|
Name |
Accession |
Description |
Interval |
E-value |
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
59-540 |
0e+00 |
|
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: 584.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 59 RPLLRGPHRTYTYRDARTEAARIAEVLTQDHGLVPGNRVLLRGGNTVEMALAWLGTVYAGLIAVATMPLLRAGELANIIE 138
Cdd:cd05958 1 RTCLRSPEREWTYRDLLALANRIANVLVGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 139 RAQPTLALCDGRLlaelaaaqdqhpvlttivpfhtatdpadllqraqgkpgsmqpcpTSADDIALMAFTSGTTGAPKAAV 218
Cdd:cd05958 81 KARITVALCAHAL--------------------------------------------TASDDICILAFTSGTTGAPKATM 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 219 HTHRDVLAGCEAWPRHVLKATPDDIVAGSPPLAFTFGLGGLLVFPMWAGAS-VYFPDQpyTPETMVTLMRDAGVTISYTA 297
Cdd:cd05958 117 HFHRDPLASADRYAVNVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASgVLLEEA--TPDLLLSAIARYKPTVLFTA 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 298 PTFYRQMAPFAKKIG--LPQLRICVSAGEGLPDATRQLWKDATGIDMTDGIGATEMFHIFISSAGGEARTGAIGKVVPGY 375
Cdd:cd05958 195 PTAYRAMLAHPDAAGpdLSSLRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEMFHIFISARPGDARPGATGKPVPGY 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 376 TAKVVDDDGNEVPRGTVGKLAVIGPTGCKYLDDPRQAKYVKDGWNYPGDAFTQDADGYFFYQARDDDMIITAGYNVGGPE 455
Cdd:cd05958 275 EAKVVDDEGNPVPDGTIGRLAVRGPTGCRYLADKRQRTYVQGGWNITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPE 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 456 VEDALLRHPAVAECGVIGVPDEERGMVVKAVCVLKPGHTGDAAMVKTLQDHVKATIAPFKYPRVVEFVTALPRTETGKLQ 535
Cdd:cd05958 355 VEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIPGPVLARELQDHAKAHIAPYKYPRAIEFVTELPRTATGKLQ 434
|
....*
gi 496182614 536 RFKLR 540
Cdd:cd05958 435 RFALR 439
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
31-544 |
2.46e-169 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 491.55 E-value: 2.46e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 31 ELQIPDQANLVHALFDqaERAERAGniDRPLLR-----GPHRTYTYRDARTEAARIAEVLtQDHGLVPGNRVLLRGGNTV 105
Cdd:COG0365 1 RWFVGGRLNIAYNCLD--RHAEGRG--DKVALIwegedGEERTLTYAELRREVNRFANAL-RALGVKKGDRVAIYLPNIP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 106 EMALAWLGTVYAGLIAVATMPLLRAGELANIIERAQPTLALCDGR---------LLAELAAAQDQHPVLTTIV------- 169
Cdd:COG0365 76 EAVIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADGglrggkvidLKEKVDEALEELPSLEHVIvvgrtga 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 170 --PFHTATDPADLLQRAqgkPGSMQPCPTSADDIALMAFTSGTTGAPKAAVHTHRDVLAGCEAWPRHVLKATPDDIVAGS 247
Cdd:COG0365 156 dvPMEGDLDWDELLAAA---SAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYVLDLKPGDVFWCT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 248 PPLAFTFGLGGLLVFPMWAGASV-------YFPDqpytPETMVTLMRDAGVTISYTAPTFYRQMA----PFAKKIGLPQL 316
Cdd:COG0365 233 ADIGWATGHSYIVYGPLLNGATVvlyegrpDFPD----PGRLWELIEKYGVTVFFTAPTAIRALMkagdEPLKKYDLSSL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 317 RICVSAGEGLPDATRQLWKDATGIDMTDGIGATEMFHIFISSAGG-EARTGAIGKVVPGYTAKVVDDDGNEVPRGTVGKL 395
Cdd:COG0365 309 RLLGSAGEPLNPEVWEWWYEAVGVPIVDGWGQTETGGIFISNLPGlPVKPGSMGKPVPGYDVAVVDEDGNPVPPGEEGEL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 396 AVIGP-TGC--KYLDDP-RQAKYVKD---GWNYPGDAFTQDADGYFFYQARDDDMIITAGYNVGGPEVEDALLRHPAVAE 468
Cdd:COG0365 389 VIKGPwPGMfrGYWNDPeRYRETYFGrfpGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAE 468
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496182614 469 CGVIGVPDEERGMVVKAVCVLKPGHTGDAAMVKTLQDHVKATIAPFKYPRVVEFVTALPRTETGKLQRFKLRQAAA 544
Cdd:COG0365 469 AAVVGVPDEIRGQVVKAFVVLKPGVEPSDELAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLRKIAE 544
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
39-540 |
1.14e-129 |
|
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: 388.27 E-value: 1.14e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 39 NLVHALFDQAeraeRAGNIDRPLLRGPHRTYTYRDARTEAARIAEVLTQdHGLVPGNRVLLRGGNTVEMALAWLGTVYAG 118
Cdd:cd05959 4 NAATLVDLNL----NEGRGDKTAFIDDAGSLTYAELEAEARRVAGALRA-LGVKREERVLLIMLDTVDFPTAFLGAIRAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 119 LIAVATMPLLRAGELANIIERAQPTLALCDGRLLAEL-AAAQDQHPVLTTIVPFHTATDPADLLQRAQ---GKPGSMQPC 194
Cdd:cd05959 79 IVPVPVNTLLTPDDYAYYLEDSRARVVVVSGELAPVLaAALTKSEHTLVVLIVSGGAGPEAGALLLAElvaAEAEQLKPA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 195 PTSADDIALMAFTSGTTGAPKAAVHTHRDVLAGCEAWPRHVLKATPDDIVAGSPPLAFTFGLGGLLVFPMWAGAS-VYFP 273
Cdd:cd05959 159 ATHADDPAFWLYSSGSTGRPKGVVHLHADIYWTAELYARNVLGIREDDVCFSAAKLFFAYGLGNSLTFPLSVGATtVLMP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 274 DQPyTPETMVTLMRDAGVTISYTAPTFYRQM--APFAKKIGLPQLRICVSAGEGLPDATRQLWKDATGIDMTDGIGATEM 351
Cdd:cd05959 239 ERP-TPAAVFKRIRRYRPTVFFGVPTLYAAMlaAPNLPSRDLSSLRLCVSAGEALPAEVGERWKARFGLDILDGIGSTEM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 352 FHIFISSAGGEARTGAIGKVVPGYTAKVVDDDGNEVPRGTVGKLAVIGP-TGCKYLDDPRQAKYV-KDGWNYPGDAFTQD 429
Cdd:cd05959 318 LHIFLSNRPGRVRYGTTGKPVPGYEVELRDEDGGDVADGEPGELYVRGPsSATMYWNNRDKTRDTfQGEWTRTGDKYVRD 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 430 ADGYFFYQARDDDMIITAGYNVGGPEVEDALLRHPAVAECGVIGVPDEERGMVVKAVCVLKPGHTGDAAMVKTLQDHVKA 509
Cdd:cd05959 398 DDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPGYEDSEALEEELKEFVKD 477
|
490 500 510
....*....|....*....|....*....|.
gi 496182614 510 TIAPFKYPRVVEFVTALPRTETGKLQRFKLR 540
Cdd:cd05959 478 RLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
41-549 |
1.20e-128 |
|
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: 383.39 E-value: 1.20e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 41 VHALFDQAerAERAGniDRPLLRGPHRTYTYRDARTEAARIAEVLtQDHGLVPGNRVLLRGGNTVEMALAWLGTVYAGLI 120
Cdd:COG0318 1 LADLLRRA--AARHP--DRPALVFGGRRLTYAELDARARRLAAAL-RALGVGPGDRVALLLPNSPEFVVAFLAALRAGAV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 121 AVATMPLLRAGELANIIERAQPTLALCdgrllaelaaaqdqhpvlttivpfhtatdpadllqraqgkpgsmqpcptsadd 200
Cdd:COG0318 76 VVPLNPRLTAEELAYILEDSGARALVT----------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 201 iALMAFTSGTTGAPKAAVHTHRDVLAGCEAWPRHvLKATPDDIVAGSPPLAFTFGLGGLLVFPMWAGASVYFPDQpYTPE 280
Cdd:COG0318 103 -ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAA-LGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLPR-FDPE 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 281 TMVTLMRDAGVTISYTAPTFYRQMA--PFAKKIGLPQLRICVSAGEGLPDATRQLWKDATGIDMTDGIGATEMFHIFISS 358
Cdd:COG0318 180 RVLELIERERVTVLFGVPTMLARLLrhPEFARYDLSSLRLVVSGGAPLPPELLERFEERFGVRIVEGYGLTETSPVVTVN 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 359 A--GGEARTGAIGKVVPGYTAKVVDDDGNEVPRGTVGKLAVIGPTGCK-YLDDPRQ-AKYVKDGWNYPGDAFTQDADGYF 434
Cdd:COG0318 260 PedPGERRPGSVGRPLPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKgYWNDPEAtAEAFRDGWLRTGDLGRLDEDGYL 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 435 FYQARDDDMIITAGYNVGGPEVEDALLRHPAVAECGVIGVPDEERGMVVKAVCVLKPGHTGDAAmvkTLQDHVKATIAPF 514
Cdd:COG0318 340 YIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPGAELDAE---ELRAFLRERLARY 416
|
490 500 510
....*....|....*....|....*....|....*
gi 496182614 515 KYPRVVEFVTALPRTETGKLQRFKLRQAAATPQAE 549
Cdd:COG0318 417 KVPRRVEFVDELPRTASGKIDRRALRERYAAGALE 451
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
59-540 |
2.70e-120 |
|
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: 361.78 E-value: 2.70e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 59 RPLLRGPHRTYTYRDARTEAARIAEVLtQDHGLVPGNRVLLRGGNTVEMALAWLGTVYAGLIAVATMPLLRAGELANIIE 138
Cdd:cd05919 1 KTAFYAADRSVTYGQLHDGANRLGSAL-RNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 139 RAQPTLALcdgrllaelaaaqdqhpvlttivpfhtatdpadllqraqgkpgsmqpcpTSADDIALMAFTSGTTGAPKAAV 218
Cdd:cd05919 80 DCEARLVV-------------------------------------------------TSADDIAYLLYSSGTTGPPKGVM 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 219 HTHRDVLAGCEAWPRHVLKATPDDIVAGSPPLAFTFGLGGLLVFPMWAGASVYFPDQPYTPETMVTLMRDAGVTISYTAP 298
Cdd:cd05919 111 HAHRDPLLFADAMAREALGLTPGDRVFSSAKMFFGYGLGNSLWFPLAVGASAVLNPGWPTAERVLATLARFRPTVLYGVP 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 299 TFYRQMAPFAKKI--GLPQLRICVSAGEGLPDATRQLWKDATGIDMTDGIGATEMFHIFISSAGGEARTGAIGKVVPGYT 376
Cdd:cd05919 191 TFYANLLDSCAGSpdALRSLRLCVSAGEALPRGLGERWMEHFGGPILDGIGATEVGHIFLSNRPGAWRLGSTGRPVPGYE 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 377 AKVVDDDGNEVPRGTVGKLAVIGPTGCK-YLDDP-RQAKYVKDGWNYPGDAFTQDADGYFFYQARDDDMIITAGYNVGGP 454
Cdd:cd05919 271 IRLVDEEGHTIPPGEEGDLLVRGPSAAVgYWNNPeKSRATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPV 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 455 EVEDALLRHPAVAECGVIGVPDEERGMVVKAVCVLKPGHTGDAAMVKTLQDHVKATIAPFKYPRVVEFVTALPRTETGKL 534
Cdd:cd05919 351 EVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPQESLARDIHRHLLERLSAHKVPRRIAFVDELPRTATGKL 430
|
....*.
gi 496182614 535 QRFKLR 540
Cdd:cd05919 431 QRFKLR 436
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
57-542 |
5.64e-105 |
|
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: 324.48 E-value: 5.64e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 57 IDRPLLRG---------PHRTYTYRDARTEAARIAEVLTQdHGLVPGNRVLLRGGNTVEMALAWLGTVYAGLIAVATMPL 127
Cdd:TIGR02262 10 LDRNVVEGrggktafidDISSLSYGELEAQVRRLAAALRR-LGVKREERVLLLMLDGVDFPIAFLGAIRAGIVPVALNTL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 128 LRAGELANIIERAQPTLALCDGRLLAELAAAQDQHPVLTTIVPFHTATDPADLLQR--AQGKPGsMQPCPTSADDIALMA 205
Cdd:TIGR02262 89 LTADDYAYMLEDSRARVVFVSGALLPVIKAALGKSPHLEHRVVVGRPEAGEVQLAEllATESEQ-FKPAATQADDPAFWL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 206 FTSGTTGAPKAAVHTHRDVLAGCEAWPRHVLKATPDDIVAGSPPLAFTFGLGGLLVFPMWAGA-SVYFPDQPyTPETMVT 284
Cdd:TIGR02262 168 YSSGSTGMPKGVVHTHSNPYWTAELYARNTLGIREDDVCFSAAKLFFAYGLGNALTFPMSVGAtTVLMGERP-TPDAVFD 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 285 LMRDAGVTISYTAPTFYRQM--APFAKKIGLPQLRICVSAGEGLPDATRQLWKDATGIDMTDGIGATEMFHIFISSAGGE 362
Cdd:TIGR02262 247 RLRRHQPTIFYGVPTLYAAMlaDPNLPSEDQVRLRLCTSAGEALPAEVGQRWQARFGVDIVDGIGSTEMLHIFLSNLPGD 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 363 ARTGAIGKVVPGYTAKVVDDDGNEVPRGTVGKLAVIGPT-GCKYLDDPRQAKYVKDG-WNYPGDAFTQDADGYFFYQARD 440
Cdd:TIGR02262 327 VRYGTSGKPVPGYRLRLVGDGGQDVADGEPGELLISGPSsATMYWNNRAKSRDTFQGeWTRSGDKYVRNDDGSYTYAGRT 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 441 DDMIITAGYNVGGPEVEDALLRHPAVAECGVIGVPDEERGMVVKAVCVLKPGHTGDAAMVKTlqdHVKATIAPFKYPRVV 520
Cdd:TIGR02262 407 DDMLKVSGIYVSPFEIESALIQHPAVLEAAVVGVADEDGLIKPKAFVVLRPGQTALETELKE---HVKDRLAPYKYPRWI 483
|
490 500
....*....|....*....|..
gi 496182614 521 EFVTALPRTETGKLQRFKLRQA 542
Cdd:TIGR02262 484 VFVDDLPKTATGKIQRFKLREG 505
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
69-540 |
5.77e-102 |
|
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: 314.27 E-value: 5.77e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 69 YTYRDARTEAARIAEVLtQDHGLVPGNRVLLRGGNTVEMALAWLGTVYAGLIAVATMPLLRAGELANIIERAQPTLALCD 148
Cdd:cd05972 1 WSFRELKRESAKAANVL-AKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 149 grllaelaaaqdqhpvlttivpfhtatdpadllqraqgkpgsmqpcptsADDIALMAFTSGTTGAPKAAVHTHRDVLAgc 228
Cdd:cd05972 80 -------------------------------------------------AEDPALIYFTSGTTGLPKGVLHTHSYPLG-- 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 229 eAWP--RHVLKATPDDIVAGSPPLAFTFGLGGLLVFPMWAGASVY-FPDQPYTPETMVTLMRDAGVTISYTAPTFYRQMA 305
Cdd:cd05972 109 -HIPtaAYWLGLRPDDIHWNIADPGWAKGAWSSFFGPWLLGATVFvYEGPRFDAERILELLERYGVTSFCGPPTAYRMLI 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 306 pfakKIGLPQ-----LRICVSAGEGLPDATRQLWKDATGIDMTDGIGATEMFHIFISSAGGEARTGAIGKVVPGYTAKVV 380
Cdd:cd05972 188 ----KQDLSSykfshLRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGLTVGNFPDMPVKPGSMGRPTPGYDVAII 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 381 DDDGNEVPRGTVGKLAV-IGPTG--CKYLDDP-RQAKYVKDGWNYPGDAFTQDADGYFFYQARDDDMIITAGYNVGGPEV 456
Cdd:cd05972 264 DDDGRELPPGEEGDIAIkLPPPGlfLGYVGDPeKTEASIRGDYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEV 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 457 EDALLRHPAVAECGVIGVPDEERGMVVKAVCVLKPGHTGDAAMVKTLQDHVKATIAPFKYPRVVEFVTALPRTETGKLQR 536
Cdd:cd05972 344 ESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYEPSEELAEELQGHVKKVLAPYKYPREIEFVEELPKTISGKIRR 423
|
....
gi 496182614 537 FKLR 540
Cdd:cd05972 424 VELR 427
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
58-540 |
8.04e-100 |
|
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: 309.88 E-value: 8.04e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 58 DRPLLRGPHRTYTYRDARTEAARIAEVLtQDHGLVPGNRVLLRGGNTVEMALAWLGTVYAGLIAVATMPLLRAGELANII 137
Cdd:cd05936 14 DKTALIFMGRKLTYRELDALAEAFAAGL-QNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYTPRELEHIL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 138 ERAQPTLALCDgrllaelaaaqdqhpvlttiVPFhtatdpADLLQRAQGKPGsmqPCPTSADDIALMAFTSGTTGAPKAA 217
Cdd:cd05936 93 NDSGAKALIVA--------------------VSF------TDLLAAGAPLGE---RVALTPEDVAVLQYTSGTTGVPKGA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 218 VHTHRDVLA---GCEAWPRHVLkaTPDDIVAGSPPLAFTFGLGGLLVFPMWAGASVYFPDQPyTPETMVTLMRDAGVTIS 294
Cdd:cd05936 144 MLTHRNLVAnalQIKAWLEDLL--EGDDVVLAALPLFHVFGLTVALLLPLALGATIVLIPRF-RPIGVLKEIRKHRVTIF 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 295 YTAPTFYRQM--APFAKKIGLPQLRICVSAGEGLPDATRQLWKDATGIDMTDGIGATEMfhifiSSA------GGEARTG 366
Cdd:cd05936 221 PGVPTMYIALlnAPEFKKRDFSSLRLCISGGAPLPVEVAERFEELTGVPIVEGYGLTET-----SPVvavnplDGPRKPG 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 367 AIGKVVPGYTAKVVDDDGNEVPRGTVGKLAVIGPTGCK-YLDDPRQ-AKYVKDGWNYPGDAFTQDADGYFFYQARDDDMI 444
Cdd:cd05936 296 SIGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKgYWNRPEEtAEAFVDGWLRTGDIGYMDEDGYFFIVDRKKDMI 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 445 ITAGYNVGGPEVEDALLRHPAVAECGVIGVPDEERGMVVKAVCVLKPGHTGDAamvKTLQDHVKATIAPFKYPRVVEFVT 524
Cdd:cd05936 376 IVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEGASLTE---EEIIAFCREQLAGYKVPRQVEFRD 452
|
490
....*....|....*.
gi 496182614 525 ALPRTETGKLQRFKLR 540
Cdd:cd05936 453 ELPKSAVGKILRRELR 468
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
200-535 |
5.64e-92 |
|
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: 285.33 E-value: 5.64e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 200 DIALMAFTSGTTGAPKAAVHTHRDVLAGCEAWpRHVLKATPDDIVAGSPPLAFTFGLGGLLvFPMWAGASVYFPDQPyTP 279
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAAL-AASGGLTEGDVFLSTLPLFHIGGLFGLL-GALLAGGTVVLLPKF-DP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 280 ETMVTLMRDAGVTISYTAPTFYRQMAPFAKKIG--LPQLRICVSAGEGLPDATRQLWKDATGIDMTDGIGATEMFHIFIS 357
Cdd:cd04433 78 EAALELIEREKVTILLGVPTLLARLLKAPESAGydLSSLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGGTVAT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 358 SAGGE--ARTGAIGKVVPGYTAKVVDDDGNEVPRGTVGKLAVIGPTGCK-YLDDPRQAKYVK-DGWNYPGDAFTQDADGY 433
Cdd:cd04433 158 GPPDDdaRKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKgYWNNPEATAAVDeDGWYRTGDLGRLDEDGY 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 434 FFYQARDDDMIITAGYNVGGPEVEDALLRHPAVAECGVIGVPDEERGMVVKAVCVLKPGHTGDAAmvkTLQDHVKATIAP 513
Cdd:cd04433 238 LYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLDAE---ELRAHVRERLAP 314
|
330 340
....*....|....*....|..
gi 496182614 514 FKYPRVVEFVTALPRTETGKLQ 535
Cdd:cd04433 315 YKVPRRVVFVDALPRTASGKID 336
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
50-536 |
6.96e-87 |
|
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: 275.26 E-value: 6.96e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 50 RAERAGniDRPLLRGPHRTYTYRDARTEAARIAEVLTqDHGLVPGNRVLLRGGNTVEMALAWLGTVYAGLIAVATMPLLR 129
Cdd:cd17631 4 RARRHP--DRTALVFGGRSLTYAELDERVNRLAHALR-ALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 130 AGELANIieraqptLALCDGRLLAelaaaqdqhpvlttivpfhtatdpadllqraqgkpgsmqpcptsaDDIALMAFTSG 209
Cdd:cd17631 81 PPEVAYI-------LADSGAKVLF---------------------------------------------DDLALLMYTSG 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 210 TTGAPKAAVHTHRDVLAGCEAWPRHvLKATPDDIVAGSPPLAFTFGLGGLLVFPMWAGASVYFPDQPyTPETMVTLMRDA 289
Cdd:cd17631 109 TTGRPKGAMLTHRNLLWNAVNALAA-LDLGPDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVILRKF-DPETVLDLIERH 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 290 GVTISYTAPTFYRQMA--PFAKKIGLPQLRICVSAGEGLPDATRQLWKDAtGIDMTDGIGATEMFHI--FISSAGGEART 365
Cdd:cd17631 187 RVTSFFLVPTMIQALLqhPRFATTDLSSLRAVIYGGAPMPERLLRALQAR-GVKFVQGYGMTETSPGvtFLSPEDHRRKL 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 366 GAIGKVVPGYTAKVVDDDGNEVPRGTVGKLAVIGPTGCK-YLDDP-RQAKYVKDGWNYPGDAFTQDADGYFFYQARDDDM 443
Cdd:cd17631 266 GSAGRPVFFVEVRIVDPDGREVPPGEVGEIVVRGPHVMAgYWNRPeATAAAFRDGWFHTGDLGRLDEDGYLYIVDRKKDM 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 444 IITAGYNVGGPEVEDALLRHPAVAECGVIGVPDEERGMVVKAVCVLKPGHTGDAAmvkTLQDHVKATIAPFKYPRVVEFV 523
Cdd:cd17631 346 IISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPGAELDED---ELIAHCRERLARYKIPKSVEFV 422
|
490
....*....|...
gi 496182614 524 TALPRTETGKLQR 536
Cdd:cd17631 423 DALPRNATGKILK 435
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
58-541 |
1.59e-86 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 277.07 E-value: 1.59e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 58 DRPLLRGPHRTYTYRDARTEAARIAEVLtQDHGLVPGNRVLLRGGNTVEMALAWLGTVYAGliAVATmPL---LRAGELA 134
Cdd:PRK06187 21 DKEAVYFDGRRTTYAELDERVNRLANAL-RALGVKKGDRVAVFDWNSHEYLEAYFAVPKIG--AVLH-PInirLKPEEIA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 135 NIIERAQPTLALCDGRLLAELAAAQDQHPVLTTIVpFHTATDPADLLQRAQ-------GKPGSMQPCPTSADDIALMAFT 207
Cdd:PRK06187 97 YILNDAEDRVVLVDSEFVPLLAAILPQLPTVRTVI-VEGDGPAAPLAPEVGeyeellaAASDTFDFPDIDENDAAAMLYT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 208 SGTTGAPKAAVHTHRDVL---AGCEAWprhvLKATPDDIVAGSPPLAFTFGLGgLLVFPMWAGASVYFPDQpYTPETMVT 284
Cdd:PRK06187 176 SGTTGHPKGVVLSHRNLFlhsLAVCAW----LKLSRDDVYLVIVPMFHVHAWG-LPYLALMAGAKQVIPRR-FDPENLLD 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 285 LMRDAGVTISYTAPTFYRQM--APFAKKIGLPQLRICVSAGEGLPDATRQLWKDATGIDMTDGIGATEMFHIfISSA--- 359
Cdd:PRK06187 250 LIETERVTFFFAVPTIWQMLlkAPRAYFVDFSSLRLVIYGGAALPPALLREFKEKFGIDLVQGYGMTETSPV-VSVLppe 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 360 ----GGEARTGAIGKVVPGYTAKVVDDDGNEVPR--GTVGKLAVIGPT---GckYLDDPRQ-AKYVKDGWNYPGDAFTQD 429
Cdd:PRK06187 329 dqlpGQWTKRRSAGRPLPGVEARIVDDDGDELPPdgGEVGEIIVRGPWlmqG--YWNRPEAtAETIDGGWLHTGDVGYID 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 430 ADGYFFYQARDDDMIITAGYNVGGPEVEDALLRHPAVAECGVIGVPDEERGMVVKAVCVLKPGHTGDAamvKTLQDHVKA 509
Cdd:PRK06187 407 EDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVLKPGATLDA---KELRAFLRG 483
|
490 500 510
....*....|....*....|....*....|..
gi 496182614 510 TIAPFKYPRVVEFVTALPRTETGKLQRFKLRQ 541
Cdd:PRK06187 484 RLAKFKLPKRIAFVDELPRTSVGKILKRVLRE 515
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
69-541 |
7.08e-85 |
|
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: 270.46 E-value: 7.08e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 69 YTYRDARTEAARIAEVLTQDhGLVPGNRVLLRGGNTVEMALAWLGTVYAGLIAVATMPLLRAGELANIIERAQPTLALCD 148
Cdd:cd05971 7 VTFKELKTASNRFANVLKEI-GLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVTD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 149 GrllaelaaaqdqhpvlttivpfhtatdpadllqraqgkpgsmqpcptsADDIALMAFTSGTTGAPKAAVHTHRdVLAG- 227
Cdd:cd05971 86 G------------------------------------------------SDDPALIIYTSGTTGPPKGALHAHR-VLLGh 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 228 -------CEAWPRhvlkatPDDIVAGSPPLAFTFGLGGLLVFPMWAGASVY-FPDQPYTPETMVTLMRDAGVTISYTAPT 299
Cdd:cd05971 117 lpgvqfpFNLFPR------DGDLYWTPADWAWIGGLLDVLLPSLYFGVPVLaHRMTKFDPKAALDLMSRYGVTTAFLPPT 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 300 FYRQMAPFAKKIGLPQ--LRICVSAGEGLPDATRQLWKDATGIDMTDGIGATEM-FHIFISSAGGEARTGAIGKVVPGYT 376
Cdd:cd05971 191 ALKMMRQQGEQLKHAQvkLRAIATGGESLGEELLGWAREQFGVEVNEFYGQTECnLVIGNCSALFPIKPGSMGKPIPGHR 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 377 AKVVDDDGNEVPRGTVGKLAVIGP---TGCKYLDDPR--QAKYVKDgWNYPGDAFTQDADGYFFYQARDDDMIITAGYNV 451
Cdd:cd05971 271 VAIVDDNGTPLPPGEVGEIAVELPdpvAFLGYWNNPSatEKKMAGD-WLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRI 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 452 GGPEVEDALLRHPAVAECGVIGVPDEERGMVVKAVCVLKPGHTGDAAMVKTLQDHVKATIAPFKYPRVVEFVTALPRTET 531
Cdd:cd05971 350 GPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGETPSDALAREIQELVKTRLAAHEYPREIEFVNELPRTAT 429
|
490
....*....|
gi 496182614 532 GKLQRFKLRQ 541
Cdd:cd05971 430 GKIRRRELRA 439
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
34-540 |
4.00e-83 |
|
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: 268.57 E-value: 4.00e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 34 IPDQANLVHALFDQAERAERAGNidRPLL--------RGPHRTYTYRDARTEAARIAEVLTQDHGLVPGNRVLLRGGNTV 105
Cdd:cd05928 1 VPEYFNFASDVLDQWADKEKAGK--RPPNpalwwvngKGDEVKWSFRELGSLSRKAANVLSGACGLQRGDRVAVILPRVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 106 EMALAWLGTVYAGLIAVATMPLLRAgelANIIERAQPTLALC---DGRLLAELAAAQDQHPVLTT--IVPFHTAT---DP 177
Cdd:cd05928 79 EWWLVNVACIRTGLVFIPGTIQLTA---KDILYRLQASKAKCivtSDELAPEVDSVASECPSLKTklLVSEKSRDgwlNF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 178 ADLLQRAQGKPGSMQpcpTSADDIALMAFTSGTTGAPKAAVHTHRDVLAGCEAWPRHVLKATPDDIVAGSPPLAFTFGLG 257
Cdd:cd05928 156 KELLNEASTEHHCVE---TGSQEPMAIYFTSGTTGSPKMAEHSHSSLGLGLKVNGRYWLDLTASDIMWNTSDTGWIKSAW 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 258 GLLVFPMWAGASVYFPDQP-YTPETMVTLMRDAGVTISYTAPTFYRQMAPF-AKKIGLPQLRICVSAGEGLPDATRQLWK 335
Cdd:cd05928 233 SSLFEPWIQGACVFVHHLPrFDPLVILKTLSSYPITTFCGAPTVYRMLVQQdLSSYKFPSLQHCVTGGEPLNPEVLEKWK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 336 DATGIDMTDGIGATEMFHIFISSAGGEARTGAIGKVVPGYTAKVVDDDGNEVPRGTVGKLAV-IGPTG-----CKYLDDP 409
Cdd:cd05928 313 AQTGLDIYEGYGQTETGLICANFKGMKIKPGSMGKASPPYDVQIIDDNGNVLPPGTEGDIGIrVKPIRpfglfSGYVDNP 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 410 -RQAKYVKDGWNYPGDAFTQDADGYFFYQARDDDMIITAGYNVGGPEVEDALLRHPAVAECGVIGVPDEERGMVVKAVCV 488
Cdd:cd05928 393 eKTAATIRGDFYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVV 472
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 496182614 489 LKPGHTGDA--AMVKTLQDHVKATIAPFKYPRVVEFVTALPRTETGKLQRFKLR 540
Cdd:cd05928 473 LAPQFLSHDpeQLTKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNELR 526
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
35-541 |
3.68e-78 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 255.21 E-value: 3.68e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 35 PDQANLVHALFDQAERaeragNIDRPLLRGPHRTYTYRDARTEAARIAEVLtQDHGLVPGNRVLLRGGNTVEMALAWLGT 114
Cdd:PRK07656 2 NEWMTLPELLARAARR-----FGDKEAYVFGDQRLTYAELNARVRRAAAAL-AALGIGKGDRVAIWAPNSPHWVIAALGA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 115 VYAGLIAVATMPLLRAGELANIIERAQPTLALCDGRLLAELAAAQDQHPVLTTIVPFHTATDPA---------DLLQRAQ 185
Cdd:PRK07656 76 LKAGAVVVPLNTRYTADEAAYILARGDAKALFVLGLFLGVDYSATTRLPALEHVVICETEEDDPhtekmktftDFLAAGD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 186 GkpgSMQPCPTSADDIALMAFTSGTTGAPKAAVHTHRDVLAGCEAWPrHVLKATPDDIVAGSPPLAFTFGLGGLLVFPMW 265
Cdd:PRK07656 156 P---AERAPEVDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWA-EYLGLTEGDRYLAANPFFHVFGYKAGVNAPLM 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 266 AGASVyFPDQPYTPETMVTLMRDAGVTISYTAPTFYRQM--APFAKKIGLPQLRICVSAGEGLPDATRQLWKDATGIDM- 342
Cdd:PRK07656 232 RGATI-LPLPVFDPDEVFRLIETERITVLPGPPTMYNSLlqHPDRSAEDLSSLRLAVTGAASMPVALLERFESELGVDIv 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 343 TDGIGATEMFHIF-ISSAGGEARTGA--IGKVVPGYTAKVVDDDGNEVPRGTVGKLAVIGPTGCK-YLDDPRQAKYV--K 416
Cdd:PRK07656 311 LTGYGLSEASGVTtFNRLDDDRKTVAgtIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKgYYDDPEATAAAidA 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 417 DGWNYPGDAFTQDADGYFFYQARDDDMIITAGYNVGGPEVEDALLRHPAVAECGVIGVPDEERGMVVKAVCVLKPGHTGD 496
Cdd:PRK07656 391 DGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVLKPGAELT 470
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 496182614 497 AAmvkTLQDHVKATIAPFKYPRVVEFVTALPRTETGKLQRFKLRQ 541
Cdd:PRK07656 471 EE---ELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRALRE 512
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
64-541 |
1.22e-77 |
|
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: 254.34 E-value: 1.22e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 64 GPHRTYTYRDARTEAARIAEVLTQdHGLVPGNRVLLRGGNTVEMALAWLGTVYAGLIAVATMPLLRAGELANIIERAQPT 143
Cdd:cd05970 43 GEERIFTFAELADYSDKTANFFKA-MGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQLTAKDIVYRIESADIK 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 144 LALCDGR--LLAELAAAQDQHPVLTTIVPFHtATDP---ADLLQRAQGKPGSMQP----CPTSADDIALMAFTSGTTGAP 214
Cdd:cd05970 122 MIVAIAEdnIPEEIEKAAPECPSKPKLVWVG-DPVPegwIDFRKLIKNASPDFERptanSYPCGEDILLVYFSSGTTGMP 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 215 KAAVHTHRDVLAgceawprHVLKAT------PDDI---VAGSpplaftfGLGGLL---VFPMW-AGASVYFPD-QPYTPE 280
Cdd:cd05970 201 KMVEHDFTYPLG-------HIVTAKywqnvrEGGLhltVADT-------GWGKAVwgkIYGQWiAGAAVFVYDyDKFDPK 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 281 TMVTLMRDAGVTISYTAPTFYRQMA-PFAKKIGLPQLRICVSAGEGLPDATRQLWKDATGIDMTDGIGATEMFHIFISSA 359
Cdd:cd05970 267 ALLEKLSKYGVTTFCAPPTIYRFLIrEDLSRYDLSSLRYCTTAGEALNPEVFNTFKEKTGIKLMEGFGQTETTLTIATFP 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 360 GGEARTGAIGKVVPGYTAKVVDDDGNEVPRGTVGKLAV-------IGPTGCKYLDDPRQAKYVKDGWNYPGDAFTQDADG 432
Cdd:cd05970 347 WMEPKPGSMGKPAPGYEIDLIDREGRSCEAGEEGEIVIrtskgkpVGLFGGYYKDAEKTAEVWHDGYYHTGDAAWMDEDG 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 433 YFFYQARDDDMIITAGYNVGGPEVEDALLRHPAVAECGVIGVPDEERGMVVKAVCVLKPGHTGDAAMVKTLQDHVKATIA 512
Cdd:cd05970 427 YLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIVLAKGYEPSEELKKELQDHVKKVTA 506
|
490 500
....*....|....*....|....*....
