|
Name |
Accession |
Description |
Interval |
E-value |
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
14-516 |
0e+00 |
|
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: 805.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 14 FNFAQ-HLIACNAQRPGKTAYIDDHGTMRYGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPV 92
Cdd:cd05959 3 YNAATlVDLNLNEGRGDKTAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 93 AVNTLLTADDYAYMLQHSRAQAVLVSGALLPVLRQAMAQGGHEAATVIVSRPAGPLPdGMIALEAWIERNAPLAAPASTG 172
Cdd:cd05959 83 PVNTLLTPDDYAYYLEDSRARVVVVSGELAPVLAAALTKSEHTLVVLIVSGGAGPEA-GALLLAELVAAEAEQLKPAATH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 173 PDDPGFWLYSSGSTGRPKGVLHSQGNPYWTAELYAKPVLSLGEADICFSAAKLYFAYGLGNALTFPLSVGATVVLMAERP 252
Cdd:cd05959 162 ADDPAFWLYSSGSTGRPKGVVHLHADIYWTAELYARNVLGIREDDVCFSAAKLFFAYGLGNSLTFPLSVGATTVLMPERP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 253 TPEATFRRWLDYQPTVFFGAPTGYAGMLAAPGLPTREQVSLRLCSSAGEALPADLGERFTAHFGCEIIDGIGSTEMLHIF 332
Cdd:cd05959 242 TPAAVFKRIRRYRPTVFFGVPTLYAAMLAAPNLPSRDLSSLRLCVSAGEALPAEVGERWKARFGLDILDGIGSTEMLHIF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 333 LSNRPGQVRYGTTGWPVPGYAVELRDEDGHAVPDGDVGDLYIQGPSAALMYWGNREKSRETFRGGWTKSGDKYVRNADGS 412
Cdd:cd05959 322 LSNRPGRVRYGTTGKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQGEWTRTGDKYVRDDDGF 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 413 YSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQAGLTKTKAFVVLKPGAQ---VSETELKAFVKERLAP 489
Cdd:cd05959 402 YTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPGYEdseALEEELKEFVKDRLAP 481
|
490 500
....*....|....*....|....*..
gi 1920939256 490 YKYPRIIEFMDALPKTATGKIQRFRLR 516
Cdd:cd05959 482 YKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
14-518 |
0e+00 |
|
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ligase, 4-hydroxybenzoate-CoA ligase, 2-aminobenzoate-CoA ligase, etc. Members are related to fatty acid and acetate CoA ligases.
Pssm-ID: 274059 [Multi-domain] Cd Length: 505 Bit Score: 771.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 14 FNFAQHLIACNAQRP--GKTAYIDDHGTMRYGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVP 91
Cdd:TIGR02262 3 YNAAEDLLDRNVVEGrgGKTAFIDDISSLSYGELEAQVRRLAAALRRLGVKREERVLLLMLDGVDFPIAFLGAIRAGIVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 92 VAVNTLLTADDYAYMLQHSRAQAVLVSGALLPVLRQAMAQGGHEAATVIVSRPagplPDGMIALEAWIERNAPLAAPAST 171
Cdd:TIGR02262 83 VALNTLLTADDYAYMLEDSRARVVFVSGALLPVIKAALGKSPHLEHRVVVGRP----EAGEVQLAELLATESEQFKPAAT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 172 GPDDPGFWLYSSGSTGRPKGVLHSQGNPYWTAELYAKPVLSLGEADICFSAAKLYFAYGLGNALTFPLSVGATVVLMAER 251
Cdd:TIGR02262 159 QADDPAFWLYSSGSTGMPKGVVHTHSNPYWTAELYARNTLGIREDDVCFSAAKLFFAYGLGNALTFPMSVGATTVLMGER 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 252 PTPEATFRRWLDYQPTVFFGAPTGYAGMLAAPGLPTREQVSLRLCSSAGEALPADLGERFTAHFGCEIIDGIGSTEMLHI 331
Cdd:TIGR02262 239 PTPDAVFDRLRRHQPTIFYGVPTLYAAMLADPNLPSEDQVRLRLCTSAGEALPAEVGQRWQARFGVDIVDGIGSTEMLHI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 332 FLSNRPGQVRYGTTGWPVPGYAVELRDEDGHAVPDGDVGDLYIQGPSAALMYWGNREKSRETFRGGWTKSGDKYVRNADG 411
Cdd:TIGR02262 319 FLSNLPGDVRYGTSGKPVPGYRLRLVGDGGQDVADGEPGELLISGPSSATMYWNNRAKSRDTFQGEWTRSGDKYVRNDDG 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 412 SYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQAGLTKTKAFVVLKPGAQVSETELKAFVKERLAPYK 491
Cdd:TIGR02262 399 SYTYAGRTDDMLKVSGIYVSPFEIESALIQHPAVLEAAVVGVADEDGLIKPKAFVVLRPGQTALETELKEHVKDRLAPYK 478
|
490 500
....*....|....*....|....*..
gi 1920939256 492 YPRIIEFMDALPKTATGKIQRFRLREM 518
Cdd:TIGR02262 479 YPRWIVFVDDLPKTATGKIQRFKLREG 505
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
30-516 |
0e+00 |
|
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: 574.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 30 KTAYIDDHGTMRYGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLLTADDYAYMLQH 109
Cdd:cd05919 1 KTAFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 110 SRAQAVLVSGallpvlrqamaqggheaatvivsrpagplpdgmialeawiernaplaapastgpDDPGFWLYSSGSTGRP 189
Cdd:cd05919 81 CEARLVVTSA------------------------------------------------------DDIAYLLYSSGTTGPP 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 190 KGVLHSQGNPYWTAELYAKPVLSLGEADICFSAAKLYFAYGLGNALTFPLSVGATVVLMAERPTPEATFRRWLDYQPTVF 269
Cdd:cd05919 107 KGVMHAHRDPLLFADAMAREALGLTPGDRVFSSAKMFFGYGLGNSLWFPLAVGASAVLNPGWPTAERVLATLARFRPTVL 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 270 FGAPTGYAGMLAAPGLPTREQVSLRLCSSAGEALPADLGERFTAHFGCEIIDGIGSTEMLHIFLSNRPGQVRYGTTGWPV 349
Cdd:cd05919 187 YGVPTFYANLLDSCAGSPDALRSLRLCVSAGEALPRGLGERWMEHFGGPILDGIGATEVGHIFLSNRPGAWRLGSTGRPV 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 350 PGYAVELRDEDGHAVPDGDVGDLYIQGPSAALMYWGNREKSRETFRGGWTKSGDKYVRNADGSYSYAGRSDDMLKVSGIY 429
Cdd:cd05919 267 PGYEIRLVDEEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQW 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 430 VSPFEVEATLAQHPAILEAAVIGVPDQAGLTKTKAFVVLKPGAQVSET---ELKAFVKERLAPYKYPRIIEFMDALPKTA 506
Cdd:cd05919 347 VSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPQESlarDIHRHLLERLSAHKVPRRIAFVDELPRTA 426
|
490
....*....|
gi 1920939256 507 TGKIQRFRLR 516
Cdd:cd05919 427 TGKLQRFKLR 436
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
9-519 |
0e+00 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 549.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 9 PPGTpFNFAQHLIACNAQ-RPGKTAYI--DDHGTMR---YGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFL 82
Cdd:COG0365 4 VGGR-LNIAYNCLDRHAEgRGDKVALIweGEDGEERtltYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAML 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 83 GAMYAGIVPVAVNTLLTADDYAYMLQHSRAQAVLVSGA---------LLPVLRQAMAQGGHEAATVIVSRPAGPLP-DGM 152
Cdd:COG0365 83 ACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADGglrggkvidLKEKVDEALEELPSLEHVIVVGRTGADVPmEGD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 153 IALEAWIERNAPLAAPASTGPDDPGFWLYSSGSTGRPKGVLHSQGNPYWTAELYAKPVLSLGEADICFSAAKLYFAYGLG 232
Cdd:COG0365 163 LDWDELLAAASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYVLDLKPGDVFWCTADIGWATGHS 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 233 NALTFPLSVGATVVLMAERPT-PEAtfRRWLD----YQPTVFFGAPTGYAGMLAAPGLPTRE--QVSLRLCSSAGEALPA 305
Cdd:COG0365 243 YIVYGPLLNGATVVLYEGRPDfPDP--GRLWEliekYGVTVFFTAPTAIRALMKAGDEPLKKydLSSLRLLGSAGEPLNP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 306 DLGERFTAHFGCEIIDGIGSTEMLHIFLSNRPGQ-VRYGTTGWPVPGYAVELRDEDGHAVPDGDVGDLYIQG--PSAALM 382
Cdd:COG0365 321 EVWEWWYEAVGVPIVDGWGQTETGGIFISNLPGLpVKPGSMGKPVPGYDVAVVDEDGNPVPPGEEGELVIKGpwPGMFRG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 383 YWGNREKSRETFRG---GWTKSGDKYVRNADGSYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQAGL 459
Cdd:COG0365 401 YWNDPERYRETYFGrfpGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVGVPDEIRG 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1920939256 460 TKTKAFVVLKPGAQVSET---ELKAFVKERLAPYKYPRIIEFMDALPKTATGKIQRFRLREME 519
Cdd:COG0365 481 QVVKAFVVLKPGVEPSDElakELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLRKIA 543
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
30-516 |
4.93e-150 |
|
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: 436.52 E-value: 4.93e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 30 KTAYIDDHGTMRYGELAERIRRVAGALQASGIHRE-ERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLLTADDYAYMLQ 108
Cdd:cd05958 1 RTCLRSPEREWTYRDLLALANRIANVLVGELGIVPgNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 109 HSRAQAVLVSGALlpvlrqamaqggheaatvivsrpagplpdgmialeawiernaplaapasTGPDDPGFWLYSSGSTGR 188
Cdd:cd05958 81 KARITVALCAHAL-------------------------------------------------TASDDICILAFTSGTTGA 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 189 PKGVLHSQGNPYWTAELYAKPVLSLGEADICFSAAKLYFAYGLGNALTFPLSVGATVVLMaERPTPEATFRRWLDYQPTV 268
Cdd:cd05958 112 PKATMHFHRDPLASADRYAVNVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLL-EEATPDLLLSAIARYKPTV 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 269 FFGAPTGYAGMLAAPGLPTREQVSLRLCSSAGEALPADLGERFTAHFGCEIIDGIGSTEMLHIFLSNRPGQVRYGTTGWP 348
Cdd:cd05958 191 LFTAPTAYRAMLAHPDAAGPDLSSLRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEMFHIFISARPGDARPGATGKP 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 349 VPGYAVELRDEDGHAVPDGDVGDLYIQGPSAalmYWGNREKSRET-FRGGWTKSGDKYVRNADGSYSYAGRSDDMLKVSG 427
Cdd:cd05958 271 VPGYEAKVVDDEGNPVPDGTIGRLAVRGPTG---CRYLADKRQRTyVQGGWNITGDTYSRDPDGYFRHQGRSDDMIVSGG 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 428 IYVSPFEVEATLAQHPAILEAAVIGVPDQAGLTKTKAFVVLKPGAQVSET---ELKAFVKERLAPYKYPRIIEFMDALPK 504
Cdd:cd05958 348 YNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIPGPVlarELQDHAKAHIAPYKYPRAIEFVTELPR 427
|
490
....*....|..
gi 1920939256 505 TATGKIQRFRLR 516
Cdd:cd05958 428 TATGKLQRFALR 439
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
16-523 |
5.67e-146 |
|
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: 426.53 E-value: 5.67e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 16 FAQHLIACNAQRPGKTAYIDDHGTMRYGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVN 95
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 96 TLLTADDYAYMLQHSRAQAVLVsgallpvlrqamaqggheaatvivsrpagplpdgmialeAWIernaplaapastgpdd 175
Cdd:COG0318 81 PRLTAEELAYILEDSGARALVT---------------------------------------ALI---------------- 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 176 pgfwLYSSGSTGRPKGVLHSQGNPYWTAELYAKpVLSLGEADICFSAAKLYFAYGLGNALTFPLSVGATVVLMaERPTPE 255
Cdd:COG0318 106 ----LYTSGTTGRPKGVMLTHRNLLANAAAIAA-ALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLL-PRFDPE 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 256 ATFRRWLDYQPTVFFGAPTGYAGMLAAPGLPTREQVSLRLCSSAGEALPADLGERFTAHFGCEIIDGIGSTEMLHIFLSN 335
Cdd:COG0318 180 RVLELIERERVTVLFGVPTMLARLLRHPEFARYDLSSLRLVVSGGAPLPPELLERFEERFGVRIVEGYGLTETSPVVTVN 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 336 --RPGQVRYGTTGWPVPGYAVELRDEDGHAVPDGDVGDLYIQGPSAALMYWGNREKSRETFRGGWTKSGDKYVRNADGSY 413
Cdd:COG0318 260 peDPGERRPGSVGRPLPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAFRDGWLRTGDLGRLDEDGYL 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 414 SYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQAGLTKTKAFVVLKPGAQVSETELKAFVKERLAPYKYP 493
Cdd:COG0318 340 YIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPGAELDAEELRAFLRERLARYKVP 419
|
490 500 510
....*....|....*....|....*....|
gi 1920939256 494 RIIEFMDALPKTATGKIQRFRLREMEGAPA 523
Cdd:COG0318 420 RRVEFVDELPRTASGKIDRRALRERYAAGA 449
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
25-516 |
2.31e-122 |
|
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: 366.89 E-value: 2.31e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 25 AQRPGKTAYIDDHGTMRYGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLLTADDYA 104
Cdd:cd05936 10 RRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYTPRELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 105 YMLQHSRAQAVLVsgallpvlrqamaqggheaatvivsrpagplpdgMIALEAWIERNAPLAAPASTGPDDPGFWLYSSG 184
Cdd:cd05936 90 HILNDSGAKALIV----------------------------------AVSFTDLLAAGAPLGERVALTPEDVAVLQYTSG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 185 STGRPKGVLHSQGNPYWTAELYAKPVLSLGEA-DICFSAAKLYFAYGLGNALTFPLSVGATVVLMaERPTPEATFRRWLD 263
Cdd:cd05936 136 TTGVPKGAMLTHRNLVANALQIKAWLEDLLEGdDVVLAALPLFHVFGLTVALLLPLALGATIVLI-PRFRPIGVLKEIRK 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 264 YQPTVFFGAPTGYAGMLAAPGLPTREQVSLRLCSSAGEALPADLGERFTAHFGCEIIDGIGSTEMLHIFLSNRPGQVRY- 342
Cdd:cd05936 215 HRVTIFPGVPTMYIALLNAPEFKKRDFSSLRLCISGGAPLPVEVAERFEELTGVPIVEGYGLTETSPVVAVNPLDGPRKp 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 343 GTTGWPVPGYAVELRDEDGHAVPDGDVGDLYIQGPSAALMYWGNREKSRETFRGGWTKSGDKYVRNADGSYSYAGRSDDM 422
Cdd:cd05936 295 GSIGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFVDGWLRTGDIGYMDEDGYFFIVDRKKDM 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 423 LKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQAGLTKTKAFVVLKPGAQVSETELKAFVKERLAPYKYPRIIEFMDAL 502
Cdd:cd05936 375 IIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEGASLTEEEIIAFCREQLAGYKVPRQVEFRDEL 454
|
490
....*....|....
gi 1920939256 503 PKTATGKIQRFRLR 516
Cdd:cd05936 455 PKSAVGKILRRELR 468
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
13-518 |
3.63e-115 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 350.26 E-value: 3.63e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 13 PFNFAqHLIACNAQ-RPGKTAYIDDHGTMRYGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVP 91
Cdd:PRK06187 5 PLTIG-RILRHGARkHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 92 VAVNTLLTADDYAYMLQHSRAQAVLVSGALLPVLRQAMAQGGHEAATVIVS-RPAGPLPDGMIALEAWIERNAPLAAPAS 170
Cdd:PRK06187 84 HPINIRLKPEEIAYILNDAEDRVVLVDSEFVPLLAAILPQLPTVRTVIVEGdGPAAPLAPEVGEYEELLAAASDTFDFPD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 171 TGPDDPGFWLYSSGSTGRPKGVLHSQGNpYWTAELYAKPVLSLGEADICFSAAKLYFAYGLGNALtFPLSVGATVVLMAE 250
Cdd:PRK06187 164 IDENDAAAMLYTSGTTGHPKGVVLSHRN-LFLHSLAVCAWLKLSRDDVYLVIVPMFHVHAWGLPY-LALMAGAKQVIPRR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 251 RPtPEATFRRWLDYQPTVFFGAPTGYAGMLAAPGLPTREQVSLRLCSSAGEALPADLGERFTAHFGCEIIDGIGSTEMLH 330
Cdd:PRK06187 242 FD-PENLLDLIETERVTFFFAVPTIWQMLLKAPRAYFVDFSSLRLVIYGGAALPPALLREFKEKFGIDLVQGYGMTETSP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 331 IFLSNRP-----GQVRY-GTTGWPVPGYAVELRDEDGHAVP--DGDVGDLYIQGPSAALMYWGNREKSRETFRGGWTKSG 402
Cdd:PRK06187 321 VVSVLPPedqlpGQWTKrRSAGRPLPGVEARIVDDDGDELPpdGGEVGEIIVRGPWLMQGYWNRPEATAETIDGGWLHTG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 403 DKYVRNADGsYSY-AGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQAGLTKTKAFVVLKPGAQVSETELKA 481
Cdd:PRK06187 401 DVGYIDEDG-YLYiTDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVLKPGATLDAKELRA 479
|
490 500 510
....*....|....*....|....*....|....*..
gi 1920939256 482 FVKERLAPYKYPRIIEFMDALPKTATGKIQRFRLREM 518
Cdd:PRK06187 480 FLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVLREQ 516
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
175-511 |
3.34e-112 |
|
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: 336.18 E-value: 3.34e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 175 DPGFWLYSSGSTGRPKGVLHSQGNPYWTAELYAKpVLSLGEADICFSAAKLYFAyGLGNALTFPLSVGATVVLMaERPTP 254
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAA-SGGLTEGDVFLSTLPLFHI-GGLFGLLGALLAGGTVVLL-PKFDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 255 EATFRRWLDYQPTVFFGAPTGYAGMLAAPGLPTREQVSLRLCSSAGEALPADLGERFTAHFGCEIIDGIGSTEMLHIFLS 334
Cdd:cd04433 78 EAALELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGGTVAT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 335 NRP--GQVRYGTTGWPVPGYAVELRDEDGHAVPDGDVGDLYIQGPSAALMYWGNREKSRETFRGGWTKSGDKYVRNADGS 412
Cdd:cd04433 158 GPPddDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVDEDGWYRTGDLGRLDEDGY 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 413 YSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQAGLTKTKAFVVLKPGAQVSETELKAFVKERLAPYKY 492
Cdd:cd04433 238 LYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLDAEELRAHVRERLAPYKV 317
|
330
....*....|....*....
gi 1920939256 493 PRIIEFMDALPKTATGKIQ 511
Cdd:cd04433 318 PRRVVFVDALPRTASGKID 336
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
25-518 |
6.93e-112 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 341.50 E-value: 6.93e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 25 AQRPGKTAYIDDHGTMRYGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLLTADDYA 104
Cdd:PRK07656 16 RRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADEAA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 105 YMLQHSRAQAVLVSGALLPVLRQAMAQGGH-EAATVIVSRPAGPLPDGMIALEAWIERNAPLAAPASTGPDDPGFWLYSS 183
Cdd:PRK07656 96 YILARGDAKALFVLGLFLGVDYSATTRLPAlEHVVICETEEDDPHTEKMKTFTDFLAAGDPAERAPEVDPDDVADILFTS 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 184 GSTGRPKGVLHSQGNPYWTAELYAKpVLSLGEADICFSAAKLYFAYGLGNALTFPLSVGATVVLMaerPT--PEATFRRW 261
Cdd:PRK07656 176 GTTGRPKGAMLTHRQLLSNAADWAE-YLGLTEGDRYLAANPFFHVFGYKAGVNAPLMRGATILPL---PVfdPDEVFRLI 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 262 LDYQPTVFFGAPTGYAGMLAAPGLPTREQVSLRLCSSAGEALPADLGERFTAHFGCEII-DGIGSTEMLHIFLSNRPGQV 340
Cdd:PRK07656 252 ETERITVLPGPPTMYNSLLQHPDRSAEDLSSLRLAVTGAASMPVALLERFESELGVDIVlTGYGLSEASGVTTFNRLDDD 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 341 RY---GTTGWPVPGyaVELR--DEDGHAVPDGDVGDLYIQGPSAALMYWGNREKSRETFRG-GWTKSGDKYVRNADGSYS 414
Cdd:PRK07656 332 RKtvaGTIGTAIAG--VENKivNELGEEVPVGEVGELLVRGPNVMKGYYDDPEATAAAIDAdGWLHTGDLGRLDEEGYLY 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 415 YAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPD----QAGltktKAFVVLKPGAQVSETELKAFVKERLAPY 490
Cdd:PRK07656 410 IVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDerlgEVG----KAYVVLKPGAELTEEELIAYCREHLAKY 485
|
490 500
....*....|....*....|....*...
gi 1920939256 491 KYPRIIEFMDALPKTATGKIQRFRLREM 518
Cdd:PRK07656 486 KVPRSIEFLDELPKNATGKVLKRALREK 513
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
42-516 |
3.45e-110 |
|
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: 334.31 E-value: 3.45e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 42 YGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLLTADDYAYMLQHSRAQAVLvsgal 121
Cdd:cd05972 3 FRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIV----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 122 lpvlrqamaqggheaatvivsrpagplpdgmialeawiernaplaapasTGPDDPGFWLYSSGSTGRPKGVLHSQGNPYw 201
Cdd:cd05972 78 -------------------------------------------------TDAEDPALIYFTSGTTGLPKGVLHTHSYPL- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 202 TAELYAKPVLSLGEADICFSAAKLYFAYGLGNALTFPLSVGATVVLMAERP-TPEATFRRWLDYQPTVFFGAPTGYAgML 280
Cdd:cd05972 108 GHIPTAAYWLGLRPDDIHWNIADPGWAKGAWSSFFGPWLLGATVFVYEGPRfDAERILELLERYGVTSFCGPPTAYR-ML 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 281 AAPGLPTREQVSLRLCSSAGEALPADLGERFTAHFGCEIIDGIGSTEmLHIFLSNRPGQ-VRYGTTGWPVPGYAVELRDE 359
Cdd:cd05972 187 IKQDLSSYKFSHLRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTE-TGLTVGNFPDMpVKPGSMGRPTPGYDVAIIDD 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 360 DGHAVPDGDVGDLYIQGPSAALM--YWGNREKSRETFRGGWTKSGDKYVRNADGSYSYAGRSDDMLKVSGIYVSPFEVEA 437
Cdd:cd05972 266 DGRELPPGEEGDIAIKLPPPGLFlgYVGDPEKTEASIRGDYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVES 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 438 TLAQHPAILEAAVIGVPDQAGLTKTKAFVVLKPGAQVSET---ELKAFVKERLAPYKYPRIIEFMDALPKTATGKIQRFR 514
Cdd:cd05972 346 ALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYEPSEElaeELQGHVKKVLAPYKYPREIEFVEELPKTISGKIRRVE 425
|
..
gi 1920939256 515 LR 516
Cdd:cd05972 426 LR 427
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
25-512 |
1.41e-105 |
|
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: 322.64 E-value: 1.41e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 25 AQRPGKTAYIDDHGTMRYGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLLTADDYA 104
Cdd:cd17631 6 RRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEVA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 105 YMLQHSRAQAVLvsgallpvlrqamaqggheaatvivsrpagplpdgmialeawiernaplaapastgpDDPGFWLYSSG 184
Cdd:cd17631 86 YILADSGAKVLF---------------------------------------------------------DDLALLMYTSG 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 185 STGRPKGVLHSQGNPYW--TAELYAkpvLSLGEADICFSAAKLYFAYGLGNALTFPLSVGATVVLMaERPTPEATFRRWL 262
Cdd:cd17631 109 TTGRPKGAMLTHRNLLWnaVNALAA---LDLGPDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVIL-RKFDPETVLDLIE 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 263 DYQPTVFFGAPTGYAGMLAAPGLPTREQVSLRLCSSAGEALPADLGERFTAhFGCEIIDGIGSTEM--LHIFLSNRPGQV 340
Cdd:cd17631 185 RHRVTSFFLVPTMIQALLQHPRFATTDLSSLRAVIYGGAPMPERLLRALQA-RGVKFVQGYGMTETspGVTFLSPEDHRR 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 341 RYGTTGWPVPGYAVELRDEDGHAVPDGDVGDLYIQGPSAALMYWGNREKSRETFRGGWTKSGDKYVRNADGSYSYAGRSD 420
Cdd:cd17631 264 KLGSAGRPVFFVEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFRDGWFHTGDLGRLDEDGYLYIVDRKK 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 421 DMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPD----QAGltktKAFVVLKPGAQVSETELKAFVKERLAPYKYPRII 496
Cdd:cd17631 344 DMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDekwgEAV----VAVVVPRPGAELDEDELIAHCRERLARYKIPKSV 419
|
490
....*....|....*.
gi 1920939256 497 EFMDALPKTATGKIQR 512
Cdd:cd17631 420 EFVDALPRNATGKILK 435
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
25-426 |
1.07e-102 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 314.64 E-value: 1.07e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 25 AQRPGKTAY-IDDHGTMRYGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLLTADDY 103
Cdd:pfam00501 6 ARTPDKTALeVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 104 AYMLQHSRAQAVLVSGAL-LPVLRQAMAQGGHEAATVIVSRPAGPLPDGMIALEAWieRNAPLAAPASTGPDDPGFWLYS 182
Cdd:pfam00501 86 AYILEDSGAKVLITDDALkLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKP--ADVPPPPPPPPDPDDLAYIIYT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 183 SGSTGRPKGVLHSQGNPYWTAELYAK---PVLSLGEADICFSAAKLYFAYGLGNALTFPLSVGATVVLMaeRPTPEATFR 259
Cdd:pfam00501 164 SGTTGKPKGVMLTHRNLVANVLSIKRvrpRGFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVVLP--PGFPALDPA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 260 RWLD----YQPTVFFGAPTGYAGMLAAPGLPTREQVSLRLCSSAGEALPADLGERFTAHFGCEIIDGIGSTEMLHIFLSN 335
Cdd:pfam00501 242 ALLElierYKVTVLYGVPTLLNMLLEAGAPKRALLSSLRLVLSGGAPLPPELARRFRELFGGALVNGYGLTETTGVVTTP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 336 RPG---QVRYGTTGWPVPGYAVELRDED-GHAVPDGDVGDLYIQGPSAALMYWGNREKSRETF-RGGWTKSGDKYVRNAD 410
Cdd:pfam00501 322 LPLdedLRSLGSVGRPLPGTEVKIVDDEtGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFdEDGWYRTGDLGRRDED 401
|
410
....*....|....*.
gi 1920939256 411 GSYSYAGRSDDMLKVS 426
Cdd:pfam00501 402 GYLEIVGRKKDQIKLG 417
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
41-516 |
9.12e-101 |
|
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: 309.99 E-value: 9.12e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 41 RYGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLLTADDYAYMLQHSRAQAVLVsga 120
Cdd:cd05934 5 TYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 121 llpvlrqamaqggheaatvivsrpagplpdgmialeawiernaplaapastgpdDPGFWLYSSGSTGRPKGVLHSQGNPY 200
Cdd:cd05934 82 ------------------------------------------------------DPASILYTSGTTGPPKGVVITHANLT 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 201 WTAELYAKpVLSLGEADICFSAAKLYFAYGLGNALTFPLSVGATVVLmAERPTPEATFRRWLDYQPTVF--FGAPTGYag 278
Cdd:cd05934 108 FAGYYSAR-RFGLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVL-LPRFSASRFWSDVRRYGATVTnyLGAMLSY-- 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 279 MLAAPGLPTREQVSLRLCSSAgeALPADLGERFTAHFGCEIIDGIGSTEMLHIFLSNRPGQVRYGTTGWPVPGYAVELRD 358
Cdd:cd05934 184 LLAQPPSPDDRAHRLRAAYGA--PNPPELHEEFEERFGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAPGYEVRIVD 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 359 EDGHAVPDGDVGDLYI---QGPSAALMYWGNREKSRETFRGGWTKSGDKYVRNADGSYSYAGRSDDMLKVSGIYVSPFEV 435
Cdd:cd05934 262 DDGQELPAGEPGELVIrglRGWGFFKGYYNMPEATAEAMRNGWFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEV 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 436 EATLAQHPAILEAAVIGVPDQAGLTKTKAFVVLKPGAQVSETELKAFVKERLAPYKYPRIIEFMDALPKTATGKIQRFRL 515
Cdd:cd05934 342 ERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLDPEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQL 421
|
.
gi 1920939256 516 R 516
Cdd:cd05934 422 R 422
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
25-517 |
2.07e-98 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 307.24 E-value: 2.07e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 25 AQR-PGKTAYIDDHGTMRYGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLLTADDY 103
Cdd:PRK08316 21 ARRyPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEEL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 104 AYMLQHSRAQAVLVSGALLPVLRQAMAQGGHEAATVIVSRPAGPLPDGMIALEAWIERNAPLAAPASTGPDDPGFWLYSS 183
Cdd:PRK08316 101 AYILDHSGARAFLVDPALAPTAEAALALLPVDTLILSLVLGGREAPGGWLDFADWAEAGSVAEPDVELADDDLAQILYTS 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 184 GSTGRPKGVLHSQGNPYWTaelYAKPV--LSLGEADICFSAAKLYFAYGLGNALTFPLSVGATVVLMaERPTPEATFRRW 261
Cdd:PRK08316 181 GTESLPKGAMLTHRALIAE---YVSCIvaGDMSADDIPLHALPLYHCAQLDVFLGPYLYVGATNVIL-DAPDPELILRTI 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 262 LDYQPTVFFGAPTGYAGMLAAPGLPTREQVSLRLCSSAGEALPADLGERFTAHF-GCEIIDGIGSTEM--LHIFLSNRPG 338
Cdd:PRK08316 257 EAERITSFFAPPTVWISLLRHPDFDTRDLSSLRKGYYGASIMPVEVLKELRERLpGLRFYNCYGQTEIapLATVLGPEEH 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 339 QVRYGTTGWPVpgYAVELR--DEDGHAVPDGDVGDLYIQGPSAALMYWGNREKSRETFRGGWTKSGDKYVRNADGSYSYA 416
Cdd:PRK08316 337 LRRPGSAGRPV--LNVETRvvDDDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEAFRGGWFHSGDLGVMDEEGYITVV 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 417 GRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQAGLTKTKAFVVLKPGAQVSETELKAFVKERLAPYKYPRII 496
Cdd:PRK08316 415 DRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAGATVTEDELIAHCRARLAGFKVPKRV 494
|
490 500
....*....|....*....|.
gi 1920939256 497 EFMDALPKTATGKIQRFRLRE 517
Cdd:PRK08316 495 IFVDELPRNPSGKILKRELRE 515
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
32-511 |
2.68e-86 |
|
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341237 [Multi-domain] Cd Length: 486 Bit Score: 274.48 E-value: 2.68e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 32 AYIDDHG--TMRYGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLLTADDYAYMLQH 109
Cdd:cd05911 1 AQIDADTgkELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 110 SRAQAVLVSGALLPVLRQAMAQGGHEAaTVIV--SRPAGPLPDGMIALEAWIERNAPLAAPASTGPDDPGFWLYSSGSTG 187
Cdd:cd05911 81 SKPKVIFTDPDGLEKVKEAAKELGPKD-KIIVldDKPDGVLSIEDLLSPTLGEEDEDLPPPLKDGKDDTAAILYSSGTTG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 188 RPKGVLHSQGNPYWTAELYAKPV-LSLGEADICFSAAKLYFAYGLGNALTFPLSvGATVVLMaERPTPEATFRRWLDYQP 266
Cdd:cd05911 160 LPKGVCLSHRNLIANLSQVQTFLyGNDGSNDVILGFLPLYHIYGLFTTLASLLN-GATVIIM-PKFDSELFLDLIEKYKI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 267 TVFFGAPTGYAGMLAAPgLPTREQV-SLRLCSSAGEALPADLGERFTAHFG-CEIIDGIGSTEMLHIFLSNRPGQVRYGT 344
Cdd:cd05911 238 TFLYLVPPIAAALAKSP-LLDKYDLsSLRVILSGGAPLSKELQELLAKRFPnATIKQGYGMTETGGILTVNPDGDDKPGS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 345 TGWPVPGYAVELRDEDG-HAVPDGDVGDLYIQGPSAALMYWGNREKSRETF-RGGWTKSGDKYVRNADGSYSYAGRSDDM 422
Cdd:cd05911 317 VGRLLPNVEAKIVDDDGkDSLGPNEPGEICVRGPQVMKGYYNNPEATKETFdEDGWLHTGDIGYFDEDGYLYIVDRKKEL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 423 LKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQAGLTKTKAFVVLKPGAQVSETELKAFVKERLAPYKypRI---IEFM 499
Cdd:cd05911 397 IKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGEKLTEKEVKDYVAKKVASYK--QLrggVVFV 474
|
490
....*....|..
gi 1920939256 500 DALPKTATGKIQ 511
Cdd:cd05911 475 DEIPKSASGKIL 486
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
42-517 |
2.64e-85 |
|
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: 272.26 E-value: 2.64e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 42 YGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLLTADDYAYMLQHSRAQAVLV-SGA 120
Cdd:cd05926 17 YADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVLTpKGE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 121 LLPVLRQAMAQG------GHEAATVIVSRPAGPLPDGMIALEAWIERNAPLaapastgPDDPGFWLYSSGSTGRPKGVLH 194
Cdd:cd05926 97 LGPASRAASKLGlailelALDVGVLIRAPSAESLSNLLADKKNAKSEGVPL-------PDDLALILHTSGTTGRPKGVPL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 195 SQGNpYWTAELYAKPVLSLGEADICFSAAKLYFAYGLGNALTFPLSVGATVVlMAERPTPeATFRRWL-DYQPTVFFGAP 273
Cdd:cd05926 170 THRN-LAASATNITNTYKLTPDDRTLVVMPLFHVHGLVASLLSTLAAGGSVV-LPPRFSA-STFWPDVrDYNATWYTAVP 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 274 TGYAGMLAAP-GLPTREQVSLRLCSSAGEALPADLGERFTAHFGCEIIDGIGSTEMLHIFLSNR--PGQVRYGTTGWPVp 350
Cdd:cd05926 247 TIHQILLNRPePNPESPPPKLRFIRSCSASLPPAVLEALEATFGAPVLEAYGMTEAAHQMTSNPlpPGPRKPGSVGKPV- 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 351 gyAVELR--DEDGHAVPDGDVGDLYIQGPSAALMYWGNREKSRE-TFRGGWTKSGDKYVRNADGSYSYAGRSDDMLKVSG 427
Cdd:cd05926 326 --GVEVRilDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEaAFKDGWFRTGDLGYLDADGYLFLTGRIKELINRGG 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 428 IYVSPFEVEATLAQHPAILEAAVIGVPDQAGLTKTKAFVVLKPGAQVSETELKAFVKERLAPYKYPRIIEFMDALPKTAT 507
Cdd:cd05926 404 EKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGASVTEEELRAFCRKHLAAFKVPKKVYFVDELPKTAT 483
|
490
....*....|
gi 1920939256 508 GKIQRFRLRE 517
Cdd:cd05926 484 GKIQRRKVAE 493
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
14-517 |
4.86e-85 |
|
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: 272.83 E-value: 4.86e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 14 FNFAQHLI-ACNAQRPGKTA--YIDDHGTMR---YGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYA 87
Cdd:cd05970 16 FNFAYDVVdAMAKEYPDKLAlvWCDDAGEERiftFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 88 GIVPVAVNTLLTADDYAYMLQHSRAQAVLV--SGALLPVLRQAMAQGGHEAATVIVsrpAGPLPDGMIALEAWIERNAPL 165
Cdd:cd05970 96 GAIAIPATHQLTAKDIVYRIESADIKMIVAiaEDNIPEEIEKAAPECPSKPKLVWV---GDPVPEGWIDFRKLIKNASPD 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 166 ----AAPASTGPDDPGFWLYSSGSTGRPKGVLHSQGNP--------YWTaelyakpvlSLGEADICFSAAKLYFAYGLGN 233
Cdd:cd05970 173 ferpTANSYPCGEDILLVYFSSGTTGMPKMVEHDFTYPlghivtakYWQ---------NVREGGLHLTVADTGWGKAVWG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 234 ALTFPLSVGATV-VLMAERPTPEATFRRWLDYQPTVFFGAPTGYAgMLAAPGLPTREQVSLRLCSSAGEALPADLGERFT 312
Cdd:cd05970 244 KIYGQWIAGAAVfVYDYDKFDPKALLEKLSKYGVTTFCAPPTIYR-FLIREDLSRYDLSSLRYCTTAGEALNPEVFNTFK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 313 AHFGCEIIDGIGSTEMLhIFLSNRPG-QVRYGTTGWPVPGYAVELRDEDGHAVPDGDVGDLYI---QGPSAALM--YWGN 386
Cdd:cd05970 323 EKTGIKLMEGFGQTETT-LTIATFPWmEPKPGSMGKPAPGYEIDLIDREGRSCEAGEEGEIVIrtsKGKPVGLFggYYKD 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 387 REKSRETFRGGWTKSGDKYVRNADGSYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQAGLTKTKAFV 466
Cdd:cd05970 402 AEKTAEVWHDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATI 481
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1920939256 467 VLKPGAQVSET---ELKAFVKERLAPYKYPRIIEFMDALPKTATGKIQRFRLRE 517
Cdd:cd05970 482 VLAKGYEPSEElkkELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEIRE 535
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
19-523 |
2.00e-81 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 263.74 E-value: 2.00e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 19 HLIACNAQR-PGKTAYIDDHGTMRYGELAERIRRVAGALQ-ASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNT 96
Cdd:PRK08314 14 HNLEVSARRyPDKTAIVFYGRAISYRELLEEAERLAGYLQqECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 97 LLTADDYAYMLQHSRAQAVLVSGALLPVLRQAMAQGGheAATVIVSRPAGPLPD-GMIALEAWIERNAPLAA-------- 167
Cdd:PRK08314 94 MNREEELAHYVTDSGARVAIVGSELAPKVAPAVGNLR--LRHVIVAQYSDYLPAePEIAVPAWLRAEPPLQAlapggvva 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 168 ------------PASTGPDDPGFWLYSSGSTGRPKGVLHSQGNpYWTAELYAKPVLSLGEADICFSAAKLYFAYGLGNAL 235
Cdd:PRK08314 172 wkealaaglappPHTAGPDDLAVLPYTSGTTGVPKGCMHTHRT-VMANAVGSVLWSNSTPESVVLAVLPLFHVTGMVHSM 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 236 TFPLSVGATVVLMAeRPTPEATFRRWLDYQPTVFFGAPTGYAGMLAAPGLPTREQVSLRLCSSAGEALPADLGERFTAHF 315
Cdd:PRK08314 251 NAPIYAGATVVLMP-RWDREAAARLIERYRVTHWTNIPTMVVDFLASPGLAERDLSSLRYIGGGGAAMPEAVAERLKELT 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 316 GCEIIDGIGSTEMLHIFLSNRPGQVRYGTTGwpVPGYAVELRDED---GHAVPDGDVGDLYIQGPSAALMYWGNREKSRE 392
Cdd:PRK08314 330 GLDYVEGYGLTETMAQTHSNPPDRPKLQCLG--IPTFGVDARVIDpetLEELPPGEVGEIVVHGPQVFKGYWNRPEATAE 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 393 TF--RGG--WTKSGDKYVRNADGSYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQAGLTKTKAFVVL 468
Cdd:PRK08314 408 AFieIDGkrFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPDPRRGETVKAVVVL 487
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1920939256 469 KPGAQ--VSETELKAFVKERLAPYKYPRIIEFMDALPKTATGKIQRFRLREMEGAPA 523
Cdd:PRK08314 488 RPEARgkTTEEEIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKILWRQLQEQEKARA 544
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
41-516 |
1.48e-79 |
|
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: 255.43 E-value: 1.48e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 41 RYGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLLTADDYAYMLQHSRAQAVLvsga 120
Cdd:cd05971 8 TFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALV---- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 121 llpvlrqamaqggheaatvivsrpagplpdgmialeawiernaplaapaSTGPDDPGFWLYSSGSTGRPKGVLHSQ---- 196
Cdd:cd05971 84 -------------------------------------------------TDGSDDPALIIYTSGTTGPPKGALHAHrvll 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 197 ---GNPYWTAELYAKPvlslgeADICFSAAKLYFAYGLGNALTFPLSVGATVVlmAERPT---PEATFRRWLDYQPTVFF 270
Cdd:cd05971 115 ghlPGVQFPFNLFPRD------GDLYWTPADWAWIGGLLDVLLPSLYFGVPVL--AHRMTkfdPKAALDLMSRYGVTTAF 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 271 GAPTGYAGMLAAPGLPTREQVSLRLCSSAGEALPADLGERFTAHFGCEIIDGIGSTEMlHIFLSNRP--GQVRYGTTGWP 348
Cdd:cd05971 187 LPPTALKMMRQQGEQLKHAQVKLRAIATGGESLGEELLGWAREQFGVEVNEFYGQTEC-NLVIGNCSalFPIKPGSMGKP 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 349 VPGYAVELRDEDGHAVPDGDVGDLYIQGPSAALM--YWGNREKSRETFRGGWTKSGDKYVRNADGSYSYAGRSDDMLKVS 426
Cdd:cd05971 266 IPGHRVAIVDDNGTPLPPGEVGEIAVELPDPVAFlgYWNNPSATEKKMAGDWLLTGDLGRKDSDGYFWYVGRDDDVITSS 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 427 GIYVSPFEVEATLAQHPAILEAAVIGVPDQAGLTKTKAFVVLKPGAQVSET---ELKAFVKERLAPYKYPRIIEFMDALP 503
Cdd:cd05971 346 GYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGETPSDAlarEIQELVKTRLAAHEYPREIEFVNELP 425
|
490
....*....|...
gi 1920939256 504 KTATGKIQRFRLR 516
Cdd:cd05971 426 RTATGKIRRRELR 438
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
42-516 |
3.25e-78 |
|
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: 252.05 E-value: 3.25e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 42 YGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLLTADDYAYMLQHSRAQAVLVSGAL 121
Cdd:cd05973 3 FGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTDAAN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 122 LPVLrqamaqggheaatvivsrpagplpdgmialeawiernaplaapastgPDDPGFWLYSSGSTGRPKGVLHS-QGNPY 200
Cdd:cd05973 83 RHKL-----------------------------------------------DSDPFVMMFTSGTTGLPKGVPVPlRALAA 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 201 WTAelYAKPVLSLGEADICFSAAKLYFAYGLGNALTFPLSVGATVVLMAERPTPEATFRRWLDYQPTVFFGAPTGYAGML 280
Cdd:cd05973 116 FGA--YLRDAVDLRPEDSFWNAADPGWAYGLYYAITGPLALGHPTILLEGGFSVESTWRVIERLGVTNLAGSPTAYRLLM 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 281 AAP-GLPTREQVSLRLCSSAGEALPADLGERFTAHFGCEIIDGIGSTEmLHIFLSNRPG---QVRYGTTGWPVPGYAVEL 356
Cdd:cd05973 194 AAGaEVPARPKGRLRRVSSAGEPLTPEVIRWFDAALGVPIHDHYGQTE-LGMVLANHHAlehPVHAGSAGRAMPGWRVAV 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 357 RDEDGHAVPDGDVGDLYIQGPSAALMYW-GNREKSRETFRGGWTKSGDKYVRNADGSYSYAGRSDDMLKVSGIYVSPFEV 435
Cdd:cd05973 273 LDDDGDELGPGEPGRLAIDIANSPLMWFrGYQLPDTPAIDGGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDV 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 436 EATLAQHPAILEAAVIGVPDQAGLTKTKAFVVLKPGAQVSET---ELKAFVKERLAPYKYPRIIEFMDALPKTATGKIQR 512
Cdd:cd05973 353 ESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHEGTPAladELQLHVKKRLSAHAYPRTIHFVDELPKTPSGKIQR 432
|
....
gi 1920939256 513 FRLR 516
Cdd:cd05973 433 FLLR 436
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
2-517 |
1.17e-76 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 251.22 E-value: 1.17e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 2 TAEPQVQPPGTPFNFAQH----LIACNAQR-PGKTAYIDDHGTMRYGELAERIRRVAGALQASGIHREERVLLLMHDGND 76
Cdd:PRK06155 4 LGAGLAARAVDPLPPSERtlpaMLARQAERyPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 77 WPVCFLGAMYAGIVPVAVNTLLTADDYAYMLQHSRAQAVLVSGALLPVLRQAMAQGGHEAATVIV-SRPAGPLPDGMIAL 155
Cdd:PRK06155 84 FLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLVVEAALLAALEAADPGDLPLPAVWLLdAPASVSVPAGWSTA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 156 EawIERNAPLAAPASTGPDDPGFWLYSSGSTGRPKGVLHSQGNPYWTAELYAKpVLSLGEADICFSAAKLYFAYGLgNAL 235
Cdd:PRK06155 164 P--LPPLDAPAPAAAVQPGDTAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAE-DLEIGADDVLYTTLPLFHTNAL-NAF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 236 TFPLSVGATVVLM----AERPTPEAtfRRwldYQPTVFFGAPTGYAGMLAAPglPTREQVSLRLCSSAGEALPADLGERF 311
Cdd:PRK06155 240 FQALLAGATYVLEprfsASGFWPAV--RR---HGATVTYLLGAMVSILLSQP--ARESDRAHRVRVALGPGVPAALHAAF 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 312 TAHFGCEIIDGIGSTEMLHIFLSNRPGQvRYGTTGWPVPGYAVELRDEDGHAVPDGDVGDLYIQG--PSA-ALMYWGNRE 388
Cdd:PRK06155 313 RERFGVDLLDGYGSTETNFVIAVTHGSQ-RPGSMGRLAPGFEARVVDEHDQELPDGEPGELLLRAdePFAfATGYFGMPE 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 389 KSRETFRGGWTKSGDKYVRNADGSYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQAGLTKTKAFVVL 468
Cdd:PRK06155 392 KTVEAWRNLWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVL 471
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1920939256 469 KPGAQVSETELKAFVKERLAPYKYPRIIEFMDALPKTATGKIQRFRLRE 517
Cdd:PRK06155 472 RDGTALEPVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVLRE 520
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
27-518 |
1.83e-76 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 251.11 E-value: 1.83e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 27 RPGKTAYIDDHGTMRYGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLLTADDYAYM 106
Cdd:PRK06178 46 RPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYE 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 107 LQHSRAQAVLVSGALLPVLRQAMAQGGHE------AATVIVSRPAGPLPDGM----IALEAWIE-----RNAPLAAPA-S 170
Cdd:PRK06178 126 LNDAGAEVLLALDQLAPVVEQVRAETSLRhvivtsLADVLPAEPTLPLPDSLraprLAAAGAIDllpalRACTAPVPLpP 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 171 TGPDDPGFWLYSSGSTGRPKGVLHSQGNPYWTAELYAKPVLSLGEADICFSAAKLYFAYGLGNALTFPLSVGATVVLMAe 250
Cdd:PRK06178 206 PALDALAALNYTGGTTGMPKGCEHTQRDMVYTAAAAYAVAVVGGEDSVFLSFLPEFWIAGENFGLLFPLFSGATLVLLA- 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 251 RPTPEATFRRWLDYQPTVFFGAPTGYAGMLAAPGLPTREQVSLR--LCSSAGEALPADLGERFTAHFGCEIID---GIGS 325
Cdd:PRK06178 285 RWDAVAFMAAVERYRVTRTVMLVDNAVELMDHPRFAEYDLSSLRqvRVVSFVKKLNPDYRQRWRALTGSVLAEaawGMTE 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 326 TEMLHIF----------LSNRPGQVrygttGWPVPGYAVELRDEDGHA-VPDGDVGDLYIQGPSAALMYWGNREKSRETF 394
Cdd:PRK06178 365 THTCDTFtagfqdddfdLLSQPVFV-----GLPVPGTEFKICDFETGElLPLGAEGEIVVRTPSLLKGYWNKPEATAEAL 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 395 RGGWTKSGDKYVRNADGSYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQAGLTKTKAFVVLKPGAQV 474
Cdd:PRK06178 440 RDGWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPGADL 519
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1920939256 475 SETELKAFVKERLAPYKYPrIIEFMDALPKTATGKIQRFRLREM 518
Cdd:PRK06178 520 TAAALQAWCRENMAVYKVP-EIRIVDALPMTATGKVRKQDLQAL 562
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
30-517 |
7.16e-75 |
|
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: 243.35 E-value: 7.16e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 30 KTAYIDDHGTMRYGELAERIRRVAGALQASG-IHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLLTADDYAYMLQ 108
Cdd:cd05941 2 RIAIVDDGDSITYADLVARAARLANRLLALGkDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVIT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 109 HSRAQAVLvsgallpvlrqamaqggheaatvivsRPAgplpdgMIaleawiernaplaapastgpddpgfwLYSSGSTGR 188
Cdd:cd05941 82 DSEPSLVL--------------------------DPA------LI--------------------------LYTSGTTGR 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 189 PKGVLHSQGNpywtaeLYAKpVLSLGEA------DICFSAAKLYFAYGLGNALTFPLSVGATVVLMAeRPTPEATFRRWL 262
Cdd:cd05941 104 PKGVVLTHAN------LAAN-VRALVDAwrwtedDVLLHVLPLHHVHGLVNALLCPLFAGASVEFLP-KFDPKEVAISRL 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 263 DYQPTVFFGAPTGYAGMLAAPGLPTREQV--------SLRLCSSAGEALPADLGERFTAHFGCEIIDGIGSTEMLhIFLS 334
Cdd:cd05941 176 MPSITVFMGVPTIYTRLLQYYEAHFTDPQfaraaaaeRLRLMVSGSAALPVPTLEEWEAITGHTLLERYGMTEIG-MALS 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 335 NR-PGQVRYGTTGWPVPGyaVELR---DEDGHAVPDGDVGDLYIQGPSAALMYWGNREKSRETFRG-GWTKSGDKYVRNA 409
Cdd:cd05941 255 NPlDGERRPGTVGMPLPG--VQARivdEETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDdGWFKTGDLGVVDE 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 410 DGSYSYAGR-SDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQAGLTKTKAFVVLKPGA-QVSETELKAFVKERL 487
Cdd:cd05941 333 DGYYWILGRsSVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGAaALSLEELKEWAKQRL 412
|
490 500 510
....*....|....*....|....*....|
gi 1920939256 488 APYKYPRIIEFMDALPKTATGKIQRFRLRE 517
Cdd:cd05941 413 APYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
42-512 |
8.76e-75 |
|
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: 242.77 E-value: 8.76e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 42 YGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLLTADDYAYMLQHSRAQAVLVSGAL 121
Cdd:cd05935 4 YLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGSEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 122 lpvlrqamaqggheaatvivsrpagplpdgmialeawiernaplaapastgpDDPGFWLYSSGSTGRPKGVLHSQGNPYW 201
Cdd:cd05935 84 ----------------------------------------------------DDLALIPYTSGTTGLPKGCMHTHFSAAA 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 202 TAELYAKpVLSLGEADICFSAAKLYFAYGLGNALTFPLSVGATVVLMA--ERPTPEATFRRwldYQPTVFFGAPTGYAGM 279
Cdd:cd05935 112 NALQSAV-WTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMArwDRETALELIEK---YKVTFWTNIPTMLVDL 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 280 LAAPGLPTREQVSLRLCSSAGEALPADLGERFTAHFGCEIIDGIGSTEMLHIFLSNRPGQVRYGTTGwpVPGYAVELR-- 357
Cdd:cd05935 188 LATPEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTETMSQTHTNPPLRPKLQCLG--IP*FGVDARvi 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 358 -DEDGHAVPDGDVGDLYIQGPSAALMYWGNREKSRETFrggWTKSGDKYVR-------NADGSYSYAGRSDDMLKVSGIY 429
Cdd:cd05935 266 dIETGRELPPNEVGEIVVRGPQIFKGYWNRPEETEESF---IEIKGRRFFRtgdlgymDEEGYFFFVDRVKRMINVSGFK 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 430 VSPFEVEATLAQHPAILEAAVIGVPDQAGLTKTKAFVVLKPG--AQVSETELKAFVKERLAPYKYPRIIEFMDALPKTAT 507
Cdd:cd05935 343 VWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEyrGKVTEEDIIEWAREQMAAYKYPREVEFVDELPRSAS 422
|
....*
gi 1920939256 508 GKIQR 512
Cdd:cd05935 423 GKILW 427
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
14-519 |
5.21e-74 |
|
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: 243.91 E-value: 5.21e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 14 FNFAQHLIACNAQ------RPGKTA--YIDDHGT-MRYG--ELAERIRRVAGAL-QASGIHREERVLLLMHDGNDWPVCF 81
Cdd:cd05928 5 FNFASDVLDQWADkekagkRPPNPAlwWVNGKGDeVKWSfrELGSLSRKAANVLsGACGLQRGDRVAVILPRVPEWWLVN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 82 LGAMYAGIVPVAVNTLLTADDYAYMLQHSRAQAVLVSGALLPVLRQAMAQGGHEAATVIVSRPAGplpDGMIALEAWIER 161
Cdd:cd05928 85 VACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSDELAPEVDSVASECPSLKTKLLVSEKSR---DGWLNFKELLNE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 162 NAPLAAPASTGPDDPGFWLYSSGSTGRPKGVLHSQGNPYWTAELYAKPVLSLGEADICFSAAKLYFAYGLGNALTFPLSV 241
Cdd:cd05928 162 ASTEHHCVETGSQEPMAIYFTSGTTGSPKMAEHSHSSLGLGLKVNGRYWLDLTASDIMWNTSDTGWIKSAWSSLFEPWIQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 242 GATV-VLMAERPTPEATFRRWLDYQPTVFFGAPTGYAgMLAAPGLPTREQVSLRLCSSAGEALPADLGERFTAHFGCEII 320
Cdd:cd05928 242 GACVfVHHLPRFDPLVILKTLSSYPITTFCGAPTVYR-MLVQQDLSSYKFPSLQHCVTGGEPLNPEVLEKWKAQTGLDIY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 321 DGIGSTEMLHIFLSNRPGQVRYGTTGWPVPGYAVELRDEDGHAVPDGDVGDLYIQ-GPSAAL----MYWGNREKSRETFR 395
Cdd:cd05928 321 EGYGQTETGLICANFKGMKIKPGSMGKASPPYDVQIIDDNGNVLPPGTEGDIGIRvKPIRPFglfsGYVDNPEKTAATIR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 396 GGWTKSGDKYVRNADGSYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQAGLTKTKAFVVLKPGAQVS 475
Cdd:cd05928 401 GDFYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLAPQFLSH 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1920939256 476 E-----TELKAFVKERLAPYKYPRIIEFMDALPKTATGKIQRFRLREME 519
Cdd:cd05928 481 DpeqltKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNELRDKE 529
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
42-519 |
7.87e-74 |
|
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: 240.87 E-value: 7.87e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 42 YGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLLTADDYAYMLQHSRAQAVLVSGAL 121
Cdd:cd05969 3 FAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 122 LpvlrqamaqggheaatvivsrpagplpdgmialeawiERnaplaapasTGPDDPGFWLYSSGSTGRPKGVLHSQgNPYW 201
Cdd:cd05969 83 Y-------------------------------------ER---------TDPEDPTLLHYTSGTTGTPKGVLHVH-DAMI 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 202 TAELYAKPVLSLGEADICFSAAKLYFAYGLGNALTFPLSVGATVVLMAERPTPEATFRRWLDYQPTVFFGAPTGYAGMLA 281
Cdd:cd05969 116 FYYFTGKYVLDLHPDDIYWCTADPGWVTGTVYGIWAPWLNGVTNVVYEGRFDAESWYGIIERVKVTVWYTAPTAIRMLMK 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 282 APGLPTR--EQVSLRLCSSAGEALPADLGERFTAHFGCEIIDGIGSTEMLHIFLSNRPGQ-VRYGTTGWPVPGYAVELRD 358
Cdd:cd05969 196 EGDELARkyDLSSLRFIHSVGEPLNPEAIRWGMEVFGVPIHDTWWQTETGSIMIANYPCMpIKPGSMGKPLPGVKAAVVD 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 359 EDGHAVPDGDVGDLYIQG--PSAALMYWGNREKSRETFRGGWTKSGDKYVRNADGSYSYAGRSDDMLKVSGIYVSPFEVE 436
Cdd:cd05969 276 ENGNELPPGTKGILALKPgwPSMFRGIWNDEERYKNSFIDGWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVE 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 437 ATLAQHPAILEAAVIGVPDQAGLTKTKAFVVLKPGAQVSE---TELKAFVKERLAPYKYPRIIEFMDALPKTATGKIQRF 513
Cdd:cd05969 356 SALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPSDelkEEIINFVRQKLGAHVAPREIEFVDNLPKTRSGKIMRR 435
|
....*.
