKGVMLTHGNLVAGIAGLGDRV--PELLGPDDRYLAYLPLAHIF-ELAAENVCLYRGGTIGYGSP----R 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 340 KALEAISRE-KGTLLYGTPTMFVDIlnqPDFssydFTSIRGGVIAGSPAPPELIRAIINK-MNMK--------------E 403
Cdd:cd17639 166 TLTDKSKRGcKGDLTEFKPTLMVGV---PAI----WDTIRKGVLAKLNPMGGLKRTLFWTaYQSKlkalkegpgtplldE 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 404 LV-------------------------------VV-------YGTTENSPVTFMNFPEDtleQKAGSVGRIMPHTEAQIV 445
Cdd:cd17639 239 LVfkkvraalggrlrymlsggaplsadtqeflnIVlcpviqgYGLTETCAGGTVQDPGD---LETGRVGPPLPCCEIKLV 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 446 NV-ETGELTNLNVP-GELYIRGYCVMQGYWGEPQKTFETVGQDKWYRTGDIALMDEQGFCKIVGRSKDMI-IRGGENIYP 522
Cdd:cd17639 316 DWeEGGYSTDKPPPrGEILIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDLVkLQNGEYIAL 395
|
490
....*....|....
gi 24418933 523 AELEDFFLKHPQVQ 536
Cdd:cd17639 396 EKLESIYRSNPLVN 409
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
99-608 |
2.70e-24 |
|
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: 106.28 E-value: 2.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 99 RLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVSVNPAYQSSELEYVLRKVGCKGIVFp 178
Cdd:cd05940 3 ALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLVV- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 179 kqfktqqyydilkqvcpelekaqpgalkserlpdlttvisvdaplpgtlllddivaaggkeqnlaqlrynqrflscyDPI 258
Cdd:cd05940 82 -----------------------------------------------------------------------------DAA 84
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 259 NIQFTSGTTGNPKGATLSHHNIVNNSMLIGQRlkmpTKTAEELRLVLPSPLYHCLGSVGGTMVSMMHGATLLLSSpSFNG 338
Cdd:cd05940 85 LYIYTSGTTGLPKAAIISHRRAWRGGAFFAGS----GGALPSDVLYTCLPLYHSTALIVGWSACLASGATLVIRK-KFSA 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 339 KKALEAISREKGTllygtptMFVDI-------LNQPDFSSYDFTSIRggVIAGSPAPPELIRAIINKMNMKELVVVYGTT 411
Cdd:cd05940 160 SNFWDDIRKYQAT-------IFQYIgelcrylLNQPPKPTERKHKVR--MIFGNGLRPDIWEEFKERFGVPRIAEFYAAT 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 412 ENSpVTFMNFPedtleQKAGSVGRIMPHTE----AQIV--NVETGEL----------TNLNVPGEL--YIRGYCVMQGYW 473
Cdd:cd05940 231 EGN-SGFINFF-----GKPGAIGRNPSLLRkvapLALVkyDLESGEPirdaegrcikVPRGEPGLLisRINPLEPFDGYT 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 474 GePQKTFETVGQ------DKWYRTGDIALMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQEAQVVGVK--- 544
Cdd:cd05940 305 D-PAATEKKILRdvfkkgDAWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQvpg 383
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24418933 545 -DERMGeeiCACIRLKSGETTTAEEIKAFCKGKISHFKIPRYIVFVEGYPLTISGKIQKFKLREQ 608
Cdd:cd05940 384 tDGRAG---MAAIVLQPNEEFDLSALAAHLEKNLPGYARPLFLRLQPEMEITGTFKQQKVDLRNE 445
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
82-594 |
2.71e-24 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 106.11 E-value: 2.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 82 AQRFPDREALVILHEniRLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVSVNPAYQSS 161
Cdd:PRK09029 13 AQVRPQAIALRLNDE--VLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 162 ELEYVLRKVGCKGIVFPKQFKTqqyydilkqvcpelekaqpgalkserlPDLTTVISVDAPlpgtlllDDIVAAGGKEQN 241
Cdd:PRK09029 91 LLEELLPSLTLDFALVLEGENT---------------------------FSALTSLHLQLV-------EGAHAVAWQPQR 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 242 LAQLrynqrflscydpiniQFTSGTTGNPKGATLSHHNIVNNSmlIGQRLKMPTKTAEELRLVLPspLYHclgsvggtmV 321
Cdd:PRK09029 137 LATM---------------TLTSGSTGLPKAAVHTAQAHLASA--EGVLSLMPFTAQDSWLLSLP--LFH---------V 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 322 S--------MMHGATLLLsspsfngkkaleaisREKGTL---LYGT------PTMFVDILNQPDFSsydfTSIRGGVIAG 384
Cdd:PRK09029 189 SgqgivwrwLYAGATLVV---------------RDKQPLeqaLAGCthaslvPTQLWRLLDNRSEP----LSLKAVLLGG 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 385 SPAPPELIRAiinkmnMKELVVV----YGTTE-NSPVTfmnfpEDTLEQKAGsVGRIMPHTEAQIVNvetgeltnlnvpG 459
Cdd:PRK09029 250 AAIPVELTEQ------AEQQGIRcwcgYGLTEmASTVC-----AKRADGLAG-VGSPLPGREVKLVD------------G 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 460 ELYIRGYCVMQGYW--GEPQktfETVGQDKWYRTGDIALMDeQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQE 537
Cdd:PRK09029 306 EIWLRGASLALGYWrqGQLV---PLVNDEGWFATRDRGEWQ-NGELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQ 381
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 24418933 538 AQVVGVKDERMGEEICACIRLKSGETTtaEEIKAFCKGKISHFKIPryivfVEGYPL 594
Cdd:PRK09029 382 VFVVPVADAEFGQRPVAVVESDSEAAV--VNLAEWLQDKLARFQQP-----VAYYLL 431
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
262-608 |
4.00e-24 |
|
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: 105.98 E-value: 4.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 262 FTSGTTGNPKGATLSHHNIVNNSMLIGQRLKMptktAEELRLVLPSPLYHCLGSVGGTMVSMMHGATLLLSsPSFNGKKA 341
Cdd:cd05937 94 YTSGTTGLPKAAAISWRRTLVTSNLLSHDLNL----KNGDRTYTCMPLYHGTAAFLGACNCLMSGGTLALS-RKFSASQF 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 342 L-EAISREKGTLLY-GTPTMFvdILNQPDfSSYDFT-SIRggVIAGSPAPPELIRAIINKMNMKELVVVYGTTEnSPVTF 418
Cdd:cd05937 169 WkDVRDSGATIIQYvGELCRY--LLSTPP-SPYDRDhKVR--VAWGNGLRPDIWERFRERFNVPEIGEFYAATE-GVFAL 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 419 MNFPEDTLeqKAGSVG-----------------RIMPHTEAQIVNVETG--ELTNLNVPGELYIRGYCV----MQGYWGE 475
Cdd:cd05937 243 TNHNVGDF--GAGAIGhhglirrwkfenqvvlvKMDPETDDPIRDPKTGfcVRAPVGEPGEMLGRVPFKnreaFQGYLHN 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 476 PQKT----FETVGQ--DKWYRTGDIALMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQEAQVVGVK----D 545
Cdd:cd05937 321 EDATesklVRDVFRkgDIYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGVKvpghD 400
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24418933 546 ERMGeeiCACIRLKSGETTTAEEIKA----FCKGKISHFKIPRYIVFVEGYPLTISGKIQKFKLREQ 608
Cdd:cd05937 401 GRAG---CAAITLEESSAVPTEFTKSllasLARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVLRDE 464
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
65-600 |
1.07e-23 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 106.67 E-value: 1.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 65 TDSHLVNTTVGECLDATAQRFPDREALVILHenIRLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLAT 144
Cdd:PRK10252 451 TAVEIPETTLSALVAQQAAKTPDAPALADAR--YQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAI 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 145 AQAGIILVSVNPAYQSSELEYVLrkvgckgivfpkqfktqqyydilkqvcpelEKAQPGAL-----KSERLPDL--TTVI 217
Cdd:PRK10252 529 VEAGAAWLPLDTGYPDDRLKMML------------------------------EDARPSLLittadQLPRFADVpdLTSL 578
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 218 SVDAPLPgtlllddivAAGGKEQNLAQlrynqrflsCYDPINIQFTSGTTGNPKGATLSHHNIVNnsmligqRLK-MPTK 296
Cdd:PRK10252 579 CYNAPLA---------PQGAAPLQLSQ---------PHHTAYIIFTSGSTGRPKGVMVGQTAIVN-------RLLwMQNH 633
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 297 ---TAEElRLVLPSPlyhCLG--SVGGTMVSMMHGATLLLSSP-SFNGKKALEA-ISREKGTLLYGTPTMFVDILNQPDF 369
Cdd:PRK10252 634 yplTADD-VVLQKTP---CSFdvSVWEFFWPFIAGAKLVMAEPeAHRDPLAMQQfFAEYGVTTTHFVPSMLAAFVASLTP 709
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 370 SSYDFT--SIRGGVIAGSPAPPELIRAIINKMNMkELVVVYGTTENS-PVTFM-NFPEDTLEQKAGSV--GRIMPHTEAQ 443
Cdd:PRK10252 710 EGARQScaSLRQVFCSGEALPADLCREWQQLTGA-PLHNLYGPTEAAvDVSWYpAFGEELAAVRGSSVpiGYPVWNTGLR 788
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 444 IVN-----VETGeltnlnVPGELYIRGYCVMQGYWGEPQKTFETVGQD------KWYRTGDIALMDEQGFCKIVGRSKDM 512
Cdd:PRK10252 789 ILDarmrpVPPG------VAGDLYLTGIQLAQGYLGRPDLTASRFIADpfapgeRMYRTGDVARWLDDGAVEYLGRSDDQ 862
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 513 I-IRgGENIYPAELEDFFLKHPQVQE----AQVVGVKDERMGEE--ICACIRLKSGETTTAEEIKAFCKGKISHFKIPRY 585
Cdd:PRK10252 863 LkIR-GQRIELGEIDRAMQALPDVEQavthACVINQAAATGGDArqLVGYLVSQSGLPLDTSALQAQLRERLPPHMVPVV 941
|
570
....*....|....*
gi 24418933 586 IVFVEGYPLTISGKI 600
Cdd:PRK10252 942 LLQLDQLPLSANGKL 956
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
76-600 |
2.29e-23 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 103.82 E-value: 2.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 76 ECLDATAQRFPDREALVILHEniRLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVSVN 155
Cdd:PRK04813 6 ETIEEFAQTQPDFPAYDYLGE--KLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPVD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 156 payQSSELEYVLrkvgckgivfpkqfktqqyyDILkqvcpelEKAQPGALKS-ERLP---DLTTVISVDAplpgtllLDD 231
Cdd:PRK04813 84 ---VSSPAERIE--------------------MII-------EVAKPSLIIAtEELPleiLGIPVITLDE-------LKD 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 232 IVAAGGKEQNLAQLRYNQRFlscYdpinIQFTSGTTGNPKGATLSHHNIVN--NSML----IGQRLKMptktaeelrlvL 305
Cdd:PRK04813 127 IFATGNPYDFDHAVKGDDNY---Y----IIFTSGTTGKPKGVQISHDNLVSftNWMLedfaLPEGPQF-----------L 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 306 PSP----------LYHCLGSvGGTMVSMMHGATLllsspsfNGKKALEAISREKGTLLYGTPTmFVDI-LNQPDFSSYDF 374