gi 496182614 513 PFKYPRVVEFVTALPRTETGKLQRFKLRQ 541
Cdd:cd05970 507 PYKYPRIVEFVDELPKTISGKIRRVEIRE 535
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
67-535 |
1.26e-77 |
|
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: 252.90 E-value: 1.26e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 67 RTYTYRDARTEAARIAEVLtQDHGLVPGNRVLLRGGNTVEMALAWLGTVYAGLIAVATMPLLRAGELANIIERAQPTLAL 146
Cdd:cd05911 9 KELTYAQLRTLSRRLAAGL-RKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 147 CDGRLLAELAAAQDQHPVLTTIVPF----HTATDPADLLQRAQGKPGSMQPCP--TSADDIALMAFTSGTTGAPKAAVHT 220
Cdd:cd05911 88 TDPDGLEKVKEAAKELGPKDKIIVLddkpDGVLSIEDLLSPTLGEEDEDLPPPlkDGKDDTAAILYSSGTTGLPKGVCLS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 221 HRDVLAGCE-AWPRHVLKATPDDIVAGSPPLAFTFGLGGLLvFPMWAGASVYFPDQPYtPETMVTLMRDAGVTISYTAPT 299
Cdd:cd05911 168 HRNLIANLSqVQTFLYGNDGSNDVILGFLPLYHIYGLFTTL-ASLLNGATVIIMPKFD-SELFLDLIEKYKITFLYLVPP 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 300 FYRQMA--PFAKKIGLPQLRICVSAGEGLpdaTRQLW----KDATGIDMTDGIGATEMFHIFISSAGGEARTGAIGKVVP 373
Cdd:cd05911 246 IAAALAksPLLDKYDLSSLRVILSGGAPL---SKELQellaKRFPNATIKQGYGMTETGGILTVNPDGDDKPGSVGRLLP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 374 GYTAKVVDDDGNE-VPRGTVGKLAVIGPTGCK-YLDDPRQAK--YVKDGWNYPGDAFTQDADGYFFYQARDDDMIITAGY 449
Cdd:cd05911 323 NVEAKIVDDDGKDsLGPNEPGEICVRGPQVMKgYYNNPEATKetFDEDGWLHTGDIGYFDEDGYLYIVDRKKELIKYKGF 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 450 NVGGPEVEDALLRHPAVAECGVIGVPDEERGMVVKAVCVLKPGHTGDAAMVKtlqDHVKATIAPFKYPRV-VEFVTALPR 528
Cdd:cd05911 403 QVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGEKLTEKEVK---DYVAKKVASYKQLRGgVVFVDEIPK 479
|
....*..
gi 496182614 529 TETGKLQ 535
Cdd:cd05911 480 SASGKIL 486
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
48-447 |
8.64e-77 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 248.38 E-value: 8.64e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 48 AERAERAGniDRP-LLRGPHRTYTYRDARTEAARIAEVLtQDHGLVPGNRVLLRGGNTVEMALAWLGTVYAGLIAVATMP 126
Cdd:pfam00501 2 ERQAARTP--DKTaLEVGEGRRLTYRELDERANRLAAGL-RALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 127 LLRAGELANIIERAQPTLALCDGRLLAE--LAAAQDQHPVLTTIVPFHTATDPADLLQRAQGKPGS--MQPCPTSADDIA 202
Cdd:pfam00501 79 RLPAEELAYILEDSGAKVLITDDALKLEelLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVppPPPPPPDPDDLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 203 LMAFTSGTTGAPKAAVHTHRDVLAGCEA---WPRHVLKATPDDIVAGSPPLAFTFGLGGLLVFPMWAGASVYFPDQ--PY 277
Cdd:pfam00501 159 YIIYTSGTTGKPKGVMLTHRNLVANVLSikrVRPRGFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVVLPPGfpAL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 278 TPETMVTLMRDAGVTISYTAPTFYRQM--APFAKKIGLPQLRICVSAGEGLPDATRQLWKDATGIDMTDGIGATEM---F 352
Cdd:pfam00501 239 DPAALLELIERYKVTVLYGVPTLLNMLleAGAPKRALLSSLRLVLSGGAPLPPELARRFRELFGGALVNGYGLTETtgvV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 353 HIFISSAGGEARTGAIGKVVPGYTAKVVDDD-GNEVPRGTVGKLAVIGPTGCK-YLDDPR--QAKYVKDGWNYPGDAFTQ 428
Cdd:pfam00501 319 TTPLPLDEDLRSLGSVGRPLPGTEVKIVDDEtGEPVPPGEPGELCVRGPGVMKgYLNDPEltAEAFDEDGWYRTGDLGRR 398
|
410
....*....|....*....
gi 496182614 429 DADGYFFYQARDDDMIITA 447
Cdd:pfam00501 399 DEDGYLEIVGRKKDQIKLG 417
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
69-541 |
2.06e-76 |
|
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: 248.20 E-value: 2.06e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 69 YTYRDARTEAARIAEVLtQDHGLVPGNRVLLRGGNTVEMALAWLGTVYAGLIAVatmPLLRAGELANIIERaqptLALCD 148
Cdd:cd05973 1 LTFGELRALSARFANAL-QELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQ---PLFTAFGPKAIEHR----LRTSG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 149 GRLLAelaaaqdqhpvlttivpfhtatdpADLLQRAQgkpgsmqpcptSADDIALMAFTSGTTGAPKAAVHTHRdVLAGC 228
Cdd:cd05973 73 ARLVV------------------------TDAANRHK-----------LDSDPFVMMFTSGTTGLPKGVPVPLR-ALAAF 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 229 EAWPRHVLKATPDDIVAGSPPLAFTFGLGGLLVFPMWAGASVYFPDQPYTPETMVTLMRDAGVTISYTAPTFYRQM---- 304
Cdd:cd05973 117 GAYLRDAVDLRPEDSFWNAADPGWAYGLYYAITGPLALGHPTILLEGGFSVESTWRVIERLGVTNLAGSPTAYRLLmaag 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 305 APFAKKIGLpQLRICVSAGEGL-PDATRqlWKDAT-GIDMTDGIGATEMfHIFISSAGGEA---RTGAIGKVVPGYTAKV 379
Cdd:cd05973 197 AEVPARPKG-RLRRVSSAGEPLtPEVIR--WFDAAlGVPIHDHYGQTEL-GMVLANHHALEhpvHAGSAGRAMPGWRVAV 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 380 VDDDGNEVPRGTVGKLAV-------IGPTGCKYLDDPRQAkyvkDGWNYPGDAFTQDADGYFFYQARDDDMIITAGYNVG 452
Cdd:cd05973 273 LDDDGDELGPGEPGRLAIdiansplMWFRGYQLPDTPAID----GGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIG 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 453 GPEVEDALLRHPAVAECGVIGVPDEERGMVVKAVCVLKPGHTGDAAMVKTLQDHVKATIAPFKYPRVVEFVTALPRTETG 532
Cdd:cd05973 349 PFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHEGTPALADELQLHVKKRLSAHAYPRTIHFVDELPKTPSG 428
|
....*....
gi 496182614 533 KLQRFKLRQ 541
Cdd:cd05973 429 KIQRFLLRR 437
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
63-536 |
3.90e-74 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 245.96 E-value: 3.90e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 63 RGPHRTYTYRDARTEAARIAEVLtQDHGLVPGNRVLLRGGNTVEMALAWLGTVYAGliAVATmPLLRA-GELAnIIERaq 141
Cdd:PRK04319 68 ASRKEKYTYKELKELSNKFANVL-KELGVEKGDRVFIFMPRIPELYFALLGALKNG--AIVG-PLFEAfMEEA-VRDR-- 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 142 ptLALCDGRLLAELAAA-----QDQHPVLTTIVPFHTATDPA----DLLQRAQGKPGSMQPCPTSADDIALMAFTSGTTG 212
Cdd:PRK04319 141 --LEDSEAKVLITTPALlerkpADDLPSLKHVLLVGEDVEEGpgtlDFNALMEQASDEFDIEWTDREDGAILHYTSGSTG 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 213 APKAAVHTHRDVLAGcEAWPRHVLKATPDDI---------VAGSpplafTFGLGGllvfPMWAGASVYFPDQPYTPETMV 283
Cdd:PRK04319 219 KPKGVLHVHNAMLQH-YQTGKYVLDLHEDDVywctadpgwVTGT-----SYGIFA----PWLNGATNVIDGGRFSPERWY 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 284 TLMRDAGVTISYTAPTFYRQM----APFAKKIGLPQLRICVSAGEGL-PDATRqlW-KDATGIDMTDGIGATEMFHIFIS 357
Cdd:PRK04319 289 RILEDYKVTVWYTAPTAIRMLmgagDDLVKKYDLSSLRHILSVGEPLnPEVVR--WgMKVFGLPIHDNWWMTETGGIMIA 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 358 S-AGGEARTGAIGKVVPGYTAKVVDDDGNEVPRGTVGKLAVigPTGC-----KYLDDP-RQAKYVKDGWNYPGDAFTQDA 430
Cdd:PRK04319 367 NyPAMDIKPGSMGKPLPGIEAAIVDDQGNELPPNRMGNLAI--KKGWpsmmrGIWNNPeKYESYFAGDWYVSGDSAYMDE 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 431 DGYFFYQARDDDMIITAGYNVGGPEVEDALLRHPAVAECGVIGVPDEERGMVVKAVCVLKPGHTGDAAMVKTLQDHVKAT 510
Cdd:PRK04319 445 DGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVALRPGYEPSEELKEEIRGFVKKG 524
|
490 500
....*....|....*....|....*.
gi 496182614 511 IAPFKYPRVVEFVTALPRTETGKLQR 536
Cdd:PRK04319 525 LGAHAAPREIEFKDKLPKTRSGKIMR 550
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
69-540 |
5.33e-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: 242.02 E-value: 5.33e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 69 YTYRDARTEAARIAEVLtQDHGLVPGNRVLLRGGNTVEMALAWLGTVYAGLIAVatmPLLRA-GELAnIIERAQptlaLC 147
Cdd:cd05969 1 YTFAQLKVLSARFANVL-KSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVIC---PLFSAfGPEA-IRDRLE----NS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 148 DGRLLaelaaaqdqhpvLTTivpfhtatdpADLLQRaqgkpgsmqpcpTSADDIALMAFTSGTTGAPKAAVHTHRDVLAG 227
Cdd:cd05969 72 EAKVL------------ITT----------EELYER------------TDPEDPTLLHYTSGTTGTPKGVLHVHDAMIFY 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 228 CEAwPRHVLKATPDDIVAGSPPLAFTFGLGGLLVFPMWAGASVYFPDQPYTPETMVTLMRDAGVTISYTAPTFYRQM--- 304
Cdd:cd05969 118 YFT-GKYVLDLHPDDIYWCTADPGWVTGTVYGIWAPWLNGVTNVVYEGRFDAESWYGIIERVKVTVWYTAPTAIRMLmke 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 305 -APFAKKIGLPQLRICVSAGEGL-PDATRqlW-KDATGIDMTDGIGATEMFHIFISS-AGGEARTGAIGKVVPGYTAKVV 380
Cdd:cd05969 197 gDELARKYDLSSLRFIHSVGEPLnPEAIR--WgMEVFGVPIHDTWWQTETGSIMIANyPCMPIKPGSMGKPLPGVKAAVV 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 381 DDDGNEVPRGTVGKLAVIG--PTGCK-YLDDP-RQAKYVKDGWNYPGDAFTQDADGYFFYQARDDDMIITAGYNVGGPEV 456
Cdd:cd05969 275 DENGNELPPGTKGILALKPgwPSMFRgIWNDEeRYKNSFIDGWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEV 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 457 EDALLRHPAVAECGVIGVPDEERGMVVKAVCVLKPGHTGDAAMVKTLQDHVKATIAPFKYPRVVEFVTALPRTETGKLQR 536
Cdd:cd05969 355 ESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPSDELKEEIINFVRQKLGAHVAPREIEFVDNLPKTRSGKIMR 434
|
....
gi 496182614 537 FKLR 540
Cdd:cd05969 435 RVLK 438
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
67-540 |
6.79e-73 |
|
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: 238.35 E-value: 6.79e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 67 RTYTYRDARTEAARIAEVLtQDHGLVPGNRVLLRGGNTVEMALAWLGTVYAGLIAVATMPLLRAGELANIIERAQPTLAL 146
Cdd:cd05934 2 RRWTYAELLRESARIAAAL-AALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 147 CDgrllaelaaaqdqhpvlttivpfhtatdPADLLqraqgkpgsmqpcptsaddialmaFTSGTTGAPKAAVHTHRDVLA 226
Cdd:cd05934 81 VD----------------------------PASIL------------------------YTSGTTGPPKGVVITHANLTF 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 227 GCEaWPRHVLKATPDDIVAGSPPLaftFGLGGLL--VFPMWAGASVYFPDQPYTPETMVTLMRDAGVTISYT----APTF 300
Cdd:cd05934 109 AGY-YSARRFGLGEDDVYLTVLPL---FHINAQAvsVLAALSVGATLVLLPRFSASRFWSDVRRYGATVTNYlgamLSYL 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 301 YRQmaPFAKKIGLPQLRICVSAGegLPDATRQLWKDATGIDMTDGIGATEMFHIFISSAGGEARTGAIGKVVPGYTAKVV 380
Cdd:cd05934 185 LAQ--PPSPDDRAHRLRAAYGAP--NPPELHEEFEERFGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAPGYEVRIV 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 381 DDDGNEVPRGTVGKLAVIGPTG----CKYLDDPRQ-AKYVKDGWNYPGDAFTQDADGYFFYQARDDDMIITAGYNVGGPE 455
Cdd:cd05934 261 DDDGQELPAGEPGELVIRGLRGwgffKGYYNMPEAtAEAMRNGWFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAE 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 456 VEDALLRHPAVAECGVIGVPDEERGMVVKAVCVLKPGHTGDAAmvkTLQDHVKATIAPFKYPRVVEFVTALPRTETGKLQ 535
Cdd:cd05934 341 VERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLDPE---ELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVA 417
|
....*
gi 496182614 536 RFKLR 540
Cdd:cd05934 418 KAQLR 422
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
58-541 |
3.61e-72 |
|
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: 237.19 E-value: 3.61e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 58 DRPLLRGPHRTYTYRDARTEAARIAEVLTQDHGLVPGNRVLLRGGNTVEMALAWLGTVYAGLIAVATMPLLRAGELANII 137
Cdd:cd05941 1 DRIAIVDDGDSITYADLVARAARLANRLLALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 138 ERAQPTLALcdgrllaelaaaqdqhpvlttivpfhtatdpadllqraqgkpgsmqpcptsadDIALMAFTSGTTGAPKAA 217
Cdd:cd05941 81 TDSEPSLVL-----------------------------------------------------DPALILYTSGTTGRPKGV 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 218 VHTHRDVLAGC----EAWprhvlKATPDDIVAGSPPLAFTFGLGGLLVFPMWAGASVYF-PdqPYTPETMVTLMRDAGVT 292
Cdd:cd05941 108 VLTHANLAANVralvDAW-----RWTEDDVLLHVLPLHHVHGLVNALLCPLFAGASVEFlP--KFDPKEVAISRLMPSIT 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 293 ISYTAPTFY-------RQMAP---FAKKIGLPQLRICVSAGEGLPDATRQLWKDATGIDMTDGIGATEMFHIFISSAGGE 362
Cdd:cd05941 181 VFMGVPTIYtrllqyyEAHFTdpqFARAAAAERLRLMVSGSAALPVPTLEEWEAITGHTLLERYGMTEIGMALSNPLDGE 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 363 ARTGAIGKVVPGYTAKVVDDDGNE-VPRGTVGKLAVIGPTGCK-YLDDPRQAK--YVKDGWNYPGDAFTQDADGYFFYQA 438
Cdd:cd05941 261 RRPGTVGMPLPGVQARIVDEETGEpLPRGEVGEIQVRGPSVFKeYWNKPEATKeeFTDDGWFKTGDLGVVDEDGYYWILG 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 439 RDDDMII-TAGYNVGGPEVEDALLRHPAVAECGVIGVPDEERGMVVKAVCVLKPGHTgdAAMVKTLQDHVKATIAPFKYP 517
Cdd:cd05941 341 RSSVDIIkSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGAA--ALSLEELKEWAKQRLAPYKRP 418
|
490 500
....*....|....*....|....
gi 496182614 518 RVVEFVTALPRTETGKLQRFKLRQ 541
Cdd:cd05941 419 RRLILVDELPRNAMGKVNKKELRK 442
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
58-545 |
1.13e-70 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 235.60 E-value: 1.13e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 58 DRPLLRGPHRTYTYRDARTEAARIAEVLtQDHGLVPGNRVLLRGGNTVEMALAWLGTVYAGLIAVATMPLLRAGELANII 137
Cdd:PRK08316 26 DKTALVFGDRSWTYAELDAAVNRVAAAL-LDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYIL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 138 ERAQPTLALCDGRLLAELAAAQDQHPVLTTIVPFHTATDPA-----DLLQRAQGKPGSMQPCPTSADDIALMAFTSGTTG 212
Cdd:PRK08316 105 DHSGARAFLVDPALAPTAEAALALLPVDTLILSLVLGGREApggwlDFADWAEAGSVAEPDVELADDDLAQILYTSGTES 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 213 APKAAVHTHRDVLA---GCEAwprhVLKATPDDIVAGSPPLaftFGLGGLLVFPM---WAGASVYFPDQPyTPETMVTLM 286
Cdd:PRK08316 185 LPKGAMLTHRALIAeyvSCIV----AGDMSADDIPLHALPL---YHCAQLDVFLGpylYVGATNVILDAP-DPELILRTI 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 287 RDAGVTISYTAPTFYRQMA--PFAKKIGLPQLRIC---VSA---------GEGLPDAtrQLWkdatgidmtDGIGATEM- 351
Cdd:PRK08316 257 EAERITSFFAPPTVWISLLrhPDFDTRDLSSLRKGyygASImpvevlkelRERLPGL--RFY---------NCYGQTEIa 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 352 -FHIFISSAGGEARTGAIGKVVPGYTAKVVDDDGNEVPRGTVGKLAVIGPTGCK-YLDDP-RQAKYVKDGWNYPGDAFTQ 428
Cdd:PRK08316 326 pLATVLGPEEHLRRPGSAGRPVLNVETRVVDDDGNDVAPGEVGEIVHRSPQLMLgYWDDPeKTAEAFRGGWFHSGDLGVM 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 429 DADGYFFYQARDDDMIITAGYNVGGPEVEDALLRHPAVAECGVIGVPDEERGMVVKAVCVLKPGHTGDAAmvkTLQDHVK 508
Cdd:PRK08316 406 DEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAGATVTED---ELIAHCR 482
|
490 500 510
....*....|....*....|....*....|....*..
gi 496182614 509 ATIAPFKYPRVVEFVTALPRTETGKLQRFKLRQAAAT 545
Cdd:PRK08316 483 ARLAGFKVPKRVIFVDELPRNPSGKILKRELRERYAG 519
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
68-541 |
2.04e-67 |
|
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: 224.57 E-value: 2.04e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 68 TYTYRDARTEAARIAEVLTQdHGLVPGNRVLLRGGNTVEMALAWLGTVYAGLIAVATMPLLRAGELANIIERAQPTLALC 147
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAA-LGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 148 DGRLlaelaaaqdqhpvlttivpfhTATDPADLlqraqgkpgsmqpcptsADDIALMAFTSGTTGAPKAAVHTHRDVLAG 227
Cdd:cd05903 80 PERF---------------------RQFDPAAM-----------------PDAVALLLFTSGTTGEPKGVMHSHNTLSAS 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 228 CEAWPRHvLKATPDDIVAGSPPLAFTFGLGGLLVFPMWAGASVYFpDQPYTPETMVTLMRDAGVTISYTAPTFYRQMAPF 307
Cdd:cd05903 122 IRQYAER-LGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVL-QDIWDPDKALALMREHGVTFMMGATPFLTDLLNA 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 308 AKKIG--LPQLRICVSAGEGLPDA-TRQLWkDATGIDMTDGIGATEMFHIFISSAGG--EARTGAIGKVVPGYTAKVVDD 382
Cdd:cd05903 200 VEEAGepLSRLRTFVCGGATVPRSlARRAA-ELLGAKVCSAYGSTECPGAVTSITPApeDRRLYTDGRPLPGVEIKVVDD 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 383 DGNEVPRGTVGKLAVIGPTGCK-YLDDPRQAK-YVKDGWNYPGDAFTQDADGYFFYQARDDDMIITAGYNVGGPEVEDAL 460
Cdd:cd05903 279 TGATLAPGVEGELLSRGPSVFLgYLDRPDLTAdAAPEGWFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLL 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 461 LRHPAVAECGVIGVPDEERGMVVKAVCVLKPGHTGD-AAMVKTLQdhvKATIAPFKYPRVVEFVTALPRTETGKLQRFKL 539
Cdd:cd05903 359 LGHPGVIEAAVVALPDERLGERACAVVVTKSGALLTfDELVAYLD---RQGVAKQYWPERLVHVDDLPRTPSGKVQKFRL 435
|
..
gi 496182614 540 RQ 541
Cdd:cd05903 436 RE 437
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
48-550 |
7.25e-66 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 227.22 E-value: 7.25e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 48 AERAERAGNIDRPLLRGPHrTYTYRDARTEAARIAEVLtQDHGLVPGNRVLLRGGNTVEMALAWLGTVYAGLIAVATMPL 127
Cdd:PRK06060 11 AEQASEAGWYDRPAFYAAD-VVTHGQIHDGAARLGEVL-RNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 128 LRAGELANIIERAQPTLALCDGRLLAELAAAqdqhpvlttivpfhTATDPADLLQRA-QGKPGSMQPcpTSADDIALMAF 206
Cdd:PRK06060 89 LHRDDHALAARNTEPALVVTSDALRDRFQPS--------------RVAEAAELMSEAaRVAPGGYEP--MGGDALAYATY 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 207 TSGTTGAPKAAVHTHRDVLAGCEAWPRHVLKATPDDIVAGSPPLAFTFGLGGLLVFPMWAGASVYFPDQPYTPETMVTLM 286
Cdd:PRK06060 153 TSGTTGPPKAAIHRHADPLTFVDAMCRKALRLTPEDTGLCSARMYFAYGLGNSVWFPLATGGSAVINSAPVTPEAAAILS 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 287 RDAGVTISYTAPTFYRQMAPFAKKIGLPQLRICVSAGEGL-PDATRQLWKDATGIDMTDGIGATEMFHIFISSAGGEART 365
Cdd:PRK06060 233 ARFGPSVLYGVPNFFARVIDSCSPDSFRSLRCVVSAGEALeLGLAERLMEFFGGIPILDGIGSTEVGQTFVSNRVDEWRL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 366 GAIGKVVPGYTAKVVDDDGNEVPRGTVGKLAVIGPTGCK-YLDDPrQAKYVKDGWNYPGDAFTQDADGYFFYQARDDDMI 444
Cdd:PRK06060 313 GTLGRVLPPYEIRVVAPDGTTAGPGVEGDLWVRGPAIAKgYWNRP-DSPVANEGWLDTRDRVCIDSDGWVTYRCRADDTE 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 445 ITAGYNVGGPEVEDALLRHPAVAECGVIGVPDEERGMVVKAVCVLKPGHTGDAAMVKTLQDHVKATIAPFKYPRVVEFVT 524
Cdd:PRK06060 392 VIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSGATIDGSVMRDLHRGLLNRLSAFKVPHRFAVVD 471
|
490 500
....*....|....*....|....*..
gi 496182614 525 ALPRTETGKLQRFKLR-QAAATPQAEV 550
Cdd:PRK06060 472 RLPRTPNGKLVRGALRkQSPTKPIWEL 498
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
69-541 |
1.21e-65 |
|
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: 221.42 E-value: 1.21e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 69 YTYRDARTEAARIAEVLTqDHGLVPGNRVLLRGGNTVEMALAWLGTVYAGLIAVATMPLLRAGELANIIERAQPTLALCD 148
Cdd:cd05926 15 LTYADLAELVDDLARQLA-ALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVLTP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 149 GRLLAELAAAQdQHPVLTTI------VPFHTATDPADLLQRAQGKPGSMQPCPTSADDIALMAFTSGTTGAPKAAVHTHR 222
Cdd:cd05926 94 KGELGPASRAA-SKLGLAILelaldvGVLIRAPSAESLSNLLADKKNAKSEGVPLPDDLALILHTSGTTGRPKGVPLTHR 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 223 DVLAGCeawpRHVLKA---TPDDIVAGSPPLAFTFGLGGLLVFPMWAGASVYFPDQpYTPETMVTLMRDAGVTIsYTA-P 298
Cdd:cd05926 173 NLAASA----TNITNTyklTPDDRTLVVMPLFHVHGLVASLLSTLAAGGSVVLPPR-FSASTFWPDVRDYNATW-YTAvP 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 299 TFYR---QMAPFAKKIGLPQLRICVSAGEGLPDATRQLWKDATGIDMTDGIGATEMFHIFISSA--GGEARTGAIGKVVp 373
Cdd:cd05926 247 TIHQillNRPEPNPESPPPKLRFIRSCSASLPPAVLEALEATFGAPVLEAYGMTEAAHQMTSNPlpPGPRKPGSVGKPV- 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 374 GYTAKVVDDDGNEVPRGTVGKLAVIGPTGCK-YLDDP--RQAKYVKDGWNYPGDAFTQDADGYFFYQARDDDMIITAGYN 450
Cdd:cd05926 326 GVEVRILDEDGEILPPGVVGEICLRGPNVTRgYLNNPeaNAEAAFKDGWFRTGDLGYLDADGYLFLTGRIKELINRGGEK 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 451 VGGPEVEDALLRHPAVAECGVIGVPDEERGMVVKAVCVLKPGHTGDAAmvkTLQDHVKATIAPFKYPRVVEFVTALPRTE 530
Cdd:cd05926 406 ISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGASVTEE---ELRAFCRKHLAAFKVPKKVYFVDELPKTA 482
|
490
....*....|.