gi 1920939256 514 RLREME 519
Cdd:cd05969 436 VLKAKE 441
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
30-516 |
1.50e-73 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 242.28 E-value: 1.50e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 30 KTAYI--DDHGTMR---YGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLLTADDYA 104
Cdd:PRK08008 23 KTALIfeSSGGVVRrysYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 105 YMLQHSRAQAVLVSGALLPVLRQAMAQGGHEAATVIVSRPAGPLPDGMIALEAWIERNAP---LAAPASTgpDDPGFWLY 181
Cdd:PRK08008 103 WILQNSQASLLVTSAQFYPMYRQIQQEDATPLRHICLTRVALPADDGVSSFTQLKAQQPAtlcYAPPLST--DDTAEILF 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 182 SSGSTGRPKGVLHSQGNPYWtAELYAKPVLSLGEADICFSAAKLYFAYGLGNALTFPLSVGATVVLMaERPTPEATFRRW 261
Cdd:PRK08008 181 TSGTTSRPKGVVITHYNLRF-AGYYSAWQCALRDDDVYLTVMPAFHIDCQCTAAMAAFSAGATFVLL-EKYSARAFWGQV 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 262 LDYQPTVFFGAPTGYAGMLAAPGLPTREQVSLR-----LCSSAGEAlpadlgERFTAHFGCEIIDGIGSTEMLHIFLSNR 336
Cdd:PRK08008 259 CKYRATITECIPMMIRTLMVQPPSANDRQHCLRevmfyLNLSDQEK------DAFEERFGVRLLTSYGMTETIVGIIGDR 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 337 PGQVR-YGTTGWPVPGYAVELRDEDGHAVPDGDVGDLYIQG-PSAALM--YWGNREKSRETFRG-GWTKSGDKYVRNADG 411
Cdd:PRK08008 333 PGDKRrWPSIGRPGFCYEAEIRDDHNRPLPAGEIGEICIKGvPGKTIFkeYYLDPKATAKVLEAdGWLHTGDTGYVDEEG 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 412 SYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQAGLTKTKAFVVLKPGAQVSETELKAFVKERLAPYK 491
Cdd:PRK08008 413 FFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEEEFFAFCEQNMAKFK 492
|
490 500
....*....|....*....|....*
gi 1920939256 492 YPRIIEFMDALPKTATGKIQRFRLR 516
Cdd:PRK08008 493 VPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
42-516 |
1.93e-73 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 246.48 E-value: 1.93e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 42 YGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLLTADDYAYMLQHSRAQAVLVSGAL 121
Cdd:PRK06060 33 HGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPALVVTSDAL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 122 lpvlrqamaQGGHEAATVIvsRPAGPLPDgmialeawiernAPLAAPASTGP---DDPGFWLYSSGSTGRPKGVLHSQGN 198
Cdd:PRK06060 113 ---------RDRFQPSRVA--EAAELMSE------------AARVAPGGYEPmggDALAYATYTSGTTGPPKAAIHRHAD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 199 PYWTAELYAKPVLSLGEADICFSAAKLYFAYGLGNALTFPLSVGATVVLMAERPTPEATFRRWLDYQPTVFFGAPTGYAG 278
Cdd:PRK06060 170 PLTFVDAMCRKALRLTPEDTGLCSARMYFAYGLGNSVWFPLATGGSAVINSAPVTPEAAAILSARFGPSVLYGVPNFFAR 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 279 MLAAPGLPTREqvSLRLCSSAGEALPADLGERFTAHF-GCEIIDGIGSTEMLHIFLSNRPGQVRYGTTGWPVPGYAVELR 357
Cdd:PRK06060 250 VIDSCSPDSFR--SLRCVVSAGEALELGLAERLMEFFgGIPILDGIGSTEVGQTFVSNRVDEWRLGTLGRVLPPYEIRVV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 358 DEDGHAVPDGDVGDLYIQGPSAALMYWgNREKSRETfRGGWTKSGDKYVRNADGSYSYAGRSDDMLKVSGIYVSPFEVEA 437
Cdd:PRK06060 328 APDGTTAGPGVEGDLWVRGPAIAKGYW-NRPDSPVA-NEGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVER 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 438 TLAQHPAILEAAVIGVPDQAGLTKTKAFVVLKPGAQVSETELKAFVKE---RLAPYKYPRIIEFMDALPKTATGKIQRFR 514
Cdd:PRK06060 406 LIIEDEAVAEAAVVAVRESTGASTLQAFLVATSGATIDGSVMRDLHRGllnRLSAFKVPHRFAVVDRLPRTPNGKLVRGA 485
|
..
gi 1920939256 515 LR 516
Cdd:PRK06060 486 LR 487
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
42-517 |
2.09e-73 |
|
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: 241.77 E-value: 2.09e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 42 YGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLLTADDYAYMLQHSRAQAVLVSGAL 121
Cdd:cd12119 28 YAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAEDRVVFVDRDF 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 122 LPVLRQAMAQGGH-EAATVIVSRPAGPLPDGM--IALEAWIERNAPLAAPASTGPDDPGFWLYSSGSTGRPKGVLHSQGN 198
Cdd:cd12119 108 LPLLEAIAPRLPTvEHVVVMTDDAAMPEPAGVgvLAYEELLAAESPEYDWPDFDENTAAAICYTSGTTGNPKGVVYSHRS 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 199 PYW-TAELYAKPVLSLGEADICFSAAKLYFAYGLGNALTFPLsVGATVVLMAERPTPEATFRRWLDYQPTVFFGAPTGYA 277
Cdd:cd12119 188 LVLhAMAALLTDGLGLSESDVVLPVVPMFHVNAWGLPYAAAM-VGAKLVLPGPYLDPASLAELIEREGVTFAAGVPTVWQ 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 278 GMLAAPGLPTREQVSLRLCSSAGEALPADLGERFTAHfGCEIIDGIGSTEMLHIFLSNRPG----------QVRY-GTTG 346
Cdd:cd12119 267 GLLDHLEANGRDLSSLRRVVIGGSAVPRSLIEAFEER-GVRVIHAWGMTETSPLGTVARPPsehsnlsedeQLALrAKQG 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 347 WPVPGYAVELRDEDGHAVP-DGD-VGDLYIQGPSAALMYWGNREKSRETFRGGWTKSGDKYVRNADGSYSYAGRSDDMLK 424
Cdd:cd12119 346 RPVPGVELRIVDDDGRELPwDGKaVGELQVRGPWVTKSYYKNDEESEALTEDGWLRTGDVATIDEDGYLTITDRSKDVIK 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 425 VSGIYVSPFEVEATLAQHPAILEAAVIGVPDQAGLTKTKAFVVLKPGAQVSETELKAFVKERLAPYKYPRIIEFMDALPK 504
Cdd:cd12119 426 SGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLKEGATVTAEELLEFLADKVAKWWLPDDVVFVDEIPK 505
|
490
....*....|...
gi 1920939256 505 TATGKIQRFRLRE 517
Cdd:cd12119 506 TSTGKIDKKALRE 518
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
25-512 |
2.14e-72 |
|
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: 238.67 E-value: 2.14e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 25 AQRPGKTAYID-DHG-TMRYGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLLTADD 102
Cdd:cd05904 16 SAHPSRPALIDaATGrALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 103 YAYMLQHSRAQAVLVSGALLPVLRQAmaqggheAATVIV--SRPAGPLPDGMIALEAwierNAPLAAPASTGPDDPGFWL 180
Cdd:cd05904 96 IAKQVKDSGAKLAFTTAELAEKLASL-------ALPVVLldSAEFDSLSFSDLLFEA----DEAEPPVVVIKQDDVAALL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 181 YSSGSTGRPKGVLHSQGNPYWTAELYAKPVLSLGEADICFSAAKLYF-AYGLGNALTFPLSVGATVVLMAERPTPEAtFR 259
Cdd:cd05904 165 YSSGTTGRSKGVMLTHRNLIAMVAQFVAGEGSNSDSEDVFLCVLPMFhIYGLSSFALGLLRLGATVVVMPRFDLEEL-LA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 260 RWLDYQPTVFFGAPTGYAGMLAAPGLPTREQVSLRLCSSAGEALPADLGERFTAHF-GCEIIDGIGSTE---MLHIFLSN 335
Cdd:cd05904 244 AIERYKVTHLPVVPPIVLALVKSPIVDKYDLSSLRQIMSGAAPLGKELIEAFRAKFpNVDLGQGYGMTEstgVVAMCFAP 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 336 RPGQVRYGTTGWPVPGYAVELRD-EDGHAVPDGDVGDLYIQGPSAALMYWGNREKSRETFRG-GWTKSGDKYVRNADGSY 413
Cdd:cd05904 324 EKDRAKYGSVGRLVPNVEAKIVDpETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDKeGWLHTGDLCYIDEDGYL 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 414 SYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQAGLTKTKAFVVLKPGAQVSETELKAFVKERLAPYKYP 493
Cdd:cd05904 404 FIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKPGSSLTEDEIMDFVAKQVAPYKKV 483
|
490
....*....|....*....
gi 1920939256 494 RIIEFMDALPKTATGKIQR 512
Cdd:cd05904 484 RKVAFVDAIPKSPSGKILR 502
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
28-515 |
4.29e-72 |
|
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: 236.27 E-value: 4.29e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 28 PGKTAYIDDHGTMRYGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLLTADDYAYML 107
Cdd:cd05930 1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 108 QHSRAQAVLvsgallpvlrqamaqggheaatvivsrpagplpdgmialeawiernaplaapasTGPDDPGFWLYSSGSTG 187
Cdd:cd05930 81 EDSGAKLVL------------------------------------------------------TDPDDLAYVIYTSGSTG 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 188 RPKGVLHSQGNP----YWTAELYAkpvlsLGEADICFSAAKLYFAYGLGNALTfPLSVGATVVLMAE--RPTPEATFRRW 261
Cdd:cd05930 107 KPKGVMVEHRGLvnllLWMQEAYP-----LTPGDRVLQFTSFSFDVSVWEIFG-ALLAGATLVVLPEevRKDPEALADLL 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 262 LDYQPTVFFGAPTGYAGMLAAPGLPTREqvSLRLCSSAGEALPADLGERFTAHF-GCEIIDGIGSTE--MLHIFLSNRPG 338
Cdd:cd05930 181 AEEGITVLHLTPSLLRLLLQELELAALP--SLRLVLVGGEALPPDLVRRWRELLpGARLVNLYGPTEatVDATYYRVPPD 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 339 QVRYGTT--GWPVPGYAVELRDEDGHAVPDGDVGDLYIQGPSAALMYWGNREKSRETFR----GGWT---KSGDKYVRNA 409
Cdd:cd05930 259 DEEDGRVpiGRPIPNTRVYVLDENLRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVpnpfGPGErmyRTGDLVRWLP 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 410 DGSYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQAGLTKTKAFVVLKPGAQVSETELKAFVKERLAP 489
Cdd:cd05930 339 DGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEGGELDEEELRAHLAERLPD 418
|
490 500
....*....|....*....|....*.
gi 1920939256 490 YKYPRIIEFMDALPKTATGKIQRFRL 515
Cdd:cd05930 419 YMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
10-519 |
1.43e-71 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 238.26 E-value: 1.43e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 10 PGTPFNFAQHLI--ACNAQRPGKTA--YIDDHG--TMRYGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLG 83
Cdd:PRK04319 38 ETGKVNIAYEAIdrHADGGRKDKVAlrYLDASRkeKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 84 AMYAGIVpvaVNTLLTAddyaYM-------LQHSRAQAVLVSGALLpvlRQAMAQGGHEAATVIVSRPAGPLPDGMIALE 156
Cdd:PRK04319 118 ALKNGAI---VGPLFEA----FMeeavrdrLEDSEAKVLITTPALL---ERKPADDLPSLKHVLLVGEDVEEGPGTLDFN 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 157 AWIERNAPLAAPASTGPDDPGFWLYSSGSTGRPKGVLHSQG---NPYWTAelyaKPVLSLGEADICFSAAKLYFAYGLGN 233
Cdd:PRK04319 188 ALMEQASDEFDIEWTDREDGAILHYTSGSTGKPKGVLHVHNamlQHYQTG----KYVLDLHEDDVYWCTADPGWVTGTSY 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 234 ALTFPLSVGATVVLMAERPTPEATFRRWLDYQPTVFFGAPTGYAgML--AAPGLPTREQVS-LRLCSSAGEALPADL--- 307
Cdd:PRK04319 264 GIFAPWLNGATNVIDGGRFSPERWYRILEDYKVTVWYTAPTAIR-MLmgAGDDLVKKYDLSsLRHILSVGEPLNPEVvrw 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 308 GERFtahFGCEIIDGIGSTEMLHIFLSNRPGQ-VRYGTTGWPVPGYAVELRDEDGHAVPDGDVGDLYIQGPSAALM--YW 384
Cdd:PRK04319 343 GMKV---FGLPIHDNWWMTETGGIMIANYPAMdIKPGSMGKPLPGIEAAIVDDQGNELPPNRMGNLAIKKGWPSMMrgIW 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 385 GNREKSRETFRGGWTKSGDKYVRNADGSYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQAGLTKTKA 464
Cdd:PRK04319 420 NNPEKYESYFAGDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVRGEIIKA 499
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1920939256 465 FVVLKPGAQVSET---ELKAFVKERLAPYKYPRIIEFMDALPKTATGKIQRFRLREME 519
Cdd:PRK04319 500 FVALRPGYEPSEElkeEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKIMRRVLKAWE 557
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
20-519 |
3.32e-69 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 231.74 E-value: 3.32e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 20 LIACNAQR-PGKTAYIDDHGTMRYGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLL 98
Cdd:PRK07788 54 LVAHAARRaPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGF 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 99 TADDYAYMLQHSRAQAVLVSGALLPVLRQAMAQGGHEAATVIVSRPAGPLPDGMIALEAWIERNAPLAAPASTGPDdpGF 178
Cdd:PRK07788 134 SGPQLAEVAAREGVKALVYDDEFTDLLSALPPDLGRLRAWGGNPDDDEPSGSTDETLDDLIAGSSTAPLPKPPKPG--GI 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 179 WLYSSGSTGRPKGVLHSQGNPYWT-AELYAKPVLSLGEADICfsAAKLYFAYGLGNaLTFPLSVGATVVLMaERPTPEAT 257
Cdd:PRK07788 212 VILTSGTTGTPKGAPRPEPSPLAPlAGLLSRVPFRAGETTLL--PAPMFHATGWAH-LTLAMALGSTVVLR-RRFDPEAT 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 258 FRRWLDYQPTVFFGAPTGYAGMLAAPG--LPTREQVSLRLCSSAGEALPADLGERFTAHFGCEIIDGIGSTEmLHIFLSN 335
Cdd:PRK07788 288 LEDIAKHKATALVVVPVMLSRILDLGPevLAKYDTSSLKIIFVSGSALSPELATRALEAFGPVLYNLYGSTE-VAFATIA 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 336 RPGQVRY--GTTGWPVPGYAVELRDEDGHAVPDGDVGDLYIQGPSAALMYWGNREKSREtfrGGWTKSGDKYVRNADGSY 413
Cdd:PRK07788 367 TPEDLAEapGTVGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFPFEGYTDGRDKQII---DGLLSSGDVGYFDEDGLL 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 414 SYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQAGLTKTKAFVVLKPGAQVSETELKAFVKERLAPYKYP 493
Cdd:PRK07788 444 FVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKAPGAALDEDAIKDYVRDNLARYKVP 523
|
490 500
....*....|....*....|....*.
gi 1920939256 494 RIIEFMDALPKTATGKIQRFRLREME 519
Cdd:PRK07788 524 RDVVFLDELPRNPTGKVLKRELREMD 549
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
28-515 |
9.93e-67 |
|
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: 222.94 E-value: 9.93e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 28 PGKTAYIDDHGTMRYGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLLTADDYAYML 107
Cdd:cd12116 1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 108 QHSRAQAVLVSGALlpvlrqamaqggheaatvivsRPAGPLPDGMIALEAWIERNAPLAAPASTGPDDPGFWLYSSGSTG 187
Cdd:cd12116 81 EDAEPALVLTDDAL---------------------PDRLPAGLPVLLLALAAAAAAPAAPRTPVSPDDLAYVIYTSGSTG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 188 RPKGVLHSQGNPYWTAELYAKpVLSLGEAD-------ICFSAAKLyfayglgnALTFPLSVGATVVlMAERPT---PEAT 257
Cdd:cd12116 140 RPKGVVVSHRNLVNFLHSMRE-RLGLGPGDrllavttYAFDISLL--------ELLLPLLAGARVV-IAPRETqrdPEAL 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 258 FRRWLDYQPTVFFGAPTGYAgMLAAPGLPTREQVSLrLCssAGEALPADLGERFTAHfGCEIIDGIGSTE------MLHI 331
Cdd:cd12116 210 ARLIEAHSITVMQATPATWR-MLLDAGWQGRAGLTA-LC--GGEALPPDLAARLLSR-VGSLWNLYGPTEttiwstAARV 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 332 FLSNRPGQVrygttGWPVPGYAVELRDEDGHAVPDGDVGDLYIQGPSAALMYWGNREKSRETFR--------GGWTKSGD 403
Cdd:cd12116 285 TAAAGPIPI-----GRPLANTQVYVLDAALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVpdpfagpgSRLYRTGD 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 404 KYVRNADGSYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQaGLTKTKAFVVLKPGAQVSETELKAFV 483
Cdd:cd12116 360 LVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDG-GDRRLVAYVVLKAGAAPDAAALRAHL 438
|
490 500 510
....*....|....*....|....*....|..
gi 1920939256 484 KERLAPYKYPRIIEFMDALPKTATGKIQRFRL 515
Cdd:cd12116 439 RATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
25-516 |
3.16e-66 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 223.74 E-value: 3.16e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 25 AQRPGKTAYIDDHGTMRYGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLLTADDYA 104
Cdd:PRK07059 34 RQYADRPAFICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVNPLYTPRELE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 105 YMLQHSRAQAVLVSGALLPVLRQAMAqggHEAATVIVSRPAGPL--PDGMIA----------LEAW-----IERNAPLAA 167
Cdd:PRK07059 114 HQLKDSGAEAIVVLENFATTVQQVLA---KTAVKHVVVASMGDLlgFKGHIVnfvvrrvkkmVPAWslpghVRFNDALAE 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 168 -------PASTGPDDPGFWLYSSGSTGRPKG--VLHSQ------GNPYWTAELYAKPvlslGEAD----ICfsAAKLYFA 228
Cdd:PRK07059 191 garqtfkPVKLGPDDVAFLQYTGGTTGVSKGatLLHRNivanvlQMEAWLQPAFEKK----PRPDqlnfVC--ALPLYHI 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 229 YGLGNALTFPLSVGATVVLMAErPTPEATFRRWLD-YQPTVFFGAPTGYAGMLAAPGLPTREQVSLRLCSSAGEALPADL 307
Cdd:PRK07059 265 FALTVCGLLGMRTGGRNILIPN-PRDIPGFIKELKkYQVHIFPAVNTLYNALLNNPDFDKLDFSKLIVANGGGMAVQRPV 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 308 GERFTAHFGCEIIDGIGSTEMLHIFLSNRPGQVRY-GTTGWPVPGYAVELRDEDGHAVPDGDVGDLYIQGPSAALMYWgN 386
Cdd:PRK07059 344 AERWLEMTGCPITEGYGLSETSPVATCNPVDATEFsGTIGLPLPSTEVSIRDDDGNDLPLGEPGEICIRGPQVMAGYW-N 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 387 R--EKSRETFRGGWTKSGDKYVRNADGSYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQAGLTKTKA 464
Cdd:PRK07059 423 RpdETAKVMTADGFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGEAVKL 502
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1920939256 465 FVVLKPGAqVSETELKAFVKERLAPYKYPRIIEFMDALPKTATGKIQRFRLR 516
Cdd:PRK07059 503 FVVKKDPA-LTEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRRELR 553
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
17-518 |
3.40e-66 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 223.88 E-value: 3.40e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 17 AQHLIACNAQRPGKTAYIDDHGTMRYG--ELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAV 94
Cdd:PRK12583 21 GDAFDATVARFPDREALVVRHQALRYTwrQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 95 NTLLTADDYAYMLQHSRAQAVLVS------------GALLPVLrqAMAQGGHEAATVI-----VSRPAGPLPDGMIALEA 157
Cdd:PRK12583 101 NPAYRASELEYALGQSGVRWVICAdafktsdyhamlQELLPGL--AEGQPGALACERLpelrgVVSLAPAPPPGFLAWHE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 158 W------IERNAPLAAPASTGPDDPGFWLYSSGSTGRPKGVLHSQ----GNPYWTAElyakpVLSLGEADICFSAAKLYF 227
Cdd:PRK12583 179 LqargetVSREALAERQASLDRDDPINIQYTSGTTGFPKGATLSHhnilNNGYFVAE-----SLGLTEHDRLCVPVPLYH 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 228 AYGLGNALTFPLSVGATVVLMAERPTPEATFRRWLDYQPTVFFGAPTGYAGMLAAPGLPTREQVSLRLCSSAGEALPADL 307
Cdd:PRK12583 254 CFGMVLANLGCMTVGACLVYPNEAFDPLATLQAVEEERCTALYGVPTMFIAELDHPQRGNFDLSSLRTGIMAGAPCPIEV 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 308 GERFTAHFGC-EIIDGIGSTE---MLHIFLSNRPGQVRYGTTGWPVPGYAVELRDEDGHAVPDGDVGDLYIQGPSAALMY 383
Cdd:PRK12583 334 MRRVMDEMHMaEVQIAYGMTEtspVSLQTTAADDLERRVETVGRTQPHLEVKVVDPDGATVPRGEIGELCTRGYSVMKGY 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 384 WGNREKSRETF-RGGWTKSGDKYVRNADGSYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQAGLTKT 462
Cdd:PRK12583 414 WNNPEATAESIdEDGWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEI 493
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1920939256 463 KAFVVLKPGAQVSETELKAFVKERLAPYKYPRIIEFMDALPKTATGKIQRFRLREM 518
Cdd:PRK12583 494 VAWVRLHPGHAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMREI 549
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
16-518 |
2.74e-65 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 221.08 E-value: 2.74e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 16 FAQHLIACNAQRPGKTAYID---DHGTMR---YGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGI 89
Cdd:PRK13295 26 INDDLDACVASCPDKTAVTAvrlGTGAPRrftYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 90 VPVAVNTLLTADDYAYMLQHSRAQAVLVSGALLPVLRQAMAQGGHEAA----TVIVSRPAGPLP-DGMIALEAWIER--- 161
Cdd:PRK13295 106 VLNPLMPIFRERELSFMLKHAESKVLVVPKTFRGFDHAAMARRLRPELpalrHVVVVGGDGADSfEALLITPAWEQEpda 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 162 NAPLAAPAsTGPDDPGFWLYSSGSTGRPKGVLHSqGNPYWTAEL-YAKPvLSLGEADICFSAAKLYFAYGLGNALTFPLS 240
Cdd:PRK13295 186 PAILARLR-PGPDDVTQLIYTSGTTGEPKGVMHT-ANTLMANIVpYAER-LGLGADDVILMASPMAHQTGFMYGLMMPVM 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 241 VGATVVLMaERPTPEATFRRWLDYQPTVFFGAPTGYAGMLAAPGLPTREQVSLRLCSSAGEALPADLGERFTAHFGCEII 320
Cdd:PRK13295 263 LGATAVLQ-DIWDPARAAELIRTEGVTFTMASTPFLTDLTRAVKESGRPVSSLRTFLCAGAPIPGALVERARAALGAKIV 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 321 DGIGSTE--MLHIFLSNRPGQVRYGTTGWPVPGYAVELRDEDGHAVPDGDVGDLYIQGPSAALMYWGnREKSRETFRGGW 398
Cdd:PRK13295 342 SAWGMTEngAVTLTKLDDPDERASTTDGCPLPGVEVRVVDADGAPLPAGQIGRLQVRGCSNFGGYLK-RPQLNGTDADGW 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 399 TKSGDKYVRNADGSYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQAGLTKTKAFVVLKPGAQVSETE 478
Cdd:PRK13295 421 FDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPRPGQSLDFEE 500
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1920939256 479 LKAFVKE-RLAPYKYPRIIEFMDALPKTATGKIQRFRLREM 518
Cdd:PRK13295 501 MVEFLKAqKVAKQYIPERLVVRDALPRTPSGKIQKFRLREM 541
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
27-518 |
1.18e-64 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 218.19 E-value: 1.18e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 27 RPGKTAYIDDHGTMRYGELAERIRRVAGALQAS-GIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLLTADDYAY 105
Cdd:PRK06839 15 HPDRIAIITEEEEMTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 106 MLQHSRAQAVLVSGALLPVLRQAMAQGGHEAATVIVSrPAGPLPDGMIALEawiernaplaapaSTGPDDPGFWLYSSGS 185
Cdd:PRK06839 95 QLKDSGTTVLFVEKTFQNMALSMQKVSYVQRVISITS-LKEIEDRKIDNFV-------------EKNESASFIICYTSGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 186 TGRPKGVLHSQGNPYWTAeLYAKPVLSLGEADICFSAAKLYFAYGLGnALTFPLSVGATVVLMAERPTPEATFRRWLDYQ 265
Cdd:PRK06839 161 TGKPKGAVLTQENMFWNA-LNNTFAIDLTMHDRSIVLLPLFHIGGIG-LFAFPTLFAGGVIIVPRKFEPTKALSMIEKHK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 266 PTVFFGAPTGYAGMLAAPGLPTREQVSLRLCSSAGEALPADLGERFTAHfGCEIIDGIGSTEML-HIF-LSNRPGQVRYG 343
Cdd:PRK06839 239 VTVVMGVPTIHQALINCSKFETTNLQSVRWFYNGGAPCPEELMREFIDR-GFLFGQGFGMTETSpTVFmLSEEDARRKVG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 344 TTGWPVPGYAVELRDEDGHAVPDGDVGDLYIQGPSAALMYWGNREKSRETFRGGWTKSGDKYVRNADGSYSYAGRSDDML 423
Cdd:PRK06839 318 SIGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEETIQDGWLCTGDLARVDEDGFVYIVGRKKEMI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 424 KVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQAGLTKTKAFVVLKPGAQVSETELKAFVKERLAPYKYPRIIEFMDALP 503
Cdd:PRK06839 398 ISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVLIEKDVIEHCRLFLAKYKIPKEIVFLKELP 477
|
490
....*....|....*
gi 1920939256 504 KTATGKIQRFRLREM 518
Cdd:PRK06839 478 KNATGKIQKAQLVNQ 492
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
39-510 |
1.19e-64 |
|
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: 220.53 E-value: 1.19e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 39 TMRYGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFL-----GA----MYAGIVPVAVNT---------LLTA 100
Cdd:cd17634 84 TISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLacariGAvhsvIFGGFAPEAVAGriidsssrlLITA 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 101 DDYaymLQHSRaqavlvSGALLPVLRQAMAQGGHEAATVIVSRPAGPLPDGMIALEAW----IERNAPLAAPASTGPDDP 176
Cdd:cd17634 164 DGG---VRAGR------SVPLKKNVDDALNPNVTSVEHVIVLKRTGSDIDWQEGRDLWwrdlIAKASPEHQPEAMNAEDP 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 177 GFWLYSSGSTGRPKGVLHSQGNPYWTAELYAKPVLSLGEADICFSAAKLYFAYGLGNALTFPLSVGATVVL---MAERPT 253
Cdd:cd17634 235 LFILYTSGTTGKPKGVLHTTGGYLVYAATTMKYVFDYGPGDIYWCTADVGWVTGHSYLLYGPLACGATTLLyegVPNWPT 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 254 PEATFRRWLDYQPTVFFGAPTGYAGMLAA--PGLPTREQVSLRLCSSAGEALPADLGERFTAHFG---CEIIDGIGSTEM 328
Cdd:cd17634 315 PARMWQVVDKHGVNILYTAPTAIRALMAAgdDAIEGTDRSSLRILGSVGEPINPEAYEWYWKKIGkekCPVVDTWWQTET 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 329 LHIFLSNRPG--QVRYGTTGWPVPGYAVELRDEDGHAVPDGDVGDLYIQG--PSAALMYWGNREKSRET----FRGGWTk 400
Cdd:cd17634 395 GGFMITPLPGaiELKAGSATRPVFGVQPAVVDNEGHPQPGGTEGNLVITDpwPGQTRTLFGDHERFEQTyfstFKGMYF- 473
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 401 SGDKYVRNADGSYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQAGLTKTKAFVVLKPGAQVSET--- 477
Cdd:cd17634 474 SGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLNHGVEPSPElya 553
|
490 500 510
....*....|....*....|....*....|...
gi 1920939256 478 ELKAFVKERLAPYKYPRIIEFMDALPKTATGKI 510
Cdd:cd17634 554 ELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
39-523 |
2.60e-63 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 216.17 E-value: 2.60e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 39 TMRYGELAERIRRVAGALQA-SGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLLTADDYAYMLQHSRAQA--- 114
Cdd:PRK05677 49 TLTYGELYKLSGAFAAWLQQhTDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVNTNPLYTAREMEHQFNDSGAKAlvc 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 115 -------------------VLVS--GALLPVLRQAMAQggheAATVIVSR--PAGPLPDGMIALEAWIERNAPLAAPAST 171
Cdd:PRK05677 129 lanmahlaekvlpktgvkhVIVTevADMLPPLKRLLIN----AVVKHVKKmvPAYHLPQAVKFNDALAKGAGQPVTEANP 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 172 GPDDPGFWLYSSGSTGRPKGVLHSQGNpYWTAELYAKPVLS--LGEA-DICFSAAKLYFAYGLGNALTFPLSVGATVVLM 248
Cdd:PRK05677 205 QADDVAVLQYTGGTTGVAKGAMLTHRN-LVANMLQCRALMGsnLNEGcEILIAPLPLYHIYAFTFHCMAMMLIGNHNILI 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 249 AERPTPEATFRRWLDYQPTVFFGAPTGYAGMLAAPGLPTREQVSLRLCSSAGEALPADLGERFTAHFGCEIIDGIGSTEM 328
Cdd:PRK05677 284 SNPRDLPAMVKELGKWKFSGFVGLNTLFVALCNNEAFRKLDFSALKLTLSGGMALQLATAERWKEVTGCAICEGYGMTET 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 329 LHIFLSNRPGQVRYGTTGWPVPGYAVELRDEDGHAVPDGDVGDLYIQGPSAALMYWGNREKSRETFRG-GWTKSGDKYVR 407
Cdd:PRK05677 364 SPVVSVNPSQAIQVGTIGIPVPSTLCKVIDDDGNELPLGEVGELCVKGPQVMKGYWQRPEATDEILDSdGWLKTGDIALI 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 408 NADGSYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQAGLTKTKAFVVLKPGAQVSETELKAFVKERL 487
Cdd:PRK05677 444 QEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIKVFVVVKPGETLTKEQVMEHMRANL 523
|
490 500 510
....*....|....*....|....*....|....*.
gi 1920939256 488 APYKYPRIIEFMDALPKTATGKIQRFRLREMEGAPA 523
Cdd:PRK05677 524 TGYKVPKAVEFRDELPTTNVGKILRRELRDEELKKA 559
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
42-519 |
2.85e-63 |
|
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: 212.81 E-value: 2.85e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 42 YGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLLTADDyaymlqhsraqavlvsgal 121
Cdd:cd05974 3 FAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDD------------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 122 lpvLRQAMAQGGHEAAtvivsrpagplpdgmialeawiernaplAAPASTGPDDPGFWLYSSGSTGRPKGVLHSQGNpYW 201
Cdd:cd05974 64 ---LRDRVDRGGAVYA----------------------------AVDENTHADDPMLLYFTSGTTSKPKLVEHTHRS-YP 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 202 TAELYAKPVLSLGEADICFSAAKLYFAYGLGNALTFPLSVGATVVLMAE-RPTPEATFRRWLDYQPTVFFGAPTGYAGML 280
Cdd:cd05974 112 VGHLSTMYWIGLKPGDVHWNISSPGWAKHAWSCFFAPWNAGATVFLFNYaRFDAKRVLAALVRYGVTTLCAPPTVWRMLI 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 281 AAPglPTREQVSLRLCSSAGEALPADLGERFTAHFGCEIIDGIGSTEMLhIFLSNRPGQ-VRYGTTGWPVPGYAVELRDE 359
Cdd:cd05974 192 QQD--LASFDVKLREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETT-ALVGNSPGQpVKAGSMGRPLPGYRVALLDP 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 360 DGHAVPDGDVG-DLYIQGPsAALM--YWGNREKSRETFRGGWTKSGDKYVRNADGSYSYAGRSDDMLKVSGIYVSPFEVE 436
Cdd:cd05974 269 DGAPATEGEVAlDLGDTRP-VGLMkgYAGDPDKTAHAMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELE 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 437 ATLAQHPAILEAAVIGVPDQAGLTKTKAFVVLKPGAQVS-ETELKAF--VKERLAPYKYPRIIEFMDaLPKTATGKIQRF 513
Cdd:cd05974 348 SVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGYEPSpETALEIFrfSRERLAPYKRIRRLEFAE-LPKTISGKIRRV 426
|
....*.
gi 1920939256 514 RLREME 519
Cdd:cd05974 427 ELRRRE 432
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
13-518 |
6.78e-63 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 214.61 E-value: 6.78e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 13 PFNFAQHLIACNAQRPGKTAYIDDHGTMRYGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPV 92
Cdd:PRK06164 9 ADTLASLLDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 93 AVNTLLTADDYAYMLQHSRAQAVLVSGA----------------LLPVLRQAMAQGGHEAATvivsrpAGPLPDGMIALE 156
Cdd:PRK06164 89 AVNTRYRSHEVAHILGRGRARWLVVWPGfkgidfaailaavppdALPPLRAIAVVDDAADAT------PAPAPGARVQLF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 157 AWIERNAPLAAPASTGPDDPGFWLY-SSGSTGRPKGVLHSQGNPYWTAELYAKpVLSLGEADICFSAAKLYFAYGLGNAL 235
Cdd:PRK06164 163 ALPDPAPPAAAGERAADPDAGALLFtTSGTTSGPKLVLHRQATLLRHARAIAR-AYGYDPGAVLLAALPFCGVFGFSTLL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 236 TFpLSVGATVVLMAERPTPeATFRRWLDYQPTVFFGAPTGYAGMLAAPGLPtREQVSLRLCSSAgEALPA--DLGERFTA 313
Cdd:PRK06164 242 GA-LAGGAPLVCEPVFDAA-RTARALRRHRVTHTFGNDEMLRRILDTAGER-ADFPSARLFGFA-SFAPAlgELAALARA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 314 HfGCEIIDGIGSTEMLHIFLSNR---PGQVRYGTTGWPV-PGYAVELRD-EDGHAVPDGDVGDLYIQGPSAALMYWGNRE 388
Cdd:PRK06164 318 R-GVPLTGLYGSSEVQALVALQPatdPVSVRIEGGGRPAsPEARVRARDpQDGALLPDGESGEIEIRAPSLMRGYLDNPD 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 389 KSRETFRG-GWTKSGDKYVRNADGSYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVpDQAGLTKTKAFVV 467
Cdd:PRK06164 397 ATARALTDdGYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGA-TRDGKTVPVAFVI 475
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1920939256 468 LKPGAQVSETELKAFVKERLAPYKYPRIIEFMDALPKTATG---KIQRFRLREM 518
Cdd:PRK06164 476 PTDGASPDEAGLMAACREALAGFKVPARVQVVEAFPVTESAngaKIQKHRLREM 529
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
1-522 |
8.32e-63 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 214.26 E-value: 8.32e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 1 MTAEPQVQPPGTPFNFAQHLIACNAQ-RPGKTAYIDDHGTMRYGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPV 79
Cdd:PRK07786 3 ALTLAQEQPYLARRQNWVNQLARHALmQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 80 CFLGAMYAGIVPVAVNTLLTADDYAYMLQHSRAQAVLVSGALLPVLrQAMAQGGHEAATVIVSrpAGPLPDGMIALEAWI 159
Cdd:PRK07786 83 SVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAHVVVTEAALAPVA-TAVRDIVPLLSTVVVA--GGSSDDSVLGYEDLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 160 ERNAPLAAPASTGPDDPGFWLYSSGSTGRPKGVLHSQGNPYWTAELYAKPVLSLGEADICFSAAKLYFAYGLGNALTFpL 239
Cdd:PRK07786 160 AEAGPAHAPVDIPNDSPALIMYTSGTTGRPKGAVLTHANLTGQAMTCLRTNGADINSDVGFVGVPLFHIAGIGSMLPG-L 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 240 SVGATVVLmaeRPT----PEATFRRWLDYQPTVFFGAPTGYAGMLAAPGLPTREqVSLRLCS-SAGEALPADLGERFTAH 314
Cdd:PRK07786 239 LLGAPTVI---YPLgafdPGQLLDVLEAEKVTGIFLVPAQWQAVCAEQQARPRD-LALRVLSwGAAPASDTLLRQMAATF 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 315 FGCEIIDGIGSTEMLHI--FLSNRPGQVRYGTTGWPVPGYAVELRDEDGHAVPDGDVGDLYIQGPSAALMYWGNREKSRE 392
Cdd:PRK07786 315 PEAQILAAFGQTEMSPVtcMLLGEDAIRKLGSVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 393 TFRGGWTKSGDkYVRNADGSYSYA-GRSDDMLkVSG---IYVSpfEVEATLAQHPAILEAAVIGVPDQAGLTKTKAFVVL 468
Cdd:PRK07786 395 AFAGGWFHSGD-LVRQDEEGYVWVvDRKKDMI-ISGgenIYCA--EVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAV 470
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1920939256 469 KPG-AQVSETELKAFVKERLAPYKYPRIIEFMDALPKTATGKIQRFRLREMEGAP 522
Cdd:PRK07786 471 RNDdAALTLEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKVLKTELRERYGAC 525
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
25-517 |
2.09e-62 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 212.92 E-value: 2.09e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 25 AQRPGKTAYIDDHGTMRYGELAERIRRVAGALQASGIHREERVLLLMhdGNDWPVCFLG--AMYAGIVPVAVNTLLTADD 102
Cdd:PRK06188 23 KRYPDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLS--LNRPEVLMAIgaAQLAGLRRTALHPLGSLDD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 103 YAYMLQHSRAQAVLVSGALLPVLRQAMAQGgheAATVIVSRPAGPLPDGM-IALEAWIERNAPLAAPAstGPDDPGFWLY 181
Cdd:PRK06188 101 HAYVLEDAGISTLIVDPAPFVERALALLAR---VPSLKHVLTLGPVPDGVdLLAAAAKFGPAPLVAAA--LPPDIAGLAY 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 182 SSGSTGRPKGVLHSQGnpywtaELYAKPVLSLGE----ADICF-SAAKLYFAyglGNALTFP-LSVGATVVLMAERpTPE 255
Cdd:PRK06188 176 TGGTTGKPKGVMGTHR------SIATMAQIQLAEwewpADPRFlMCTPLSHA---GGAFFLPtLLRGGTVIVLAKF-DPA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 256 ATFRRWLDYQPTVFFGAPTGYAGMLAAPGLPTREQVSLRLCSSAGEAL-PADLGErftahfGCEIIDGI-----GSTE-- 327
Cdd:PRK06188 246 EVLRAIEEQRITATFLVPTMIYALLDHPDLRTRDLSSLETVYYGASPMsPVRLAE------AIERFGPIfaqyyGQTEap 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 328 MLHIFLSNR---PGQV-RYGTTGWPVPGYAVELRDEDGHAVPDGDVGDLYIQGPSAALMYWGNREKSRETFRGGWTKSGD 403
Cdd:PRK06188 320 MVITYLRKRdhdPDDPkRLTSCGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAFRDGWLHTGD 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 404 KYVRNADGSYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQAGLTKTKAFVVLKPGAQVSETELKAFV 483
Cdd:PRK06188 400 VAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRPGAAVDAAELQAHV 479
|
490 500 510
....*....|....*....|....*....|....
gi 1920939256 484 KERLAPYKYPRIIEFMDALPKTATGKIQRFRLRE 517
Cdd:PRK06188 480 KERKGSVHAPKQVDFVDSLPLTALGKPDKKALRA 513
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
25-518 |
3.97e-62 |
|
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: 212.31 E-value: 3.97e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 25 AQRPGKTAYIDDHGTMRYGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVntlLTADDYA 104
Cdd:COG1021 36 ERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAIPVFA---LPAHRRA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 105 ---YMLQHSRAQAVLVSGALLPVLRQAMA---QGGHEA-ATVIVSRPAGPlpdgMIALEAWIERNAPLAAPAsTGPDDPG 177
Cdd:COG1021 113 eisHFAEQSEAVAYIIPDRHRGFDYRALArelQAEVPSlRHVLVVGDAGE----FTSLDALLAAPADLSEPR-PDPDDVA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 178 FWLYSSGSTGRPKGV--LHsqgNPYW-TAELYakpvlslgeADIC-FSAAKLYFAyglgnALT----FPLS--------- 240
Cdd:COG1021 188 FFQLSGGTTGLPKLIprTH---DDYLySVRAS---------AEICgLDADTVYLA-----ALPaahnFPLSspgvlgvly 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 241 VGATVVlMAERPTPEATFRRWLDYQPTVFFGAPTGYAGMLAAPGLPTREQVSLRLCSSAGEALPADLGERFTAHFGCEII 320
Cdd:COG1021 251 AGGTVV-LAPDPSPDTAFPLIERERVTVTALVPPLALLWLDAAERSRYDLSSLRVLQVGGAKLSPELARRVRPALGCTLQ 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 321 DGIGSTEMLHIFlsNRPG---QVRYGTTGWPV-PGYAVELRDEDGHAVPDGDVGDLYIQGPSAALMYWGNREKSRETF-R 395
Cdd:COG1021 330 QVFGMAEGLVNY--TRLDdpeEVILTTQGRPIsPDDEVRIVDEDGNPVPPGEVGELLTRGPYTIRGYYRAPEHNARAFtP 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 396 GGWTKSGDKYVRNADGSYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQAGLTKTKAFVVLKpGAQVS 475
Cdd:COG1021 408 DGFYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGERSCAFVVPR-GEPLT 486
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1920939256 476 ETELKAFVKER-LAPYKYPRIIEFMDALPKTATGKIQRFRLREM 518
Cdd:COG1021 487 LAELRRFLRERgLAAFKLPDRLEFVDALPLTAVGKIDKKALRAA 530
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
42-519 |
6.20e-62 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 212.59 E-value: 6.20e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 42 YGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLLTADDYAYMLQHSRAQAVLVSGAL 121
Cdd:PRK06710 52 FSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILCLDLV 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 122 LPvlRQAMAQGGHEAATVIVSRPAG--PLPDGMI-------------------ALEAW--IERNAPLAAPASTGPD-DPG 177
Cdd:PRK06710 132 FP--RVTNVQSATKIEHVIVTRIADflPFPKNLLypfvqkkqsnlvvkvseseTIHLWnsVEKEVNTGVEVPCDPEnDLA 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 178 FWLYSSGSTGRPKGVLHSQGNPYWTAELYAKPVLSLGEAD-ICFSAAKLYFAYGLGNALTFPLSVGATVVLMAERPTpEA 256
Cdd:PRK06710 210 LLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLYNCKEGEeVVLGVLPFFHVYGMTAVMNLSIMQGYKMVLIPKFDM-KM 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 257 TFRRWLDYQPTVFFGAPTGYAGMLAAPGLPTREQVSLRLCSSAGEALPADLGERFTAHFGCEIIDGIGSTEMLHIFLSNR 336
Cdd:PRK06710 289 VFEAIKKHKVTLFPGAPTIYIALLNSPLLKEYDISSIRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTESSPVTHSNF 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 337 PGQVRY-GTTGWPVPGY-AVELRDEDGHAVPDGDVGDLYIQGPSAALMYWGNREKSRETFRGGWTKSGDKYVRNADGSYS 414
Cdd:PRK06710 369 LWEKRVpGSIGVPWPDTeAMIMSLETGEALPPGEIGEIVVKGPQIMKGYWNKPEETAAVLQDGWLHTGDVGYMDEDGFFY 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 415 YAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQAGLTKTKAFVVLKPGAQVSETELKAFVKERLAPYKYPR 494
Cdd:PRK06710 449 VKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVLKEGTECSEEELNQFARKYLAAYKVPK 528
|
490 500
....*....|....*....|....*
gi 1920939256 495 IIEFMDALPKTATGKIQRFRLREME 519
Cdd:PRK06710 529 VYEFRDELPKTTVGKILRRVLIEEE 553
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
16-512 |
2.59e-61 |
|
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: 209.12 E-value: 2.59e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 16 FAQHLiacnAQRPGKTAYIDDHGTMRYGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVN 95
Cdd:cd17651 1 FERQA----ARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 96 TLLTADDYAYMLQHSRAQAVLVSGALLPVLrqamaqggheaatvivsrpAGPLPDGMIALEAWIERNAPLAAPASTGPDD 175
Cdd:cd17651 77 PAYPAERLAFMLADAGPVLVLTHPALAGEL-------------------AVELVAVTLLDQPGAAAGADAEPDPALDADD 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 176 PGFWLYSSGSTGRPKGVLHSQGN----PYWTAELYAkpvlslgeadICFSAAKLYFAyglgnALTF---------PLSVG 242
Cdd:cd17651 138 LAYVIYTSGSTGRPKGVVMPHRSlanlVAWQARASS----------LGPGARTLQFA-----GLGFdvsvqeifsTLCAG 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 243 ATVVLMAE--RPTPEAtFRRWLDYQPTVFFGAPTGYAGMLAAPGLPT-REQVSLRLCSSAGEALP--ADLGERFTAHFGC 317
Cdd:cd17651 203 ATLVLPPEevRTDPPA-LAAWLDEQRISRVFLPTVALRALAEHGRPLgVRLAALRYLLTGGEQLVltEDLREFCAGLPGL 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 318 EIIDGIGSTEMlHIF----LSNRPGqvRYGTT---GWPVPGYAVELRDEDGHAVPDGDVGDLYIQGPSAALMYWGNREKS 390
Cdd:cd17651 282 RLHNHYGPTET-HVVtalsLPGDPA--AWPAPppiGRPIDNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELT 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 391 RETF-----RGG--WTKSGDKYVRNADGSYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQAGLTKTK 463
Cdd:cd17651 359 AERFvpdpfVPGarMYRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLV 438
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1920939256 464 AFVVLKPGAQVSETELKAFVKERLAPYKYPRIIEFMDALPKTATGKIQR 512
Cdd:cd17651 439 AYVVGDPEAPVDAAELRAALATHLPEYMVPSAFVLLDALPLTPNGKLDR 487
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
25-523 |
4.36e-61 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 210.30 E-value: 4.36e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 25 AQRPGKTAYIDDHGTMRYGELAERIRRVAGALQAS-GIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLLTADDY 103
Cdd:PRK08974 34 ARYADQPAFINMGEVMTFRKLEERSRAFAAYLQNGlGLKKGDRVALMMPNLLQYPIALFGILRAGMIVVNVNPLYTPREL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 104 AYMLQHSRAQAVLVSGALLPVLRQAMAQGghEAATVIVSR------------------------PAGPLPDGMIALEAW- 158
Cdd:PRK08974 114 EHQLNDSGAKAIVIVSNFAHTLEKVVFKT--PVKHVILTRmgdqlstakgtlvnfvvkyikrlvPKYHLPDAISFRSALh 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 159 IERNAPLAAPASTGpDDPGFWLYSSGSTGRPKGVLHSQGN---PYWTAELYAKPVLSLGEaDICFSAAKLYFAYGLG-NA 234
Cdd:PRK08974 192 KGRRMQYVKPELVP-EDLAFLQYTGGTTGVAKGAMLTHRNmlaNLEQAKAAYGPLLHPGK-ELVVTALPLYHIFALTvNC 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 235 LTFpLSVGATVVLMAERPTPEATFRRWLDYQPTVFFGAPTGYAGMLAAPGLPTREQVSLRLCSSAGEALPADLGERFTAH 314
Cdd:PRK08974 270 LLF-IELGGQNLLITNPRDIPGFVKELKKYPFTAITGVNTLFNALLNNEEFQELDFSSLKLSVGGGMAVQQAVAERWVKL 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 315 FGCEIIDGIGSTEMLHIFLSNRPGQVRY-GTTGWPVPGYAVELRDEDGHAVPDGDVGDLYIQGPSAALMYWGNREKSRET 393
Cdd:PRK08974 349 TGQYLLEGYGLTECSPLVSVNPYDLDYYsGSIGLPVPSTEIKLVDDDGNEVPPGEPGELWVKGPQVMLGYWQRPEATDEV 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 394 FRGGWTKSGDKYVRNADGSYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQAGLTKTKAFVVLKpGAQ 473
Cdd:PRK08974 429 IKDGWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAVKIFVVKK-DPS 507
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1920939256 474 VSETELKAFVKERLAPYKYPRIIEFMDALPKTATGKIQRFRLREMEGAPA 523
Cdd:PRK08974 508 LTEEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELRDEARAKV 557
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
39-517 |
5.74e-61 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 208.60 E-value: 5.74e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 39 TMRYGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLLTADDYAYMLQHSRAQAVLVS 118
Cdd:PRK08276 11 VVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVLIVS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 119 GALLPVLRQAMAQGGHEAATVIVSrpAGPLPdGMIALEAWIErnaplAAPASTGPDDP--GFWLYSSGSTGRPKGVLH-- 194
Cdd:PRK08276 91 AALADTAAELAAELPAGVPLLLVV--AGPVP-GFRSYEEALA-----AQPDTPIADETagADMLYSSGTTGRPKGIKRpl 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 195 SQGNPYWTAELYAKPVL---SLGEADICFSAAKLYFAYGL---GNALTFplsvGATVVLMaERPTPEATFRRWLDYQPTV 268
Cdd:PRK08276 163 PGLDPDEAPGMMLALLGfgmYGGPDSVYLSPAPLYHTAPLrfgMSALAL----GGTVVVM-EKFDAEEALALIERYRVTH 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 269 FFGAPTGYAGMLAAPglptrEQV-------SLRLCSSAGEALPADLGERFTAHFGCEIIDGIGSTEMLHIFLSN------ 335
Cdd:PRK08276 238 SQLVPTMFVRMLKLP-----EEVrarydvsSLRVAIHAAAPCPVEVKRAMIDWWGPIIHEYYASSEGGGVTVITsedwla 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 336 RPGQVrygttGWPVPGyavELR--DEDGHAVPDGDVGDLYIQGPSAALMYWGNREKSRETFRG-GWTKSGD-KYVrNADG 411
Cdd:PRK08276 313 HPGSV-----GKAVLG---EVRilDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARNPhGWVTVGDvGYL-DEDG 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 412 sYSY-AGRSDDMLkVSG---IYvsPFEVEATLAQHPAILEAAVIGVPDQAGLTKTKAFVVLKPGAQVSE---TELKAFVK 484
Cdd:PRK08276 384 -YLYlTDRKSDMI-ISGgvnIY--PQEIENLLVTHPKVADVAVFGVPDEEMGERVKAVVQPADGADAGDalaAELIAWLR 459
|
490 500 510
....*....|....*....|....*....|...