Cdd:PRK04813 189 NQApysfdlsvmdLYPTLAS-GGTLVALPKDMTA-------NFKQLFETLPQLPINVWVSTPS-FADMcLLDPSFNEEHL 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 375 TSIRGGVIAGSPAPPELIRAIINKMNMKELVVVYGTTENS-PVTFMNFPEDTLEQ-KAGSVGRIMPHTEAQIVNvETGEL 452
Cdd:PRK04813 260 PNLTHFLFCGEELPHKTAKKLLERFPSATIYNTYGPTEATvAVTSIEITDEMLDQyKRLPIGYAKPDSPLLIID-EEGTK 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 453 TNLNVPGELYIRGYCVMQGYWGEPQKT----FETVGQdKWYRTGDIALMDE-QGFCKivGRSkDMIIRggENIYPAELED 527
Cdd:PRK04813 339 LPDGEQGEIVISGPSVSKGYLNNPEKTaeafFTFDGQ-PAYHTGDAGYLEDgLLFYQ--GRI-DFQIK--LNGYRIELEE 412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 528 --FFL-KHPQVQEAQVVGVKDERMGEEICACIRLKSG----ETTTAEEIKAFCKGKISHFKIPRYIVFVEGYPLTISGKI 600
Cdd:PRK04813 413 ieQNLrQSSYVESAVVVPYNKDHKVQYLIAYVVPKEEdferEFELTKAIKKELKERLMEYMIPRKFIYRDSLPLTPNGKI 492
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
262-608 |
4.09e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 103.22 E-value: 4.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 262 FTSGTTGNPKGATLSHHNIVN-NSMLIGQRLKMPTKTAeelrlVLPSPLYHCLGSVGGTMVSMMHGATLLLSsPSFNGKK 340
Cdd:PRK07867 159 FTSGTSGDPKAVRCTHRKVASaGVMLAQRFGLGPDDVC-----YVSMPLFHSNAVMAGWAVALAAGASIALR-RKFSASG 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 341 ALEAISREKGTLL-Y-GTPTMFvdIL---NQPDFSSydfTSIRggVIAGSPAPPELIRAIINKMNmkeLVVV--YGTTEN 413
Cdd:PRK07867 233 FLPDVRRYGATYAnYvGKPLSY--VLatpERPDDAD---NPLR--IVYGNEGAPGDIARFARRFG---CVVVdgFGSTEG 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 414 SpVTFMNFPeDTleqKAGSVGRIMPHTeaQIVNVETGE-----------LTNLNVP-GELY-IRGYCVMQGYWGEPQKTF 480
Cdd:PRK07867 303 G-VAITRTP-DT---PPGALGPLPPGV--AIVDPDTGTecppaedadgrLLNADEAiGELVnTAGPGGFEGYYNDPEADA 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 481 ETVgQDKWYRTGDIALMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQEAQVVGVKDERMGEEICACIRLKS 560
Cdd:PRK07867 376 ERM-RGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVMAALVLAP 454
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 24418933 561 GETTTAEEIKAFCKGK--ISHFKIPRYIVFVEGYPLTISGKIQKFKLREQ 608
Cdd:PRK07867 455 GAKFDPDAFAEFLAAQpdLGPKQWPSYVRVCAELPRTATFKVLKRQLSAE 504
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
253-605 |
5.35e-23 |
|
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: 102.17 E-value: 5.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 253 SCYdpinIQFTSGTTGNPKGATLSHHNIVNNsmLIGQRLKMptKTAEELRLVLPSPLyHCLGSVGGTMVSMMHGATLLLS 332
Cdd:cd17654 120 LAY----VIHTSGTTGTPKIVAVPHKCILPN--IQHFRSLF--NITSEDILFLTSPL-TFDPSVVEIFLSLSSGATLLIV 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 333 SPSFNGKKALEA---ISREKGTLLYGTPT---MFVDILNQPDFSSYDfTSIRGGVIAGSPAPPELI-RAIINKMNMKELV 405
Cdd:cd17654 191 PTSVKVLPSKLAdilFKRHRITVLQATPTlfrRFGSQSIKSTVLSAT-SSLRVLALGGEPFPSLVIlSSWRGKGNRTRIF 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 406 VVYGTTENSP-VTFMNFPEDTLEQKAGSvgrimphtEAQIVNVETGELTNLNVPGELYIRGY---CVMQGYWGEPQKTfe 481
Cdd:cd17654 270 NIYGITEVSCwALAYKVPEEDSPVQLGS--------PLLGTVIEVRDQNGSEGTGQVFLGGLnrvCILDDEVTVPKGT-- 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 482 tvgqdkWYRTGDIALMdEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQEAQVVGVKDERmgeeICACIRLKSG 561
Cdd:cd17654 340 ------MRATGDFVTV-KDGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGVESCAVTLSDQQR----LIAFIVGESS 408
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 24418933 562 ETTTAEEIKAFCKGkiSHfKIPRYIVFVEGYPLTISGKIQKFKL 605
Cdd:cd17654 409 SSRIHKELQLTLLS--SH-AIPDTFVQIDKLPLTSHGKVDKSEL 449
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
72-608 |
5.89e-23 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 103.42 E-value: 5.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 72 TTVGECLDATAQRFPDREALviLHENIRLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIIL 151
Cdd:PRK08279 37 RSLGDVFEEAAARHPDRPAL--LFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 152 VSVNPAYQSSELEYVLRKVGCKGIVfpkqfktqqyydilkqVCPEL----EKAQPGALKSERLPDLTTVISVDAPLPGTL 227
Cdd:PRK08279 115 ALLNTQQRGAVLAHSLNLVDAKHLI----------------VGEELveafEEARADLARPPRLWVAGGDTLDDPEGYEDL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 228 lldDIVAAGGKEQNLAQlrynQRFLSCYDPINIQFTSGTTGNPKGATLSHHNIvnnsMLIGQRLKMPTKTAEELRLVLPS 307
Cdd:PRK08279 179 ---AAAAAGAPTTNPAS----RSGVTAKDTAFYIYTSGTTGLPKAAVMSHMRW----LKAMGGFGGLLRLTPDDVLYCCL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 308 PLYH------CLGSVggtmvsMMHGATLLLsSPSFNGKKALEAISREKGtllygtpTMFVDI-------LNQPDfSSYDF 374
Cdd:PRK08279 248 PLYHntggtvAWSSV------LAAGATLAL-RRKFSASRFWDDVRRYRA-------TAFQYIgelcrylLNQPP-KPTDR 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 375 T-SIRggVIAGSPAPPELIRAIINKMNMKELVVVYGTTEnSPVTFMNFpedtlEQKAGSVGRI--MPHTEAQIV--NVET 449
Cdd:PRK08279 313 DhRLR--LMIGNGLRPDIWDEFQQRFGIPRILEFYAASE-GNVGFINV-----FNFDGTVGRVplWLAHPYAIVkyDVDT 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 450 GEltnlnvpgelYIR---GYCVM----------------QGYWG--EPQKT--------FEtVGqDKWYRTGDIALMDEQ 500
Cdd:PRK08279 385 GE----------PVRdadGRCIKvkpgevglligritdrGPFDGytDPEASekkilrdvFK-KG-DAWFNTGDLMRDDGF 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 501 GFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQEAQVVGVK----DERMGeeiCACIRLKSGETTTAEEIKAFCKGK 576
Cdd:PRK08279 453 GHAQFVDRLGDTFRWKGENVATTEVENALSGFPGVEEAVVYGVEvpgtDGRAG---MAAIVLADGAEFDLAALAAHLYER 529
|
570 580 590
....*....|....*....|....*....|..
gi 24418933 577 ISHFKIPRYIVFVEGYPLTISGKIQKFKLREQ 608
Cdd:PRK08279 530 LPAYAVPLFVRLVPELETTGTFKYRKVDLRKE 561
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
86-601 |
5.04e-22 |
|
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: 100.42 E-value: 5.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 86 PDREALVIL---HENIRLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVSVNPAYqsse 162
Cdd:cd05943 82 ADDPAAIYAaedGERTEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPDF---- 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 163 leyvlrkvGCKGIVfpkqfktqqyyDILKQVCPEL----------EKAQPGALK----SERLPDLTTVISVD-------- 220
Cdd:cd05943 158 --------GVPGVL-----------DRFGQIEPKVlfavdaytynGKRHDVREKvaelVKGLPSLLAVVVVPytvaagqp 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 221 --APLPGTLLLDDIVAAG-GKEQNLAQLRYNqrflscyDPINIQFTSGTTGNPKGATLSHhnivnNSMLIgQRLKmptkt 297
Cdd:cd05943 219 dlSKIAKALTLEDFLATGaAGELEFEPLPFD-------HPLYILYSSGTTGLPKCIVHGA-----GGTLL-QHLK----- 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 298 aeELRL---VLPSPLYHCLGSVGGTM----VS-MMHGATLLL--SSPSFNGKKALEAISREKGTLLYGTPTMFVDILNQP 367
Cdd:cd05943 281 --EHILhcdLRPGDRLFYYTTCGWMMwnwlVSgLAVGATIVLydGSPFYPDTNALWDLADEEGITVFGTSAKYLDALEKA 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 368 DFS---SYDFTSIRGGVIAGSPAPPELIRAIINKMNMKELVVVY--GTTENSPVTFMNFpedTLEQKAGSVGRIMPHTEA 442
Cdd:cd05943 359 GLKpaeTHDLSSLRTILSTGSPLKPESFDYVYDHIKPDVLLASIsgGTDIISCFVGGNP---LLPVYRGEIQCRGLGMAV 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 443 QIVNVETGELTNlnVPGELYI-RGYCVMQ-GYWGEPQ---------KTFETVgqdkWyRTGDIALMDEQGFCKIVGRSKD 511
Cdd:cd05943 436 EAFDEEGKPVWG--EKGELVCtKPFPSMPvGFWNDPDgsryraayfAKYPGV----W-AHGDWIEITPRGGVVILGRSDG 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 512 MIIRGGENIYPAELEDFFLKHPQVQEAQVVGVKDERMGEEICACIRLKSGETTT---AEEIKAFCKGKISHFKIPRYIVF 588
Cdd:cd05943 509 TLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDERVILFVKLREGVELDdelRKRIRSTIRSALSPRHVPAKIIA 588
|
570
....*....|...
gi 24418933 589 VEGYPLTISGKIQ 601
Cdd:cd05943 589 VPDIPRTLSGKKV 601
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
524-599 |
7.05e-22 |
|
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: 89.53 E-value: 7.05e-22
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24418933 524 ELEDFFLKHPQVQEAQVVGVKDERMGEEICACIRLKSGETTTAEEIKAFCKGKISHFKIPRYIVFVEGYPLTISGK 599
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
263-608 |
2.34e-21 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 95.88 E-value: 2.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 263 TSGTTGNPKGATLSHHNIVNNSMLIGQRLKMPTktaeelRLVLPSPLYHclgsVGGTMV---SMMHGA--TLLLSSPSFN 337
Cdd:PRK07824 43 TSGTTGTPKGAMLTAAALTASADATHDRLGGPG------QWLLALPAHH----IAGLQVlvrSVIAGSepVELDVSAGFD 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 338 GKKALEAISREKGTLLYG--TPTMFVDILNQPDFSSY--DFTSIrggVIAGSPAP-PELIRAIINKMNmkeLVVVYGTTE 412
Cdd:PRK07824 113 PTALPRAVAELGGGRRYTslVPMQLAKALDDPAATAAlaELDAV---LVGGGPAPaPVLDAAAAAGIN---VVRTYGMSE 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 413 NSpvtfmnfpedtleqkAGSV--GRIMPHTEAQIVNvetgeltnlnvpGELYIRGYCVMQGYWGEPQktFETVGQDKWYR 490
Cdd:PRK07824 187 TS---------------GGCVydGVPLDGVRVRVED------------GRIALGGPTLAKGYRNPVD--PDPFAEPGWFR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 491 TGDIALMDEqGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQEAQVVGVKDERMGEEICACIRLKSGETTTAEEIK 570
Cdd:PRK07824 238 TDDLGALDD-GVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAVVGDGGPAPTLEALR 316
|
330 340 350
....*....|....*....|....*....|....*...