gi 496182614 531 TGKLQRFKLRQ 541
Cdd:cd05926 483 TGKIQRRKVAE 493
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
44-548 |
2.77e-64 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 219.06 E-value: 2.77e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 44 LFDQAER-AERAGniDRPLLRGPHRTYTYRDARTEAARIAEVLTQDHGLVPGNRVLLRGGNTVEMALAWLGTVYAGLIAV 122
Cdd:PRK08314 12 LFHNLEVsARRYP--DKTAIVFYGRAISYRELLEEAERLAGYLQQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 123 ATMPLLRAGELANIIERAQPTLALCDGRLLAELAAAQDQHPVLTTIV-------PFHTATDPADLLQ------------- 182
Cdd:PRK08314 90 PVNPMNREEELAHYVTDSGARVAIVGSELAPKVAPAVGNLRLRHVIVaqysdylPAEPEIAVPAWLRaepplqalapggv 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 183 -------RAQGKPGSMQPcptSADDIALMAFTSGTTGAPKAAVHTHRDVLA---GCEAWPRhvlkATPDDIVAGSPPLAF 252
Cdd:PRK08314 170 vawkealAAGLAPPPHTA---GPDDLAVLPYTSGTTGVPKGCMHTHRTVMAnavGSVLWSN----STPESVVLAVLPLFH 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 253 TFGLGGLLVFPMWAGASVYFPDQpYTPETMVTLMRDAGVTISYTAPT----FYRQmaPFAKKIGLPQLRICVSAGEGLPD 328
Cdd:PRK08314 243 VTGMVHSMNAPIYAGATVVLMPR-WDREAAARLIERYRVTHWTNIPTmvvdFLAS--PGLAERDLSSLRYIGGGGAAMPE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 329 ATRQLWKDATGIDMTDGIGATEMFHIFISSAGGEARTGAIGKVVPGYTAKVVD-DDGNEVPRGTVGKLAVIGPTGCK-YL 406
Cdd:PRK08314 320 AVAERLKELTGLDYVEGYGLTETMAQTHSNPPDRPKLQCLGIPTFGVDARVIDpETLEELPPGEVGEIVVHGPQVFKgYW 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 407 DDP---RQAKYVKDGWNY--PGDAFTQDADGYFFYQARDDDMIITAGYNVGGPEVEDALLRHPAVAECGVIGVPDEERGM 481
Cdd:PRK08314 400 NRPeatAEAFIEIDGKRFfrTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPDPRRGE 479
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496182614 482 VVKAVCVLKPGHTGDAAmVKTLQDHVKATIAPFKYPRVVEFVTALPRTETGKLQRFKLRQAAATPQA 548
Cdd:PRK08314 480 TVKAVVVLRPEARGKTT-EEEIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKILWRQLQEQEKARAA 545
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
48-547 |
2.10e-62 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 214.24 E-value: 2.10e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 48 AERAERAGniDRPLLRGPHRTYTYRDARTEAARIAEVLtQDHGLVPGNRVLLRGGNTVEMALAWLGTVYAGLIAVATMPL 127
Cdd:PRK06155 28 ARQAERYP--DRPLLVFGGTRWTYAEAARAAAAAAHAL-AAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 128 LRAGELANIIERAQPTLALCDGRLLAELAAAQDQHPVLTTIVPFHTATDPA-DLLQRAQGKPGSMQPCPTSA---DDIAL 203
Cdd:PRK06155 105 LRGPQLEHILRNSGARLLVVEAALLAALEAADPGDLPLPAVWLLDAPASVSvPAGWSTAPLPPLDAPAPAAAvqpGDTAA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 204 MAFTSGTTGAPKAAVHTHrdvlAGCEAWPRHV---LKATPDDIVAGSPPLAFTFGL---------GGLLVFPMWAGASVY 271
Cdd:PRK06155 185 ILYTSGTTGPSKGVCCPH----AQFYWWGRNSaedLEIGADDVLYTTLPLFHTNALnaffqallaGATYVLEPRFSASGF 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 272 FPDQPYTPETmVTLMRDAGVTISYTAPTFYRQMAPfakkiglpqlRICVSAGEGLPDATRQLWKDATGIDMTDGIGATEM 351
Cdd:PRK06155 261 WPAVRRHGAT-VTYLLGAMVSILLSQPARESDRAH----------RVRVALGPGVPAALHAAFRERFGVDLLDGYGSTET 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 352 fHIFISSAGGEARTGAIGKVVPGYTAKVVDDDGNEVPRGTVGKLAVIG------PTGckYLDDPrqAKYV---KDGWNYP 422
Cdd:PRK06155 330 -NFVIAVTHGSQRPGSMGRLAPGFEARVVDEHDQELPDGEPGELLLRAdepfafATG--YFGMP--EKTVeawRNLWFHT 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 423 GDAFTQDADGYFFYQARDDDMIITAGYNVGGPEVEDALLRHPAVAECGVIGVPDEERGMVVKAVCVLKPGHTGDAAmvkT 502
Cdd:PRK06155 405 GDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDGTALEPV---A 481
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 496182614 503 LQDHVKATIAPFKYPRVVEFVTALPRTETGKLQRFKLRQAAATPQ 547
Cdd:PRK06155 482 LVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVLREQGVTAD 526
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
48-548 |
1.03e-60 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 209.91 E-value: 1.03e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 48 AERAERAGNIDRPLLRGPHRTYTYRDARTEAARIAEVLTqDHGLVPGNRVLLRGGNTVEMALAWLGTVYAGLIAVATMPL 127
Cdd:PRK13295 35 ASCPDKTAVTAVRLGTGAPRRFTYRELAALVDRVAVGLA-RLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 128 LRAGELANIIERAQPTLALCDGRL-----LAELAAAQDQHPVLTTIVPF--HTATDPADLL-----QRAQGKPGSMQPCP 195
Cdd:PRK13295 114 FRERELSFMLKHAESKVLVVPKTFrgfdhAAMARRLRPELPALRHVVVVggDGADSFEALLitpawEQEPDAPAILARLR 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 196 TSADDIALMAFTSGTTGAPKAAVHTHRDVLAGCEAWPRHvLKATPDDIVAGSPPLAFTFGLGGLLVFPMWAGASVYFPDQ 275
Cdd:PRK13295 194 PGPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAER-LGLGADDVILMASPMAHQTGFMYGLMMPVMLGATAVLQDI 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 276 pYTPETMVTLMRDAGVTISYTAPTFYRQMAPFAKKIG--LPQLRICVSAGEGLPDATRQlwkdatgiDMTDGIGATemfh 353
Cdd:PRK13295 273 -WDPARAAELIRTEGVTFTMASTPFLTDLTRAVKESGrpVSSLRTFLCAGAPIPGALVE--------RARAALGAK---- 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 354 ifISSAGGEARTGAI----------------GKVVPGYTAKVVDDDGNEVPRGTVGKLAVIGPTG-CKYLDDPRQAKYVK 416
Cdd:PRK13295 340 --IVSAWGMTENGAVtltklddpderasttdGCPLPGVEVRVVDADGAPLPAGQIGRLQVRGCSNfGGYLKRPQLNGTDA 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 417 DGWNYPGDAFTQDADGYFFYQARDDDMIITAGYNVGGPEVEDALLRHPAVAECGVIGVPDEERGMVVKAVCVLKPGHTGD 496
Cdd:PRK13295 418 DGWFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPRPGQSLD 497
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 496182614 497 -AAMVKTLQDHvkaTIAPFKYPRVVEFVTALPRTETGKLQRFKLRQAAATPQA 548
Cdd:PRK13295 498 fEEMVEFLKAQ---KVAKQYIPERLVVRDALPRTPSGKIQKFRLREMLRGEDA 547
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
35-540 |
1.35e-60 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 209.62 E-value: 1.35e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 35 PDQANLVHALFDQAerAERAGniDRPLLRGPHRTYTYRDARTEAARIAEVLTQDHGLVPGNRVLLRGGNTVEMALAWLGT 114
Cdd:PRK05677 20 PDEYPNIQAVLKQS--CQRFA--DKPAFSNLGKTLTYGELYKLSGAFAAWLQQHTDLKPGDRIAVQLPNVLQYPVAVFGA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 115 VYAGLIAVATMPLLRAGE---------------LANIIERAQPTLALCDGR--LLAELAaaqDQHPVLTTIV-------- 169
Cdd:PRK05677 96 MRAGLIVVNTNPLYTAREmehqfndsgakalvcLANMAHLAEKVLPKTGVKhvIVTEVA---DMLPPLKRLLinavvkhv 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 170 -----PFH--TATDPADLLQRAQGKPgsMQPCPTSADDIALMAFTSGTTGAPKAAVHTHRDVLAG---CEAWPRHVLKAT 239
Cdd:PRK05677 173 kkmvpAYHlpQAVKFNDALAKGAGQP--VTEANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANmlqCRALMGSNLNEG 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 240 PDDIVAgspPL------AFTFGLGGLlvfpMWAGASVYFPDQPYTPETMVTLMRDAGVTISYTAPTFYRQMA---PFaKK 310
Cdd:PRK05677 251 CEILIA---PLplyhiyAFTFHCMAM----MLIGNHNILISNPRDLPAMVKELGKWKFSGFVGLNTLFVALCnneAF-RK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 311 IGLPQLRICVSAGEGLPDATRQLWKDATGIDMTDGIGATEMFHIFISSAGGEARTGAIGKVVPGYTAKVVDDDGNEVPRG 390
Cdd:PRK05677 323 LDFSALKLTLSGGMALQLATAERWKEVTGCAICEGYGMTETSPVVSVNPSQAIQVGTIGIPVPSTLCKVIDDDGNELPLG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 391 TVGKLAVIGPTGCK-YLDDPRQAKYV--KDGWNYPGDAFTQDADGYFFYQARDDDMIITAGYNVGGPEVEDALLRHPAVA 467
Cdd:PRK05677 403 EVGELCVKGPQVMKgYWQRPEATDEIldSDGWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVL 482
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496182614 468 ECGVIGVPDEERGMVVKAVCVLKPGHTGDAAMVKtlqDHVKATIAPFKYPRVVEFVTALPRTETGKLQRFKLR 540
Cdd:PRK05677 483 QCAAIGVPDEKSGEAIKVFVVVKPGETLTKEQVM---EHMRANLTGYKVPKAVEFRDELPTTNVGKILRRELR 552
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
38-542 |
1.22e-59 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 205.88 E-value: 1.22e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 38 ANLVHALFDQAERAeragniDRPLLRGPH-RTYTYRDARTEAARIAEVLTQdHGLVPGNRVLLRGGNTVEMALAWLGTVY 116
Cdd:PRK07514 3 NNLFDALRAAFADR------DAPFIETPDgLRYTYGDLDAASARLANLLVA-LGVKPGDRVAVQVEKSPEALALYLATLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 117 AGLIavaTMPL---LRAGELANIIERAQPTLALCDGRLLAELAAAQDQHPVLttivpfHTATDPAD----LLQRAQGKPG 189
Cdd:PRK07514 76 AGAV---FLPLntaYTLAELDYFIGDAEPALVVCDPANFAWLSKIAAAAGAP------HVETLDADgtgsLLEAAAAAPD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 190 SMQPCPTSADDIALMAFTSGTTGAPKAAVHTHRDVLAGC----EAWprhvlKATPDDIVAGSPPLAFTFGL-----GGLL 260
Cdd:PRK07514 147 DFETVPRGADDLAAILYTSGTTGRSKGAMLSHGNLLSNAltlvDYW-----RFTPDDVLIHALPIFHTHGLfvatnVALL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 261 vfpmwAGASVYFpdQP-YTPETMVTLMRDA----GVtisytaPTFYRQM--APFAKKIGLPQLRICVSAGEGLPDATRQL 333
Cdd:PRK07514 222 -----AGASMIF--LPkFDPDAVLALMPRAtvmmGV------PTFYTRLlqEPRLTREAAAHMRLFISGSAPLLAETHRE 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 334 WKDATGIDMTDGIGATEMfhIFISSA--GGEARTGAIGKVVPGYTAKVVD-DDGNEVPRGTVGKLAVIGPTGCK-YLDDP 409
Cdd:PRK07514 289 FQERTGHAILERYGMTET--NMNTSNpyDGERRAGTVGFPLPGVSLRVTDpETGAELPPGEIGMIEVKGPNVFKgYWRMP 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 410 RQ--AKYVKDGWNYPGDAFTQDADGYFFYQARDDDMIITAGYNVGGPEVEDALLRHPAVAECGVIGVPDEERGMVVKAVC 487
Cdd:PRK07514 367 EKtaEEFRADGFFITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVV 446
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 496182614 488 VLKPGHTGD-AAMVKTLqdhvKATIAPFKYPRVVEFVTALPRTETGKLQRFKLRQA 542
Cdd:PRK07514 447 VPKPGAALDeAAILAAL----KGRLARFKQPKRVFFVDELPRNTMGKVQKNLLREQ 498
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
58-542 |
1.00e-58 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 203.68 E-value: 1.00e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 58 DRPLLRGPHRTYTYRDARTEAARIAEVLtQDHGLVPGNRVLLRGGNTVEMALAWLGTVYAGLIAVATMPLLRAGELANII 137
Cdd:PRK06188 27 DRPALVLGDTRLTYGQLADRISRYIQAF-EALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHPLGSLDDHAYVL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 138 ERAQPTLALCDGRLLAELAAA-QDQHPVLTTIVPFHTATDPADLLQRAQGKPGSMQPCPTSADDIALMAFTSGTTGAPKA 216
Cdd:PRK06188 106 EDAGISTLIVDPAPFVERALAlLARVPSLKHVLTLGPVPDGVDLLAAAAKFGPAPLVAAALPPDIAGLAYTGGTTGKPKG 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 217 AVHTHRDV-------LAGCEaWPRHV--LKATPDDIVagspplaftfglGGLLVFP-MWAGASVYFPDQpYTPETMVTLM 286
Cdd:PRK06188 186 VMGTHRSIatmaqiqLAEWE-WPADPrfLMCTPLSHA------------GGAFFLPtLLRGGTVIVLAK-FDPAEVLRAI 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 287 RDAGVTISYTAPT-FYRQM-APFAKKIGLPQLRIcVSAGEGLPDATRQlwkdATGIDMTDGI-----GATEMfHIFIS-- 357
Cdd:PRK06188 252 EEQRITATFLVPTmIYALLdHPDLRTRDLSSLET-VYYGASPMSPVRL----AEAIERFGPIfaqyyGQTEA-PMVITyl 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 358 -----SAGGEARTGAIGKVVPGYTAKVVDDDGNEVPRGTVGKLAVIGPTGCK-YLDDPRQ-AKYVKDGWNYPGDAFTQDA 430
Cdd:PRK06188 326 rkrdhDPDDPKRLTSCGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDgYWNRPEEtAEAFRDGWLHTGDVAREDE 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 431 DGYFFYQARDDDMIITAGYNVGGPEVEDALLRHPAVAECGVIGVPDEERGMVVKAVCVLKPGHTGDAAmvkTLQDHVKAT 510
Cdd:PRK06188 406 DGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRPGAAVDAA---ELQAHVKER 482
|
490 500 510
....*....|....*....|....*....|..
gi 496182614 511 IAPFKYPRVVEFVTALPRTETGKLQRFKLRQA 542
Cdd:PRK06188 483 KGSVHAPKQVDFVDSLPLTALGKPDKKALRAR 514
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
68-541 |
2.39e-58 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 203.44 E-value: 2.39e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 68 TYTYRDARTEAARIAEVLTQdHGLVPGNRVLLRGGNTVEMALAWLGTVYAGLIAVATMPLLRAGELANIIERAQPTLALC 147
Cdd:PRK06087 49 SYTYSALDHAASRLANWLLA-KGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 148 -----DGRLLAELAAAQDQHPVLTTIV------PFHTATDPADLLQRaqGKPGSmQPCPTSADDIALMAFTSGTTGAPKA 216
Cdd:PRK06087 128 ptlfkQTRPVDLILPLQNQLPQLQQIVgvdklaPATSSLSLSQIIAD--YEPLT-TAITTHGDELAAVLFTSGTEGLPKG 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 217 AVHTHRDVLAGCEAWPRhVLKATPDDIVAGSPPLAFTFGLGGLLVFPMWAGASVYFPDQpYTPETMVTLMRDAGVTISYT 296
Cdd:PRK06087 205 VMLTHNNILASERAYCA-RLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVLLDI-FTPDACLALLEQQRCTCMLG 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 297 APTFYRQMAPFAKKIG--LPQLRICVSAGEGLP-DATRQLWKdaTGIDMTDGIGATEMF-HIFISSAGGEARTGAI-GKV 371
Cdd:PRK06087 283 ATPFIYDLLNLLEKQPadLSALRFFLCGGTTIPkKVARECQQ--RGIKLLSVYGSTESSpHAVVNLDDPLSRFMHTdGYA 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 372 VPGYTAKVVDDDGNEVPRGTVGKLAVIGP---TGckYLDDP-RQAKYV-KDGWNYPGDAFTQDADGYFFYQARDDDMIIT 446
Cdd:PRK06087 361 AAGVEIKVVDEARKTLPPGCEGEEASRGPnvfMG--YLDEPeLTARALdEEGWYYSGDLCRMDEAGYIKITGRKKDIIVR 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 447 AGYNVGGPEVEDALLRHPAVAECGVIGVPDEERGMVVKAVCVLKPGHtgdaaMVKTLQDHV----KATIAPFKYPRVVEF 522
Cdd:PRK06087 439 GGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVVLKAPH-----HSLTLEEVVaffsRKRVAKYKYPEHIVV 513
|
490
....*....|....*....
gi 496182614 523 VTALPRTETGKLQRFKLRQ 541
Cdd:PRK06087 514 IDKLPRTASGKIQKFLLRK 532
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
39-534 |
1.20e-57 |
|
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: 202.42 E-value: 1.20e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 39 NLVHALFDQ--AERAERAGNIDRPLLRGPHRTYTYRDARTEAARIAEVLtQDHGLVPGNRVLLRGGNTVEMALAWLGTVY 116
Cdd:cd17634 53 NLAANALDRhlRENGDRTAIIYEGDDTSQSRTISYRELHREVCRFAGTL-LDLGVKKGDRVAIYMPMIPEAAVAMLACAR 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 117 AGLIAVATMPLLRAGELANIIERAQPTLALC------DGRLLAELAAAQDQ-----HPVLTTIVPFHTATD-----PADL 180
Cdd:cd17634 132 IGAVHSVIFGGFAPEAVAGRIIDSSSRLLITadggvrAGRSVPLKKNVDDAlnpnvTSVEHVIVLKRTGSDidwqeGRDL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 181 LQRAQ--GKPGSMQPCPTSADDIALMAFTSGTTGAPKAAVHTHRDVLAGCEAWPRHVLKATPDDIVAGSPPLAFTFGLGG 258
Cdd:cd17634 212 WWRDLiaKASPEHQPEAMNAEDPLFILYTSGTTGKPKGVLHTTGGYLVYAATTMKYVFDYGPGDIYWCTADVGWVTGHSY 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 259 LLVFPMWAGASVYF----PDQPyTPETMVTLMRDAGVTISYTAPTFYRQMAP----FAKKIGLPQLRICVSAGEGL-PDA 329
Cdd:cd17634 292 LLYGPLACGATTLLyegvPNWP-TPARMWQVVDKHGVNILYTAPTAIRALMAagddAIEGTDRSSLRILGSVGEPInPEA 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 330 TRQLWK--DATGIDMTDGIGATEMFHIFISSAGG--EARTGAIGKVVPGYTAKVVDDDGNEVPRGTVGKLAVIGP----T 401
Cdd:cd17634 371 YEWYWKkiGKEKCPVVDTWWQTETGGFMITPLPGaiELKAGSATRPVFGVQPAVVDNEGHPQPGGTEGNLVITDPwpgqT 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 402 GCKYLDDPR-QAKYVK--DGWNYPGDAFTQDADGYFFYQARDDDMIITAGYNVGGPEVEDALLRHPAVAECGVIGVPDEE 478
Cdd:cd17634 451 RTLFGDHERfEQTYFStfKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAI 530
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 496182614 479 RGMVVKAVCVLKPGHTGDAAMVKTLQDHVKATIAPFKYPRVVEFVTALPRTETGKL 534
Cdd:cd17634 531 KGQAPYAYVVLNHGVEPSPELYAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
48-545 |
8.45e-57 |
|
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: 198.83 E-value: 8.45e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 48 AERAERAGniDRPLLRGPHRTYTYRDARTEAARIAEVLtQDHGLVPGNRVLLRGGNTVEMALAWLGTVYAGLIAVATMPL 127
Cdd:COG1021 32 RRRAERHP--DRIAVVDGERRLSYAELDRRADRLAAGL-LALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAIPVFALPA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 128 LRAGELANIIERAQPTLALCDGRLL----AELAAA-QDQHPVLTTIVpfhTATDPADL--LQRAQGKPGSMQPCPTSADD 200
Cdd:COG1021 109 HRRAEISHFAEQSEAVAYIIPDRHRgfdyRALARElQAEVPSLRHVL---VVGDAGEFtsLDALLAAPADLSEPRPDPDD 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 201 IALMAFTSGTTGAPKAAVHTHRD----VLAGCEAWprhvlKATPDDIVAGSPPLAFTFGLG--GLL-VFpmWAGASVYFP 273
Cdd:COG1021 186 VAFFQLSGGTTGLPKLIPRTHDDylysVRASAEIC-----GLDADTVYLAALPAAHNFPLSspGVLgVL--YAGGTVVLA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 274 DQPYtPETMVTLMRDAGVTISYTAPTFYRQMAPFAKKIG--LPQLRICVSAGEGLPDAtrqlwkDATGIDMTDGIGATEM 351
Cdd:COG1021 259 PDPS-PDTAFPLIERERVTVTALVPPLALLWLDAAERSRydLSSLRVLQVGGAKLSPE------LARRVRPALGCTLQQV 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 352 FhifiSSAGG-----------EARTGAIGK-VVPGYTAKVVDDDGNEVPRGTVGKLAVIGP-TGCKYLDDPR--QAKYVK 416
Cdd:COG1021 332 F----GMAEGlvnytrlddpeEVILTTQGRpISPDDEVRIVDEDGNPVPPGEVGELLTRGPyTIRGYYRAPEhnARAFTP 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 417 DGWNYPGDAFTQDADGYFFYQARDDDMIITAGYNVGGPEVEDALLRHPAVAECGVIGVPDEERGMVVKAVCVLKpghtGD 496
Cdd:COG1021 408 DGFYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGERSCAFVVPR----GE 483
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 496182614 497 AAMVKTLQDHVKAT-IAPFKYPRVVEFVTALPRTETGKLQRFKLRQAAAT 545
Cdd:COG1021 484 PLTLAELRRFLRERgLAAFKLPDRLEFVDALPLTAVGKIDKKALRAALAA 533
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
58-539 |
9.96e-56 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 195.08 E-value: 9.96e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 58 DRPLLRGPHRTYTYRDARTEAARIAEVLTQDHGLVPGNRVLLRGGNTVEMALAWLGTVYAGLIAVATMPLLRAGELANII 137
Cdd:PRK06839 17 DRIAIITEEEEMTYKQLHEYVSKVAAYLIYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 138 ERAQPTLALCDgrllAELAAAQDQHPVLTTIVPFHTATDPADLLQRaqgKPGSMQPcpTSADDIALMAFTSGTTGAPKAA 217
Cdd:PRK06839 97 KDSGTTVLFVE----KTFQNMALSMQKVSYVQRVISITSLKEIEDR---KIDNFVE--KNESASFIICYTSGTTGKPKGA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 218 VHTHRDVLagceaWPR----HVLKATPDDIVAGSPPLaFTFGLGGLLVFPMW-AGASVYFPDQpYTPETMVTLMRDAGVT 292
Cdd:PRK06839 168 VLTQENMF-----WNAlnntFAIDLTMHDRSIVLLPL-FHIGGIGLFAFPTLfAGGVIIVPRK-FEPTKALSMIEKHKVT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 293 ISYTAPTFYRQM--APFAKKIGLPQLRICVSAGEGLPDATRQLWKDaTGIDMTDGIGATEMF-HIFISSAGGEAR-TGAI 368
Cdd:PRK06839 241 VVMGVPTIHQALinCSKFETTNLQSVRWFYNGGAPCPEELMREFID-RGFLFGQGFGMTETSpTVFMLSEEDARRkVGSI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 369 GKVVPGYTAKVVDDDGNEVPRGTVGKLAVIGPTGCK-YLDDPRQ-AKYVKDGWNYPGDAFTQDADGYFFYQARDDDMIIT 446
Cdd:PRK06839 320 GKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKeYWNRPDAtEETIQDGWLCTGDLARVDEDGFVYIVGRKKEMIIS 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 447 AGYNVGGPEVEDALLRHPAVAECGVIGVPDEERGMVVKAVCVLKPGHTgdaAMVKTLQDHVKATIAPFKYPRVVEFVTAL 526
Cdd:PRK06839 400 GGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSV---LIEKDVIEHCRLFLAKYKIPKEIVFLKEL 476
|
490
....*....|...
gi 496182614 527 PRTETGKLQRFKL 539
Cdd:PRK06839 477 PKNATGKIQKAQL 489
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
70-536 |
2.84e-55 |
|
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: 192.31 E-value: 2.84e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 70 TYRDARTEAARIAEVLtQDHGLVPGNRVLLRGGNTVEMALAWLGTVYAGLIAVATMPLLRAGELANIIERAQPTLALcdg 149
Cdd:cd05935 3 TYLELLEVVKKLASFL-SNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAV--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 150 rLLAELaaaqdqhpvlttivpfhtatdpadllqraqgkpgsmqpcptsaDDIALMAFTSGTTGAPKAAVHTHRDVLAGCE 229
Cdd:cd05935 79 -VGSEL-------------------------------------------DDLALIPYTSGTTGLPKGCMHTHFSAAANAL 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 230 AwPRHVLKATPDDIVAGSPPLAFTFGLGGLLVFPMWAGASVYFPDQpYTPETMVTLMRDAGVTISYTAPTFYRQM--APF 307
Cdd:cd05935 115 Q-SAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMAR-WDRETALELIEKYKVTFWTNIPTMLVDLlaTPE 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 308 AKKIGLPQLRICVSAGEGLPDATRQLWKDATGIDMTDGIGATEMFHIFISSAGGEARTGAIGKVVPGYTAKVVD-DDGNE 386
Cdd:cd05935 193 FKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTETMSQTHTNPPLRPKLQCLGIP*FGVDARVIDiETGRE 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 387 VPRGTVGKLAVIGPTGCK-YLDDPR---QAKYVKDGWNY--PGDAFTQDADGYFFYQARDDDMIITAGYNVGGPEVEDAL 460
Cdd:cd05935 273 LPPNEVGEIVVRGPQIFKgYWNRPEeteESFIEIKGRRFfrTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKL 352
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496182614 461 LRHPAVAECGVIGVPDEERGMVVKAVCVLKPGHTGDAamvkTLQD---HVKATIAPFKYPRVVEFVTALPRTETGKLQR 536
Cdd:cd05935 353 YKHPAI*EVCVISVPDERVGEEVKAFIVLRPEYRGKV----TEEDiieWAREQMAAYKYPREVEFVDELPRSASGKILW 427
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
67-544 |
2.06e-54 |
|
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: 193.93 E-value: 2.06e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 67 RTYTYRDARTEAARIAEVLTqDHGLVPGNRVLLRGGNTVEMALAWLG---------TVYAGLIAVAtmpllrageLANII 137
Cdd:cd05966 83 RTITYRELLREVCRFANVLK-SLGVKKGDRVAIYMPMIPELVIAMLAcarigavhsVVFAGFSAES---------LADRI 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 138 ERAQPTLAL-CDGRL-------LAELA--AAQDQHPVLTTIVPFHTATDPA----------DLLQRAqgkPGSMQPCPTS 197
Cdd:cd05966 153 NDAQCKLVItADGGYrggkvipLKEIVdeALEKCPSVEKVLVVKRTGGEVPmtegrdlwwhDLMAKQ---SPECEPEWMD 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 198 ADDIALMAFTSGTTGAPKAAVHTHRDVLAGCEAWPRHVLKATPDDI---------VAGSpplafTFGLGGllvfPMWAGA 268
Cdd:cd05966 230 SEDPLFILYTSGSTGKPKGVVHTTGGYLLYAATTFKYVFDYHPDDIywctadigwITGH-----SYIVYG----PLANGA 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 269 -SVYF---PDQPyTPETMVTLMRDAGVTISYTAPT----FYRQMAPFAKKIGLPQLRICVSAGEGL-PDATRQLWKDATG 339
Cdd:cd05966 301 tTVMFegtPTYP-DPGRYWDIVEKHKVTIFYTAPTairaLMKFGDEWVKKHDLSSLRVLGSVGEPInPEAWMWYYEVIGK 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 340 --IDMTDGIGATEMFHIFISSAGGEART--GAIGKVVPGYTAKVVDDDGNEVPRGTVGKLAVIGP------TgcKYLDDP 409
Cdd:cd05966 380 erCPIVDTWWQTETGGIMITPLPGATPLkpGSATRPFFGIEPAILDEEGNEVEGEVEGYLVIKRPwpgmarT--IYGDHE 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 410 RqakYVKDGWN-YPGDAFT-----QDADGYFFYQARDDDMIITAGYNVGGPEVEDALLRHPAVAECGVIGVPDEERGMVV 483
Cdd:cd05966 458 R---YEDTYFSkFPGYYFTgdgarRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAI 534
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496182614 484 KAVCVLKPGHTGDAAMVKTLQDHVKATIAPFKYPRVVEFVTALPRTETGKLQRFKLRQAAA 544
Cdd:cd05966 535 YAFVTLKDGEEPSDELRKELRKHVRKEIGPIATPDKIQFVPGLPKTRSGKIMRRILRKIAA 595
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
64-541 |
1.13e-53 |
|
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: 190.15 E-value: 1.13e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 64 GPHRTYTYRDARTEAARIAEVLtQDHGLVPGNRVLLRGGNTVEMALAWLGTVYAGLIAVATMPLLRAGELANIIERAQPT 143
Cdd:cd12119 21 GEVHRYTYAEVAERARRLANAL-RRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAEDR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 144 LALCDGRLLAELAAAQDQHPVLTTIVPFHTATDPA-----------DLLqrAQGKPGSMQPcptSAD--DIALMAFTSGT 210
Cdd:cd12119 100 VVFVDRDFLPLLEAIAPRLPTVEHVVVMTDDAAMPepagvgvlayeELL--AAESPEYDWP---DFDenTAAAICYTSGT 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 211 TGAPKAAVHTHRD-VLagceawprHVLKATPDDivagspplafTFGLGG----LLVFPM-------------WAGASVYF 272
Cdd:cd12119 175 TGNPKGVVYSHRSlVL--------HAMAALLTD----------GLGLSEsdvvLPVVPMfhvnawglpyaaaMVGAKLVL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 273 PDQPYTPETMVTLMRDAGVTISYTAPTFYRQMAPF--AKKIGLPQLRICVSAGEGLPDATRQLWKDAtGIDMTDGIGATE 350
Cdd:cd12119 237 PGPYLDPASLAELIEREGVTFAAGVPTVWQGLLDHleANGRDLSSLRRVVIGGSAVPRSLIEAFEER-GVRVIHAWGMTE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 351 M-----------FHIFISSAGGEARTGAIGKVVPGYTAKVVDDDGNEVPR--GTVGKLAVIGP--TGCKYLDDPRQAKYV 415
Cdd:cd12119 316 TsplgtvarppsEHSNLSEDEQLALRAKQGRPVPGVELRIVDDDGRELPWdgKAVGELQVRGPwvTKSYYKNDEESEALT 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 416 KDGWNYPGDAFTQDADGYFFYQARDDDMIITAGYNVGGPEVEDALLRHPAVAECGVIGVPDE---ERGMvvkAVCVLKPG 492
Cdd:cd12119 396 EDGWLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPkwgERPL---AVVVLKEG 472
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 496182614 493 HTGDAamvKTLQDHVKATIAPFKYPRVVEFVTALPRTETGKLQRFKLRQ 541
Cdd:cd12119 473 ATVTA---EELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKALRE 518
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
58-543 |
2.33e-53 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 190.03 E-value: 2.33e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 58 DRPLLRGPHRTYTYRDARTEAARIAEVLTQDHGLVPGNRVLLRGGNTVEMALAWLGTVYAGLIAVATMPLLRAGELA--- 134
Cdd:PRK12492 39 DRPAFSNLGVTLSYAELERHSAAFAAYLQQHTDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVNTNPLYTAREMRhqf 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 135 -----------NII-ERAQPTLALCDGRLLAElAAAQDQHPVL-----TTIVPFHTATDPADLLQRA--------QGKPG 189
Cdd:PRK12492 119 kdsgaralvylNMFgKLVQEVLPDTGIEYLIE-AKMGDLLPAAkgwlvNTVVDKVKKMVPAYHLPQAvpfkqalrQGRGL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 190 SMQPCPTSADDIALMAFTSGTTGAPKAAVHTHRDVLAGCEAWPRHVLKATPD---------DIVAGSPPLAFTFGLGGLL 260
Cdd:PRK12492 198 SLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVRACLSQLGPDgqplmkegqEVMIAPLPLYHIYAFTANC 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 261 VFPMWAGasvyfpdqpyTPETMVTLMRDAGVTIS------YTA-----PTFYRQMA-PFAKKIGLPQLRICVSAGEGLPD 328
Cdd:PRK12492 278 MCMMVSG----------NHNVLITNPRDIPGFIKelgkwrFSAllglnTLFVALMDhPGFKDLDFSALKLTNSGGTALVK 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 329 ATRQLWKDATGIDMTDGIGATEMFHIFISSAGGE-ARTGAIGKVVPGYTAKVVDDDGNEVPRGTVGKLAVIGPTGCK-YL 406
Cdd:PRK12492 348 ATAERWEQLTGCTIVEGYGLTETSPVASTNPYGElARLGTVGIPVPGTALKVIDDDGNELPLGERGELCIKGPQVMKgYW 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 407 DDPRQAKYVKD--GWNYPGDAFTQDADGYFFYQARDDDMIITAGYNVGGPEVEDALLRHPAVAECGVIGVPDEERGMVVK 484
Cdd:PRK12492 428 QQPEATAEALDaeGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVK 507
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 496182614 485 AVCVLKPGhtgdAAMVKTLQDHVKATIAPFKYPRVVEFVTALPRTETGKLQRFKLRQAA 543
Cdd:PRK12492 508 LFVVARDP----GLSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRRELRDIA 562
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
199-540 |
3.74e-53 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 184.02 E-value: 3.74e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 199 DDIALMAFTSGTTGAPKAAVHTHRDVL-----AGceawprHVLKATPDDIVAGSPPLAFTFGL-GGLLVFPMWaGASVYF 272
Cdd:cd05917 2 DDVINIQFTSGTTGSPKGATLTHHNIVnngyfIG------ERLGLTEQDRLCIPVPLFHCFGSvLGVLACLTH-GATMVF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 273 PDQPYTPETMVTLMRDAGVTISYTAPTFYRQM--APFAKKIGLPQLRICVSAGEGLPDAT-RQLWKDATGIDMTDGIGAT 349
Cdd:cd05917 75 PSPSFDPLAVLEAIEKEKCTALHGVPTMFIAEleHPDFDKFDLSSLRTGIMAGAPCPPELmKRVIEVMNMKDVTIAYGMT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 350 EMFH-IFISSAGG--EARTGAIGKVVPGYTAKVVDDDGNEVP-RGTVGKLAVIGPTGCK-YLDDPRQAKYV--KDGWNYP 422
Cdd:cd05917 155 ETSPvSTQTRTDDsiEKRVNTVGRIMPHTEAKIVDPEGGIVPpVGVPGELCIRGYSVMKgYWNDPEKTAEAidGDGWLHT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 423 GDAFTQDADGYFFYQARDDDMIITAGYNVGGPEVEDALLRHPAVAECGVIGVPDEERGMVVKAVCVLKPGHTGDAAMVKt 502
Cdd:cd05917 235 GDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLKEGAELTEEDIK- 313
|
330 340 350
....*....|....*....|....*....|....*...