gi 1920939256 485 ERLAPYKYPRIIEFMDALPKTATGKIQRFRLRE 517
Cdd:PRK08276 460 GRLAHYKCPRSIDFEDELPRTPTGKLYKRRLRD 492
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
9-518 |
1.82e-60 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 208.70 E-value: 1.82e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 9 PPGTPFNFAQ------HLIACNAQRPGKTAYIDDHG-TMRYGELAERIRRVAGALQASGIHREERVLLLMhdgndwPVC- 80
Cdd:PRK05605 20 APWTPHDLDYgdttlvDLYDNAVARFGDRPALDFFGaTTTYAELGKQVRRAAAGLRALGVRPGDRVAIVL------PNCp 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 81 -FLGAMYA----GIVPVAVNTLLTADDYAYMLQHSRAQAVLVSGALLPVLRQAMAQGGHE---AATVIVSRPAG------ 146
Cdd:PRK05605 94 qHIVAFYAvlrlGAVVVEHNPLYTAHELEHPFEDHGARVAIVWDKVAPTVERLRRTTPLEtivSVNMIAAMPLLqrlalr 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 147 -PLP-------------DGMIALEAWIERNAP----LAAPASTGPDDPGFWLYSSGSTGRPKGVLHSQGNPYWTAELYAK 208
Cdd:PRK05605 174 lPIPalrkaraaltgpaPGTVPWETLVDAAIGgdgsDVSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFANAAQGKA 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 209 PVLSLGEADICFSAA-KLYFAYGLGNALTFPLSVGATVVLMaerPTPEA-----TFRRwldYQPTVFFGAPTGYAGMLAA 282
Cdd:PRK05605 254 WVPGLGDGPERVLAAlPMFHAYGLTLCLTLAVSIGGELVLL---PAPDIdlildAMKK---HPPTWLPGVPPLYEKIAEA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 283 P---GLPTReqvSLRLCSSAGEALPADLGERFTAHFGCEIIDGIGSTEMLHIFLSNRPGQVRY-GTTGWPVPGYAVELRD 358
Cdd:PRK05605 328 AeerGVDLS---GVRNAFSGAMALPVSTVELWEKLTGGLLVEGYGLTETSPIIVGNPMSDDRRpGYVGVPFPDTEVRIVD 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 359 ED--GHAVPDGDVGDLYIQGPSAALMYWGNREKSRETFRGGWTKSGDKYVRNADGSYSYAGRSDDMLKVSGIYVSPFEVE 436
Cdd:PRK05605 405 PEdpDETMPDGEEGELLVRGPQVFKGYWNRPEETAKSFLDGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVE 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 437 ATLAQHPAILEAAVIGVPDQAGLTKTKAFVVLKPGAQVSETELKAFVKERLAPYKYPRIIEFMDALPKTATGKIQRFRLR 516
Cdd:PRK05605 485 EVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEPGAALDPEGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRREVR 564
|
..
gi 1920939256 517 EM 518
Cdd:PRK05605 565 EE 566
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
42-517 |
2.51e-60 |
|
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: 204.92 E-value: 2.51e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 42 YGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLLTADDYAYMLQHSRAQAVLVSGAL 121
Cdd:cd05903 4 YSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVPERF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 122 lpvlrqamaqGGHEaatvivsrpagPLPDgmialeawiernaplaapastgPDDPGFWLYSSGSTGRPKGVLHSQGNPYW 201
Cdd:cd05903 84 ----------RQFD-----------PAAM----------------------PDAVALLLFTSGTTGEPKGVMHSHNTLSA 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 202 TAELYAKPvLSLGEADICFSAAKLYFAYGLGNALTFPLSVGATVVLMaERPTPEATFRRWLDYQPTVFFGAPTGYAGMLA 281
Cdd:cd05903 121 SIRQYAER-LGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQ-DIWDPDKALALMREHGVTFMMGATPFLTDLLN 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 282 APGLPTREQVSLRLCSSAGEALPADLGERFTAHFGCEIIDGIGSTEMLHIFLSNRPGQV--RYGTTGWPVPGYAVELRDE 359
Cdd:cd05903 199 AVEEAGEPLSRLRTFVCGGATVPRSLARRAAELLGAKVCSAYGSTECPGAVTSITPAPEdrRLYTDGRPLPGVEIKVVDD 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 360 DGHAVPDGDVGDLYIQGPSAALMYWGNREKSRETFRGGWTKSGDKYVRNADGSYSYAGRSDDMLKVSGIYVSPFEVEATL 439
Cdd:cd05903 279 TGATLAPGVEGELLSRGPSVFLGYLDRPDLTADAAPEGWFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLL 358
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1920939256 440 AQHPAILEAAVIGVPDQAGLTKTKAFVVLKPGAQVSETELKAFV-KERLAPYKYPRIIEFMDALPKTATGKIQRFRLRE 517
Cdd:cd05903 359 LGHPGVIEAAVVALPDERLGERACAVVVTKSGALLTFDELVAYLdRQGVAKQYWPERLVHVDDLPRTPSGKVQKFRLRE 437
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
25-515 |
2.65e-60 |
|
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: 206.36 E-value: 2.65e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 25 AQRPGKTAYIDDHGTMRYGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLLTADDYA 104
Cdd:cd17646 9 ARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRLA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 105 YMLQHSRAQAVLVSGALLPVLRqamaqGGHEAATVIVSRPAGPLPDGmialeawiernaPLAAPastGPDDPGFWLYSSG 184
Cdd:cd17646 89 YMLADAGPAVVLTTADLAARLP-----AGGDVALLGDEALAAPPATP------------PLVPP---RPDNLAYVIYTSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 185 STGRPKGVLHSQG----NPYWTAELYakpvlSLGEADICFSAAKLYFAYGLgNALTFPLSVGATVVlMAE---RPTPEAT 257
Cdd:cd17646 149 STGRPKGVMVTHAgivnRLLWMQDEY-----PLGPGDRVLQKTPLSFDVSV-WELFWPLVAGARLV-VARpggHRDPAYL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 258 FRRWLDYQPTVFFGAPTGYAGMLAAPGLPTReqVSLRLCSSAGEALPADLGERFTAHFGCEIIDGIGSTE----MLHIfl 333
Cdd:cd17646 222 AALIREHGVTTCHFVPSMLRVFLAEPAAGSC--ASLRRVFCSGEALPPELAARFLALPGAELHNLYGPTEaaidVTHW-- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 334 SNRPGQVRYGTT-GWPVPGYAVELRDEDGHAVPDGDVGDLYIQGPSAALMYWGNREKSRETFRGGW-------TKSGDKY 405
Cdd:cd17646 298 PVRGPAETPSVPiGRPVPNTRLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPfgpgsrmYRTGDLA 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 406 VRNADGSYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQAGLTKTKAFVVLKPGAQ-VSETELKAFVK 484
Cdd:cd17646 378 RWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAAGAAgPDTAALRAHLA 457
|
490 500 510
....*....|....*....|....*....|.
gi 1920939256 485 ERLAPYKYPRIIEFMDALPKTATGKIQRFRL 515
Cdd:cd17646 458 ERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
20-517 |
7.43e-60 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 206.53 E-value: 7.43e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 20 LIACNAQR-PGKTAYIDDHGTMRYGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLL 98
Cdd:PRK13382 48 GFAIAAQRcPDRPGLIDELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSF 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 99 TADDYAYMLQHSRAQAVLVSGALLPVLRQAMAqgGHEAATVIVSRPAGPlpdGMIALEAWIERNAPLAAPAStgPDDPGF 178
Cdd:PRK13382 128 AGPALAEVVTREGVDTVIYDEEFSATVDRALA--DCPQATRIVAWTDED---HDLTVEVLIAAHAGQRPEPT--GRKGRV 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 179 WLYSSGSTGRPKGVLHSQGNPYWTAelyaKPVLS---LGEADICFSAAKLYFAYGLGNaLTFPLSVGATVVlMAERPTPE 255
Cdd:PRK13382 201 ILLTSGTTGTPKGARRSGPGGIGTL----KAILDrtpWRAEEPTVIVAPMFHAWGFSQ-LVLAASLACTIV-TRRRFDPE 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 256 ATFRRWLDYQPTVFFGAPTGYAGMLAAP--GLPTREQVSLRLCSSAGEALPADLGERFTAHFGCEIIDGIGSTEMLHIFL 333
Cdd:PRK13382 275 ATLDLIDRHRATGLAVVPVMFDRIMDLPaeVRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFGDVIYNNYNATEAGMIAT 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 334 SNrPGQVRYG--TTGWPVPGYAVELRDEDGHAVPDGDVGDLYIQGPSaalMYWGNREKSRETFRGGWTKSGDKYVRNADG 411
Cdd:PRK13382 355 AT-PADLRAApdTAGRPAEGTEIRILDQDFREVPTGEVGTIFVRNDT---QFDGYTSGSTKDFHDGFMASGDVGYLDENG 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 412 SYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQAGLTKTKAFVVLKPGAQVSETELKAFVKERLAPYK 491
Cdd:PRK13382 431 RLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPGASATPETLKQHVRDNLANYK 510
|
490 500
....*....|....*....|....*.
gi 1920939256 492 YPRIIEFMDALPKTATGKIQRFRLRE 517
Cdd:PRK13382 511 VPRDIVVLDELPRGATGKILRRELQA 536
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
40-517 |
3.53e-59 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 203.78 E-value: 3.53e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 40 MRYGELAERIRRVAGALQASGIHREERVLLLMHdgNDWPV--CFLGAMYAGIVPVAVNTLLTADDYAYMLQHSRAQAVLV 117
Cdd:PRK12406 12 RSFDELAQRAARAAGGLAALGVRPGDCVALLMR--NDFAFfeAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 118 SGALLPVLRQAMAQGgheAATVIVSRPA------------GPLPDGMIALEAWIERNAPLAAPASTGPddpGFWLYSSGS 185
Cdd:PRK12406 90 HADLLHGLASALPAG---VTVLSVPTPPeiaaayrispalLTPPAGAIDWEGWLAQQEPYDGPPVPQP---QSMIYTSGT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 186 TGRPKGVLHSQGNPYWTA--ELYAKPVLSLGEADICFSAAKLY----FAYGLgNALTFplsvGATVVLMAeRPTPEATFR 259
Cdd:PRK12406 164 TGHPKGVRRAAPTPEQAAaaEQMRALIYGLKPGIRALLTGPLYhsapNAYGL-RAGRL----GGVLVLQP-RFDPEELLQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 260 RWLDYQPTVFFGAPTGYAGMLAAPglptrEQV-------SLRLCSSAGEALPADLGERFTAHFGCEIIDGIGSTEM-LHI 331
Cdd:PRK12406 238 LIERHRITHMHMVPTMFIRLLKLP-----EEVrakydvsSLRHVIHAAAPCPADVKRAMIEWWGPVIYEYYGSTESgAVT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 332 FLSNRPGQVRYGTTGWPVPGYAVELRDEDGHAVPDGDVGDLYIQGPSAALM-YWGNREKSRETFRGGWTKSGDKYVRNAD 410
Cdd:PRK12406 313 FATSEDALSHPGTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPDFtYHNKPEKRAEIDRGGFITSGDVGYLDAD 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 411 GSYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQAGLTKTKAFVVLKPGAQVSETELKAFVKERLAPY 490
Cdd:PRK12406 393 GYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPGATLDEADIRAQLKARLAGY 472
|
490 500
....*....|....*....|....*..
gi 1920939256 491 KYPRIIEFMDALPKTATGKIQRFRLRE 517
Cdd:PRK12406 473 KVPKHIEIMAELPREDSGKIFKRRLRD 499
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
28-517 |
2.27e-58 |
|
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: 200.99 E-value: 2.27e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 28 PGKTAYIddHGTMRY--GELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLLTADDYAY 105
Cdd:cd12118 18 PDRTSIV--YGDRRYtwRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 106 MLQHSRAQAVLVSGALLpvLRQAMAQGgheaatvivSRPAGPLP----DGMIALEawiernaplaapastgpddpgfwlY 181
Cdd:cd12118 96 ILRHSEAKVLFVDREFE--YEDLLAEG---------DPDFEWIPpadeWDPIALN------------------------Y 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 182 SSGSTGRPKGVLHSQGNPYWTAElyakpvlslgeADICFSAAKLYFAYgL-------GNALTFPLSV---GATVVLMaER 251
Cdd:cd12118 141 TSGTTGRPKGVVYHHRGAYLNAL-----------ANILEWEMKQHPVY-LwtlpmfhCNGWCFPWTVaavGGTNVCL-RK 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 252 PTPEATFRRWLDYQPTVFFGAPTGYAGMLAAP-----GLPTREQVSlrlcsSAGEALPADLGERFTAhFGCEIIDGIGST 326
Cdd:cd12118 208 VDAKAIYDLIEKHKVTHFCGAPTVLNMLANAPpsdarPLPHRVHVM-----TAGAPPPAAVLAKMEE-LGFDVTHVYGLT 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 327 EMLHIFLS--------NRPGQVRYGT---TGWPVPGY-AVELRDEDGH-AVP-DGD-VGDLYIQGPSAALMYWGNREKSR 391
Cdd:cd12118 282 ETYGPATVcawkpewdELPTEERARLkarQGVRYVGLeEVDVLDPETMkPVPrDGKtIGEIVFRGNIVMKGYLKNPEATA 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 392 ETFRGGWTKSGDKYVRNADGSYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQAGLTKTKAFVVLKPG 471
Cdd:cd12118 362 EAFRGGWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVELKEG 441
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1920939256 472 AQVSETELKAFVKERLAPYKYPRIIEFMDaLPKTATGKIQRFRLRE 517
Cdd:cd12118 442 AKVTEEEIIAFCREHLAGFMVPKTVVFGE-LPKTSTGKIQKFVLRD 486
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
19-517 |
2.30e-58 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 202.19 E-value: 2.30e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 19 HLIACNAQR-PGKTAYIDDHGTMRYGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTL 97
Cdd:PRK07470 11 HFLRQAARRfPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 98 LTADDYAYMLQHSRAQAVLVSGALlpvlrQAMAQGGHEAATVIVSRPAGPLPDGMIALEAWIERNA-PLAAPASTGPDDP 176
Cdd:PRK07470 91 QTPDEVAYLAEASGARAMICHADF-----PEHAAAVRAASPDLTHVVAIGGARAGLDYEALVARHLgARVANAAVDHDDP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 177 GFWLYSSGSTGRPK-GVL-HSQGNPYWTAELyAKPVLSLGEADICFSAAKLyfAYGLG-NALTFPLSVGATVVLMAERPT 253
Cdd:PRK07470 166 CWFFFTSGTTGRPKaAVLtHGQMAFVITNHL-ADLMPGTTEQDASLVVAPL--SHGAGiHQLCQVARGAATVLLPSERFD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 254 PEATFRRWLDYQPTVFFGAPTGYAGMLAAPGLPTREQVSLRLCSSAG---------EALpADLGERFTAHFGC-EIIDGI 323
Cdd:PRK07470 243 PAEVWALVERHRVTNLFTVPTILKMLVEHPAVDRYDHSSLRYVIYAGapmyradqkRAL-AKLGKVLVQYFGLgEVTGNI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 324 gsTEMLHIFLSNRPG-QVRYGTTGWPVPGYAVELRDEDGHAVPDGDVGDLYIQGPSAALMYWGNREKSRETFRGGWTKSG 402
Cdd:PRK07470 322 --TVLPPALHDAEDGpDARIGTCGFERTGMEVQIQDDEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAFRDGWFRTG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 403 DKYVRNADGSYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPD----QAGLtktkAFVVLKPGAQVSETE 478
Cdd:PRK07470 400 DLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDpvwgEVGV----AVCVARDGAPVDEAE 475
|
490 500 510
....*....|....*....|....*....|....*....
gi 1920939256 479 LKAFVKERLAPYKYPRIIEFMDALPKTATGKIQRFRLRE 517
Cdd:PRK07470 476 LLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMVRE 514
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
173-516 |
4.83e-58 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 196.34 E-value: 4.83e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 173 PDDPGFWLYSSGSTGRPKGVLHSQ----GNPYWTAELyakpvLSLGEADICFSAAKLYFAYGLGNALTFPLSVGATVVLM 248
Cdd:cd05917 1 PDDVINIQFTSGTTGSPKGATLTHhnivNNGYFIGER-----LGLTEQDRLCIPVPLFHCFGSVLGVLACLTHGATMVFP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 249 AERPTPEATFRRWLDYQPTVFFGAPTGYAGMLAAPGLPTREQVSLRLCSSAGEALPADLGERFTAHFGC-EIIDGIGSTE 327
Cdd:cd05917 76 SPSFDPLAVLEAIEKEKCTALHGVPTMFIAELEHPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEVMNMkDVTIAYGMTE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 328 MLHIFLSNRPG---QVRYGTTGWPVPGYAVELRDEDGHAVPD-GDVGDLYIQGPSAALMYWGNREKSRETFRG-GWTKSG 402
Cdd:cd05917 156 TSPVSTQTRTDdsiEKRVNTVGRIMPHTEAKIVDPEGGIVPPvGVPGELCIRGYSVMKGYWNDPEKTAEAIDGdGWLHTG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 403 DKYVRNADGSYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQAGLTKTKAFVVLKPGAQVSETELKAF 482
Cdd:cd05917 236 DLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLKEGAELTEEDIKAY 315
|
330 340 350
....*....|....*....|....*....|....
gi 1920939256 483 VKERLAPYKYPRIIEFMDALPKTATGKIQRFRLR 516
Cdd:cd05917 316 CKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
25-518 |
6.79e-58 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 201.58 E-value: 6.79e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 25 AQRPGKTAYIDDHGTMR--YGELAERIRRVAGALQASGIHREERVLLLMHDGNDWpvcfLGAMYA----GIVPVAVNTLL 98
Cdd:PRK08315 27 ARYPDREALVYRDQGLRwtYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEW----VLTQFAtakiGAILVTINPAY 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 99 TADDYAYMLQHSRAQAVLVSGA------------LLPVLRQAMAQGGHEAA-----TVIvsRPAGPLPDGMIALEAWIER 161
Cdd:PRK08315 103 RLSELEYALNQSGCKALIAADGfkdsdyvamlyeLAPELATCEPGQLQSARlpelrRVI--FLGDEKHPGMLNFDELLAL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 162 -----NAPLAAPAST-GPDDPGFWLYSSGSTGRPKGVLHSQ----GNPYWTAELyakpvLSLGEAD-ICFSAAkLYFAYG 230
Cdd:PRK08315 181 gravdDAELAARQATlDPDDPINIQYTSGTTGFPKGATLTHrnilNNGYFIGEA-----MKLTEEDrLCIPVP-LYHCFG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 231 --LGN-ALtfpLSVGATVVLMAERPTPEATFRRWLDYQPTVFFGAPTGYAGMLAAPGLPTREQVSLRLCSSAGEALPADL 307
Cdd:PRK08315 255 mvLGNlAC---VTHGATMVYPGEGFDPLATLAAVEEERCTALYGVPTMFIAELDHPDFARFDLSSLRTGIMAGSPCPIEV 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 308 GERFTAHFGC-EIIDGIGSTE---MLHIFLSNRPGQVRYGTTGWPVPGYAVELRDED-GHAVPDGDVGDLYIQGPSAALM 382
Cdd:PRK08315 332 MKRVIDKMHMsEVTIAYGMTEtspVSTQTRTDDPLEKRVTTVGRALPHLEVKIVDPEtGETVPRGEQGELCTRGYSVMKG 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 383 YWGNREKSRETF-RGGWTKSGDKYVRNADGSYSYAGRSDDMLKVSG--IYvsPFEVEATLAQHPAILEAAVIGVPDQagl 459
Cdd:PRK08315 412 YWNDPEKTAEAIdADGWMHTGDLAVMDEEGYVNIVGRIKDMIIRGGenIY--PREIEEFLYTHPKIQDVQVVGVPDE--- 486
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1920939256 460 tktK------AFVVLKPGAQVSETELKAFVKERLAPYKYPRIIEFMDALPKTATGKIQRFRLREM 518
Cdd:PRK08315 487 ---KygeevcAWIILRPGATLTEEDVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGKIQKFKMREM 548
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
1-452 |
5.51e-57 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 199.94 E-value: 5.51e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 1 MTAEPQVQPPGTpfnFAQHLIACNAQRPGKTAYIDDHG----TMRYGELAERIRRVAGALQASGIHREERVLLLMHDGND 76
Cdd:COG1022 1 MSEFSDVPPADT---LPDLLRRRAARFPDRVALREKEDgiwqSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 77 WPVCFLGAMYAGIVPVAVNTLLTADDYAYMLQHSRAQAVLVSG-ALLPVLRQAMAQGGHEAATVIVSRPAGPLPDGMIAL 155
Cdd:COG1022 78 WVIADLAILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVEDqEQLDKLLEVRDELPSLRHIVVLDPRGLRDDPRLLSL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 156 EAWIERNAPLAAP-------ASTGPDDPGFWLYSSGSTGRPKGVLHSQGNpyWTAELYA-KPVLSLGEADICFS------ 221
Cdd:COG1022 158 DELLALGREVADPaelearrAAVKPDDLATIIYTSGTTGRPKGVMLTHRN--LLSNARAlLERLPLGPGDRTLSflplah 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 222 -AAKLyFAYGLgnaltfpLSVGATVVLmAERPtpeATFRRWL-DYQPTVFFGAP-------TG-YAGMLAAPGL------ 285
Cdd:COG1022 236 vFERT-VSYYA-------LAAGATVAF-AESP---DTLAEDLrEVKPTFMLAVPrvwekvyAGiQAKAEEAGGLkrklfr 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 286 ----------PTREQ---VS-------------------------LRLCSSAGEALPADLGERFTAhFGCEIIDGIGSTE 327
Cdd:COG1022 304 walavgrryaRARLAgksPSlllrlkhaladklvfsklrealggrLRFAVSGGAALGPELARFFRA-LGIPVLEGYGLTE 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 328 MLHIFLSNRPGQVRYGTTGWPVPGyaVELR-DEDghavpdgdvGDLYIQGPSAALMYWGNREKSRETF-RGGWTKSGDKY 405
Cdd:COG1022 383 TSPVITVNRPGDNRIGTVGPPLPG--VEVKiAED---------GEILVRGPNVMKGYYKNPEATAEAFdADGWLHTGDIG 451
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1920939256 406 VRNADGSYSYAGRSDDMLKVS-GIYVSPFEVEATLAQHPAILEAAVIG 452
Cdd:COG1022 452 ELDEDGFLRITGRKKDLIVTSgGKNVAPQPIENALKASPLIEQAVVVG 499
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
25-523 |
1.10e-56 |
|
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: 204.71 E-value: 1.10e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 25 AQRPGKTAYIDDHGTMRYGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAG--IVPVAVntlltadD 102
Cdd:COG1020 487 ARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGaaYVPLDP-------A 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 103 Y-----AYMLQHSRAQAVLVSGALLPVLRQAMAQggheaatvivsrpagplpdgMIALEAWIERNAPLAAPAST-GPDDP 176
Cdd:COG1020 560 YpaerlAYMLEDAGARLVLTQSALAARLPELGVP--------------------VLALDALALAAEPATNPPVPvTPDDL 619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 177 GFWLYSSGSTGRPKGVLHSQGN----PYWTAELYAkpvlsLGEADICfsaakLYFAyglgnALTF---------PLSVGA 243
Cdd:COG1020 620 AYVIYTSGSTGRPKGVMVEHRAlvnlLAWMQRRYG-----LGPGDRV-----LQFA-----SLSFdasvweifgALLSGA 684
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 244 TVVLMAE--RPTPEATFRRWLDYQPTVFFgAPTGYAGMLAAPGLPTREqvSLRLCSSAGEALPADLGERFTAHF-GCEII 320
Cdd:COG1020 685 TLVLAPPeaRRDPAALAELLARHRVTVLN-LTPSLLRALLDAAPEALP--SLRLVLVGGEALPPELVRRWRARLpGARLV 761
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 321 DGIGSTE----MLHIFLSNRPGQVRYGTTGWPVPGYAVELRDEDGHAVPDGDVGDLYIQGPSAALMYWGNREKSRETF-- 394
Cdd:COG1020 762 NLYGPTEttvdSTYYEVTPPDADGGSVPIGRPIANTRVYVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFva 841
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 395 ----RGG--WTKSGDKYVRNADGSYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQAGLTKTKAFVVL 468
Cdd:COG1020 842 dpfgFPGarLYRTGDLARWLPDGNLEFLGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVP 921
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1920939256 469 KPGAQVSETELKAFVKERLAPYKYPRIIEFMDALPKTATGKIQRFRLREMEGAPA 523
Cdd:COG1020 922 EAGAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALPAPAAAAA 976
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
21-520 |
1.25e-56 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 196.65 E-value: 1.25e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 21 IACNAQR-PGKTAYIDDHGTMRYGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLLT 99
Cdd:PRK06145 8 IAFHARRtPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 100 ADDYAYMLQHSRAQAVLVSG--ALLPVLRQAMAQGGhEAATVIVSRPAGPlpdgmialeawierNAPLAAPASTGPDDPG 177
Cdd:PRK06145 88 ADEVAYILGDAGAKLLLVDEefDAIVALETPKIVID-AAAQADSRRLAQG--------------GLEIPPQAAVAPTDLV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 178 FWLYSSGSTGRPKGVLHSQGNPYWTAelyAKPVLSLG--EADICFSAAKLYFAyglgNALTFP----LSVGATVVLMAER 251
Cdd:PRK06145 153 RLMYTSGTTDRPKGVMHSYGNLHWKS---IDHVIALGltASERLLVVGPLYHV----GAFDLPgiavLWVGGTLRIHREF 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 252 pTPEATFRRWLDYQPTVFFGAPTGYAGMLAAPGLPTREQVSLRLCSSAGEALPADLGERFTAHF-GCEIIDGIGSTEML- 329
Cdd:PRK06145 226 -DPEAVLAAIERHRLTCAWMAPVMLSRVLTVPDRDRFDLDSLAWCIGGGEKTPESRIRDFTRVFtRARYIDAYGLTETCs 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 330 -HIFLSNRPGQVRYGTTGWPVPGYAVELRDEDGHAVPDGDVGDLYIQGPSAALMYWGNREKSRETFRGGWTKSGDKYVRN 408
Cdd:PRK06145 305 gDTLMEAGREIEKIGSTGRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGDWFRSGDVGYLD 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 409 ADGSYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQAGLTKTKAFVVLKPGAQVSETELKAFVKERLA 488
Cdd:PRK06145 385 EEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPGATLTLEALDRHCRQRLA 464
|
490 500 510
....*....|....*....|....*....|...
gi 1920939256 489 PYKYPRIIEFMDALPKTATGKIQRFRLR-EMEG 520
Cdd:PRK06145 465 SFKVPRQLKVRDELPRNPSGKVLKRVLRdELNG 497
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
18-515 |
2.39e-56 |
|
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: 194.84 E-value: 2.39e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 18 QHLIACNAQR-PGKTAYIDDHGTMRYGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNT 96
Cdd:cd12115 2 HDLVEAQAARtPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 97 LLTADDYAYMLQHSRAQAVLvsgallpvlrqamaqggheaatvivsrpagplpdgmialeawiernaplaapasTGPDDP 176
Cdd:cd12115 82 AYPPERLRFILEDAQARLVL------------------------------------------------------TDPDDL 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 177 GFWLYSSGSTGRPKGVLHSQGNP----YWTAELYAKPVLS--LGEADICF--SAAKLyFAyglgnaltfPLSVGATVVLM 248
Cdd:cd12115 108 AYVIYTSGSTGRPKGVAIEHRNAaaflQWAAAAFSAEELAgvLASTSICFdlSVFEL-FG---------PLATGGKVVLA 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 249 AERPTPEATFRRwldYQPTVFFGAPTGYAGMLAAPGLPTreqvSLRLCSSAGEALPADLGERFTAHFGCE-IIDGIGSTE 327
Cdd:cd12115 178 DNVLALPDLPAA---AEVTLINTVPSAAAELLRHDALPA----SVRVVNLAGEPLPRDLVQRLYARLQVErVVNLYGPSE 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 328 --MLHIFLSNRPGQVRYGTTGWPVPGYAVELRDEDGHAVPDGDVGDLYIQGPSAALMYWGNREKSRETFR-------GGW 398
Cdd:cd12115 251 dtTYSTVAPVPPGASGEVSIGRPLANTQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLpdpfgpgARL 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 399 TKSGDKYVRNADGSYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQAGLTKTKAFVVLKPGAQVSETE 478
Cdd:cd12115 331 YRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEPGAAGLVED 410
|
490 500 510
....*....|....*....|....*....|....*..
gi 1920939256 479 LKAFVKERLAPYKYPRIIEFMDALPKTATGKIQRFRL 515
Cdd:cd12115 411 LRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
27-516 |
2.89e-56 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 195.21 E-value: 2.89e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 27 RPGKTAYIDDHGT-MRYGELA---ERIRRVAGALqASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLLTADD 102
Cdd:PRK07787 5 NPAAVAAAADIADaVRIGGRVlsrSDLAGAATAV-AERVAGARRVAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 103 YAYMLQHSRAQAVLvsgallpvlrqamaqggheaatvivsrpaGPLPDGMIALEAW-IERNAPLA-APASTGPDDPGFWL 180
Cdd:PRK07787 84 RRHILADSGAQAWL-----------------------------GPAPDDPAGLPHVpVRLHARSWhRYPEPDPDAPALIV 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 181 YSSGSTGRPKGVLHSQgnPYWTAELYAkpvlsLGEA------DICFSAAKLYFAYGLGNALTFPLSVGATVVLMAeRPTP 254
Cdd:PRK07787 135 YTSGTTGPPKGVVLSR--RAIAADLDA-----LAEAwqwtadDVLVHGLPLFHVHGLVLGVLGPLRIGNRFVHTG-RPTP 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 255 EAtFRRWLDYQPTVFFGAPTGYAGMLAAPGLPtREQVSLRLCSSAGEALPADLGERFTAHFGCEIIDGIGSTEMLhIFLS 334
Cdd:PRK07787 207 EA-YAQALSEGGTLYFGVPTVWSRIAADPEAA-RALRGARLLVSGSAALPVPVFDRLAALTGHRPVERYGMTETL-ITLS 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 335 NRP-GQVRYGTTGWPVPGYAVELRDEDGHAVP-DGD-VGDLYIQGPSAALMYWGNREKSRETFRG-GWTKSGDKYVRNAD 410
Cdd:PRK07787 284 TRAdGERRPGWVGLPLAGVETRLVDEDGGPVPhDGEtVGELQVRGPTLFDGYLNRPDATAAAFTAdGWFRTGDVAVVDPD 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 411 GSYSYAGR-SDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQAGLTKTKAFVVlkPGAQVSETELKAFVKERLAP 489
Cdd:PRK07787 364 GMHRIVGReSTDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVV--GADDVAADELIDFVAQQLSV 441
|
490 500
....*....|....*....|....*..
gi 1920939256 490 YKYPRIIEFMDALPKTATGKIQRFRLR 516
Cdd:PRK07787 442 HKRPREVRFVDALPRNAMGKVLKKQLL 468
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
25-516 |
7.65e-56 |
|
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: 197.01 E-value: 7.65e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 25 AQRPGKTAYI---DDHGTMR---YGELAERIRRVAGALQASGIHREERVlllmhdgndwpvcflgAMYAGIVPVAVNTLL 98
Cdd:cd05966 64 KERGDKVAIIwegDEPDQSRtitYRELLREVCRFANVLKSLGVKKGDRV----------------AIYMPMIPELVIAML 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 99 ----------------TADDYAYMLQHSRAQAVLVSGA---------LLPVLRQAmAQGGHEAATVIVSRPAG---PLPD 150
Cdd:cd05966 128 acarigavhsvvfagfSAESLADRINDAQCKLVITADGgyrggkvipLKEIVDEA-LEKCPSVEKVLVVKRTGgevPMTE 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 151 GM-IALEAWIERNAPLAAPASTGPDDPGFWLYSSGSTGRPKGVLHSQGNpYwtaELYA----KPVLSLGEADICFSAAKL 225
Cdd:cd05966 207 GRdLWWHDLMAKQSPECEPEWMDSEDPLFILYTSGSTGKPKGVVHTTGG-Y---LLYAattfKYVFDYHPDDIYWCTADI 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 226 -------YFAYGlgnaltfPLSVGATVVLMAERPT-PeaTFRRWLD----YQPTVFFGAPTGY-AGMLAAPGLPTR-EQV 291
Cdd:cd05966 283 gwitghsYIVYG-------PLANGATTVMFEGTPTyP--DPGRYWDivekHKVTIFYTAPTAIrALMKFGDEWVKKhDLS 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 292 SLRLCSSAGEALPADLGERFTAHFG---CEIIDGIGSTEMLHIFLSNRPGQV--RYGTTGWPVPGYAVELRDEDGHAVPD 366
Cdd:cd05966 354 SLRVLGSVGEPINPEAWMWYYEVIGkerCPIVDTWWQTETGGIMITPLPGATplKPGSATRPFFGIEPAILDEEGNEVEG 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 367 GDVGDLYIQG--PSAALMYWGNREKSRETFrggWTK------SGDKYVRNADGSYSYAGRSDDMLKVSGIYVSPFEVEAT 438
Cdd:cd05966 434 EVEGYLVIKRpwPGMARTIYGDHERYEDTY---FSKfpgyyfTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESA 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 439 LAQHPAILEAAVIGVPD----QAGltktKAFVVLKPGAQVS---ETELKAFVKERLAPYKYPRIIEFMDALPKTATGKIQ 511
Cdd:cd05966 511 LVAHPAVAEAAVVGRPHdikgEAI----YAFVTLKDGEEPSdelRKELRKHVRKEIGPIATPDKIQFVPGLPKTRSGKIM 586
|
....*
gi 1920939256 512 RFRLR 516
Cdd:cd05966 587 RRILR 591
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
27-517 |
1.26e-55 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 194.52 E-value: 1.26e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 27 RPGKTAYI--DDHGTMRYGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLLTADDYA 104
Cdd:PRK13391 10 TPDKPAVImaSTGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 105 YMLQHSRAQAVLVSGALLPVLRQAMAQGGHEAATVIVsrpagplpDGMIALEAWIERNAPLAA-PASTGPDDP--GFWLY 181
Cdd:PRK13391 90 YIVDDSGARALITSAAKLDVARALLKQCPGVRHRLVL--------DGDGELEGFVGYAEAVAGlPATPIADESlgTDMLY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 182 SSGSTGRPKGVLH--SQGNPYWTAELYA--KPVLSLGEADICFSAAKLYFAYGLGNALTFpLSVGATVVLMaERPTPEAT 257
Cdd:PRK13391 162 SSGTTGRPKGIKRplPEQPPDTPLPLTAflQRLWGFRSDMVYLSPAPLYHSAPQRAVMLV-IRLGGTVIVM-EHFDAEQY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 258 FRRWLDYQPTVFFGAPTGYAGMLAAPglptrEQV-------SLRLCSSAGEALPADLGERFTAHFGCEIIDGIGSTEMLH 330
Cdd:PRK13391 240 LALIEEYGVTHTQLVPTMFSRMLKLP-----EEVrdkydlsSLEVAIHAAAPCPPQVKEQMIDWWGPIIHEYYAATEGLG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 331 I-FLSNRPGQVRYGTTGWPVPGyAVELRDEDGHAVPDGDVGDLYIQGPSaALMYWGNREKSRETF--RGGWTKSGD-KYV 406
Cdd:PRK13391 315 FtACDSEEWLAHPGTVGRAMFG-DLHILDDDGAELPPGEPGTIWFEGGR-PFEYLNDPAKTAEARhpDGTWSTVGDiGYV 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 407 rNADGSYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQAGLTKTKAFVVLKPGAQVSE---TELKAFV 483
Cdd:PRK13391 393 -DEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPVDGVDPGPalaAELIAFC 471
|
490 500 510
....*....|....*....|....*....|....
gi 1920939256 484 KERLAPYKYPRIIEFMDALPKTATGKIQRFRLRE 517
Cdd:PRK13391 472 RQRLSRQKCPRSIDFEDELPRLPTGKLYKRLLRD 505
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
47-516 |
1.61e-55 |
|
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: 192.66 E-value: 1.61e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 47 ERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAG----IVPVAVNTLLTADDYAYMLQHSRAQAVLVSGALL 122
Cdd:cd05922 1 LGVSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGgrlgLVFVPLNPTLKESVLRYLVADAGGRIVLADAGAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 123 PVLRQAMaqggheaatvivsrPAGPLPDGMIALEAWIERNAPLAAPASTgPDDPGFWLYSSGSTGRPKGVLHSQGNPYWT 202
Cdd:cd05922 81 DRLRDAL--------------PASPDPGTVLDADGIRAARASAPAHEVS-HEDLALLLYTSGSTGSPKLVRLSHQNLLAN 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 203 AELYAKpVLSLGEADICFSAAKLYFAYGLgNALTFPLSVGATVVLMAERPTPEATFRRWLDYQPTVFFGAPTGYAgMLAA 282
Cdd:cd05922 146 ARSIAE-YLGITADDRALTVLPLSYDYGL-SVLNTHLLRGATLVLTNDGVLDDAFWEDLREHGATGLAGVPSTYA-MLTR 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 283 PGLPTREQVSLRLCSSAGEALPADLGERFTAHF-GCEIIDGIGSTEMLHIFLSNRPGQV--RYGTTGWPVPGYAVELRDE 359
Cdd:cd05922 223 LGFDPAKLPSLRYLTQAGGRLPQETIARLRELLpGAQVYVMYGQTEATRRMTYLPPERIleKPGSIGLAIPGGEFEILDD 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 360 DGHAVPDGDVGDLYIQGPSAALMYWGNREKSRETFRGG---WTksGDKYVRNADGSYSYAGRSDDMLKVSGIYVSPFEVE 436
Cdd:cd05922 303 DGTPTPPGEPGEIVHRGPNVMKGYWNDPPYRRKEGRGGgvlHT--GDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIE 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 437 ATLAQHPAILEAAVIGVPDQAGlTKTKAFVVLKPGAQVSetELKAFVKERLAPYKYPRIIEFMDALPKTATGKIQRFRLR 516
Cdd:cd05922 381 AAARSIGLIIEAAAVGLPDPLG-EKLALFVTAPDKIDPK--DVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
28-512 |
2.72e-55 |
|
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: 192.14 E-value: 2.72e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 28 PGKTAYIDDHGTMRYGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLLTADDYAYML 107
Cdd:cd17643 1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 108 QHSRAQAVLvsgallpvlrqamaqggheaatvivsrpagplpdgmialeawiernaplaapasTGPDDPGFWLYSSGSTG 187
Cdd:cd17643 81 ADSGPSLLL------------------------------------------------------TDPDDLAYVIYTSGSTG 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 188 RPKGVLHSQGNpywtaelyakpVLSLgeadicFSAAKLYFAYG------LGNALTF---------PLSVGATVVLMAE-- 250
Cdd:cd17643 107 RPKGVVVSHAN-----------VLAL------FAATQRWFGFNeddvwtLFHSYAFdfsvweiwgALLHGGRLVVVPYev 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 251 RPTPEAtFRRWLDYQP-TVFFGAPTGYAGMLAAPGLPTREQVSLRLCSSAGEALPADLGERFTAHFGC---EIIDGIGST 326
Cdd:cd17643 170 ARSPED-FARLLRDEGvTVLNQTPSAFYQLVEAADRDGRDPLALRYVIFGGEALEAAMLRPWAGRFGLdrpQLVNMYGIT 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 327 EMLhIFLSNRPGQVRY------GTTGWPVPGYAVELRDEDGHAVPDGDVGDLYIQGPSAALMYWGNREKSRETFR----G 396
Cdd:cd17643 249 ETT-VHVTFRPLDAADlpaaaaSPIGRPLPGLRVYVLDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVanpfG 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 397 GWT----KSGDKYVRNADGSYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQAGLTKTKAFVVLKPGA 472
Cdd:cd17643 328 GPGsrmyRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVADDGA 407
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1920939256 473 QVSETELKAFVKERLAPYKYPRIIEFMDALPKTATGKIQR 512
Cdd:cd17643 408 AADIAELRALLKELLPDYMVPARYVPLDALPLTVNGKLDR 447
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
42-450 |
4.07e-55 |
|
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: 190.55 E-value: 4.07e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 42 YGELAERIRRVAGALQAS-GIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLLTADDYAYMLQHSRAQAVLVSGA 120
Cdd:TIGR01733 2 YRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDSA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 121 LLPVLRQAmaqggheaatvivsrPAGPLPDGMIALEAWIERNAPLAAPASTGPDDPGFWLYSSGSTGRPKGVLHSQGNP- 199
Cdd:TIGR01733 82 LASRLAGL---------------VLPVILLDPLELAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLv 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 200 ---YWTAELYAkpvlsLGEADICFSAAklyfayglgnALTF---------PLSVGATVVLM--AERPTPEATFRRWLDYQ 265
Cdd:TIGR01733 147 nllAWLARRYG-----LDPDDRVLQFA----------SLSFdasveeifgALLAGATLVVPpeDEERDDAALLAALIAEH 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 266 PTVFFGAPTGYAGMLAAPGLPtrEQVSLRLCSSAGEALPADLGERFTAHFG-CEIIDGIGSTE---MLHIFLSNRPGQVR 341
Cdd:TIGR01733 212 PVTVLNLTPSLLALLAAALPP--ALASLRLVILGGEALTPALVDRWRARGPgARLINLYGPTEttvWSTATLVDPDDAPR 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 342 YGTT--GWPVPGYAVELRDEDGHAVPDGDVGDLYIQGPSAALMYWGNREKSRETF---------RGGWTKSGDKYVRNAD 410
Cdd:TIGR01733 290 ESPVpiGRPLANTRLYVLDDDLRPVPVGVVGELYIGGPGVARGYLNRPELTAERFvpdpfaggdGARLYRTGDLVRYLPD 369
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1920939256 411 GSYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAV 450
Cdd:TIGR01733 370 GNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
25-515 |
8.32e-55 |
|
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: 190.54 E-value: 8.32e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 25 AQRPGKTAYIDDHGTMRYGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTlltaddya 104
Cdd:cd05945 2 AANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDA-------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 105 ymlqHSraqavlvsgallPVLRQAMaqggheaaTVIVSRPAGPLPDGmialeawiernaplaapastgpDDPGFWLYSSG 184
Cdd:cd05945 74 ----SS------------PAERIRE--------ILDAAKPALLIADG----------------------DDNAYIIFTSG 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 185 STGRPKGVLHSQGNPY----WTAELYAkpvlsLGEADICFSAAKLYFayGLGNALTFP-LSVGATVVLMAERPT--PEAT 257
Cdd:cd05945 108 STGRPKGVQISHDNLVsftnWMLSDFP-----LGPGDVFLNQAPFSF--DLSVMDLYPaLASGATLVPVPRDATadPKQL 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 258 FRRWLDYQPTVFFGAPTgYAGMLAAPGLPTREQV-SLRLCSSAGEALPADLGERFTAHF-GCEIIDGIGSTEMLHIFLSN 335
Cdd:cd05945 181 FRFLAEHGITVWVSTPS-FAAMCLLSPTFTPESLpSLRHFLFCGEVLPHKTARALQQRFpDARIYNTYGPTEATVAVTYI 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 336 RPGQ---VRYGT--TGWPVPGYAVELRDEDGHAVPDGDVGDLYIQGPSAALMYWGNREKSRETFR----GGWTKSGDKYV 406
Cdd:cd05945 260 EVTPevlDGYDRlpIGYAKPGAKLVILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFpdegQRAYRTGDLVR 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 407 RNADGSYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQAGLTKTKAFVVLKPGA-QVSETELKAFVKE 485
Cdd:cd05945 340 LEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPGAeAGLTKAIKAELAE 419
|
490 500 510
....*....|....*....|....*....|
gi 1920939256 486 RLAPYKYPRIIEFMDALPKTATGKIQRFRL 515
Cdd:cd05945 420 RLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
25-518 |
9.74e-55 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 193.11 E-value: 9.74e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 25 AQRPgktAYIDDHGTMRYGELAERIRRVAGALQA-SGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLLTADDY 103
Cdd:PRK12492 38 ADRP---AFSNLGVTLSYAELERHSAAFAAYLQQhTDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVNTNPLYTAREM 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 104 AYMLQHSRAQAVLV------------------------SGALLPVLRQAMAQGGHEAATVIVsrPAGPLPDGMIALEAWI 159
Cdd:PRK12492 115 RHQFKDSGARALVYlnmfgklvqevlpdtgieylieakMGDLLPAAKGWLVNTVVDKVKKMV--PAYHLPQAVPFKQALR 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 160 ERNAPLAAPASTGPDDPGFWLYSSGSTGRPKGVLHSQGNPYWTA-ELYA---------KPVLSLGEaDICFSAAKLYFAY 229
Cdd:PRK12492 193 QGRGLSLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVANMlQVRAclsqlgpdgQPLMKEGQ-EVMIAPLPLYHIY 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 230 GL-GNALTFPLSVGATVVLMAERPTPE--ATFRRWldyQPTVFFGAPTGYAGMLAAPGLPTREQVSLRLCSSAGEALPAD 306
Cdd:PRK12492 272 AFtANCMCMMVSGNHNVLITNPRDIPGfiKELGKW---RFSALLGLNTLFVALMDHPGFKDLDFSALKLTNSGGTALVKA 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 307 LGERFTAHFGCEIIDGIGSTEMLHIFLSNRPGQV-RYGTTGWPVPGYAVELRDEDGHAVPDGDVGDLYIQGPSAALMYWG 385
Cdd:PRK12492 349 TAERWEQLTGCTIVEGYGLTETSPVASTNPYGELaRLGTVGIPVPGTALKVIDDDGNELPLGERGELCIKGPQVMKGYWQ 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 386 NREKSRETFRG-GWTKSGDKYVRNADGSYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQAGLTKTKA 464
Cdd:PRK12492 429 QPEATAEALDAeGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVKL 508
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1920939256 465 FVVLKPGAqVSETELKAFVKERLAPYKYPRIIEFMDALPKTATGKIQRFRLREM 518
Cdd:PRK12492 509 FVVARDPG-LSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRRELRDI 561
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
28-515 |
1.74e-54 |
|
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: 190.56 E-value: 1.74e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 28 PGKTAYIDDHGTMRYGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLLTADdyayml 107
Cdd:cd12114 1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAA------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 108 qhsRAQAVLVSGAllpvLRQAMAQGGHEAATVIVSRpagPLPDGMIALEAWiernaPLAAPASTGPDDPGFWLYSSGSTG 187
Cdd:cd12114 75 ---RREAILADAG----ARLVLTDGPDAQLDVAVFD---VLILDLDALAAP-----APPPPVDVAPDDLAYVIFTSGSTG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 188 RPKGVLHSQGNPYWTA----ELYAkpvlsLGEADICFSAAKLYF---AYGLgnaltF-PLSVGATVVLM--AERPTPEAT 257
Cdd:cd12114 140 TPKGVMISHRAALNTIldinRRFA-----VGPDDRVLALSSLSFdlsVYDI-----FgALSAGATLVLPdeARRRDPAHW 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 258 FRRWLDYQPTVFFGAPtGYAGML-AAPGLPTREQVSLRLCSSAGEALPADLGERFTAHF-GCEIIDGIGSTE--MLHIFL 333
Cdd:cd12114 210 AELIERHGVTLWNSVP-ALLEMLlDVLEAAQALLPSLRLVLLSGDWIPLDLPARLRALApDARLISLGGATEasIWSIYH 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 334 SNRP-----GQVRYGTtgwPVPGYAVELRDEDGHAVPDGDVGDLYIQGPSAALMYWGNREKSRETF-----RGGWTKSGD 403
Cdd:cd12114 289 PIDEvppdwRSIPYGR---PLANQRYRVLDPRGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFvthpdGERLYRTGD 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 404 KYVRNADGSYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVpDQAGLTKTKAFVVLKP-GAQVSETELKAF 482
Cdd:cd12114 366 LGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVL-GDPGGKRLAAFVVPDNdGTPIAPDALRAF 444
|
490 500 510
....*....|....*....|....*....|...