gi 24418933 571 AFCKGKISHFKIPRYIVFVEGYPLTISGKIQKFKLREQ 608
Cdd:PRK07824 317 AHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALVRR 354
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
260-599 |
3.78e-21 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 97.19 E-value: 3.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 260 IQFTSGTTGNPKGATLSHHNIVNNsmligQR--LKMPTKTAEELRLVLPSPlYHCLGSVGGTMVSMMHGATLLLSSPSFN 337
Cdd:PRK06334 188 ILFTSGTEKLPKGVPLTHANLLAN-----QRacLKFFSPKEDDVMMSFLPP-FHAYGFNSCTLFPLLSGVPVVFAYNPLY 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 338 GKKALEAISREKGTLLYGTPTMFVDILNQPDFSSYDFTSIRGGVIAGSPAPPELIRAIINKMNMKELVVVYGTTENSPVT 417
Cdd:PRK06334 262 PKKIVEMIDEAKVTFLGSTPVFFDYILKTAKKQESCLPSLRFVVIGGDAFKDSLYQEALKTFPHIQLRQGYGTTECSPVI 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 418 FMNFPEDTleQKAGSVGRIMPHTEAQIVNVETGELTNLNVPGELYIRGYCVMQGYWGE-PQKTFETVGQDKWYRTGDIAL 496
Cdd:PRK06334 342 TINTVNSP--KHESCVGMPIRGMDVLIVSEETKVPVSSGETGLVLTRGTSLFSGYLGEdFGQGFVELGGETWYVTGDLGY 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 497 MDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKH---PQVQEAQ---VVGVKDERmgEEICacirLKSGETTTAEEIK 570
Cdd:PRK06334 420 VDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEGfgqNAADHAGplvVCGLPGEK--VRLC----LFTTFPTSISEVN 493
|
330 340 350
....*....|....*....|....*....|
gi 24418933 571 AFCKG-KISHFKIPRYIVFVEGYPLTISGK 599
Cdd:PRK06334 494 DILKNsKTSSILKISYHHQVESIPMLGTGK 523
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
73-502 |
1.87e-20 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 95.33 E-value: 1.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 73 TVGECLDATAQRFPDREALV---ILHENIRLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGI 149
Cdd:PRK08180 40 RLTDRLVHWAQEAPDRVFLAergADGGWRRLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALAAMYAGV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 150 ILVSVNPAYqS------SELEYVLRKVGcKGIVFpkqfktqqyydilkqvcpelekAQPG-----ALKSERLPDlTTVIS 218
Cdd:PRK08180 120 PYAPVSPAY-SlvsqdfGKLRHVLELLT-PGLVF----------------------ADDGaafarALAAVVPAD-VEVVA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 219 VDAPLPG--TLLLDDIVAA---GGKEQNLAQLRYNQ--RFLscydpiniqFTSGTTGNPKGATLSHHNIVNNSMLIGQRl 291
Cdd:PRK08180 175 VRGAVPGraATPFAALLATpptAAVDAAHAAVGPDTiaKFL---------FTSGSTGLPKAVINTHRMLCANQQMLAQT- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 292 kMPTKTAEELRLVLPSPLYHCLGsvGGTMVSMM--HGATLLLSspsfNGK-------KALEAISREKGTLLYGTPT---M 359
Cdd:PRK08180 245 -FPFLAEEPPVLVDWLPWNHTFG--GNHNLGIVlyNGGTLYID----DGKptpggfdETLRNLREISPTVYFNVPKgweM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 360 FVDILNQPD------FSSYDFTSIRGgviAGSPAPpelIRAIINKMNMKE------LVVVYGTTENSPV-TFMNFPEDtl 426
Cdd:PRK08180 318 LVPALERDAalrrrfFSRLKLLFYAG---AALSQD---VWDRLDRVAEATcgerirMMTGLGMTETAPSaTFTTGPLS-- 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 427 eqKAGSVGRIMPHTEAQIVNVEtGELtnlnvpgELYIRGYCVMQGYWGEPQKTFETVGQDKWYRTGD-IALMD----EQG 501
Cdd:PRK08180 390 --RAGNIGLPAPGCEVKLVPVG-GKL-------EVRVKGPNVTPGYWRAPELTAEAFDEEGYYRSGDaVRFVDpadpERG 459
|
.
gi 24418933 502 F 502
Cdd:PRK08180 460 L 460
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
98-543 |
3.18e-20 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 93.68 E-value: 3.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 98 IRLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVSVNPAYQSSELeyvlrkVGCkgivf 177
Cdd:cd05910 1 SRLSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNL------KQC----- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 178 pkqfktqqyydilkqvcpeLEKAQPGALKSERLPDlttvisvdaplpgtlllddivaaggkeqnlaqlrynqrflscyDP 257
Cdd:cd05910 70 -------------------LQEAEPDAFIGIPKAD-------------------------------------------EP 87
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 258 INIQFTSGTTGNPKGATLSHhnivnnSMLIGQ--RLKMPTKTAEELRLVLPSPLYHCLGSVGG--TMVSMMHGATLLLSS 333
Cdd:cd05910 88 AAILFTSGSTGTPKGVVYRH------GTFAAQidALRQLYGIRPGEVDLATFPLFALFGPALGltSVIPDMDPTRPARAD 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 334 PsfngKKALEAISREKGTLLYGTPTMFVDILNQPDFSSYDFTSIRGGVIAGSPAPPELIRAIiNKM--NMKELVVVYGTT 411
Cdd:cd05910 162 P----QKLVGAIRQYGVSIVFGSPALLERVARYCAQHGITLPSLRRVLSAGAPVPIALAARL-RKMlsDEAEILTPYGAT 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 412 ENSPVTFMNFPE------DTLEQKAGS-VGRIMPHTEAQIVNVETGELT--------NLNVPGELYIRGYCVMQGYWGEP 476
Cdd:cd05910 237 EALPVSSIGSREllatttAATSGGAGTcVGRPIPGVRVRIIEIDDEPIAewddtlelPRGEIGEITVTGPTVTPTYVNRP 316
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24418933 477 QKT----FETVGQDKWYRTGDIALMDEQG---FCkivGRSKDMIIRGGENIYPAELEDFFLKHPQVQEAQVVGV 543
Cdd:cd05910 317 VATalakIDDNSEGFWHRMGDLGYLDDEGrlwFC---GRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVGV 387
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
429-600 |
5.33e-20 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 94.05 E-value: 5.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 429 KAGSVGRIMPHTEAQIVNvETGELtnlnVPGElyIRGYCV--------MQGYWGEPQKTFETV-GQDKW-YRTGDIALMD 498
Cdd:PRK00174 422 KPGSATRPLPGIQPAVVD-EEGNP----LEGG--EGGNLVikdpwpgmMRTIYGDHERFVKTYfSTFKGmYFTGDGARRD 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 499 EQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQEAQVVGVKDERMGEEICACIRLKSGETTTAE---EIKAFCKG 575
Cdd:PRK00174 495 EDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLKGGEEPSDElrkELRNWVRK 574
|
170 180
....*....|....*....|....*
gi 24418933 576 KISHFKIPRYIVFVEGYPLTISGKI 600
Cdd:PRK00174 575 EIGPIAKPDVIQFAPGLPKTRSGKI 599
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
99-608 |
5.81e-20 |
|
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: 93.51 E-value: 5.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 99 RLNFAQLKEEVDKAASGLLS-IGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVSVNPAYQSSELEYVLRKVGCKGIVF 177
Cdd:cd05938 5 TYTYRDVDRRSNQAARALLAhAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAKVLVV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 178 PKQFKtqqyyDILKQVCPELEKAQPGALkserlpdlttVISVDAPLPGTLLLDDIVAAGGKEQNLAQLRYNQRFLScydP 257
Cdd:cd05938 85 APELQ-----EAVEEVLPALRADGVSVW----------YLSHTSNTEGVISLLDKVDAASDEPVPASLRAHVTIKS---P 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 258 INIQFTSGTTGNPKGATLSHHNIVNNS---MLIGQrlkmptkTAEELrLVLPSPLYHCLGSVGGTMVSMMHGATLLL--- 331
Cdd:cd05938 147 ALYIYTSGTTGLPKAARISHLRVLQCSgflSLCGV-------TADDV-IYITLPLYHSSGFLLGIGGCIELGATCVLkpk 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 332 -SSPSF--NGKKALEAISREKGTLL-YgtptmfvdILNQPDFSSYDFTSIRggVIAGSPAPPELIRAIINKMNMKELVVV 407
Cdd:cd05938 219 fSASQFwdDCRKHNVTVIQYIGELLrY--------LCNQPQSPNDRDHKVR--LAIGNGLRADVWREFLRRFGPIRIREF 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 408 YGTTENSpVTFMNFPEdtleqKAGSVGRI-----MPHTEAQI-VNVETGEltnlnvPgelyIR---GYCV---------- 468
Cdd:cd05938 289 YGSTEGN-IGFFNYTG-----KIGAVGRVsylykLLFPFELIkFDVEKEE------P----VRdaqGFCIpvakgepgll 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 469 ---------MQGYWGEPQKT--------FETvgQDKWYRTGDIALMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLK 531
Cdd:cd05938 353 vakitqqspFLGYAGDKEQTekkllrdvFKK--GDVYFNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGL 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 532 HPQVQEAQVVGVK----DERMGeeiCACIRLKSGETTTAEEIKAFCKGKISHFKIPRYIVFVEGYPLTISGKIQKFKLRE 607
Cdd:cd05938 431 LDFLQEVNVYGVTvpghEGRIG---MAAVKLKPGHEFDGKKLYQHVREYLPAYARPRFLRIQDSLEITGTFKQQKVRLVE 507
|
.