gi 496182614 503 lqDHVKATIAPFKYPRVVEFVTALPRTETGKLQRFKLR 540
Cdd:cd05917 314 --AYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
50-543 |
3.88e-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: 190.60 E-value: 3.88e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 50 RAERAGNIDRPLLRGPHRTYTYRDARTEAARIAEVLtQDHGLVPGNRVLLRGGNTVEMALAWLGTVYAGLIAVATMPLLR 129
Cdd:cd05967 64 RGDQIALIYDSPVTGTERTYTYAELLDEVSRLAGVL-RKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGFA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 130 AGELANIIERAQPTLALCD------GRL-----LAELAAAQDQHPVLTTIV---------PFHTATDP--ADLLQRAQgk 187
Cdd:cd05967 143 AKELASRIDDAKPKLIVTAscgiepGKVvpykpLLDKALELSGHKPHHVLVlnrpqvpadLTKPGRDLdwSELLAKAE-- 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 188 pgSMQPCPTSADDIALMAFTSGTTGAPKAAVhthRDVLAGCEA--WP-RHVLKATPDDIVAGSPPLAFTFGLGGLLVFPM 264
Cdd:cd05967 221 --PVDCVPVAATDPLYILYTSGTTGKPKGVV---RDNGGHAVAlnWSmRNIYGIKPGDVWWAASDVGWVVGHSYIVYGPL 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 265 WAGA-SVYFPDQP-YTPETMV--TLMRDAGVTISYTAPTFYRQM------APFAKKIGLPQLRICVSAGEGLPDATRQLW 334
Cdd:cd05967 296 LHGAtTVLYEGKPvGTPDPGAfwRVIEKYQVNALFTAPTAIRAIrkedpdGKYIKKYDLSSLRTLFLAGERLDPPTLEWA 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 335 KDATGIDMTDGIGATEMFHIFISSAGGEA----RTGAIGKVVPGYTAKVVDDDGNEVPRGTVGKLAVIGPT--GCK---Y 405
Cdd:cd05967 376 ENTLGVPVIDHWWQTETGWPITANPVGLEplpiKAGSPGKPVPGYQVQVLDEDGEPVGPNELGNIVIKLPLppGCLltlW 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 406 LDDPRqakYVKDGWN-YPG-----DAFTQDADGYFFYQARDDDMIITAGYNVGGPEVEDALLRHPAVAECGVIGVPDEER 479
Cdd:cd05967 456 KNDER---FKKLYLSkFPGyydtgDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELK 532
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496182614 480 GMVVKAVCVLKPGHTGDAA-MVKTLQDHVKATIAPFKYPRVVEFVTALPRTETGKLQRFKLRQAA 543
Cdd:cd05967 533 GQVPLGLVVLKEGVKITAEeLEKELVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTLRKIA 597
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
69-544 |
3.04e-51 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 184.21 E-value: 3.04e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 69 YTYRDARTEAARIAEVLTQdHGLVPGNRVLLRGGNTVEMALAWLGTVYAGLIAVATMPLLRAGELANIIERAQPTLALCD 148
Cdd:PRK12583 46 YTWRQLADAVDRLARGLLA-LGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWVICA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 149 ------------GRLLAELAAAQ------DQHPVLTTIVPFHTATDP-----ADLLQRAQGKpgSMQPCPT-----SADD 200
Cdd:PRK12583 125 dafktsdyhamlQELLPGLAEGQpgalacERLPELRGVVSLAPAPPPgflawHELQARGETV--SREALAErqaslDRDD 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 201 IALMAFTSGTTGAPKAAVHTHRDVLAgcEAW-PRHVLKATPDDIVAGSPPLAFTFGLGGLLVFPMWAGASVYFPDQPYTP 279
Cdd:PRK12583 203 PINIQYTSGTTGFPKGATLSHHNILN--NGYfVAESLGLTEHDRLCVPVPLYHCFGMVLANLGCMTVGACLVYPNEAFDP 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 280 ETMVTLMRDAGVTISYTAPT-FYRQMA-PFAKKIGLPQLRICVSAGEGLP-DATRQLWKDATGIDMTDGIGATEMFHIFI 356
Cdd:PRK12583 281 LATLQAVEEERCTALYGVPTmFIAELDhPQRGNFDLSSLRTGIMAGAPCPiEVMRRVMDEMHMAEVQIAYGMTETSPVSL 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 357 SSAGG---EARTGAIGKVVPGYTAKVVDDDGNEVPRGTVGKLAVIGPTGCK--YLDDPRQAKYV-KDGWNYPGDAFTQDA 430
Cdd:PRK12583 361 QTTAAddlERRVETVGRTQPHLEVKVVDPDGATVPRGEIGELCTRGYSVMKgyWNNPEATAESIdEDGWMHTGDLATMDE 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 431 DGYFFYQARDDDMIITAGYNVGGPEVEDALLRHPAVAECGVIGVPDEERGMVVKAVCVLKPGHtgdAAMVKTLQDHVKAT 510
Cdd:PRK12583 441 QGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRLHPGH---AASEEELREFCKAR 517
|
490 500 510
....*....|....*....|....*....|....
gi 496182614 511 IAPFKYPRVVEFVTALPRTETGKLQRFKLRQAAA 544
Cdd:PRK12583 518 IAHFKVPRYFRFVDEFPMTVTGKVQKFRMREISI 551
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
195-543 |
3.34e-51 |
|
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: 182.53 E-value: 3.34e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 195 PTSADDIALMAFTSGTTGAPKAAVHTHRDVLAGCEAWPRHVlKATPDDIVAGSPPLAFTFGLGGLLVFPMWAGASVYFPD 274
Cdd:cd05909 143 PVQPDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIF-DPNPEDVVFGALPFFHSFGLTGCLWLPLLSGIKVVFHP 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 275 QPYTPETMVTLMRDAGVTISYTAPTFYRQMAPFAKKIGLPQLRICVSAGEGLPDATRQLWKDATGIDMTDGIGATEMFH- 353
Cdd:cd05909 222 NPLDYKKIPELIYDKKATILLGTPTFLRGYARAAHPEDFSSLRLVVAGAEKLKDTLRQEFQEKFGIRILEGYGTTECSPv 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 354 IFISSAGGEARTGAIGKVVPGYTAKVVD-DDGNEVPRGTVGKLAVIGPTGCK-YL--DDPRQAKYVkDGWNYPGDAFTQD 429
Cdd:cd05909 302 ISVNTPQSPNKEGTVGRPLPGMEVKIVSvETHEEVPIGEGGLLLVRGPNVMLgYLnePELTSFAFG-DGWYDTGDIGKID 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 430 ADGYFFYQARDDDMIITAGYNVGGPEVEDALLRH-PAVAECGVIGVPDEERGMVVKAVcvlkpgHTGDAAMVKTLQDHVK 508
Cdd:cd05909 381 GEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVPDGRKGEKIVLL------TTTTDTDPSSLNDILK 454
|
330 340 350
....*....|....*....|....*....|....*.
gi 496182614 509 ATIAPFKY-PRVVEFVTALPRTETGKLQRFKLRQAA 543
Cdd:cd05909 455 NAGISNLAkPSYIHQVEEIPLLGTGKPDYVTLKALA 490
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
67-542 |
4.10e-51 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 182.80 E-value: 4.10e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 67 RTYTYRDARTEAARIAEVLtQDHGLVPGNRVLLRGGNTVEMALAWLGTVYAGLIAVATMPLLRAGELANIIERAQPTLAL 146
Cdd:PRK08276 10 EVVTYGELEARSNRLAHGL-RALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVLI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 147 CDGRLLAELAAAQD--QHPVLTTIVPFHTATDPADLLQRAQGKPGSMQPCPTSADDialMAFTSGTTGAPKAAVH--THR 222
Cdd:PRK08276 89 VSAALADTAAELAAelPAGVPLLLVVAGPVPGFRSYEEALAAQPDTPIADETAGAD---MLYSSGTTGRPKGIKRplPGL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 223 DVLAGCEAWPRHVL---KATPDDIVAGSPPLAFTfglgGLLVFPMWA----GASVYFPDqpYTPETMVTLMRDAGVTISY 295
Cdd:PRK08276 166 DPDEAPGMMLALLGfgmYGGPDSVYLSPAPLYHT----APLRFGMSAlalgGTVVVMEK--FDAEEALALIERYRVTHSQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 296 TAPTFYRQMapfakkIGLPQ----------LRICVSAGEGLPDATRQLWKDATG--ID----MTDGIGATemfhiFISSA 359
Cdd:PRK08276 240 LVPTMFVRM------LKLPEevrarydvssLRVAIHAAAPCPVEVKRAMIDWWGpiIHeyyaSSEGGGVT-----VITSE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 360 GGEARTGAIGKVVPGyTAKVVDDDGNEVPRGTVGKLAVIGPTGC-KYLDDP--RQAKYVKDGWNYPGDAFTQDADGYFFY 436
Cdd:PRK08276 309 DWLAHPGSVGKAVLG-EVRILDEDGNELPPGEIGTVYFEMDGYPfEYHNDPekTAAARNPHGWVTVGDVGYLDEDGYLYL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 437 QARDDDMIITAGYNVGGPEVEDALLRHPAVAECGVIGVPDEERGMVVKAVCVLKPGHTGDAAMVKTLQDHVKATIAPFKY 516
Cdd:PRK08276 388 TDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKAVVQPADGADAGDALAAELIAWLRGRLAHYKC 467
|
490 500
....*....|....*....|....*.
gi 496182614 517 PRVVEFVTALPRTETGKLQRFKLRQA 542
Cdd:PRK08276 468 PRSIDFEDELPRTPTGKLYKRRLRDR 493
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
17-541 |
6.08e-51 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 183.66 E-value: 6.08e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 17 PPQSAW---PTLRYDLP----ELQIPDQAnLVHaLFDQAerAERAGniDRPLLRGPHRTYTYRDARTEAARIAEVLtQDH 89
Cdd:PRK05605 5 QEMSAFadkPWLQSYAPwtphDLDYGDTT-LVD-LYDNA--VARFG--DRPALDFFGATTTYAELGKQVRRAAAGL-RAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 90 GLVPGNRVLLRGGNTVEMALAWLGTVYAGLIAVATMPLLRAGEL------------------ANIIER------------ 139
Cdd:PRK05605 78 GVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVEHNPLYTAHELehpfedhgarvaivwdkvAPTVERlrrttpletivs 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 140 -----AQPT---LALcdgRL-LAELAAAQDQ-HPVLTTIVPFHTatdpadLLQRAQGKPGSMQPCPT-SADDIALMAFTS 208
Cdd:PRK05605 158 vnmiaAMPLlqrLAL---RLpIPALRKARAAlTGPAPGTVPWET------LVDAAIGGDGSDVSHPRpTPDDVALILYTS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 209 GTTGAPKAAVHTHRDVLAGC---EAWprhvLKATPDD--IVAGSPPLAFTFGLGGLLVFPMWAGAS-VYFPdQPYTPETM 282
Cdd:PRK05605 229 GTTGKPKGAQLTHRNLFANAaqgKAW----VPGLGDGpeRVLAALPMFHAYGLTLCLTLAVSIGGElVLLP-APDIDLIL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 283 vTLMRDAGVTISYTAPTFYRQMAPFAKK--IGLPQLRICVSAGEGLPDATRQLWKDATGIDMTDGIGATEMFHIFISS-A 359
Cdd:PRK05605 304 -DAMKKHPPTWLPGVPPLYEKIAEAAEErgVDLSGVRNAFSGAMALPVSTVELWEKLTGGLLVEGYGLTETSPIIVGNpM 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 360 GGEARTGAIGKVVPGYTAKVVD--DDGNEVPRGTVGKLAVIGPTGCK-YLDDPRQ-AKYVKDGWNYPGDAFTQDADGYFF 435
Cdd:PRK05605 383 SDDRRPGYVGVPFPDTEVRIVDpeDPDETMPDGEEGELLVRGPQVFKgYWNRPEEtAKSFLDGWFRTGDVVVMEEDGFIR 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 436 YQARDDDMIITAGYNVGGPEVEDALLRHPAVAECGVIGVPDEERGMVVKAVCVLKPGHTGDAAmvkTLQDHVKATIAPFK 515
Cdd:PRK05605 463 IVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEPGAALDPE---GLRAYCREHLTRYK 539
|
570 580
....*....|....*....|....*.
gi 496182614 516 YPRVVEFVTALPRTETGKLQRFKLRQ 541
Cdd:PRK05605 540 VPRRFYHVDELPRDQLGKVRRREVRE 565
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
67-544 |
6.42e-51 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 183.70 E-value: 6.42e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 67 RTYTYRDARTEAARIAEVLTQdHGLVPGNRVLLRGGNTVEMALAWLGTVYAGLIAVATMPLLRAGELANIIERAQPTLAL 146
Cdd:PRK06178 57 HVITYAELDELSDRFAALLRQ-RGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 147 CDGRLLAELAAAQDQHPVLTTIVPFHTATDPA---------------------DLLQRAQGKPGSMQPCPTSADDIALMA 205
Cdd:PRK06178 136 ALDQLAPVVEQVRAETSLRHVIVTSLADVLPAeptlplpdslraprlaaagaiDLLPALRACTAPVPLPPPALDALAALN 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 206 FTSGTTGAPKAAVHTHRDVLAGCEAWPRHVLKATPDDIVAGSPPLAFTFGLGGLLVFPMWAGASVYFPDQpYTPETMVTL 285
Cdd:PRK06178 216 YTGGTTGMPKGCEHTQRDMVYTAAAAYAVAVVGGEDSVFLSFLPEFWIAGENFGLLFPLFSGATLVLLAR-WDAVAFMAA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 286 MRDAGVTI-SYTAPTFYRQMA-PFAKKIGLPQLRI--CVSAGEGLPDATRQLWKDATGIDMTDGI-GATEMFHIFISSAG 360
Cdd:PRK06178 295 VERYRVTRtVMLVDNAVELMDhPRFAEYDLSSLRQvrVVSFVKKLNPDYRQRWRALTGSVLAEAAwGMTETHTCDTFTAG 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 361 GE-------ARTGAIGKVVPGYTAKVVD-DDGNEVPRGTVGKLAVIGPTGCK-YLDDPR-QAKYVKDGWNYPGDAFTQDA 430
Cdd:PRK06178 375 FQdddfdllSQPVFVGLPVPGTEFKICDfETGELLPLGAEGEIVVRTPSLLKgYWNKPEaTAEALRDGWLHTGDIGKIDE 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 431 DGYFFYQARDDDMIITAGYNVGGPEVEDALLRHPAVAECGVIGVPDEERGMVVKAVCVLKPGHTGDAAmvkTLQDHVKAT 510
Cdd:PRK06178 455 QGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPGADLTAA---ALQAWCREN 531
|
490 500 510
....*....|....*....|....*....|....
gi 496182614 511 IAPFKYPrVVEFVTALPRTETGKLQRFKLRQAAA 544
Cdd:PRK06178 532 MAVYKVP-EIRIVDALPMTATGKVRKQDLQALAE 564
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
58-545 |
1.78e-50 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 182.38 E-value: 1.78e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 58 DRPLLRGPHRTYTYRDARTEAARIAEVLTQDHGLVPGNRVLLRGGNTVEMALAWLGTVYAGLIAVATMPLLRAGELAN-I 136
Cdd:PRK08751 40 DRPAYHSFGKTITYREADQLVEQFAAYLLGELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHqL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 137 IERAQPTLALCD--GRLLAELAAAQDQHPVLTT-----------------------IVPFHTATDPADLLQR-AQGKPGS 190
Cdd:PRK08751 120 IDSGASVLVVIDnfGTTVQQVIADTPVKQVITTglgdmlgfpkaalvnfvvkyvkkLVPEYRINGAIRFREAlALGRKHS 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 191 MQPCPTSADDIALMAFTSGTTGAPKAAVHTHRDVLAGCE---AWPRHVLKATP-DDIVAGSPPLAFTFGL-GGLLVFpMW 265
Cdd:PRK08751 200 MPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQqahQWLAGTGKLEEgCEVVITALPLYHIFALtANGLVF-MK 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 266 AGASVYFPDQPYTPETMVTLMRDAGVTISYTAPTFYRQM--APFAKKIGLPQLRICVSAGEGLPDATRQLWKDATGIDMT 343
Cdd:PRK08751 279 IGGCNHLISNPRDMPGFVKELKKTRFTAFTGVNTLFNGLlnTPGFDQIDFSSLKMTLGGGMAVQRSVAERWKQVTGLTLV 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 344 DGIGATEMF-HIFISSAGGEARTGAIGKVVPGYTAKVVDDDGNEVPRGTVGKLAVIGPTGCK-YLDDPRQAKYVKD--GW 419
Cdd:PRK08751 359 EAYGLTETSpAACINPLTLKEYNGSIGLPIPSTDACIKDDAGTVLAIGEIGELCIKGPQVMKgYWKRPEETAKVMDadGW 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 420 NYPGDAFTQDADGYFFYQARDDDMIITAGYNVGGPEVEDALLRHPAVAECGVIGVPDEERGMVVKAVCVLK-PGHTgdAA 498
Cdd:PRK08751 439 LHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEIVKVVIVKKdPALT--AE 516
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 496182614 499 MVKTlqdHVKATIAPFKYPRVVEFVTALPRTETGKLQRFKLRQAAAT 545
Cdd:PRK08751 517 DVKA---HARANLTGYKQPRIIEFRKELPKTNVGKILRRELRDAAKA 560
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
58-548 |
1.91e-50 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 181.90 E-value: 1.91e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 58 DRPLLRGPHRTYTYRDARTEAARIAEVLTQdHGLVPGNRVLLRGGNTVEMALAWLGTVYAGLIAVATMPLLRAGELANII 137
Cdd:PRK07786 32 DAPALRFLGNTTTWRELDDRVAALAGALSR-RGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 138 ERAQPTLALCDGRLLAELAAAQDQHPVLTTIVPFHTATDPADL----LQRAQGKPgsMQPCPTSADDIALMAFTSGTTGA 213
Cdd:PRK07786 111 SDCGAHVVVTEAALAPVATAVRDIVPLLSTVVVAGGSSDDSVLgyedLLAEAGPA--HAPVDIPNDSPALIMYTSGTTGR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 214 PKAAVHTHRDVLAGCEAWPRHVLKATPDDIVAGSPPLAFTFGLGGLLVFPMWAGASVYFPDQPYTPETMVTLMRDAGVTI 293
Cdd:PRK07786 189 PKGAVLTHANLTGQAMTCLRTNGADINSDVGFVGVPLFHIAGIGSMLPGLLLGAPTVIYPLGAFDPGQLLDVLEAEKVTG 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 294 SYTAPTFYRQM--APFAKKIGLPQLRICVSAGEGLPDATRQLWKDATGIDMTDGIGATEMFHIFISSAGGEA--RTGAIG 369
Cdd:PRK07786 269 IFLVPAQWQAVcaEQQARPRDLALRVLSWGAAPASDTLLRQMAATFPEAQILAAFGQTEMSPVTCMLLGEDAirKLGSVG 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 370 KVVPGYTAKVVDDDGNEVPRGTVGKLAVIGPTGCK-YLDDPR-QAKYVKDGWNYPGDAFTQDADGYFFYQARDDDMIITA 447
Cdd:PRK07786 349 KVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSgYWNNPEaTAEAFAGGWFHSGDLVRQDEEGYVWVVDRKKDMIISG 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 448 GYNVGGPEVEDALLRHPAVAECGVIGVPDEERGMVVKAVCVLKPGhtGDAAMVKTLQDHVKATIAPFKYPRVVEFVTALP 527
Cdd:PRK07786 429 GENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRND--DAALTLEDLAEFLTDRLARYKHPKALEIVDALP 506
|
490 500
....*....|....*....|.
gi 496182614 528 RTETGKLQRFKLRQAAATPQA 548
Cdd:PRK07786 507 RNPAGKVLKTELRERYGACVN 527
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
87-540 |
1.28e-49 |
|
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: 177.63 E-value: 1.28e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 87 QDHGLVPGNRVLLRGGNTVEMALAWLGTVYAG----LIAVATMPLLRAGELANIIERAQPTLALCDGRLLAELAAAQDQH 162
Cdd:cd05922 11 LEAGGVRGERVVLILPNRFTYIELSFAVAYAGgrlgLVFVPLNPTLKESVLRYLVADAGGRIVLADAGAADRLRDALPAS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 163 PVLTTIVpfhtatDPADLLQRAQGKPGSmqpcPTSADDIALMAFTSGTTGAPKAAVHTHRDVLAGCEAWpRHVLKATPDD 242
Cdd:cd05922 91 PDPGTVL------DADGIRAARASAPAH----EVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSI-AEYLGITADD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 243 IVAGSPPLAFTFGLGGLLVfPMWAGASVYFPDQPYTPETMVTLMRDAGVTISYTAPTFYRQMAPFA-KKIGLPQLRICVS 321
Cdd:cd05922 160 RALTVLPLSYDYGLSVLNT-HLLRGATLVLTNDGVLDDAFWEDLREHGATGLAGVPSTYAMLTRLGfDPAKLPSLRYLTQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 322 AGEGLPDAT-RQLWKDATGIDMTDGIGATEMFHI--FISSAGGEARTGAIGKVVPGYTAKVVDDDGNEVPRGTVGKLAVI 398
Cdd:cd05922 239 AGGRLPQETiARLRELLPGAQVYVMYGQTEATRRmtYLPPERILEKPGSIGLAIPGGEFEILDDDGTPTPPGEPGEIVHR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 399 GPTGCK-YLDDP--RQAKYVKDGWNYPGDAFTQDADGYFFYQARDDDMIITAGYNVGGPEVEDALLRHPAVAECGVIGVP 475
Cdd:cd05922 319 GPNVMKgYWNDPpyRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLP 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496182614 476 DEErGMVVKAVCVLKPGHTGDAAMvktlqDHVKATIAPFKYPRVVEFVTALPRTETGKLQRFKLR 540
Cdd:cd05922 399 DPL-GEKLALFVTAPDKIDPKDVL-----RSLAERLPPYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
70-536 |
2.40e-49 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 179.07 E-value: 2.40e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 70 TYRDARTEAARIAEVLtQDHGLVPGNRVLLRGGNTVEMALAWLGTVYAGLIAVATMPLLRAGELANIIERAQPTLALCDG 149
Cdd:PRK06710 51 TFSVFHDKVKRFANYL-QKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILCLD 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 150 RLLAELAAAQD----QHPVLTTI---VPFhtatdPADLL----QRAQGK----------------------PGSMQPCPT 196
Cdd:PRK06710 130 LVFPRVTNVQSatkiEHVIVTRIadfLPF-----PKNLLypfvQKKQSNlvvkvsesetihlwnsvekevnTGVEVPCDP 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 197 SaDDIALMAFTSGTTGAPKAAVHTHRDV----LAGCEaWPRHVLKAtpDDIVAGSPPLAFTFGLGGLLVFPMWAGAS-VY 271
Cdd:PRK06710 205 E-NDLALLQYTGGTTGFPKGVMLTHKNLvsntLMGVQ-WLYNCKEG--EEVVLGVLPFFHVYGMTAVMNLSIMQGYKmVL 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 272 FPDqpYTPETMVTLMRDAGVTISYTAPTFYRQM--APFAKKIGLPQLRICVSAGEGLPDATRQLWKDATGIDMTDGIGAT 349
Cdd:PRK06710 281 IPK--FDMKMVFEAIKKHKVTLFPGAPTIYIALlnSPLLKEYDISSIRACISGSAPLPVEVQEKFETVTGGKLVEGYGLT 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 350 EMFHIFISSAGGEART-GAIGKVVPGYTAKVVD-DDGNEVPRGTVGKLAVIGPTGCK-YLDDPRQ-AKYVKDGWNYPGDA 425
Cdd:PRK06710 359 ESSPVTHSNFLWEKRVpGSIGVPWPDTEAMIMSlETGEALPPGEIGEIVVKGPQIMKgYWNKPEEtAAVLQDGWLHTGDV 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 426 FTQDADGYFFYQARDDDMIITAGYNVGGPEVEDALLRHPAVAECGVIGVPDEERGMVVKAVCVLKpghTGDAAMVKTLQD 505
Cdd:PRK06710 439 GYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVLK---EGTECSEEELNQ 515
|
490 500 510
....*....|....*....|....*....|.
gi 496182614 506 HVKATIAPFKYPRVVEFVTALPRTETGKLQR 536
Cdd:PRK06710 516 FARKYLAAYKVPKVYEFRDELPKTTVGKILR 546
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
51-541 |
2.79e-49 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 177.10 E-value: 2.79e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 51 AERAGNIDRPLLRGPHRTYTYRDARTEAARIAEVLTQDHglvpgnRVLLRGGNTVEMALAWLGTVYAGLIAVATMPLLRA 130
Cdd:PRK07787 8 AVAAAADIADAVRIGGRVLSRSDLAGAATAVAERVAGAR------RVAVLATPTLATVLAVVGALIAGVPVVPVPPDSGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 131 GELANIIERAQPTLalcdgrLLAELAAAQDQHPVLttivpfhtatdPADLLQRAqgkpGSMQPCPtSADDIALMAFTSGT 210
Cdd:PRK07787 82 AERRHILADSGAQA------WLGPAPDDPAGLPHV-----------PVRLHARS----WHRYPEP-DPDAPALIVYTSGT 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 211 TGAPKAAVHTHR------DVLAgcEAWprhvlKATPDDIVAGSPPLAFTFGLGGLLVFPMWAGASVYFPDQPyTPETmVT 284
Cdd:PRK07787 140 TGPPKGVVLSRRaiaadlDALA--EAW-----QWTADDVLVHGLPLFHVHGLVLGVLGPLRIGNRFVHTGRP-TPEA-YA 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 285 LMRDAGVTISYTAPTFYRQMA--PFAKKiGLPQLRICVSAGEGLPDATRQLWKDATGIDMTDGIGATEMFHIFISSAGGE 362
Cdd:PRK07787 211 QALSEGGTLYFGVPTVWSRIAadPEAAR-ALRGARLLVSGSAALPVPVFDRLAALTGHRPVERYGMTETLITLSTRADGE 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 363 ARTGAIGKVVPGYTAKVVDDDGNEVPRG--TVGKLAVIGPT-GCKYLDDPR--QAKYVKDGWNYPGDAFTQDADGYFFYQ 437
Cdd:PRK07787 290 RRPGWVGLPLAGVETRLVDEDGGPVPHDgeTVGELQVRGPTlFDGYLNRPDatAAAFTADGWFRTGDVAVVDPDGMHRIV 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 438 ARDD-DMIITAGYNVGGPEVEDALLRHPAVAECGVIGVPDEERGMVVKAVCVlkpGHTGDAAmvKTLQDHVKATIAPFKY 516
Cdd:PRK07787 370 GREStDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVV---GADDVAA--DELIDFVAQQLSVHKR 444
|
490 500
....*....|....*....|....*
gi 496182614 517 PRVVEFVTALPRTETGKLQRFKLRQ 541
Cdd:PRK07787 445 PREVRFVDALPRNAMGKVLKKQLLS 469
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
39-542 |
1.61e-48 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 176.39 E-value: 1.61e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 39 NLVHALFDQAERaeragNIDRPLLRGPHRTYTYR--DARTEAarIAEVLtQDHGLVPGNRVLLRGGNTVEMALAWLGTVY 116
Cdd:PRK07470 8 NLAHFLRQAARR-----FPDRIALVWGDRSWTWReiDARVDA--LAAAL-AARGVRKGDRILVHSRNCNQMFESMFAAFR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 117 AGLIAVATMPLLRAGELANIIERAQPTLALCDGRLLAELAAAQDQHPVLTTIVPFHTAT---DPADLLQRAQGKPGsmQP 193
Cdd:PRK07470 80 LGAVWVPTNFRQTPDEVAYLAEASGARAMICHADFPEHAAAVRAASPDLTHVVAIGGARaglDYEALVARHLGARV--AN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 194 CPTSADDIALMAFTSGTTGAPKAAVHTHR-----------DVLAGceawprhvlkATPDD---IVAgspPLAFTFGLGGL 259
Cdd:PRK07470 158 AAVDHDDPCWFFFTSGTTGRPKAAVLTHGqmafvitnhlaDLMPG----------TTEQDaslVVA---PLSHGAGIHQL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 260 LVFPMWAgASVYFPDQPYTPETMVTLMRDAGVTISYTAPTFYRQMA--PFAKKIGLPQLRICVSAGEGLPDATRQLWKDA 337
Cdd:PRK07470 225 CQVARGA-ATVLLPSERFDPAEVWALVERHRVTNLFTVPTILKMLVehPAVDRYDHSSLRYVIYAGAPMYRADQKRALAK 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 338 TGIDMTDGIGATEMF--------HIFISSAGGEARTGAIGKVVPGYTAKVVDDDGNEVPRGTVGKLAVIGP---TGckYL 406
Cdd:PRK07470 304 LGKVLVQYFGLGEVTgnitvlppALHDAEDGPDARIGTCGFERTGMEVQIQDDEGRELPPGETGEICVIGPavfAG--YY 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 407 DDPR-QAKYVKDGWNYPGDAFTQDADGYFFYQARDDDMIITAGYNVGGPEVEDALLRHPAVAECGVIGVPDEERGMVVKA 485
Cdd:PRK07470 382 NNPEaNAKAFRDGWFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVA 461
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 496182614 486 VCVLKPGHTGDAAmvkTLQDHVKATIAPFKYPRVVEFVTALPRTETGKLQRFKLRQA 542
Cdd:PRK07470 462 VCVARDGAPVDEA---ELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMVREE 515
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
67-536 |
2.02e-48 |
|
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: 175.50 E-value: 2.02e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 67 RTYTYRDARTEAARIAEVLTQdHGLVPGNRVLLRGGNTVEMALAWLGTVYAGLIAVATMPLLRAGELANIIERAQPTLAL 146
Cdd:cd05904 31 RALTYAELERRVRRLAAGLAK-RGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLAF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 147 CDGRLLAELAAAQDQhPVLTTIVPFHTATDPADLlqrAQGKPGSMQPCPTSADDIALMAFTSGTTGAPKAAVHTHRDVLA 226
Cdd:cd05904 110 TTAELAEKLASLALP-VVLLDSAEFDSLSFSDLL---FEADEAEPPVVVIKQDDVAALLYSSGTTGRSKGVMLTHRNLIA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 227 GCEAW-PRHVLKATPDDIVAGSPPLAFTFGLGGLLVFPMWAGAS-VYFPDqpYTPETMVTLMRDAGVTISYTAPTFYRQM 304
Cdd:cd05904 186 MVAQFvAGEGSNSDSEDVFLCVLPMFHIYGLSSFALGLLRLGATvVVMPR--FDLEELLAAIERYKVTHLPVVPPIVLAL 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 305 A--PFAKKIGLPQLRICVSAGEGLP----DATRQLWKDA---TGIDMTD--GIGATEMfhifiSSAGGEARTGAIGKVVP 373
Cdd:cd05904 264 VksPIVDKYDLSSLRQIMSGAAPLGkeliEAFRAKFPNVdlgQGYGMTEstGVVAMCF-----APEKDRAKYGSVGRLVP 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 374 GYTAKVVD-DDGNEVPRGTVGKLAVIGPTGCK-YLDDPR--QAKYVKDGWNYPGDAFTQDADGYFFYQARDDDMIITAGY 449
Cdd:cd05904 339 NVEAKIVDpETGESLPPNQTGELWIRGPSIMKgYLNNPEatAATIDKEGWLHTGDLCYIDEDGYLFIVDRLKELIKYKGF 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 450 NVGGPEVEDALLRHPAVAECGVIGVPDEERGMVVKAVCVLKPGHTGDAAMVktlQDHVKATIAPFKYPRVVEFVTALPRT 529
Cdd:cd05904 419 QVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKPGSSLTEDEI---MDFVAKQVAPYKKVRKVAFVDAIPKS 495
|
....*..