gi 1920939256 483 VKERLAPYKYPRIIEFMDALPKTATGKIQRFRL 515
Cdd:cd12114 445 LAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
26-517 |
5.63e-54 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 189.70 E-value: 5.63e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 26 QRPGKTA-YIDDHGTMRYGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLLTADDYA 104
Cdd:PRK07514 14 ADRDAPFiETPDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 105 YMLQHSRAQAVLVSGALLPVLRQAMAQGGHEAATVIVSRPAGPLPDGmiALEAwiernAPLAAPASTGPDDPGFWLYSSG 184
Cdd:PRK07514 94 YFIGDAEPALVVCDPANFAWLSKIAAAAGAPHVETLDADGTGSLLEA--AAAA-----PDDFETVPRGADDLAAILYTSG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 185 STGRPKGVLHSQGNPYWTAELYAKpVLSLGEADICFSAAKLYFAYGLGNALTFPLSVGATVVLMAeRPTPEATFRrWLDy 264
Cdd:PRK07514 167 TTGRSKGAMLSHGNLLSNALTLVD-YWRFTPDDVLIHALPIFHTHGLFVATNVALLAGASMIFLP-KFDPDAVLA-LMP- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 265 QPTVFFGAPTGYAGMLAAPGLpTREQVS-LRLCSSAGEALPADLGERFTAHFGCEIIDGIGSTE--MLhifLSNrP--GQ 339
Cdd:PRK07514 243 RATVMMGVPTFYTRLLQEPRL-TREAAAhMRLFISGSAPLLAETHREFQERTGHAILERYGMTEtnMN---TSN-PydGE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 340 VRYGTTGWPVPGyaVELR---DEDGHAVPDGDVGDLYIQGPSAALMYWGNREKSRETFRG-GWTKSGDKYVRNADGSYSY 415
Cdd:PRK07514 318 RRAGTVGFPLPG--VSLRvtdPETGAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRAdGFFITGDLGKIDERGYVHI 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 416 AGRSDDmLKVSGIY-VSPFEVEATLAQHPAILEAAVIGVPD----QAGLtktkAFVVLKPGAQVSETELKAFVKERLAPY 490
Cdd:PRK07514 396 VGRGKD-LIISGGYnVYPKEVEGEIDELPGVVESAVIGVPHpdfgEGVT----AVVVPKPGAALDEAAILAALKGRLARF 470
|
490 500
....*....|....*....|....*..
gi 1920939256 491 KYPRIIEFMDALPKTATGKIQRFRLRE 517
Cdd:PRK07514 471 KQPKRVFFVDELPRNTMGKVQKNLLRE 497
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
23-518 |
8.53e-53 |
|
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: 189.06 E-value: 8.53e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 23 CNAQRPGKTAYIDDHG------TMRYGELAERIRRVAGALQASGIHREERVLLLMhdgndwPvcflgamyagIVPVAVNT 96
Cdd:cd05967 60 VEAGRGDQIALIYDSPvtgterTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYM------P----------MIPEAAIA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 97 LL----------------TADDYAYMLQHsrAQAVLVSGA-----------LLPVLRQAMAQGGHEAATVIVSR----PA 145
Cdd:cd05967 124 MLacarigaihsvvfggfAAKELASRIDD--AKPKLIVTAscgiepgkvvpYKPLLDKALELSGHKPHHVLVLNrpqvPA 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 146 GPLPDGMIALEAWIERNAPLAAPASTGPDDPGFWLYSSGSTGRPKGVLHSQGNpYWTAELYA-KPVLSLGEADICFSAAK 224
Cdd:cd05967 202 DLTKPGRDLDWSELLAKAEPVDCVPVAATDPLYILYTSGTTGKPKGVVRDNGG-HAVALNWSmRNIYGIKPGDVWWAASD 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 225 L-------YFAYGlgnaltfPLSVGATVVLMAERPT----PEATFRRWLDYQPTVFFGAPTGYAGMLAAPglPTREQV-- 291
Cdd:cd05967 281 VgwvvghsYIVYG-------PLLHGATTVLYEGKPVgtpdPGAFWRVIEKYQVNALFTAPTAIRAIRKED--PDGKYIkk 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 292 ----SLRLCSSAGEALPADLGERFTAHFGCEIIDGIGSTEMLHIFLSNRPGQ----VRYGTTGWPVPGYAVELRDEDGHA 363
Cdd:cd05967 352 ydlsSLRTLFLAGERLDPPTLEWAENTLGVPVIDHWWQTETGWPITANPVGLeplpIKAGSPGKPVPGYQVQVLDEDGEP 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 364 VPDGDVGDLYIQGP---SAALMYWGNREKSRETFRG---GWTKSGDKYVRNADGSYSYAGRSDDMLKVSGIYVSPFEVEA 437
Cdd:cd05967 432 VGPNELGNIVIKLPlppGCLLTLWKNDERFKKLYLSkfpGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEE 511
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 438 TLAQHPAILEAAVIGVPDQAGLTKTKAFVVLKPGAQVS----ETELKAFVKERLAPYKYPRIIEFMDALPKTATGKIQRF 513
Cdd:cd05967 512 SVLSHPAVAECAVVGVRDELKGQVPLGLVVLKEGVKITaeelEKELVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRR 591
|
....*
gi 1920939256 514 RLREM 518
Cdd:cd05967 592 TLRKI 596
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
175-512 |
2.86e-52 |
|
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: 180.54 E-value: 2.86e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 175 DPGFWLYSSGSTGRPKGVLHSQGNpYWTAELYAKPVLSLGEADICFSAAKLYFAYGLGNALTFpLSVGATVVLMaERPTP 254
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGN-LIAANLQLIHAMGLTEADVYLNMLPLFHIAGLNLALAT-FHAGGANVVM-EKFDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 255 EATFRRWLDYQPTVFFGAPTGYAGMLAAPGLPTREQVSLRLCSsaGEALPADLgERFTAHFGCEIIDGIGSTEMlHIFLS 334
Cdd:cd17637 78 AEALELIEEEKVTLMGSFPPILSNLLDAAEKSGVDLSSLRHVL--GLDAPETI-QRFEETTGATFWSLYGQTET-SGLVT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 335 NRPGQVRYGTTGWPVPGYAVELRDEDGHAVPDGDVGDLYIQGPSAALMYWGNREKSRETFRGGWTKSGDKYVRNADGSYS 414
Cdd:cd17637 154 LSPYRERPGSAGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTFRNGWHHTGDLGRFDEDGYLW 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 415 YAGRS--DDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQAGLTKTKAFVVLKPGAQVSETELKAFVKERLAPYKY 492
Cdd:cd17637 234 YAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKPGATLTADELIEFVGSRIARYKK 313
|
330 340
....*....|....*....|
gi 1920939256 493 PRIIEFMDALPKTATGKIQR 512
Cdd:cd17637 314 PRYVVFVEALPKTADGSIDR 333
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
25-515 |
3.57e-52 |
|
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: 184.33 E-value: 3.57e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 25 AQRPGKTAYIDDHGTMRYGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLLTADDYA 104
Cdd:cd12117 8 ARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAERLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 105 YMLQHSRAQAVLVSGALLPvlrqamaqggheaatvivsRPAGPLPDGMIaLEAWIERNAPLAAPAStGPDDPGFWLYSSG 184
Cdd:cd12117 88 FMLADAGAKVLLTDRSLAG-------------------RAGGLEVAVVI-DEALDAGPAGNPAVPV-SPDDLAYVMYTSG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 185 STGRPKGVLHSQ-------GNPYWtaelyakpvLSLGEADICFSAAKLYFayglgNALTF----PLSVGATVVLMA-ERP 252
Cdd:cd12117 147 STGRPKGVAVTHrgvvrlvKNTNY---------VTLGPDDRVLQTSPLAF-----DASTFeiwgALLNGARLVLAPkGTL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 253 TPEATFRRWLDYQ-PTVFFgAPTGYAGMLAApglpTREQV--SLRLCSSAGEALPADLGERF-TAHFGCEIIDGIGSTEM 328
Cdd:cd12117 213 LDPDALGALIAEEgVTVLW-LTAALFNQLAD----EDPECfaGLRELLTGGEVVSPPHVRRVlAACPGLRLVNGYGPTEN 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 329 LHIFLSNRPGQVRYGTT----GWPVPGYAVELRDEDGHAVPDGDVGDLYIQGPSAALMYWGNREKSRETF-------RGG 397
Cdd:cd12117 288 TTFTTSHVVTELDEVAGsipiGRPIANTRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFvadpfgpGER 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 398 WTKSGDKYVRNADGSYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQAGLTKTKAFVVlkPGAQVSET 477
Cdd:cd12117 368 LYRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVV--AEGALDAA 445
|
490 500 510
....*....|....*....|....*....|....*...
gi 1920939256 478 ELKAFVKERLAPYKYPRIIEFMDALPKTATGKIQRFRL 515
Cdd:cd12117 446 ELRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
39-519 |
3.70e-52 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 187.47 E-value: 3.70e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 39 TMRYGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVpVAVNTLLTADDYAYMLQHSRAQaVLVS 118
Cdd:PRK07529 58 TWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGEAAGIA-NPINPLLEPEQIAELLRAAGAK-VLVT 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 119 GALLPVLR-----QAMAQGGHEAATVIVSRPAGPLPDGMIALEAWIERNAP-----------------LAAPASTGPDDP 176
Cdd:PRK07529 136 LGPFPGTDiwqkvAEVLAALPELRTVVEVDLARYLPGPKRLAVPLIRRKAHarildfdaelarqpgdrLFSGRPIGPDDV 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 177 GFWLYSSGSTGRPKGVLHSQGNPYWTAELYAKpVLSLGEADICFSAAKLYFAYGLGNALTFPLSVGATVVLmaerPTP-- 254
Cdd:PRK07529 216 AAYFHTGGTTGMPKLAQHTHGNEVANAWLGAL-LLGLGPGDTVFCGLPLFHVNALLVTGLAPLARGAHVVL----ATPqg 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 255 ---EATFRRWLD----YQPTVFFGAPTGYAGMLAAPgLPTREQVSLRLCSSAGEALPADLGERFTAHFGCEIIDGIGSTE 327
Cdd:PRK07529 291 yrgPGVIANFWKiverYRINFLSGVPTVYAALLQVP-VDGHDISSLRYALCGAAPLPVEVFRRFEAATGVRIVEGYGLTE 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 328 MLHIFLSNRP-GQVRYGTTGWPVPGYAVEL--RDEDGHAVPD---GDVGDLYIQGPSAALMYWGNREKSRETFRGGWTKS 401
Cdd:PRK07529 370 ATCVSSVNPPdGERRIGSVGLRLPYQRVRVviLDDAGRYLRDcavDEVGVLCIAGPNVFSGYLEAAHNKGLWLEDGWLNT 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 402 GDKYVRNADGSYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPD-QAGLTKTkAFVVLKPGAQVSETELK 480
Cdd:PRK07529 450 GDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPDaHAGELPV-AYVQLKPGASATEAELL 528
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1920939256 481 AFVKERLA-PYKYPRIIEFMDALPKTATGKIQRFRLREME 519
Cdd:PRK07529 529 AFARDHIAeRAAVPKHVRILDALPKTAVGKIFKPALRRDA 568
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
28-515 |
2.42e-51 |
|
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: 182.32 E-value: 2.42e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 28 PGKTAYIDDHGTMR--YGELAERIRRVAGALQASGIHREERVLLLMhdGNDWPVC--FLGAMYAGIVPVAVNTLLTADDY 103
Cdd:cd05923 15 PDACAIADPARGLRltYSELRARIEAVAARLHARGLRPGQRVAVVL--PNSVEAViaLLALHRLGAVPALINPRLKAAEL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 104 AYMLQHSRAQAVLVSGALLPVlrQAMAQGGHEAATVivsrpaGPLPDGMIAleawiERNAPLAAPASTGPDDPGFWLYSS 183
Cdd:cd05923 93 AELIERGEMTAAVIAVDAQVM--DAIFQSGVRVLAL------SDLVGLGEP-----ESAGPLIEDPPREPEQPAFVFYTS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 184 GSTGRPKGVLHSQGNPYWTAELYAKPV-LSLGEADICFSAAKLYFAYGLGNALTFPLSVGATVVLMAERPTPEATfrRWL 262
Cdd:cd05923 160 GTTGLPKGAVIPQRAAESRVLFMSTQAgLRHGRHNVVLGLMPLYHVIGFFAVLVAALALDGTYVVVEEFDPADAL--KLI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 263 D-YQPTVFFGAPTGYAGMLAAPGLPTREQVSLRLCSSAGEALPADLGERFTAHFGCEIIDGIGSTEMLHiFLSNRpgQVR 341
Cdd:cd05923 238 EqERVTSLFATPTHLDALAAAAEFAGLKLSSLRHVTFAGATMPDAVLERVNQHLPGEKVNIYGTTEAMN-SLYMR--DAR 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 342 YGTTGwpVPGYAVELR-----DEDGHAVPDGDVGDLYI--QGPSAALMYWGNREKSRETFRGGWTKSGDKYVRNADGSYS 414
Cdd:cd05923 315 TGTEM--RPGFFSEVRivrigGSPDEALANGEEGELIVaaAADAAFTGYLNQPEATAKKLQDGWYRTGDVGYVDPSGDVR 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 415 YAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQAGLTKTKAFVVLKPGaQVSETELKAFVKE-RLAPYKYP 493
Cdd:cd05923 393 ILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREG-TLSADELDQFCRAsELADFKRP 471
|
490 500
....*....|....*....|..
gi 1920939256 494 RIIEFMDALPKTATGKIQRFRL 515
Cdd:cd05923 472 RRYFFLDELPKNAMNKVLRRQL 493
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
21-523 |
1.69e-50 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 180.00 E-value: 1.69e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 21 IACNAQR-PGKTAYIDDHGTMR--YGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTL 97
Cdd:PRK09088 1 IAFHARLqPQRLAAVDLALGRRwtYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 98 LTADDYAYMLQhsRAQAVLVSGallpvlRQAMAQGGheaatvivsrpagPLPDGMIALEAWIERNAPLAAPaSTGPDDPG 177
Cdd:PRK09088 81 LSASELDALLQ--DAEPRLLLG------DDAVAAGR-------------TDVEDLAAFIASADALEPADTP-SIPPERVS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 178 FWLYSSGSTGRPKGVLHSQGNPYWTAELYAkpVLS-LGEADICFSAAKLYFAYGLGNALTFPLSVGATVvLMAERPTPEA 256
Cdd:PRK09088 139 LILFTSGTSGQPKGVMLSERNLQQTAHNFG--VLGrVDAHSSFLCDAPMFHIIGLITSVRPVLAVGGSI-LVSNGFEPKR 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 257 TFRRWLD--YQPTVFFGAPTGYAGMLAAPGLPTREQVSLRLCSSAGEALPADLGERFTAHfGCEIIDGIGSTEMLHIF-L 333
Cdd:PRK09088 216 TLGRLGDpaLGITHYFCVPQMAQAFRAQPGFDAAALRHLTALFTGGAPHAAEDILGWLDD-GIPMVDGFGMSEAGTVFgM 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 334 SNRPGQVR--YGTTGWPVPGYAVELRDEDGHAVPDGDVGDLYIQGPSAALMYWGNREKSRETFRG-GWTKSGDKYVRNAD 410
Cdd:PRK09088 295 SVDCDVIRakAGAAGIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFTGdGWFRTGDIARRDAD 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 411 GSYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQAGLTKTKAFVVLKPGAQVSETELKAFVKERLAPY 490
Cdd:PRK09088 375 GFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADGAPLDLERIRSHLSTRLAKY 454
|
490 500 510
....*....|....*....|....*....|...
gi 1920939256 491 KYPRIIEFMDALPKTATGKIQRFRLREMEGAPA 523
Cdd:PRK09088 455 KVPKHLRLVDALPRTASGKLQKARLRDALAAGR 487
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
27-517 |
2.06e-50 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 179.77 E-value: 2.06e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 27 RPGKTAYIDDHGTMRYGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLLTADDYAYM 106
Cdd:PRK03640 15 TPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 107 LQHSRAQAVLVSGALLPVLRqamaqgghEAATVIVSR-PAGPLPDGMIaLEAWiernaPLAAPASTgpddpgfwLYSSGS 185
Cdd:PRK03640 95 LDDAEVKCLITDDDFEAKLI--------PGISVKFAElMNGPKEEAEI-QEEF-----DLDEVATI--------MYTSGT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 186 TGRPKGVLHSQGNPYWTAelyAKPVLSLG--EADICFSAAKLYFAYGLgNALTFPLSVGATVVLMaERPTPEATFRRWLD 263
Cdd:PRK03640 153 TGKPKGVIQTYGNHWWSA---VGSALNLGltEDDCWLAAVPIFHISGL-SILMRSVIYGMRVVLV-EKFDAEKINKLLQT 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 264 YQPTVFFGAPTGYAGMLAApgLPTRE-QVSLRLCSSAGEALPADLGERFTAHfGCEIIDGIGSTEMLH--IFLSNRPGQV 340
Cdd:PRK03640 228 GGVTIISVVSTMLQRLLER--LGEGTyPSSFRCMLLGGGPAPKPLLEQCKEK-GIPVYQSYGMTETASqiVTLSPEDALT 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 341 RYGTTGWPVpgYAVELRDE-DGHAVPDGDVGDLYIQGPSAALMYWGNREKSRETFRGGWTKSGD-KYVrNADGSYSYAGR 418
Cdd:PRK03640 305 KLGSAGKPL--FPCELKIEkDGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQDGWFKTGDiGYL-DEEGFLYVLDR 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 419 SDDMLkVSG---IYvsPFEVEATLAQHPAILEAAVIGVPDQAGLTKTKAFVVLkpGAQVSETELKAFVKERLAPYKYPRI 495
Cdd:PRK03640 382 RSDLI-ISGgenIY--PAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVK--SGEVTEEELRHFCEEKLAKYKVPKR 456
|
490 500
....*....|....*....|..
gi 1920939256 496 IEFMDALPKTATGKIQRFRLRE 517
Cdd:PRK03640 457 FYFVEELPRNASGKLLRHELKQ 478
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
25-517 |
3.59e-50 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 180.33 E-value: 3.59e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 25 AQRPGKTAYIDDHGT-MRYGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLLTADDY 103
Cdd:PRK06087 34 RAMPDKIAVVDNHGAsYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAEL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 104 AYMLQHSRAQAVLV-----SGALLPVLRQAMAQGGHEAATVIVSRPAGPLPDgmIALEAWIERNAPLAAPASTGPDDPGF 178
Cdd:PRK06087 114 VWVLNKCQAKMFFAptlfkQTRPVDLILPLQNQLPQLQQIVGVDKLAPATSS--LSLSQIIADYEPLTTAITTHGDELAA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 179 WLYSSGSTGRPKGVLHSQGNPYWTAELYAKpVLSLGEADICFSAAKLYFAYGLGNALTFPLSVGATVVLMaERPTPEATF 258
Cdd:PRK06087 192 VLFTSGTEGLPKGVMLTHNNILASERAYCA-RLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVLL-DIFTPDACL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 259 RRWLDYQPTVFFGAPTGYAGMLAAPGLPTREQVSLRLCSSAGEALPADLGERFTAHfGCEIIDGIGSTEML-HIFLS-NR 336
Cdd:PRK06087 270 ALLEQQRCTCMLGATPFIYDLLNLLEKQPADLSALRFFLCGGTTIPKKVARECQQR-GIKLLSVYGSTESSpHAVVNlDD 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 337 PGQVRYGTTGWPVPGYAVELRDEDGHAVPDGDVGDLYIQGPSAALMYWGNREksrETFRG----GWTKSGDKYVRNADGS 412
Cdd:PRK06087 349 PLSRFMHTDGYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYLDEPE---LTARAldeeGWYYSGDLCRMDEAGY 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 413 YSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQAGLTKTKAFVVLKPGAQVSETE--LKAFVKERLAPY 490
Cdd:PRK06087 426 IKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVVLKAPHHSLTLEevVAFFSRKRVAKY 505
|
490 500
....*....|....*....|....*..
gi 1920939256 491 KYPRIIEFMDALPKTATGKIQRFRLRE 517
Cdd:PRK06087 506 KYPEHIVVIDKLPRTASGKIQKFLLRK 532
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
12-509 |
7.31e-50 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 179.31 E-value: 7.31e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 12 TPFNFAQHLIACNAQRPGKTAYIDDHGTMRYGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVP 91
Cdd:PRK07798 1 MAWNIADLFEAVADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 92 VAVNTLLTADDYAYMLQHSRAQAVLVSGALLPVLRQAMAQGGHEAATVIVSRPAG-PLPDGMIALEAWIERNAPLAAPAS 170
Cdd:PRK07798 81 VNVNYRYVEDELRYLLDDSDAVALVYEREFAPRVAEVLPRLPKLRTLVVVEDGSGnDLLPGAVDYEDALAAGSPERDFGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 171 TGPDDpGFWLYSSGSTGRPKGVLHSQ---------------GNPYWTAELYAKPVLSlGEADICFSAAKLYFAYGLGNAL 235
Cdd:PRK07798 161 RSPDD-LYLLYTGGTTGMPKGVMWRQedifrvllggrdfatGEPIEDEEELAKRAAA-GPGMRRFPAPPLMHGAGQWAAF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 236 TFPLSVGATVVLMAERPTPEATFRRWLDYQPTVFFGAPTGYAG-MLAApgLPTREQV---SLRLCSSAGEALPADLGERF 311
Cdd:PRK07798 239 AALFSGQTVVLLPDVRFDADEVWRTIEREKVNVITIVGDAMARpLLDA--LEARGPYdlsSLFAIASGGALFSPSVKEAL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 312 TAHF-GCEIIDGIGSTE---MLHIFLSNRPGQvrygtTGWPV--PGYAVELRDEDGHAVPDGDVGDLYI-QGPSAALMYW 384
Cdd:PRK07798 317 LELLpNVVLTDSIGSSEtgfGGSGTVAKGAVH-----TGGPRftIGPRTVVLDEDGNPVEPGSGEIGWIaRRGHIPLGYY 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 385 GNREKSRETFR--GG--WTKSGDKYVRNADGSYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQAGLT 460
Cdd:PRK07798 392 KDPEKTAETFPtiDGvrYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVPDERWGQ 471
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1920939256 461 KTKAFVVLKPGAQVSETELKAFVKERLAPYKYPRIIEFMDALPKTATGK 509
Cdd:PRK07798 472 EVVAVVQLREGARPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
39-516 |
1.92e-49 |
|
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: 179.61 E-value: 1.92e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 39 TMRYGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLLTADDYAYMLQHSRAQAVLVS 118
Cdd:cd05968 91 TLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKALITA 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 119 GA---------LLPVLRQAMAQGGHEAATVIVSRPAGPLPDGMIALEAWIE-RNAPLAAPASTGPDDPGFWLYSSGSTGR 188
Cdd:cd05968 171 DGftrrgrevnLKEEADKACAQCPTVEKVVVVRHLGNDFTPAKGRDLSYDEeKETAGDGAERTESEDPLMIIYTSGTTGK 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 189 PKGVLHSQGNPYWTAELYAKPVLSLGEADICFSAAKLyfAYGLGNALTF-PLSVGATVVLMAERPTPEATFRRWL---DY 264
Cdd:cd05968 251 PKGTVHVHAGFPLKAAQDMYFQFDLKPGDLLTWFTDL--GWMMGPWLIFgGLILGATMVLYDGAPDHPKADRLWRmveDH 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 265 QPTVFFGAPTGYAGMLAAPGLPTREQ--VSLRLCSSAGEALPADLGERFTAHFG---CEIIDGIGSTEMLHIFLSN---R 336
Cdd:cd05968 329 EITHLGLSPTLIRALKPRGDAPVNAHdlSSLRVLGSTGEPWNPEPWNWLFETVGkgrNPIINYSGGTEISGGILGNvliK 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 337 PgqVRYGTTGWPVPGYAVELRDEDGHAVPDgDVGDLYIQGPSAALM--YWGNREKSRET----FRGGWTKsGDKYVRNAD 410
Cdd:cd05968 409 P--IKPSSFNGPVPGMKADVLDESGKPARP-EVGELVLLAPWPGMTrgFWRDEDRYLETywsrFDNVWVH-GDFAYYDEE 484
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 411 GSYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQAGLTKTKAFVVLKPGAQVSET---ELKAFVKERL 487
Cdd:cd05968 485 GYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVLKPGVTPTEAlaeELMERVADEL 564
|
490 500
....*....|....*....|....*....
gi 1920939256 488 APYKYPRIIEFMDALPKTATGKIQRFRLR 516
Cdd:cd05968 565 GKPLSPERILFVKDLPKTRNAKVMRRVIR 593
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
16-515 |
8.16e-48 |
|
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: 172.51 E-value: 8.16e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 16 FAQHLIACNAQRPGKTAYIDDHGTMRYGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVN 95
Cdd:cd05920 17 LGDLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPVLAL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 96 TLLTADDYAYMLQHSRAQAVLVSGALLPVLRQAMAQggheaaTVIVSRPagplpdgmialeawiernaplaapastgpdD 175
Cdd:cd05920 97 PSHRRSELSAFCAHAEAVAYIVPDRHAGFDHRALAR------ELAESIP------------------------------E 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 176 PGFWLYSSGSTGRPKGVLHSQGNPYWTAElyakpvlslGEADIC-FSAAKLYFAyGLGNALTFPLS---------VGATV 245
Cdd:cd05920 141 VALFLLSGGTTGTPKLIPRTHNDYAYNVR---------ASAEVCgLDQDTVYLA-VLPAAHNFPLAcpgvlgtllAGGRV 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 246 VLmAERPTPEATFRRWLDYQPTVFFGAPTGYAGMLAAPGLPTREQVSLRLCSSAGEALPADLGERFTAHFGCEIIDGIGS 325
Cdd:cd05920 211 VL-APDPSPDAAFPLIEREGVTVTALVPALVSLWLDAAASRRADLSSLRLLQVGGARLSPALARRVPPVLGCTLQQVFGM 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 326 TEMLHIFLS-NRPGQVRYGTTGWPV-PGYAVELRDEDGHAVPDGDVGDLYIQGPSAALMYWGNREKSRETFRG-GWTKSG 402
Cdd:cd05920 290 AEGLLNYTRlDDPDEVIIHTQGRPMsPDDEIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPdGFYRTG 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 403 DKYVRNADGSYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQAGLTKTKAFVVLKPgAQVSETELKAF 482
Cdd:cd05920 370 DLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVLRD-PPPSAAQLRRF 448
|
490 500 510
....*....|....*....|....*....|....
gi 1920939256 483 VKER-LAPYKYPRIIEFMDALPKTATGKIQRFRL 515
Cdd:cd05920 449 LRERgLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
35-464 |
2.45e-47 |
|
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: 170.47 E-value: 2.45e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 35 DDHGTMRYGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLLTADDYAYMLQHSRAQA 114
Cdd:cd05907 1 GVWQPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 115 VLVSGallpvlrqamaqggheaatvivsrpagplpdgmialeawiernaplaapastgPDDPGFWLYSSGSTGRPKGVLH 194
Cdd:cd05907 81 LFVED-----------------------------------------------------PDDLATIIYTSGTTGRPKGVML 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 195 SQGNPYWTAELYAKPV-LSLGEADICFsaakLYFAYGLGN--ALTFPLSVGATVVLMAERPTPEATFRRwldYQPTVFFG 271
Cdd:cd05907 108 SHRNILSNALALAERLpATEGDRHLSF----LPLAHVFERraGLYVPLLAGARIYFASSAETLLDDLSE---VRPTVFLA 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 272 AP----TGYAGMLAAPGLPTREQV-------SLRLCSSAGEALPADLGeRFTAHFGCEIIDGIGSTEMLHIFLSNRPGQV 340
Cdd:cd05907 181 VPrvweKVYAAIKVKAVPGLKRKLfdlavggRLRFAASGGAPLPAELL-HFFRALGIPVYEGYGLTETSAVVTLNPPGDN 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 341 RYGTTGWPVPGyaVELRdedghavpDGDVGDLYIQGPSAALMYWGNREKSRETF-RGGWTKSGDKYVRNADGSYSYAGRS 419
Cdd:cd05907 260 RIGTVGKPLPG--VEVR--------IADDGEILVRGPNVMLGYYKNPEATAEALdADGWLHTGDLGEIDEDGFLHITGRK 329
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1920939256 420 DDMLKVS-GIYVSPFEVEATLAQHPAILEAAVIG----------VPDQAGLTKTKA 464
Cdd:cd05907 330 KDLIITSgGKNISPEPIENALKASPLISQAVVIGdgrpflvaliVPDPEALEAWAE 385
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
42-517 |
5.45e-47 |
|
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: 168.68 E-value: 5.45e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 42 YGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLLTADDYAYMLQHSRAQAvlvsgal 121
Cdd:cd05912 4 FAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVKL------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 122 lpvlrqamaqgghEAATVIvsrpagplpdgmialeawiernaplaapastgpddpgfwLYSSGSTGRPKGVLHSQGNPYW 201
Cdd:cd05912 77 -------------DDIATI---------------------------------------MYTSGTTGKPKGVQQTFGNHWW 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 202 TAelyAKPVLSLG--EADICFSAAKLYFAYGLgNALTFPLSVGATVVLMaERPTPEATFRRWLDYQPTVFFGAPTGYAGM 279
Cdd:cd05912 105 SA---IGSALNLGltEDDNWLCALPLFHISGL-SILMRSVIYGMTVYLV-DKFDAEQVLHLINSGKVTIISVVPTMLQRL 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 280 LAApgLPTREQVSLRLCSSAGEALPADLGERfTAHFGCEIIDGIGSTEMLHIFLSNRP--GQVRYGTTGWPVPGYAVELR 357
Cdd:cd05912 180 LEI--LGEGYPNNLRCILLGGGPAPKPLLEQ-CKEKGIPVYQSYGMTETCSQIVTLSPedALNKIGSAGKPLFPVELKIE 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 358 DEDGhavPDGDVGDLYIQGPSAALMYWGNREKSRETFRGGWTKSGDKYVRNADGS-YSYAGRSDdmLKVSG---IYvsPF 433
Cdd:cd05912 257 DDGQ---PPYEVGEILLKGPNVTKGYLNRPDATEESFENGWFKTGDIGYLDEEGFlYVLDRRSD--LIISGgenIY--PA 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 434 EVEATLAQHPAILEAAVIGVPDQAGLTKTKAFVVLKpgAQVSETELKAFVKERLAPYKYPRIIEFMDALPKTATGKIQRF 513
Cdd:cd05912 330 EIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSE--RPISEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRH 407
|
....
gi 1920939256 514 RLRE 517
Cdd:cd05912 408 ELKQ 411
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
28-518 |
6.24e-47 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 171.67 E-value: 6.24e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 28 PGKTAYIddHGTMRY--GELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLLTADDYAY 105
Cdd:PRK08162 32 PDRPAVI--HGDRRRtwAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAASIAF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 106 MLQHSRAQAVLVSGALLPVLRQAMAQGGHEAATVI-VSRPA--GPLPDGMIALEAWIERNAPLAAPasTGPDDPgfWL-- 180
Cdd:PRK08162 110 MLRHGEAKVLIVDTEFAEVAREALALLPGPKPLVIdVDDPEypGGRFIGALDYEAFLASGDPDFAW--TLPADE--WDai 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 181 ---YSSGSTGRPKGVL-HSQGnpywtAELyakpvlslgeadicfSAAKLYFAYGLG--------------NALTFPLSV- 241
Cdd:PRK08162 186 alnYTSGTTGNPKGVVyHHRG-----AYL---------------NALSNILAWGMPkhpvylwtlpmfhcNGWCFPWTVa 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 242 ---GATVVLmaERPTPEATFRRWLDYQPTVFFGAPTGYAGMLAAPGLPtREQVSLRLCS-SAGEALPADLGERfTAHFGC 317
Cdd:PRK08162 246 araGTNVCL--RKVDPKLIFDLIREHGVTHYCGAPIVLSALINAPAEW-RAGIDHPVHAmVAGAAPPAAVIAK-MEEIGF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 318 EIIDGIGSTEML-------------------HIFLSNRPGqVRYGTtgwpVPGYAVeLRDEDGHAVP-DGD-VGDLYIQG 376
Cdd:PRK08162 322 DLTHVYGLTETYgpatvcawqpewdalpldeRAQLKARQG-VRYPL----QEGVTV-LDPDTMQPVPaDGEtIGEIMFRG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 377 PSAALMYWGNREKSRETFRGGWTKSGDKYVRNADGSYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQ 456
Cdd:PRK08162 396 NIVMKGYLKNPKATEEAFAGGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDP 475
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1920939256 457 AGLTKTKAFVVLKPGAQVSETELKAFVKERLAPYKYPRIIEFmDALPKTATGKIQRFRLREM 518
Cdd:PRK08162 476 KWGEVPCAFVELKDGASATEEEIIAHCREHLAGFKVPKAVVF-GELPKTSTGKIQKFVLREQ 536
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
19-516 |
2.81e-46 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 171.09 E-value: 2.81e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 19 HLiacnAQRPGKTAYI---DDHGTMR---YGELAERIRRVAGALQASGIHREERVLLLM-------------------HD 73
Cdd:PRK00174 76 HL----KTRGDKVAIIwegDDPGDSRkitYRELHREVCRFANALKSLGVKKGDRVAIYMpmipeaavamlacarigavHS 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 74 gndwpVCFLG----AMYAGIVPVAVNTLLTADDyaymlQHSRAQAVlvsgALLPVLRQAMAQGGHEAATVIVSRPAGPLP 149
Cdd:PRK00174 152 -----VVFGGfsaeALADRIIDAGAKLVITADE-----GVRGGKPI----PLKANVDEALANCPSVEKVIVVRRTGGDVD 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 150 --DGMialEAWIERnapLAAPAST-------GPDDPGFWLYSSGSTGRPKGVLHSQGNpYwtaELYA----KPVLSLGEA 216
Cdd:PRK00174 218 wvEGR---DLWWHE---LVAGASDecepepmDAEDPLFILYTSGSTGKPKGVLHTTGG-Y---LVYAamtmKYVFDYKDG 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 217 DICFSAAKL-------YFAYGlgnaltfPLSVGATVVLMAERPT-PEATfrRWLD----YQPTVFFGAPTGY-AGMLAAP 283
Cdd:PRK00174 288 DVYWCTADVgwvtghsYIVYG-------PLANGATTLMFEGVPNyPDPG--RFWEvidkHKVTIFYTAPTAIrALMKEGD 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 284 GLPTREQV-SLRLCSSAGEALPADLGERFTAHFG---CEIIDGIGSTEMLHIFLSNRPGQVRY--GTTGWPVPGYAVELR 357
Cdd:PRK00174 359 EHPKKYDLsSLRLLGSVGEPINPEAWEWYYKVVGgerCPIVDTWWQTETGGIMITPLPGATPLkpGSATRPLPGIQPAVV 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 358 DEDGHAVPDGDVGDLYIQGPSAALM--YWGNREKSRET----FRGGWTkSGDKYVRNADGSYSYAGRSDDMLKVSGIYVS 431
Cdd:PRK00174 439 DEEGNPLEGGEGGNLVIKDPWPGMMrtIYGDHERFVKTyfstFKGMYF-TGDGARRDEDGYYWITGRVDDVLNVSGHRLG 517
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 432 PFEVEATLAQHPAILEAAVIGVPDQagltkTK-----AFVVLKPGAQVSE---TELKAFVKERLAPYKYPRIIEFMDALP 503
Cdd:PRK00174 518 TAEIESALVAHPKVAEAAVVGRPDD-----IKgqgiyAFVTLKGGEEPSDelrKELRNWVRKEIGPIAKPDVIQFAPGLP 592
|
570
....*....|...
gi 1920939256 504 KTATGKIQRFRLR 516
Cdd:PRK00174 593 KTRSGKIMRRILR 605
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
25-517 |
5.14e-46 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 169.29 E-value: 5.14e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 25 AQRPgktAYIDDHGTMRYGELAERIRRVA----GALQasgIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLLTA 100
Cdd:PRK08751 39 ADRP---AYHSFGKTITYREADQLVEQFAayllGELQ---LKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 101 DDYAYMLQHSRAQAVLVSGALLPVLRQAMAQ---------------GGHEAATV--IVSRPAGPLPDGMI--------AL 155
Cdd:PRK08751 113 RELKHQLIDSGASVLVVIDNFGTTVQQVIADtpvkqvittglgdmlGFPKAALVnfVVKYVKKLVPEYRIngairfreAL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 156 EAWIERNAPlaaPASTGPDDPGFWLYSSGSTGRPKGVLHSQGNPYWTAELYAKPVLSLGE----ADICFSAAKLYFAYGL 231
Cdd:PRK08751 193 ALGRKHSMP---TLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQWLAGTGKleegCEVVITALPLYHIFAL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 232 -GNALTFpLSVGATVVLMAErPTPEATFRRWLDYQP-TVFFGAPTGYAGMLAAPGLPTREQVSLRLCSSAGEALPADLGE 309
Cdd:PRK08751 270 tANGLVF-MKIGGCNHLISN-PRDMPGFVKELKKTRfTAFTGVNTLFNGLLNTPGFDQIDFSSLKMTLGGGMAVQRSVAE 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 310 RFTAHFGCEIIDGIGSTEMLHIFLSNRPGQVRY-GTTGWPVPGYAVELRDEDGHAVPDGDVGDLYIQGPSAALMYWGNRE 388
Cdd:PRK08751 348 RWKQVTGLTLVEAYGLTETSPAACINPLTLKEYnGSIGLPIPSTDACIKDDAGTVLAIGEIGELCIKGPQVMKGYWKRPE 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 389 KSRETFRG-GWTKSGDKYVRNADGSYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQAGLTKTKAFVV 467
Cdd:PRK08751 428 ETAKVMDAdGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEIVKVVIV 507
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1920939256 468 LKPGAQVSEtELKAFVKERLAPYKYPRIIEFMDALPKTATGKIQRFRLRE 517
Cdd:PRK08751 508 KKDPALTAE-DVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRRELRD 556
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
39-516 |
5.91e-46 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 167.88 E-value: 5.91e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 39 TMRYGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLLTADDYAYMLQHSRAQAVLVS 118
Cdd:PRK13390 24 QVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYIVGDSGARVLVAS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 119 GALlpvlrqamaqggheaaTVIVSRPAGPLP---------DGMIALEAWIERNAPLAAPASTGpddpGFWLYSSGSTGRP 189
Cdd:PRK13390 104 AAL----------------DGLAAKVGADLPlrlsfggeiDGFGSFEAALAGAGPRLTEQPCG----AVMLYSSGTTGFP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 190 KGV--------LHSQGNPYWTAelyAKPVLSLGEADICFSAAKLYFAYGLgNALTFPLSVGATVVLmAERPTPEATFRRW 261
Cdd:PRK13390 164 KGIqpdlpgrdVDAPGDPIVAI---ARAFYDISESDIYYSSAPIYHAAPL-RWCSMVHALGGTVVL-AKRFDAQATLGHV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 262 LDYQPTVFFGAPTGYAGMLAAPG-LPTREQV-SLRLCSSAGEALPADLGERFTAHFGCEIIDGIGSTEMLHIFLSNRPGQ 339
Cdd:PRK13390 239 ERYRITVTQMVPTMFVRLLKLDAdVRTRYDVsSLRAVIHAAAPCPVDVKHAMIDWLGPIVYEYYSSTEAHGMTFIDSPDW 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 340 VRY-GTTGWPVPGyAVELRDEDGHAVPDGDVGDLYIQGPSAALMYWGNREKSRETFRGG---WTKSGDKYVRNADGSYSY 415
Cdd:PRK13390 319 LAHpGSVGRSVLG-DLHICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAAAQHPAhpfWTTVGDLGSVDEDGYLYL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 416 AGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQAGLTKTKAFVVLKPGAQVSET---ELKAFVKERLAPYKY 492
Cdd:PRK13390 398 ADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLVEGIRGSDElarELIDYTRSRIAHYKA 477
|
490 500
....*....|....*....|....
gi 1920939256 493 PRIIEFMDALPKTATGKIQRFRLR 516
Cdd:PRK13390 478 PRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
28-516 |
6.16e-46 |
|
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: 166.77 E-value: 6.16e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 28 PGKTAYIDDHGTMRYGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLLTADDYAYML 107
Cdd:cd17649 1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 108 QHSRAQAVLvsgallpvlrqamAQGGHEAATVIvsrpagplpdgmialeawiernaplaapastgpddpgfwlYSSGSTG 187
Cdd:cd17649 81 EDSGAGLLL-------------THHPRQLAYVI----------------------------------------YTSGSTG 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 188 RPKGVLHSQGnpywtaELYAKPVLSLGEADICFSAAKLYFAyglgnALTF---------PLSVGATVVLMAERP-TPEAT 257
Cdd:cd17649 108 TPKGVAVSHG------PLAAHCQATAERYGLTPGDRELQFA-----SFNFdgaheqllpPLICGACVVLRPDELwASADE 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 258 FRRWLDYQPTVFFGAPTGYAGMLA--APGLPTREQVSLRLCSSAGEALPADLGERfTAHFGCEIIDGIGSTE--MLHIFL 333
Cdd:cd17649 177 LAEMVRELGVTVLDLPPAYLQQLAeeADRTGDGRPPSLRLYIFGGEALSPELLRR-WLKAPVRLFNAYGPTEatVTPLVW 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 334 SNRPGQVRYGTT---GWPVPGYAVELRDEDGHAVPDGDVGDLYIQGPSAALMYWGNREKSRETF-------RGG-WTKSG 402
Cdd:cd17649 256 KCEAGAARAGASmpiGRPLGGRSAYILDADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFvpdpfgaPGSrLYRTG 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 403 DKYVRNADGSYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQAGlTKTKAFVVLKPGAQVSET--ELK 480
Cdd:cd17649 336 DLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAGG-KQLVAYVVLRAAAAQPELraQLR 414
|
490 500 510
....*....|....*....|....*....|....*.
gi 1920939256 481 AFVKERLAPYKYPRIIEFMDALPKTATGKIQRFRLR 516
Cdd:cd17649 415 TALRASLPDYMVPAHLVFLARLPLTPNGKLDRKALP 450
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
180-512 |
7.54e-46 |
|
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: 163.44 E-value: 7.54e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 180 LYSSGSTGRPKGVL--HSQgnpywTAELYAK--PVLSLGEADICFSAAKLYFAYGLGNALTFPLSVGATVVLMAERpTPE 255
Cdd:cd17638 6 MFTSGTTGRSKGVMcaHRQ-----TLRAAAAwaDCADLTEDDRYLIINPFFHTFGYKAGIVACLLTGATVVPVAVF-DVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 256 ATFRRWLDYQPTVFFGAPTGYAGMLAAPGLPTREQVSLRLCSSAGEALPADLGERFTAHFGCEII-DGIGSTEMLHIFLS 334
Cdd:cd17638 80 AILEAIERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFETVlTAYGLTEAGVATMC 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 335 nRPGQ--VRYGTT-GWPVPGYAVELrdedghavpdGDVGDLYIQGPSAALMYWGNREKSRETFRG-GWTKSGDKYVRNAD 410
Cdd:cd17638 160 -RPGDdaETVATTcGRACPGFEVRI----------ADDGEVLVRGYNVMQGYLDDPEATAEAIDAdGWLHTGDVGELDER 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 411 GSYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQAGLTKTKAFVVLKPGAQVSETELKAFVKERLAPY 490
Cdd:cd17638 229 GYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGVTLTEEDVIAWCRERLANY 308
|
330 340
....*....|....*....|..
gi 1920939256 491 KYPRIIEFMDALPKTATGKIQR 512
Cdd:cd17638 309 KVPRFVRFLDELPRNASGKVMK 330
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
28-512 |
3.20e-43 |
|
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: 158.96 E-value: 3.20e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 28 PGKTAYIDDHGTMRYGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLLTADDYAYML 107
Cdd:cd17652 1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 108 QHSRAQAVLvsgallpvlrqamaqggheaatvivsrpagplpdgmialeawiernaplaapasTGPDDPGFWLYSSGSTG 187
Cdd:cd17652 81 ADARPALLL------------------------------------------------------TTPDNLAYVIYTSGSTG 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 188 RPKGVL--HSqGNPYWTAELYAKpvLSLGEADICFSAAKLYF---AYGLGNALTfplsVGATVVLM-AERPTPEATFRRW 261
Cdd:cd17652 107 RPKGVVvtHR-GLANLAAAQIAA--FDVGPGSRVLQFASPSFdasVWELLMALL----AGATLVLApAEELLPGEPLADL 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 262 LDYQPTVFFGAPTGYAGMLAAPGLPtreqvSLRLCSSAGEALPADLGERFTAhfGCEIIDGIGSTEM---LHIFLSNRPG 338
Cdd:cd17652 180 LREHRITHVTLPPAALAALPPDDLP-----DLRTLVVAGEACPAELVDRWAP--GRRMINAYGPTETtvcATMAGPLPGG 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 339 QVRygTTGWPVPGYAVELRDEDGHAVPDGDVGDLYIQGPSAALMYWGNREKSRETF-------RGG-WTKSGDKYVRNAD 410
Cdd:cd17652 253 GVP--PIGRPVPGTRVYVLDARLRPVPPGVPGELYIAGAGLARGYLNRPGLTAERFvadpfgaPGSrMYRTGDLARWRAD 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 411 GSYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQAGLTKTKAFVVLKPGAQVSETELKAFVKERLAPY 490
Cdd:cd17652 331 GQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAPGAAPTAAELRAHLAERLPGY 410
|
490 500
....*....|....*....|..
gi 1920939256 491 KYPRIIEFMDALPKTATGKIQR 512
Cdd:cd17652 411 MVPAAFVVLDALPLTPNGKLDR 432
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
343-508 |
3.60e-43 |
|
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: 156.31 E-value: 3.60e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 343 GTTGWPVPGYAVELRDEDGHAVPDGDVGDLYIQGPSAALMYWGNREKSRETFRGGWTKSGDKYVRNADGSYSYAGRSDDM 422
Cdd:cd17636 163 GGAGRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRTRGGWHHTNDLGRREPDGSLSFVGPKTRM 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 423 LK--VSGIYvsPFEVEATLAQHPAILEAAVIGVPDQAGLTKTKAFVVLKPGAQVSETELKAFVKERLAPYKYPRIIEFMD 500
Cdd:cd17636 243 IKsgAENIY--PAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPGASVTEAELIEHCRARIASYKKPKSVEFAD 320
|
....*...
gi 1920939256 501 ALPKTATG 508
Cdd:cd17636 321 ALPRTAGG 328
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
25-518 |
8.28e-43 |
|
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: 160.00 E-value: 8.28e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 25 AQRPGKTAYIDDHG--TMRYGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLLTADD 102
Cdd:cd17642 28 ASVPGTIAFTDAHTgvNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 103 YAYMLQHSRAQAVLVSGALLPvlRQAMAQGGHEAATVIVSRPAGPLPDGMIALEAWIERNAPLA-------APASTGPDD 175
Cdd:cd17642 108 LDHSLNISKPTIVFCSKKGLQ--KVLNVQKKLKIIKTIIILDSKEDYKGYQCLYTFITQNLPPGfneydfkPPSFDRDEQ 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 176 PGFWLYSSGSTGRPKGVLHSQGNPYWTAELYAKPVL--SLGEADICFSAAKLYFAYGLGNALTFpLSVGATVVLMAErpT 253
Cdd:cd17642 186 VALIMNSSGSTGLPKGVQLTHKNIVARFSHARDPIFgnQIIPDTAILTVIPFHHGFGMFTTLGY-LICGFRVVLMYK--F 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 254 PEATFRRWL-DYQPTVFFGAPTGYAGMLAAPGLPTREQVSLRLCSSAGEALPADLGERFTAHFGCEII-DGIGSTEMLHI 331
Cdd:cd17642 263 EEELFLRSLqDYKVQSALLVPTLFAFFAKSTLVDKYDLSNLHEIASGGAPLSKEVGEAVAKRFKLPGIrQGYGLTETTSA 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 332 FLSNRPGQVRYGTTGWPVPGYAVELRDED-GHAVPDGDVGDLYIQGPSAALMYWGNREKSRETF-RGGWTKSGDKYVRNA 409
Cdd:cd17642 343 ILITPEGDDKPGAVGKVVPFFYAKVVDLDtGKTLGPNERGELCVKGPMIMKGYVNNPEATKALIdKDGWLHSGDIAYYDE 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 410 DGSYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQAGLTKTKAFVVLKPGAQVSETELKAFVKERLAP 489
Cdd:cd17642 423 DGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVVLEAGKTMTEKEVMDYVASQVST 502
|
490 500 510
....*....|....*....|....*....|
gi 1920939256 490 YKYPR-IIEFMDALPKTATGKIQRFRLREM 518
Cdd:cd17642 503 AKRLRgGVKFVDEVPKGLTGKIDRRKIREI 532
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
1-512 |
2.01e-42 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 158.90 E-value: 2.01e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 1 MTAEPQVQPPGTPF--NFAQHLIACNAQRPGKTAYI--DDHGTMRYGELAERIRRVAGALQASGIHREERVLLLMHDGND 76
Cdd:PRK05852 1 MRFMGGAAPMASDFgpRIADLVEVAATRLPEAPALVvtADRIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 77 WPVCFLGAMYAGIVPVAVNTLLTADDYAYMLQHSRAQAVLVSGalLPVLRQAMAQGGHEAATVIVSRPAGPLPDGM-IAL 155
Cdd:PRK05852 81 FVVALLAASRADLVVVPLDPALPIAEQRVRSQAAGARVVLIDA--DGPHDRAEPTTRWWPLTVNVGGDSGPSGGTLsVHL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 156 EAWIERNAPLAAPASTGPDDpGFWLYSSGSTGRPKGVlhsqgnPyWTAELYAKPVLS------LGEADICFSAAKLYFAY 229
Cdd:PRK05852 159 DAATEPTPATSTPEGLRPDD-AMIMFTGGTTGLPKMV------P-WTHANIASSVRAiitgyrLSPRDATVAVMPLYHGH 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 230 GLGNALTFPLSVGATVVLMAERPTPEATFrrWLDYQ---PTVFFGAPTGYAGML--AAPGLPTREQVSLRLCSSAGEALP 304
Cdd:PRK05852 231 GLIAALLATLASGGAVLLPARGRFSAHTF--WDDIKavgATWYTAVPTIHQILLerAATEPSGRKPAALRFIRSCSAPLT 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 305 ADLGERFTAHFGCEIIDGIGSTEMLHIFLSNRPGQVRYG-----TTGWPVPGYAVELR--DEDGHAVPDGDVGDLYIQGP 377
Cdd:PRK05852 309 AETAQALQTEFAAPVVCAFGMTEATHQVTTTQIEGIGQTenpvvSTGLVGRSTGAQIRivGSDGLPLPAGAVGEVWLRGT 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 378 SAALMYWGNREKSRETFRGGWTKSGDKYVRNADGSYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQA 457
Cdd:PRK05852 389 TVVRGYLGDPTITAANFTDGWLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQL 468
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1920939256 458 GLTKTKAFVVLKPGAQVSETELKAFVKERLAPYKYPRIIEFMDALPKTATGKIQR 512
Cdd:PRK05852 469 YGEAVAAVIVPRESAPPTAEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDR 523
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
173-516 |
5.83e-42 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 153.79 E-value: 5.83e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 173 PDDPGFWLYSSGSTGRPKGVLHSQGNPYWTAELYAKPVLSlGEADICFSAAKLYFAYGLGNALTFPLSVGATVVLMA--- 249
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLF-DPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVVLAGpag 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 250 -ERPTPEATFRRWLD-YQPTVFFGAPTGYAGMLAAPGlpTREQVSLRLCSSAGEALPADLGERFTAHFGCEIIDGIGSTE 327
Cdd:cd05944 80 yRNPGLFDNFWKLVErYRITSLSTVPTVYAALLQVPV--NADISSLRFAMSGAAPLPVELRARFEDATGLPVVEGYGLTE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 328 MLHIFLSNRP-GQVRYGTTGWPVPGYAVELR--DEDGHAVPD---GDVGDLYIQGPSAALMYWGNREKSRETFRGGWTKS 401
Cdd:cd05944 158 ATCLVAVNPPdGPKRPGSVGLRLPYARVRIKvlDGVGRLLRDcapDEVGEICVAGPGVFGGYLYTEGNKNAFVADGWLNT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 402 GDKYVRNADGSYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQAGLTKTKAFVVLKPGAQVSETELKA 481
Cdd:cd05944 238 GDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPGAVVEEEELLA 317
|
330 340 350
....*....|....*....|....*....|....*.