gi 24418933 608 Q 608
Cdd:cd05938 508 E 508
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
256-610 |
2.41e-19 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 91.75 E-value: 2.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 256 DPINIQFTSGTTGNPKGATLSHHNIVNNSMLIGQRLKMPTKTAEELRLVlpsPLYHCLGsVGGTMVSMMHGATLLLS-SP 334
Cdd:PRK05851 153 GPAVLQGTAGSTGTPRTAILSPGAVLSNLRGLNARVGLDAATDVGCSWL---PLYHDMG-LAFLLTAALAGAPLWLApTT 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 335 SFNGK--KALEAISREKGTLLYGtPTMFVDILNQ--PDFSSYDFTSIRGGVIAGSPAPPELIRAIINKM-----NMKELV 405
Cdd:PRK05851 229 AFSASpfRWLSWLSDSRATLTAA-PNFAYNLIGKyaRRVSDVDLGALRVALNGGEPVDCDGFERFATAMapfgfDAGAAA 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 406 VVYGTTENS-------PVTFMNFPEDTLE-----QKAGSVGRIMPHTEAQIVNVETGELTNLNVPGELYIRGYCVMQGYW 473
Cdd:PRK05851 308 PSYGLAESTcavtvpvPGIGLRVDEVTTDdgsgaRRHAVLGNPIPGMEVRISPGDGAAGVAGREIGEIEIRGASMMSGYL 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 474 GEPqktfeTVGQDKWYRTGDIALMDEQGFCkIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQEAQVVGV-KDE---RMG 549
Cdd:PRK05851 388 GQA-----PIDPDDWFPTGDLGYLVDGGLV-VCGRAKELITVAGRNIFPTEIERVAAQVRGVREGAVVAVgTGEgsaRPG 461
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24418933 550 EEICACIRLKSGETTTAEEIK---AFCKgkishfKIPRYIVFVE--GYPLTISGKIQKFKLREQME 610
Cdd:PRK05851 462 LVIAAEFRGPDEAGARSEVVQrvaSECG------VVPSDVVFVApgSLPRTSSGKLRRLAVKRSLE 521
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
84-542 |
5.14e-19 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 90.93 E-value: 5.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 84 RFPDREALVILHEN-----------------IR----------LNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYA 136
Cdd:PLN02736 36 RFPDHPEIGTLHDNfvyavetfrdykylgtrIRvdgtvgeykwMTYGEAGTARTAIGSGLVQHGIPKGACVGLYFINRPE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 137 WVLIQLATAQAGiiLVSVnPAYQS---SELEYVLRKVGCKGIvfpkqFKTQQYYDILKQVCPELekaqpgalKSERLpdL 213
Cdd:PLN02736 116 WLIVDHACSAYS--YVSV-PLYDTlgpDAVKFIVNHAEVAAI-----FCVPQTLNTLLSCLSEI--------PSVRL--I 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 214 TTVISVDAPLPGTlllddIVAAGGK----EQNLAQLRYNQRFLSCYDP---INIQFTSGTTGNPKGATLSHHNIVNNSML 286
Cdd:PLN02736 178 VVVGGADEPLPSL-----PSGTGVEivtySKLLAQGRSSPQPFRPPKPedvATICYTSGTTGTPKGVVLTHGNLIANVAG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 287 IGQRLKMptktaeelrlvLPS-------PLYHCLGSVggTMVSMMH-GATLLLsspsFNGK--KALEAISREKGTLLYGT 356
Cdd:PLN02736 253 SSLSTKF-----------YPSdvhisylPLAHIYERV--NQIVMLHyGVAVGF----YQGDnlKLMDDLAALRPTIFCSV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 357 PTMFVDI-------------LNQPDFSSYdFTSIRGGVIAGSPAPPELIRAIINKMNMK--------------------E 403
Cdd:PLN02736 316 PRLYNRIydgitnavkesggLKERLFNAA-YNAKKQALENGKNPSPMWDRLVFNKIKAKlggrvrfmssgasplspdvmE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 404 LVVV---------YGTTENSPVTFMNFPEDTLeqkAGSVGRIMPHTEAQIVNVETGELTNLNVP---GELYIRGYCVMQG 471
Cdd:PLN02736 395 FLRIcfggrvlegYGMTETSCVISGMDEGDNL---SGHVGSPNPACEVKLVDVPEMNYTSEDQPyprGEICVRGPIIFKG 471
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24418933 472 YWGEPQKTFETVGQDKWYRTGDIALMDEQGFCKIVGRSKDMI-IRGGENIYPAELEDFFLKHPQVQEAQVVG 542
Cdd:PLN02736 472 YYKDEVQTREVIDEDGWLHTGDIGLWLPGGRLKIIDRKKNIFkLAQGEYIAPEKIENVYAKCKFVAQCFVYG 543
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
76-613 |
1.13e-18 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 91.00 E-value: 1.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 76 ECLDATAQRFPDREALVilHENIRLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVSVN 155
Cdd:PRK05691 1135 ELLNEQARQTPERIALV--WDGGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLD 1212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 156 PAYQSSELEYVLRKVGCkgivfpkqfktqqyydilkqvcpELEKAQPGALksERLPDLTTVISVDAplpGTLLLDDI-VA 234
Cdd:PRK05691 1213 PDYPAERLAYMLADSGV-----------------------ELLLTQSHLL--ERLPQAEGVSAIAL---DSLHLDSWpSQ 1264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 235 AGG---KEQNLAQLRYnqrflscydpiniqfTSGTTGNPKGATLSHhnivnnsMLIGQRLKMPTKT---AEELRLVLPSP 308
Cdd:PRK05691 1265 APGlhlHGDNLAYVIY---------------TSGSTGQPKGVGNTH-------AALAERLQWMQATyalDDSDVLMQKAP 1322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 309 LYHCLgSVGGTMVSMMHGATLLLSSPS--FNGKKALEAISREKGTLLYGTPTMFVDILNQPDfsSYDFTSIRGGVIAGSP 386
Cdd:PRK05691 1323 ISFDV-SVWECFWPLITGCRLVLAGPGehRDPQRIAELVQQYGVTTLHFVPPLLQLFIDEPL--AAACTSLRRLFSGGEA 1399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 387 APPELIRAIINKMNMKELVVVYGTTENS-PVTFMNFPEDTLEQKAgsVGRIMPHTEAQIVNVETgELTNLNVPGELYIRG 465
Cdd:PRK05691 1400 LPAELRNRVLQRLPQVQLHNRYGPTETAiNVTHWQCQAEDGERSP--IGRPLGNVLCRVLDAEL-NLLPPGVAGELCIGG 1476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 466 YCVMQGYWGEPQKTFE-----TVGQD--KWYRTGDIALMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQEA 538
Cdd:PRK05691 1477 AGLARGYLGRPALTAErfvpdPLGEDgaRLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQA 1556
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24418933 539 QVVgVKDERMGEEICACIRLKSGETTTAEEIKAFCKGKISHFKIPRYIVFVEGYPLTISGKIQKFKLRE---QMEQHL 613
Cdd:PRK05691 1557 AVL-VREGAAGAQLVGYYTGEAGQEAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRALPEpvwQQREHV 1633
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
58-612 |
3.71e-17 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 85.99 E-value: 3.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 58 LSYIQGHTDSHLVNTTVGECLDATAQRFPDREALVILHENirLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAW 137
Cdd:PRK05691 2174 LDSLAGEAGEARLDQTLHGLFAAQAARTPQAPALTFAGQT--LSYAELDARANRLARALRERGVGPQVRVGLALERSLEM 2251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 138 VLIQLATAQAGIILVSVNPAYQSSELEYVLRKVGCkGIVFPkqfktqqyYDILKQVCPELekaqPGALKSERLPDLTTVI 217
Cdd:PRK05691 2252 VVGLLAILKAGGAYVPLDPEYPLERLHYMIEDSGI-GLLLS--------DRALFEALGEL----PAGVARWCLEDDAAAL 2318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 218 SV--DAPLPGTLLlddivaaggkEQNLAQLRYnqrflscydpiniqfTSGTTGNPKGATLSHHNIVNNSMLIGQRLKMPT 295
Cdd:PRK05691 2319 AAysDAPLPFLSL----------PQHQAYLIY---------------TSGSTGKPKGVVVSHGEIAMHCQAVIERFGMRA 2373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 296 KTAE-----------ELRLVLPsplyhclgsvggtmvsMMHGATLLLSSpsfNGKKALEAIS---REKGTLLYG-TPTmF 360
Cdd:PRK05691 2374 DDCElhfysinfdaaSERLLVP----------------LLCGARVVLRA---QGQWGAEEICqliREQQVSILGfTPS-Y 2433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 361 VDILNQPDFSSYDFTSIRGGVIAGSPAPPELIRAIINKMNMKELVVVYGTTENSPVTFMNFPEDTLEQKAGSV--GRIMP 438
Cdd:PRK05691 2434 GSQLAQWLAGQGEQLPVRMCITGGEALTGEHLQRIRQAFAPQLFFNAYGPTETVVMPLACLAPEQLEEGAASVpiGRVVG 2513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 439 HTEAQIVNVETGeLTNLNVPGELYIRGYCVMQGYWGEPQKTFETVGQD-------KWYRTGDIALMDEQGFCKIVGRSKD 511
Cdd:PRK05691 2514 ARVAYILDADLA-LVPQGATGELYVGGAGLAQGYHDRPGLTAERFVADpfaadggRLYRTGDLVRLRADGLVEYVGRIDH 2592
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 512 MI-IRGGEnIYPAELEDFFLKHPQVQEAQVVGVkDERMGEEIC---ACIRLKSGETTTA---EEIKAFCKGKISHFKIPR 584
Cdd:PRK05691 2593 QVkIRGFR-IELGEIESRLLEHPAVREAVVLAL-DTPSGKQLAgylVSAVAGQDDEAQAalrEALKAHLKQQLPDYMVPA 2670
|
570 580 590
....*....|....*....|....*....|..