gi 496182614 530 ETGKLQR 536
Cdd:cd05904 496 PSGKILR 502
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
67-546 |
2.04e-48 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 175.00 E-value: 2.04e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 67 RTYTYRDARTEAARIAEVLtQDHGLVPGNRVLLRGGNTVEMALAWLGTVYAGLIAVATMPLLRAGELANIIERAQPTLAL 146
Cdd:PRK09088 21 RRWTYAELDALVGRLAAVL-RRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 147 CDgrllAELAAAQdqhPVLTTIVPFHTATDPADLLQRAqgkpgsmqpcPTSADDIALMAFTSGTTGAPKAAVHTHRDVLA 226
Cdd:PRK09088 100 GD----DAVAAGR---TDVEDLAAFIASADALEPADTP----------SIPPERVSLILFTSGTSGQPKGVMLSERNLQQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 227 GCEAWPRhVLKATPDDIVAGSPPLAFTFGLGGLLVFPMWAGASVYFPDQPYTPETMVTLMRDA-GVTISYTAPtfyrQMA 305
Cdd:PRK09088 163 TAHNFGV-LGRVDAHSSFLCDAPMFHIIGLITSVRPVLAVGGSILVSNGFEPKRTLGRLGDPAlGITHYFCVP----QMA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 306 ------PFAKKIGLPQLRICVSAGEGLPDATRQLWKDAtGIDMTDGIGATEMFHIFISSAGGE---ARTGAIGKVVPGYT 376
Cdd:PRK09088 238 qafraqPGFDAAALRHLTALFTGGAPHAAEDILGWLDD-GIPMVDGFGMSEAGTVFGMSVDCDvirAKAGAAGIPTPTVQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 377 AKVVDDDGNEVPRGTVGKLAVIGPT-GCKYLDDPR--QAKYVKDGWNYPGDAFTQDADGYFFYQARDDDMIITAGYNVGG 453
Cdd:PRK09088 317 TRVVDDQGNDCPAGVPGELLLRGPNlSPGYWRRPQatARAFTGDGWFRTGDIARRDADGFFWVVDRKKDMFISGGENVYP 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 454 PEVEDALLRHPAVAECGVIGVPDEERGMVVKAVCVLKPGHTGDAAMVKTlqdHVKATIAPFKYPRVVEFVTALPRTETGK 533
Cdd:PRK09088 397 AEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADGAPLDLERIRS---HLSTRLAKYKVPKHLRLVDALPRTASGK 473
|
490
....*....|...
gi 496182614 534 LQRFKLRQAAATP 546
Cdd:PRK09088 474 LQKARLRDALAAG 486
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
58-539 |
4.58e-48 |
|
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: 173.20 E-value: 4.58e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 58 DRPLLRGPHRTYTYRDARTEAARIAEVLtQDHGLVPGNRVLLRGGNTVEMALAWLGTVYAGLIAVATMPLLRAGELANII 137
Cdd:cd05945 6 DRPAVVEGGRTLTYRELKERADALAAAL-ASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERIREIL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 138 ERAQPTLALCDGrllaelaaaqdqhpvlttivpfhtatdpadllqraqgkpgsmqpcptsaDDIALMAFTSGTTGAPKAA 217
Cdd:cd05945 85 DAAKPALLIADG-------------------------------------------------DDNAYIIFTSGSTGRPKGV 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 218 VHTHRDVLAGCEaWPRHVLKATPDDIVAGSPPLAFTFGLGGLlvFPMWA-GASVYF--PDQPYTPETMVTLMRDAGVTIS 294
Cdd:cd05945 116 QISHDNLVSFTN-WMLSDFPLGPGDVFLNQAPFSFDLSVMDL--YPALAsGATLVPvpRDATADPKQLFRFLAEHGITVW 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 295 YTAPTFYRQM---APFAKKiGLPQLRICVSAGEGLPDATRQLWKDA---TGIDMTdgIGATEM------FHIFISSAGGE 362
Cdd:cd05945 193 VSTPSFAAMCllsPTFTPE-SLPSLRHFLFCGEVLPHKTARALQQRfpdARIYNT--YGPTEAtvavtyIEVTPEVLDGY 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 363 ARTgAIGKVVPGYTAKVVDDDGNEVPRGTVGKLAVIGPTGCK-YLDDP--RQAKYVKD---GWNYPGDAFTQDADGYFFY 436
Cdd:cd05945 270 DRL-PIGYAKPGAKLVILDEDGRPVPPGEKGELVISGPSVSKgYLNNPekTAAAFFPDegqRAYRTGDLVRLEADGLLFY 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 437 QARDDDMIITAGYNVGGPEVEDALLRHPAVAECGVIGVPDEERGMVVKAVCVLKPGhtGDAAMVKTLQDHVKATIAPFKY 516
Cdd:cd05945 349 RGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPG--AEAGLTKAIKAELAERLPPYMI 426
|
490 500
....*....|....*....|...
gi 496182614 517 PRVVEFVTALPRTETGKLQRFKL 539
Cdd:cd05945 427 PRRFVYLDELPLNANGKIDRKAL 449
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
69-541 |
5.60e-48 |
|
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: 174.64 E-value: 5.60e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 69 YTYRDARTEAARIAEVLtQDHGLVPGNRVLLRGGNTVEMALAWLGTVYAGLIAVATMPLLRAGELANIIERAQPTLALCD 148
Cdd:cd17642 45 YSYAEYLEMSVRLAEAL-KKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFCS 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 149 GRLLAELAAAQDQHPVLTTIVPFHTATDPADLLQ----RAQGKPGSMQPC---PTSAD---DIALMAFTSGTTGAPKAAV 218
Cdd:cd17642 124 KKGLQKVLNVQKKLKIIKTIIILDSKEDYKGYQClytfITQNLPPGFNEYdfkPPSFDrdeQVALIMNSSGSTGLPKGVQ 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 219 HTHRDVLAGCEAW--PRHVLKATPDDIVAGSPPLAFTFGLGGLLVFPMWAGASVYFPDqpYTPETMVTLMRDAGVTISYT 296
Cdd:cd17642 204 LTHKNIVARFSHArdPIFGNQIIPDTAILTVIPFHHGFGMFTTLGYLICGFRVVLMYK--FEEELFLRSLQDYKVQSALL 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 297 APTFyrqMAPFAK-----KIGLPQLRICVSAGEGLPDATRQLWKDATGID-MTDGIGATEMFHIFISSAGGEARTGAIGK 370
Cdd:cd17642 282 VPTL---FAFFAKstlvdKYDLSNLHEIASGGAPLSKEVGEAVAKRFKLPgIRQGYGLTETTSAILITPEGDDKPGAVGK 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 371 VVPGYTAKVVD-DDGNEVPRGTVGKLAVIGPTGCK-YLDDPR--QAKYVKDGWNYPGDAFTQDADGYFFYQARDDDMIIT 446
Cdd:cd17642 359 VVPFFYAKVVDlDTGKTLGPNERGELCVKGPMIMKgYVNNPEatKALIDKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKY 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 447 AGYNVGGPEVEDALLRHPAVAECGVIGVPDEERGMVVKAVCVLKPGHTGDAamvKTLQDHVKATIAPFKYPR-VVEFVTA 525
Cdd:cd17642 439 KGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVVLEAGKTMTE---KEVMDYVASQVSTAKRLRgGVKFVDE 515
|
490
....*....|....*.
gi 496182614 526 LPRTETGKLQRFKLRQ 541
Cdd:cd17642 516 VPKGLTGKIDRRKIRE 531
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
207-536 |
6.04e-48 |
|
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: 169.76 E-value: 6.04e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 207 TSGTTGAPKAAVHTHRDVLAgCEAWPRHVLKATPDDIVAGSPPLAFTFGLGGLLVFPMWAGASVYFPDqpYTPETMVTLM 286
Cdd:cd17637 8 TAAVAGRPRGAVLSHGNLIA-ANLQLIHAMGLTEADVYLNMLPLFHIAGLNLALATFHAGGANVVMEK--FDPAEALELI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 287 RDAGVTISYTAPTFYRQMAPFAKKIG--LPQLRICvsAGEGLPDaTRQLWKDATGIDMTDGIGATEMfHIFISSAGGEAR 364
Cdd:cd17637 85 EEEKVTLMGSFPPILSNLLDAAEKSGvdLSSLRHV--LGLDAPE-TIQRFEETTGATFWSLYGQTET-SGLVTLSPYRER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 365 TGAIGKVVPGYTAKVVDDDGNEVPRGTVGKLAVIGPTGCK-YLDDPRQAKYV-KDGWNYPGDAFTQDADGYFFYQAR--D 440
Cdd:cd17637 161 PGSAGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQgYWNLPELTAYTfRNGWHHTGDLGRFDEDGYLWYAGRkpE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 441 DDMIITAGYNVGGPEVEDALLRHPAVAECGVIGVPDEERGMVVKAVCVLKPGHTGDAamvKTLQDHVKATIAPFKYPRVV 520
Cdd:cd17637 241 KELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKPGATLTA---DELIEFVGSRIARYKKPRYV 317
|
330
....*....|....*.
gi 496182614 521 EFVTALPRTETGKLQR 536
Cdd:cd17637 318 VFVEALPKTADGSIDR 333
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
58-539 |
8.16e-47 |
|
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: 169.63 E-value: 8.16e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 58 DRPLLRGPHRTYTYRDARTEAARIAEVLtQDHGLVPGNRVLLRGGNTVEMALAWLGTVYAGLIAV---ATMPLLRageLA 134
Cdd:cd05930 2 DAVAVVDGDQSLTYAELDARANRLARYL-RERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVpldPSYPAER---LA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 135 NIIERAQPTLALcdgrllaelaaaqdqhpvlttivpfhtatdpadllqraqgkpgsmqpcpTSADDIALMAFTSGTTGAP 214
Cdd:cd05930 78 YILEDSGAKLVL-------------------------------------------------TDPDDLAYVIYTSGSTGKP 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 215 KAAVHTHRDVLAGCeAWPRHVLKATPDDIVAGSPPLAFTFGLGGLlvFPMW-AGASVYFPDQ--PYTPETMVTLMRDAGV 291
Cdd:cd05930 109 KGVMVEHRGLVNLL-LWMQEAYPLTPGDRVLQFTSFSFDVSVWEI--FGALlAGATLVVLPEevRKDPEALADLLAEEGI 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 292 TISYTAPTFYRQMAPFAKKIGLPQLRICVSAGEGLPDATRQLWKDA-TGIDMTDGIGATE------MFHifISSAGGEAR 364
Cdd:cd05930 186 TVLHLTPSLLRLLLQELELAALPSLRLVLVGGEALPPDLVRRWRELlPGARLVNLYGPTEatvdatYYR--VPPDDEEDG 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 365 TGAIGKVVPGYTAKVVDDDGNEVPRGTVGKLAVIGP---TGckYLDDPR--QAKYVKDGWN-----YP-GDAFTQDADGY 433
Cdd:cd05930 264 RVPIGRPIPNTRVYVLDENLRPVPPGVPGELYIGGAglaRG--YLNRPEltAERFVPNPFGpgermYRtGDLVRWLPDGN 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 434 FFYQARDDDMIITAGYNV--GgpEVEDALLRHPAVAECGVIGVPDEERGMVVKAVCVLKPGHTGDAAmvkTLQDHVKATI 511
Cdd:cd05930 342 LEFLGRIDDQVKIRGYRIelG--EIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEGGELDEE---ELRAHLAERL 416
|
490 500
....*....|....*....|....*...
gi 496182614 512 APFKYPRVVEFVTALPRTETGKLQRFKL 539
Cdd:cd05930 417 PDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
62-540 |
4.15e-45 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 166.40 E-value: 4.15e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 62 LRGPHRTYTYRDARTEAARIAEvLTQDHGLVPGNRVLLRGGNTVEMALAWLGTVYAGLIAVATMPLLRAGELANIIERAQ 141
Cdd:PRK08008 31 SGGVVRRYSYLELNEEINRTAN-LFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 142 PTLALCDGRLLAELAAAQDQHPVLTTIVPFHTATDPAD------LLQRAQgkpgsmQPC------PTSADDIALMAFTSG 209
Cdd:PRK08008 110 ASLLVTSAQFYPMYRQIQQEDATPLRHICLTRVALPADdgvssfTQLKAQ------QPAtlcyapPLSTDDTAEILFTSG 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 210 TTGAPKAAVHTHRDVL-AGC-EAWpRHVLKAtpDDIVAGSPPlAF-----------TFGLGGLLVFPMWAGASVyFPDQp 276
Cdd:PRK08008 184 TTSRPKGVVITHYNLRfAGYySAW-QCALRD--DDVYLTVMP-AFhidcqctaamaAFSAGATFVLLEKYSARA-FWGQ- 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 277 ytpetmvtlMRDAGVTISYTAPTFYRQM-----APFAKKIGLPQLRICVSagegLPDATRQLWKDATGIDMTDGIGATE- 350
Cdd:PRK08008 258 ---------VCKYRATITECIPMMIRTLmvqppSANDRQHCLREVMFYLN----LSDQEKDAFEERFGVRLLTSYGMTEt 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 351 MFHIFISSAGGEARTGAIGKVVPGYTAKVVDDDGNEVPRGTVGKLAVIGPTG----CKYLDDPRQ-AKYVK-DGWNYPGD 424
Cdd:PRK08008 325 IVGIIGDRPGDKRRWPSIGRPGFCYEAEIRDDHNRPLPAGEIGEICIKGVPGktifKEYYLDPKAtAKVLEaDGWLHTGD 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 425 AFTQDADGYFFYQARDDDMIITAGYNVGGPEVEDALLRHPAVAECGVIGVPDEERGMVVKAVCVLKPGHTgdaAMVKTLQ 504
Cdd:PRK08008 405 TGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGET---LSEEEFF 481
|
490 500 510
....*....|....*....|....*....|....*.
gi 496182614 505 DHVKATIAPFKYPRVVEFVTALPRTETGKLQRFKLR 540
Cdd:PRK08008 482 AFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
39-542 |
1.58e-44 |
|
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: 166.51 E-value: 1.58e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 39 NLVHALFDQAERAERagniDRPLLR-----GPHRTYTYRDARTEAARIAEVLtQDHGLVPGNRVLLRGGNTVEMALAWLG 113
Cdd:cd05968 61 NIVEQLLDKWLADTR----TRPALRwegedGTSRTLTYGELLYEVKRLANGL-RALGVGKGDRVGIYLPMIPEIVPAFLA 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 114 TVYAGLIAVATMPLLRAGELANIIERAQPTLALC-DG--------RLLAELAAAQDQHPVLTTIV---------PFHTAT 175
Cdd:cd05968 136 VARIGGIVVPIFSGFGKEAAATRLQDAEAKALITaDGftrrgrevNLKEEADKACAQCPTVEKVVvvrhlgndfTPAKGR 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 176 DPADLLQRAQGKPGSMQpcpTSADDIALMAFTSGTTGAPKAAVHTHRDVLAGCEAWPRHVLKATPDDIVAGSPPLAFTFG 255
Cdd:cd05968 216 DLSYDEEKETAGDGAER---TESEDPLMIIYTSGTTGKPKGTVHVHAGFPLKAAQDMYFQFDLKPGDLLTWFTDLGWMMG 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 256 ----LGGLLVfpmwaGASVYF----PDQPyTPETMVTLMRDAGVTISYTAPTFYRQMAPFA----KKIGLPQLRICVSAG 323
Cdd:cd05968 293 pwliFGGLIL-----GATMVLydgaPDHP-KADRLWRMVEDHEITHLGLSPTLIRALKPRGdapvNAHDLSSLRVLGSTG 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 324 EGL-PDATRQLWKdatgidmTDGIGATEMFHIfisSAGGEARTGAIGKV-------------VPGYTAKVVDDDGNEVpR 389
Cdd:cd05968 367 EPWnPEPWNWLFE-------TVGKGRNPIINY---SGGTEISGGILGNVlikpikpssfngpVPGMKADVLDESGKPA-R 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 390 GTVGKLAVIGP----TGCKYLDDPRqakYVKDGWN------YPGDAFTQDADGYFFYQARDDDMIITAGYNVGGPEVEDA 459
Cdd:cd05968 436 PEVGELVLLAPwpgmTRGFWRDEDR---YLETYWSrfdnvwVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESV 512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 460 LLRHPAVAECGVIGVPDEERGMVVKAVCVLKPGHTGDAAMVKTLQDHVKATIA-PFKyPRVVEFVTALPRTETGKLQRFK 538
Cdd:cd05968 513 LNAHPAVLESAAIGVPHPVKGEAIVCFVVLKPGVTPTEALAEELMERVADELGkPLS-PERILFVKDLPKTRNAKVMRRV 591
|
....
gi 496182614 539 LRQA 542
Cdd:cd05968 592 IRAA 595
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
68-540 |
2.08e-44 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 164.41 E-value: 2.08e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 68 TYTYRDARTEAARIAEVLtQDHGLVPGNRVLLRGGNTVEMALAWLGTVYAGLIAVATMPLLRAGELANII----ERAQPT 143
Cdd:PRK13390 24 QVSYRQLDDDSAALARVL-YDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYIVgdsgARVLVA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 144 LALCDGrLLAELAAAqdqhpvLTTIVPFHTATDPADLLQR---AQGKPGSMQPCPtsaddiALMAFTSGTTGAPKAAVHT 220
Cdd:PRK13390 103 SAALDG-LAAKVGAD------LPLRLSFGGEIDGFGSFEAalaGAGPRLTEQPCG------AVMLYSSGTTGFPKGIQPD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 221 --HRDVLAGCE---AWPRHVLKATPDDIVAGSPPL---------AFTFGLGGLLVFPmwagasvyfpdQPYTPETMVTLM 286
Cdd:PRK13390 170 lpGRDVDAPGDpivAIARAFYDISESDIYYSSAPIyhaaplrwcSMVHALGGTVVLA-----------KRFDAQATLGHV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 287 RDAGVTISYTAPTFYRQM----APFAKKIGLPQLRICVSAGEGLPDATRQLWKDATGIDMTDGIGATEMFHI-FISSAGG 361
Cdd:PRK13390 239 ERYRITVTQMVPTMFVRLlkldADVRTRYDVSSLRAVIHAAAPCPVDVKHAMIDWLGPIVYEYYSSTEAHGMtFIDSPDW 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 362 EARTGAIGKVVPGyTAKVVDDDGNEVPRGTVGKLAV-IGPTGCKYLDDPRQAKYVKDG----WNYPGDAFTQDADGYFFY 436
Cdd:PRK13390 319 LAHPGSVGRSVLG-DLHICDDDGNELPAGRIGTVYFeRDRLPFRYLNDPEKTAAAQHPahpfWTTVGDLGSVDEDGYLYL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 437 QARDDDMIITAGYNVGGPEVEDALLRHPAVAECGVIGVPDEERGMVVKAVCVLKPGHTGDAAMVKTLQDHVKATIAPFKY 516
Cdd:PRK13390 398 ADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLVEGIRGSDELARELIDYTRSRIAHYKA 477
|
490 500
....*....|....*....|....
gi 496182614 517 PRVVEFVTALPRTETGKLQRFKLR 540
Cdd:PRK13390 478 PRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
72-540 |
6.51e-44 |
|
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: 162.55 E-value: 6.51e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 72 RDARTEAARIAEVLtqdHGLVPGNRVLLRGGNTVEMALAWLG-TVYAGLIAVATMP--LLRAGELANIIERAQPTLALCd 148
Cdd:cd05929 4 RDLDRAQVFHQRRL---LLLDVYSIALNRNARAAAAEGVWIAdGVYIYLINSILTVfaAAAAWKCGACPAYKSSRAPRA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 149 grllAELAAAQDQHPVLTTIVPfhTATDPADLLqRAQGKPGSMQPCPTSADDIA--LMAFTSGTTGAPKAavhthrdVLA 226
Cdd:cd05929 80 ----EACAIIEIKAAALVCGLF--TGGGALDGL-EDYEAAEGGSPETPIEDEAAgwKMLYSGGTTGRPKG-------IKR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 227 GCEAWPrhvlkatPDDIVAGSPPLAFTFGLGG--LLVFPMW--AGASVYFPDQ----------PYTPETMVTLMRDAGVT 292
Cdd:cd05929 146 GLPGGP-------PDNDTLMAAALGFGPGADSvyLSPAPLYhaAPFRWSMTALfmggtlvlmeKFDPEEFLRLIERYRVT 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 293 ISYTAPTFYRQMAPF----AKKIGLPQLRICVSAGEGLPDATRQLWKDATGIDM------TDGIGATemfhiFISSAGGE 362
Cdd:cd05929 219 FAQFVPTMFVRLLKLpeavRNAYDLSSLKRVIHAAAPCPPWVKEQWIDWGGPIIweyyggTEGQGLT-----IINGEEWL 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 363 ARTGAIGKVVPGyTAKVVDDDGNEVPRGTVGKLAVIGPTGCKYLDDPRQ--AKYVKDGWNYPGDAFTQDADGYFFYQARD 440
Cdd:cd05929 294 THPGSVGRAVLG-KVHILDEDGNEVPPGEIGEVYFANGPGFEYTNDPEKtaAARNEGGWSTLGDVGYLDEDGYLYLTDRR 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 441 DDMIITAGYNVGGPEVEDALLRHPAVAECGVIGVPDEERGMVVKAVCVLKPGHTGDAAMVKTLQDHVKATIAPFKYPRVV 520
Cdd:cd05929 373 SDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVQPAPGADAGTALAEELIAFLRDRLSRYKCPRSI 452
|
490 500
....*....|....*....|
gi 496182614 521 EFVTALPRTETGKLQRFKLR 540
Cdd:cd05929 453 EFVAELPRDDTGKLYRRLLR 472
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
51-540 |
7.50e-44 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 163.56 E-value: 7.50e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 51 AERAGniDRPLLRGPHRTYTYRDARTEAARIAEVLtQDHGLVPGNRVLLRGGNTVEMALAWLGTVYAGliavATMPLLRA 130
Cdd:PRK07788 59 ARRAP--DRAALIDERGTLTYAELDEQSNALARGL-LALGVRAGDGVAVLARNHRGFVLALYAAGKVG----ARIILLNT 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 131 G----ELANIIERAQPTLALCDGRLLAELAAAQDQHPVLTTIVPFHTATDPAD-----LLQRAQGKPGSMQPCPTSADDI 201
Cdd:PRK07788 132 GfsgpQLAEVAAREGVKALVYDDEFTDLLSALPPDLGRLRAWGGNPDDDEPSGstdetLDDLIAGSSTAPLPKPPKPGGI 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 202 ALMafTSGTTGAPKAAVHTHRDVLAGCEAWPRHV-LKAtpDDIVAGSPPLAFTFGLGGLLVfPMWAGASVYFPDQpYTPE 280
Cdd:PRK07788 212 VIL--TSGTTGTPKGAPRPEPSPLAPLAGLLSRVpFRA--GETTLLPAPMFHATGWAHLTL-AMALGSTVVLRRR-FDPE 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 281 TMVTLMRDAGVTISYTAPTFYRQM----APFAKKIGLPQLRICVSAGEGL-PD-ATRQLwkDATGIDMTDGIGATEMfhI 354
Cdd:PRK07788 286 ATLEDIAKHKATALVVVPVMLSRIldlgPEVLAKYDTSSLKIIFVSGSALsPElATRAL--EAFGPVLYNLYGSTEV--A 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 355 FISSAGGE---ARTGAIGKVVPGYTAKVVDDDGNEVPRGTVGKLAVIGPTGCKYLDDPRqAKYVKDGWNYPGDAFTQDAD 431
Cdd:PRK07788 362 FATIATPEdlaEAPGTVGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFPFEGYTDGR-DKQIIDGLLSSGDVGYFDED 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 432 GYFFYQARDDDMIITAGYNVGGPEVEDALLRHPAVAECGVIGVPDEERGMVVKAVCVLKPGHTGDAAMVKtlqDHVKATI 511
Cdd:PRK07788 441 GLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKAPGAALDEDAIK---DYVRDNL 517
|
490 500
....*....|....*....|....*....
gi 496182614 512 APFKYPRVVEFVTALPRTETGKLQRFKLR 540
Cdd:PRK07788 518 ARYKVPRDVVFLDELPRNPTGKVLKRELR 546
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
69-543 |
1.75e-43 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 160.43 E-value: 1.75e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 69 YTYRDARTEAARIAEVLtQDHGLVPGNRVLLRGGNTVEMALAWLGTVYAGLIAVATMPLLRAGELANIIERAQPTLAlcd 148
Cdd:cd05974 1 VSFAEMSARSSRVANFL-RSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRDRVDRGGAVYA--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 149 grllaelaaAQDQHpvlttivpfhtatdpadllqraqgkpgsmqpcpTSADDIALMAFTSGTTGAPKAAVHTHRDVLAGC 228
Cdd:cd05974 77 ---------AVDEN---------------------------------THADDPMLLYFTSGTTSKPKLVEHTHRSYPVGH 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 229 EAwPRHVLKATPDDIVAGSPPLAFTFGLGGLLVFPMWAGASVYFPDQP-YTPETMVTLMRDAGVTISYTAPTFYR----- 302
Cdd:cd05974 115 LS-TMYWIGLKPGDVHWNISSPGWAKHAWSCFFAPWNAGATVFLFNYArFDAKRVLAALVRYGVTTLCAPPTVWRmliqq 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 303 QMAPFAKKiglpqLRICVSAGEGL-PDATRQLwKDATGIDMTDGIGATEMFHIFISSAGGEARTGAIGKVVPGYTAKVVD 381
Cdd:cd05974 194 DLASFDVK-----LREVVGAGEPLnPEVIEQV-RRAWGLTIRDGYGQTETTALVGNSPGQPVKAGSMGRPLPGYRVALLD 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 382 DDGNEVPRGTVG-KLAVIGPTGCK--YLDDPRQAKYVKDGWNYP-GDAFTQDADGYFFYQARDDDMIITAGYNVGGPEVE 457
Cdd:cd05974 268 PDGAPATEGEVAlDLGDTRPVGLMkgYAGDPDKTAHAMRGGYYRtGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELE 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 458 DALLRHPAVAECGVIGVPDEERGMVVKAVCVLKPGHTGDAAMVKTLQDHVKATIAPFKYPRVVEFVtALPRTETGKLQRF 537
Cdd:cd05974 348 SVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGYEPSPETALEIFRFSRERLAPYKRIRRLEFA-ELPKTISGKIRRV 426
|
....*.
gi 496182614 538 KLRQAA 543
Cdd:cd05974 427 ELRRRE 432
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
28-540 |
5.57e-43 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 161.37 E-value: 5.57e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 28 DLPELQIPDQ-ANLVHaLFDQAERaERAgniDRPLLRGPHRTYTYRDARTEAARIAEVLTQDHGLVPGNRVLLRGGNTVE 106
Cdd:PRK08974 12 DVPAEINPDRyQSLVD-MFEQAVA-RYA---DQPAFINMGEVMTFRKLEERSRAFAAYLQNGLGLKKGDRVALMMPNLLQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 107 MALAWLGTVYAGLIAVATMPLLRAGELANIIERAQPTLALCDGRLLAELAAAQDQHPVLTTIVpfhtaTDPADLLQRAQG 186
Cdd:PRK08974 87 YPIALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAKAIVIVSNFAHTLEKVVFKTPVKHVIL-----TRMGDQLSTAKG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 187 K------------------PGS------------MQPC-PT-SADDIALMAFTSGTTGAPKAAVHTHRDVLAGCE--AWP 232
Cdd:PRK08974 162 TlvnfvvkyikrlvpkyhlPDAisfrsalhkgrrMQYVkPElVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEqaKAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 233 RHVLKATPDDIVAGSPPLAFTFGL--GGLLVFPMwaGASVYFPDQPYTPETMVTLMRD------AGVTISYTA----PTF 300
Cdd:PRK08974 242 YGPLLHPGKELVVTALPLYHIFALtvNCLLFIEL--GGQNLLITNPRDIPGFVKELKKypftaiTGVNTLFNAllnnEEF 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 301 yrqmapfaKKIGLPQLRICVSAGEGLPDATRQLWKDATGIDMTDGIGATEMFH-IFISSAGGEARTGAIGKVVPGYTAKV 379
Cdd:PRK08974 320 --------QELDFSSLKLSVGGGMAVQQAVAERWVKLTGQYLLEGYGLTECSPlVSVNPYDLDYYSGSIGLPVPSTEIKL 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 380 VDDDGNEVPRGTVGKLAVIGPTGCK-YLDDPRQ-AKYVKDGWNYPGDAFTQDADGYFFYQARDDDMIITAGYNVGGPEVE 457
Cdd:PRK08974 392 VDDDGNEVPPGEPGELWVKGPQVMLgYWQRPEAtDEVIKDGWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIE 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 458 DALLRHPAVAECGVIGVPDEERGMVVKaVCVLKPghtgDAAMVK-TLQDHVKATIAPFKYPRVVEFVTALPRTETGKLQR 536
Cdd:PRK08974 472 DVVMLHPKVLEVAAVGVPSEVSGEAVK-IFVVKK----DPSLTEeELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILR 546
|
....