gi 1920939256 482 FVKERLAPY-KYPRIIEFMDALPKTATGKIQRFRLR 516
Cdd:cd05944 318 WARDHVPERaAVPKHIEVLEELPVTAVGKVFKPALR 353
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
83-517 |
1.13e-41 |
|
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: 155.61 E-value: 1.13e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 83 GAMYAGIVPVAVNTLLTADDYAYMLQHSRAqavlvsgALLPVLRQAMAQggheAATVIVSRPAGP-LPDGMIALEAWIER 161
Cdd:cd05929 41 IADGVYIYLINSILTVFAAAAAWKCGACPA-------YKSSRAPRAEAC----AIIEIKAAALVCgLFTGGGALDGLEDY 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 162 NAPLAAPASTGPDD---PGFWLYSSGSTGRPKGVL-HSQGNPYWTAELYAKPVLS-LGEADICFSAAKLYFAYGLGNALT 236
Cdd:cd05929 110 EAAEGGSPETPIEDeaaGWKMLYSGGTTGRPKGIKrGLPGGPPDNDTLMAAALGFgPGADSVYLSPAPLYHAAPFRWSMT 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 237 fPLSVGATVVLMaERPTPEATFRRWLDYQPTVFFGAPTGYAGMLAAPG-LPTREQV-SLRLCSSAGEALPADLGERFTAH 314
Cdd:cd05929 190 -ALFMGGTLVLM-EKFDPEEFLRLIERYRVTFAQFVPTMFVRLLKLPEaVRNAYDLsSLKRVIHAAAPCPPWVKEQWIDW 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 315 FGCEIIDGIGSTEMLHIFLSNRPGQVRY-GTTGWPVPGyAVELRDEDGHAVPDGDVGDLYIQGPSAALM---YWGNREKS 390
Cdd:cd05929 268 GGPIIWEYYGGTEGQGLTIINGEEWLTHpGSVGRAVLG-KVHILDEDGNEVPPGEIGEVYFANGPGFEYtndPEKTAAAR 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 391 REtfrGGWTKSGDKYVRNADGSYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQAGLTKTKAFVVLKP 470
Cdd:cd05929 347 NE---GGWSTLGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVQPAP 423
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1920939256 471 GA---QVSETELKAFVKERLAPYKYPRIIEFMDALPKTATGKIQRFRLRE 517
Cdd:cd05929 424 GAdagTALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLRD 473
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
27-519 |
1.24e-41 |
|
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: 155.95 E-value: 1.24e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 27 RPGKTAYIDDHGTMRYGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLLTADDYAYM 106
Cdd:cd17655 10 TPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEERIQYI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 107 LQHSRAQAVLVSGALlpvlrqamAQGGHEAATVIVsrpagpLPDGMIAleawIERNAPLAAPAStgPDDPGFWLYSSGST 186
Cdd:cd17655 90 LEDSGADILLTQSHL--------QPPIAFIGLIDL------LDEDTIY----HEESENLEPVSK--SDDLAYVIYTSGST 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 187 GRPKGVL--HSQGNPYWTAelyAKPVLSLGEADICFSAAKLYFAYGLGNALTfPLSVGATVVLM-AERPTPEATFRRWL- 262
Cdd:cd17655 150 GKPKGVMieHRGVVNLVEW---ANKVIYQGEHLRVALFASISFDASVTEIFA-SLLSGNTLYIVrKETVLDGQALTQYIr 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 263 DYQPTVFFGAPTgYAGMLAAPGLptREQVSLRLCSSAGEALPADLGERFTAHFG--CEIIDGIGSTE-----MLHIFLSN 335
Cdd:cd17655 226 QNRITIIDLTPA-HLKLLDAADD--SEGLSLKHLIVGGEALSTELAKKIIELFGtnPTITNAYGPTEttvdaSIYQYEPE 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 336 RPGQVRYgTTGWPVPGYAVELRDEDGHAVPDGDVGDLYIQGPSAALMYWGNREKSRETFRGGWTKSGDKYVRNAD----- 410
Cdd:cd17655 303 TDQQVSV-PIGKPLGNTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVPGERMYRTGDlarwl 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 411 --GSYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQAGLTKTKAFVVLKPGAQVSetELKAFVKERLA 488
Cdd:cd17655 382 pdGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEKELPVA--QLREFLARELP 459
|
490 500 510
....*....|....*....|....*....|.
gi 1920939256 489 PYKYPRIIEFMDALPKTATGKIQRFRLREME 519
Cdd:cd17655 460 DYMIPSYFIKLDEIPLTPNGKVDRKALPEPD 490
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
26-518 |
2.09e-41 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 155.32 E-value: 2.09e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 26 QRPGKTAYIDDHGTMRYGELAERIRRVAGALQASGiHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLLTADDyay 105
Cdd:PRK07638 13 LQPNKIAIKENDRVLTYKDWFESVCKVANWLNEKE-SKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDE--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 106 mlqhsRAQAVLVSgallpvlrqamaqgghEAATVIVSR-PAGPLPDG---MIALEAW---IERNAPLAAPASTGPDDPGF 178
Cdd:PRK07638 89 -----LKERLAIS----------------NADMIVTERyKLNDLPDEegrVIEIDEWkrmIEKYLPTYAPIENVQNAPFY 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 179 WLYSSGSTGRPKGVLHSQGNpyWTAELY-AKPVLSLGEADICFSAAKL---YFAYGLGNALTFplsvGATVVLMaERPTP 254
Cdd:PRK07638 148 MGFTSGSTGKPKAFLRAQQS--WLHSFDcNVHDFHMKREDSVLIAGTLvhsLFLYGAISTLYV----GQTVHLM-RKFIP 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 255 EATFRRWLDYQPTVFFGAPTGYAGMLAAPGLPtrEQVsLRLCSSaGEALPADLGERFTAHF-GCEIIDGIGSTEMLHI-F 332
Cdd:PRK07638 221 NQVLDKLETENISVMYTVPTMLESLYKENRVI--ENK-MKIISS-GAKWEAEAKEKIKNIFpYAKLYEFYGASELSFVtA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 333 LSNRPGQVRYGTTGWPVPGYAVELRDEDGHAVPDGDVGDLYIQGPSAALMYWGNREKSRETFRGGWTKSGDKYVRNADGS 412
Cdd:PRK07638 297 LVDEESERRPNSVGRPFHNVQVRICNEAGEEVQKGEIGTVYVKSPQFFMGYIIGGVLARELNADGWMTVRDVGYEDEEGF 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 413 YSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQAGLTKTKAFVvlkpGAQVSETELKAFVKERLAPYKY 492
Cdd:PRK07638 377 IYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAII----KGSATKQQLKSFCLQRLSSFKI 452
|
490 500
....*....|....*....|....*.
gi 1920939256 493 PRIIEFMDALPKTATGKIQRFRLREM 518
Cdd:PRK07638 453 PKEWHFVDEIPYTNSGKIARMEAKSW 478
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
25-517 |
5.56e-41 |
|
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: 155.09 E-value: 5.56e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 25 AQRPGKTAY--IDDHG----TMRYGELAERIRRVAGALQASGIHREeRVLLLMHDGNDWPVCFLGAMYAGIVPVAV---N 95
Cdd:cd05931 4 AARPDRPAYtfLDDEGgreeTLTYAELDRRARAIAARLQAVGKPGD-RVLLLAPPGLDFVAAFLGCLYAGAIAVPLpppT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 96 TLLTADDYAYMLQHSRAQAVLVSGALLPVLRQamaqggheaatvIVSRPAGPLPDGMIALEAWIERNAPLAAPASTGPDD 175
Cdd:cd05931 83 PGRHAERLAAILADAGPRVVLTTAAALAAVRA------------FAASRPAAGTPRLLVVDLLPDTSAADWPPPSPDPDD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 176 PGFWLYSSGSTGRPKGVLHSQGNPYWTAELYAKpVLSLGEADICFSAAKLYFAYGLGNALTFPLSVGATVVLMA-----E 250
Cdd:cd05931 151 IAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRR-AYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGPSVLMSpaaflR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 251 RPtpeatfRRWL----DYQPTvFFGAPT-GYAgmLAAPGLpTREQV------SLRLCSSAGEALPADLGERFTAHF---- 315
Cdd:cd05931 230 RP------LRWLrlisRYRAT-ISAAPNfAYD--LCVRRV-RDEDLegldlsSWRVALNGAEPVRPATLRRFAEAFapfg 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 316 --------------------GCEIIDGIGSTEMLHIFLSNRPGQVRYGTT--------GWPVPGYAVELRDEDGHA-VPD 366
Cdd:cd05931 300 frpeafrpsyglaeatlfvsGGPPGTGPVVLRVDRDALAGRAVAVAADDPaarelvscGRPLPDQEVRIVDPETGReLPD 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 367 GDVGDLYIQGPSAALMYWGNREKSRETFR-------GGWTKSGD-KYVrnADGSYSYAGRSDDMLKVSG--IYvsPFEVE 436
Cdd:cd05931 380 GEVGEIWVRGPSVASGYWGRPEATAETFGalaatdeGGWLRTGDlGFL--HDGELYITGRLKDLIIVRGrnHY--PQDIE 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 437 ATLAQ-HPAILE--AAVIGVPDQAGLTKTKAFVVLKPGAQVSETELKAFVKERLA-----PykyPRIIEFM--DALPKTA 506
Cdd:cd05931 456 ATAEEaHPALRPgcVAAFSVPDDGEERLVVVAEVERGADPADLAAIAAAIRAAVArehgvA---PADVVLVrpGSIPRTS 532
|
570
....*....|.
gi 1920939256 507 TGKIQRFRLRE 517
Cdd:cd05931 533 SGKIQRRACRA 543
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
42-488 |
8.24e-41 |
|
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: 153.78 E-value: 8.24e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 42 YGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLLTADDYAYMLQHSRAQAVLVsGAL 121
Cdd:cd05932 9 WGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFV-GKL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 122 LPvlRQAMAQGGHEAatvIVSRPAgPLPDGMIALEAW---IERNAPLAAPASTGPDDPGFWLYSSGSTGRPKGVLHSQGN 198
Cdd:cd05932 88 DD--WKAMAPGVPEG---LISISL-PPPSAANCQYQWddlIAQHPPLEERPTRFPEQLATLIYTSGTTGQPKGVMLTFGS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 199 PYWTAELYAKpVLSLGEADICFS-------AAKLYFAYGL---GNALTFPLSVGaTVVLMAERPTPEATF---RRWLDYQ 265
Cdd:cd05932 162 FAWAAQAGIE-HIGTEENDRMLSylplahvTERVFVEGGSlygGVLVAFAESLD-TFVEDVQRARPTLFFsvpRLWTKFQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 266 PTVFFGAPTGYAGML---------------AAPGLptrEQVSLRLCSSAgeALPADLGERFTAhFGCEIIDGIGSTEMLH 330
Cdd:cd05932 240 QGVQDKIPQQKLNLLlkipvvnslvkrkvlKGLGL---DQCRLAGCGSA--PVPPALLEWYRS-LGLNILEAYGMTENFA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 331 IFLSNRPGQVRYGTTGWPVPGyaVELR-DEDGHavpdgdvgdlyIQGPSAALM--YWGNREKSRETFRG-GWTKSGDKYV 406
Cdd:cd05932 314 YSHLNYPGRDKIGTVGNAGPG--VEVRiSEDGE-----------ILVRSPALMmgYYKDPEATAEAFTAdGFLRTGDKGE 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 407 RNADGSYSYAGRSDDMLKVS-GIYVSPFEVEATLAQHPAILEAAVIGvpdqAGLTKTKAFVVLKPGAQV-----SETELK 480
Cdd:cd05932 381 LDADGNLTITGRVKDIFKTSkGKYVAPAPIENKLAEHDRVEMVCVIG----SGLPAPLALVVLSEEARLradafARAELE 456
|
....*...
gi 1920939256 481 AFVKERLA 488
Cdd:cd05932 457 ASLRAHLA 464
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
5-516 |
9.38e-41 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 154.61 E-value: 9.38e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 5 PQVQPPGTPFNFAQHLIACNAQRPGKTAYIDDHG--TMRYGELAERIRRVAGAL-QASGIHREERVLLLMHDGNDWPVCF 81
Cdd:PLN02574 30 PPVPLPSDPNLDAVSFIFSHHNHNGDTALIDSSTgfSISYSELQPLVKSMAAGLyHVMGVRQGDVVLLLLPNSVYFPVIF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 82 LGAMYAGIVPVAVNTLLTaddyaymLQHSRAQAVLVSGALLPVLRQAMAQGGHEAATVIVSRPAGPLPDGMIAL----EA 157
Cdd:PLN02574 110 LAVLSLGGIVTTMNPSSS-------LGEIKKRVVDCSVGLAFTSPENVEKLSPLGVPVIGVPENYDFDSKRIEFpkfyEL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 158 WIERNAPLAAPAsTGPDDPGFWLYSSGSTGRPKGVLHSQGNPYWTAELYAKPVLSLGEADIC----FSAAKLYFAYGLGN 233
Cdd:PLN02574 183 IKEDFDFVPKPV-IKQDDVAAIMYSSGTTGASKGVVLTHRNLIAMVELFVRFEASQYEYPGSdnvyLAALPMFHIYGLSL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 234 ALTFPLSVGATVVLMAERPTPE---ATFRRWLDYQPTVffgAPTGYAGMLAAPGLPTREQVSLRLCSSAGEALPADLGER 310
Cdd:PLN02574 262 FVVGLLSLGSTIVVMRRFDASDmvkVIDRFKVTHFPVV---PPILMALTKKAKGVCGEVLKSLKQVSCGAAPLSGKFIQD 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 311 FTAHFG-CEIIDGIGSTEMLHIFLS--NRPGQVRYGTTGWPVPGYAVELRD-EDGHAVPDGDVGDLYIQGPSAALMYWGN 386
Cdd:PLN02574 339 FVQTLPhVDFIQGYGMTESTAVGTRgfNTEKLSKYSSVGLLAPNMQAKVVDwSTGCLLPPGNCGELWIQGPGVMKGYLNN 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 387 REKSRETF-RGGWTKSGDKYVRNADGSYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQAGLTKTKAF 465
Cdd:PLN02574 419 PKATQSTIdKDGWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAF 498
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1920939256 466 VVLKPGAQVSETELKAFVKERLAPYKYPRIIEFMDALPKTATGKIQRFRLR 516
Cdd:PLN02574 499 VVRRQGSTLSQEAVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRRELK 549
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
63-517 |
1.77e-40 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 153.30 E-value: 1.77e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 63 REERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLLTADDYAYMLQHSRAQAVLVSGALLPVLRqamaqGGHEAATVIVs 142
Cdd:PRK07867 53 RPPHVGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARDIAHADCQLVLTESAHAELLD-----GLDPGVRVIN- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 143 rpagplpdgmIALEAWIERNAPLA----APASTGPDDPGFWLYSSGSTGRPKGVLHSQGNPYWTAELYAKPvLSLGEADI 218
Cdd:PRK07867 127 ----------VDSPAWADELAAHRdaepPFRVADPDDLFMLIFTSGTSGDPKAVRCTHRKVASAGVMLAQR-FGLGPDDV 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 219 CFSAAKLYFAYGLGNALTFPLSVGATVVLmaERPTPEATF----RRwldYQPTVF--FGAPTGYagMLAAPGLPTREQVS 292
Cdd:PRK07867 196 CYVSMPLFHSNAVMAGWAVALAAGASIAL--RRKFSASGFlpdvRR---YGATYAnyVGKPLSY--VLATPERPDDADNP 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 293 LRLcSSAGEALPADLgERFTAHFGCEIIDGIGSTEmLHIFLSNRPGqVRYGTTGWPVPGYAV-----------ELRDEDG 361
Cdd:PRK07867 269 LRI-VYGNEGAPGDI-ARFARRFGCVVVDGFGSTE-GGVAITRTPD-TPPGALGPLPPGVAIvdpdtgtecppAEDADGR 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 362 HAVPDGDVGDLY-IQGPSAALMYWGNREKSRETFRGGWTKSGDKYVRNADGSYSYAGRSDDMLKVSGIYVSPFEVEATLA 440
Cdd:PRK07867 345 LLNADEAIGELVnTAGPGGFEGYYNDPEADAERMRGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILL 424
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1920939256 441 QHPAILEAAVIGVPDQAGLTKTKAFVVLKPGAQVSETELKAFVKER--LAPYKYPRIIEFMDALPKTATGKIQRFRLRE 517
Cdd:PRK07867 425 RYPDATEVAVYAVPDPVVGDQVMAALVLAPGAKFDPDAFAEFLAAQpdLGPKQWPSYVRVCAELPRTATFKVLKRQLSA 503
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
17-522 |
2.22e-40 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 156.86 E-value: 2.22e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 17 AQHLIACNAQR-PGKTAYIDDHGTMRYGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVN 95
Cdd:PRK12467 514 VHQLIEAQARQhPERPALVFGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLD 593
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 96 TLLTADDYAYMLQHSRAQAVLVSGALLPVLrqamaqggheaatvivsrpagPLPDGMIAL-----EAWIERNAPLAAPAS 170
Cdd:PRK12467 594 PEYPQDRLAYMLDDSGVRLLLTQSHLLAQL---------------------PVPAGLRSLcldepADLLCGYSGHNPEVA 652
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 171 TGPDDPGFWLYSSGSTGRPKGVLHSQGNPY----WTAELYakpvlSLGEADICFSAAKLYFAYGlGNALTFPLSVGATVV 246
Cdd:PRK12467 653 LDPDNLAYVIYTSGSTGQPKGVAISHGALAnyvcVIAERL-----QLAADDSMLMVSTFAFDLG-VTELFGALASGATLH 726
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 247 LMAERPT--PEATFRRWLDYQPTVFFGAPTGYAGML--AAPGLPTReqvsLRLCSSAGEALPADLGER-FTAHFGCEIID 321
Cdd:PRK12467 727 LLPPDCArdAEAFAALMADQGVTVLKIVPSHLQALLqaSRVALPRP----QRALVCGGEALQVDLLARvRALGPGARLIN 802
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 322 GIGSTE----MLHIFLSNRPGQVRYGTTGWPVPGYAVELRDEDGHAVPDGDVGDLYIQGPSAALMYWGNREKSRETF--- 394
Cdd:PRK12467 803 HYGPTEttvgVSTYELSDEERDFGNVPIGQPLANLGLYILDHYLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFvpd 882
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 395 ----RGG-WTKSGDKYVRNADGSYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQAGLtKTKAFVVLK 469
Cdd:PRK12467 883 pfgaDGGrLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAGL-QLVAYLVPA 961
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1920939256 470 PGA-----QVSETELKAFVKERLAPYKYPRIIEFMDALPKTATGKIQRFRLREMEGAP 522
Cdd:PRK12467 962 AVAdgaehQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALPKPDASA 1019
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
42-518 |
2.28e-40 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 153.32 E-value: 2.28e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 42 YGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLLTADDYAYMLQHSRAQAVLVSGAL 121
Cdd:PRK07008 42 YRDCERRAKQLAQALAALGVEPGDRVGTLAWNGYRHLEAYYGVSGSGAVCHTINPRLFPEQIAYIVNHAEDRYVLFDLTF 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 122 LPVLRQAMAQ----GGHEAATVIVSRPAGPLPdgMIALEAWIERNAPLAAPASTGPDDPGFWLYSSGSTGRPKGVLHSQG 197
Cdd:PRK07008 122 LPLVDALAPQcpnvKGWVAMTDAAHLPAGSTP--LLCYETLVGAQDGDYDWPRFDENQASSLCYTSGTTGNPKGALYSHR 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 198 NPYWTAELYAKP-VLSLGEADICFSAAKLYFAYGLGNALTFPLsVGATVVLMAERPTPEATFRRWLDYQPTVFFGAPTGY 276
Cdd:PRK07008 200 STVLHAYGAALPdAMGLSARDAVLPVVPMFHVNAWGLPYSAPL-TGAKLVLPGPDLDGKSLYELIEAERVTFSAGVPTVW 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 277 AGMLA---APGLptrEQVSLRLCSSAGEALPADLGERFTAHFGCEIIDGIGSTEM--------LHIFLSNRPGQVRYG-- 343
Cdd:PRK07008 279 LGLLNhmrEAGL---RFSTLRRTVIGGSACPPAMIRTFEDEYGVEVIHAWGMTEMsplgtlckLKWKHSQLPLDEQRKll 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 344 -TTGWPVpgYAVELR--DEDGHAVP-DGDV-GDLYIQGPSAALMYWGNREksrETFRGGWTKSGDKYVRNADGSYSYAGR 418
Cdd:PRK07008 356 eKQGRVI--YGVDMKivGDDGRELPwDGKAfGDLQVRGPWVIDRYFRGDA---SPLVDGWFPTGDVATIDADGFMQITDR 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 419 SDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQAGLTKTKAFVVLKPGAQVSETELKAFVKERLAPYKYPRIIEF 498
Cdd:PRK07008 431 SKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLVVVKRPGAEVTREELLAFYEGKVAKWWIPDDVVF 510
|
490 500
....*....|....*....|
gi 1920939256 499 MDALPKTATGKIQRFRLREM 518
Cdd:PRK07008 511 VDAIPHTATGKLQKLKLREQ 530
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
25-515 |
2.32e-40 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 156.66 E-value: 2.32e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 25 AQRPGKTAYIDDHGTMRYGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLLTADDYA 104
Cdd:PRK12316 2014 ARAPEAIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLA 2093
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 105 YMLQHSRAQAVLVSGALLPVLrqamaqggheaatvivsrpagPLPDGMIALEawIERNAPLAAPASTGP------DDPGF 178
Cdd:PRK12316 2094 YMLEDSGAALLLTQRHLLERL---------------------PLPAGVARLP--LDRDAEWADYPDTAPavqlagENLAY 2150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 179 WLYSSGSTGRPKGVLHSQG----NPYWTAELYakpvlSLGEADICFSAAKLYFAyGLGNALTFPLSVGATVVLM-AERPT 253
Cdd:PRK12316 2151 VIYTSGSTGLPKGVAVSHGalvaHCQAAGERY-----ELSPADCELQFMSFSFD-GAHEQWFHPLLNGARVLIRdDELWD 2224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 254 PEATFRRWLDYQPTVfFGAPTGYAGMLAAPGLPTREQVSLRLCSSAGEALPADLGERFTAHFGCE-IIDGIGSTE----- 327
Cdd:PRK12316 2225 PEQLYDEMERHGVTI-LDFPPVYLQQLAEHAERDGRPPAVRVYCFGGEAVPAASLRLAWEALRPVyLFNGYGPTEavvtp 2303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 328 MLHIFLSNRPGQVRYGTTGWPVPGYAVELRDEDGHAVPDGDVGDLYIQGPSAALMYWGNREKSRETF-------RGG-WT 399
Cdd:PRK12316 2304 LLWKCRPQDPCGAAYVPIGRALGNRRAYILDADLNLLAPGMAGELYLGGEGLARGYLNRPGLTAERFvpdpfsaSGErLY 2383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 400 KSGDKYVRNADGSYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVpDQAGLTKTKAFVVLKPGAQVSETEL 479
Cdd:PRK12316 2384 RTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQ-DGASGKQLVAYVVPDDAAEDLLAEL 2462
|
490 500 510
....*....|....*....|....*....|....*.
gi 1920939256 480 KAFVKERLAPYKYPRIIEFMDALPKTATGKIQRFRL 515
Cdd:PRK12316 2463 RAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKAL 2498
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
35-518 |
2.09e-39 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 150.56 E-value: 2.09e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 35 DDHGTMRYGE--------LAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLLTADDYAYM 106
Cdd:PRK13388 15 DDTIAVRYGDrtwtwrevLAEAAARAAALIALADPDRPLHVGVLLGNTPEMLFWLAAAALGGYVLVGLNTTRRGAALAAD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 107 LQHSRAQAVLVSGALLPVLRqamaqgGHEAATVIVSRPAGPlpdgmialeAWIER--NAPLAAPAST-GPDDPGFWLYSS 183
Cdd:PRK13388 95 IRRADCQLLVTDAEHRPLLD------GLDLPGVRVLDVDTP---------AYAELvaAAGALTPHREvDAMDPFMLIFTS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 184 GSTGRPKGVLHSQGNPYWTAELYAKPvLSLGEADICFSAAKLYFayglGNAL----TFPLSVGATVVLmaeRPTPEATfr 259
Cdd:PRK13388 160 GTTGAPKAVRCSHGRLAFAGRALTER-FGLTRDDVCYVSMPLFH----SNAVmagwAPAVASGAAVAL---PAKFSAS-- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 260 RWLD----YQPTVF--FGAPTGYagMLAAPGLPTREQVSLRLcSSAGEALPADLgERFTAHFGCEIIDGIGSTEMLHIFL 333
Cdd:PRK13388 230 GFLDdvrrYGATYFnyVGKPLAY--ILATPERPDDADNPLRV-AFGNEASPRDI-AEFSRRFGCQVEDGYGSSEGAVIVV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 334 snRPGQVRYGTTGWPVPGYAV------------ELrDEDGHAV-PDGDVGDLY-IQGPSAALMYWGNREKSRETFRGGWT 399
Cdd:PRK13388 306 --REPGTPPGSIGRGAPGVAIynpetltecavaRF-DAHGALLnADEAIGELVnTAGAGFFEGYYNNPEATAERMRHGMY 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 400 KSGDKYVRNADGSYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQAGLTKTKAFVVLKPGAQVSETEL 479
Cdd:PRK13388 383 WSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVGDQVMAALVLRDGATFDPDAF 462
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1920939256 480 KAFV--KERLAPYKYPRIIEFMDALPKTATGKIQRFRLREM 518
Cdd:PRK13388 463 AAFLaaQPDLGTKAWPRYVRIAADLPSTATNKVLKRELIAQ 503
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
19-512 |
3.54e-39 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 153.19 E-value: 3.54e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 19 HLIACNAQR-PGKTAYIDDHGTMRYGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTL 97
Cdd:PRK12316 515 RLFEEQVERtPEAPALAFGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPE 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 98 LTADDYAYMLQHSRAQAVLVSGALLPVLrqamaqggheaatvivsrpagPLPDGM--IALE---AWIERNAPLAAPASTG 172
Cdd:PRK12316 595 YPAERLAYMLEDSGVQLLLSQSHLGRKL---------------------PLAAGVqvLDLDrpaAWLEGYSEENPGTELN 653
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 173 PDDPGFWLYSSGSTGRPKGVLHSQGNPY----WTAELYAkpvLSLGEAdicfSAAKLYFAYGLGNALTF-PLSVGATVVL 247
Cdd:PRK12316 654 PENLAYVIYTSGSTGKPKGAGNRHRALSnrlcWMQQAYG---LGVGDT----VLQKTPFSFDVSVWEFFwPLMSGARLVV 726
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 248 MA--ERPTPEATFRRWLDYQPTVFFGAPTGYAGMLAAPGLPTreQVSLRLCSSAGEALPADLGERFTAHF-GCEIIDGIG 324
Cdd:PRK12316 727 AApgDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVAS--CTSLRRIVCSGEALPADAQEQVFAKLpQAGLYNLYG 804
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 325 STEMLhIFLSNRPGQVRYGTT---GWPVPGYAVELRDEDGHAVPDGDVGDLYIQGPSAALMYWGNREKSRETFRGG---- 397
Cdd:PRK12316 805 PTEAA-IDVTHWTCVEEGGDSvpiGRPIANLACYILDANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFVPSpfva 883
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 398 ---WTKSGDKYVRNADGSYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQAGLtktkAFVVLKPGAQV 474
Cdd:PRK12316 884 gerMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDGKQLV----GYVVLESEGGD 959
|
490 500 510
....*....|....*....|....*....|....*...
gi 1920939256 475 SETELKAFVKERLAPYKYPRIIEFMDALPKTATGKIQR 512
Cdd:PRK12316 960 WREALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDR 997
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
20-515 |
5.31e-39 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 148.99 E-value: 5.31e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 20 LIACNAQR-PGKTAYIDDHGTMRYGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLL 98
Cdd:PRK13383 40 LLAVTAARwPGRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEF 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 99 TADDYAYMLQHSRAQAVLVSGALLPVLrqamaQGGHEAATVIVSRPAGPLPDGmialeawierNAPLAAPastgpddPG- 177
Cdd:PRK13383 120 RSDALAAALRAHHISTVVADNEFAERI-----AGADDAVAVIDPATAGAEESG----------GRPAVAA-------PGr 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 178 FWLYSSGSTGRPKGVLH----SQGNPYWTAeLYAKPVLSLGEADICfsAAKLYFAYGLGnALTFPLSVGATVvLMAERPT 253
Cdd:PRK13383 178 IVLLTSGTTGKPKGVPRapqlRSAVGVWVT-ILDRTRLRTGSRISV--AMPMFHGLGLG-MLMLTIALGGTV-LTHRHFD 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 254 PEATFRRWLDYQPTVFFGAPTGYAGMLAapgLPTREQV-----SLRLCSSAGEALPADLGERFTAHFGCEIIDGIGSTEm 328
Cdd:PRK13383 253 AEAALAQASLHRADAFTAVPVVLARILE---LPPRVRArnplpQLRVVMSSGDRLDPTLGQRFMDTYGDILYNGYGSTE- 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 329 LHIFLSNRPGQVRYG--TTGWPVPGYAVELRDEDGHAVPDGDVGDLYIQGPSAALMYWGNREKSretFRGGWTKSGDKYV 406
Cdd:PRK13383 329 VGIGALATPADLRDApeTVGKPVAGCPVRILDRNNRPVGPRVTGRIFVGGELAGTRYTDGGGKA---VVDGMTSTGDMGY 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 407 RNADGSYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQAGLTKTKAFVVLKPGAQVSETELKAFVKER 486
Cdd:PRK13383 406 LDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPGSGVDAAQLRDYLKDR 485
|
490 500
....*....|....*....|....*....
gi 1920939256 487 LAPYKYPRIIEFMDALPKTATGKIQRFRL 515
Cdd:PRK13383 486 VSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
20-512 |
6.58e-39 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 152.42 E-value: 6.58e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 20 LIACNAQR-PGKTAYIDDHGTMRYGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLL 98
Cdd:PRK12316 4556 LVAERARMtPDAVAVVFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEY 4635
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 99 TADDYAYMLQHSRAQAVLVSGALLPVLrqamaqggheaatvivsrpagPLPDGMIAL-----EAWIERnaPLAAPAS-TG 172
Cdd:PRK12316 4636 PRERLAYMMEDSGAALLLTQSHLLQRL---------------------PIPDGLASLaldrdEDWEGF--PAHDPAVrLH 4692
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 173 PDDPGFWLYSSGSTGRPKGVLHSQGN----PYWTAELYakpvlSLGEADICFSAAKLYFAyGLGNALTFPLSVGATVVLM 248
Cdd:PRK12316 4693 PDNLAYVIYTSGSTGRPKGVAVSHGSlvnhLHATGERY-----ELTPDDRVLQFMSFSFD-GSHEGLYHPLINGASVVIR 4766
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 249 -AERPTPEATFRRWLDYQPTVFFGAPTgYAGMLAAPGLPTREQVSLRLCSSAGEAL-PADLGERFTAHFGCEIIDGIGST 326
Cdd:PRK12316 4767 dDSLWDPERLYAEIHEHRVTVLVFPPV-YLQQLAEHAERDGEPPSLRVYCFGGEAVaQASYDLAWRALKPVYLFNGYGPT 4845
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 327 E--MLHIFLSNRPGQVR---YGTTGWPVPGYAVELRDEDGHAVPDGDVGDLYIQGPSAALMYWGNREKSRETF------- 394
Cdd:PRK12316 4846 EttVTVLLWKARDGDACgaaYMPIGTPLGNRSGYVLDGQLNPLPVGVAGELYLGGEGVARGYLERPALTAERFvpdpfga 4925
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 395 RGG-WTKSGDKYVRNADGSYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQAGlTKTKAFVVLKPGAQ 473
Cdd:PRK12316 4926 PGGrLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAVG-KQLVGYVVPQDPAL 5004
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1920939256 474 VSETE--------LKAFVKERLAPYKYPRIIEFMDALPKTATGKIQR 512
Cdd:PRK12316 5005 ADADEaqaelrdeLKAALRERLPEYMVPAHLVFLARMPLTPNGKLDR 5051
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
181-512 |
7.97e-39 |
|
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain
Pssm-ID: 341288 [Multi-domain] Cd Length: 320 Bit Score: 144.09 E-value: 7.97e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 181 YSSGSTGRPKGVLHSQgnPYWTAELYA-KPVLSLGEADICFSAAKLYFAYGLgNALTFPLSVGATVVLMaeRPTPEATFR 259
Cdd:cd17633 7 FTSGTTGLPKAYYRSE--RSWIESFVCnEDLFNISGEDAILAPGPLSHSLFL-YGAISALYLGGTFIGQ--RKFNPKSWI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 260 RWLD-YQPTVFFGAPTgyagMLAAPGLPTREQVSLRLCSSAGEALPADLGERFTAHF-GCEIIDGIGSTEMLHI-FLSNR 336
Cdd:cd17633 82 RKINqYNATVIYLVPT----MLQALARTLEPESKIKSIFSSGQKLFESTKKKLKNIFpKANLIEFYGTSELSFItYNFNQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 337 PGQVRyGTTGWPVPGYAVELRDEDGhavpdGDVGDLYIQGPSAALMYWGNREKSRetfrGGWTKSGD-KYVRNaDGSYSY 415
Cdd:cd17633 158 ESRPP-NSVGRPFPNVEIEIRNADG-----GEIGKIFVKSEMVFSGYVRGGFSNP----DGWMSVGDiGYVDE-EGYLYL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 416 AGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQAGLTKTKAFVVlkpGAQVSETELKAFVKERLAPYKYPRI 495
Cdd:cd17633 227 VGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYS---GDKLTYKQLKRFLKQKLSRYEIPKK 303
|
330
....*....|....*..
gi 1920939256 496 IEFMDALPKTATGKIQR 512
Cdd:cd17633 304 IIFVDSLPYTSSGKIAR 320
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
25-512 |
4.87e-38 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 149.72 E-value: 4.87e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 25 AQRPGKTAYIDDHGTMRYGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLLTADDYA 104
Cdd:PRK12316 3068 ERTPDAVALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLA 3147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 105 YMLQHSRAQAVLVSgallPVLRQAMAQGGHeaatvivsrpagplpdgMIALEAWIERNAPLAAPASTGPDDPGFWLYSSG 184
Cdd:PRK12316 3148 YMLEDSGAQLLLSQ----SHLRLPLAQGVQ-----------------VLDLDRGDENYAEANPAIRTMPENLAYVIYTSG 3206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 185 STGRPKGVLHSQG----NPYWTAELYAkpvlsLGEADICFSAAKLYFAyGLGNALTFPLSVGATVVLMAERPTPEATFRR 260
Cdd:PRK12316 3207 STGKPKGVGIRHSalsnHLCWMQQAYG-----LGVGDRVLQFTTFSFD-VFVEELFWPLMSGARVVLAGPEDWRDPALLV 3280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 261 WLDYQPTVffGAPTGYAGMLAAPGLPTREQ--VSLRLCSSAGEALPADLGERFTAHFGCEIIDGIGSTEMLHIFLSNRPG 338
Cdd:PRK12316 3281 ELINSEGV--DVLHAYPSMLQAFLEEEDAHrcTSLKRIVCGGEALPADLQQQVFAGLPLYNLYGPTEATITVTHWQCVEE 3358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 339 QVRYGTTGWPVPGYAVELRDEDGHAVPDGDVGDLYIQGPSAALMYWGNREKSRETFR-------GGWTKSGDKYVRNADG 411
Cdd:PRK12316 3359 GKDAVPIGRPIANRACYILDGSLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVpdpfvpgERLYRTGDLARYRADG 3438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 412 SYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQagltKTKAFVVLKPGAQVSETELKAFVKERLAPYK 491
Cdd:PRK12316 3439 VIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLAVDGR----QLVAYVVPEDEAGDLREALKAHLKASLPEYM 3514
|
490 500
....*....|....*....|.
gi 1920939256 492 YPRIIEFMDALPKTATGKIQR 512
Cdd:PRK12316 3515 VPAHLLFLERMPLTPNGKLDR 3535
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
27-518 |
7.73e-38 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 145.90 E-value: 7.73e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 27 RPGKTAYIDDHGTMRYGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVavNTLLTADDY--- 103
Cdd:PRK10946 36 ASDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLGVAPV--NALFSHQRSeln 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 104 AYMLQ-------HSRAQAVLVSGALLPVLRQAmaqggHEAATVIVSRPAgplpDGMIALEAWIERNAPLAAPASTGPDDP 176
Cdd:PRK10946 114 AYASQiepalliADRQHALFSDDDFLNTLVAE-----HSSLRVVLLLND----DGEHSLDDAINHPAEDFTATPSPADEV 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 177 GFWLYSSGSTGRPKGVLHSQGNPYWTAElyakpvlslGEADICFSAAKLYFAYGLGNALTFPLS---------VGATVVl 247
Cdd:PRK10946 185 AFFQLSGGSTGTPKLIPRTHNDYYYSVR---------RSVEICGFTPQTRYLCALPAAHNYPMSspgalgvflAGGTVV- 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 248 MAERPTPEATFRRWLDYQPTVFFGAPTGYAGMLAAPGLPTREQ--VSLRLCSSAGEALPADLGERFTAHFGCEIIDGIGS 325
Cdd:PRK10946 255 LAPDPSATLCFPLIEKHQVNVTALVPPAVSLWLQAIAEGGSRAqlASLKLLQVGGARLSETLARRIPAELGCQLQQVFGM 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 326 TEMLHIFLS-NRPGQVRYGTTGWPV-PGYAVELRDEDGHAVPDGDVGDLYIQGPSAALMYWGNREKSRETF-RGGWTKSG 402
Cdd:PRK10946 335 AEGLVNYTRlDDSDERIFTTQGRPMsPDDEVWVADADGNPLPQGEVGRLMTRGPYTFRGYYKSPQHNASAFdANGFYCSG 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 403 DKYVRNADGSYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQAGLTKTKAFVVLKPGaqVSETELKAF 482
Cdd:PRK10946 415 DLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAFLVVKEP--LKAVQLRRF 492
|
490 500 510
....*....|....*....|....*....|....*..
gi 1920939256 483 VKER-LAPYKYPRIIEFMDALPKTATGKIQRFRLREM 518
Cdd:PRK10946 493 LREQgIAEFKLPDRVECVDSLPLTAVGKVDKKQLRQW 529
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
151-510 |
2.28e-36 |
|
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: 140.93 E-value: 2.28e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 151 GMIALEAWIERNAPLAapaSTGPDDPGFWLYSSGSTGRPKGVLHSQGNPYWTAElYAKPVLSLGEADICFSAAKLYFAYG 230
Cdd:cd05909 127 AGKFPPKWLLRIFGVA---PVQPDDPAVILFTSGSEGLPKGVVLSHKNLLANVE-QITAIFDPNPEDVVFGALPFFHSFG 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 231 LGNALTFPLSVGATVVlMAERPT-----PEATFrrwlDYQPTVFFGAPTGYAGMLAApglPTREQV-SLRLCSSAGEALP 304
Cdd:cd05909 203 LTGCLWLPLLSGIKVV-FHPNPLdykkiPELIY----DKKATILLGTPTFLRGYARA---AHPEDFsSLRLVVAGAEKLK 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 305 ADLGERFTAHFGCEIIDGIGSTEMLHIFLSNRPGQ-VRYGTTGWPVPGYAVELRDEDGHA-VPDGDVGDLYIQGPSAALM 382
Cdd:cd05909 275 DTLRQEFQEKFGIRILEGYGTTECSPVISVNTPQSpNKEGTVGRPLPGMEVKIVSVETHEeVPIGEGGLLLVRGPNVMLG 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 383 YWGNREKSRETFRGGWTKSGDKYVRNADGSYSYAGRSDDMLKVSGIYVSPFEVEATLAQH-PAILEAAVIGVPDQaglTK 461
Cdd:cd05909 355 YLNEPELTSFAFGDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVPDG---RK 431
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1920939256 462 TKAFVVLKPGAQVSETELKAFVKERLAPYKY-PRIIEFMDALPKTATGKI 510
Cdd:cd05909 432 GEKIVLLTTTTDTDPSSLNDILKNAGISNLAkPSYIHQVEEIPLLGTGKP 481
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
42-517 |
2.59e-36 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 141.81 E-value: 2.59e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 42 YGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLLTADDYAYMLQHSRAQAVLVSGAL 121
Cdd:PRK06018 42 YAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVITDLTF 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 122 LPVLrQAMAQGGHEAATVIVSRPAGPLPD----GMIALEAWIERNAPLAAPASTGPDDPGFWLYSSGSTGRPKGVLHSQG 197
Cdd:PRK06018 122 VPIL-EKIADKLPSVERYVVLTDAAHMPQttlkNAVAYEEWIAEADGDFAWKTFDENTAAGMCYTSGTTGDPKGVLYSHR 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 198 NPYWTAELYAKP-VLSLGEADICFSAAKLYFAYGLGNALTFPlSVGATVVLMAERPTPEATFRRWLDYQPTVFFGAPTGY 276
Cdd:PRK06018 201 SNVLHALMANNGdALGTSAADTMLPVVPLFHANSWGIAFSAP-SMGTKLVMPGAKLDGASVYELLDTEKVTFTAGVPTVW 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 277 AGML---AAPG--LPTreqvsLRLCSSAGEALPADLGERFTaHFGCEIIDGIGSTEM--------LHIFLSNRPGQVRYG 343
Cdd:PRK06018 280 LMLLqymEKEGlkLPH-----LKMVVCGGSAMPRSMIKAFE-DMGVEVRHAWGMTEMsplgtlaaLKPPFSKLPGDARLD 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 344 ---TTGWPVPGYAVELRDEDGHAVP-DGDV-GDLYIQGPSAALMYWgnREKSRETFRGGWTKSGDKYVRNADGSYSYAGR 418
Cdd:PRK06018 354 vlqKQGYPPFGVEMKITDDAGKELPwDGKTfGRLKVRGPAVAAAYY--RVDGEILDDDGFFDTGDVATIDAYGYMRITDR 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 419 SDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQAGLTKTKAFVVLKPGAQVSETELKAFVKERLAPYKYPRIIEF 498
Cdd:PRK06018 432 SKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQLKPGETATREEILKYMDGKIAKWWMPDDVAF 511
|
490
....*....|....*....
gi 1920939256 499 MDALPKTATGKIQRFRLRE 517
Cdd:PRK06018 512 VDAIPHTATGKILKTALRE 530
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
175-512 |
2.49e-35 |
|
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: 134.77 E-value: 2.49e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 175 DPGFWLYSSGSTGRPKGVLHSQGNPYWTAELYAKPvLSLGEADICFSAAKLYFAYGLGNALTFPLSVGATVVLMAERPTP 254
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSR-LGFGGGDSWLLSLPLYHVGGLAILVRSLLAGAELVLLERNQALA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 255 EATfrrwLDYQPTVFFGAPTGYAGMLAAPGLPTReQVSLRLCSSAGEALPADLGERFTAHfGCEIIDGIGSTEML-HIFL 333
Cdd:cd17630 80 EDL----APPGVTHVSLVPTQLQRLLDSGQGPAA-LKSLRAVLLGGAPIPPELLERAADR-GIPLYTTYGMTETAsQVAT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 334 SnRPGQVRYGTTGWPVPGyaVELR-DEDGHavpdgdvgdLYIQGPSAALMYWgNREKSRETFRGGWTKSGDKYVRNADGS 412
Cdd:cd17630 154 K-RPDGFGRGGVGVLLPG--RELRiVEDGE---------IWVGGASLAMGYL-RGQLVPEFNEDGWFTTKDLGELHADGR 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 413 YSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQAGLTKTKAFVVLKPGAQVSetELKAFVKERLAPYKY 492
Cdd:cd17630 221 LTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRGPADPA--ELRAWLKDKLARFKL 298
|
330 340
....*....|....*....|
gi 1920939256 493 PRIIEFMDALPKTATGKIQR 512
Cdd:cd17630 299 PKRIYPVPELPRTGGGKVDR 318
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
25-517 |
9.60e-35 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 137.03 E-value: 9.60e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 25 AQRPGKTAYIDDH--GTMRYGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLLTADD 102
Cdd:PLN02246 34 SEFSDRPCLIDGAtgRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 103 YAYMLQHSRAQAVLVSGALLPVLRQAMAQGGHEAATVivsrpaGPLPDGMIALEAWIERNAPLAAPASTGPDDPGFWLYS 182
Cdd:PLN02246 114 IAKQAKASGAKLIITQSCYVDKLKGLAEDDGVTVVTI------DDPPEGCLHFSELTQADENELPEVEISPDDVVALPYS 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 183 SGSTGRPKGV-LHSQGNPYWTAELY--AKPVLSLGEADICFSAAKLYFAYGLGNALTFPLSVGATVVLMAERPTP---EA 256
Cdd:PLN02246 188 SGTTGLPKGVmLTHKGLVTSVAQQVdgENPNLYFHSDDVILCVLPMFHIYSLNSVLLCGLRVGAAILIMPKFEIGallEL 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 257 TFRrwldYQPTVffgAPTGYAGMLAAPGLPTREQ---VSLRLCSSAGEALPADLGERFTAHFGCEII-DGIGSTE----- 327
Cdd:PLN02246 268 IQR----HKVTI---APFVPPIVLAIAKSPVVEKydlSSIRMVLSGAAPLGKELEDAFRAKLPNAVLgQGYGMTEagpvl 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 328 -MLHIFlSNRPGQVRYGTTGWPVPGYAVELRD-EDGHAVPDGDVGDLYIQGPSAALMYWGNREKSRETF-RGGWTKSGD- 403
Cdd:PLN02246 341 aMCLAF-AKEPFPVKSGSCGTVVRNAELKIVDpETGASLPRNQPGEICIRGPQIMKGYLNDPEATANTIdKDGWLHTGDi 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 404 KYVRNADGSYsYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQAGLTKTKAFVVLKPGAQVSETELKAFV 483
Cdd:PLN02246 420 GYIDDDDELF-IVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVVRSNGSEITEDEIKQFV 498
|
490 500 510
....*....|....*....|....*....|....
gi 1920939256 484 KERLAPYKYPRIIEFMDALPKTATGKIQRFRLRE 517
Cdd:PLN02246 499 AKQVVFYKRIHKVFFVDSIPKAPSGKILRKDLRA 532
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
35-513 |
1.28e-34 |
|
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: 135.65 E-value: 1.28e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 35 DDHG--TMRYGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLLTADDYAYMLQHSRA 112
Cdd:cd05914 1 LYYGgePLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 113 QAVLVSGallpvlrqamaqggheaatvivsrpagplpdgmialeawiernaplaapastgPDDPGFWLYSSGSTGRPKGV 192
Cdd:cd05914 81 KAIFVSD-----------------------------------------------------EDDVALINYTSGTTGNSKGV 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 193 LHSQGNPYWTAElYAKPVLSLGEADICFSAAKLYFAYGLGNALTFPLSVGATVVLMAERPTPEATFRRWldYQPTVFFGA 272
Cdd:cd05914 108 MLTYRNIVSNVD-GVKEVVLLGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFLDKIPSAKIIALAF--AQVTPTLGV 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 273 PTGY----------------AGM---LAAPGLPT------REQVS------LRLCSSAGEALPADLgERFTAHFGCEIID 321
Cdd:cd05914 185 PVPLviekifkmdiipkltlKKFkfkLAKKINNRkirklaFKKVHeafggnIKEFVIGGAKINPDV-EEFLRTIGFPYTI 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 322 GIGSTEMLHIFLSNRPGQVRYGTTGWPVPGYAVELRDEDghavPDGDVGDLYIQGPSAALMYWGNREKSRETF-RGGWTK 400
Cdd:cd05914 264 GYGMTETAPIISYSPPNRIRLGSAGKVIDGVEVRIDSPD----PATGEGEIIVRGPNVMKGYYKNPEATAEAFdKDGWFH 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 401 SGDKYVRNADGSYSYAGRSDDMLKV-SGIYVSPFEVEATLAQHPAILEAAVIGVPDqagltKTKAFVVLKPG-AQVSE-- 476
Cdd:cd05914 340 TGDLGKIDAEGYLYIRGRKKEMIVLsSGKNIYPEEIEAKINNMPFVLESLVVVQEK-----KLVALAYIDPDfLDVKAlk 414
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1920939256 477 -TELKAFVKE--------RLAPY-KYPRIIEFMDALPKTATGKIQRF 513
Cdd:cd05914 415 qRNIIDAIKWevrdkvnqKVPNYkKISKVKIVKEEFEKTPKGKIKRF 461
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
25-512 |
3.10e-34 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 136.62 E-value: 3.10e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 25 AQRPGKTAYI------DDHGTMRYGELAERIRRVAGALQASGIHREERVLLLMhdgndwP----VCFlgAMYA-----GI 89
Cdd:PRK10524 64 AKRPEQLALIavstetDEERTYTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYM------PmiaeAAF--AMLAcarigAI 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 90 VPV-----AVNTLLT-ADDyaymlqhsrAQAVLVSGA-----------LLPVLRQAMAQGGHEAATV-IVSR---PAGPL 148
Cdd:PRK10524 136 HSVvfggfASHSLAArIDD---------AKPVLIVSAdagsrggkvvpYKPLLDEAIALAQHKPRHVlLVDRglaPMARV 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 149 PDGMIALEAWIERNAPLAAP----ASTgpdDPGFWLYSSGSTGRPKGVLHSQGNpYWTAELYAKPVLSLGEA-DICFSAA 223
Cdd:PRK10524 207 AGRDVDYATLRAQHLGARVPvewlESN---EPSYILYTSGTTGKPKGVQRDTGG-YAVALATSMDTIFGGKAgETFFCAS 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 224 KL-------YFAYGlgnaltfPLSVGATVVlMAE----RPTPEATFRRWLDYQPTVFFGAPTGyAGMLA--APGLPTREQ 290
Cdd:PRK10524 283 DIgwvvghsYIVYA-------PLLAGMATI-MYEglptRPDAGIWWRIVEKYKVNRMFSAPTA-IRVLKkqDPALLRKHD 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 291 VS-LRLCSSAGEALPADLGERFTAHFGCEIIDGIGSTEMLHIFLSNRPG----QVRYGTTGWPVPGYAVELRDE-DGHAV 364
Cdd:PRK10524 354 LSsLRALFLAGEPLDEPTASWISEALGVPVIDNYWQTETGWPILAIARGvedrPTRLGSPGVPMYGYNVKLLNEvTGEPC 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 365 PDGDVGDLYIQGP---SAALMYWGNREKSRETFrggWTKSG-------DKYVRNADGSYSYAGRSDDMLKVSGIYVSPFE 434
Cdd:PRK10524 434 GPNEKGVLVIEGPlppGCMQTVWGDDDRFVKTY---WSLFGrqvystfDWGIRDADGYYFILGRTDDVINVAGHRLGTRE 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 435 VEATLAQHPAILEAAVIGVPDQAGLTKTKAFVVLKPGAQVS--------ETELKAFVKERLAPYKYPRIIEFMDALPKTA 506
Cdd:PRK10524 511 IEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPKDSDSLAdrearlalEKEIMALVDSQLGAVARPARVWFVSALPKTR 590
|
....*.