gi 24418933 585 YIVFVEGYPLTISGKIQKFKLR----EQMEQH 612
Cdd:PRK05691 2671 HLILLDSLPLTANGKLDRRALPapdpELNRQA 2702
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
99-613 |
4.31e-17 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 84.95 E-value: 4.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 99 RLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVSVNPAYQSSELEYvlRKVGCKgivfP 178
Cdd:PLN02654 120 SLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQ--RIVDCK----P 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 179 KQFKTqqyydilkqvCPELEKAqpgaLKSERLPDLttvisVDAPLP---------GTLLLDDIVAAGGKEQNLAQLRYN- 248
Cdd:PLN02654 194 KVVIT----------CNAVKRG----PKTINLKDI-----VDAALDesakngvsvGICLTYENQLAMKREDTKWQEGRDv 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 249 --QRFLSCY------------DPINIQFTSGTTGNPKGA--TLSHHNIVNNSMLigqrlkmptKTAEELRlvlPSPLYHC 312
Cdd:PLN02654 255 wwQDVVPNYptkcevewvdaeDPLFLLYTSGSTGKPKGVlhTTGGYMVYTATTF---------KYAFDYK---PTDVYWC 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 313 LGSVGG-------TMVSMMHGATLLL--SSPSF-NGKKALEAISREKGTLLYGTPTMFVDILNQPD--FSSYDFTSIR-- 378
Cdd:PLN02654 323 TADCGWitghsyvTYGPMLNGATVLVfeGAPNYpDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGDeyVTRHSRKSLRvl 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 379 GGViaGSPAPPELIRAIINKMNMKELVV--VYGTTENSpvTFMNFP-EDTLEQKAGSVgrIMPHTEAQIVNV-ETGEltn 454
Cdd:PLN02654 403 GSV--GEPINPSAWRWFFNVVGDSRCPIsdTWWQTETG--GFMITPlPGAWPQKPGSA--TFPFFGVQPVIVdEKGK--- 473
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 455 lNVPGElyIRGYCVMQGYWgepQKTFETVGQDK-------------WYRTGDIALMDEQGFCKIVGRSKDMIIRGGENIY 521
Cdd:PLN02654 474 -EIEGE--CSGYLCVKKSW---PGAFRTLYGDHeryettyfkpfagYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIG 547
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 522 PAELEDFFLKHPQVQEAQVVGVKDERMGEEICACIRLKSGETTTAEEIKAF---CKGKISHFKIPRYIVFVEGYPLTISG 598
Cdd:PLN02654 548 TAEVESALVSHPQCAEAAVVGIEHEVKGQGIYAFVTLVEGVPYSEELRKSLiltVRNQIGAFAAPDKIHWAPGLPKTRSG 627
|
570
....*....|....*
gi 24418933 599 KIQKFKLREQMEQHL 613
Cdd:PLN02654 628 KIMRRILRKIASRQL 642
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
102-542 |
7.00e-17 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 84.48 E-value: 7.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 102 FAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILV---------SVNPAYQSSELEYVL---RK 169
Cdd:PLN02430 79 YKEVYEEVLQIGSALRASGAEPGSRVGIYGSNCPQWIVAMEACAAHSLICVplydtlgpgAVDYIVDHAEIDFVFvqdKK 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 170 VgcKGIVFP-----KQFKTQQYYDILKQvcPELEKAQPGALKSERLPDLTTVisvdaplpgtlllddivaagGKEqNLAQ 244
Cdd:PLN02430 159 I--KELLEPdcksaKRLKAIVSFTSVTE--EESDKASQIGVKTYSWIDFLHM--------------------GKE-NPSE 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 245 LRYNQRFLSCydpiNIQFTSGTTGNPKGATLSHHNIVnnSMLIGQRLKMPT----KTAEELRLVLpSPLYHCLGSV---- 316
Cdd:PLN02430 214 TNPPKPLDIC----TIMYTSGTSGDPKGVVLTHEAVA--TFVRGVDLFMEQfedkMTHDDVYLSF-LPLAHILDRMieey 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 317 ---GGTMVSMMHG-------------ATLLLSSPS-----FNG-KKALEAISREKGTLLYGTPTMFVDILNQPDFSSY-- 372
Cdd:PLN02430 287 ffrKGASVGYYHGdlnalrddlmelkPTLLAGVPRvferiHEGiQKALQELNPRRRLIFNALYKYKLAWMNRGYSHKKas 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 373 ---DFTSIR------GG-----VIAGSPAPPElIRAIINKMNMKELVVVYGTTENSPVTFMNFPEDTleQKAGSVGRIMP 438
Cdd:PLN02430 367 pmaDFLAFRkvkaklGGrlrllISGGAPLSTE-IEEFLRVTSCAFVVQGYGLTETLGPTTLGFPDEM--CMLGTVGAPAV 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 439 HTEAQIVNVETGELTNLNVP--GELYIRGYCVMQGYWGEPQKTFETVgQDKWYRTGDIALMDEQGFCKIVGRSKDMI-IR 515
Cdd:PLN02430 444 YNELRLEEVPEMGYDPLGEPprGEICVRGKCLFSGYYKNPELTEEVM-KDGWFHTGDIGEILPNGVLKIIDRKKNLIkLS 522
|
490 500
....*....|....*....|....*..
gi 24418933 516 GGENIYPAELEDFFLKHPQVQEAQVVG 542
Cdd:PLN02430 523 QGEYVALEYLENVYGQNPIVEDIWVYG 549
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
82-600 |
1.77e-16 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 83.07 E-value: 1.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 82 AQRfPDREALVIL----HENIRLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGII------- 150
Cdd:PRK10524 64 AKR-PEQLALIAVstetDEERTYTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLACARIGAIhsvvfgg 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 151 LVSVNPAYQSSELEYVL--------RkvGCKgiVFPkqfktqqYYDILKQVCpELEKAQPGAlkserlpdlttVISVDAP 222
Cdd:PRK10524 143 FASHSLAARIDDAKPVLivsadagsR--GGK--VVP-------YKPLLDEAI-ALAQHKPRH-----------VLLVDRG 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 223 LpgtlllDDIVAAGGKEQNLAQLRynQRF---------LSCYDPINIQFTSGTTGNPKGAtlshhnivnnsmligQRlkm 293
Cdd:PRK10524 200 L------APMARVAGRDVDYATLR--AQHlgarvpvewLESNEPSYILYTSGTTGKPKGV---------------QR--- 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 294 ptktaeelrlvlpsplyhclgSVGGTMV----SMMH------GATLLLSS--------------PSFNGKkaleaisrek 349
Cdd:PRK10524 254 ---------------------DTGGYAValatSMDTifggkaGETFFCASdigwvvghsyivyaPLLAGM---------- 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 350 GTLLY-GTPT------------------MF-----VDILNQPD---FSSYDFTSIRGGVIAGSPAPPELIRAIINKMNmK 402
Cdd:PRK10524 303 ATIMYeGLPTrpdagiwwrivekykvnrMFsaptaIRVLKKQDpalLRKHDLSSLRALFLAGEPLDEPTASWISEALG-V 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 403 ELVVVYGTTENS-PV-TFMNFPEDTlEQKAGSVGRIMPHTEAQIVNVETGELTNLNVPGELYIRGY----CvMQGYWGEP 476
Cdd:PRK10524 382 PVIDNYWQTETGwPIlAIARGVEDR-PTRLGSPGVPMYGYNVKLLNEVTGEPCGPNEKGVLVIEGPlppgC-MQTVWGDD 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 477 Q---KT-FETVGQdKWYRTGDIALMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQEAQVVGVKDERMGEEI 552
Cdd:PRK10524 460 DrfvKTyWSLFGR-QVYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALKGQVA 538
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 24418933 553 CACIRLKSGETTTAE--------EIKAFCKGKISHFKIPRYIVFVEGYPLTISGKI 600
Cdd:PRK10524 539 VAFVVPKDSDSLADRearlalekEIMALVDSQLGAVARPARVWFVSALPKTRSGKL 594
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
86-601 |
1.82e-16 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 82.92 E-value: 1.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 86 PDREALVILHEN---IRLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVSVNPAYqsse 162
Cdd:PRK03584 98 DDRPAIIFRGEDgprRELSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLATASLGAIWSSCSPDF---- 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 163 leyvlrkvGCKGIVfpkqfktqqyyDILKQVCPELEKAQPG---------------ALkSERLPDLTTVISVD------- 220
Cdd:PRK03584 174 --------GVQGVL-----------DRFGQIEPKVLIAVDGyryggkafdrrakvaEL-RAALPSLEHVVVVPylgpaaa 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 221 -APLPGTLLLDDIVAAGGKeqnlAQLRYNQRFLScyDPINIQFTSGTTGNPKGATLSHHNIVnnsmLigQRLKmptktae 299
Cdd:PRK03584 234 aAALPGALLWEDFLAPAEA----AELEFEPVPFD--HPLWILYSSGTTGLPKCIVHGHGGIL----L--EHLK------- 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 300 ELRLvlpsplyHC-LG---------SVGGTM----VS-MMHGATLLL--SSPSFNGKKAL-EAISREKGTLLyGTPTMFV 361
Cdd:PRK03584 295 ELGL-------HCdLGpgdrffwytTCGWMMwnwlVSgLLVGATLVLydGSPFYPDPNVLwDLAAEEGVTVF-GTSAKYL 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 362 DILNQPDFS---SYDFTSIRGGVIAGSPAPPELIRAIINkmNMKE---LVVVYGTTenspvtfmnfpeDTLEQKAGSVgR 435
Cdd:PRK03584 367 DACEKAGLVpgeTHDLSALRTIGSTGSPLPPEGFDWVYE--HVKAdvwLASISGGT------------DICSCFVGGN-P 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 436 IMPHTEAQI------VNVE---------TGELtnlnvpGELYIRgycvmQ-------GYWGEPQ---------KTFETVg 484
Cdd:PRK03584 432 LLPVYRGEIqcrglgMAVEawdedgrpvVGEV------GELVCT-----KpfpsmplGFWNDPDgsryrdayfDTFPGV- 499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 485 qdkWyRTGDIALMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQEAQVVGVKDERMGEEICACIRLKSGETT 564
Cdd:PRK03584 500 ---W-RHGDWIEITEHGGVVIYGRSDATLNRGGVRIGTAEIYRQVEALPEVLDSLVIGQEWPDGDVRMPLFVVLAEGVTL 575
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 24418933 565 TAE---EIKAFCKGKIS--HfkIPRYIVFVEGYPLTISGKIQ 601
Cdd:PRK03584 576 DDAlraRIRTTIRTNLSprH--VPDKIIAVPDIPRTLSGKKV 615
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
257-602 |
2.00e-16 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 82.87 E-value: 2.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 257 PINIQFTSGTTGNPKGATLShhnivNNSMLIGQRLKMPTKTAEELRLVLPSplYHCLGSV---GGTMVSMMHGATLLLSS 333
Cdd:PTZ00237 256 PLYILYTSGTTGNSKAVVRS-----NGPHLVGLKYYWRSIIEKDIPTVVFS--HSSIGWVsfhGFLYGSLSLGNTFVMFE 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 334 PSFNGKKALE-----AISREKGTLLYGTP-TMFVDILNQPD----FSSYDFTSIRGGVIAGSPAPPELIRAIINKMNMKE 403
Cdd:PTZ00237 329 GGIIKNKHIEddlwnTIEKHKVTHTLTLPkTIRYLIKTDPEatiiRSKYDLSNLKEIWCGGEVIEESIPEYIENKLKIKS 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 404 LVVvYGTTENSPVTFMNFpeDTLEQKAGSVGRIMPHTEAQIVNvETGELTNLNVPGELYIRgYCVMQGYWGEPQKTFETV 483
Cdd:PTZ00237 409 SRG-YGQTEIGITYLYCY--GHINIPYNATGVPSIFIKPSILS-EDGKELNVNEIGEVAFK-LPMPPSFATTFYKNDEKF 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 484 GQ-----DKWYRTGDIALMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQEAQVVGVKDERMGEEICACIRL 558
Cdd:PTZ00237 484 KQlfskfPGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPIGLLVL 563
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 24418933 559 KSGETTTA-------EEIKAFCKGKISHFKIPRYIVFVEGYPLTISGKIQK 602
Cdd:PTZ00237 564 KQDQSNQSidlnklkNEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPR 614
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
100-510 |
3.49e-16 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 82.33 E-value: 3.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 100 LNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWvliqLATAQA----GIILVSVNPAYQSSELEYVLRKVGCKGI 175
Cdd:PTZ00216 122 ITYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEW----LASIYGiwsqSMVAATVYANLGEDALAYALRETECKAI 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 176 VFPKqfktqqyydilKQVCPELEKAQPGALKSerlpdlTTVISVDApLPGTLLLD--------DIVAAGGKEQNLAQLRY 247
Cdd:PTZ00216 198 VCNG-----------KNVPNLLRLMKSGGMPN------TTIIYLDS-LPASVDTEgcrlvawtDVVAKGHSAGSHHPLNI 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 248 NqrfLSCYDPINIQFTSGTTGNPKGATLSHHNIVNNSMLIGQRLKMPTKTAEELRLVLPS-PLYHCLgSVGGTMVSMMHG 326