gi 496182614 537 FKLR 540
Cdd:PRK08974 547 RELR 550
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
53-545 |
2.39e-42 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 160.51 E-value: 2.39e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 53 RAGNIDRPLLR-----GPHR---TYTYRDARTEAARIAEVLTqDHGLVPGNRVLLRGGNTVEMALAWLGTVYAGlIAVAT 124
Cdd:PRK07529 35 AARHPDAPALSflldaDPLDrpeTWTYAELLADVTRTANLLH-SLGVGPGDVVAFLLPNLPETHFALWGGEAAG-IANPI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 125 MPLLRAGELANIIERAQP----TLA-LCDGRLLAELAAAQDQHPVLTTIVpfhtATDPADLLQRAQGKPGSMQ------- 192
Cdd:PRK07529 113 NPLLEPEQIAELLRAAGAkvlvTLGpFPGTDIWQKVAEVLAALPELRTVV----EVDLARYLPGPKRLAVPLIrrkahar 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 193 ------------------PCPTSADDIALMAFTSGTTGAPKAAVHTHRDVLAgcEAWPRH-VLKATPDDIVAGSPPLAFT 253
Cdd:PRK07529 189 ildfdaelarqpgdrlfsGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVA--NAWLGAlLLGLGPGDTVFCGLPLFHV 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 254 FGLGGLLVFPMWAGASVYFPD-QPYTPETMV----TLMRDAGVTISYTAPTFYR---QMAPFAKKIGlpQLRICVSAGEG 325
Cdd:PRK07529 267 NALLVTGLAPLARGAHVVLATpQGYRGPGVIanfwKIVERYRINFLSGVPTVYAallQVPVDGHDIS--SLRYALCGAAP 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 326 LPDATRQLWKDATGIDMTDGIGATEMFHIF-ISSAGGEARTGAIGKVVPGYTAKVV--DDDGN---EVPRGTVGKLAVIG 399
Cdd:PRK07529 345 LPVEVFRRFEAATGVRIVEGYGLTEATCVSsVNPPDGERRIGSVGLRLPYQRVRVVilDDAGRylrDCAVDEVGVLCIAG 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 400 PT---GckYLDdPRQAK--YVKDGWNYPGDAFTQDADGYFFYQARDDDMIITAGYNVGGPEVEDALLRHPAVAECGVIGV 474
Cdd:PRK07529 425 PNvfsG--YLE-AAHNKglWLEDGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAAVGR 501
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496182614 475 PDEERGMVVKAVCVLKPGHTGDAAmvkTLQDHVKATIA-PFKYPRVVEFVTALPRTETGKLQRFKLRQAAAT 545
Cdd:PRK07529 502 PDAHAGELPVAYVQLKPGASATEA---ELLAFARDHIAeRAAVPKHVRILDALPKTAVGKIFKPALRRDAIR 570
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
70-471 |
4.09e-42 |
|
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: 155.89 E-value: 4.09e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 70 TYRDARTEAARIAEVLTQDHGLVPGNRVLLRGGNTVEMALAWLGTVYAGLIAV---ATMPLLRageLANIIERAQPTLAL 146
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVpldPAYPAER---LAFILEDAGARLLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 147 CDGRLlAELAAAQDQHPVLTTIVPFHTATDPADLLQRAQgkpgsmqpcPTSADDIALMAFTSGTTGAPKAAVHTHRDVLA 226
Cdd:TIGR01733 78 TDSAL-ASRLAGLVLPVILLDPLELAALDDAPAPPPPDA---------PSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVN 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 227 GCeAWPRHVLKATPDDIVAGSPPLAFTFGlggllVFPMW----AGASVYFPDQPYTPETMV---TLMRDAGVTISYTAPT 299
Cdd:TIGR01733 148 LL-AWLARRYGLDPDDRVLQFASLSFDAS-----VEEIFgallAGATLVVPPEDEERDDAAllaALIAEHPVTVLNLTPS 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 300 FYRQMAPfAKKIGLPQLRICVSAGEGLPDATRQLWKD-ATGIDMTDGIGATE---MFHIFISSAGGEARTGA--IGKVVP 373
Cdd:TIGR01733 222 LLALLAA-ALPPALASLRLVILGGEALTPALVDRWRArGPGARLINLYGPTEttvWSTATLVDPDDAPRESPvpIGRPLA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 374 GYTAKVVDDDGNEVPRGTVGKLAVIGPT---GckYLDDPRQ--AKYVKDGWNYP--------GDAFTQDADGYFFYQARD 440
Cdd:TIGR01733 301 NTRLYVLDDDLRPVPVGVVGELYIGGPGvarG--YLNRPELtaERFVPDPFAGGdgarlyrtGDLVRYLPDGNLEFLGRI 378
|
410 420 430
....*....|....*....|....*....|.
gi 496182614 441 DDMIITAGYNVGGPEVEDALLRHPAVAECGV 471
Cdd:TIGR01733 379 DDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
200-536 |
5.56e-42 |
|
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: 153.43 E-value: 5.56e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 200 DIALMAFTSGTTGAPKAAVHTHRDVLAGCEAWPrHVLKATPDDIVAGSPPLAFTFGLGGLLVFPMWAGASVYfPDQPYTP 279
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWA-DCADLTEDDRYLIINPFFHTFGYKAGIVACLLTGATVV-PVAVFDV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 280 ETMVTLMRDAGVTISYTAPTFYRQM--APFAKKIGLPQLRICVSAGEGLPDATRQLWKDATGID-MTDGIGATEMFHIFI 356
Cdd:cd17638 79 DAILEAIERERITVLPGPPTLFQSLldHPGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFEtVLTAYGLTEAGVATM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 357 SSAGGEARTGA--IGKVVPGYTAKVVDDdgnevprgtvGKLAVIGPTGCK-YLDDPRQ-AKYV-KDGWNYPGDAFTQDAD 431
Cdd:cd17638 159 CRPGDDAETVAttCGRACPGFEVRIADD----------GEVLVRGYNVMQgYLDDPEAtAEAIdADGWLHTGDVGELDER 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 432 GYFFYQARDDDMIITAGYNVGGPEVEDALLRHPAVAECGVIGVPDEERGMVVKAVCVLKPGHTGDAAMVKTLqdhVKATI 511
Cdd:cd17638 229 GYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGVTLTEEDVIAW---CRERL 305
|
330 340
....*....|....*....|....*
gi 496182614 512 APFKYPRVVEFVTALPRTETGKLQR 536
Cdd:cd17638 306 ANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
28-540 |
9.25e-42 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 157.87 E-value: 9.25e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 28 DLPELQIPDQANLVHALFDQaeraeragNIDRPLLRGPHRTYTYRDARTEAARIAEVLtQDHGLVPGNRVLLRGGNTVEM 107
Cdd:PRK07059 16 EIDASQYPSLADLLEESFRQ--------YADRPAFICMGKAITYGELDELSRALAAWL-QSRGLAKGARVAIMMPNVLQY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 108 ALAWLGTVYAGLIAVATMPLLRAGELAN-----------IIERAQPTLAlcdgrllAELAAAQDQHPVLTT--------- 167
Cdd:PRK07059 87 PVAIAAVLRAGYVVVNVNPLYTPRELEHqlkdsgaeaivVLENFATTVQ-------QVLAKTAVKHVVVASmgdllgfkg 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 168 ------------IVPFHT---ATDPADLLqrAQGKPGSMQPCPTSADDIALMAFTSGTTGAPKAAVHTHRDVLAGC---E 229
Cdd:PRK07059 160 hivnfvvrrvkkMVPAWSlpgHVRFNDAL--AEGARQTFKPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVlqmE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 230 AWPRHVLKATPDD---IVAGSPPLAFTFGLGGLLVFPMWAGA-SVYFPDqPYTPETMVTLMRDAGVTISYTAPTFYRQM- 304
Cdd:PRK07059 238 AWLQPAFEKKPRPdqlNFVCALPLYHIFALTVCGLLGMRTGGrNILIPN-PRDIPGFIKELKKYQVHIFPAVNTLYNALl 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 305 -APFAKKIGLPQLRICVSAGEGLPDATRQLWKDATGIDMTDGIGATEMFHIFISS-AGGEARTGAIGKVVPGYTAKVVDD 382
Cdd:PRK07059 317 nNPDFDKLDFSKLIVANGGGMAVQRPVAERWLEMTGCPITEGYGLSETSPVATCNpVDATEFSGTIGLPLPSTEVSIRDD 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 383 DGNEVPRGTVGKLAVIGP---TGckYLDDPRQAKYV--KDGWNYPGDAFTQDADGYFFYQARDDDMIITAGYNVGGPEVE 457
Cdd:PRK07059 397 DGNDLPLGEPGEICIRGPqvmAG--YWNRPDETAKVmtADGFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIE 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 458 DALLRHPAVAECGVIGVPDEERGMVVKAVCVLK-PGHTGDAamvktLQDHVKATIAPFKYPRVVEFVTALPRTETGKLQR 536
Cdd:PRK07059 475 EVVASHPGVLEVAAVGVPDEHSGEAVKLFVVKKdPALTEED-----VKAFCKERLTNYKRPKFVEFRTELPKTNVGKILR 549
|
....
gi 496182614 537 FKLR 540
Cdd:PRK07059 550 RELR 553
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
58-540 |
3.06e-41 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 155.62 E-value: 3.06e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 58 DRP--LLRGPHRTYTYRDARTEAARIAEVLtQDHGLVPGNRVLLRGGNTVEMALAWLGTVYAGLIAVATMPLLRAGELAN 135
Cdd:PRK13391 12 DKPavIMASTGEVVTYRELDERSNRLAHLF-RSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAAY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 136 IIERAQPTLALCDGRLLAELAAAQDQHPVLTTIVpfhtATDPADLLQRAQGKPGSMQPCPTS--ADDI--ALMAFTSGTT 211
Cdd:PRK13391 91 IVDDSGARALITSAAKLDVARALLKQCPGVRHRL----VLDGDGELEGFVGYAEAVAGLPATpiADESlgTDMLYSSGTT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 212 GAPKA--------AVHTHRDVLAGCeawprHVLKATPDDIVAGSP-------PLAF---TFGLGGLLVFpMwagasvyfp 273
Cdd:PRK13391 167 GRPKGikrplpeqPPDTPLPLTAFL-----QRLWGFRSDMVYLSPaplyhsaPQRAvmlVIRLGGTVIV-M--------- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 274 dQPYTPETMVTLMRDAGVTISYTAPTFYRQMA--PFA--KKIGLPQLRICVSAGEGLPDATRQLWKDATG--ID----MT 343
Cdd:PRK13391 232 -EHFDAEQYLALIEEYGVTHTQLVPTMFSRMLklPEEvrDKYDLSSLEVAIHAAAPCPPQVKEQMIDWWGpiIHeyyaAT 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 344 DGIGATemfhiFISSAGGEARTGAIGKVVPGyTAKVVDDDGNEVPRGTVGKLAVIGPTGCKYLDDP---RQAKYVKDGWN 420
Cdd:PRK13391 311 EGLGFT-----ACDSEEWLAHPGTVGRAMFG-DLHILDDDGAELPPGEPGTIWFEGGRPFEYLNDPaktAEARHPDGTWS 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 421 YPGDAFTQDADGYFFYQARDDDMIITAGYNVGGPEVEDALLRHPAVAECGVIGVPDEERGMVVKAVCVLKPGHTGDAAMV 500
Cdd:PRK13391 385 TVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPVDGVDPGPALA 464
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 496182614 501 KTLQDHVKATIAPFKYPRVVEFVTALPRTETGKLQRFKLR 540
Cdd:PRK13391 465 AELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLLR 504
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
203-532 |
8.18e-41 |
|
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: 150.53 E-value: 8.18e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 203 LMAFTSGTTGAPKAAVHTHRDVLAgcEAWPRHVL-KATPDDIVAGSPPLaFTFG--LGGLLVFPMwAGASVYFPDqpYTP 279
Cdd:cd17636 4 LAIYTAAFSGRPNGALLSHQALLA--QALVLAVLqAIDEGTVFLNSGPL-FHIGtlMFTLATFHA-GGTNVFVRR--VDA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 280 ETMVTLMRDAGVTISYTAPTFYRQMAPFAKKiGLPQLRiCVSAGEGLPDatrqlWKDATGIDMTD------GIGATEMFH 353
Cdd:cd17636 78 EEVLELIEAERCTHAFLLPPTIDQIVELNAD-GLYDLS-SLRSSPAAPE-----WNDMATVDTSPwgrkpgGYGQTEVMG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 354 IFISSAGGEARTGAIGKVVPGYTAKVVDDDGNEVPRGTVGKLAVIGPT-GCKYLDDPR-QAKYVKDGWNYPGDAFTQDAD 431
Cdd:cd17636 151 LATFAALGGGAIGGAGRPSPLVQVRILDEDGREVPDGEVGEIVARGPTvMAGYWNRPEvNARRTRGGWHHTNDLGRREPD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 432 GYFFYQARDDDMIITAGYNVGGPEVEDALLRHPAVAECGVIGVPDEERGMVVKAVCVLKPGHTGDAAmvkTLQDHVKATI 511
Cdd:cd17636 231 GSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPGASVTEA---ELIEHCRARI 307
|
330 340
....*....|....*....|.
gi 496182614 512 APFKYPRVVEFVTALPRTETG 532
Cdd:cd17636 308 ASYKKPKSVEFADALPRTAGG 328
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
52-540 |
8.46e-41 |
|
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: 153.99 E-value: 8.46e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 52 ERAGNI--DRPLLRGPHRTYTYRDARTEAARIAEVLtQDHGLVPGNRVLLRGGNTVEMALAWLGTVYAGLIAVATMPLLR 129
Cdd:cd12118 11 ERAAAVypDRTSIVYGDRRYTWRQTYDRCRRLASAL-AALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 130 AGELANIIERAQPTLALCDGRLLAElaaaqdqhpvlttivpfhtatdpaDLLqrAQGKPGSMQPCPTSADD-IALmAFTS 208
Cdd:cd12118 90 AEEIAFILRHSEAKVLFVDREFEYE------------------------DLL--AEGDPDFEWIPPADEWDpIAL-NYTS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 209 GTTGAPKAAVHTHRdvlaGCeawprhVLKATPDdivagspplAFTFGLGGLLVF----PM---------WA-----GASV 270
Cdd:cd12118 143 GTTGRPKGVVYHHR----GA------YLNALAN---------ILEWEMKQHPVYlwtlPMfhcngwcfpWTvaavgGTNV 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 271 YFPDqpYTPETMVTLMRDAGVTISYTAPTFYRQM--APFAKKIGLPQlRICVSAGEGLPDATRQLWKDATGIDMTDGIGA 348
Cdd:cd12118 204 CLRK--VDAKAIYDLIEKHKVTHFCGAPTVLNMLanAPPSDARPLPH-RVHVMTAGAPPPAAVLAKMEELGFDVTHVYGL 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 349 TEMFHIFIS--------------SAGGEARTGAigkvvpGYTAK----VVDDDGNE-VPRG--TVGKLAVIGPTGCK-YL 406
Cdd:cd12118 281 TETYGPATVcawkpewdelpteeRARLKARQGV------RYVGLeevdVLDPETMKpVPRDgkTIGEIVFRGNIVMKgYL 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 407 DDPR-QAKYVKDGWNYPGDAFTQDADGYFFYQARDDDMIITAGYNVGGPEVEDALLRHPAVAECGVIGVPDEERGMVVKA 485
Cdd:cd12118 355 KNPEaTAEAFRGGWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCA 434
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 496182614 486 VCVLKPGHTgdaAMVKTLQDHVKATIAPFKYPRVVEFVTaLPRTETGKLQRFKLR 540
Cdd:cd12118 435 FVELKEGAK---VTEEEIIAFCREHLAGFMVPKTVVFGE-LPKTSTGKIQKFVLR 485
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
58-533 |
1.96e-40 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 153.89 E-value: 1.96e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 58 DRPLLRGPHRTYTYRDARTEAARIAEVLtQDHGLVPGNRVLLRGGNTVEMALAWLGTVYAGLIAVATMPLLRAGELANII 137
Cdd:PRK07798 18 DRVALVCGDRRLTYAELEERANRLAHYL-IAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 138 ERAQPTLALCDGRLLAELAAAQDQHPVLTTIV---------PFHTATDPADLLqrAQGKPGSMQPcPTSADDIaLMAFTS 208
Cdd:PRK07798 97 DDSDAVALVYEREFAPRVAEVLPRLPKLRTLVvvedgsgndLLPGAVDYEDAL--AAGSPERDFG-ERSPDDL-YLLYTG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 209 GTTGAPKAAVHTHRD---VLAGCEAWPRHVLKATPDDIVAGsppLAFTFGLGGLLVFPMWAGAS--------------VY 271
Cdd:PRK07798 173 GTTGMPKGVMWRQEDifrVLLGGRDFATGEPIEDEEELAKR---AAAGPGMRRFPAPPLMHGAGqwaafaalfsgqtvVL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 272 FPDQPYTPETMVTLMRDAGVT-ISYTAPTFYRQMAP---FAKKIGLPQLRICVSAGEGLPDATRQLWKDA-TGIDMTDGI 346
Cdd:PRK07798 250 LPDVRFDADEVWRTIEREKVNvITIVGDAMARPLLDaleARGPYDLSSLFAIASGGALFSPSVKEALLELlPNVVLTDSI 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 347 GATEM-FHIFISSAGGEARTGAiGKVVPGYTAKVVDDDGNEVPRGT--VGKLAVIGPTGCKYLDDP---RQAKYVKDG-- 418
Cdd:PRK07798 330 GSSETgFGGSGTVAKGAVHTGG-PRFTIGPRTVVLDEDGNPVEPGSgeIGWIARRGHIPLGYYKDPektAETFPTIDGvr 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 419 WNYPGDAFTQDADGYFFYQARDDDMIITAGYNVGGPEVEDALLRHPAVAECGVIGVPDEERGMVVKAVCVLKPGHTGDAA 498
Cdd:PRK07798 409 YAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVPDERWGQEVVAVVQLREGARPDLA 488
|
490 500 510
....*....|....*....|....*....|....*
gi 496182614 499 mvkTLQDHVKATIAPFKYPRVVEFVTALPRTETGK 533
Cdd:PRK07798 489 ---ELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
70-539 |
2.07e-40 |
|
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: 153.05 E-value: 2.07e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 70 TYRDARTEAARIAEVLTQDhGLVPGNRVLLRGGNTVEMALAWLGTVYAGLIAVATMPLLRAGELANIIERAQPTLA-LCD 148
Cdd:cd05923 30 TYSELRARIEAVAARLHAR-GLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERGEMTAAvIAV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 149 GRLLAElAAAQDQHPVLTTivpfhtATDPADLLQRAQGKPGSMQPCPTSADdiALMAFTSGTTGAPKAAVHTHRdvlagc 228
Cdd:cd05923 109 DAQVMD-AIFQSGVRVLAL------SDLVGLGEPESAGPLIEDPPREPEQP--AFVFYTSGTTGLPKGAVIPQR------ 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 229 EAWPRHVLKAT-------PDDIVAGSPPLAFTFGLGGLLVFPMwAGASVYFPDQPYTPETMVTLMRDAGVTISYTAPTFY 301
Cdd:cd05923 174 AAESRVLFMSTqaglrhgRHNVVLGLMPLYHVIGFFAVLVAAL-ALDGTYVVVEEFDPADALKLIEQERVTSLFATPTHL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 302 RQMAPFAKKIG--LPQLRICVSAGEGLPDATRQLWKDATGIDMTDGIGATEMFHIFISSAggeARTGAIGKvvPGYTAKV 379
Cdd:cd05923 253 DALAAAAEFAGlkLSSLRHVTFAGATMPDAVLERVNQHLPGEKVNIYGTTEAMNSLYMRD---ARTGTEMR--PGFFSEV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 380 vdddgnEVPR--GTVGKLAVIGPTGC------------KYLDDPR-QAKYVKDGWNYPGDAFTQDADGYFFYQARDDDMI 444
Cdd:cd05923 328 ------RIVRigGSPDEALANGEEGElivaaaadaaftGYLNQPEaTAKKLQDGWYRTGDVGYVDPSGDVRILGRVDDMI 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 445 ITAGYNVGGPEVEDALLRHPAVAECGVIGVPDEERGMVVKAVCVLKPGHTGDAAMVKTLQDhvkATIAPFKYPRVVEFVT 524
Cdd:cd05923 402 ISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREGTLSADELDQFCRA---SELADFKRPRRYFFLD 478
|
490
....*....|....*
gi 496182614 525 ALPRTETGKLQRFKL 539
Cdd:cd05923 479 ELPKNAMNKVLRRQL 493
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
43-544 |
5.16e-40 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 153.04 E-value: 5.16e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 43 ALFDQAerAERAGniDRPLLRGPHRT--YTYRDARTEAARIAEVLTQdHGLVPGNRVLLRGGNTVEmalaWLGTVYA--- 117
Cdd:PRK08315 20 QLLDRT--AARYP--DREALVYRDQGlrWTYREFNEEVDALAKGLLA-LGIEKGDRVGIWAPNVPE----WVLTQFAtak 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 118 -GLIAVATMPLLRAGELANIIERAQ-PTLALCDG-----------RLLAELAAAQDQH------PVLTTIV--------- 169
Cdd:PRK08315 91 iGAILVTINPAYRLSELEYALNQSGcKALIAADGfkdsdyvamlyELAPELATCEPGQlqsarlPELRRVIflgdekhpg 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 170 --PFH------TATDPADLLQRAQGkpgsmqpcpTSADDIALMAFTSGTTGAPKAAVHTHRDVL------AGCeawprhv 235
Cdd:PRK08315 171 mlNFDellalgRAVDDAELAARQAT---------LDPDDPINIQYTSGTTGFPKGATLTHRNILnngyfiGEA------- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 236 LKATPDDIVAGSPPLAFTFG--LGGLLVFPmwAGASVYFPDQPYTPETMVTLMRDAGVTISYTAPTFYrqMA----PFAK 309
Cdd:PRK08315 235 MKLTEEDRLCIPVPLYHCFGmvLGNLACVT--HGATMVYPGEGFDPLATLAAVEEERCTALYGVPTMF--IAeldhPDFA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 310 KIGLPQLRICVSAGEGLPDAT-RQLWKDATGIDMTDGIGATE----MFHIFISSAGgEARTGAIGKVVPGYTAKVVD-DD 383
Cdd:PRK08315 311 RFDLSSLRTGIMAGSPCPIEVmKRVIDKMHMSEVTIAYGMTEtspvSTQTRTDDPL-EKRVTTVGRALPHLEVKIVDpET 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 384 GNEVPRGTVGKLAVIGPTGCK-YLDDPRQAKYV--KDGWNYPGDAFTQDADGYFFYQARDDDMIITAGYNVGGPEVEDAL 460
Cdd:PRK08315 390 GETVPRGEQGELCTRGYSVMKgYWNDPEKTAEAidADGWMHTGDLAVMDEEGYVNIVGRIKDMIIRGGENIYPREIEEFL 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 461 LRHPAVAECGVIGVPDEERGMVVKAVCVLKPGHTGDAAMVktlQDHVKATIAPFKYPRVVEFVTALPRTETGKLQRFKLR 540
Cdd:PRK08315 470 YTHPKIQDVQVVGVPDEKYGEEVCAWIILRPGATLTEEDV---RDFCRGKIAHYKIPRYIRFVDEFPMTVTGKIQKFKMR 546
|
....
gi 496182614 541 QAAA 544
Cdd:PRK08315 547 EMMI 550
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
43-539 |
2.93e-39 |
|
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: 149.66 E-value: 2.93e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 43 ALFdqAERAERAGniDRPLLRGPHRTYTYRDARTEAARIAEVLtQDHGLVPGNRVLLRGGNTVEMALAWLGTVYAGLIAV 122
Cdd:cd12117 1 ELF--EEQAARTP--DAVAVVYGDRSLTYAELNERANRLARRL-RAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 123 ATMPLLRAGELANIIERAQPTLALCDGrllaelaAAQDQHPVLTTIVPFHTATDPAdllqraqgkPGSMQPCPTSADDIA 202
Cdd:cd12117 76 PLDPELPAERLAFMLADAGAKVLLTDR-------SLAGRAGGLEVAVVIDEALDAG---------PAGNPAVPVSPDDLA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 203 LMAFTSGTTGAPKAAVHTHRDVLAGCEAwPRHVLkATPDDIVAGSPPLAF---TFGLGGLLVFpmwaGASVYF--PDQPY 277
Cdd:cd12117 140 YVMYTSGSTGRPKGVAVTHRGVVRLVKN-TNYVT-LGPDDRVLQTSPLAFdasTFEIWGALLN----GARLVLapKGTLL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 278 TPETMVTLMRDAGVTISY-TAPTFyRQMAPFAKKIgLPQLRICVSAGEGL-PDATRQLWKDATGIDMTDGIGATE--MFH 353
Cdd:cd12117 214 DPDALGALIAEEGVTVLWlTAALF-NQLADEDPEC-FAGLRELLTGGEVVsPPHVRRVLAACPGLRLVNGYGPTEntTFT 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 354 IFISSAGGEARTGA--IGKVVPGYTAKVVDDDGNEVPRGTVGKLAVIGPTGCK-YLDDPR--QAKYVKDGWN-----Y-P 422
Cdd:cd12117 292 TSHVVTELDEVAGSipIGRPIANTRVYVLDEDGRPVPPGVPGELYVGGDGLALgYLNRPAltAERFVADPFGpgerlYrT 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 423 GDAFTQDADGYFFYQARDDDMIITAGYNVGGPEVEDALLRHPAVAECGVigVPDEERGMVVKAVCVLKPGHTGDAAmvkT 502
Cdd:cd12117 372 GDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVV--VVREDAGGDKRLVAYVVAEGALDAA---E 446
|
490 500 510
....*....|....*....|....*....|....*..
gi 496182614 503 LQDHVKATIAPFKYPRVVEFVTALPRTETGKLQRFKL 539
Cdd:cd12117 447 LRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
48-540 |
8.42e-39 |
|
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341306 [Multi-domain] Cd Length: 491 Bit Score: 148.65 E-value: 8.42e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 48 AERAERAGniDRPLLRGPHRTYTYRDARTEAARIAEVLTQDhGLVPGNRVLLRGGNTVEMALAWLGTVYAGLIAVATMPL 127
Cdd:cd17651 2 ERQAARTP--DAPALVAEGRRLTYAELDRRANRLAHRLRAR-GVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 128 LRAGELANIIERAQPTLALCDGRLLAELAaaQDQHPVLTTIVPFHTATDPADLlqraqgkpgsmqPCPTSADDIALMAFT 207
Cdd:cd17651 79 YPAERLAFMLADAGPVLVLTHPALAGELA--VELVAVTLLDQPGAAAGADAEP------------DPALDADDLAYVIYT 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 208 SGTTGAPKAAVHTHRdVLAGCEAWPRHVLKATPDDIVAGSPPLAF---------TFGLGGLLVFPMwagasvyfPDQPYT 278
Cdd:cd17651 145 SGSTGRPKGVVMPHR-SLANLVAWQARASSLGPGARTLQFAGLGFdvsvqeifsTLCAGATLVLPP--------EEVRTD 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 279 PETMVTLMRDAGVTISYTAPTFYRQMAPFAKKIG--LPQLRICVSAGEGLP--DATRQLWKDATGIDMTDGIGATEM--- 351
Cdd:cd17651 216 PPALAAWLDEQRISRVFLPTVALRALAEHGRPLGvrLAALRYLLTGGEQLVltEDLREFCAGLPGLRLHNHYGPTEThvv 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 352 -FHIFISSAGGEARTGAIGKVVPGYTAKVVDDDGNEVPRGTVGKLAVIGP------------TGCKYLDDPrqakYVKDG 418
Cdd:cd17651 296 tALSLPGDPAAWPAPPPIGRPIDNTRVYVLDAALRPVPPGVPGELYIGGAglargylnrpelTAERFVPDP----FVPGA 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 419 WNY-PGDAFTQDADGYFFYQARDDDMIITAGYNVGGPEVEDALLRHPAVAECGVIGVPDEERGMVVKAVCVLKPGHTGDA 497
Cdd:cd17651 372 RMYrTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPEAPVDA 451
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 496182614 498 AmvkTLQDHVKATIAPFKYPRVVEFVTALPRTETGKLQRFKLR 540
Cdd:cd17651 452 A---ELRAALATHLPEYMVPSAFVLLDALPLTPNGKLDRRALP 491
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
64-539 |
2.55e-38 |
|
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: 146.20 E-value: 2.55e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 64 GPHRTYTYRDARTEAARIAEVLtQDHGLVPGNRVLLRGGNTVEMALAWLGTVYAGLIAVATMPLLRAGELANIIERAQPT 143
Cdd:cd05907 1 GVWQPITWAEFAEEVRALAKGL-IALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 144 LALCDGrllaelaaaqdqhpvlttivpfhtatdpadllqraqgkpgsmqpcptsADDIALMAFTSGTTGAPKAAVHTHRD 223
Cdd:cd05907 80 ALFVED------------------------------------------------PDDLATIIYTSGTTGRPKGVMLSHRN 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 224 VLAGCEAWPrHVLKATPDDIVAGSPPLAFTFGLGGLLVFPMWAGASVYFPDQpytPETMVTLMRDAGVTISYTAPTFYR- 302
Cdd:cd05907 112 ILSNALALA-ERLPATEGDRHLSFLPLAHVFERRAGLYVPLLAGARIYFASS---AETLLDDLSEVRPTVFLAVPRVWEk 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 303 --------QMAPFAKKIG----LPQLRICVSAGEGLPDATRQLWKdATGIDMTDGIGATEMFHIFISSAGGEARTGAIGK 370
Cdd:cd05907 188 vyaaikvkAVPGLKRKLFdlavGGRLRFAASGGAPLPAELLHFFR-ALGIPVYEGYGLTETSAVVTLNPPGDNRIGTVGK 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 371 VVPGYTAKVVDDdgnevprgtvGKLAVIGPTGCK-YLDDPRQAKYVK--DGWNYPGDAFTQDADGYFFYQARDDDMIITA 447
Cdd:cd05907 267 PLPGVEVRIADD----------GEILVRGPNVMLgYYKNPEATAEALdaDGWLHTGDLGEIDEDGFLHITGRKKDLIITS 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 448 -GYNVGGPEVEDALLRHPAVAECGVIG----------VPDEErgmVVKAVCVLKPGHTGDAAMVKTlQDHVKATIApfky 516
Cdd:cd05907 337 gGKNISPEPIENALKASPLISQAVVIGdgrpflvaliVPDPE---ALEAWAEEHGIAYTDVAELAA-NPAVRAEIE---- 408
|
490 500
....*....|....*....|...
gi 496182614 517 PRVVEFVTALPRTEtgKLQRFKL 539
Cdd:cd05907 409 AAVEAANARLSRYE--QIKKFLL 429
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
68-541 |
3.10e-38 |
|
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: 145.18 E-value: 3.10e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 68 TYTYRDARTEAARIAEVLTQdHGLVPGNRVLLRGGNTVEMALAWLGTVYAGLIAVATMPLLRAGELANIIERAQPTLalc 147
Cdd:cd05912 1 SYTFAELFEEVSRLAEHLAA-LGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVKL--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 148 dgrllaelaaaqdqhpvlttivpfhtatdpadllqraqgkpgsmqpcptsaDDIALMAFTSGTTGAPKAAVHTHRDVLAG 227
Cdd:cd05912 77 ---------------------------------------------------DDIATIMYTSGTTGKPKGVQQTFGNHWWS 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 228 CEAwPRHVLKATPDDIVAGSPPLaftFGLGGL--LVFPMWAGASVYFPDQpYTPETMVTLMRDAGVTISYTAPTFYRQMA 305
Cdd:cd05912 106 AIG-SALNLGLTEDDNWLCALPL---FHISGLsiLMRSVIYGMTVYLVDK-FDAEQVLHLINSGKVTIISVVPTMLQRLL 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 306 PFAKKIGLPQLRiCVSAGEGLPDATRQLWKDATGIDMTDGIGATEMFHIFI--SSAGGEARTGAIGKVVPGYTAKVVDDD 383
Cdd:cd05912 181 EILGEGYPNNLR-CILLGGGPAPKPLLEQCKEKGIPVYQSYGMTETCSQIVtlSPEDALNKIGSAGKPLFPVELKIEDDG 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 384 GNEvprGTVGKLAVIGPTGCK-YLDDP-RQAKYVKDGWNYPGDAFTQDADGYFFYQARDDDMIITAGYNVGGPEVEDALL 461
Cdd:cd05912 260 QPP---YEVGEILLKGPNVTKgYLNRPdATEESFENGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLL 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 462 RHPAVAECGVIGVPDEERGMVVKAVCVLKPGHTgdaamVKTLQDHVKATIAPFKYPRVVEFVTALPRTETGKLQRFKLRQ 541
Cdd:cd05912 337 SHPAIKEAGVVGIPDDKWGQVPVAFVVSERPIS-----EEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHELKQ 411
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
48-536 |
4.24e-38 |
|
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: 146.32 E-value: 4.24e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 48 AERAERAGniDRPLLRGPHRTYTYRDARTEAARIAEVLtQDHGLVPGNRVLLRGGNTVEMALAWLGTVYAGLIAVATMPL 127
Cdd:cd05920 22 ARSAARHP--DRIAVVDGDRRLTYRELDRRADRLAAGL-RGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPVLALPS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 128 LRAGELANIIERAQPTLALCDGRllaelaaaqdqhpvlttivpfHTATDPADLLQRAQGKpgsmqpCPtsadDIALMAFT 207
Cdd:cd05920 99 HRRSELSAFCAHAEAVAYIVPDR---------------------HAGFDHRALARELAES------IP----EVALFLLS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 208 SGTTGAPKAAVHTHRD----VLAGCEawprhVLKATPDDIVAGSPPLAFTFGLGGLLVF-PMWAGASVYFPDQPyTPETM 282
Cdd:cd05920 148 GGTTGTPKLIPRTHNDyaynVRASAE-----VCGLDQDTVYLAVLPAAHNFPLACPGVLgTLLAGGRVVLAPDP-SPDAA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 283 VTLMRDAGVTISYTAPTFYRQMAPFA--KKIGLPQLRICVSAGEGLPDATRQLWKDATGIDMTDGIGATEMFHIFissag 360
Cdd:cd05920 222 FPLIEREGVTVTALVPALVSLWLDAAasRRADLSSLRLLQVGGARLSPALARRVPPVLGCTLQQVFGMAEGLLNY----- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 361 geARTGAIGKVV---------PGYTAKVVDDDGNEVPRGTVGKLAVIGP-TGCKYLDDPR--QAKYVKDGWNYPGDAFTQ 428
Cdd:cd05920 297 --TRLDDPDEVIihtqgrpmsPDDEIRVVDEEGNPVPPGEEGELLTRGPyTIRGYYRAPEhnARAFTPDGFYRTGDLVRR 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 429 DADGYFFYQARDDDMIITAGYNVGGPEVEDALLRHPAVAECGVIGVPDEERGMVVKAVCVLKPGHTGDAAMVKTLQdhvK 508
Cdd:cd05920 375 TPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVLRDPPPSAAQLRRFLR---E 451
|
490 500
....*....|....*....|....*...