gi 1920939256 507 TGKIQR 512
Cdd:PRK10524 591 SGKLLR 596
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
25-512 |
3.29e-34 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 138.37 E-value: 3.29e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 25 AQRPGKTAYIDDHGTMRYGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLLTADDYA 104
Cdd:PRK12467 1585 AATPEAVALVFGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLA 1664
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 105 YMLQHSRAQAVLVSGALLPVLrqamaqggheaatvivsrpagPLPDGMIALE-----AWIErNAPLAAPAS-TGPDDPGF 178
Cdd:PRK12467 1665 YMIEDSGIELLLTQSHLQARL---------------------PLPDGLRSLVldqedDWLE-GYSDSNPAVnLAPQNLAY 1722
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 179 WLYSSGSTGRPKGVLHSQGNP----YWTAELYAkpvlslgeadicFSAA-----KLYFAYGLGNALTF-PLSVGATVVLM 248
Cdd:PRK12467 1723 VIYTSGSTGRPKGAGNRHGALvnrlCATQEAYQ------------LSAAdvvlqFTSFAFDVSVWELFwPLINGARLVIA 1790
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 249 A--ERPTPEATFRRWLDYQPTVFFGAPTGYAGMLAAPGLPTReQVSLRLCSSAGEALPADLGERFTAHFG-CEIIDGIGS 325
Cdd:PRK12467 1791 PpgAHRDPEQLIQLIERQQVTTLHFVPSMLQQLLQMDEQVEH-PLSLRRVVCGGEALEVEALRPWLERLPdTGLFNLYGP 1869
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 326 TE----MLHIFLSNRPGQVR-YGTTGWPVPGYAVELRDEDGHAVPDGDVGDLYIQGPSAALMYWGNREKSRETF------ 394
Cdd:PRK12467 1870 TEtavdVTHWTCRRKDLEGRdSVPIGQPIANLSTYILDASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFvadpfg 1949
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 395 RGG--WTKSGDKYVRNADGSYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVpDQAGLTKTKAFVVLKPGA 472
Cdd:PRK12467 1950 TVGsrLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIAQ-DGANGKQLVAYVVPTDPG 2028
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1920939256 473 QVSETE--------LKAFVKERLAPYKYPRIIEFMDALPKTATGKIQR 512
Cdd:PRK12467 2029 LVDDDEaqvalraiLKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDR 2076
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
5-517 |
8.82e-34 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 134.33 E-value: 8.82e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 5 PQVQPPGTPFNFAQHLIACNAQRPGK-TAYIDDHGT---MRYGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVC 80
Cdd:cd05906 1 PLHRPEGAPRTLLELLLRAAERGPTKgITYIDADGSeefQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 81 FLGAMYAGIVPVAVNTLLTADDYAYMLQHSR-------AQAVLVSGALLPVLRQAMAQGGHEAATVIvsrpagplpdgmi 153
Cdd:cd05906 81 FWACVLAGFVPAPLTVPPTYDEPNARLRKLRhiwqllgSPVVLTDAELVAEFAGLETLSGLPGIRVL------------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 154 ALEAWIERNAPLAAPASTgPDDPGFWLYSSGSTGRPKGVLHSQGNpyWTAELYAKPVLS-LGEADICFSAAKLYFAYGLG 232
Cdd:cd05906 148 SIEELLDTAADHDLPQSR-PDDLALLMLTSGSTGFPKAVPLTHRN--ILARSAGKIQHNgLTPQDVFLNWVPLDHVGGLV 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 233 NALTFPLSVGATVV-----LMAERPTpeatfrRWLD----YQPTVFFgAPTGYAGMLAApGLPTREQV-----SLRLCSS 298
Cdd:cd05906 225 ELHLRAVYLGCQQVhvpteEILADPL------RWLDlidrYRVTITW-APNFAFALLND-LLEEIEDGtwdlsSLRYLVN 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 299 AGEALPADLGERFT---AHFGCE---IIDGIGSTEM-------LHIFLSNRPGQVRYGTTGWPVPGYAVELRDEDGHAVP 365
Cdd:cd05906 297 AGEAVVAKTIRRLLrllEPYGLPpdaIRPAFGMTETcsgviysRSFPTYDHSQALEFVSLGRPIPGVSMRIVDDEGQLLP 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 366 DGDVGDLYIQGPSAALMYWGNREKSRETFR-GGWTKSGD-KYVRNadGSYSYAGRSDDMLKVSGIYVSPFEVEATLAQHP 443
Cdd:cd05906 377 EGEVGRLQVRGPVVTKGYYNNPEANAEAFTeDGWFRTGDlGFLDN--GNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVP 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 444 aILE---AAVIGVPDQAGLTKTKAFVVL-------KPGAQVSETELKAFVKERLAPykyPRIIEF-MDALPKTATGKIQR 512
Cdd:cd05906 455 -GVEpsfTAAFAVRDPGAETEELAIFFVpeydlqdALSETLRAIRSVVSREVGVSP---AYLIPLpKEEIPKTSLGKIQR 530
|
....*
gi 1920939256 513 FRLRE 517
Cdd:cd05906 531 SKLKA 535
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
10-517 |
1.62e-33 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 134.23 E-value: 1.62e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 10 PGTPFNFAQHLIACNAQRPGKTAYIDDHGTMRYGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGI 89
Cdd:PRK08279 33 PDSKRSLGDVFEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 90 VPVAVNTLLTADDYAYMLQHSRAQAVLVSGALLPVLRQAMAQGGHEAATVIVSRPAGPLPDGMIALEAWIeRNAPLAAPA 169
Cdd:PRK08279 113 VVALLNTQQRGAVLAHSLNLVDAKHLIVGEELVEAFEEARADLARPPRLWVAGGDTLDDPEGYEDLAAAA-AGAPTTNPA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 170 STG---PDDPGFWLYSSGSTGRPKGVLHSQGNpyWTAEL--YAKpVLSLGEADICFSAAKLYFAYGLGNALTFPLSVGAT 244
Cdd:PRK08279 192 SRSgvtAKDTAFYIYTSGTTGLPKAAVMSHMR--WLKAMggFGG-LLRLTPDDVLYCCLPLYHNTGGTVAWSSVLAAGAT 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 245 VVLmaeRPTPEATfRRWLD---YQPTVFfgaptGYAG-----MLAAPGLPTREQVSLRLCssAGEALPADLGERFTAHFG 316
Cdd:PRK08279 269 LAL---RRKFSAS-RFWDDvrrYRATAF-----QYIGelcryLLNQPPKPTDRDHRLRLM--IGNGLRPDIWDEFQQRFG 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 317 CE-IIDGIGSTE----MLHIFlsNRPGQVRYGTTGWPVPGYAVE--------LRDEDGHA--VPDGDVGDLyIQGPSAAL 381
Cdd:PRK08279 338 IPrILEFYAASEgnvgFINVF--NFDGTVGRVPLWLAHPYAIVKydvdtgepVRDADGRCikVKPGEVGLL-IGRITDRG 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 382 MYWG--NREKS-----RETFRGG--WTKSGDKYVRNADGSYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIG 452
Cdd:PRK08279 415 PFDGytDPEASekkilRDVFKKGdaWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVATTEVENALSGFPGVEEAVVYG 494
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 453 VP-----DQAGLtktkAFVVLKPGAQVSETELKAFVKERLAPYKYPRIIEFMDALPKTATGKIQRFRLRE 517
Cdd:PRK08279 495 VEvpgtdGRAGM----AAIVLADGAEFDLAALAAHLYERLPAYAVPLFVRLVPELETTGTFKYRKVDLRK 560
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
175-512 |
4.07e-33 |
|
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: 128.92 E-value: 4.07e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 175 DPGFWLYSSGSTGRPKGVLHSQGNPYWTAELYAKPVLSLGEADICFSAAKLYFAYGLGNALTFpLSVGATVVLMAERPTP 254
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLNWVVGDVTYLPLPATHIGGLWWILTC-LIHGGLCVTGGENTTY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 255 EATFRRWLDYQPTVFFGAPTGYAGMLAAPGLPTREQVSLRLCSSAGEALPADLGERFTAHFGCEIIDGIGSTEMLHI-FL 333
Cdd:cd17635 81 KSLFKILTTNAVTTTCLVPTLLSKLVSELKSANATVPSLRLIGYGGSRAIAADVRFIEATGLTNTAQVYGLSETGTAlCL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 334 SNRPGQVRYGTTGWPVPGYAVELRDEDGHAVPDGDVGDLYIQGPSAALMYWGNREKSRETFRGGWTKSGDKYVRNADGSY 413
Cdd:cd17635 161 PTDDDSIEINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLIDGWVNTGDLGERREDGFL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 414 SYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQAGLTKTKAFVVLKpgAQVSE---TELKAFVKERLAPY 490
Cdd:cd17635 241 FITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVAS--AELDEnaiRALKHTIRRELEPY 318
|
330 340
....*....|....*....|..
gi 1920939256 491 KYPRIIEFMDALPKTATGKIQR 512
Cdd:cd17635 319 ARPSTIVIVTDIPRTQSGKVKR 340
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
20-512 |
4.44e-33 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 134.40 E-value: 4.44e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 20 LIACNAQR-PGKTAYIDDHGTMRYGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLL 98
Cdd:PRK10252 463 LVAQQAAKtPDAPALADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGY 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 99 TADDYAYMLQHSRAQAVLVSGALLPVLrqamaqggHEAATVIVSRPAGPLPDGmialeawieRNAPLAAPAstgPDDPGF 178
Cdd:PRK10252 543 PDDRLKMMLEDARPSLLITTADQLPRF--------ADVPDLTSLCYNAPLAPQ---------GAAPLQLSQ---PHHTAY 602
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 179 WLYSSGSTGRPKGVLHSQ----GNPYWTAELYAkpvlsLGEADICFSAAKLYFAYGLGNaLTFPLSVGATVVlMAErPT- 253
Cdd:PRK10252 603 IIFTSGSTGRPKGVMVGQtaivNRLLWMQNHYP-----LTADDVVLQKTPCSFDVSVWE-FFWPFIAGAKLV-MAE-PEa 674
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 254 ---PEATFRRWLDYQPTVFFGAPTGYAGMLAAPG--LPTREQVSLR--LCSsaGEALPADLGERFTAHFGCEIIDGIGST 326
Cdd:PRK10252 675 hrdPLAMQQFFAEYGVTTTHFVPSMLAAFVASLTpeGARQSCASLRqvFCS--GEALPADLCREWQQLTGAPLHNLYGPT 752
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 327 EMLhIFLSNRP--GQVRYGTTGWPVP-GYAV-----ELRDEDGHAVPDGDVGDLYIQGPSAALMYWGNREKSRETFRGGW 398
Cdd:PRK10252 753 EAA-VDVSWYPafGEELAAVRGSSVPiGYPVwntglRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADP 831
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 399 TKSGDKYVRNAD-------GSYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVI------GVPDQAGLTKTKAF 465
Cdd:PRK10252 832 FAPGERMYRTGDvarwlddGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAVTHacvinqAAATGGDARQLVGY 911
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1920939256 466 VVLKPGAQVSETELKAFVKERLAPYKYPRIIEFMDALPKTATGKIQR 512
Cdd:PRK10252 912 LVSQSGLPLDTSALQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDR 958
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
25-512 |
8.85e-33 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 133.75 E-value: 8.85e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 25 AQRPGKTAYIDDHGTMRYGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLLTADDYA 104
Cdd:PRK12467 3106 ARTPEAPALVFGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLA 3185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 105 YMLQHSRAQAVLVSGALLPVLRQAmaqggHEAATVIVSRpagplpdgmIALEAWIERNAPlaapASTGPDDPGFWLYSSG 184
Cdd:PRK12467 3186 YMIEDSGVKLLLTQAHLLEQLPAP-----AGDTALTLDR---------LDLNGYSENNPS----TRVMGENLAYVIYTSG 3247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 185 STGRPKGVLHSQG----NPYWTAELYAkpvLSLGEADICFSAaklyFAYGLGNALTF-PLSVGATVVLMAERPTPEATFR 259
Cdd:PRK12467 3248 STGKPKGVGVRHGalanHLCWIAEAYE---LDANDRVLLFMS----FSFDGAQERFLwTLICGGCLVVRDNDLWDPEELW 3320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 260 RWLDYQPTVFFGAPTGYAGMLAAPGLPtREQVSLRLCSSAGEALPADLGERFTAHFG-CEIIDGIGSTEMLHIFL----- 333
Cdd:PRK12467 3321 QAIHAHRISIACFPPAYLQQFAEDAGG-ADCASLDIYVFGGEAVPPAAFEQVKRKLKpRGLTNGYGPTEAVVTVTlwkcg 3399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 334 SNRPGQVRYGTTGWPVPGYAVELRDEDGHAVPDGDVGDLYIQGPSAALMYWGNREKSRETF--------RGGWTKSGDKY 405
Cdd:PRK12467 3400 GDAVCEAPYAPIGRPVAGRSIYVLDGQLNPVPVGVAGELYIGGVGLARGYHQRPSLTAERFvadpfsgsGGRLYRTGDLA 3479
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 406 VRNADGSYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQAGlTKTKAFVVLKPGAQVSETELKAFVKE 485
Cdd:PRK12467 3480 RYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLARDGAGG-KQLVAYVVPADPQGDWRETLRDHLAA 3558
|
490 500
....*....|....*....|....*..
gi 1920939256 486 RLAPYKYPRIIEFMDALPKTATGKIQR 512
Cdd:PRK12467 3559 SLPDYMVPAQLLVLAAMPLGPNGKVDR 3585
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
25-517 |
1.32e-32 |
|
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: 129.35 E-value: 1.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 25 AQRPGKTAYIDDHGTMRYGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLLTADDYA 104
Cdd:cd17653 8 AAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSARIQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 105 YMLQHSRAQAVLvsgallpvlrqamaqggheaatvivsrpagplpdgmialeawiernaplaapASTGPDDPGFWLYSSG 184
Cdd:cd17653 88 AILRTSGATLLL----------------------------------------------------TTDSPDDLAYIIFTSG 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 185 STGRPKGVLHSQGN-----PYWTAELYAKP------VLSLGeADICfsaAKLYFAyglgnaltfPLSVGATVVLmAERPT 253
Cdd:cd17653 116 STGIPKGVMVPHRGvlnyvSQPPARLDVGPgsrvaqVLSIA-FDAC---IGEIFS---------TLCNGGTLVL-ADPSD 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 254 PEATFRRWLDyqptVFFGAPTgYAGMLAAPGLPTREQVSLrlcssAGEALPADLGERFTahFGCEIIDGIGSTE--MLHI 331
Cdd:cd17653 182 PFAHVARTVD----ALMSTPS-ILSTLSPQDFPNLKTIFL-----GGEAVPPSLLDRWS--PGRRLYNAYGPTEctISST 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 332 FLSNRPGQvrYGTTGWPVPGYAVELRDEDGHAVPDGDVGDLYIQGPSAALMYWGNREKSRE-----TFRGGWT--KSGDK 404
Cdd:cd17653 250 MTELLPGQ--PVTIGKPIPNSTCYILDADLQPVPEGVVGEICISGVQVARGYLGNPALTASkfvpdPFWPGSRmyRTGDY 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 405 YVRNADGSYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQAGLtktkAFVVlkPgAQVSETELKAFVK 484
Cdd:cd17653 328 GRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEVVLQSQPEVTQAAAIVVNGRLV----AFVT--P-ETVDVDGLRSELA 400
|
490 500 510
....*....|....*....|....*....|...
gi 1920939256 485 ERLAPYKYPRIIEFMDALPKTATGKIQRFRLRE 517
Cdd:cd17653 401 KHLPSYAVPDRIIALDSFPLTANGKVDRKALRE 433
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
38-518 |
2.24e-32 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 131.56 E-value: 2.24e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 38 GTMRYGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLLTADDYAYMLQHSRAQAVLV 117
Cdd:PLN02654 119 ASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQRIVDCKPKVVIT 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 118 SGA---------LLPVLRQAMAQGGHEAATV----------IVSRPAGPLPDGMialEAW---IERNAPLAAPAS-TGPD 174
Cdd:PLN02654 199 CNAvkrgpktinLKDIVDAALDESAKNGVSVgicltyenqlAMKREDTKWQEGR---DVWwqdVVPNYPTKCEVEwVDAE 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 175 DPGFWLYSSGSTGRPKGVLHSQGN-PYWTAELYaKPVLSLGEADICFSAAKLYFAYGLGNALTFPLSVGATVVLMAERPT 253
Cdd:PLN02654 276 DPLFLLYTSGSTGKPKGVLHTTGGyMVYTATTF-KYAFDYKPTDVYWCTADCGWITGHSYVTYGPMLNGATVLVFEGAPN 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 254 PEATFRRW--LD-YQPTVFFGAPTGYAGMLAAPGLP-TR-EQVSLRLCSSAGEALPADLGERFTAHFG---CEIIDGIGS 325
Cdd:PLN02654 355 YPDSGRCWdiVDkYKVTIFYTAPTLVRSLMRDGDEYvTRhSRKSLRVLGSVGEPINPSAWRWFFNVVGdsrCPISDTWWQ 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 326 TEMLHIFLSNRPGQ--VRYGTTGWPVPGYAVELRDEDGHAVPDGDVGDLYIQG--PSAALMYWGNREKSRETFR---GGW 398
Cdd:PLN02654 435 TETGGFMITPLPGAwpQKPGSATFPFFGVQPVIVDEKGKEIEGECSGYLCVKKswPGAFRTLYGDHERYETTYFkpfAGY 514
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 399 TKSGDKYVRNADGSYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQAGLTKTKAFVVLKPGAQVSETE 478
Cdd:PLN02654 515 YFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEVKGQGIYAFVTLVEGVPYSEEL 594
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1920939256 479 LKAF---VKERLAPYKYPRIIEFMDALPKTATGKIQRFRLREM 518
Cdd:PLN02654 595 RKSLiltVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRKI 637
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
17-518 |
4.83e-32 |
|
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: 128.43 E-value: 4.83e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 17 AQHLIACNAQ-RPGKTAYIDDHGTMRYGELAERIRRVAGALQASGIHREERVlllmhdgndwPVCFLGAMYAgivPVAvn 95
Cdd:cd05918 1 VHDLIEERARsQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFV----------PLCFEKSKWA---VVA-- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 96 tlltaddyayMLqhsraqAVLVSGA-------LLPVLR-QAMAQGGhEAATVIVSRPagplpdgmialeawiernaplaa 167
Cdd:cd05918 66 ----------ML------AVLKAGGafvpldpSHPLQRlQEILQDT-GAKVVLTSSP----------------------- 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 168 pastgpDDPGFWLYSSGSTGRPKGVLHSQGNpYWTAELYAKPVLSLGEAD--ICFSAaklyFAYG--LGNALTfPLSVGA 243
Cdd:cd05918 106 ------SDAAYVIFTSGSTGKPKGVVIEHRA-LSTSALAHGRALGLTSESrvLQFAS----YTFDvsILEIFT-TLAAGG 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 244 TVVLMAE---RPTPEATFRR----WLDYQPTVffgaptgyAGMLaapglpTREQV-SLRLCSSAGEALPADLGERFTAHf 315
Cdd:cd05918 174 CLCIPSEedrLNDLAGFINRlrvtWAFLTPSV--------ARLL------DPEDVpSLRTLVLGGEALTQSDVDTWADR- 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 316 gCEIIDGIGSTEmLHIF--LSNRPGQVRYGTTGWPVPG--YAVELRDEDGHaVPDGDVGDLYIQGPSAALMYWGNREKSR 391
Cdd:cd05918 239 -VRLINAYGPAE-CTIAatVSPVVPSTDPRNIGRPLGAtcWVVDPDNHDRL-VPIGAVGELLIEGPILARGYLNDPEKTA 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 392 ETF---------RGGWT-----KSGDkYVR-NADGSYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQ 456
Cdd:cd05918 316 AAFiedpawlkqEGSGRgrrlyRTGD-LVRyNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSLPGAKEVVVEVVKP 394
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 457 AGLTKTK---AFVVLKPG-----------------AQVSETELKAFVKERLAPYKYPRIIEFMDALPKTATGKIQRFRLR 516
Cdd:cd05918 395 KDGSSSPqlvAFVVLDGSssgsgdgdslflepsdeFRALVAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRALR 474
|
..
gi 1920939256 517 EM 518
Cdd:cd05918 475 EL 476
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
28-512 |
6.84e-32 |
|
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: 127.58 E-value: 6.84e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 28 PGKTAYIDDHGTMRYGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLLTADDYAYML 107
Cdd:cd17650 1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 108 QHSRAQAVLvsgallpvlrqamaqggheaatvivsrpagplpdgmialeawiernaplaapasTGPDDPGFWLYSSGSTG 187
Cdd:cd17650 81 EDSGAKLLL------------------------------------------------------TQPEDLAYVIYTSGTTG 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 188 RPKGVLHSQGNPYWTA-------ELYAKPVLSLGEADICFSAaklyFAYGLGNALTFplsvGATVVLMAE--RPTPEATF 258
Cdd:cd17650 107 KPKGVMVEHRNVAHAAhawrreyELDSFPVRLLQMASFSFDV----FAGDFARSLLN----GGTLVICPDevKLDPAALY 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 259 RRWLDYQPTVFFGAPTGYAGMLAapgLPTREQV---SLRLCSSAGEALPA----DLGERFTAHFgcEIIDGIGSTEML-- 329
Cdd:cd17650 179 DLILKSRITLMESTPALIRPVMA---YVYRNGLdlsAMRLLIVGSDGCKAqdfkTLAARFGQGM--RIINSYGVTEATid 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 330 -HIFLSNRPGQVRYGTT--GWPVPGYAVELRDEDGHAVPDGDVGDLYIQGPSAALMYWGNREKSRETFR-------GGWT 399
Cdd:cd17650 254 sTYYEEGRDPLGDSANVpiGRPLPNTAMYVLDERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVenpfapgERMY 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 400 KSGDKYVRNADGSYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQAGLTKTKAFVVlkPGAQVSETEL 479
Cdd:cd17650 334 RTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVREDKGGEARLCAYVV--AAATLNTAEL 411
|
490 500 510
....*....|....*....|....*....|...
gi 1920939256 480 KAFVKERLAPYKYPRIIEFMDALPKTATGKIQR 512
Cdd:cd17650 412 RAFLAKELPSYMIPSYYVQLDALPLTPNGKVDR 444
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
18-512 |
1.67e-31 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 129.90 E-value: 1.67e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 18 QHLIACNA-QRPGKTAYIDDHGTMRYGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNT 96
Cdd:PRK05691 2191 HGLFAAQAaRTPQAPALTFAGQTLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDP 2270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 97 LLTADDYAYMLQHSRAQAVLVSGALLPVLrqamaqggheaatvivsrpaGPLPDGmiaLEAW-IERNAPLAA-------P 168
Cdd:PRK05691 2271 EYPLERLHYMIEDSGIGLLLSDRALFEAL--------------------GELPAG---VARWcLEDDAAALAaysdaplP 2327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 169 ASTGPDDPGFWLYSSGSTGRPKGVLHSQGNpywtAELYAKPVL-SLG-EADIC--------FSAAKlyfayglgNALTFP 238
Cdd:PRK05691 2328 FLSLPQHQAYLIYTSGSTGKPKGVVVSHGE----IAMHCQAVIeRFGmRADDCelhfysinFDAAS--------ERLLVP 2395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 239 LSVGATVVLMAERPTPEATFRRWLDYQPTVFFGAPTGYAGMLAAPGLPTREQVSLRLCSSAGEALPADLGERFTAHFGCE 318
Cdd:PRK05691 2396 LLCGARVVLRAQGQWGAEEICQLIREQQVSILGFTPSYGSQLAQWLAGQGEQLPVRMCITGGEALTGEHLQRIRQAFAPQ 2475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 319 II-DGIGSTEMLHIFLSNR-PGQVRYGTTGWPVpGYAVELR-----DEDGHAVPDGDVGDLYIQGPSAALMYWGNREKSR 391
Cdd:PRK05691 2476 LFfNAYGPTETVVMPLACLaPEQLEEGAASVPI-GRVVGARvayilDADLALVPQGATGELYVGGAGLAQGYHDRPGLTA 2554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 392 ETF--------RGGWTKSGDKYVRNADGSYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVpDQAGLTKTK 463
Cdd:PRK05691 2555 ERFvadpfaadGGRLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLAL-DTPSGKQLA 2633
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1920939256 464 AFVVLKPGAQVSETE------LKAFVKERLAPYKYPRIIEFMDALPKTATGKIQR 512
Cdd:PRK05691 2634 GYLVSAVAGQDDEAQaalreaLKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDR 2688
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
28-516 |
3.34e-31 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 127.27 E-value: 3.34e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 28 PGKTAYIddHGTMRY--GELAERIRRVAGALQASGIHREERVLLL------MHDGNdwpvcfLGAMYAGIVPVAVNTLLT 99
Cdd:PLN02479 34 PTRKSVV--HGSVRYtwAQTYQRCRRLASALAKRSIGPGSTVAVIapnipaMYEAH------FGVPMAGAVVNCVNIRLN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 100 ADDYAYMLQHSRAQAVLVSGALLPVLRQAM------AQGGHEAATVIV-----SRPAG---PLPDGMIALEAWIERNAPl 165
Cdd:PLN02479 106 APTIAFLLEHSKSEVVMVDQEFFTLAEEALkilaekKKSSFKPPLLIVigdptCDPKSlqyALGKGAIEYEKFLETGDP- 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 166 aAPASTGPDDPgfWL-----YSSGSTGRPKGVLHSQGNPYWTAeLYAKPVLSLGEADICFSAAKLYFAYGLGNALTFPLS 240
Cdd:PLN02479 185 -EFAWKPPADE--WQsialgYTSGTTASPKGVVLHHRGAYLMA-LSNALIWGMNEGAVYLWTLPMFHCNGWCFTWTLAAL 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 241 VGATVVLmaERPTPEATFRRWLDYQPTVFFGAPTGYAGMLAAPG----LPTREQVSLrlcSSAGEALPADL-------GE 309
Cdd:PLN02479 261 CGTNICL--RQVTAKAIYSAIANYGVTHFCAAPVVLNTIVNAPKsetiLPLPRVVHV---MTAGAAPPPSVlfamsekGF 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 310 RFTAHFGCEIIDGIGST-----------EMLHIFLSNRPGqVRYG----------TTGWPVPGyavelrdeDGHAVpdgd 368
Cdd:PLN02479 336 RVTHTYGLSETYGPSTVcawkpewdslpPEEQARLNARQG-VRYIglegldvvdtKTMKPVPA--------DGKTM---- 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 369 vGDLYIQGPSAALMYWGNREKSRETFRGGWTKSGDKYVRNADGSYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEA 448
Cdd:PLN02479 403 -GEIVMRGNMVMKGYLKNPKANEEAFANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEA 481
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1920939256 449 AVIGVPDQAGLTKTKAFVVLKPGAQVS-----ETELKAFVKERLAPYKYPRIIEFmDALPKTATGKIQRFRLR 516
Cdd:PLN02479 482 SVVARPDERWGESPCAFVTLKPGVDKSdeaalAEDIMKFCRERLPAYWVPKSVVF-GPLPKTATGKIQKHVLR 553
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
25-512 |
6.34e-31 |
|
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: 124.59 E-value: 6.34e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 25 AQR-PGKTAYIDDHGTMRYGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLLTADDY 103
Cdd:cd17645 8 VERtPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGERI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 104 AYMLQHSRAQAVLvsgallpvlrqamaqggheaatvivsrpagplpdgmialeawiernaplaapasTGPDDPGFWLYSS 183
Cdd:cd17645 88 AYMLADSSAKILL------------------------------------------------------TNPDDLAYVIYTS 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 184 GSTGRPKGVLHSQGNPYWTAELYaKPVLSLGEADicfsAAKLYFAYGLGNAL--TFP-LSVGAT--VVLMAERPTPEATF 258
Cdd:cd17645 114 GSTGLPKGVMIEHHNLVNLCEWH-RPYFGVTPAD----KSLVYASFSFDASAweIFPhLTAGAAlhVVPSERRLDLDALN 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 259 RRWLDYQPTVFFgAPTGYAGMLAApglptREQVSLRLCSSAGEALpadlgERFTAHfGCEIIDGIGSTEMLhIFLSNRPG 338
Cdd:cd17645 189 DYFNQEGITISF-LPTGAAEQFMQ-----LDNQSLRVLLTGGDKL-----KKIERK-GYKLVNNYGPTENT-VVATSFEI 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 339 QVRYGT--TGWPVPGYAVELRDEDGHAVPDGDVGDLYIQGPSAALMYWGNREKSRETFRGGWTKSGDKYVRNAD------ 410
Cdd:cd17645 256 DKPYANipIGKPIDNTRVYILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFVPGERMYRTGDlakflp 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 411 -GSYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQAGLTKTKAFVVlkPGAQVSETELKAFVKERLAP 489
Cdd:cd17645 336 dGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVT--APEEIPHEELREWLKNDLPD 413
|
490 500
....*....|....*....|...
gi 1920939256 490 YKYPRIIEFMDALPKTATGKIQR 512
Cdd:cd17645 414 YMIPTYFVHLKALPLTANGKVDR 436
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
10-511 |
8.15e-31 |
|
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: 126.62 E-value: 8.15e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 10 PGTPFNFAQHLIACNAQrPGKTA-YIDDHGTMR---YGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFL--- 82
Cdd:cd05943 66 PGARLNYAENLLRHADA-DDPAAiYAAEDGERTevtWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLata 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 83 --GAMYAGIVP-------------VAVNTLLTADDYAYM-LQHSRAQAVLVSGALLPVLrqamaqggheAATVIVSR-PA 145
Cdd:cd05943 145 siGAIWSSCSPdfgvpgvldrfgqIEPKVLFAVDAYTYNgKRHDVREKVAELVKGLPSL----------LAVVVVPYtVA 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 146 GPLPDGMIALEA--WIERNAPLAAP----ASTGPDDPGFWLYSSGSTGRPKGVLHSQGNPYwtaeLYAKPVLSLgEADIC 219
Cdd:cd05943 215 AGQPDLSKIAKAltLEDFLATGAAGelefEPLPFDHPLYILYSSGTTGLPKCIVHGAGGTL----LQHLKEHIL-HCDLR 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 220 FSAAKLYF---AYGLGNALTFPLSVGATVVLMAERPT--PEATFRRWLDYQPTVFFGAPTGYAGMLAAPGLPTREQV--- 291
Cdd:cd05943 290 PGDRLFYYttcGWMMWNWLVSGLAVGATIVLYDGSPFypDTNALWDLADEEGITVFGTSAKYLDALEKAGLKPAETHdls 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 292 SLRLCSSAGEALPADLGERFTAHFGCEIIDGIGS--TEMLHIFLSNRPGQ-VRYGTTGWPVPGYAVELRDEDGHAVPdGD 368
Cdd:cd05943 370 SLRTILSTGSPLKPESFDYVYDHIKPDVLLASISggTDIISCFVGGNPLLpVYRGEIQCRGLGMAVEAFDEEGKPVW-GE 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 369 VGDLYIQG--PSAALMYWGNREKSR------ETFRGGWTKsGDKYVRNADGSYSYAGRSDDMLKVSGIYVSPFEVEATLA 440
Cdd:cd05943 449 KGELVCTKpfPSMPVGFWNDPDGSRyraayfAKYPGVWAH-GDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVE 527
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1920939256 441 QHPAILEAAVIGVPDQAGLTKTKAFVVLKPGAQVSET---ELKAFVKERLAPYKYP-RIIEfMDALPKTATGKIQ 511
Cdd:cd05943 528 KIPEVEDSLVVGQEWKDGDERVILFVKLREGVELDDElrkRIRSTIRSALSPRHVPaKIIA-VPDIPRTLSGKKV 601
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
173-509 |
2.03e-30 |
|
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: 121.72 E-value: 2.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 173 PDDpGFWLYSSGSTGRPKGVLHSQGN-------------PYWTAELYAKPVLSLGEADICFSAAKLYFAYGLGNALTFPL 239
Cdd:cd05924 3 ADD-LYILYTGGTTGMPKGVMWRQEDifrmlmggadfgtGEFTPSEDAHKAAAAAAGTVMFPAPPLMHGTGSWTAFGGLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 240 SvGATVVLMAERPTPEATFRRWLDYQPTVFFGAPTGYAGML--AAPGLPTREQVSLRLCSSAGEALPADLGERFTAHF-G 316
Cdd:cd05924 82 G-GQTVVLPDDRFDPEEVWRTIEKHKVTSMTIVGDAMARPLidALRDAGPYDLSSLFAISSGGALLSPEVKQGLLELVpN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 317 CEIIDGIGSTEM-LHIFLSNRPGQVRYGTTGWPVPGYAVelRDEDGHAV-PDGDVGDLYIQGPSAALMYWGNREKSRETF 394
Cdd:cd05924 161 ITLVDAFGSSETgFTGSGHSAGSGPETGPFTRANPDTVV--LDDDGRVVpPGSGGVGWIARRGHIPLGYYGDEAKTAETF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 395 R--GG--WTKSGDKYVRNADGSYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQAGLTKTKAFVVLKP 470
Cdd:cd05924 239 PevDGvrYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQEVVAVVQLRE 318
|
330 340 350
....*....|....*....|....*....|....*....
gi 1920939256 471 GAQVSETELKAFVKERLAPYKYPRIIEFMDALPKTATGK 509
Cdd:cd05924 319 GAGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
171-512 |
5.24e-30 |
|
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: 122.54 E-value: 5.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 171 TGPDDPGFWLYSSGSTGRPKGVL---HSQGNPYWT--AELYAKPVLSLGE-ADICFSAAklyfayglGNALTFPLSVGAT 244
Cdd:cd17644 103 TQPENLAYVIYTSGSTGKPKGVMiehQSLVNLSHGliKEYGITSSDRVLQfASIAFDVA--------AEEIYVTLLSGAT 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 245 VVLMAE--RPTPEATFRRWLDYQPTVFfGAPTGYAGMLAAPGLPTREQV--SLRLCSSAGEALPADLGERFTAHFGCEI- 319
Cdd:cd17644 175 LVLRPEemRSSLEDFVQYIQQWQLTVL-SLPPAYWHLLVLELLLSTIDLpsSLRLVIVGGEAVQPELVRQWQKNVGNFIq 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 320 -IDGIGSTE-----MLHIFLSNRPGQVRYGTTGWPVPGYAVELRDEDGHAVPDGDVGDLYIQGPSAALMYWGNREKSRET 393
Cdd:cd17644 254 lINVYGPTEatiaaTVCRLTQLTERNITSVPIGRPIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEK 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 394 F---------RGGWTKSGD--KYVrnADGSYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQAGLTKT 462
Cdd:cd17644 334 FishpfnsseSERLYKTGDlaRYL--PDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRL 411
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1920939256 463 KAFVVLKPGAQVSETELKAFVKERLAPYKYPRIIEFMDALPKTATGKIQR 512
Cdd:cd17644 412 VAYIVPHYEESPSTVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDR 461
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
28-515 |
1.17e-29 |
|
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: 121.35 E-value: 1.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 28 PGKTAYIDDHGTMRYGELAERIRRVAGALQASGIHR-EERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLLTADDYAYM 106
Cdd:cd17648 1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAEIRpDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 107 LQHSRAQAVLvsgallpvlrqamaqggheaatvivsrpagplpdgmialeawiernaplaapasTGPDDPGFWLYSSGST 186
Cdd:cd17648 81 LEDTGARVVI------------------------------------------------------TNSTDLAYAIYTSGTT 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 187 GRPKGVLHSQGNpywtaelyakpVLSLgeadiCFSAAKLYFAYGLGN----------------ALTFPLSVGATVVLMAE 250
Cdd:cd17648 107 GKPKGVLVEHGS-----------VVNL-----RTSLSERYFGRDNGDeavlffsnyvfdffveQMTLALLNGQKLVVPPD 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 251 --RPTPEATFRRWLDYQPTVFFGAPTgyagMLAAPGLPTREqvSLRLCSSAGEALPADLGERFTAHFGCEIIDGIGSTEM 328
Cdd:cd17648 171 emRFDPDRFYAYINREKVTYLSGTPS----VLQQYDLARLP--HLKRVDAAGEEFTAPVFEKLRSRFAGLIINAYGPTET 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 329 lHIFLSNR--PGQVRYGTT-GWPVPGYAVELRDEDGHAVPDGDVGDLYIQGPSAALMYWGNREKSRETF----------- 394
Cdd:cd17648 245 -TVTNHKRffPGDQRFDKSlGRPVRNTKCYVLNDAMKRVPVGAVGELYLGGDGVARGYLNRPELTAERFlpnpfqteqer 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 395 -RGGWT---KSGDKYVRNADGSYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIG--VPDQAGLTKTKAFV-- 466
Cdd:cd17648 324 aRGRNArlyKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAkeDASQAQSRIQKYLVgy 403
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1920939256 467 -VLKPGAqVSETELKAFVKERLAPYKYPRIIEFMDALPKTATGKIQRFRL 515
Cdd:cd17648 404 yLPEPGH-VPESDLLSFLRAKLPRYMVPARLVRLEGIPVTINGKLDVRAL 452
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
42-518 |
1.70e-29 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 122.04 E-value: 1.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 42 YGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVnTLLTA--------DDYAYMLQHSRAQ 113
Cdd:PRK09192 52 YQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPL-PLPMGfggresyiAQLRGMLASAQPA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 114 AVLVSGALLPVLRQAM-AQGGHEAATvivsrpagplPDGMIALEAwiernAPLAAPASTgPDDPGFWLYSSGSTGRPKGV 192
Cdd:PRK09192 131 AIITPDELLPWVNEAThGNPLLHVLS----------HAWFKALPE-----ADVALPRPT-PDDIAYLQYSSGSTRFPRGV 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 193 LHSQGNPYWTAELYAKPVLSLGEADICFSAAKLYFAYGLGNALTFPLSVGATVVLMAERptpeATFRR---WLDY----Q 265
Cdd:PRK09192 195 IITHRALMANLRAISHDGLKVRPGDRCVSWLPFYHDMGLVGFLLTPVATQLSVDYLPTR----DFARRplqWLDLisrnR 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 266 PTVFFGAPTGYAgmLAAPGLPTREQVSL-----RLCSSAGEALPADLGERFTAHFG------------------------ 316
Cdd:PRK09192 271 GTISYSPPFGYE--LCARRVNSKDLAELdlscwRVAGIGADMIRPDVLHQFAEAFApagfddkafmpsyglaeatlavsf 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 317 --------CEIID-GIGSTEMLHIFLSNRPGQVR-YGTTGWPVPGYAVELRDEDGHAVPDGDVGDLYIQGPSaaLM--YW 384
Cdd:PRK09192 349 splgsgivVEEVDrDRLEYQGKAVAPGAETRRVRtFVNCGKALPGHEIEIRNEAGMPLPERVVGHICVRGPS--LMsgYF 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 385 GNREKSRETFRGGWTKSGD-KYVrnADGSYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAIL--EAAVIGVPDQAGLTk 461
Cdd:PRK09192 427 RDEESQDVLAADGWLDTGDlGYL--LDGYLYITGRAKDLIIINGRNIWPQDIEWIAEQEPELRsgDAAAFSIAQENGEK- 503
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1920939256 462 tkafVVLKPGAQVSETELKAFVKERLApyKYPRIIEFMD---------ALPKTATGKIQRFRLREM 518
Cdd:PRK09192 504 ----IVLLVQCRISDEERRGQLIHALA--ALVRSEFGVEaavelvpphSLPRTSSGKLSRAKAKKR 563
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
39-517 |
1.01e-28 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 119.70 E-value: 1.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 39 TMRYGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLLTADDYAYMLQHSRAQAVL-- 116
Cdd:PLN02330 55 AVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVtn 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 117 ------VSGALLPVL---RQAMAQGGHEAATVIVSRPAGPLPDGMIALEAWIernapLAAPastgpddpgfwlYSSGSTG 187
Cdd:PLN02330 135 dtnygkVKGLGLPVIvlgEEKIEGAVNWKELLEAADRAGDTSDNEEILQTDL-----CALP------------FSSGTTG 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 188 RPKGVLHSQGNpyWTAELyAKPVLSLGEADI----CFSAAKLYFAYGLGNALTFPLSVGATVVLMAERPTpeATFRRWLD 263
Cdd:PLN02330 198 ISKGVMLTHRN--LVANL-CSSLFSVGPEMIgqvvTLGLIPFFHIYGITGICCATLRNKGKVVVMSRFEL--RTFLNALI 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 264 YQPTVFfgAPTGYAGMLAAPGLPTREQ-----VSLRLCSSAGEALPADLGERFTAHF-GCEIIDGIGSTEMLHIFLSN-R 336
Cdd:PLN02330 273 TQEVSF--APIVPPIILNLVKNPIVEEfdlskLKLQAIMTAAAPLAPELLTAFEAKFpGVQVQEAYGLTEHSCITLTHgD 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 337 P----GQVRYGTTGWPVPGYAVELRDED-GHAVPDGDVGDLYIQGPSAALMYWGNREKSRETF-RGGWTKSGDKYVRNAD 410
Cdd:PLN02330 351 PekghGIAKKNSVGFILPNLEVKFIDPDtGRSLPKNTPGELCVRSQCVMQGYYNNKEETDRTIdEDGWLHTGDIGYIDDD 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 411 GSYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQAGLTKTKAFVVLKPGAQVSETELKAFVKERLAPY 490
Cdd:PLN02330 431 GDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVVINPKAKESEEDILNFVAANVAHY 510
|
490 500
....*....|....*....|....*..
gi 1920939256 491 KYPRIIEFMDALPKTATGKIQRFRLRE 517
Cdd:PLN02330 511 KKVRVVQFVDSIPKSLSGKIMRRLLKE 537
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
42-459 |
2.57e-28 |
|
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341295 [Multi-domain] Cd Length: 468 Bit Score: 117.46 E-value: 2.57e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 42 YGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLLTADDYAYMLQHSRAQAVLVSgal 121
Cdd:cd17640 8 YKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALVVE--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 122 lpvlrqamaqggheaatvivsrpagplpdgmialeawiernaplaapasTGPDDPGFWLYSSGSTGRPKGVLHSQGNPYW 201
Cdd:cd17640 85 -------------------------------------------------NDSDDLATIIYTSGTTGNPKGVMLTHANLLH 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 202 -TAELYAkpVLSLGEADICFSAAKLYFAYGLgNALTFPLSVGatvvlMAERPTPEATFRRWL-DYQPTVFFGAPTGYAGM 279
Cdd:cd17640 116 qIRSLSD--IVPPQPGDRFLSILPIWHSYER-SAEYFIFACG-----CSQAYTSIRTLKDDLkRVKPHYIVSVPRLWESL 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 280 LA------APGLPTREQVSLRLCS--------SAGEALPADLgERFTAHFGCEIIDGIGSTEMLHIFLSNRPGQVRYGTT 345
Cdd:cd17640 188 YSgiqkqvSKSSPIKQFLFLFFLSggifkfgiSGGGALPPHV-DTFFEAIGIEVLNGYGLTETSPVVSARRLKCNVRGSV 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 346 GWPVPGYAVELRDEDGHAV-PDGDVGDLYIQGPSAALMYWGNREKSRETFRG-GWTKSGDKYVRNADGSYSYAGRSDDML 423
Cdd:cd17640 267 GRPLPGTEIKIVDPEGNVVlPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSdGWFNTGDLGWLTCGGELVLTGRAKDTI 346
|
410 420 430
....*....|....*....|....*....|....*..
gi 1920939256 424 KVS-GIYVSPFEVEATLAQHPAILEAAVIGvPDQAGL 459
Cdd:cd17640 347 VLSnGENVEPQPIEEALMRSPFIEQIMVVG-QDQKRL 382
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
13-515 |
4.49e-28 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 117.80 E-value: 4.49e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 13 PFNFAQHLIACNAQRPGKTAYIDDHGT--MRYGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIV 90
Cdd:PRK05857 13 PSTVLDRVFEQARQQPEAIALRRCDGTsaLRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 91 PVAVNTLLTADDYAYMLQHSRAQAVLVSgallpvlrQAMAQGGHEAATVIVSRPAGPLPDGMIALEAW--IERNAPLAAP 168
Cdd:PRK05857 93 AVMADGNLPIAAIERFCQITDPAAALVA--------PGSKMASSAVPEALHSIPVIAVDIAAVTRESEhsLDAASLAGNA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 169 AStGPDDPGFWLYSSGSTGRPKGVLHSQgnpywtAELYAKPvlslgeaDICFSAAKLYFAYGLGNALTFPLSV------- 241
Cdd:PRK05857 165 DQ-GSEDPLAMIFTSGTTGEPKAVLLAN------RTFFAVP-------DILQKEGLNWVTWVVGETTYSPLPAthigglw 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 242 --------GATVVLMAERptpEATFRRWL-DYQPTVFFGAPTGYAGMLAAPGLPTREQVSLRLCSSAG-EALPADLgeRF 311
Cdd:PRK05857 231 wiltclmhGGLCVTGGEN---TTSLLEILtTNAVATTCLVPTLLSKLVSELKSANATVPSLRLVGYGGsRAIAADV--RF 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 312 TAHFGCEI--IDGIGSTEMLHIFLSNRPG---QVRYGTTGWPVPGYAVELRDEDG------HAVPDGDVGDLYIQGPSAA 380
Cdd:PRK05857 306 IEATGVRTaqVYGLSETGCTALCLPTDDGsivKIEAGAVGRPYPGVDVYLAATDGigptapGAGPSASFGTLWIKSPANM 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 381 LMYWGNREKSRETFRGGWTKSGDKYVRNADGSYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQaglt 460
Cdd:PRK05857 386 LGYWNNPERTAEVLIDGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDE---- 461
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1920939256 461 ktkAFVVLKPGAQVSETELKAF----VKERLAP-YK-------YPRIIEFMDALPKTATGKIQRFRL 515
Cdd:PRK05857 462 ---EFGALVGLAVVASAELDESaaraLKHTIAArFRresepmaRPSTIVIVTDIPRTQSGKVMRASL 525
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
25-517 |
5.31e-28 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 119.50 E-value: 5.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 25 AQRPGKTAYIDDHGTMRYGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLLTADDYA 104
Cdd:PRK05691 1142 RQTPERIALVWDGGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLA 1221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 105 YMLQHSRAQAVLVSGALLPVLRQAmaqgghEAATVIvsrpagplPDGMIALEAWiernaPLAAPA-STGPDDPGFWLYSS 183
Cdd:PRK05691 1222 YMLADSGVELLLTQSHLLERLPQA------EGVSAI--------ALDSLHLDSW-----PSQAPGlHLHGDNLAYVIYTS 1282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 184 GSTGRPKGVLHSQG----NPYWTAELYAkpvlsLGEADICFSAAKLYFAYGLGNALtFPLSVGATVVLMA--ERPTPEAT 257
Cdd:PRK05691 1283 GSTGQPKGVGNTHAalaeRLQWMQATYA-----LDDSDVLMQKAPISFDVSVWECF-WPLITGCRLVLAGpgEHRDPQRI 1356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 258 FRRWLDYQPTVFFGAPTGYAGMLAAPGLptREQVSLRLCSSAGEALPADLGERFTAHF-GCEIIDGIGSTEMLhIFLSNR 336
Cdd:PRK05691 1357 AELVQQYGVTTLHFVPPLLQLFIDEPLA--AACTSLRRLFSGGEALPAELRNRVLQRLpQVQLHNRYGPTETA-INVTHW 1433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 337 PGQVRYGT---TGWPVPGYAVELRDEDGHAVPDGDVGDLYIQGPSAALMYWGNREKSRETF------RGG--WTKSGDKY 405
Cdd:PRK05691 1434 QCQAEDGErspIGRPLGNVLCRVLDAELNLLPPGVAGELCIGGAGLARGYLGRPALTAERFvpdplgEDGarLYRTGDRA 1513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 406 VRNADGSYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIgVPDQAGLTKTKAFVVLKPGAQVSETELKAFVKE 485
Cdd:PRK05691 1514 RWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVL-VREGAAGAQLVGYYTGEAGQEAEAERLKAALAA 1592
|
490 500 510
....*....|....*....|....*....|..