Cdd:PTZ00216 260 P---ENNDDLALIMYTSGTTGDPKGVMHTHGSLTAGILALEDRLNDLIGPPEEDETYCSYlPLAHIM-EFGVTNIFLARG 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 327 ATLLLSSPsfngKKALEAISREKGTLLYGTPTMFVDIlnqPDFssydFTSIRGGVIAGSPAPPELIRAIINK-------- 398
Cdd:PTZ00216 336 ALIGFGSP----RTLTDTFARPHGDLTEFRPVFLIGV---PRI----FDTIKKAVEAKLPPVGSLKRRVFDHayqsrlra 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 399 ---------MNMK----------------------------ELV-VV-------YGTTENSPVTFMNFPEDTleqKAGSV 433
Cdd:PTZ00216 405 lkegkdtpyWNEKvfsapravlggrvramlsgggplsaatqEFVnVVfgmviqgWGLTETVCCGGIQRTGDL---EPNAV 481
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24418933 434 GRIMPHTEAQIVNVETGELTNLNVP-GELYIRGYCVMQGYWGEPQKTFETVGQDKWYRTGDIALMDEQGFCKIVGRSK 510
Cdd:PTZ00216 482 GQLLKGVEMKLLDTEEYKHTDTPEPrGEILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANGTLRIIGRVK 559
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
100-500 |
1.15e-15 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 80.48 E-value: 1.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 100 LNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVSVNPAYQ--SSELEyvlrkvgckgivf 177
Cdd:PRK12582 81 VTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAGVPAAPVSPAYSlmSHDHA------------- 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 178 pkqfKTQQYYDILKqvcPELEKAQPGAL--KSERLPDLT--TVISVDAPLPG--TLLLDDIVA---AGGKEQNLAQLRYN 248
Cdd:PRK12582 148 ----KLKHLFDLVK---PRVVFAQSGAPfaRALAALDLLdvTVVHVTGPGEGiaSIAFADLAAtppTAAVAAAIAAITPD 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 249 Q--RFLscydpiniqFTSGTTGNPKGATLSHHNI-VNNSMLIGQRLKMPTktaEELRLVLP-SPLYHCLGSVGGTMVSMM 324
Cdd:PRK12582 221 TvaKYL---------FTSGSTGMPKAVINTQRMMcANIAMQEQLRPREPD---PPPPVSLDwMPWNHTMGGNANFNGLLW 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 325 HGATLLLSspsfNGK----------KALEAISRekgTLLYGTP---TMFVDILNQPD------FSSYDFTSIRGGVIags 385
Cdd:PRK12582 289 GGGTLYID----DGKplpgmfeetiRNLREISP---TVYGNVPagyAMLAEAMEKDDalrrsfFKNLRLMAYGGATL--- 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 386 papPELIRAIINKMNMKE------LVVVYGTTENSPVTfMNFPEDTleQKAGSVGRIMPHTEAQIVNVETGEltnlnvpg 459
Cdd:PRK12582 359 ---SDDLYERMQALAVRTtghripFYTGYGATETAPTT-TGTHWDT--ERVGLIGLPLPGVELKLAPVGDKY-------- 424
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 24418933 460 ELYIRGYCVMQGYWGEPQKTFETVGQDKWYRTGDIA-LMDEQ 500
Cdd:PRK12582 425 EVRVKGPNVTPGYHKDPELTAAAFDEEGFYRLGDAArFVDPD 466
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
99-608 |
1.55e-15 |
|
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: 79.39 E-value: 1.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 99 RLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVSVNPAYQSSELEYVLRKVGCKGIVFP 178
Cdd:cd05939 3 HWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALIFN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 179 KQfktqqyYDILKQVCPELEKAQPGALKSeRLpdlttvisvdaplpgtlllddivaaggkeqnlaqlrynqrflsCYdpi 258
Cdd:cd05939 83 LL------DPLLTQSSTEPPSQDDVNFRD-KL-------------------------------------------FY--- 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 259 niQFTSGTTGNPKGATLSHHNIVNNSMLIGQRLKMptktAEELRLVLPSPLYHCLGSVGGTMVSMMHGATLLLSSpSFNG 338
Cdd:cd05939 110 --IYTSGTTGLPKAAVIVHSRYYRIAAGAYYAFGM----RPEDVVYDCLPLYHSAGGIMGVGQALLHGSTVVIRK-KFSA 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 339 KKALEAISREKGTLLYGTPTMFVDILNQPDFSSYDFTSIRggVIAGSPAPPELIRAIINKMNMKELVVVYGTTE-NSpvT 417
Cdd:cd05939 183 SNFWDDCVKYNCTIVQYIGEICRYLLAQPPSEEEQKHNVR--LAVGNGLRPQIWEQFVRRFGIPQIGEFYGATEgNS--S 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 418 FMNFpedtlEQKAGSVG---RIMPHT-EAQIVNV--ETGELT----------NLNVPGELY---IRGYCVMQ--GYWGEP 476
Cdd:cd05939 259 LVNI-----DNHVGACGfnsRILPSVyPIRLIKVdeDTGELIrdsdglcipcQPGEPGLLVgkiIQNDPLRRfdGYVNEG 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 477 ---QKTFETVGQ--DKWYRTGDIALMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQEAQVVGVKDERM-GE 550
Cdd:cd05939 334 atnKKIARDVFKkgDSAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVYGVEVPGVeGR 413
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 24418933 551 EICACIRLKSgETTTAEEIKAFCKGKISHFKIPRYIVFVEGYPLTISGKIQKFKLREQ 608
Cdd:cd05939 414 AGMAAIVDPE-RKVDLDRFSAVLAKSLPPYARPQFIRLLPEVDKTGTFKLQKTDLQKE 470
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
263-541 |
2.10e-15 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 78.65 E-value: 2.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 263 TSGTTGNPKGATLSHHNIVNNSMLIGQRLKMPTKTAEELRLVLPSplYHcLGSVGgtmvSMMH------GATLLLSSPSf 336
Cdd:COG1541 91 SSGTTGKPTVVGYTRKDLDRWAELFARSLRAAGVRPGDRVQNAFG--YG-LFTGG----LGLHygaerlGATVIPAGGG- 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 337 NGKKALEAISREKGTLLYGTPTMFVDILNQPDFSSYDF--TSIRGGVIAGSPAPPELIRAIINKMNMKeLVVVYGTTENS 414
Cdd:COG1541 163 NTERQLRLMQDFGPTVLVGTPSYLLYLAEVAEEEGIDPrdLSLKKGIFGGEPWSEEMRKEIEERWGIK-AYDIYGLTEVG 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 415 PVTF--------MNFPEDTLeqkagsvgrimpHTEaqIVNVETGE-----------LTNLNVpgELY--IRgycvmqgyw 473
Cdd:COG1541 242 PGVAyeceaqdgLHIWEDHF------------LVE--IIDPETGEpvpegeegelvVTTLTK--EAMplIR--------- 296
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24418933 474 gepqktfetvgqdkwYRTGDI-ALMDEQGFC--------KIVGRSKDMIIRGGENIYPAELEDFFLKHPQV-QEAQVV 541
Cdd:COG1541 297 ---------------YRTGDLtRLLPEPCPCgrthprigRILGRADDMLIIRGVNVFPSQIEEVLLRIPEVgPEYQIV 359
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
99-495 |
2.32e-15 |
|
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.
Pssm-ID: 341245 [Multi-domain] Cd Length: 561 Bit Score: 79.40 E-value: 2.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 99 RLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVSVNPAYQSSELEYVLRKvgckgivfp 178
Cdd:cd05921 25 RVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSPAYSLMSQDLAKLK--------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 179 kqfktqqyyDILKQVCPELEKAQPG-----ALKsERLPDLTTVISVDAPLPG--TLLLDDIVA--AGGKEQNL---AQLR 246
Cdd:cd05921 96 ---------HLFELLKPGLVFAQDAapfarALA-AIFPLGTPLVVSRNAVAGrgAISFAELAAtpPTAAVDAAfaaVGPD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 247 YNQRFLscydpiniqFTSGTTGNPKGATLSHHNIVNNSMLIGQRLKMPTKtaEELRLVLPSPLYHCLGSVGGTMVSMMHG 326
Cdd:cd05921 166 TVAKFL---------FTSGSTGLPKAVINTQRMLCANQAMLEQTYPFFGE--EPPVLVDWLPWNHTFGGNHNFNLVLYNG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 327 ATLLLSSpsfnGKKALEAIS------REKGTLLYGT-P---TMFVDIL-NQPDFSSYDFTSIRGGVIAGSPAPPELIRAI 395
Cdd:cd05921 235 GTLYIDD----GKPMPGGFEetlrnlREISPTVYFNvPagwEMLVAALeKDEALRRRFFKRLKLMFYAGAGLSQDVWDRL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 396 iNKMNMKE------LVVVYGTTENSPV-TFMNFPEDtleqKAGSVGRIMPHTEAQIVNVEtGELtnlnvpgELYIRGYCV 468
Cdd:cd05921 311 -QALAVATvgeripMMAGLGATETAPTaTFTHWPTE----RSGLIGLPAPGTELKLVPSG-GKY-------EVRVKGPNV 377
|
410 420
....*....|....*....|....*..
gi 24418933 469 MQGYWGEPQKTFETVGQDKWYRTGDIA 495
Cdd:cd05921 378 TPGYWRQPELTAQAFDEEGFYCLGDAA 404
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
262-602 |
6.30e-15 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 79.06 E-value: 6.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 262 FTSGTTGNPKGATLSHHNIVNNsmligQRLKMPTKTAEElRLVLPSPLYHCLGsvggtmVSMMHgatlLLSSPSFNGK-- 339
Cdd:PRK05691 3876 YTSGSTGLPKGVMVEQRGMLNN-----QLSKVPYLALSE-ADVIAQTASQSFD------ISVWQ----FLAAPLFGARve 3939
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 340 ----------KALEAISREKG-TLLYGTPTMFVDILNQPDFSsydFTSIRGGVIAGSPAPPELIRAIINKMNMKELVVVY 408
Cdd:PRK05691 3940 ivpnaiahdpQGLLAHVQAQGiTVLESVPSLIQGMLAEDRQA---LDGLRWMLPTGEAMPPELARQWLQRYPQIGLVNAY 4016
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 409 GTTENSP-VTFmnFPEDtLEQKAGSVGRIMPHTEAQIVNV--ETGELTNLNVPGELYIRGYCVMQGYWGEPQKT------ 479
Cdd:PRK05691 4017 GPAECSDdVAF--FRVD-LASTRGSYLPIGSPTDNNRLYLldEALELVPLGAVGELCVAGTGVGRGYVGDPLRTalafvp 4093
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 480 --FETVGQdKWYRTGDIALMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQEAqVVGVKDERMGEEICACIR 557
Cdd:PRK05691 4094 hpFGAPGE-RLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREA-AVAVQEGVNGKHLVGYLV 4171
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 24418933 558 LKSGETTTA---EEIKAFCKGKISHFKIPRYIVFVEGYPLTISGKIQK 602
Cdd:PRK05691 4172 PHQTVLAQGallERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDR 4219
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
102-542 |
4.86e-14 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 75.44 E-value: 4.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 102 FAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVSVNPAYQSSELEYVLRKVGCKgIVFPKQF 181
Cdd:PLN02614 82 YQEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVS-IVFVEEK 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 182 KTqqyydilkqvcPELEKAQPGALKSerlpdLTTVISV---------DAPLPGTLL--LDDIVAAGGKEQnlaqlrYNQR 250
Cdd:PLN02614 161 KI-----------SELFKTCPNSTEY-----MKTVVSFggvsreqkeEAETFGLVIyaWDEFLKLGEGKQ------YDLP 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 251 FLSCYDPINIQFTSGTTGNPKGATLSHHNIVNNSMLIGQRLKMPTKTAEELRLVLPS-PLYH--------CLGSVGGTMV 321
Cdd:PLN02614 219 IKKKSDICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRLLKSANAALTVKDVYLSYlPLAHifdrvieeCFIQHGAAIG 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 322 SMMHGATLL-----------------------------LSSPSFNGKKALE-AISREKGTLLYGTPtmfvDILNQPDFSS 371
Cdd:PLN02614 299 FWRGDVKLLiedlgelkptifcavprvldrvysglqkkLSDGGFLKKFVFDsAFSYKFGNMKKGQS----HVEASPLCDK 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 372 YDFTSIRGG-------VIAGSPAPPELIRAIINKMNMKELVVVYGTTENSPVTFMNFPEDTleQKAGSVGRIMPHTEAQI 444
Cdd:PLN02614 375 LVFNKVKQGlggnvriILSGAAPLASHVESFLRVVACCHVLQGYGLTESCAGTFVSLPDEL--DMLGTVGPPVPNVDIRL 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 445 VNVETGELTNL--NVPGELYIRGYCVMQGYWGEPQKTFEtVGQDKWYRTGDIALMDEQGFCKIVGRSKDMI-IRGGENIY 521
Cdd:PLN02614 453 ESVPEMEYDALasTPRGEICIRGKTLFSGYYKREDLTKE-VLIDGWLHTGDVGEWQPNGSMKIIDRKKNIFkLSQGEYVA 531
|
490 500
....*....|....*....|.