gi 496182614 509 ATIAPFKYPRVVEFVTALPRTETGKLQR 536
Cdd:cd05920 452 RGLAAYKLPDRIEFVDSLPLTAVGKIDK 479
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
58-539 |
5.11e-38 |
|
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: 145.90 E-value: 5.11e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 58 DRPLLRGPHRTYTYRDARTEAARIAEVLtQDHGLVPGNRVLLRGGNTVEMALAWLGTVYAGLIAVATMPLLRAGELANII 137
Cdd:cd12116 2 DATAVRDDDRSLSYAELDERANRLAARL-RARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 138 ERAQPTLALCDGRLLAELAAaqdqhpvlttivpfhTATDPADLLQRAQGKPGSMQPcPTSADDIALMAFTSGTTGAPKAA 217
Cdd:cd12116 81 EDAEPALVLTDDALPDRLPA---------------GLPVLLLALAAAAAAPAAPRT-PVSPDDLAYVIYTSGSTGRPKGV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 218 VHTHRDVLAGCEAWpRHVLKATPDD-IVAGSPPlafTFGLGGL-LVFPMWAGASVYF--PDQPYTPETMVTLMRDAGVTI 293
Cdd:cd12116 145 VVSHRNLVNFLHSM-RERLGLGPGDrLLAVTTY---AFDISLLeLLLPLLAGARVVIapRETQRDPEALARLIEAHSITV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 294 SYTAPTFYRqMAPFAKKIGLPQLRICVsAGEGLP-DATRQLWkdATGIDMTDGIGATEMFhifISSAGGEARTGA----I 368
Cdd:cd12116 221 MQATPATWR-MLLDAGWQGRAGLTALC-GGEALPpDLAARLL--SRVGSLWNLYGPTETT---IWSTAARVTAAAgpipI 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 369 GKVVPGYTAKVVDDDGNEVPRGTVGKLAVIGPTGCK-YLDDPR--QAKYVKDGWNYP-------GDAFTQDADGYFFYQA 438
Cdd:cd12116 294 GRPLANTQVYVLDAALRPVPPGVPGELYIGGDGVAQgYLGRPAltAERFVPDPFAGPgsrlyrtGDLVRRRADGRLEYLG 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 439 RDDDMIITAGYNVGGPEVEDALLRHPAVAECGVIGVPDEERGMVVkAVCVLKPGHTGDAAMV-KTLQDHVKATIAPFKYP 517
Cdd:cd12116 374 RADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGGDRRLV-AYVVLKAGAAPDAAALrAHLRATLPAYMVPSAFV 452
|
490 500
....*....|....*....|..
gi 496182614 518 RvvefVTALPRTETGKLQRFKL 539
Cdd:cd12116 453 R----LDALPLTANGKLDRKAL 470
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
200-536 |
6.27e-38 |
|
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: 142.16 E-value: 6.27e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 200 DIALMAFTSGTTGAPKAAVHTHRDVLAGCEAwPRHVLKATPDDIVAGSPPLAFTFGLGGLLvFPMWAGASVYFpDQPYTP 279
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRSERSWIESFVC-NEDLFNISGEDAILAPGPLSHSLFLYGAI-SALYLGGTFIG-QRKFNP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 280 ETMVTLMRDAGVTISYTAPTFYRQMApfakKIGLPQL--RICVSAGEGLPDAT----RQLWKDATGIDMtdgIGATEMFH 353
Cdd:cd17633 78 KSWIRKINQYNATVIYLVPTMLQALA----RTLEPESkiKSIFSSGQKLFESTkkklKNIFPKANLIEF---YGTSELSF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 354 IFISSAGGEARTGAIGKVVPGYTAKVVDDDGNEVprgtvGKLAVIGPTgcKYLDDPRQAKYVKDGWNYPGDAFTQDADGY 433
Cdd:cd17633 151 ITYNFNQESRPPNSVGRPFPNVEIEIRNADGGEI-----GKIFVKSEM--VFSGYVRGGFSNPDGWMSVGDIGYVDEEGY 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 434 FFYQARDDDMIITAGYNVGGPEVEDALLRHPAVAECGVIGVPDEERGMVVKAVcvlkpgHTGDAAMVKTLQDHVKATIAP 513
Cdd:cd17633 224 LYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVAL------YSGDKLTYKQLKRFLKQKLSR 297
|
330 340
....*....|....*....|...
gi 496182614 514 FKYPRVVEFVTALPRTETGKLQR 536
Cdd:cd17633 298 YEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
199-544 |
8.07e-38 |
|
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: 143.00 E-value: 8.07e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 199 DDIALMAFTSGTTGAPKAAVHTHRDVLAgcEAWP-RHVLKATPDDIVAGSPPLAFTFGLGGLLVFPMWAGASVYFPD-QP 276
Cdd:cd05944 2 DDVAAYFHTGGTTGTPKLAQHTHSNEVY--NAWMlALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVVLAGpAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 277 YTPETMV----TLMRDAGVTISYTAPTFYRQMAPFAKKIGLPQLRICVSAGEGLPDATRQLWKDATGIDMTDGIGATEMF 352
Cdd:cd05944 80 YRNPGLFdnfwKLVERYRITSLSTVPTVYAALLQVPVNADISSLRFAMSGAAPLPVELRARFEDATGLPVVEGYGLTEAT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 353 HIF-ISSAGGEARTGAIGKVVPGYTAKVVDDDGN-----EVPRGTVGKLAVIGPT---GCKYLDDPRQAkYVKDGWNYPG 423
Cdd:cd05944 160 CLVaVNPPDGPKRPGSVGLRLPYARVRIKVLDGVgrllrDCAPDEVGEICVAGPGvfgGYLYTEGNKNA-FVADGWLNTG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 424 DAFTQDADGYFFYQARDDDMIITAGYNVGGPEVEDALLRHPAVAECGVIGVPDEERGMVVKAVCVLKPGHTGDAAmvkTL 503
Cdd:cd05944 239 DLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPGAVVEEE---EL 315
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 496182614 504 QDHVKATIAP-FKYPRVVEFVTALPRTETGKLQRFKLRQAAA 544
Cdd:cd05944 316 LAWARDHVPErAAVPKHIEVLEELPVTAVGKVFKPALRADAI 357
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
52-548 |
1.20e-37 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 146.25 E-value: 1.20e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 52 ERAGNI--DRP-LLRGPHRtYTYRDARTEAARIAEVLTQdHGLVPGNRVLLRGGNTVEMALAWLGTVYAGLIAVATMPLL 128
Cdd:PRK08162 25 ERAAEVypDRPaVIHGDRR-RTWAETYARCRRLASALAR-RGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 129 RAGELANIIERAQPTLALCD---GRLLAE-LAAAQDQHPVLTTIV-------PFHTATDPADLLqrAQGKPGSMQPCPTS 197
Cdd:PRK08162 103 DAASIAFMLRHGEAKVLIVDtefAEVAREaLALLPGPKPLVIDVDdpeypggRFIGALDYEAFL--ASGDPDFAWTLPAD 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 198 A-DDIALmAFTSGTTGAPKAAVHTHRDVlagceawprhVLKATPDDIVAGSPPLAFTfglggLLVFPM---------W-- 265
Cdd:PRK08162 181 EwDAIAL-NYTSGTTGNPKGVVYHHRGA----------YLNALSNILAWGMPKHPVY-----LWTLPMfhcngwcfpWtv 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 266 ---AGASVYFpdQPYTPETMVTLMRDAGVTISYTAPTFYRQM--APFAKKIGLPQLRICVSAGEGLPDATRQLWKDAtGI 340
Cdd:PRK08162 245 aarAGTNVCL--RKVDPKLIFDLIREHGVTHYCGAPIVLSALinAPAEWRAGIDHPVHAMVAGAAPPAAVIAKMEEI-GF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 341 DMTDGIGATEMF-HIFISSAGGE-------------ARTGAIGKVVPGYTakVVD-DDGNEVPRG--TVGKLAVIGPTGC 403
Cdd:PRK08162 322 DLTHVYGLTETYgPATVCAWQPEwdalplderaqlkARQGVRYPLQEGVT--VLDpDTMQPVPADgeTIGEIMFRGNIVM 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 404 K-YLDDPR-QAKYVKDGWNYPGDAFTQDADGYFFYQARDDDMIITAGYNVGGPEVEDALLRHPAVAECGVIGVPDEERGM 481
Cdd:PRK08162 400 KgYLKNPKaTEEAFAGGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDPKWGE 479
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496182614 482 VVKAVCVLKPGHTGDAAmvkTLQDHVKATIAPFKYPRVVEFvTALPRTETGKLQRFKLRQAAATPQA 548
Cdd:PRK08162 480 VPCAFVELKDGASATEE---EIIAHCREHLAGFKVPKAVVF-GELPKTSTGKIQKFVLREQAKSLKA 542
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
63-539 |
1.82e-37 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 145.14 E-value: 1.82e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 63 RGPHRT--------YTYRDARTEAARIAEVLTQDhGLVPGNRV--LLRGGNTVEMALAWLGTVYAGLIAVATMplLRAGE 132
Cdd:PRK13383 47 RWPGRTaiidddgaLSYRELQRATESLARRLTRD-GVAPGRAVgvMCRNGRGFVTAVFAVGLLGADVVPISTE--FRSDA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 133 LANIIERAQPTLALCDGRLLAELAAAQDQHPVLttivpfhtatDPADLLQRAQGKpgsmQPCPTSADDIALMafTSGTTG 212
Cdd:PRK13383 124 LAAALRAHHISTVVADNEFAERIAGADDAVAVI----------DPATAGAEESGG----RPAVAAPGRIVLL--TSGTTG 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 213 APKAaVHTHRDVLAGCEAW----PRHVLKATPDDIVAgsPPLAFTFGLGgLLVFPMWAGASV----YFPDQPYTPETmvT 284
Cdd:PRK13383 188 KPKG-VPRAPQLRSAVGVWvtilDRTRLRTGSRISVA--MPMFHGLGLG-MLMLTIALGGTVlthrHFDAEAALAQA--S 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 285 LMRDAGVTISYTAPTFYRQMAPFAK-KIGLPQLRICVSAGEGLPDATRQLWKDATGIDMTDGIGATEMfHIFISSAGGEA 363
Cdd:PRK13383 262 LHRADAFTAVPVVLARILELPPRVRaRNPLPQLRVVMSSGDRLDPTLGQRFMDTYGDILYNGYGSTEV-GIGALATPADL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 364 RTG--AIGKVVPGYTAKVVDDDGNEVPRGTVGKLAVIGP-TGCKYLDDprQAKYVKDGWNYPGDAFTQDADGYFFYQARD 440
Cdd:PRK13383 341 RDApeTVGKPVAGCPVRILDRNNRPVGPRVTGRIFVGGElAGTRYTDG--GGKAVVDGMTSTGDMGYLDNAGRLFIVGRE 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 441 DDMIITAGYNVGGPEVEDALLRHPAVAECGVIGVPDEERGMVVKAVCVLKPGHTGDAAmvkTLQDHVKATIAPFKYPRVV 520
Cdd:PRK13383 419 DDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPGSGVDAA---QLRDYLKDRVSRFEQPRDI 495
|
490
....*....|....*....
gi 496182614 521 EFVTALPRTETGKLQRFKL 539
Cdd:PRK13383 496 NIVSSIPRNPTGKVLRKEL 514
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
64-544 |
3.24e-37 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 146.05 E-value: 3.24e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 64 GPHRTYTYRDARTEAARIAEVLTqDHGLVPGNRVLLRGGNTVEMALAWLG---------TVYAGLIAVAtmpllrageLA 134
Cdd:PRK00174 94 GDSRKITYRELHREVCRFANALK-SLGVKKGDRVAIYMPMIPEAAVAMLAcarigavhsVVFGGFSAEA---------LA 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 135 NIIERAQPTLALC-D-----GRLLAeLAAAQDQ-----HPVLTTIVPFHTATDPA----------DLLQRAqgkPGSMQP 193
Cdd:PRK00174 164 DRIIDAGAKLVITaDegvrgGKPIP-LKANVDEalancPSVEKVIVVRRTGGDVDwvegrdlwwhELVAGA---SDECEP 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 194 CPTSADDIALMAFTSGTTGAPKAAVHTHRDVLAGCEAWPRHVLKATPDD----------------IVAGspPLAftfgLG 257
Cdd:PRK00174 240 EPMDAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAAMTMKYVFDYKDGDvywctadvgwvtghsyIVYG--PLA----NG 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 258 GLLVfpMWAGAsvyfPDQPyTPETMVTLMRDAGVTISYTAPT----FYRQMAPFAKKIGLPQLRICVSAGEGL-PDATRQ 332
Cdd:PRK00174 314 ATTL--MFEGV----PNYP-DPGRFWEVIDKHKVTIFYTAPTairaLMKEGDEHPKKYDLSSLRLLGSVGEPInPEAWEW 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 333 LWKDatgidmtdgIGA-----------TEMFHIFISSAGGEART--GAIGKVVPGYTAKVVDDDGNEVPRGTVGKLAVIG 399
Cdd:PRK00174 387 YYKV---------VGGercpivdtwwqTETGGIMITPLPGATPLkpGSATRPLPGIQPAVVDEEGNPLEGGEGGNLVIKD 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 400 P------TgcKYLDDPRqakYVKDGWN-YPGDAFT-----QDADGYFFYQARDDDMIITAGYNVGGPEVEDALLRHPAVA 467
Cdd:PRK00174 458 PwpgmmrT--IYGDHER---FVKTYFStFKGMYFTgdgarRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVA 532
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496182614 468 ECGVIGVPDEERGMVVKAVCVLKPGHTGDAAMVKTLQDHVKATIAPFKYPRVVEFVTALPRTETGKLQRFKLRQAAA 544
Cdd:PRK00174 533 EAAVVGRPDDIKGQGIYAFVTLKGGEEPSDELRKELRNWVRKEIGPIAKPDVIQFAPGLPKTRSGKIMRRILRKIAE 609
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
42-536 |
5.24e-37 |
|
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341301 [Multi-domain] Cd Length: 488 Bit Score: 143.18 E-value: 5.24e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 42 HALFdqAERAERAGniDRPLLRGPHRTYTYRDARTEAARIAEVLTQdHGLVPGNRVLLRGGNTVEMALAWLGTVYAGLIA 121
Cdd:cd17646 1 HALV--AEQAARTP--DAPAVVDEGRTLTYRELDERANRLAHLLRA-RGVGPEDRVAVLLPRSADLVVALLAVLKAGAAY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 122 VATMPLLRAGELANIIERAQPTLALCDGRLLAELAAAqdqhPVLTTIVPFHTATDPADLLQRaqgkpgsmqpcPTSADDI 201
Cdd:cd17646 76 LPLDPGYPADRLAYMLADAGPAVVLTTADLAARLPAG----GDVALLGDEALAAPPATPPLV-----------PPRPDNL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 202 ALMAFTSGTTGAPKAAVHTHRDVlAGCEAWPRHVLKATPDDIVAGSPPLAFTFGLGGLLVfPMWAGASVYF--PDQPYTP 279
Cdd:cd17646 141 AYVIYTSGSTGRPKGVMVTHAGI-VNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFW-PLVAGARLVVarPGGHRDP 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 280 ETMVTLMRDAGVTISYTAPTFYRQMAPFAKKIGLPQLRICVSAGEGLPDATRQLWKDATGIDMTDGIGATE----MFHiF 355
Cdd:cd17646 219 AYLAALIREHGVTTCHFVPSMLRVFLAEPAAGSCASLRRVFCSGEALPPELAARFLALPGAELHNLYGPTEaaidVTH-W 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 356 ISSAGGEARTGAIGKVVPGYTAKVVDDDGNEVPRGTVGKLAVIG-PTGCKYLDDPRQ--AKYVKDGWN-----Y-PGDAF 426
Cdd:cd17646 298 PVRGPAETPSVPIGRPVPNTRLYVLDDALRPVPVGVPGELYLGGvQLARGYLGRPALtaERFVPDPFGpgsrmYrTGDLA 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 427 TQDADGYFFYQARDDDMIITAGYNVGGPEVEDALLRHPAVAECGVIGVPDEERGMVVKAVCVLKPGHTG-DAAmvkTLQD 505
Cdd:cd17646 378 RWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAAGAAGpDTA---ALRA 454
|
490 500 510
....*....|....*....|....*....|.
gi 496182614 506 HVKATIAPFKYPRVVEFVTALPRTETGKLQR 536
Cdd:cd17646 455 HLAERLPEYMVPAAFVVLDALPLTANGKLDR 485
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
67-542 |
5.79e-37 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 143.69 E-value: 5.79e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 67 RTYTYRDARTEAARIAEVLtQDHGLVPGNRV--LLRGGNTV-EMALAwlgtvyAGLIAVATMPL---LRAGELANIIERA 140
Cdd:PRK12406 10 RRRSFDELAQRAARAAGGL-AALGVRPGDCValLMRNDFAFfEAAYA------AMRLGAYAVPVnwhFKPEEIAYILEDS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 141 QPTLALCDGRLLAELAAAQDQH-PVLTTIVPFHTAT----DPADLLQRA----------QGKP--GSMQPCPTSaddial 203
Cdd:PRK12406 83 GARVLIAHADLLHGLASALPAGvTVLSVPTPPEIAAayriSPALLTPPAgaidwegwlaQQEPydGPPVPQPQS------ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 204 MAFTSGTTGAPK-----------AAVHTHRDVLAgceawprHVLKATPDDIVAG----SPPLAF---TFGLGGLLVFpmw 265
Cdd:PRK12406 157 MIYTSGTTGHPKgvrraaptpeqAAAAEQMRALI-------YGLKPGIRALLTGplyhSAPNAYglrAGRLGGVLVL--- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 266 agasvyfpdQP-YTPETMVTLMRDAGVTISYTAPT-FYRQM---APFAKKIGLPQLRICVSAGEGLPDATRQLWKDATGI 340
Cdd:PRK12406 227 ---------QPrFDPEELLQLIERHRITHMHMVPTmFIRLLklpEEVRAKYDVSSLRHVIHAAAPCPADVKRAMIEWWGP 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 341 DMTDGIGATEMFHI-FISSAGGEARTGAIGKVVPGYTAKVVDDDGNEVPRGTVGKLAV--IGPTGCKYLDDP-RQAKYVK 416
Cdd:PRK12406 298 VIYEYYGSTESGAVtFATSEDALSHPGTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSriAGNPDFTYHNKPeKRAEIDR 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 417 DGWNYPGDAFTQDADGYFFYQARDDDMIITAGYNVGGPEVEDALLRHPAVAECGVIGVPDEERGMVVKAVCVLKPGHTGD 496
Cdd:PRK12406 378 GGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPGATLD 457
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 496182614 497 AAMVKTlqdHVKATIAPFKYPRVVEFVTALPRTETGKLQRFKLRQA 542
Cdd:PRK12406 458 EADIRA---QLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLRDP 500
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
37-536 |
2.75e-36 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 143.17 E-value: 2.75e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 37 QANLVHALFDQ--AERAERAGNIDRPLLRGPHRTYTYRDARTEAARIAEVLtQDHGLVPGNRVLLRGGNTVEMALAWLGT 114
Cdd:PRK10524 51 RTNLCHNAVDRhlAKRPEQLALIAVSTETDEERTYTFRQLHDEVNRMAAML-RSLGVQRGDRVLIYMPMIAEAAFAMLAC 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 115 VYAGLIAVATMPLLRAGELANIIERAQPTLALC-DG-----------RLLAElAAAQDQHP---VLTT---IVPFHTAT- 175
Cdd:PRK10524 130 ARIGAIHSVVFGGFASHSLAARIDDAKPVLIVSaDAgsrggkvvpykPLLDE-AIALAQHKprhVLLVdrgLAPMARVAg 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 176 ---DPADLlqRAQGKpGSMQPCP-TSADDIALMAFTSGTTGAPKAAvhtHRDVLAGCEAwprhvLKATPDDIVAGSPPLA 251
Cdd:PRK10524 209 rdvDYATL--RAQHL-GARVPVEwLESNEPSYILYTSGTTGKPKGV---QRDTGGYAVA-----LATSMDTIFGGKAGET 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 252 F--TFGLG-----GLLVF-PMWAG-ASVYFPDQPYTPETMV--TLMRDAGVTISYTAPTFYR----QMAPFAKKIGLPQL 316
Cdd:PRK10524 278 FfcASDIGwvvghSYIVYaPLLAGmATIMYEGLPTRPDAGIwwRIVEKYKVNRMFSAPTAIRvlkkQDPALLRKHDLSSL 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 317 RICVSAGEGLPDATRQLWKDATGIDMTDGIGATEMFHIFISSAGG----EARTGAIGKVVPGYTAKVVDD-DGNEVPRGT 391
Cdd:PRK10524 358 RALFLAGEPLDEPTASWISEALGVPVIDNYWQTETGWPILAIARGvedrPTRLGSPGVPMYGYNVKLLNEvTGEPCGPNE 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 392 VGKLAVIGPT--GCK---YLDDPRqakYVKDGWNYPG-------DAFTQDADGYFFYQARDDDMIITAGYNVGGPEVEDA 459
Cdd:PRK10524 438 KGVLVIEGPLppGCMqtvWGDDDR---FVKTYWSLFGrqvystfDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEES 514
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 460 LLRHPAVAECGVIGVPDEERGMVVKAVCVLKPGHTGD-----AAMVKTLQDHVKATIAPFKYPRVVEFVTALPRTETGKL 534
Cdd:PRK10524 515 ISSHPAVAEVAVVGVKDALKGQVAVAFVVPKDSDSLAdrearLALEKEIMALVDSQLGAVARPARVWFVSALPKTRSGKL 594
|
..
gi 496182614 535 QR 536
Cdd:PRK10524 595 LR 596
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
40-553 |
4.23e-36 |
|
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: 144.23 E-value: 4.23e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 40 LVHALFdqAERAERAGniDRPLLRGPHRTYTYRDARTEAARIAEVLtQDHGLVPGNRVLLRGGNTVEMALAWLGTVYAGl 119
Cdd:COG1020 477 TLHELF--EAQAARTP--DAVAVVFGDQSLTYAELNARANRLAHHL-RALGVGPGDLVGVCLERSLEMVVALLAVLKAG- 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 120 iAV-----ATMPLLRageLANIIERAQPTLALCDGRLLAELAAAQDQHPVLttivpfhtatDPADLLQRAQGKPgsmqPC 194
Cdd:COG1020 551 -AAyvpldPAYPAER---LAYMLEDAGARLVLTQSALAARLPELGVPVLAL----------DALALAAEPATNP----PV 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 195 PTSADDIALMAFTSGTTGAPKAAVHTHRDVLAGCEAWpRHVLKATPDDIVAGSPPLAFTFGLGGLLVfPMWAGASVYF-- 272
Cdd:COG1020 613 PVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWM-QRRYGLGPGDRVLQFASLSFDASVWEIFG-ALLSGATLVLap 690
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 273 PDQPYTPETMVTLMRDAGVTISYTAPTFYRQMAPFAKKiGLPQLRICVSAGEGLPDAT-RQLWKDATGIDMTDGIGATEm 351
Cdd:COG1020 691 PEARRDPAALAELLARHRVTVLNLTPSLLRALLDAAPE-ALPSLRLVLVGGEALPPELvRRWRARLPGARLVNLYGPTE- 768
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 352 FHIF-----ISSAGGEARTGAIGKVVPGYTAKVVDDDGNEVPRGTVGKLAVIGPT---GckYLDDPRQ--AKYVKDGWNY 421
Cdd:COG1020 769 TTVDstyyeVTPPDADGGSVPIGRPIANTRVYVLDAHLQPVPVGVPGELYIGGAGlarG--YLNRPELtaERFVADPFGF 846
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 422 P-------GDAFTQDADGYFFYQARDDDMIITAGYNV--GgpEVEDALLRHPAVAECGVIGVPDEERGMVVKAVCVLKPG 492
Cdd:COG1020 847 PgarlyrtGDLARWLPDGNLEFLGRADDQVKIRGFRIelG--EIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAG 924
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496182614 493 HTGDAAmvkTLQDHVKATIAPFKYPRVVEFVTALPRTETGKLQRFKLRQAAATPQAEVKAP 553
Cdd:COG1020 925 AAAAAA---LLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALPAPAAAAAAAAAAP 982
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
58-536 |
4.34e-36 |
|
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: 140.14 E-value: 4.34e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 58 DRPLLRGPHRTYTYRDARTEAARIAEVLtQDHGLVPGNRVLLRGGNTVEMALAWLGTVYAGliaVATMPLlragELANII 137
Cdd:cd17643 2 EAVAVVDEDRRLTYGELDARANRLARTL-RAEGVGPGDRVALALPRSAELIVALLAILKAG---GAYVPI----DPAYPV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 138 ERAQPTLAlcdgrllaelaaaqDQHPVLttivpfhtatdpadLLqraqgkpgsmqpcpTSADDIALMAFTSGTTGAPKAA 217
Cdd:cd17643 74 ERIAFILA--------------DSGPSL--------------LL--------------TDPDDLAYVIYTSGSTGRPKGV 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 218 VHTHRDV---LAGCEAWprhvLKATPDDIVAGSPPLAFTFGlggllVFPMWA----GASVYFP--DQPYTPETMVTLMRD 288
Cdd:cd17643 112 VVSHANVlalFAATQRW----FGFNEDDVWTLFHSYAFDFS-----VWEIWGallhGGRLVVVpyEVARSPEDFARLLRD 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 289 AGVTISYTAPTFYRQMAPFAK--KIGLPQLRICVSAGEGLPDATRQLWKDATGIDMTDGI---GATEM-----FHIFISS 358
Cdd:cd17643 183 EGVTVLNQTPSAFYQLVEAADrdGRDPLALRYVIFGGEALEAAMLRPWAGRFGLDRPQLVnmyGITETtvhvtFRPLDAA 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 359 AGGEARTGAIGKVVPGYTAKVVDDDGNEVPRGTVGKLAVIGPTGCK-YLDDPRQA--KYVKDGWNYP-------GDAFTQ 428
Cdd:cd17643 263 DLPAAAASPIGRPLPGLRVYVLDADGRPVPPGVVGELYVSGAGVARgYLGRPELTaeRFVANPFGGPgsrmyrtGDLARR 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 429 DADGYFFYQARDDDMIITAGYNVGGPEVEDALLRHPAVAECGVIGVPDEERGMVVKAVCVLKPGHTGDAAMVKTlqdHVK 508
Cdd:cd17643 343 LPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVADDGAAADIAELRA---LLK 419
|
490 500
....*....|....*....|....*...