gi 1920939256 486 RLAPYKYPRIIEFMDALPKTATGKIQRFRLRE 517
Cdd:PRK05691 1593 ELPEYMVPAQLIRLDQMPLGPSGKLDRRALPE 1624
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
39-459 |
5.68e-28 |
|
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: 117.53 E-value: 5.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 39 TMRYGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGI--VPVAVNTLLTADDYAyMLQHSRAQ--- 113
Cdd:cd05921 25 RVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVpaAPVSPAYSLMSQDLA-KLKHLFELlkp 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 114 -AVLVSGAllPVLRQAMAQGGHEAATVIVSRpAGPLPDGMIALEAWIERNAPLAAPAS---TGPDDPGFWLYSSGSTGRP 189
Cdd:cd05921 104 gLVFAQDA--APFARALAAIFPLGTPLVVSR-NAVAGRGAISFAELAATPPTAAVDAAfaaVGPDTVAKFLFTSGSTGLP 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 190 KGVLHSQ----GNPYWTAELYAKPVlslGEADICFSAAKLYFAYGLGNALTFPLSVGATVVLMAERPTP---EATFRRWL 262
Cdd:cd05921 181 KAVINTQrmlcANQAMLEQTYPFFG---EEPPVLVDWLPWNHTFGGNHNFNLVLYNGGTLYIDDGKPMPggfEETLRNLR 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 263 DYQPTVFFGAPTGYAGMLAA----PGLPTREQVSLRLCSSAGEALPADLGERFTA----HFGCEI--IDGIGSTEMLHIF 332
Cdd:cd05921 258 EISPTVYFNVPAGWEMLVAAlekdEALRRRFFKRLKLMFYAGAGLSQDVWDRLQAlavaTVGERIpmMAGLGATETAPTA 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 333 LSNRPGQVRYGTTGWPVPGYAVELrdedghaVPDGDVGDLYIQGPSAALMYWGNREKSRETF-RGGWTKSGD--KYVRNA 409
Cdd:cd05921 338 TFTHWPTERSGLIGLPAPGTELKL-------VPSGGKYEVRVKGPNVTPGYWRQPELTAQAFdEEGFYCLGDaaKLADPD 410
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1920939256 410 D--GSYSYAGR-SDDMLKVSGIYVS--PFEVEATLAQHPAILEAAVIGvPDQAGL 459
Cdd:cd05921 411 DpaKGLVFDGRvAEDFKLASGTWVSvgPLRARAVAACAPLVHDAVVAG-EDRAEV 464
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
39-517 |
5.75e-28 |
|
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 116.30 E-value: 5.75e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 39 TMRYGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLLTADDYAYMLQHSRAQAVLVs 118
Cdd:cd05940 3 ALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLVV- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 119 gallpvlrqamaqggheaatvivsrpagplpdgmialeawiernaplaapastgpdDPGFWLYSSGSTGRPKGVLHSQGN 198
Cdd:cd05940 82 --------------------------------------------------------DAALYIYTSGTTGLPKAAIISHRR 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 199 PYWTAELYAKPVLSLGEaDICFSAAKLYFAYGLGNALTFPLSVGATVVLmaeRPTPEATfRRWLD---YQPTVFfgaptG 275
Cdd:cd05940 106 AWRGGAFFAGSGGALPS-DVLYTCLPLYHSTALIVGWSACLASGATLVI---RKKFSAS-NFWDDirkYQATIF-----Q 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 276 YAG-----MLAAPGLPTREQVSLRLCSsaGEALPADLGERFTAHFGC-EIIDGIGSTEMLHIF--LSNRPGQV-RYGTTG 346
Cdd:cd05940 176 YIGelcryLLNQPPKPTERKHKVRMIF--GNGLRPDIWEEFKERFGVpRIAEFYAATEGNSGFinFFGKPGAIgRNPSLL 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 347 WPVPGYAV---------ELRDEDGH--AVPDGDVGDL------------YIqGPSAAlmywgNREKSRETFRGG--WTKS 401
Cdd:cd05940 254 RKVAPLALvkydlesgePIRDAEGRciKVPRGEPGLLisrinplepfdgYT-DPAAT-----EKKILRDVFKKGdaWFNT 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 402 GDKYVRNADGSYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVP-----DQAGLtktkAFVVLKPGAQVSE 476
Cdd:cd05940 328 GDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQvpgtdGRAGM----AAIVLQPNEEFDL 403
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1920939256 477 TELKAFVKERLAPYKYPRIIEFMDALPKTATGKIQRFRLRE 517
Cdd:cd05940 404 SALAAHLEKNLPGYARPLFLRLQPEMEITGTFKQQKVDLRN 444
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
39-522 |
5.96e-28 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 117.67 E-value: 5.96e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 39 TMRYGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGI--VPVAVNTLLTADDYA---YMLQHSRAQ 113
Cdd:PRK08180 69 RLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALAAMYAGVpyAPVSPAYSLVSQDFGklrHVLELLTPG 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 114 AVLVSGAllPVLRQAMAQGGHEAATVIVSRPA--GPLPDGMIALEAWIERNAPLAAPASTGPDDPGFWLYSSGSTGRPKG 191
Cdd:PRK08180 149 LVFADDG--AAFARALAAVVPADVEVVAVRGAvpGRAATPFAALLATPPTAAVDAAHAAVGPDTIAKFLFTSGSTGLPKA 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 192 VLHSQGN---------PYWTAELYAKPVL--------SLGEADIcfsaaklyfaygLGNALTFplsvGATVVLMAERPTP 254
Cdd:PRK08180 227 VINTHRMlcanqqmlaQTFPFLAEEPPVLvdwlpwnhTFGGNHN------------LGIVLYN----GGTLYIDDGKPTP 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 255 ---EATFRRWLDYQPTVFFGAPTGYAGMLAA----PGLPTREQVSLRLCSSAGEALPADLGERFTA----HFGCEI--ID 321
Cdd:PRK08180 291 ggfDETLRNLREISPTVYFNVPKGWEMLVPAlerdAALRRRFFSRLKLLFYAGAALSQDVWDRLDRvaeaTCGERIrmMT 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 322 GIGSTE-----MLHIFLSNRPGQVrygttGWPVPGYAVELrdedghaVPDGDVGDLYIQGPSAALMYWGNREKSRETF-R 395
Cdd:PRK08180 371 GLGMTEtapsaTFTTGPLSRAGNI-----GLPAPGCEVKL-------VPVGGKLEVRVKGPNVTPGYWRAPELTAEAFdE 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 396 GGWTKSGD--KYVRNADGS--YSYAGR-SDDMLKVSGIYVS--PFEVEATLAQHPAILEAAVIGvPDQAGLTktkAFVVL 468
Cdd:PRK08180 439 EGYYRSGDavRFVDPADPErgLMFDGRiAEDFKLSSGTWVSvgPLRARAVSAGAPLVQDVVITG-HDRDEIG---LLVFP 514
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1920939256 469 KPGA--QVSETELKAFVKERLAPYK-YPRIIEFMDALPKTATGKIQRF-RLREMEGAP 522
Cdd:PRK08180 515 NLDAcrRLAGLLADASLAEVLAHPAvRAAFRERLARLNAQATGSSTRVaRALLLDEPP 572
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
28-515 |
1.13e-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: 116.03 E-value: 1.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 28 PGKTAYIDDHGTMRYGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLLTADDYAYML 107
Cdd:cd17656 2 PDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 108 QHSRAQAVLVSGALLPVLRQamaqggheaaTVIVSRPAGPLPDGMIALEAWIERNAplaapastgpDDPGFWLYSSGSTG 187
Cdd:cd17656 82 LDSGVRVVLTQRHLKSKLSF----------NKSTILLEDPSISQEDTSNIDYINNS----------DDLLYIIYTSGTTG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 188 RPKGVlhsqgnpywtaELYAKPVLSLGE-----ADICFSAAKLYFAyglgnALTFPLSV---------GATVVLMaerpt 253
Cdd:cd17656 142 KPKGV-----------QLEHKNMVNLLHferekTNINFSDKVLQFA-----TCSFDVCYqeifstllsGGTLYII----- 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 254 PEATFR------RWLDYQP--TVFFgaPTGYAGMLA-----APGLPTreqvSLRLCSSAGEALP-ADLGERFTAHFGCEI 319
Cdd:cd17656 201 REETKRdveqlfDLVKRHNieVVFL--PVAFLKFIFserefINRFPT----CVKHIITAGEQLViTNEFKEMLHEHNVHL 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 320 IDGIGSTEMlHIF----LSNRPGQVRYGTTGWPVPGYAVELRDEDGHAVPDGDVGDLYIQGPSAALMYWGNREKSRETFR 395
Cdd:cd17656 275 HNHYGPSET-HVVttytINPEAEIPELPPIGKPISNTWIYILDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFF 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 396 GG-------WTKSGDKYVRNADGSYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQAGLTKTKAFVVl 468
Cdd:cd17656 354 PDpfdpnerMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFV- 432
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1920939256 469 kPGAQVSETELKAFVKERLAPYKYPRIIEFMDALPKTATGKIQRFRL 515
Cdd:cd17656 433 -MEQELNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
42-452 |
3.88e-26 |
|
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341296 [Multi-domain] Cd Length: 569 Bit Score: 112.13 E-value: 3.88e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 42 YGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLLTADDYAYMLQHSRAQAVLVSG-- 119
Cdd:cd17641 14 WADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIAEDee 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 120 ---ALLPVLRQAmaqggHEAATVIVSRPAG--PLPDG-MIALEAWIERNAPLAAP---------ASTGPDDPGFWLYSSG 184
Cdd:cd17641 94 qvdKLLEIADRI-----PSVRYVIYCDPRGmrKYDDPrLISFEDVVALGRALDRRdpglyerevAAGKGEDVAVLCTTSG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 185 STGRPKGVLHSQGN--PYWTAELYAKPvlsLGEADICFSAAKL----YFAYGLGNALT------FPLS----------VG 242
Cdd:cd17641 169 TTGKPKLAMLSHGNflGHCAAYLAADP---LGPGDEYVSVLPLpwigEQMYSVGQALVcgfivnFPEEpetmmedlreIG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 243 ATVVLMAER-----------------PTPEATFRRWLD--YQ--PTVFFGAPTGYAGMLAApGL-------PTREQVSLR 294
Cdd:cd17641 246 PTFVLLPPRvwegiaadvrarmmdatPFKRFMFELGMKlgLRalDRGKRGRPVSLWLRLAS-WLadallfrPLRDRLGFS 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 295 LCSSA---GEALPADLGERFTAhFGCEIIDGIGSTEMLHIFLSNRPGQVRYGTTGWPVPGyaVELR-DEdghavpdgdVG 370
Cdd:cd17641 325 RLRSAatgGAALGPDTFRFFHA-IGVPLKQLYGQTELAGAYTVHRDGDVDPDTVGVPFPG--TEVRiDE---------VG 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 371 DLYIQGPSAALMYWGNREKSRETF-RGGWTKSGDKYVRNADGSYSYAGRSDDMLKVS-GIYVSPFEVEATLAQHPAILEA 448
Cdd:cd17641 393 EILVRSPGVFVGYYKNPEATAEDFdEDGWLHTGDAGYFKENGHLVVIDRAKDVGTTSdGTRFSPQFIENKLKFSPYIAEA 472
|
....
gi 1920939256 449 AVIG 452
Cdd:cd17641 473 VVLG 476
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
10-521 |
4.07e-26 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 112.03 E-value: 4.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 10 PGTPFNFAQHLIACnaqRPGKTAYIDDHGTMRYGELAERIRRVAGALQASGIHREERVLLLMHDgndwpvcfLGAMY--- 86
Cdd:PLN03102 13 PLTPITFLKRASEC---YPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPN--------TPAMYemh 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 87 -----AGIVPVAVNTLLTADDYAYMLQHSRAQAVLVSGALLPVLRQAMAQGGHEAAT----VI----VSRPAGPLPDGMi 153
Cdd:PLN03102 82 favpmAGAVLNPINTRLDATSIAAILRHAKPKILFVDRSFEPLAREVLHLLSSEDSNlnlpVIfiheIDFPKRPSSEEL- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 154 ALEAWIERNAPLAAPAST-----GPDDPGFWLYSSGSTGRPKGVLHSQGNPYWTAeLYAKPVLSLGEADICFSAAKLYFA 228
Cdd:PLN03102 161 DYECLIQRGEPTPSLVARmfriqDEHDPISLNYTSGTTADPKGVVISHRGAYLST-LSAIIGWEMGTCPVYLWTLPMFHC 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 229 yglgNALTFPLSV---GATVVLMAERPTPEaTFRRWLDYQPTVFFGAPTGYAGMLAAPGLPTREQVSLRLCSSAGEALPA 305
Cdd:PLN03102 240 ----NGWTFTWGTaarGGTSVCMRHVTAPE-IYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSPRSGPVHVLTGGSPPPA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 306 DLGERfTAHFGCEIIDGIGSTEML-------------------HIFLSNRPGQVRYGTTGwpvpgyaVELRD-EDGHAVP 365
Cdd:PLN03102 315 ALVKK-VQRLGFQVMHAYGLTEATgpvlfcewqdewnrlpenqQMELKARQGVSILGLAD-------VDVKNkETQESVP 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 366 -DGD-VGDLYIQGPSAALMYWGNREKSRETFRGGWTKSGDKYVRNADGSYSYAGRSDDMLKVSGIYVSPFEVEATLAQHP 443
Cdd:PLN03102 387 rDGKtMGEIVIKGSSIMKGYLKNPKATSEAFKHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYP 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 444 AILEAAVIGVPDQAGLTKTKAFVVLKPGA----------QVSETELKAFVKERLAPYKYPRIIEFMDALPKTATGKIQRF 513
Cdd:PLN03102 467 KVLETAVVAMPHPTWGETPCAFVVLEKGEttkedrvdklVTRERDLIEYCRENLPHFMCPRKVVFLQELPKNGNGKILKP 546
|
....*...
gi 1920939256 514 RLREMEGA 521
Cdd:PLN03102 547 KLRDIAKG 554
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
173-518 |
4.78e-26 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 111.81 E-value: 4.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 173 PDDPGFWLYSSGSTGRPKGVLHSQgNPYWTAELYAKPVLSLGEADICFSAAKLYFAYGLGNALTFpLSVGATVVLMaerP 252
Cdd:PLN02860 171 PDDAVLICFTSGTTGRPKGVTISH-SALIVQSLAKIAIVGYGEDDVYLHTAPLCHIGGLSSALAM-LMVGACHVLL---P 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 253 TPEAT--FRRWLDYQPTVFFGAPTGYAGMLAapglPTREQV------SLRLCSSAGEALPADLGERFTAHFGC-EIIDGI 323
Cdd:PLN02860 246 KFDAKaaLQAIKQHNVTSMITVPAMMADLIS----LTRKSMtwkvfpSVRKILNGGGSLSSRLLPDAKKLFPNaKLFSAY 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 324 GSTEM--------LH--------------IFLSNRPGQVRYGT-TGWPVPgyAVELR---DEDGHavpdgdVGDLYIQGP 377
Cdd:PLN02860 322 GMTEAcssltfmtLHdptlespkqtlqtvNQTKSSSVHQPQGVcVGKPAP--HVELKiglDESSR------VGRILTRGP 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 378 SAALMYWG-NREKSRETFRGGWTKSGDKYVRNADGSYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQ 456
Cdd:PLN02860 394 HVMLGYWGqNSETASVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDS 473
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1920939256 457 AGLTKTKAFVVLKPG--------------AQVSETELKAFVKER-LAPYKYPR-IIEFMDALPKTATGKIQRFRLREM 518
Cdd:PLN02860 474 RLTEMVVACVRLRDGwiwsdnekenakknLTLSSETLRHHCREKnLSRFKIPKlFVQWRKPFPLTTTGKIRRDEVRRE 551
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
434-509 |
6.66e-26 |
|
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.
Pssm-ID: 463804 [Multi-domain] Cd Length: 76 Bit Score: 100.70 E-value: 6.66e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1920939256 434 EVEATLAQHPAILEAAVIGVPDQAGLTKTKAFVVLKPGAQVSETELKAFVKERLAPYKYPRIIEFMDALPKTATGK 509
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
13-521 |
7.46e-26 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 112.57 E-value: 7.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 13 PFNFAQHLIACNAQRPGKTA--YIDDHG----TMRYGELAERIRRVAGALQASGIHrEERVLLLMHDGNDWPVCFLGAMY 86
Cdd:PRK05691 8 PLTLVQALQRRAAQTPDRLAlrFLADDPgegvVLSYRDLDLRARTIAAALQARASF-GDRAVLLFPSGPDYVAAFFGCLY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 87 AGIVPVAvntlltaddyAYMLQHSRAQ---------------AVLVSGALLPVLRQAMAQGGHEAATVIVSRPAGPLPdg 151
Cdd:PRK05691 87 AGVIAVP----------AYPPESARRHhqerllsiiadaeprLLLTVADLRDSLLQMEELAAANAPELLCVDTLDPAL-- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 152 miaLEAWIERNAPlaapastgPDDPGFWLYSSGSTGRPKGVLHSQGNpywtaeLYAKPVL-------SLGEADICFSAAK 224
Cdd:PRK05691 155 ---AEAWQEPALQ--------PDDIAFLQYTSGSTALPKGVQVSHGN------LVANEQLirhgfgiDLNPDDVIVSWLP 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 225 LYFAYGLGNALTFPLSVGATVVLMA-----ERPTpeatfrRWLD----YQPTVFFGAPTGYAGMLAAPGLPTREQVSL-- 293
Cdd:PRK05691 218 LYHDMGLIGGLLQPIFSGVPCVLMSpayflERPL------RWLEaiseYGGTISGGPDFAYRLCSERVSESALERLDLsr 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 294 -RLCSSAGEALPADLGERFTAHF------------------------GCEIIDGIGSTEM-LHIFLSNR--PGQvryGTT 345
Cdd:PRK05691 292 wRVAYSGSEPIRQDSLERFAEKFaacgfdpdsffasyglaeatlfvsGGRRGQGIPALELdAEALARNRaePGT---GSV 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 346 ----GWPVPGYAVELRD-EDGHAVPDGDVGDLYIQGPSAALMYWGNREKSRETF--RGG--WTKSGD-KYVRnaDGSYSY 415
Cdd:PRK05691 369 lmscGRSQPGHAVLIVDpQSLEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTFveHDGrtWLRTGDlGFLR--DGELFV 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 416 AGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAvigvpdqagltKTKAFVVLKPG-------AQVSETELKAFVKERL- 487
Cdd:PRK05691 447 TGRLKDMLIVRGHNLYPQDIEKTVEREVEVVRKG-----------RVAAFAVNHQGeegigiaAEISRSVQKILPPQALi 515
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 1920939256 488 ---------APYKYPRIIEFMD--ALPKTATGKIQR--FRLREMEGA 521
Cdd:PRK05691 516 ksirqavaeACQEAPSVVLLLNpgALPKTSSGKLQRsaCRLRLADGS 562
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
38-517 |
1.50e-25 |
|
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: 109.83 E-value: 1.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 38 GTMRYGELA-------ERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLLTADDYAYMLQHS 110
Cdd:cd05915 16 RLHTGEVHRttyaevyQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 111 RAQAVLVSGALLPVlrqamaqgGHEAATVIVSRPAGPLPDGMI-ALEAWIERNAPLAAPASTGPD-DPGFWLYSSGSTGR 188
Cdd:cd05915 96 EDKVLLFDPNLLPL--------VEAIRGELKTVQHFVVMDEKApEGYLAYEEALGEEADPVRVPErAACGMAYTTGTTGL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 189 PKGVLHSQGNPYWTA-------ELYAKPVlslgeaDICFSAAKLYFAYGLGNALTFPlSVGATVVLMAERPTPEATFRRW 261
Cdd:cd05915 168 PKGVVYSHRALVLHSlaaslvdGTALSEK------DVVLPVVPMFHVNAWCLPYAAT-LVGAKQVLPGPRLDPASLVELF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 262 LDYQPTVFFGAPTgYAGMLAAPGLPTREQVSLRLCSSAGEALPAD-------LGE-RFTAHFGCEIIDGIGST------- 326
Cdd:cd05915 241 DGEGVTFTAGVPT-VWLALADYLESTGHRLKTLRRLVVGGSAAPRsliarfeRMGvEVRQGYGLTETSPVVVQnfvkshl 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 327 ----EMLHIFLSNRPGQVRYGTtgwpvpgyAVELRDEDGHAVP-DGD-VGDLYIQGPSAALMYWGNREKSR-ETFRGGWT 399
Cdd:cd05915 320 eslsEEEKLTLKAKTGLPIPLV--------RLRVADEEGRPVPkDGKaLGEVQLKGPWITGGYYGNEEATRsALTPDGFF 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 400 KSGDKYVRNADGSYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQAGLTKTKAFVVLKPgAQVSETEL 479
Cdd:cd05915 392 RTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVVVPRG-EKPTPEEL 470
|
490 500 510
....*....|....*....|....*....|....*....
gi 1920939256 480 KAFVKERLAPYKY-PRIIEFMDALPKTATGKIQRFRLRE 517
Cdd:cd05915 471 NEHLLKAGFAKWQlPDAYVFAEEIPRTSAGKFLKRALRE 509
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
28-518 |
6.62e-25 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 109.28 E-value: 6.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 28 PGKTAYID-DHGTMRYGELAERiRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVN------TLLTA 100
Cdd:PRK06814 646 FKKLAVEDpVNGPLTYRKLLTG-AFVLGRKLKKNTPPGENVGVMLPNANGAAVTFFALQSAGRVPAMINfsagiaNILSA 724
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 101 DDYAYM--LQHSRAqavLVSGALLPVLRQAMAQGgheaATVI----VSRPAGPlpdgMIALEAWIERNAPLAAPASTGPD 174
Cdd:PRK06814 725 CKAAQVktVLTSRA---FIEKARLGPLIEALEFG----IRIIyledVRAQIGL----ADKIKGLLAGRFPLVYFCNRDPD 793
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 175 DPGFWLYSSGSTGRPKGVLHSQGNpyWTAELY-AKPVLSLGEADICFSAAKLYFAYGLGNALTFPLSVGATVVL----MA 249
Cdd:PRK06814 794 DPAVILFTSGSEGTPKGVVLSHRN--LLANRAqVAARIDFSPEDKVFNALPVFHSFGLTGGLVLPLLSGVKVFLypspLH 871
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 250 ERPTPEATFrrwlDYQPTVFFGAPT---GYAGMlAAPglptREQVSLRLCSSAGEALPADLGERFTAHFGCEIIDGIGST 326
Cdd:PRK06814 872 YRIIPELIY----DTNATILFGTDTflnGYARY-AHP----YDFRSLRYVFAGAEKVKEETRQTWMEKFGIRILEGYGVT 942
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 327 EMLHIFLSNRPGQVRYGTTGWPVPGyaVELRDEDGHAVPDGdvGDLYIQGPSAALMYW-GNREKSRETFRGGWTKSGDKY 405
Cdd:PRK06814 943 ETAPVIALNTPMHNKAGTVGRLLPG--IEYRLEPVPGIDEG--GRLFVRGPNVMLGYLrAENPGVLEPPADGWYDTGDIV 1018
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 406 VRNADGSYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQaglTKTKAFVVLKPGAQVSETELKAFVKE 485
Cdd:PRK06814 1019 TIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELWPDALHAAVSIPDA---RKGERIILLTTASDATRAAFLAHAKA 1095
|
490 500 510
....*....|....*....|....*....|....
gi 1920939256 486 RLAPYKY-PRIIEFMDALPKTATGKIQRFRLREM 518
Cdd:PRK06814 1096 AGASELMvPAEIITIDEIPLLGTGKIDYVAVTKL 1129
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
169-517 |
1.67e-24 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 108.09 E-value: 1.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 169 ASTGPDDPGFWLYSSGSTGRPKGVLHSQGNPYWTAELYAKpVLSLGEADICFSAAKLYFAYGLGNALTFPLSVGATVVLM 248
Cdd:PRK08633 777 PTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISD-VFNLRNDDVILSSLPFFHSFGLTVTLWLPLLEGIKVVYH 855
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 249 AErPTPEATFRRWLD-YQPTVFFGAPTGYAGMLAAPGLPTREQVSLRLCSSAGEALPADLGERFTAHFGCEIIDGIGSTE 327
Cdd:PRK08633 856 PD-PTDALGIAKLVAkHRATILLGTPTFLRLYLRNKKLHPLMFASLRLVVAGAEKLKPEVADAFEEKFGIRILEGYGATE 934
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 328 MLHIFLSNRP----GQV------RYGTTGWPVPGYAVELRD-EDGHAVPDGDVGDLYIQGPSAALMYWGNREKS----RE 392
Cdd:PRK08633 935 TSPVASVNLPdvlaADFkrqtgsKEGSVGMPLPGVAVRIVDpETFEELPPGEDGLILIGGPQVMKGYLGDPEKTaeviKD 1014
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 393 TFRGGWTKSGDKYVRNADGSYSYAGRSDDMLKVSGIYVSPFEVEATLAQhpaILEA-----AVIGVPDQAgltKTKAFVV 467
Cdd:PRK08633 1015 IDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAK---ALGGeevvfAVTAVPDEK---KGEKLVV 1088
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1920939256 468 L-KPGAQVSETELKAFVKERLAPYKYPRIIEFMDALPKTATGKIQRFRLRE 517
Cdd:PRK08633 1089 LhTCGAEDVEELKRAIKESGLPNLWKPSRYFKVEALPLLGSGKLDLKGLKE 1139
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
10-511 |
3.98e-24 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 106.42 E-value: 3.98e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 10 PGTPFNFAQHLIAcnAQRPGKTA--YIDDHGTMR---YGELAERIRRVAGALQASGIHREERVLLLMhdGNDWP--VCFL 82
Cdd:PRK03584 82 PGARLNYAENLLR--HRRDDRPAiiFRGEDGPRRelsWAELRRQVAALAAALRALGVGPGDRVAAYL--PNIPEtvVAML 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 83 -----GAMYAG----------------IVPVAvntLLTADDYAYM-LQHSRAQAV--LVSGalLPVLRQamaqggheaaT 138
Cdd:PRK03584 158 ataslGAIWSScspdfgvqgvldrfgqIEPKV---LIAVDGYRYGgKAFDRRAKVaeLRAA--LPSLEH----------V 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 139 VIV----SRPAGPLPDGMIALEAWIERNAPLA-APASTGPDDPGFWLYSSGSTGRPKGVLHSQGNpywtaelyakpVL-- 211
Cdd:PRK03584 223 VVVpylgPAAAAAALPGALLWEDFLAPAEAAElEFEPVPFDHPLWILYSSGTTGLPKCIVHGHGG-----------ILle 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 212 ---------SLGEADICFsaaklYF---AYGLGNALTFPLSVGATVVLM---AERPTPEATFRRWLDYQPTVFfGAPTGY 276
Cdd:PRK03584 292 hlkelglhcDLGPGDRFF-----WYttcGWMMWNWLVSGLLVGATLVLYdgsPFYPDPNVLWDLAAEEGVTVF-GTSAKY 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 277 AGMLAAPGLPTREQ---VSLRLCSSAGEALPADLGERFTAHFGCEI-IDGI-GSTEMLHIF-LSNRPGQVRYGTTGWPVP 350
Cdd:PRK03584 366 LDACEKAGLVPGEThdlSALRTIGSTGSPLPPEGFDWVYEHVKADVwLASIsGGTDICSCFvGGNPLLPVYRGEIQCRGL 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 351 GYAVELRDEDGHAVpDGDVGDLYIQG--PSAALMYWGNREKSR------ETFRGGWtKSGDKYVRNADGSYSYAGRSDDM 422
Cdd:PRK03584 446 GMAVEAWDEDGRPV-VGEVGELVCTKpfPSMPLGFWNDPDGSRyrdayfDTFPGVW-RHGDWIEITEHGGVVIYGRSDAT 523
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 423 LKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQAGLTKTKAFVVLKPGAQVSET---ELKAFVKERLAPYKYPRIIEFM 499
Cdd:PRK03584 524 LNRGGVRIGTAEIYRQVEALPEVLDSLVIGQEWPDGDVRMPLFVVLAEGVTLDDAlraRIRTTIRTNLSPRHVPDKIIAV 603
|
570
....*....|..
gi 1920939256 500 DALPKTATGKIQ 511
Cdd:PRK03584 604 PDIPRTLSGKKV 615
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
173-522 |
1.01e-23 |
|
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: 104.05 E-value: 1.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 173 PDDPGFWLYSSGSTGRPKGVLHSQGNPYWTAELYAKpVLSLGEADICFSAAKLYFAYGLGNALTFPLSVGATVVLmaERP 252
Cdd:cd05937 86 PDDPAILIYTSGTTGLPKAAAISWRRTLVTSNLLSH-DLNLKNGDRTYTCMPLYHGTAAFLGACNCLMSGGTLAL--SRK 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 253 TPEATFrrW---LDYQPTVFFgaptgYAG-----MLAAPGLPTREQVSLRLcsSAGEALPADLGERFTAHFGCEII---- 320
Cdd:cd05937 163 FSASQF--WkdvRDSGATIIQ-----YVGelcryLLSTPPSPYDRDHKVRV--AWGNGLRPDIWERFRERFNVPEIgefy 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 321 ---DGIGSTE-----------------MLHIFLSNRPGQVRYGT-TG--W--PVPGYAVEL-RDEDGHAVpdgdvGDLYI 374
Cdd:cd05937 234 aatEGVFALTnhnvgdfgagaighhglIRRWKFENQVVLVKMDPeTDdpIrdPKTGFCVRApVGEPGEML-----GRVPF 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 375 QGPSAALMYWGNREKS-----RETFRGG--WTKSGDKYVRNADGSYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILE 447
Cdd:cd05937 309 KNREAFQGYLHNEDATesklvRDVFRKGdiYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAE 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 448 AAVIGV--PD---QAGLtktkAFVVLKPGAQVSET----ELKAFVKERLAPYKYPRIIEFMDALPKTATGKIQRFRLREm 518
Cdd:cd05937 389 ANVYGVkvPGhdgRAGC----AAITLEESSAVPTEftksLLASLARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVLRD- 463
|
....
gi 1920939256 519 EGAP 522
Cdd:cd05937 464 EGVD 467
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
38-520 |
1.03e-23 |
|
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: 104.68 E-value: 1.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 38 GTMRYGELAERIRRVAGAL-QASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLLTADDYAYMLQHSRAQAVL 116
Cdd:cd05938 4 ETYTYRDVDRRSNQAARALlAHAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAKVLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 117 VSGALLPVLRQAMAQGGHEAATVIVSRPAGPlPDGMIALEAWIERNAPLAAPAS----TGPDDPGFWLYSSGSTGRPKGV 192
Cdd:cd05938 84 VAPELQEAVEEVLPALRADGVSVWYLSHTSN-TEGVISLLDKVDAASDEPVPASlrahVTIKSPALYIYTSGTTGLPKAA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 193 LHSQgnpywTAELYAKPVLSL---GEADICFSAAKLYFAYGLGNALTFPLSVGATVVLmaeRPTPEATfRRWLD---YQP 266
Cdd:cd05938 163 RISH-----LRVLQCSGFLSLcgvTADDVIYITLPLYHSSGFLLGIGGCIELGATCVL---KPKFSAS-QFWDDcrkHNV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 267 TVFFgaptgYAGMLA-----APGLPTREQVSLRLcsSAGEALPADLGERFTAHFG-CEIIDGIGSTEMLHIFL--SNRPG 338
Cdd:cd05938 234 TVIQ-----YIGELLrylcnQPQSPNDRDHKVRL--AIGNGLRADVWREFLRRFGpIRIREFYGSTEGNIGFFnyTGKIG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 339 QVryGTTGW----PVP----GYAVE----LRDEDGH--AVPDGDVGDLY--IQGPSAALMYWGNREKS-----RETFRGG 397
Cdd:cd05938 307 AV--GRVSYlyklLFPfeliKFDVEkeepVRDAQGFciPVAKGEPGLLVakITQQSPFLGYAGDKEQTekkllRDVFKKG 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 398 --WTKSGDKYVRNADGSYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVP-----DQAGLtktkAFVVLKP 470
Cdd:cd05938 385 dvYFNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVYGVTvpgheGRIGM----AAVKLKP 460
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1920939256 471 GAQVSETELKAFVKERLAPYKYPRIIEFMDALPKTATGKIQRFRLREmEG 520
Cdd:cd05938 461 GHEFDGKKLYQHVREYLPAYARPRFLRIQDSLEITGTFKQQKVRLVE-EG 509
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
10-503 |
6.06e-23 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 102.28 E-value: 6.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 10 PGTPFNFAQHLIACNAQRPGKTAYIDDHG----------TMRYGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPV 79
Cdd:PRK09274 2 MASMANIARHLPRAAQERPDQLAVAVPGGrgadgklaydELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 80 CFLGAMYAGIVPVAVNTLLTADDYAYMLQHSRAQA------------------------VLVSGALLPvlrqamaqGGHE 135
Cdd:PRK09274 82 LTFALFKAGAVPVLVDPGMGIKNLKQCLAEAQPDAfigipkahlarrlfgwgkpsvrrlVTVGGRLLW--------GGTT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 136 AATVIVSRPAGPLPdgmialeawiernaplaaPASTGPDDPGFWLYSSGSTGRPKGVLHSQGNpyWTAELYA-------K 208
Cdd:PRK09274 154 LATLLRDGAAAPFP------------------MADLAPDDMAAILFTSGSTGTPKGVVYTHGM--FEAQIEAlredygiE 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 209 PvlslGEADICfsaaklyfayglgnalTFPL------SVGATVVL--M-AERPT---PEATFRRWLDYQPTVFFGAPT-- 274
Cdd:PRK09274 214 P----GEIDLP----------------TFPLfalfgpALGMTSVIpdMdPTRPAtvdPAKLFAAIERYGVTNLFGSPAll 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 275 ---GYAGMLAAPGLPtreqvSLRLCSSAGEALPADLGERFTAHF--GCEIIDGIGSTEMLHI-FLSNRpgQVRYGTT--- 345
Cdd:PRK09274 274 erlGRYGEANGIKLP-----SLRRVISAGAPVPIAVIERFRAMLppDAEILTPYGATEALPIsSIESR--EILFATRaat 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 346 --------GWPVPGYAVELRD---------EDGHAVPDGDVGDLYIQGPSAALMYWGNRE-----KSRETFRGGWTKSGD 403
Cdd:PRK09274 347 dngagicvGRPVDGVEVRIIAisdapipewDDALRLATGEIGEIVVAGPMVTRSYYNRPEatrlaKIPDGQGDVWHRMGD 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 404 KYVRNADGSYSYAGR-SDDMLKVSGIYVSpFEVEATLAQHPAILEAAVIGVPDQAGltKTKAFVV-LKPGAQVSETELKA 481
Cdd:PRK09274 427 LGYLDAQGRLWFCGRkAHRVETAGGTLYT-IPCERIFNTHPGVKRSALVGVGVPGA--QRPVLCVeLEPGVACSKSALYQ 503
|
570 580
....*....|....*....|....*
gi 1920939256 482 FVKERLAPYKYPRIIE---FMDALP 503
Cdd:PRK09274 504 ELRALAAAHPHTAGIErflIHPSFP 528
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
42-490 |
5.24e-22 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 99.74 E-value: 5.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 42 YGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGI--VPVAVNTLLTADDYA---YMLQHSRAQAVL 116
Cdd:PRK12582 83 YGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAGVpaAPVSPAYSLMSHDHAklkHLFDLVKPRVVF 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 117 V-SGALLpvlRQAMAQGGHEAATVIVsrpAGPLPDGM--IALEAWIE---RNAPLAAPASTGPDDPGFWLYSSGSTGRPK 190
Cdd:PRK12582 163 AqSGAPF---ARALAALDLLDVTVVH---VTGPGEGIasIAFADLAAtppTAAVAAAIAAITPDTVAKYLFTSGSTGMPK 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 191 GVLHSQGNPYWTAELYAKPVLSLGEADICFSAAKLYFAYGLGNALTFP--LSVGATVVLMAERPTP---EATFRRWLDYQ 265
Cdd:PRK12582 237 AVINTQRMMCANIAMQEQLRPREPDPPPPVSLDWMPWNHTMGGNANFNglLWGGGTLYIDDGKPLPgmfEETIRNLREIS 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 266 PTVFFGAPTGYAgMLAA-----PGLPTREQVSLRLCSSAGEALPADLGERFTAHFGCE------IIDGIGSTEMLHIFLS 334
Cdd:PRK12582 317 PTVYGNVPAGYA-MLAEamekdDALRRSFFKNLRLMAYGGATLSDDLYERMQALAVRTtghripFYTGYGATETAPTTTG 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 335 NRPGQVRYGTTGWPVPGYAVELrdedghaVPDGDVGDLYIQGPSAALMYWGNREKSRETF-RGGWTKSGD--KYVRNADG 411
Cdd:PRK12582 396 THWDTERVGLIGLPLPGVELKL-------APVGDKYEVRVKGPNVTPGYHKDPELTAAAFdEEGFYRLGDaaRFVDPDDP 468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 412 SYS--YAGR-SDDMLKVSGIYVS--PFEVEATLAQHPAILEAAVIGV----------PDQAGLTKTKAFVVLKPGAQVSE 476
Cdd:PRK12582 469 EKGliFDGRvAEDFKLSTGTWVSvgTLRPDAVAACSPVIHDAVVAGQdrafigllawPNPAACRQLAGDPDAAPEDVVKH 548
|
490
....*....|....
gi 1920939256 477 TELKAFVKERLAPY 490
Cdd:PRK12582 549 PAVLAILREGLSAH 562
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
42-519 |
1.46e-21 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 99.47 E-value: 1.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 42 YGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLLTADDYAYMLQHSRAqAVLVSGAl 121
Cdd:PRK05691 3748 YAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGLPAQRLQRIIELSRT-PVLVCSA- 3825
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 122 lpvlrqAMAQGGHE--AATVIVSRPAgplpdgmiaLEAWIE---RNAPLAAPA-STGPDDPGFWLYSSGSTGRPKGVLHS 195
Cdd:PRK05691 3826 ------ACREQARAllDELGCANRPR---------LLVWEEvqaGEVASHNPGiYSGPDNLAYVIYTSGSTGLPKGVMVE 3890
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 196 QGNpYWTAELYAKPVLSLGEADICFSAAKLYFAYGLGNALTFPLsVGATVVLM--AERPTPEATFRRWLDYQPTVFFGAP 273
Cdd:PRK05691 3891 QRG-MLNNQLSKVPYLALSEADVIAQTASQSFDISVWQFLAAPL-FGARVEIVpnAIAHDPQGLLAHVQAQGITVLESVP 3968
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 274 TGYAGMLAAPGLPTReqvSLRLCSSAGEALPADLGERFTAHF-GCEIIDGIGSTE------MLHIFLSNRPGQvrYGTTG 346
Cdd:PRK05691 3969 SLIQGMLAEDRQALD---GLRWMLPTGEAMPPELARQWLQRYpQIGLVNAYGPAEcsddvaFFRVDLASTRGS--YLPIG 4043
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 347 WPVPGYAVELRDEDGHAVPDGDVGDLYIQGPSAALMYWGNREKSRETF----RGG----WTKSGDKYVRNADGSYSYAGR 418
Cdd:PRK05691 4044 SPTDNNRLYLLDEALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFvphpFGApgerLYRTGDLARRRSDGVLEYVGR 4123
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 419 SDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIgvpDQAGLTKTKAFVVLKPG-AQVSETELKAFVKERLAP----YKYP 493
Cdd:PRK05691 4124 IDHQVKIRGYRIELGEIEARLHEQAEVREAAVA---VQEGVNGKHLVGYLVPHqTVLAQGALLERIKQRLRAelpdYMVP 4200
|
490 500
....*....|....*....|....*.
gi 1920939256 494 RIIEFMDALPKTATGKIQRFRLREME 519
Cdd:PRK05691 4201 LHWLWLDRLPLNANGKLDRKALPALD 4226
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
42-517 |
1.51e-21 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 97.93 E-value: 1.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 42 YGELAERIRRVAGALQAS-GIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLLTADDYAYMLQHSRAQAVLVSGA 120
Cdd:PRK05620 41 FAAIGARAAALAHALHDElGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIVADPR 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 121 LLPVLRQAMAQ-GGHEAATVI----VSRPAGPLPDGM--IALEAWIERNAPLAAPASTGPDDPGFWLYSSGSTGRPKGVL 193
Cdd:PRK05620 121 LAEQLGEILKEcPCVRAVVFIgpsdADSAAAHMPEGIkvYSYEALLDGRSTVYDWPELDETTAAAICYSTGTTGAPKGVV 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 194 HSQgNPYWTAELYAKPVLSL----GEADICfsAAKLYFAYGLGNALTFPLSvGATVVLMAERPTPEATFRRWLDYQPTVF 269
Cdd:PRK05620 201 YSH-RSLYLQSLSLRTTDSLavthGESFLC--CVPIYHVLSWGVPLAAFMS-GTPLVFPGPDLSAPTLAKIIATAMPRVA 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 270 FGAPTGYAGMLAAPGLPTREQVSLRLCSSAGEALPADLGERFTAHFGCEIIDGIGSTEMLHIFLSNRPGQVRYGTTGW-- 347
Cdd:PRK05620 277 HGVPTLWIQLMVHYLKNPPERMSLQEIYVGGSAVPPILIKAWEERYGVDVVHVWGMTETSPVGTVARPPSGVSGEARWay 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 348 -------PVpgyAVELR-DEDGHAVP--DGDVGDLYIQGPSAALMYW----GNREKSRETFRG-------------GWTK 400
Cdd:PRK05620 357 rvsqgrfPA---SLEYRiVNDGQVMEstDRNEGEIQVRGNWVTASYYhsptEEGGGAASTFRGedvedandrftadGWLR 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 401 SGDKYVRNADGSYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQAGLTKTKAFVVLKPGAQVSE---T 477
Cdd:PRK05620 434 TGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLAVTVLAPGIEPTRetaE 513
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1920939256 478 ELKAFVKERLAPYKYPRIIEFMDALPKTATGKIQRFRLRE 517
Cdd:PRK05620 514 RLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDLRQ 553
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
42-516 |
1.85e-21 |
|
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: 97.11 E-value: 1.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 42 YGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLLTADDYAYMLQHSRAQAVLVsgal 121
Cdd:cd05939 6 FRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALIF---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 122 lpvlrqamaqggheaatvivsrpagplpdgmialeawiERNAPLAAPASTGP--------DDPGFWLYSSGSTGRPKGVL 193
Cdd:cd05939 82 --------------------------------------NLLDPLLTQSSTEPpsqddvnfRDKLFYIYTSGTTGLPKAAV 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 194 HSQGNPYWTAELYAKpVLSLGEADICFSAAKLYFA----YGLGNALTFplsvGATVVLmaeRPTPEATfRRWLD---YQP 266
Cdd:cd05939 124 IVHSRYYRIAAGAYY-AFGMRPEDVVYDCLPLYHSaggiMGVGQALLH----GSTVVI---RKKFSAS-NFWDDcvkYNC 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 267 TVffgapTGYAG-----MLAAPGLPTREQVSLRLcsSAGEALPADLGERFTAHFGCEIIDGI-GSTEMlHIFLSNRPGQV 340
Cdd:cd05939 195 TI-----VQYIGeicryLLAQPPSEEEQKHNVRL--AVGNGLRPQIWEQFVRRFGIPQIGEFyGATEG-NSSLVNIDNHV 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 341 -------RYGTTGWPVPGYAVE------LRDEDGHAVPDGD------VGDLYIQGPSAALMYWGNREKS-----RETFRG 396
Cdd:cd05939 267 gacgfnsRILPSVYPIRLIKVDedtgelIRDSDGLCIPCQPgepgllVGKIIQNDPLRRFDGYVNEGATnkkiaRDVFKK 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 397 G--WTKSGDKYVRNADGSYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGV--PDQAGLTKTKAFVVlkPGA 472
Cdd:cd05939 347 GdsAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVYGVevPGVEGRAGMAAIVD--PER 424
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1920939256 473 QVSETELKAFVKERLAPYKYPRIIEFMDALPKTATGKIQRFRLR 516
Cdd:cd05939 425 KVDLDRFSAVLAKSLPPYARPQFIRLLPEVDKTGTFKLQKTDLQ 468
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
176-512 |
1.94e-20 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 94.81 E-value: 1.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 176 PGFWLYSSGSTGRPKGVLHSQGNPYWTAELYAKPVLSLGEADICFSAAKL------YFAYGLgnaltfpLSVGATVVLMA 249
Cdd:PTZ00237 256 PLYILYTSGTTGNSKAVVRSNGPHLVGLKYYWRSIIEKDIPTVVFSHSSIgwvsfhGFLYGS-------LSLGNTFVMFE 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 250 ERPTPEATFRRWL-----DYQPTVFFGAPTGYAGMLAAPglPTREQV-------SLRLCSSAGEALPADLGERFTAHFGC 317
Cdd:PTZ00237 329 GGIIKNKHIEDDLwntieKHKVTHTLTLPKTIRYLIKTD--PEATIIrskydlsNLKEIWCGGEVIEESIPEYIENKLKI 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 318 EIIDGIGSTE--MLHIF---LSNRPgqvrYGTTGWPVPGYAVELRDEDGHAVPDGDVGDLYIQ---GPSAALMYWGNREK 389
Cdd:PTZ00237 407 KSSRGYGQTEigITYLYcygHINIP----YNATGVPSIFIKPSILSEDGKELNVNEIGEVAFKlpmPPSFATTFYKNDEK 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 390 SRETFRG--GWTKSGDKYVRNADGSYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQAGLTKTKAFVV 467
Cdd:PTZ00237 483 FKQLFSKfpGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPIGLLV 562
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1920939256 468 LKPGAQVS-------ETELKAFVKERLAPYKYPRIIEFMDALPKTATGKIQR 512
Cdd:PTZ00237 563 LKQDQSNQsidlnklKNEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPR 614
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
39-497 |
8.23e-20 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.
Pssm-ID: 341294 [Multi-domain] Cd Length: 507 Bit Score: 92.28 E-value: 8.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 39 TMRYGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLLTADDYAYMLQHSRAQAVLVS 118
Cdd:cd17639 5 YMSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECSAIFTD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 119 GallpvlrqamaqggheaatvivsrpagplpdgmialeawiernaplaapastGPDDPGFWLYSSGSTGRPKGVLHSQGN 198
Cdd:cd17639 85 G----------------------------------------------------KPDDLACIMYTSGSTGNPKGVMLTHGN 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 199 PYWTAELYAKPVLS-LGEADIcfsaaklYFAYgLGNALTFPLSV-------GATVVLMAERPTPEATFRR----WLDYQP 266
Cdd:cd17639 113 LVAGIAGLGDRVPElLGPDDR-------YLAY-LPLAHIFELAAenvclyrGGTIGYGSPRTLTDKSKRGckgdLTEFKP 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 267 TVFFGAP--------------------------TGYAGMLAA----PGLPTREQV-----------SLRLCSSAGEALPA 305
Cdd:cd17639 185 TLMVGVPaiwdtirkgvlaklnpmgglkrtlfwTAYQSKLKAlkegPGTPLLDELvfkkvraalggRLRYMLSGGAPLSA 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 306 DlGERFTAHFGCEIIDGIGSTEMLHIFLSNRPGQVRYGTTGWPVPGYAVELRD-EDGHAVPDGDV--GDLYIQGPSAALM 382
Cdd:cd17639 265 D-TQEFLNIVLCPVIQGYGLTETCAGGTVQDPGDLETGRVGPPLPCCEIKLVDwEEGGYSTDKPPprGEILIRGPNVFKG 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 383 YWGNREKSRETFRG-GWTKSGDKYVRNADGSYSYAGRSDDMLKVS-GIYVSPFEVEATLAQHPAILEAAVIGVPDQaglT 460
Cdd:cd17639 344 YYKNPEKTKEAFDGdGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQnGEYIALEKLESIYRSNPLVNNICVYADPDK---S 420
|
490 500 510
....*....|....*....|....*....|....*...