gi 24418933 522 PAELEDFFLKHPQVQEAQVVG 542
Cdd:PLN02614 532 VENIENIYGEVQAVDSVWVYG 552
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
100-542 |
1.73e-13 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 73.34 E-value: 1.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 100 LNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVSVNPAYQSSELEYVLRKVGCKgIVFPK 179
Cdd:PLN02861 78 LTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVS-IAFVQ 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 180 QFKTQQYYDILKQVCPELEkaqpgALKSerLPDLTTVISVDAPLPGTLLL--DDIVAAGGKEQNLAQLRYNqrflscyDP 257
Cdd:PLN02861 157 ESKISSILSCLPKCSSNLK-----TIVS--FGDVSSEQKEEAEELGVSCFswEEFSLMGSLDCELPPKQKT-------DI 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 258 INIQFTSGTTGNPKGATLSHHNIVNNSMLIGQRLKMPTKTA-EELRLVLPSPLYHCLGSVGGTMVsMMHGATLLLSSPSF 336
Cdd:PLN02861 223 CTIMYTSGTTGEPKGVILTNRAIIAEVLSTDHLLKVTDRVAtEEDSYFSYLPLAHVYDQVIETYC-ISKGASIGFWQGDI 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 337 ngKKALEAISREKGTLLYGTPTMFVDI---LNQP------------DFS-SYDFTSIRGGvIAGSPAPPELIRAIINKM- 399
Cdd:PLN02861 302 --RYLMEDVQALKPTIFCGVPRVYDRIytgIMQKissggmlrkklfDFAyNYKLGNLRKG-LKQEEASPRLDRLVFDKIk 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 400 -------------------NMKELVVV---------YGTTENSPVTFMN----FPedtleqKAGSVGRIMPHTEAQIVNV 447
Cdd:PLN02861 379 eglggrvrlllsgaaplprHVEEFLRVtscsvlsqgYGLTESCGGCFTSianvFS------MVGTVGVPMTTIEARLESV 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 448 -ETGELTNLNVP-GELYIRGYCVMQGYWGEPQKTfETVGQDKWYRTGDIALMDEQGFCKIVGRSKDMI-IRGGENIYPAE 524
Cdd:PLN02861 453 pEMGYDALSDVPrGEICLRGNTLFSGYHKRQDLT-EEVLIDGWFHTGDIGEWQPNGAMKIIDRKKNIFkLSQGEYVAVEN 531
|
490
....*....|....*...
gi 24418933 525 LEDFFLKHPQVQEAQVVG 542
Cdd:PLN02861 532 LENTYSRCPLIASIWVYG 549
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
261-600 |
4.21e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 72.28 E-value: 4.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 261 QFTSGTTGNPKGATLSHHNIVNN-----SMLIGQRLKMPTktaEELRLVLPSPLYHCLGSVGGTMVSMMHGATLLLSSP- 334
Cdd:PRK05850 166 QYTSGSTRTPAGVMVSHRNVIANfeqlmSDYFGDTGGVPP---PDTTVVSWLPFYHDMGLVLGVCAPILGGCPAVLTSPv 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 335 SFNGKKA--LEAISREKGTLLYGTPTMF---VDILNQPDFSSYDFTSIRGgVIAGS----PA--------------PPEL 391
Cdd:PRK05850 243 AFLQRPArwMQLLASNPHAFSAAPNFAFelaVRKTSDDDMAGLDLGGVLG-IISGServhPAtlkrfadrfapfnlRETA 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 392 IRAiinKMNMKELVVVYGTTE-NSPVTFMNFPEDTL--------EQKAGS--VGRIMPHTEA-QIVNVETGELTNLNVPG 459
Cdd:PRK05850 322 IRP---SYGLAEATVYVATREpGQPPESVRFDYEKLsaghakrcETGGGTplVSYGSPRSPTvRIVDPDTCIECPAGTVG 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 460 ELYIRGYCVMQGYWGEPQKTFETVG-----------QDKWYRTGDIALMDEQGFCkIVGRSKDMIIRGGENIYPAELEdf 528
Cdd:PRK05850 399 EIWVHGDNVAAGYWQKPEETERTFGatlvdpspgtpEGPWLRTGDLGFISEGELF-IVGRIKDLLIVDGRNHYPDDIE-- 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 529 flkhPQVQE-----AQVVGVKDERmGEEICACIRLKSGETTTAEEIKAFC--KGKI------SHFKIPRYIVFVE--GYP 593
Cdd:PRK05850 476 ----ATIQEitggrVAAISVPDDG-TEKLVAIIELKKRGDSDEEAMDRLRtvKREVtsaiskSHGLSVADLVLVApgSIP 550
|
....*..
gi 24418933 594 LTISGKI 600
Cdd:PRK05850 551 ITTSGKI 557
|
|
| PaaK |
cd05913 |
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic ... |
337-581 |
2.07e-11 |
|
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: 66.11 E-value: 2.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 337 NGKKALEAISREKGTLLYGTPTMFVDILNQPDFSSYDF--TSIRGGVIAGSPAPPELIRAIINKMNMKELVVvYGTTEns 414
Cdd:cd05913 158 NTERQLQLIKDFGPTVLCCTPSYALYLAEEAEEEGIDPreLSLKVGIFGAEPWTEEMRKRIERRLGIKAYDI-YGLTE-- 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 415 pVTFMNFPEDTLEQKAGSVGR-------IMPHTEAQIVNVETGEL--TNLNVPGELYIRgycvmqgywgepqktfetvgq 485
Cdd:cd05913 235 -IIGPGVAFECEEKDGLHIWEdhfipeiIDPETGEPVPPGEVGELvfTTLTKEAMPLIR--------------------- 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 486 dkwYRTGDIA-LMDEQGFC--------KIVGRSKDMIIRGGENIYPAELEDFFLKHPQV-QEAQVVGVKDERMGEeicac 555
Cdd:cd05913 293 ---YRTRDITrLLPGPCPCgrthrridRITGRSDDMLIIRGVNVFPSQIEDVLLKIPGLgPHYQLILTRQEHLDE----- 364
|
250 260
....*....|....*....|....*....
gi 24418933 556 IRLK---SGETTTAEEIKAFCKGKISHFK 581
Cdd:cd05913 365 LTIKvevRPEADDDEKLEALKQRLERHIK 393
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
260-526 |
1.50e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 63.98 E-value: 1.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 260 IQFTSGTTGNPKGATLSHHNIVNN--SMLIGQRLKMPTKTAEELrlvlpsPLYHCLGSVGgTMVSMMHGATLLLSSPSFN 337
Cdd:PRK07769 185 LQYTSGSTRIPAGVQITHLNLPTNvlQVIDALEGQEGDRGVSWL------PFFHDMGLIT-VLLPALLGHYITFMSPAAF 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 338 GKKALEAIsREKGTLLYGTPTMFVdilNQPDFSsYDFTSIRG---------------GVIAGS-PAPPELIR-------- 393
Cdd:PRK07769 258 VRRPGRWI-RELARKPGGTGGTFS---AAPNFA-FEHAAARGlpkdgeppldlsnvkGLLNGSePVSPASMRkfneafap 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 394 ------AIINKMNMKELVVVYGTT--ENSPV------------TFMNFPEDTLEQKAG-SVGRIMPHTEAQIVNVETG-E 451
Cdd:PRK07769 333 yglpptAIKPSYGMAEATLFVSTTpmDEEPTviyvdrdelnagRFVEVPADAPNAVAQvSAGKVGVSEWAVIVDPETAsE 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 452 LTNLNVpGELYIRGYCVMQGYWGEPQKTFET----------------VGQD-KWYRTGDIALMDEqGFCKIVGRSKDMII 514
Cdd:PRK07769 413 LPDGQI-GEIWLHGNNIGTGYWGKPEETAATfqnilksrlseshaegAPDDaLWVRTGDYGVYFD-GELYITGRVKDLVI 490
|
330
....*....|..