gi 1920939256 461 KTKAFVVlkpgaqVSETELKAFVKERLAPYK-YPRIIE 497
Cdd:cd17639 421 YPVAIVV------PNEKHLTKLAEKHGVINSeWEELCE 452
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
28-515 |
6.87e-19 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 89.57 E-value: 6.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 28 PGKTAYIDDHGTMRYGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGI--VPVAVNTllTADDYAY 105
Cdd:PRK04813 16 PDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHayIPVDVSS--PAERIEM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 106 MLQHSRAQAVLVSGAL------LPVLRQAMAQggheaatvivsrpAGPLPDGMIALEAWIErnaplaapastgPDDPGFW 179
Cdd:PRK04813 94 IIEVAKPSLIIATEELpleilgIPVITLDELK-------------DIFATGNPYDFDHAVK------------GDDNYYI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 180 LYSSGSTGRPKGVLHSQGN----PYWTAELYAKPvlslgEADICFSAAklyfayglgnALTFPLSV---------GATVV 246
Cdd:PRK04813 149 IFTSGTTGKPKGVQISHDNlvsfTNWMLEDFALP-----EGPQFLNQA----------PYSFDLSVmdlyptlasGGTLV 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 247 LMAERPT--PEATFRRWLDYQPTVFFGAPTgYAGM-LAAPGLPTREQVSLR---LCssaGEALPAD----LGERF-TAHf 315
Cdd:PRK04813 214 ALPKDMTanFKQLFETLPQLPINVWVSTPS-FADMcLLDPSFNEEHLPNLThflFC---GEELPHKtakkLLERFpSAT- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 316 gceIIDGIGSTE-------------MLhiflsnrpgqvrygTTGWPVP-GYAVE-----LRDEDGHAVPDGDVGDLYIQG 376
Cdd:PRK04813 289 ---IYNTYGPTEatvavtsieitdeML--------------DQYKRLPiGYAKPdspllIIDEEGTKLPDGEQGEIVISG 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 377 PSAALMYWGNREKSRE---TFRGGWT-KSGDKyVRNADGSYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIG 452
Cdd:PRK04813 352 PSVSKGYLNNPEKTAEaffTFDGQPAyHTGDA-GYLEDGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVVP 430
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1920939256 453 VPDQAGLTKTKAFVVLKPGAQVSETEL----KAFVKERLAPYKYPRIIEFMDALPKTATGKIQRFRL 515
Cdd:PRK04813 431 YNKDHKVQYLIAYVVPKEEDFEREFELtkaiKKELKERLMEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
42-453 |
2.63e-16 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 81.35 E-value: 2.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 42 YGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLLTaddyaymlqhsraqavlvsgal 121
Cdd:cd05910 5 FRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMG---------------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 122 lpvlRQAMAQGGHEAAtvivsrpagplPDGMIALeawiernaPLAapastgpDDPGFWLYSSGSTGRPKGVLHSQGNpyw 201
Cdd:cd05910 63 ----RKNLKQCLQEAE-----------PDAFIGI--------PKA-------DEPAAILFTSGSTGTPKGVVYRHGT--- 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 202 taelyakpvlslGEADICFSAAKLYFAYGLGNALTFPL------SVGATVVLMAERPT------PEATFRRWLDYQPTVF 269
Cdd:cd05910 110 ------------FAAQIDALRQLYGIRPGEVDLATFPLfalfgpALGLTSVIPDMDPTrparadPQKLVGAIRQYGVSIV 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 270 FGAPTGYAGMLAAPGLPTREQVSLRLCSSAGEALPADLGERFTA--HFGCEIIDGIGSTEMLHI--------FLSNRPGQ 339
Cdd:cd05910 178 FGSPALLERVARYCAQHGITLPSLRRVLSAGAPVPIALAARLRKmlSDEAEILTPYGATEALPVssigsrelLATTTAAT 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 340 VRYGTT--GWPVPGYAV---ELRDE------DGHAVPDGDVGDLYIQGPSAALMYWGNRE-----KSRETFRGGWTKSGD 403
Cdd:cd05910 258 SGGAGTcvGRPIPGVRVriiEIDDEpiaewdDTLELPRGEIGEITVTGPTVTPTYVNRPVatalaKIDDNSEGFWHRMGD 337
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1920939256 404 KYVRNADGSYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGV 453
Cdd:cd05910 338 LGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVGV 387
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
409-523 |
3.60e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 80.47 E-value: 3.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 409 ADGSYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQAGLTKTKAFVVLKPGaqVSETELKAFVKERLA 488
Cdd:PRK08308 303 ERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVISHEE--IDPVQLREWCIQHLA 380
|
90 100 110
....*....|....*....|....*....|....*
gi 1920939256 489 PYKYPRIIEFMDALPKTATGKIQRfRLREMEGAPA 523
Cdd:PRK08308 381 PYQVPHEIESVTEIPKNANGKVSR-KLLELGEVTA 414
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
182-514 |
7.94e-16 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 79.42 E-value: 7.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 182 SSGSTGRPKGVLHSQGNPYWTAELYAKPVLSLG--EADICFSAaklyFAYGLGNA-LTFPLS---VGATVVlmaerPT-- 253
Cdd:COG1541 91 SSGTTGKPTVVGYTRKDLDRWAELFARSLRAAGvrPGDRVQNA----FGYGLFTGgLGLHYGaerLGATVI-----PAgg 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 254 --PEATFRRWLDYQPTVFFGAPTgYAGMLA----APGLPTREqVSLR--LCSsaGEALPADLGERFTAHFGCEIIDGIGS 325
Cdd:COG1541 162 gnTERQLRLMQDFGPTVLVGTPS-YLLYLAevaeEEGIDPRD-LSLKkgIFG--GEPWSEEMRKEIEERWGIKAYDIYGL 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 326 TEM-------------LHI----FLsnrpgqvrygttgwpvpgyaVELRD-EDGHAVPDGDVGDL--------------- 372
Cdd:COG1541 238 TEVgpgvayeceaqdgLHIwedhFL--------------------VEIIDpETGEPVPEGEEGELvvttltkeampliry 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 373 -------YIQGPSAalmyWGnreksRETFR-GGWTksgdkyvrnadgsysyaGRSDDMLKVSGIYVSPFEVEATLAQHPA 444
Cdd:COG1541 298 rtgdltrLLPEPCP----CG-----RTHPRiGRIL-----------------GRADDMLIIRGVNVFPSQIEEVLLRIPE 351
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1920939256 445 ILEAAVIGVPDQAGLTKTKAFVVLKPGAqvSETELKAFVKERLapYKYPRI---IEF--MDALPKTaTGKIQRFR 514
Cdd:COG1541 352 VGPEYQIVVDREGGLDELTVRVELAPGA--SLEALAEAIAAAL--KAVLGLraeVELvePGSLPRS-EGKAKRVI 421
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
158-522 |
1.31e-15 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 79.75 E-value: 1.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 158 WIERN--APLAAPASTGPDDPGFWLYSSGSTGRPKGVLHSQGNPYWTAElYAKPVLSLGEADICFSAAKLYFAYGLGNAL 235
Cdd:PRK08043 347 WIFAHllMPRLAQVKQQPEDAALILFTSGSEGHPKGVVHSHKSLLANVE-QIKTIADFTPNDRFMSALPLFHSFGLTVGL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 236 TFPLSVGATVVL----MAERPTPEATFrrwlDYQPTVFFGAPT--GYAGMLAAPGLPTReqvsLRLCSSAGEALPADLGE 309
Cdd:PRK08043 426 FTPLLTGAEVFLypspLHYRIVPELVY----DRNCTVLFGTSTflGNYARFANPYDFAR----LRYVVAGAEKLQESTKQ 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 310 RFTAHFGCEIIDGIGSTEMLHIFLSNRPGQVRYGTTGWPVPGYAVELRDEDGhaVPDGdvGDLYIQGPSAALMYW----- 384
Cdd:PRK08043 498 LWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLSVPG--IEQG--GRLQLKGPNIMNGYLrvekp 573
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 385 --------GNREKSRETfrgGWTKSGDKYVRNADGSYSYAGRSDDMLKVSGIYVSPFEVEA-TLAQHPAILEAAVIgVPD 455
Cdd:PRK08043 574 gvlevptaENARGEMER---GWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQlALGVSPDKQHATAI-KSD 649
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1920939256 456 QAgltKTKAFVVLKPGAQVSETELKAFVKERLAP-YKYPRIIEFMDALPKTATGKIQRFRLREMEGAP 522
Cdd:PRK08043 650 AS---KGEALVLFTTDSELTREKLQQYAREHGVPeLAVPRDIRYLKQLPLLGSGKPDFVTLKSMVDEP 714
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
39-452 |
1.50e-15 |
|
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: 79.32 E-value: 1.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 39 TMRYGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLLTADDYAYMLQHSRAQAVLVS 118
Cdd:cd05933 8 TLTYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSEANILVVE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 119 GA-LLPVLRQAMAQGGHEAATVIVSrpaGPLPDGMIALEAW---------IERNAPLAAPASTGPDDPGFWLYSSGSTGR 188
Cdd:cd05933 88 NQkQLQKILQIQDKLPHLKAIIQYK---EPLKEKEPNLYSWdefmelgrsIPDEQLDAIISSQKPNQCCTLIYTSGTTGM 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 189 PKGVLHSQGNPYWTAElYAKPVLSLGEADI-----------CFSAAKLYFAYglgnaltFPLSVGATVVLmaerPTPEA- 256
Cdd:cd05933 165 PKGVMLSHDNITWTAK-AASQHMDLRPATVgqesvvsylplSHIAAQILDIW-------LPIKVGGQVYF----AQPDAl 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 257 ------TFRrwlDYQPTVFFGAP-----------------TGYAGMLAA-------------PGLPTREQVSLRL----- 295
Cdd:cd05933 233 kgtlvkTLR---EVRPTAFMGVPrvwekiqekmkavgaksGTLKRKIASwakgvgletnlklMGGESPSPLFYRLakklv 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 296 ---------------CSSAGEALPADLGERFTAhFGCEIIDGIGSTEMLHIFLSNRPGQVRYGTTGWPVPGYAVELRDED 360
Cdd:cd05933 310 fkkvrkalgldrcqkFFTGAAPISRETLEFFLS-LNIPIMELYGMSETSGPHTISNPQAYRLLSCGKALPGCKTKIHNPD 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 361 GhavpDGDvGDLYIQGPSAALMYWGNREKSRETF-RGGWTKSGDKYVRNADGSYSYAGRSDDMLKVS-GIYVSPFEVEAT 438
Cdd:cd05933 389 A----DGI-GEICFWGRHVFMGYLNMEDKTEEAIdEDGWLHSGDLGKLDEDGFLYITGRIKELIITAgGENVPPVPIEDA 463
|
490
....*....|....*
gi 1920939256 439 LAQH-PAILEAAVIG 452
Cdd:cd05933 464 VKKElPIISNAMLIG 478
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
42-517 |
5.68e-15 |
|
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: 77.14 E-value: 5.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 42 YGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTlltADDYAYMLQhsraqavlvsgaL 121
Cdd:cd05908 18 YRHLREEALGYLGALQELGIKPGQEVVFQITHNNKFLYLFWACLLGGMIAVPVSI---GSNEEHKLK------------L 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 122 LPVLRqamaqggheaatvIVSRPAgplpdgMIALEAWIERNaplaapastgPDDPGFWLYSSGSTGRPKGVLHSQGNPYW 201
Cdd:cd05908 83 NKVWN-------------TLKNPY------LITEEEVLCEL----------ADELAFIQFSSGSTGDPKGVMLTHENLVH 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 202 TAELYAKPvLSLGEADICFSAAKLYFAYGLGNALTFPLSVGATVVLMaerptPEATFRR----WL----DYQPTVFFGAP 273
Cdd:cd05908 134 NMFAILNS-TEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGMNQYLM-----PTRLFIRrpilWLkkasEHKATIVSSPN 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 274 TGYAGMLAAPGLPTREQV---SLRLCSSAGEALPADLGERFTAHFGceiIDGIGSTEMLHIF--------LSNRPGQVRY 342
Cdd:cd05908 208 FGYKYFLKTLKPEKANDWdlsSIRMILNGAEPIDYELCHEFLDHMS---KYGLKRNAILPVYglaeasvgASLPKAQSPF 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 343 GT---------TGWPVP---------------GYAV---ELR--DEDGHAVPDGDVGDLYIQGPSAALMYWGNREKSRET 393
Cdd:cd05908 285 KTitlgrrhvtHGEPEPevdkkdsecltfvevGKPIdetDIRicDEDNKILPDGYIGHIQIRGKNVTPGYYNNPEATAKV 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 394 FRG-GWTKSGDK-YVRNadGSYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAIL--EAAVIGVPDQAglTKTKAFVVLK 469
Cdd:cd05908 365 FTDdGWLKTGDLgFIRN--GRLVITGREKDIIFVNGQNVYPHDIERIAEELEGVElgRVVACGVNNSN--TRNEEIFCFI 440
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1920939256 470 PGAQvSETELKAF---VKERLAPYKYPRIIEF--MDALPKTATGKIQRFRLRE 517
Cdd:cd05908 441 EHRK-SEDDFYPLgkkIKKHLNKRGGWQINEVlpIRRIPKTTSGKVKRYELAQ 492
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
42-512 |
1.66e-14 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 76.19 E-value: 1.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 42 YGELAERIRRVAGALQASGIHREERVlllmhdgndwpvcflgAMYAGiVPVAVNTLltaddyaymlqhsrAQAVLVSGAL 121
Cdd:PRK07768 32 WGEVHERARRIAGGLAAAGVGPGDAV----------------AVLAG-APVEIAPT--------------AQGLWMRGAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 122 LPVLRQAMAQ--------------GGHEAATVIVSRP---AGPL--PDGMIALEAWIERNAPLAAPASTGPDDPGFWLYS 182
Cdd:PRK07768 81 LTMLHQPTPRtdlavwaedtlrviGMIGAKAVVVGEPflaAAPVleEKGIRVLTVADLLAADPIDPVETGEDDLALMQLT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 183 SGSTGRPKGVLHSQGNPYWTAELYAKPVLSLGEADICFSAAKLYFAYGLGNALTFPLSVGATVVLMaerpTPEATFRR-- 260
Cdd:PRK07768 161 SGSTGSPKAVQITHGNLYANAEAMFVAAEFDVETDVMVSWLPLFHDMGMVGFLTVPMYFGAELVKV----TPMDFLRDpl 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 261 -WLD----YQPTVFFGAPTGYAgmLAAPGL---PTREQV---SLRLCSSAGEAL-PADLgERFT---AHFG--------- 316
Cdd:PRK07768 237 lWAEliskYRGTMTAAPNFAYA--LLARRLrrqAKPGAFdlsSLRFALNGAEPIdPADV-EDLLdagARFGlrpeailpa 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 317 --------------------CEIIDGiGSTEMLHIFL-SNRPGQVRYGTTGWPVPGYAVELRDEDGHAVPDGDVGDLYIQ 375
Cdd:PRK07768 314 ygmaeatlavsfspcgaglvVDEVDA-DLLAALRRAVpATKGNTRRLATLGPPLPGLEVRVVDEDGQVLPPRGVGVIELR 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 376 GPSAALMYW---GNREKSREtfrGGWTKSGDKYVRNADGSYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIG 452
Cdd:PRK07768 393 GESVTPGYLtmdGFIPAQDA---DGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVRPGNAVA 469
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1920939256 453 VPDQAGLTKTKAFVVLKPGAQVSETELKAFVKE-----RLAPYKYPRIIEFMDA--LPKTATGKIQR 512
Cdd:PRK07768 470 VRLDAGHSREGFAVAVESNAFEDPAEVRRIRHQvahevVAEVGVRPRNVVVLGPgsIPKTPSGKLRR 536
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
362-518 |
4.19e-14 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 74.26 E-value: 4.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 362 HA---VPDGDVGDLYIQGPSAALMYWGNREKSRETFrggwtKSGDKYVRNADGSYSYAGRSDDMLKVSGIYVSPFEVEAT 438
Cdd:PRK07445 291 HAqitIPANQTGNITIQAQSLALGYYPQILDSQGIF-----ETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAA 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 439 LAQHPAILEAAVIGVPDQAGLTKTKAFVVLKPGaQVSETELKAFVKERLAPYKYPRIIEFMDALPKTATGKIQRFRLREM 518
Cdd:PRK07445 366 ILATGLVQDVCVLGLPDPHWGEVVTAIYVPKDP-SISLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQQI 444
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
346-518 |
6.76e-14 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 73.16 E-value: 6.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 346 GWPVPGyaVELRDEDGHavpdgdvgdLYIQGPSAALMYwGNREKSRETFRGGWTKSGDKYVRNaDGSYSYAGRSDDMLKV 425
Cdd:PRK07824 195 GVPLDG--VRVRVEDGR---------IALGGPTLAKGY-RNPVDPDPFAEPGWFRTDDLGALD-DGVLTVLGRADDAIST 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 426 SGIYVSPFEVEATLAQHPAILEAAVIGVPDQAGLTKTKAFVVLKPGAQVSETELKAFVKERLAPYKYPRIIEFMDALPKT 505
Cdd:PRK07824 262 GGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAVVGDGGPAPTLEALRAHVARTLDRTAAPRELHVVDELPRR 341
|
170
....*....|...
gi 1920939256 506 ATGKIQRFRLREM 518
Cdd:PRK07824 342 GIGKVDRRALVRR 354
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
42-456 |
9.26e-14 |
|
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: 73.79 E-value: 9.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 42 YGELAERIRRVAGALQASGIHR--EERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLLTADDYAYMLQHSRAQAVLVSG 119
Cdd:cd05927 8 YKEVAERADNIGSALRSLGGKPapASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVFCDA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 120 AL-LPVLRQAMAQGgheaatvivsrpagplpdgmialeawieRNAPLAAPASTgPDDPGFWLYSSGSTGRPKGVLHSQGN 198
Cdd:cd05927 88 GVkVYSLEEFEKLG----------------------------KKNKVPPPPPK-PEDLATICYTSGTTGNPKGVMLTHGN 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 199 pywTAELYAKPVLSLGEADiCFSAAKLYFAYglgnaltFPLSvgatvvLMAERPTPEATF-------------RRWLD-- 263
Cdd:cd05927 139 ---IVSNVAGVFKILEILN-KINPTDVYISY-------LPLA------HIFERVVEALFLyhgakigfysgdiRLLLDdi 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 264 --YQPTVFFGAPTGY--------AGMLAAPGL--------------------PTRE-----------QVSL----RLCSS 298
Cdd:cd05927 202 kaLKPTVFPGVPRVLnriydkifNKVQAKGPLkrklfnfalnyklaelrsgvVRASpfwdklvfnkiKQALggnvRLMLT 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 299 AGEALPADLGERFTAHFGCEIIDGIGSTEMLHIFLSNRPGQVRYGTTGWPVPGYAVELRD--EDG-HAVPDGDVGDLYIQ 375
Cdd:cd05927 282 GSAPLSPEVLEFLRVALGCPVLEGYGQTECTAGATLTLPGDTSVGHVGGPLPCAEVKLVDvpEMNyDAKDPNPRGEVCIR 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 376 GPSAALMYWGNREKSRETFR-GGWTKSGDKYVRNADGSYSYAGRSDDMLKVS-GIYVSPFEVEATLAQHPAI-------- 445
Cdd:cd05927 362 GPNVFSGYYKDPEKTAEALDeDGWLHTGDIGEWLPNGTLKIIDRKKNIFKLSqGEYVAPEKIENIYARSPFVaqifvygd 441
|
490
....*....|....
gi 1920939256 446 -LEAAVIG--VPDQ 456
Cdd:cd05927 442 sLKSFLVAivVPDP 455
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
39-497 |
1.65e-13 |
|
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.
Pssm-ID: 341287 [Multi-domain] Cd Length: 588 Bit Score: 72.87 E-value: 1.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 39 TMRYGELAERIRRVAGALQA-SGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLLTADDYAYMLQHSRAQAVLV 117
Cdd:cd17632 67 TITYAELWERVGAVAAAHDPeQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLAV 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 118 SGALLPVLRQAMAQGG----------------HEAATVIVSRPAGPLPDGMIALE--AWIERNAPLAAPASTGPDD--PG 177
Cdd:cd17632 147 SAEHLDLAVEAVLEGGtpprlvvfdhrpevdaHRAALESARERLAAVGIPVTTLTliAVRGRDLPPAPLFRPEPDDdpLA 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 178 FWLYSSGSTGRPKGVLHSQGN--PYWTaelyakpVLSLGEADICFSAAKLYF-----AYGLgNALTFPLSVGATVVLMAE 250
Cdd:cd17632 227 LLIYTSGSTGTPKGAMYTERLvaTFWL-------KVSSIQDIRPPASITLNFmpmshIAGR-ISLYGTLARGGTAYFAAA 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 251 -------------RPTPEATFRRWLD-----YQPTVFFGAPTGYAGMLAAPGLPT--REQV-----SLRLCSSAgeALPA 305
Cdd:cd17632 299 sdmstlfddlalvRPTELFLVPRVCDmlfqrYQAELDRRSVAGADAETLAERVKAelRERVlggrlLAAVCGSA--PLSA 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 306 DLGERFTAHFGCEIIDGIGSTEMLHIFLSN---RPGQVRYGTTGWPVPGYaveLRDEDGHavPDgdvGDLYIQGPSAALM 382
Cdd:cd17632 377 EMKAFMESLLDLDLHDGYGSTEAGAVILDGvivRPPVLDYKLVDVPELGY---FRTDRPH--PR---GELLVKTDTLFPG 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 383 YWGNREKSRETF-RGGWTKSGDKYVRNADGSYSYAGRSDDMLKVS-GIYVSPFEVEATLAQHPAILEAAVIGVPDQAGLT 460
Cdd:cd17632 449 YYKRPEVTAEVFdEDGFYRTGDVMAELGPDRLVYVDRRNNVLKLSqGEFVTVARLEAVFAASPLVRQIFVYGNSERAYLL 528
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1920939256 461 ktkAFVVLKPGAQVSET--ELKAFVKER---------LAPYKYPR--IIE 497
Cdd:cd17632 529 ---AVVVPTQDALAGEDtaRLRAALAESlqriareagLQSYEIPRdfLIE 575
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
39-516 |
1.75e-13 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 73.19 E-value: 1.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 39 TMRYGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLLTADDYAYMLQHSRAQAV--- 115
Cdd:PLN03052 208 RMTLSELRSQVSRVANALDALGFEKGDAIAIDMPMNVHAVIIYLAIILAGCVVVSIADSFAPSEIATRLKISKAKAIftq 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 116 ---LVSGALLPVLRQAMaqgGHEAATVIVSrPAG------PLPDGMIALEAWIERNAPLAAPASTGP-----DDPGFWLY 181
Cdd:PLN03052 288 dviVRGGKSIPLYSRVV---EAKAPKAIVL-PADgksvrvKLREGDMSWDDFLARANGLRRPDEYKAveqpvEAFTNILF 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 182 SSGSTGRPKGVLHSQGNPYWTA-ELYAKpvLSLGEADICFSAAKLyfAYGLGNALTFP-LSVGATVVLMAERPTpEATFR 259
Cdd:PLN03052 364 SSGTTGEPKAIPWTQLTPLRAAaDAWAH--LDIRKGDIVCWPTNL--GWMMGPWLVYAsLLNGATLALYNGSPL-GRGFA 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 260 RWL-DYQPTVFFGAPTGYAGMLAAPGLPTREQVSLRLCSSAGEALPAD----LGERftAHFGcEIIDGIGSTEMLHIFLS 334
Cdd:PLN03052 439 KFVqDAKVTMLGTVPSIVKTWKNTNCMAGLDWSSIRCFGSTGEASSVDdylwLMSR--AGYK-PIIEYCGGTELGGGFVT 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 335 NRPGQVR-YGTTGWPVPGYAVELRDEDGHAVPD-----GDVG-DLYIQGPSAALMywgNREKSRETFRG-----GWT--K 400
Cdd:PLN03052 516 GSLLQPQaFAAFSTPAMGCKLFILDDSGNPYPDdapctGELAlFPLMFGASSTLL---NADHYKVYFKGmpvfnGKIlrR 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 401 SGDKYVRNADGSYSYAGRSDDMLKVSGIYVSPFEVEATL-AQHPAILEAAVIGV-PDQAGLTKTKAFVVLK--PGAQVSE 476
Cdd:PLN03052 593 HGDIFERTSGGYYRAHGRADDTMNLGGIKVSSVEIERVCnAADESVLETAAIGVpPPGGGPEQLVIAAVLKdpPGSNPDL 672
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1920939256 477 TELKAF----VKERLAPYKYPRIIEFMDALPKTATGKIQRFRLR 516
Cdd:PLN03052 673 NELKKIfnsaIQKKLNPLFKVSAVVIVPSFPRTASNKVMRRVLR 716
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
34-490 |
4.02e-12 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 68.59 E-value: 4.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 34 IDDHGT------MRYGELAERIRRVAGALQASGIHREERVLLLMHDGNDWpVCFLGAMYA-GIVPVAVNTLLTADDYAYM 106
Cdd:PLN02736 67 IRVDGTvgeykwMTYGEAGTARTAIGSGLVQHGIPKGACVGLYFINRPEW-LIVDHACSAySYVSVPLYDTLGPDAVKFI 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 107 LQHSRAQAVLVSGALLPVLRQAMAQGGHEAATVIVSRPAGPLPD----------GMIALEAwiERNAPLAAPASTGPDDP 176
Cdd:PLN02736 146 VNHAEVAAIFCVPQTLNTLLSCLSEIPSVRLIVVVGGADEPLPSlpsgtgveivTYSKLLA--QGRSSPQPFRPPKPEDV 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 177 GFWLYSSGSTGRPKGVLHSQGNPYWTAELYAKpVLSLGEADICFSAAKLYFAYGLGNALTFpLSVGATV--------VLM 248
Cdd:PLN02736 224 ATICYTSGTTGTPKGVVLTHGNLIANVAGSSL-STKFYPSDVHISYLPLAHIYERVNQIVM-LHYGVAVgfyqgdnlKLM 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 249 AERptpeATFRrwldyqPTVFFGAPTG----YAGMLAA--PGLPTREQV------------------------------- 291
Cdd:PLN02736 302 DDL----AALR------PTIFCSVPRLynriYDGITNAvkESGGLKERLfnaaynakkqalengknpspmwdrlvfnkik 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 292 -----SLRLCSSAGEALPADLGERFTAHFGCEIIDGIGSTEMLHIFLSNRPGQVRYGTTGWPVPGYAVELRDedghaVPD 366
Cdd:PLN02736 372 aklggRVRFMSSGASPLSPDVMEFLRICFGGRVLEGYGMTETSCVISGMDEGDNLSGHVGSPNPACEVKLVD-----VPE 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 367 GDV---------GDLYIQGPSAALMYWGNREKSRETFRG-GWTKSGDKYVRNADGSYSYAGRSDDMLKVS-GIYVSPFEV 435
Cdd:PLN02736 447 MNYtsedqpyprGEICVRGPIIFKGYYKDEVQTREVIDEdGWLHTGDIGLWLPGGRLKIIDRKKNIFKLAqGEYIAPEKI 526
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1920939256 436 EATLAQHPAILEAAVIGVPDQAGLTktkAFVVLKPgaqvsETeLKAFVKERLAPY 490
Cdd:PLN02736 527 ENVYAKCKFVAQCFVYGDSLNSSLV---AVVVVDP-----EV-LKAWAASEGIKY 572
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
27-497 |
1.24e-10 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 63.84 E-value: 1.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 27 RPGKTAYIDDHGTMRYGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLLTADDYAYM 106
Cdd:PTZ00216 109 RTMEVTHFNETRYITYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYA 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 107 LQHSRAQAVLVSGALLPVLRQAMAQGGHEAATVIVsrpAGPLPDGMIA----LEAWIE---------RNAPLAAPasTGP 173
Cdd:PTZ00216 189 LRETECKAIVCNGKNVPNLLRLMKSGGMPNTTIIY---LDSLPASVDTegcrLVAWTDvvakghsagSHHPLNIP--ENN 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 174 DDPGFWLYSSGSTGRPKGVLHSQGNPY--------WTAELYAKPvlSLGEAdicfsaaklYFAYgLGNALTFPLSVgaTV 245
Cdd:PTZ00216 264 DDLALIMYTSGTTGDPKGVMHTHGSLTagilaledRLNDLIGPP--EEDET---------YCSY-LPLAHIMEFGV--TN 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 246 VLMAERP-----TPEA---TFRR----WLDYQPTVFFGAP--------------------------TGYAGMLAA--PGL 285
Cdd:PTZ00216 330 IFLARGAligfgSPRTltdTFARphgdLTEFRPVFLIGVPrifdtikkaveaklppvgslkrrvfdHAYQSRLRAlkEGK 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 286 PT---REQV----------SLRLCSSAGEALPADLGERFTAHFGCeIIDGIGSTEMLHIFLSNRPGQVRYGTTGWPVPGY 352
Cdd:PTZ00216 410 DTpywNEKVfsapravlggRVRAMLSGGGPLSAATQEFVNVVFGM-VIQGWGLTETVCCGGIQRTGDLEPNAVGQLLKGV 488
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 353 AVELRDEDGHAVPDGDV--GDLYIQGPSAALMYWGNREKSRETF-RGGWTKSGDKYVRNADGSYSYAGRSDDMLK-VSGI 428
Cdd:PTZ00216 489 EMKLLDTEEYKHTDTPEprGEILLRGPFLFKGYYKQEELTREVLdEDGWFHTGDVGSIAANGTLRIIGRVKALAKnCLGE 568
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1920939256 429 YVSPFEVEATLAQHPAILEAAVIGV--PDQAGLTktkAFVVlkpgaqVSETELKAFVKERLAPYKYPRIIE 497
Cdd:PTZ00216 569 YIALEALEALYGQNELVVPNGVCVLvhPARSYIC---ALVL------TDEAKAMAFAKEHGIEGEYPAILK 630
|
|
| PaaK |
cd05913 |
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic ... |
182-444 |
1.88e-10 |
|
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: 63.03 E-value: 1.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 182 SSGSTGRPKGVLHSQGNPYWTAELYAkpvlslgeadICFSAAKLY--------FAYGLGNA-LTFPLS---VGATVVLMA 249
Cdd:cd05913 86 SSGTTGKPTVVGYTKNDLDVWAELVA----------RCLDAAGVTpgdrvqnaYGYGLFTGgLGFHYGaerLGALVIPAG 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 250 erptPEATFRRW---LDYQPTVFFGAPTgYAGMLAAP----GLPTREqVSLRLCSSAGEALPADLGERFTAHFGCEIIDG 322
Cdd:cd05913 156 ----GGNTERQLqliKDFGPTVLCCTPS-YALYLAEEaeeeGIDPRE-LSLKVGIFGAEPWTEEMRKRIERRLGIKAYDI 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 323 IGSTEMLHiflsnrPG-----QVRYGTTGWPvPGYAVE-LRDEDGHAVPDGDVGDLYIQ--GPSAALM--YWGnREKSRE 392
Cdd:cd05913 230 YGLTEIIG------PGvafecEEKDGLHIWE-DHFIPEiIDPETGEPVPPGEVGELVFTtlTKEAMPLirYRT-RDITRL 301
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1920939256 393 TFRggwTKSGDKYVRNADGsysYAGRSDDMLKVSGIYVSPFEVEATLAQHPA 444
Cdd:cd05913 302 LPG---PCPCGRTHRRIDR---ITGRSDDMLIIRGVNVFPSQIEDVLLKIPG 347
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
180-510 |
1.67e-09 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341309 [Multi-domain] Cd Length: 449 Bit Score: 59.79 E-value: 1.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 180 LYSSGSTGRPKGVL--HSQGNPYWTaelYAKPVLSLGEADICFSAAKLYFAYGLGNaLTFPLSVGATVVL----MAERPT 253
Cdd:cd17654 124 IHTSGTTGTPKIVAvpHKCILPNIQ---HFRSLFNITSEDILFLTSPLTFDPSVVE-IFLSLSSGATLLIvptsVKVLPS 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 254 --PEATFRRwldYQPTVFFGAPTGYAGMLAAPGLPT--REQVSLRLCSSAGEALPADLGERFTAHFG--CEIIDGIGSTE 327
Cdd:cd17654 200 klADILFKR---HRITVLQATPTLFRRFGSQSIKSTvlSATSSLRVLALGGEPFPSLVILSSWRGKGnrTRIFNIYGITE 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 328 M------LHIFLSNRPGQVrygttGWPVPGYAVELRDEDGHAVPdgdvGDLYIQGpsaalmywgnreKSRETFR------ 395
Cdd:cd17654 277 VscwalaYKVPEEDSPVQL-----GSPLLGTVIEVRDQNGSEGT----GQVFLGG------------LNRVCILddevtv 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 396 --GGWTKSGDkYVRNADGSYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQagltKTKAFVVLKPgaq 473
Cdd:cd17654 336 pkGTMRATGD-FVTVKDGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGVESCAVTLSDQQ----RLIAFIVGES--- 407
|
330 340 350
....*....|....*....|....*....|....*..
gi 1920939256 474 VSETELKAFVKERLAPYKYPRIIEFMDALPKTATGKI 510
Cdd:cd17654 408 SSSRIHKELQLTLLSSHAIPDTFVQIDKLPLTSHGKV 444
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
44-441 |
3.64e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 59.36 E-value: 3.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 44 ELAERIRRVAGALQASGiHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAvntLLTADDYAYMlqhSRAQAVLVSGALLP 123
Cdd:PRK07769 60 QFGARNRAVGARLQQVT-KPGDRVAILAPQNLDYLIAFFGALYAGRIAVP---LFDPAEPGHV---GRLHAVLDDCTPSA 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 124 VLRQAMAQGGheAATVIVSRPAGPLPDgMIALEAWIERNAPLAAPASTGPDDPGFWLYSSGSTGRPKGVLHSQGNpYWTA 203
Cdd:PRK07769 133 ILTTTDSAEG--VRKFFRARPAKERPR-VIAVDAVPDEVGATWVPPEANEDTIAYLQYTSGSTRIPAGVQITHLN-LPTN 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 204 ELYAKPVLSLGEADICFSAAKLYFAYGLGNALtFPLSVGATVVLMaerpTPEATFRR---WL-------DYQPTVFFGAP 273
Cdd:PRK07769 209 VLQVIDALEGQEGDRGVSWLPFFHDMGLITVL-LPALLGHYITFM----SPAAFVRRpgrWIrelarkpGGTGGTFSAAP 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 274 TGYAGMLAAPGLPTREQVSLRLCSSAG-----EALPADLGERFTAHFG------CEIIDGIGSTEMLhIFLSNRP----- 337
Cdd:PRK07769 284 NFAFEHAAARGLPKDGEPPLDLSNVKGllngsEPVSPASMRKFNEAFApyglppTAIKPSYGMAEAT-LFVSTTPmdeep 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 338 --------------------------GQVRYGTTGwpVPGYAVELRDEDGHAVPDGDVGDLYIQGPSAALMYWGNREKSR 391
Cdd:PRK07769 363 tviyvdrdelnagrfvevpadapnavAQVSAGKVG--VSEWAVIVDPETASELPDGQIGEIWLHGNNIGTGYWGKPEETA 440
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1920939256 392 ETFR------------------GGWTKSGDkYVRNADGSYSYAGRSDDMLKVSGIYVSPFEVEATlAQ 441
Cdd:PRK07769 441 ATFQnilksrlseshaegapddALWVRTGD-YGVYFDGELYITGRVKDLVIIDGRNHYPQDLEYT-AQ 506
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
42-443 |
6.01e-09 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 58.59 E-value: 6.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 42 YGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLLTADDYAYMLQHSRAQAVLVSGAL 121
Cdd:PLN02387 109 YGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVICDSKQ 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 122 LPVLrQAMAQGGHEAATVIVSRPAGP-LPDGMIALEAW-------IE---RNAPlAAPASTGPDDPGFWLYSSGSTGRPK 190
Cdd:PLN02387 189 LKKL-IDISSQLETVKRVIYMDDEGVdSDSSLSGSSNWtvssfseVEklgKENP-VDPDLPSPNDIAVIMYTSGSTGLPK 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 191 GVLHSQGNPYWTAELYAKPVLSLGEADIcfsaaklYFAY----------------------GLGNALTF-----PLSVGA 243
Cdd:PLN02387 267 GVMMTHGNIVATVAGVMTVVPKLGKNDV-------YLAYlplahilelaaesvmaavgaaiGYGSPLTLtdtsnKIKKGT 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 244 TVVLMAERPTPEATFRRWLD---------------YQPTVFfgaPTGYAGMLAAP--------GLptrEQV--------- 291
Cdd:PLN02387 340 KGDASALKPTLMTAVPAILDrvrdgvrkkvdakggLAKKLF---DIAYKRRLAAIegswfgawGL---EKLlwdalvfkk 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 292 -------SLRLCSSAGEALPADlGERFT-AHFGCEIIDGIGSTEMLHIFLSNRPGQVRYGTTGWPVPGYAVELRD--EDG 361
Cdd:PLN02387 414 iravlggRIRFMLSGGAPLSGD-TQRFInICLGAPIGQGYGLTETCAGATFSEWDDTSVGRVGPPLPCCYVKLVSweEGG 492
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 362 HAVPDGDV--GDLYIQGPSAALMYWGNREKSRETF----RG-GWTKSGDKYVRNADGSYSYAGRSDDMLKVS-GIYVSPF 433
Cdd:PLN02387 493 YLISDKPMprGEIVIGGPSVTLGYFKNQEKTDEVYkvdeRGmRWFYTGDIGQFHPDGCLEIIDRKKDIVKLQhGEYVSLG 572
|
490
....*....|
gi 1920939256 434 EVEATLAQHP 443
Cdd:PLN02387 573 KVEAALSVSP 582
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
26-517 |
7.16e-09 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 57.96 E-value: 7.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 26 QRPGKTAYIDDHGTMRYGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLLTAddyay 105
Cdd:PRK09029 15 VRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQ----- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 106 MLQHsraqavlvsgALLPVL--RQAMAQGGHEAATVIVSRPAgPLPDGMIALEAWIERNAPLAapastgpddpgfwlYSS 183
Cdd:PRK09029 90 PLLE----------ELLPSLtlDFALVLEGENTFSALTSLHL-QLVEGAHAVAWQPQRLATMT--------------LTS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 184 GSTGRPKGVLHSQGnpywtAELY-AKPVLSLgeadICFSAAK-------LYFAYGLGnALTFPLSVGATVVLMAERPTPE 255
Cdd:PRK09029 145 GSTGLPKAAVHTAQ-----AHLAsAEGVLSL----MPFTAQDswllslpLFHVSGQG-IVWRWLYAGATLVVRDKQPLEQ 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 256 ATF------------RRWLDYQptvffgaptgyagmlaapglptREQVSLRLCSSAGEALPADLGERFTAHfGCEIIDGI 323
Cdd:PRK09029 215 ALAgcthaslvptqlWRLLDNR----------------------SEPLSLKAVLLGGAAIPVELTEQAEQQ-GIRCWCGY 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 324 GSTEMlhiflsnrpgqvryGTT------------GWPVPGYAVELRDedghavpdgdvGDLYIQGPSAALMYWGNREKSR 391
Cdd:PRK09029 272 GLTEM--------------ASTvcakradglagvGSPLPGREVKLVD-----------GEIWLRGASLALGYWRQGQLVP 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 392 ETFRGGWTKSGDKYVRNaDGSYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDqagltktKAF-----V 466
Cdd:PRK09029 327 LVNDEGWFATRDRGEWQ-NGELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVPVAD-------AEFgqrpvA 398
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1920939256 467 VLKPGAQVSETELKAFVKERLAPYKYPriIEFMdALPKT-ATG--KIQRFRLRE 517
Cdd:PRK09029 399 VVESDSEAAVVNLAEWLQDKLARFQQP--VAYY-LLPPElKNGgiKISRQALKE 449
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
9-440 |
3.06e-08 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 56.29 E-value: 3.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 9 PPGTPFNfaqHLIACNAQRPGKTA---YIDDHGT-------MRYGELAERIRRVAGALQASgIHREERVLLLMHDGNDWP 78
Cdd:PRK12476 31 PPGTTLI---SLIERNIANVGDTVayrYLDHSHSaagcaveLTWTQLGVRLRAVGARLQQV-AGPGDRVAILAPQGIDYV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 79 VCFLGAMYAGIVPV---AVNTLLTADDYAYMLQHSRAQAVLVSGALLPVLRQAMAQGGHeaatviVSRPAgplpdgMIAL 155
Cdd:PRK12476 107 AGFFAAIKAGTIAVplfAPELPGHAERLDTALRDAEPTVVLTTTAAAEAVEGFLRNLPR------LRRPR------VIAI 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 156 EAWIERNAPLAAPASTGPDDPGFWLYSSGSTGRPKGVlhsqgnpywtaELYAKPV--------LSLGEADI---CFSAAK 224
Cdd:PRK12476 175 DAIPDSAGESFVPVELDTDDVSHLQYTSGSTRPPVGV-----------EITHRAVgtnlvqmiLSIDLLDRnthGVSWLP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 225 LYFAYGLgNALTFPLSVGATVVLMaerpTPEATFR---RWL-------DYQPTvfFGAPTGYAGMLAAP-GLPTR-EQVS 292
Cdd:PRK12476 244 LYHDMGL-SMIGFPAVYGGHSTLM----SPTAFVRrpqRWIkalsegsRTGRV--VTAAPNFAYEWAAQrGLPAEgDDID 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 293 LR--LCSSAGEALPADLGERFTAHFG------CEIIDGIGSTEMLhIFLSN-----RPGQVRYGTTGWPVpGYAVELRDE 359
Cdd:PRK12476 317 LSnvVLIIGSEPVSIDAVTTFNKAFApyglprTAFKPSYGIAEAT-LFVATiapdaEPSVVYLDREQLGA-GRAVRVAAD 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 360 DGHAV-------------------------PDGDVGDLYIQGPSAALMYWGNREKSRETFR------------------- 395
Cdd:PRK12476 395 APNAVahvscgqvarsqwavivdpdtgaelPDGEVGEIWLHGDNIGRGYWGRPEETERTFGaklqsrlaegshadgaadd 474
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1920939256 396 GGWTKSGDKYVRnADGSYSYAGRSDDMLKVSGIYVSPFEVEATLA 440
Cdd:PRK12476 475 GTWLRTGDLGVY-LDGELYITGRIADLIVIDGRNHYPQDIEATVA 518
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
126-518 |
1.08e-07 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 54.39 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 126 RQAMAQGGHEAATvivsRPAGP-LPDGMIALEAWIERNAPLAAPASTGPddpGFWLYSSGSTGRPKGVLHSQGNPYWTAE 204
Cdd:PRK05851 110 RTVLSHGSHLERL----RAVDSsVTVHDLATAAHTNRSASLTPPDSGGP---AVLQGTAGSTGTPRTAILSPGAVLSNLR 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 205 LYAKPVLSLGEADICFSAAKLYFAYGLGNALTFPLSvGATVVLmaerpTPEATFR----RWLDY----------QPTVFF 270
Cdd:PRK05851 183 GLNARVGLDAATDVGCSWLPLYHDMGLAFLLTAALA-GAPLWL-----APTTAFSaspfRWLSWlsdsratltaAPNFAY 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 271 GAPTGYAGMLAAPGLPTreqvsLRLCSSAGEALPADLGERF---TAHFG----------------CEIIDGIGSTEMLHI 331
Cdd:PRK05851 257 NLIGKYARRVSDVDLGA-----LRVALNGGEPVDCDGFERFataMAPFGfdagaaapsyglaestCAVTVPVPGIGLRVD 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 332 FLSNRPGQV--RYGTTGWPVPGYAVELRDEDGHA-VPDGDVGDLYIQGPSAALMYWGnrEKSREtfRGGWTKSGD-KYVr 407
Cdd:PRK05851 332 EVTTDDGSGarRHAVLGNPIPGMEVRISPGDGAAgVAGREIGEIEIRGASMMSGYLG--QAPID--PDDWFPTGDlGYL- 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 408 nADGSYSYAGRSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQAGLTKtKAFVVLKPGAQVSETELKAFVKERL 487
Cdd:PRK05851 407 -VDGGLVVCGRAKELITVAGRNIFPTEIERVAAQVRGVREGAVVAVGTGEGSAR-PGLVIAAEFRGPDEAGARSEVVQRV 484
|
410 420 430
....*....|....*....|....*....|....*
gi 1920939256 488 APY--KYPRIIEFMD--ALPKTATGKIQRFRLREM 518
Cdd:PRK05851 485 ASEcgVVPSDVVFVApgSLPRTSSGKLRRLAVKRS 519
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
367-515 |
2.18e-07 |
|
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Pssm-ID: 341302 [Multi-domain] Cd Length: 520 Bit Score: 53.29 E-value: 2.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 367 GDVGDLYIQGPSAALMYWGNREKSRETF----------------------RGGWTKSGDKYVRNAD-------GSYSYAG 417
Cdd:cd17647 313 GEVGEIYVRAGGLAEGYRGLPELNKEKFvnnwfvepdhwnyldkdnnepwRQFWLGPRDRLYRTGDlgrylpnGDCECCG 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 418 RSDDMLKVSGIYVSPFEVEATLAQHPAILEAAVIGVPDQAGLTKTKAFVVLKPGAQVSETE------------------- 478
Cdd:cd17647 393 RADDQVKIRGFRIELGEIDTHISQHPLVRENITLVRRDKDEEPTLVSYIVPRFDKPDDESFaqedvpkevstdpivkgli 472
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1920939256 479 --------LKAFVKERLAPYKYPRIIEFMDALPKTATGKIQRFRL 515
Cdd:cd17647 473 gyrklikdIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKL 517
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
27-452 |
3.21e-07 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 53.10 E-value: 3.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 27 RPGKTAYiddhgtMRYGELAERIRRVAGALQASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLLTADDYAYM 106
Cdd:PLN02614 73 KPGKYVW------QTYQEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFI 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 107 LQHSRAQAVLVSGALLPVLRQAMAQGGHEAATVI----VSRPAGPLPDGM-IALEAWIE---------RNAPLAAPAstg 172
Cdd:PLN02614 147 ISHSEVSIVFVEEKKISELFKTCPNSTEYMKTVVsfggVSREQKEEAETFgLVIYAWDEflklgegkqYDLPIKKKS--- 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 173 pdDPGFWLYSSGSTGRPKGVLHSQGNpywTAELYAKPVLSLGEADICFSAAKLYFAYgLGNALTFP-------LSVGAT- 244
Cdd:PLN02614 224 --DICTIMYTSGTTGDPKGVMISNES---IVTLIAGVIRLLKSANAALTVKDVYLSY-LPLAHIFDrvieecfIQHGAAi 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 245 ------VVLMAE-----RPTPEATFRRWLD---------------YQPTVF---FGAPTGY--AGMLAAPGLPTREQV-- 291
Cdd:PLN02614 298 gfwrgdVKLLIEdlgelKPTIFCAVPRVLDrvysglqkklsdggfLKKFVFdsaFSYKFGNmkKGQSHVEASPLCDKLvf 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 292 ---------SLRLCSSAGEALPADLGERFTAHFGCEIIDGIGSTEMLHIFLSNRPGQV-RYGTTGWPVPGyaVELRDEdg 361
Cdd:PLN02614 378 nkvkqglggNVRIILSGAAPLASHVESFLRVVACCHVLQGYGLTESCAGTFVSLPDELdMLGTVGPPVPN--VDIRLE-- 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 362 hAVPDGDV--------GDLYIQGPSAALMYWGNREKSRETFRGGWTKSGDKYVRNADGSYSYAGRSDDMLKVS-GIYVSP 432
Cdd:PLN02614 454 -SVPEMEYdalastprGEICIRGKTLFSGYYKREDLTKEVLIDGWLHTGDVGEWQPNGSMKIIDRKKNIFKLSqGEYVAV 532
|
490 500
....*....|....*....|
gi 1920939256 433 FEVEATLAQHPAILEAAVIG 452
Cdd:PLN02614 533 ENIENIYGEVQAVDSVWVYG 552
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
81-518 |
4.41e-07 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 52.51 E-value: 4.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 81 FLGAMYAGIVPVAVNTLLTADDYAYMLQHSRAQAV------LVSGALLPVLRQAMAQGGHEAATVIVS-RPAG-PLPDGM 152
Cdd:PLN03051 11 YLAIVLAGCVVVSVADSFSAKEIATRLDISGAKGVftqdvvLRGGRALPLYSKVVEAAPAKAIVLPAAgEPVAvPLREQD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 153 IAleaWIERNAPLAAPASTGP----------DDPGFWLYSSGSTGRPKGVLHSQGNPYWTA-ELYAKPVLSLGEAdICFS 221
Cdd:PLN03051 91 LS---WCDFLGVAAAQGSVGGneyspvyapvESVTNILFSSGTTGEPKAIPWTHLSPLRCAsDGWAHMDIQPGDV-VCWP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 222 AAklyFAYGLGNALTF-PLSVGATVVLMAERPTPEATFRRWLDYQPTVFFGAPT-----GYAGMLAAPGLptrEQVSLRL 295
Cdd:PLN03051 167 TN---LGWMMGPWLLYsAFLNGATLALYGGAPLGRGFGKFVQDAGVTVLGLVPSivkawRHTGAFAMEGL---DWSKLRV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 296 CSSAGEALPAD--LGERFTAHFGCEIIDGIGSTEMLHIFLSNRPGQVR-YGTTGWPVPGYAVELRDEDGHAVPD-----G 367
Cdd:PLN03051 241 FASTGEASAVDdvLWLSSVRGYYKPVIEYCGGTELASGYISSTLLQPQaPGAFSTASLGTRFVLLNDNGVPYPDdqpcvG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 368 DVG-DLYIQGPSAALMywgNREKSRETFRG----GWT-----KSGDKYVRNADGSYSYAGRSDDMLKVSGIYVSPFEVE- 436
Cdd:PLN03051 321 EVAlAPPMLGASDRLL---NADHDKVYYKGmpmyGSKgmplrRHGDIMKRTPGGYFCVQGRADDTMNLGGIKTSSVEIEr 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 437 ATLAQHPAILEAAVIGVPDQAG----LTKTKAFVVLKPGAQVSETE--LKAF---VKERLAP-YKYPRIIeFMDALPKTA 506
Cdd:PLN03051 398 ACDRAVAGIAETAAVGVAPPDGgpelLVIFLVLGEEKKGFDQARPEalQKKFqeaIQTNLNPlFKVSRVK-IVPELPRNA 476
|
490
....*....|..
gi 1920939256 507 TGKIQRFRLREM 518
Cdd:PLN03051 477 SNKLLRRVLRDQ 488
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
20-442 |
6.21e-07 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 52.13 E-value: 6.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 20 LIACnAQRPGKTAYIDDH-GTMRYGELAERIrrVAGALQASGiHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLL 98
Cdd:PRK06334 26 LKLC-SEMTTATVCWDEQlGKLSYNQVRKAV--IALATKVSK-YPDQHIGIMMPASAGAYIAYFATLLSGKIPVMINWSQ 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 99 TADDYAYMLQHSRAQAVLVSGALLPVLRQAMAQGGHEAATVIVS---RPAGPLPDGM-IAL-----EAWIERnapLAAPA 169
Cdd:PRK06334 102 GLREVTACANLVGVTHVLTSKQLMQHLAQTHGEDAEYPFSLIYMeevRKELSFWEKCrIGIymsipFEWLMR---WFGVS 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 170 STGPDDPGFWLYSSGSTGRPKGVlhsqgnPYWTAELYAKPVLSLG-----EADICFSAAKLYFAYGLGNALTFPLSVGAT 244
Cdd:PRK06334 179 DKDPEDVAVILFTSGTEKLPKGV------PLTHANLLANQRACLKffspkEDDVMMSFLPPFHAYGFNSCTLFPLLSGVP 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 245 VVLmAERPTPEATFRRWLDYQPTVFFGA-PTGYAGMLAAPGLPTREQVSLRLCSSAGEALPADLGERFTAHF-GCEIIDG 322
Cdd:PRK06334 253 VVF-AYNPLYPKKIVEMIDEAKVTFLGStPVFFDYILKTAKKQESCLPSLRFVVIGGDAFKDSLYQEALKTFpHIQLRQG 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 323 IGSTE---MLHIFLSNRPGQVRygTTGWPVPGYAVELRDEDGHA-VPDGDVGDLYIQGPSAALMYWGNREKSRETFRGG- 397
Cdd:PRK06334 332 YGTTEcspVITINTVNSPKHES--CVGMPIRGMDVLIVSEETKVpVSSGETGLVLTRGTSLFSGYLGEDFGQGFVELGGe 409
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1920939256 398 -WTKSGDKYVRNADGSYSYAGRSDDMLKVSGIYVSPFEVEATLAQH 442
Cdd:PRK06334 410 tWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEG 455
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
20-455 |
5.56e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 49.17 E-value: 5.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 20 LIACNAQRPGKTAY--ID-DHG------TMRYGELAERIRRVAGALQASGIHREeRVLLLMHDGNDWPVCFLGAMYAGIV 90
Cdd:PRK05850 7 LRERASLQPDDAAFtfIDyEQDpagvaeTLTWSQLYRRTLNVAEELRRHGSTGD-RAVILAPQGLEYIVAFLGALQAGLI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 91 PVAVNTLLTAddyaymLQHSRAQAVLVSGALLPVLRQAMAQGghEAATVIVSRPAGPLPdGMIALEAWIERNAPLAAPAS 170
Cdd:PRK05850 86 AVPLSVPQGG------AHDERVSAVLRDTSPSVVLTTSAVVD--DVTEYVAPQPGQSAP-PVIEVDLLDLDSPRGSDARP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 171 TGPDDPGFWLYSSGSTGRPKGVLHSQGN----------PYWTAELYAKPVLSlgeadICFSAAKLYFAYGLGNALTFPLS 240
Cdd:PRK05850 157 RDLPSTAYLQYTSGSTRTPAGVMVSHRNvianfeqlmsDYFGDTGGVPPPDT-----TVVSWLPFYHDMGLVLGVCAPIL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 241 VGATVVLMA-----ERPTpeatfrRW---LDYQPTVFFGAPTgYAGMLAA--------PGLPTREQVSlrLCSSAGEALP 304
Cdd:PRK05850 232 GGCPAVLTSpvaflQRPA------RWmqlLASNPHAFSAAPN-FAFELAVrktsdddmAGLDLGGVLG--IISGSERVHP 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 305 ADLgERFT---AHFGCeiidgigstemlhiflsnRPGQVR--YG---------TTGWPVPGYAVELRDE---DGHAV--- 364
Cdd:PRK05850 303 ATL-KRFAdrfAPFNL------------------RETAIRpsYGlaeatvyvaTREPGQPPESVRFDYEklsAGHAKrce 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 365 -----------------------------PDGDVGDLYIQGPSAALMYWGNREKSRETF------------RGGWTKSGD 403
Cdd:PRK05850 364 tgggtplvsygsprsptvrivdpdtciecPAGTVGEIWVHGDNVAAGYWQKPEETERTFgatlvdpspgtpEGPWLRTGD 443
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1920939256 404 KYVRnADGSYSYAGRSDDMLKVSGIYVSPFEVEATlaqhpaILE-----AAVIGVPD 455
Cdd:PRK05850 444 LGFI-SEGELFIVGRIKDLLIVDGRNHYPDDIEAT------IQEitggrVAAISVPD 493
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
29-125 |
2.40e-03 |
|
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.
Pssm-ID: 341231 [Multi-domain] Cd Length: 571 Bit Score: 40.41 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 29 GKTAYiddhgTMRYGELAERIRRVAGALQ-ASGIHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLLTADDYAYML 107
Cdd:cd05905 9 GKEAT-----TLTWGKLLSRAEKIAAVLQkKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLGFLL 83
|
90
....*....|....*...
gi 1920939256 108 QHSRAQAVLVSGALLPVL 125
Cdd:cd05905 84 GTCKVRVALTVEACLKGL 101
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
293-452 |
4.00e-03 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 39.80 E-value: 4.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 293 LRLCSSAGEALPADLGERFTAHFGCEIIDGIGSTEMLHIFLSNRPGQV-RYGTTGwpVPGYAVELRDEDghaVPD----- 366
Cdd:PLN02430 385 LRLLISGGAPLSTEIEEFLRVTSCAFVVQGYGLTETLGPTTLGFPDEMcMLGTVG--APAVYNELRLEE---VPEmgydp 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920939256 367 -GD--VGDLYIQGPSAALMYWGNREKSRETFRGGWTKSGDKYVRNADGSYSYAGRSDDMLKVS-GIYVSPFEVEATLAQH 442
Cdd:PLN02430 460 lGEppRGEICVRGKCLFSGYYKNPELTEEVMKDGWFHTGDIGEILPNGVLKIIDRKKNLIKLSqGEYVALEYLENVYGQN 539
|
170
....*....|
gi 1920939256 443 PAILEAAVIG 452
Cdd:PLN02430 540 PIVEDIWVYG 549
|
|
| PRK09188 |
PRK09188 |
serine/threonine protein kinase; Provisional |
437-511 |
6.77e-03 |
|
serine/threonine protein kinase; Provisional
Pssm-ID: 236400 [Multi-domain] Cd Length: 365 Bit Score: 38.98 E-value: 6.77e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1920939256 437 ATLAQHPAILEAAVIGVPDQAGLTKTKAFVvlKPGAQVSETELKAFVKERLAPyKYPRIIEFMDALPKTATGKIQ 511
Cdd:PRK09188 247 AALKSDPAVSDVAIALFSLPAKGVGLYAFV--EAELPADEKSLRARLAGAKPP-KPPEHIQPVAALPRDADGTVR 318
|
|
| |