gi 24418933 515 RGGENIYPAELE 526
Cdd:PRK07769 491 IDGRNHYPQDLE 502
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
260-520 |
1.86e-10 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 63.97 E-value: 1.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 260 IQFTSGTTGNPKGATLSHHNIVN-------NSMligqRLKMPTKTaeELRLVlpsPLYHCLGSVGgTMVSMMHGATLLLS 332
Cdd:PTZ00342 309 IVYTSGTSGKPKGVMLSNKNLYNtvvplckHSI----FKKYNPKT--HLSYL---PISHIYERVI-AYLSFMLGGTINIW 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 333 SPSFNGKKalEAISREKGTLLYGTPTMF--------VDILNQPDF-------------SSYDFTS-------------IR 378
Cdd:PTZ00342 379 SKDINYFS--KDIYNSKGNILAGVPKVFnriytnimTEINNLPPLkrflvkkilslrkSNNNGGFskflegithisskIK 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 379 GGV--------IAGSPAPPELIRAIINKMNMKeLVVVYGTTENSPVTFMNFPEDTLEQKAGsvGRIMPHTEAQIVNVETG 450
Cdd:PTZ00342 457 DKVnpnlevilNGGGKLSPKIAEELSVLLNVN-YYQGYGLTETTGPIFVQHADDNNTESIG--GPISPNTKYKVRTWETY 533
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24418933 451 ELTNLNVPGELYIRGYCVMQGYWGEPQKTFETVGQDKWYRTGDIALMDEQGFCKIVGRSKDMI-IRGGENI 520
Cdd:PTZ00342 534 KATDTLPKGELLIKSDSIFSGYFLEKEQTKNAFTEDGYFKTGDIVQINKNGSLTFLDRSKGLVkLSQGEYI 604
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
56-526 |
1.63e-09 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 60.91 E-value: 1.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 56 GGLSYIQGHTDSHLVNTTVGECLDATAQRFPDREALVILHEnIRLNFAQLKEEVDKAASGLLSIGlRKGDRLGMWGPNSY 135
Cdd:PRK12476 26 GNIALPPGTTLISLIERNIANVGDTVAYRYLDHSHSAAGCA-VELTWTQLGVRLRAVGARLQQVA-GPGDRVAILAPQGI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 136 AWVLIQLATAQAGIILVsvnPAYqSSELeyvlrkvgckgivfpkqfktQQYYDILKQVcpeLEKAQPGALkserlpdLTT 215
Cdd:PRK12476 104 DYVAGFFAAIKAGTIAV---PLF-APEL--------------------PGHAERLDTA---LRDAEPTVV-------LTT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 216 VISVDA------PLPGT-----LLLDDIVAAGGKEQNLAQLRYNqrflscyDPINIQFTSGTTGNPKGATLSHHNIVNN- 283
Cdd:PRK12476 150 TAAAEAvegflrNLPRLrrprvIAIDAIPDSAGESFVPVELDTD-------DVSHLQYTSGSTRPPVGVEITHRAVGTNl 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 284 -SMLI-GQRLKMPTKTAEELrlvlpsPLYHCLGsVGGTMVSMMHGATLLLSSP-SFNGK-----KALEAISREKGTllyg 355
Cdd:PRK12476 223 vQMILsIDLLDRNTHGVSWL------PLYHDMG-LSMIGFPAVYGGHSTLMSPtAFVRRpqrwiKALSEGSRTGRV---- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 356 tptmfvdILNQPDFSsYDFTSIRG-------------GVIAGS-PAPPELIR--------------AIINKMNMKELVVV 407
Cdd:PRK12476 292 -------VTAAPNFA-YEWAAQRGlpaegddidlsnvVLIIGSePVSIDAVTtfnkafapyglprtAFKPSYGIAEATLF 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 408 YGTT----ENSPVTFmnfpeDTLEQKAG----------------SVGRIMPHTEAQIVNVETG-ELTNLNVpGELYIRGY 466
Cdd:PRK12476 364 VATIapdaEPSVVYL-----DREQLGAGravrvaadapnavahvSCGQVARSQWAVIVDPDTGaELPDGEV-GEIWLHGD 437
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24418933 467 CVMQGYWGEPQKTFETVG------------------QDKWYRTGDIAL-MDeqGFCKIVGRSKDMIIRGGENIYPAELE 526
Cdd:PRK12476 438 NIGRGYWGRPEETERTFGaklqsrlaegshadgaadDGTWLRTGDLGVyLD--GELYITGRIADLIVIDGRNHYPQDIE 514
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
100-520 |
6.00e-09 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 58.97 E-value: 6.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 100 LNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVSVNPAYQSSELEYVLRKVGCKGIVF-P 178
Cdd:PLN02387 107 ITYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVICdS 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 179 KQFKTqqYYDIlkqvcpelekaqpgalkSERLPDLTTVI-----SVDAPLPGTLLLDDIVAAGGKEQNLAQLRYNQ-RFL 252
Cdd:PLN02387 187 KQLKK--LIDI-----------------SSQLETVKRVIymddeGVDSDSSLSGSSNWTVSSFSEVEKLGKENPVDpDLP 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 253 SCYDPINIQFTSGTTGNPKGATLSHHNIVnnsmligqrlkmptKTAEELRLVLPS-----------PLYHCL-----GSV 316
Cdd:PLN02387 248 SPNDIAVIMYTSGSTGLPKGVMMTHGNIV--------------ATVAGVMTVVPKlgkndvylaylPLAHILelaaeSVM 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 317 GGTMVSMMHGATLLLSSPSFNGKK---------------ALEAI-----------SREKGTLL----------------- 353
Cdd:PLN02387 314 AAVGAAIGYGSPLTLTDTSNKIKKgtkgdasalkptlmtAVPAIldrvrdgvrkkVDAKGGLAkklfdiaykrrlaaieg 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 354 -----YGTPTMFVDILNQPDFSSYDFTSIRGGVIAGSPAPPELIRaIINKMNMKELVVVYGTTEN-SPVTFMNFpEDTle 427
Cdd:PLN02387 394 swfgaWGLEKLLWDALVFKKIRAVLGGRIRFMLSGGAPLSGDTQR-FINICLGAPIGQGYGLTETcAGATFSEW-DDT-- 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 428 qkagSVGRI---MPHTEAQIVNVETGELTNLNVP---GELYIRGYCVMQGYWGEPQKTFETVGQD----KWYRTGDIALM 497
Cdd:PLN02387 470 ----SVGRVgppLPCCYVKLVSWEEGGYLISDKPmprGEIVIGGPSVTLGYFKNQEKTDEVYKVDergmRWFYTGDIGQF 545
|
490 500
....*....|....*....|....
gi 24418933 498 DEQGFCKIVGRSKDMI-IRGGENI 520
Cdd:PLN02387 546 HPDGCLEIIDRKKDIVkLQHGEYV 569
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
260-605 |
3.30e-08 |
|
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: 56.37 E-value: 3.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 260 IQFTSGTTGNPKGATLSHHNIVNNSMLIGQRLKMptktAEELRLVLPSPLYHclGSVGGTMVSMMH-GATLLLSSPS--- 335
Cdd:cd17647 114 LSFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFNL----SENDKFTMLSGIAH--DPIQRDMFTPLFlGAQLLVPTQDdig 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 336 FNGKKAlEAISREKGTLLYGTPTMFVDILNQpdfssydftsirggviAGSPAPPeLIRA-----IINKMNMKEL------ 404
Cdd:cd17647 188 TPGRLA-EWMAKYGATVTHLTPAMGQLLTAQ----------------ATTPFPK-LHHAffvgdILTKRDCLRLqtlaen 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 405 ---VVVYGTTENS-PVTFMNFP----EDTLEQKAGSV---GRIMPHTEAQIVN-VETGELTNLNVPGELYIRGYCVMQGY 472
Cdd:cd17647 250 vriVNMYGTTETQrAVSYFEVPsrssDPTFLKNLKDVmpaGRGMLNVQLLVVNrNDRTQICGIGEVGEIYVRAGGLAEGY 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 473 WG----------------------------EPQKTFETVGQDKWYRTGDIALMDEQGFCKIVGRSKDMI-IRGGEnIYPA 523
Cdd:cd17647 330 RGlpelnkekfvnnwfvepdhwnyldkdnnEPWRQFWLGPRDRLYRTGDLGRYLPNGDCECCGRADDQVkIRGFR-IELG 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 524 ELEDFFLKHPQVQE-----------------------------AQVVGVKDERMGEEICACIRLKSGETTtaEEIKAFCK 574
Cdd:cd17647 409 EIDTHISQHPLVREnitlvrrdkdeeptlvsyivprfdkpddeSFAQEDVPKEVSTDPIVKGLIGYRKLI--KDIREFLK 486
|
410 420 430
....*....|....*....|....*....|.
gi 24418933 575 GKISHFKIPRYIVFVEGYPLTISGKIQKFKL 605
Cdd:cd17647 487 KRLASYAIPSLIVVLDKLPLNPNGKVDKPKL 517
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
99-278 |
2.24e-07 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 53.93 E-value: 2.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 99 RLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVSVNPAYQSSELEYVLRKVGCKGIVfp 178
Cdd:PLN03052 208 RMTLSELRSQVSRVANALDALGFEKGDAIAIDMPMNVHAVIIYLAIILAGCVVVSIADSFAPSEIATRLKISKAKAIF-- 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 179 kqfkTQQYydILKQvcpelEKAQPgaLKS---ERLPDLTTVISVDAPLPGTLLLDDIVAAGGKEQNLAQLRYNQRFLSCY 255
Cdd:PLN03052 286 ----TQDV--IVRG-----GKSIP--LYSrvvEAKAPKAIVLPADGKSVRVKLREGDMSWDDFLARANGLRRPDEYKAVE 352
|
170 180
....*....|....*....|....*..
gi 24418933 256 DPI----NIQFTSGTTGNPKGATLSHH 278
Cdd:PLN03052 353 QPVeaftNILFSSGTTGEPKAIPWTQL 379
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
138-613 |
2.34e-04 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 44.04 E-value: 2.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 138 VLIQLATAQAGIILVSVNPAYQSSELEYVLRKVGCKGIVfpkqfkTQQYydILK--QVCPELEK-AQPGALKSERLPDLT 214
Cdd:PLN03051 8 VIIYLAIVLAGCVVVSVADSFSAKEIATRLDISGAKGVF------TQDV--VLRggRALPLYSKvVEAAPAKAIVLPAAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 215 TVISVdaPL-PGTLLLDDIVAAGGKEQNLAQLRYNQRFLSCYDPINIQFTSGTTGNPKGATLSHHNIVNNS--------M 285
Cdd:PLN03051 80 EPVAV--PLrEQDLSWCDFLGVAAAQGSVGGNEYSPVYAPVESVTNILFSSGTTGEPKAIPWTHLSPLRCAsdgwahmdI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 286 LIGQRLKMPTKtaeeLRLVL-PSPLYHCLgsvggtmvsmMHGATLLLSSPSFNGKKALEAISREKGTLLYGTPTMfVDIL 364
Cdd:PLN03051 158 QPGDVVCWPTN----LGWMMgPWLLYSAF----------LNGATLALYGGAPLGRGFGKFVQDAGVTVLGLVPSI-VKAW 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 365 ---NQPDFSSYDFTSIRGGVIAG-SPAPPELIRAIINKMNMKELVVVYGTTE-------------NSPVTFM-------- 419
Cdd:PLN03051 223 rhtGAFAMEGLDWSKLRVFASTGeASAVDDVLWLSSVRGYYKPVIEYCGGTElasgyisstllqpQAPGAFStaslgtrf 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 420 -----NFPEDTLEQKA-GSVGRIMPHTEAqivnveTGELTNLNvPGELYIRGYcVMQGYWGEPQKtfetvgqdkwyRTGD 493
Cdd:PLN03051 303 vllndNGVPYPDDQPCvGEVALAPPMLGA------SDRLLNAD-HDKVYYKGM-PMYGSKGMPLR-----------RHGD 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 494 IALMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQ-VQEAQVVGVKDERMGEEICAcIRLKSGETTTA------ 566
Cdd:PLN03051 364 IMKRTPGGYFCVQGRADDTMNLGGIKTSSVEIERACDRAVAgIAETAAVGVAPPDGGPELLV-IFLVLGEEKKGfdqarp 442
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 24418933 567 EEIKAFCKGKISH-----FKIPRyIVFVEGYPLTISGKIQKFKLREQMEQHL 613
Cdd:PLN03051 443 EALQKKFQEAIQTnlnplFKVSR-VKIVPELPRNASNKLLRRVLRDQLKKEL 493
|
|
| PRK07868 |
PRK07868 |
acyl-CoA synthetase; Validated |
33-128 |
7.49e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236121 [Multi-domain] Cd Length: 994 Bit Score: 42.78 E-value: 7.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418933 33 NSKLQSVRALSsgmVNCTNPLP-IGGLSYIQGHTDSHLvnttvGECLDATAQRFPDREALviLHENIRLNFAQLKEEVDK 111
Cdd:PRK07868 415 VAANRSVRTLA---VETARTLPrLARLGQINDHTRISL-----GRIIAEQARDAPKGEFL--LFDGRVHTYEAVNRRINN 484
|
90
....*....|....*..
gi 24418933 112 AASGLLSIGLRKGDRLG 128
Cdd:PRK07868 485 VVRGLIAVGVRQGDRVG 501
|
|
| |