gi 496182614 509 ATIAPFKYPRVVEFVTALPRTETGKLQR 536
Cdd:cd17643 420 ELLPDYMVPARYVPLDALPLTVNGKLDR 447
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
68-537 |
5.06e-36 |
|
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: 140.27 E-value: 5.06e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 68 TYTYRDARTEAARIAEVLtQDHGLVPGNRVLLRGGNTVEMALAWLGTVYAGLIAVATMPLLRAGELANIIERAQPTLALC 147
Cdd:cd05914 7 PLTYKDLADNIAKFALLL-KINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 148 dgrllaelaaaqdqhpvlttivpfhtaTDPadllqraqgkpgsmqpcptsaDDIALMAFTSGTTGAPKAAVHTHRDVLAG 227
Cdd:cd05914 86 ---------------------------SDE---------------------DDVALINYTSGTTGNSKGVMLTYRNIVSN 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 228 CEAWpRHVLKATPDDIVAGSPPLAFTFGLGGLLVFPMWAGASVYFPDQPYTPetMVTLMRDAGVTISYTAPTFYrQMAPF 307
Cdd:cd05914 118 VDGV-KEVVLLGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFLDKIPSA--KIIALAFAQVTPTLGVPVPL-VIEKI 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 308 AKKIGLPQ----------------------------------LRICVSAGEGL-PDATRQLWKdaTGIDMTDGIGATEMF 352
Cdd:cd05914 194 FKMDIIPKltlkkfkfklakkinnrkirklafkkvheafggnIKEFVIGGAKInPDVEEFLRT--IGFPYTIGYGMTETA 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 353 HIFISSAGGEARTGAIGKVVPGYTAKVVDDDgnevPRGTVGKLAVIGPTGCK-YLDDPR--QAKYVKDGWNYPGDAFTQD 429
Cdd:cd05914 272 PIISYSPPNRIRLGSAGKVIDGVEVRIDSPD----PATGEGEIIVRGPNVMKgYYKNPEatAEAFDKDGWFHTGDLGKID 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 430 ADGYFFYQARDDDMIIT-AGYNVGGPEVEDALLRHPAVAECGVIGVPDEERGMVVKAVCVLKPGHTGDAAMVKTLQDHVK 508
Cdd:cd05914 348 AEGYLYIRGRKKEMIVLsSGKNIYPEEIEAKINNMPFVLESLVVVQEKKLVALAYIDPDFLDVKALKQRNIIDAIKWEVR 427
|
490 500 510
....*....|....*....|....*....|....*
gi 496182614 509 ATI---APfKYPRVVEFV---TALPRTETGKLQRF 537
Cdd:cd05914 428 DKVnqkVP-NYKKISKVKivkEEFEKTPKGKIKRF 461
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
51-540 |
1.09e-35 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 140.20 E-value: 1.09e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 51 AERAGnIDRPLLRGPHRTYTYRDARTEAARIAEVLTQ--DHGLVPGNRVLLrgGNTVEMALAWLGTVYAGLIAVATMPLL 128
Cdd:PRK07867 12 LPLAE-DDDRGLYFEDSFTSWREHIRGSAARAAALRArlDPTRPPHVGVLL--DNTPEFSLLLGAAALSGIVPVGLNPTR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 129 RAGELANIIERAQPTLALCDGRLLAELAAAQDQHPVLTTIVPFHtatdpADLLQRAQGKPGSmqPCPTSADDIALMAFTS 208
Cdd:PRK07867 89 RGAALARDIAHADCQLVLTESAHAELLDGLDPGVRVINVDSPAW-----ADELAAHRDAEPP--FRVADPDDLFMLIFTS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 209 GTTGAPKAAVHTHRDVlagceAWPRHVLKA----TPDDIVAGSPPL--------AFTFGL--GGLLVFPMWAGASVYFPD 274
Cdd:PRK07867 162 GTSGDPKAVRCTHRKV-----ASAGVMLAQrfglGPDDVCYVSMPLfhsnavmaGWAVALaaGASIALRRKFSASGFLPD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 275 qpyTPETMVTLMRDAGVTISYTAPTfyrqmapfakkiglPQ--------LRIcVSAGEGLPDATRQlWKDATGIDMTDGI 346
Cdd:PRK07867 237 ---VRRYGATYANYVGKPLSYVLAT--------------PErpddadnpLRI-VYGNEGAPGDIAR-FARRFGCVVVDGF 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 347 GATEMFHIFISSAGGeaRTGAIGKVVPGytAKVVD-DDGNEVPRG------------TVGKLA-VIGPTGCK-YLDDPR- 410
Cdd:PRK07867 298 GSTEGGVAITRTPDT--PPGALGPLPPG--VAIVDpDTGTECPPAedadgrllnadeAIGELVnTAGPGGFEgYYNDPEa 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 411 QAKYVKDGWNYPGDAFTQDADGYFFYQARDDDMIITAGYNVGGPEVEDALLRHPAVAECGVIGVPDEERGMVVKAVCVLK 490
Cdd:PRK07867 374 DAERMRGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVMAALVLA 453
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 496182614 491 PGHTGDAAMVkTLQDHVKATIAPFKYPRVVEFVTALPRTETGKLQRFKLR 540
Cdd:PRK07867 454 PGAKFDPDAF-AEFLAAQPDLGPKQWPSYVRVCAELPRTATFKVLKRQLS 502
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
40-541 |
2.07e-35 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 139.50 E-value: 2.07e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 40 LVHALFDQAERAERAGNIDRPLLRGP-HRTyTYRDARTEAARIAEVLTQDhGLVPGNRVLLRGGNTVEMALAWLGTVYAG 118
Cdd:PRK06018 11 LCHRIIDHAARIHGNREVVTRSVEGPiVRT-TYAQIHDRALKVSQALDRD-GIKLGDRVATIAWNTWRHLEAWYGIMGIG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 119 LIAVATMPLLRAGELANIIERAQPTLALCDGRLLAELAAAQDQHP-VLTTIVPFHTATDPADLLQRA-------QGKPGS 190
Cdd:PRK06018 89 AICHTVNPRLFPEQIAWIINHAEDRVVITDLTFVPILEKIADKLPsVERYVVLTDAAHMPQTTLKNAvayeewiAEADGD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 191 MQPCPTSADDIALMAFTSGTTGAPKAAVHTHR-DVLAGCEAWPRHVLKATPDDIV--------AGSPPLAFTF-GLGGLL 260
Cdd:PRK06018 169 FAWKTFDENTAAGMCYTSGTTGDPKGVLYSHRsNVLHALMANNGDALGTSAADTMlpvvplfhANSWGIAFSApSMGTKL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 261 VFP--MWAGASVYfpdqpytpetmvTLMRDAGVTISYTAPTFYRQMAPFAKKIG--LPQLRICVSAGEGLPDATRQLWKD 336
Cdd:PRK06018 249 VMPgaKLDGASVY------------ELLDTEKVTFTAGVPTVWLMLLQYMEKEGlkLPHLKMVVCGGSAMPRSMIKAFED 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 337 aTGIDMTDGIGATEMFHI--------FISSAGGEARTGAI---GKVVPGYTAKVVDDDGNEVPRG--TVGKLAVIGPT-- 401
Cdd:PRK06018 317 -MGVEVRHAWGMTEMSPLgtlaalkpPFSKLPGDARLDVLqkqGYPPFGVEMKITDDAGKELPWDgkTFGRLKVRGPAva 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 402 ------GCKYLDDprqakyvkDGWNYPGDAFTQDADGYFFYQARDDDMIITAGYNVGGPEVEDALLRHPAVAECGVIGVP 475
Cdd:PRK06018 396 aayyrvDGEILDD--------DGFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVY 467
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496182614 476 D---EERGMVvkaVCVLKPGHTgdaAMVKTLQDHVKATIAPFKYPRVVEFVTALPRTETGKLQRFKLRQ 541
Cdd:PRK06018 468 HpkwDERPLL---IVQLKPGET---ATREEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALRE 530
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
56-540 |
3.43e-35 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 138.48 E-value: 3.43e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 56 NIDRPLL--RGPHRTYTYRDARTEAAriAEVLtQDHGLVPGNRVLLRGGNT---VEMALAwlgTVYAGLIAVATMPLLRA 130
Cdd:PRK06145 15 TPDRAALvyRDQEISYAEFHQRILQA--AGML-HARGIGQGDVVALLMKNSaafLELAFA---ASYLGAVFLPINYRLAA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 131 GELANIIERAQPTLALCDGRLLAELAAaqdQHPVLTTivpfhTATDPADLLQRAQGKPGSMQPCPTSADDIALMAFTSGT 210
Cdd:PRK06145 89 DEVAYILGDAGAKLLLVDEEFDAIVAL---ETPKIVI-----DAAAQADSRRLAQGGLEIPPQAAVAPTDLVRLMYTSGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 211 TGAPKAAVHTHRDVlagceAWPR--HV--LKATPDD--IVAGSPPLAFTFGLGGLLVfpMWAGASVYFpDQPYTPETMVT 284
Cdd:PRK06145 161 TDRPKGVMHSYGNL-----HWKSidHViaLGLTASErlLVVGPLYHVGAFDLPGIAV--LWVGGTLRI-HREFDPEAVLA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 285 LMRDAGVTISYTAPTFYRQM--APFAKKIGLPQLRICVSAGEGLPDA-TRQLWKDATGIDMTDGIGATEmfhifisSAGG 361
Cdd:PRK06145 233 AIERHRLTCAWMAPVMLSRVltVPDRDRFDLDSLAWCIGGGEKTPESrIRDFTRVFTRARYIDAYGLTE-------TCSG 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 362 EA---------RTGAIGKVVPGYTAKVVDDDGNEVPRGTVGKLAVIGPTGCK-YLDDP-RQAKYVKDGWNYPGDAFTQDA 430
Cdd:PRK06145 306 DTlmeagreieKIGSTGRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKgYWKDPeKTAEAFYGDWFRSGDVGYLDE 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 431 DGYFFYQARDDDMIITAGYNVGGPEVEDALLRHPAVAECGVIGVPDEERGMVVKAVCVLKPGHTgdaAMVKTLQDHVKAT 510
Cdd:PRK06145 386 EGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPGAT---LTLEALDRHCRQR 462
|
490 500 510
....*....|....*....|....*....|
gi 496182614 511 IAPFKYPRVVEFVTALPRTETGKLQRFKLR 540
Cdd:PRK06145 463 LASFKVPRQLKVRDELPRNPSGKVLKRVLR 492
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
33-541 |
6.99e-35 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 137.92 E-value: 6.99e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 33 QIPDQANLVHALFDQAERAERAGNIDRPLLRGP-HRtYTYRDARTEAARIAEVLTQdHGLVPGNRVLLRGGNTVEMALAW 111
Cdd:PRK07008 4 QMMDMPLLISSLIAHAARHAGDTEIVSRRVEGDiHR-YTYRDCERRAKQLAQALAA-LGVEPGDRVGTLAWNGYRHLEAY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 112 LGTVYAGLIAVATMPLLRAGELANIIERAQPTLALCDgrlLAELAAAQDQHPVLTTIVPFHTATD----PAD---LL--- 181
Cdd:PRK07008 82 YGVSGSGAVCHTINPRLFPEQIAYIVNHAEDRYVLFD---LTFLPLVDALAPQCPNVKGWVAMTDaahlPAGstpLLcye 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 182 QRAQGKPGSMQPCPTSADDIALMAFTSGTTGAPKAAVHTHRD-VLAGCEAWPRHVLKATPDDIVAGSPPL--AFTFGL-- 256
Cdd:PRK07008 159 TLVGAQDGDYDWPRFDENQASSLCYTSGTTGNPKGALYSHRStVLHAYGAALPDAMGLSARDAVLPVVPMfhVNAWGLpy 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 257 -----GGLLVFPMWA--GASVYfpdqpytpetmvTLMRDAGVTISYTAPTFYRQMAPFAKKIGL--PQLRICVSAGEGLP 327
Cdd:PRK07008 239 sapltGAKLVLPGPDldGKSLY------------ELIEAERVTFSAGVPTVWLGLLNHMREAGLrfSTLRRTVIGGSACP 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 328 DATRQLWKDATGIDMTDGIGATEMF-----------HIFISSAGGEARTGAIGKVVPGYTAKVVDDDGNEVPRGTV--GK 394
Cdd:PRK07008 307 PAMIRTFEDEYGVEVIHAWGMTEMSplgtlcklkwkHSQLPLDEQRKLLEKQGRVIYGVDMKIVGDDGRELPWDGKafGD 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 395 LAVIGP-TGCKYLDdpRQAKYVKDGWNYPGDAFTQDADGYFFYQARDDDMIITAGYNVGGPEVEDALLRHPAVAECGVIG 473
Cdd:PRK07008 387 LQVRGPwVIDRYFR--GDASPLVDGWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIA 464
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496182614 474 VP----DEERGMVVkavcVLKPG-HTGDAAMVKtlqdHVKATIAPFKYPRVVEFVTALPRTETGKLQRFKLRQ 541
Cdd:PRK07008 465 CAhpkwDERPLLVV----VKRPGaEVTREELLA----FYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKLRE 529
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
67-540 |
7.09e-35 |
|
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: 136.73 E-value: 7.09e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 67 RTYTYRDARTEAARIAEVLTQdHGLVPGNRVLLRGGNTVEMALAWLGTVYAGLIAVATMPLLRAGELANIIERAQPTLAL 146
Cdd:cd17649 11 QSLSYAELDARANRLAHRLRA-LGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYMLEDSGAGLLL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 147 CdgrllaelaaaqdQHPvlttivpfhtatdpadllqraqgkpgsmqpcptsaDDIALMAFTSGTTGAPKAAVHTHRDVLA 226
Cdd:cd17649 90 T-------------HHP-----------------------------------RQLAYVIYTSGSTGTPKGVAVSHGPLAA 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 227 GCEAwPRHVLKATPDDIVAGSPPLAFTFGLGGLLVfPMWAGASVYFPDQP--YTPETMVTLMRDAGVTISYTAPTFYRQM 304
Cdd:cd17649 122 HCQA-TAERYGLTPGDRELQFASFNFDGAHEQLLP-PLICGACVVLRPDElwASADELAEMVRELGVTVLDLPPAYLQQL 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 305 APFAKKIG---LPQLRICVSAGEGLPDATRQLWKdATGIDMTDGIGATE------MFHIfissAGGEARTGA---IGKVV 372
Cdd:cd17649 200 AEEADRTGdgrPPSLRLYIFGGEALSPELLRRWL-KAPVRLFNAYGPTEatvtplVWKC----EAGAARAGAsmpIGRPL 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 373 PGYTAKVVDDDGNEVPRGTVGKLAVIGPTGCK-YLDDPRQ--AKYVKDGWNYP-------GDAFTQDADGYFFYQARDDD 442
Cdd:cd17649 275 GGRSAYILDADLNPVPVGVTGELYIGGEGLARgYLGRPELtaERFVPDPFGAPgsrlyrtGDLARWRDDGVIEYLGRVDH 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 443 MIITAGYNVGGPEVEDALLRHPAVAECGVIGVPDEERGMVVkAVCVLKPGHTGdAAMVKTLQDHVKATIAPFKYPRVVEF 522
Cdd:cd17649 355 QVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAGGKQLV-AYVVLRAAAAQ-PELRAQLRTALRASLPDYMVPAHLVF 432
|
490
....*....|....*...
gi 496182614 523 VTALPRTETGKLQRFKLR 540
Cdd:cd17649 433 LARLPLTPNGKLDRKALP 450
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
197-533 |
7.46e-35 |
|
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: 134.82 E-value: 7.46e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 197 SADDIaLMAFTSGTTGAPKAAVHTHRD---VLAG----------CEAWPRHVLKATPDDIVAGSPPL-------AFTFGL 256
Cdd:cd05924 2 SADDL-YILYTGGTTGMPKGVMWRQEDifrMLMGgadfgtgeftPSEDAHKAAAAAAGTVMFPAPPLmhgtgswTAFGGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 257 GGllvfpmwaGASVYFPDQPYTPETMVTLMRDAGVT-ISYTAPTFYRQMAPFAKKIG---LPQLRICVSAGEGLPDATRQ 332
Cdd:cd05924 81 LG--------GQTVVLPDDRFDPEEVWRTIEKHKVTsMTIVGDAMARPLIDALRDAGpydLSSLFAISSGGALLSPEVKQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 333 -LWKDATGIDMTDGIGATEM-FHIFISSAGGEARTGAIGKVVPGYTakVVDDDGNEVP--RGTVGKLAVIG--PTGckYL 406
Cdd:cd05924 153 gLLELVPNITLVDAFGSSETgFTGSGHSAGSGPETGPFTRANPDTV--VLDDDGRVVPpgSGGVGWIARRGhiPLG--YY 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 407 DDPRQAK---YVKDG--WNYPGDAFTQDADGYFFYQARDDDMIITAGYNVGGPEVEDALLRHPAVAECGVIGVPDEERGM 481
Cdd:cd05924 229 GDEAKTAetfPEVDGvrYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQ 308
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 496182614 482 VVKAVCVLKPGHTGDAAmvkTLQDHVKATIAPFKYPRVVEFVTALPRTETGK 533
Cdd:cd05924 309 EVVAVVQLREGAGVDLE---ELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
200-541 |
1.31e-34 |
|
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: 133.23 E-value: 1.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 200 DIALMAFTSGTTGAPKAAVHTHRDVLAGCEAWPRHVLKATPDDIVAGSPPlaftFGLGGL--LVFPMWAGASVYFPDqpY 277
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPL----YHVGGLaiLVRSLLAGAELVLLE--R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 278 TPETMVTLMRDAGVTISYTAPTFYRQMAPFAKKIGLPQLRICVSAGEGLPDATRQLWKDAtGIDMTDGIGATEM-FHIFI 356
Cdd:cd17630 75 NQALAEDLAPPGVTHVSLVPTQLQRLLDSGQGPAALKSLRAVLLGGAPIPPELLERAADR-GIPLYTTYGMTETaSQVAT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 357 SSAGGEARTGAiGKVVPGYTAKVVDDdgnevprgtvGKLAVIGPTGCK-YLDDPRQAKYVKDGWNYPGDAFTQDADGYFF 435
Cdd:cd17630 154 KRPDGFGRGGV-GVLLPGRELRIVED----------GEIWVGGASLAMgYLRGQLVPEFNEDGWFTTKDLGELHADGRLT 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 436 YQARDDDMIITAGYNVGGPEVEDALLRHPAVAECGVIGVPDEERGMVVKAVCVLKPGHTgdaamVKTLQDHVKATIAPFK 515
Cdd:cd17630 223 VLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRGPAD-----PAELRAWLKDKLARFK 297
|
330 340
....*....|....*....|....*.
gi 496182614 516 YPRVVEFVTALPRTETGKLQRFKLRQ 541
Cdd:cd17630 298 LPKRIYPVPELPRTGGGKVDRRALRA 323
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
33-478 |
1.44e-34 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 137.92 E-value: 1.44e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 33 QIPDQANLVHALFDQAERAEragniDRPLLR----GPHRTYTYRDARTEAARIAEVLtQDHGLVPGNRVLLRGGNTVEMA 108
Cdd:COG1022 6 DVPPADTLPDLLRRRAARFP-----DRVALRekedGIWQSLTWAEFAERVRALAAGL-LALGVKPGDRVAILSDNRPEWV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 109 LAWLGTVYAGLIAVATMPLLRAGELANIIERAQPTLALC-DGRLLAELAAAQDQHPVLTTIVPFHTATDP--------AD 179
Cdd:COG1022 80 IADLAILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVeDQEQLDKLLEVRDELPSLRHIVVLDPRGLRddprllslDE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 180 LLQ--RAQGKPGSMQPCPTSA--DDIALMAFTSGTTGAPKAAVHTHRDVLAGCEAWPRhVLKATPDDIVAGSPPLAFTFG 255
Cdd:COG1022 160 LLAlgREVADPAELEARRAAVkpDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLE-RLPLGPGDRTLSFLPLAHVFE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 256 lGGLLVFPMWAGASVYFPDQpytPETMVTLMRDAGVTISYTAPTFY-----------RQMAPFAKKI------------- 311
Cdd:COG1022 239 -RTVSYYALAAGATVAFAES---PDTLAEDLREVKPTFMLAVPRVWekvyagiqakaEEAGGLKRKLfrwalavgrryar 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 312 ----GLP--------------------------QLRICVSAGEGLPDATrQLWKDATGIDMTDGIGATEmfhifiSSAG- 360
Cdd:COG1022 315 arlaGKSpslllrlkhaladklvfsklrealggRLRFAVSGGAALGPEL-ARFFRALGIPVLEGYGLTE------TSPVi 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 361 -----GEARTGAIGKVVPGYTAKvVDDDGnEVprgtvgkLaVIGPTGCK-YLDDP---RQAKyVKDGWNYPGDAFTQDAD 431
Cdd:COG1022 388 tvnrpGDNRIGTVGPPLPGVEVK-IAEDG-EI-------L-VRGPNVMKgYYKNPeatAEAF-DADGWLHTGDIGELDED 456
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 496182614 432 GYFFYQARDDDMIITA-GYNVGGPEVEDALLRHPAVAECGVIG----------VPDEE 478
Cdd:COG1022 457 GFLRITGRKKDLIVTSgGKNVAPQPIENALKASPLIEQAVVVGdgrpflaaliVPDFE 514
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
40-542 |
2.93e-34 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 136.26 E-value: 2.93e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 40 LVHALFDQAERAERAGnIDRPLLRGPHRTYTYRDARTEAARIAEVLTQDhGLVPGNRVLLRGGNTVEMALAWLGTVYAGL 119
Cdd:cd05906 12 LLELLLRAAERGPTKG-ITYIDADGSEEFQSYQDLLEDARRLAAGLRQL-GLRPGDSVILQFDDNEDFIPAFWACVLAGF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 120 IAVATMPLL-------RAGELANIIERAQPTLALCDGRLLAELAA--AQDQHPVLTTIVpfhtatdpADLLQRAQGKPGS 190
Cdd:cd05906 90 VPAPLTVPPtydepnaRLRKLRHIWQLLGSPVVLTDAELVAEFAGleTLSGLPGIRVLS--------IEELLDTAADHDL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 191 MQPcptSADDIALMAFTSGTTGAPKAAVHTHRDVLAGCEAWPRHVLkATPDDIVAGSPPLAFTFGLGGLLVFPMWAGAsv 270
Cdd:cd05906 162 PQS---RPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNG-LTPQDVFLNWVPLDHVGGLVELHLRAVYLGC-- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 271 yfpDQPYTP-ETMVT-------LMRDAGVTISYtAPTF-YRQMAPFAKKI-----GLPQLRICVSAGEGLPDAT------ 330
Cdd:cd05906 236 ---QQVHVPtEEILAdplrwldLIDRYRVTITW-APNFaFALLNDLLEEIedgtwDLSSLRYLVNAGEAVVAKTirrllr 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 331 ----RQLWKDAtgidMTDGIGATEMFH--IFISSAGGEARTGA-----IGKVVPGYTAKVVDDDGNEVPRGTVGKLAVIG 399
Cdd:cd05906 312 llepYGLPPDA----IRPAFGMTETCSgvIYSRSFPTYDHSQAlefvsLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRG 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 400 PTGCK-YLDDPR--QAKYVKDGWNYPGD-AFTQdaDGYFFYQARDDDMIITAGYNVGGPEVEDAL-----LRHPAVAECG 470
Cdd:cd05906 388 PVVTKgYYNNPEanAEAFTEDGWFRTGDlGFLD--NGNLTITGRTKDTIIVNGVNYYSHEIEAAVeevpgVEPSFTAAFA 465
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496182614 471 VIGVPDEERGMVVkavcVLKPGHTGDAAMVKTLQ---DHV--KATIAPfkyPRVVEF-VTALPRTETGKLQRFKLRQA 542
Cdd:cd05906 466 VRDPGAETEELAI----FFVPEYDLQDALSETLRairSVVsrEVGVSP---AYLIPLpKEEIPKTSLGKIQRSKLKAA 536
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
200-536 |
8.87e-34 |
|
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.
Pssm-ID: 341290 [Multi-domain] Cd Length: 340 Bit Score: 131.23 E-value: 8.87e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 200 DIALMAFTSGTTGAPKAAVHTHRDVLAGCEAWPRHVLKATPDDIVAGSPPLAFTFGLGGLLVFPMWAGASVYFPDQPyTP 279
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGENT-TY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 280 ETMVTLMRDAGVTISYTAPTFYRQMAPFAKKIG--LPQLRICVSAGEGLPDATRQ--LWKDATGIDMTDGIGATEMFhIF 355
Cdd:cd17635 81 KSLFKILTTNAVTTTCLVPTLLSKLVSELKSANatVPSLRLIGYGGSRAIAADVRfiEATGLTNTAQVYGLSETGTA-LC 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 356 ISSAGGEARTGAIGKVVPGYTAKVVDDDGNEVPRGTVGKLAVIGPTGCK-YLDDP-RQAKYVKDGWNYPGDAFTQDADGY 433
Cdd:cd17635 160 LPTDDDSIEINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLgYWNNPeRTAEVLIDGWVNTGDLGERREDGF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 434 FFYQARDDDMIITAGYNVGGPEVEDALLRHPAVAECGVIGVPDEERGMVVKAVcVLKPGHTgDAAMVKTLQDHVKATIAP 513
Cdd:cd17635 240 LFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLA-VVASAEL-DENAIRALKHTIRRELEP 317
|
330 340
....*....|....*....|...
gi 496182614 514 FKYPRVVEFVTALPRTETGKLQR 536
Cdd:cd17635 318 YARPSTIVIVTDIPRTQSGKVKR 340
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
48-543 |
9.54e-34 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 134.87 E-value: 9.54e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 48 AERAERAGNIDRPllrgphRTYTYRDARTEAARIAEVLTQdHGLVPGNRVLLRGGNTVEMALAWLGTVYAGLIAVATMPL 127
Cdd:PRK06164 21 RARPDAVALIDED------RPLSRAELRALVDRLAAWLAA-QGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 128 LRAGELANIIERAQPT-LALCDG-------RLLAELAAAQDQHPVLTTIVPFHTATDPADLLQRAQGKPGSMQPCPTSA- 198
Cdd:PRK06164 94 YRSHEVAHILGRGRARwLVVWPGfkgidfaAILAAVPPDALPPLRAIAVVDDAADATPAPAPGARVQLFALPDPAPPAAa 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 199 -------DDIALMAFTSGTTGAPKAAVHTHRDVLAGCEAWPRhVLKATPDDIVAGSPPLAFTFGLGGLLVFpMWAGASVY 271
Cdd:PRK06164 174 geraadpDAGALLFTTSGTTSGPKLVLHRQATLLRHARAIAR-AYGYDPGAVLLAALPFCGVFGFSTLLGA-LAGGAPLV 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 272 FPDQPYTPETmVTLMRDAGVTISYTAPTFYRQMAPFAKKIG-LPQLRICVSAGegLPDATRQL--WKDATGIDMTDGIGA 348
Cdd:PRK06164 252 CEPVFDAART-ARALRRHRVTHTFGNDEMLRRILDTAGERAdFPSARLFGFAS--FAPALGELaaLARARGVPLTGLYGS 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 349 TEMFHIF----ISSAGGEARTGAIGKVVPGYTAKVVD-DDGNEVPRGTVGKLAVIGPTGCK-YLDDPR--QAKYVKDGWN 420
Cdd:PRK06164 329 SEVQALValqpATDPVSVRIEGGGRPASPEARVRARDpQDGALLPDGESGEIEIRAPSLMRgYLDNPDatARALTDDGYF 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 421 YPGDAFTQDADGYFFYQARDDDMIITAGYNVGGPEVEDALLRHPAVAECGVIGVPDEERGMVVkAVCVLKPGHTGDAAMV 500
Cdd:PRK06164 409 RTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGATRDGKTVPV-AFVIPTDGASPDEAGL 487
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 496182614 501 KTlqdHVKATIAPFKYPRVVEFVTALPRTETG---KLQRFKLRQAA 543
Cdd:PRK06164 488 MA---ACREALAGFKVPARVQVVEAFPVTESAngaKIQKHRLREMA 530
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
28-553 |
1.00e-33 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 137.21 E-value: 1.00e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 28 DLPELQIPDQANL---------------VHALFdqaERAERAGNiDRPLLRGPHRTYTYRDARTEAARIAEVLtQDHGLV 92
Cdd:PRK12467 486 ELPLLDAEERARElvrwnapateyapdcVHQLI---EAQARQHP-ERPALVFGEQVLSYAELNRQANRLAHVL-IAAGVG 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 93 PGNRVLLRGGNTVEMALAWLGTVYAGliaVATMPLlragELANIIERAQPTLALCDGRLLAELAAAQDQHPVLTTiVPFH 172
Cdd:PRK12467 561 PDVLVGIAVERSIEMVVGLLAVLKAG---GAYVPL----DPEYPQDRLAYMLDDSGVRLLLTQSHLLAQLPVPAG-LRSL 632
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 173 TATDPADLLQraqGKPGSMQPCPTSADDIALMAFTSGTTGAPKAAVHTHRDvLAGCEAWPRHVLKATPDDIVAGSPPLAF 252
Cdd:PRK12467 633 CLDEPADLLC---GYSGHNPEVALDPDNLAYVIYTSGSTGQPKGVAISHGA-LANYVCVIAERLQLAADDSMLMVSTFAF 708
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 253 TFGlGGLLVFPMWAGASVYF--PDQPYTPETMVTLMRDAGVTISYTAPTFYRQMAPFAKKIGLPQLRICVSAGEGLPDAT 330
Cdd:PRK12467 709 DLG-VTELFGALASGATLHLlpPDCARDAEAFAALMADQGVTVLKIVPSHLQALLQASRVALPRPQRALVCGGEALQVDL 787
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 331 RQLWKD-ATGIDMTDGIGATE----MFHIFISSAGGEARTGAIGKVVPGYTAKVVDDDGNEVPRGTVGKLAVIGP----- 400
Cdd:PRK12467 788 LARVRAlGPGARLINHYGPTEttvgVSTYELSDEERDFGNVPIGQPLANLGLYILDHYLNPVPVGVVGELYIGGAglarg 867
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 401 -------TGCKYLDDPRQAkyvkDGWNY--PGDAFTQDADGYFFYQARDDDMIITAGYNVGGPEVEDALLRHPAVAECGV 471
Cdd:PRK12467 868 yhrrpalTAERFVPDPFGA----DGGRLyrTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVV 943
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 472 IGVP-DEERGMVVKAVCVLKPGHTGDAAMVKTLQDHVKATIAPFKYPRVVEFVTALPRTETGKLQRFKLRQA-AATPQAE 549
Cdd:PRK12467 944 LAQPgDAGLQLVAYLVPAAVADGAEHQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALPKPdASAVQAT 1023
|
....
gi 496182614 550 VKAP 553
Cdd:PRK12467 1024 FVAP 1027
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
67-542 |
3.36e-33 |
|
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: 133.13 E-value: 3.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 67 RTYTYRDARTEAARIAEVLtQDHGLvPGNRVLLRGGNTVEMALAWLGTVYAGLIAVATMPLLRAGE---LANIIERAQPT 143
Cdd:cd05931 23 ETLTYAELDRRARAIAARL-QAVGK-PGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPPTPGRHaerLAAILADAGPR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 144 LALCDGRLLAELAAAQDQHPVLTTIVPFHTATDPADLlqraqgkPGSMQPCPTSADDIALMAFTSGTTGAPKAAVHTHRD 223
Cdd:cd05931 101 VVLTTAAALAAVRAFAASRPAAGTPRLLVVDLLPDTS-------AADWPPPSPDPDDIAYLQYTSGSTGTPKGVVVTHRN 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 224 VLAGCEAWpRHVLKATPDDIVAGSPPLAFTFGLGGLLVFPMWAGASVYFpdqpYTPETMVT-------LMRDAGVTISYt 296
Cdd:cd05931 174 LLANVRQI-RRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGPSVL----MSPAAFLRrplrwlrLISRYRATISA- 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 297 APTFYRQMApfAKKIGLPQL--------RICVSAGE----------------------------GLPDATrqLWkdATGI 340
Cdd:cd05931 248 APNFAYDLC--VRRVRDEDLegldlsswRVALNGAEpvrpatlrrfaeafapfgfrpeafrpsyGLAEAT--LF--VSGG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 341 DMTDGIGATEM------FHIFISSAGGEARTG--AIGKVVPGYTAKVVDDDGN-EVPRGTVGKLAVIGPTGCK-YLDDPR 410
Cdd:cd05931 322 PPGTGPVVLRVdrdalaGRAVAVAADDPAARElvSCGRPLPDQEVRIVDPETGrELPDGEVGEIWVRGPSVASgYWGRPE 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 411 QAKYVK--------DGWNYPGD-AFTqdADGYFFYQARDDDMIITAGYNVGGPEVEDALLRHPAV---AECGVIGVPDEE 478
Cdd:cd05931 402 ATAETFgalaatdeGGWLRTGDlGFL--HDGELYITGRLKDLIIVRGRNHYPQDIEATAEEAHPAlrpGCVAAFSVPDDG 479
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496182614 479 RGMVVkAVCVLKPGHTGDAAmvKTLQDHVKATIA-----PfkyPRVVEFVT--ALPRTETGKLQRFKLRQA 542
Cdd:cd05931 480 EERLV-VVAEVERGADPADL--AAIAAAIRAAVArehgvA---PADVVLVRpgSIPRTSSGKIQRRACRAA 544
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
40-552 |
3.45e-33 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 135.86 E-value: 3.45e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 40 LVHALFdqAERAERAGNIDRPLLRGPHRTYTYRDARteAARIAEVLTqDHGLVPGNRVLLRGGNTVEMALAWLGTVYAGL 119
Cdd:PRK12316 2004 GVHQRI--AEQAARAPEAIAVVFGDQHLSYAELDSR--ANRLAHRLR-ARGVGPEVRVAIAAERSFELVVALLAVLKAGG 2078
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 120 IAVATMPLLRAGELANIIERAQPTLALCDGRLLAELAaaqdqhpvLTTIVPFHTATDPADLLQRAQGKPGSMqpcpTSAD 199
Cdd:PRK12316 2079 AYVPLDPNYPAERLAYMLEDSGAALLLTQRHLLERLP--------LPAGVARLPLDRDAEWADYPDTAPAVQ----LAGE 2146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 200 DIALMAFTSGTTGAPKAAVHTHRDVLAGCEAWPRHVlKATPDDIVAGSPPLAFTFGLGGLLVfPMWAGASVYF-PDQPYT 278
Cdd:PRK12316 2147 NLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERY-ELSPADCELQFMSFSFDGAHEQWFH-PLLNGARVLIrDDELWD 2224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 279 PETMVTLMRDAGVTISYTAPTFYRQMAPFAKKIG-LPQLRICVSAGEGLPDATRQLWKDATGID-MTDGIGATE-----M 351
Cdd:PRK12316 2225 PEQLYDEMERHGVTILDFPPVYLQQLAEHAERDGrPPAVRVYCFGGEAVPAASLRLAWEALRPVyLFNGYGPTEavvtpL 2304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 352 FHIFISSAGGEARTGAIGKVVPGYTAKVVDDDGNEVPRGTVGKLaVIGPTGC--KYLDDPRQA--KYVKDGWNYPG---- 423
Cdd:PRK12316 2305 LWKCRPQDPCGAAYVPIGRALGNRRAYILDADLNLLAPGMAGEL-YLGGEGLarGYLNRPGLTaeRFVPDPFSASGerly 2383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 424 ---DAFTQDADGYFFYQARDDDMIITAGYNVGGPEVEDALLRHPAVAECGVIGVpDEERGMVVKAVCVLKPGHTGDAAMV 500
Cdd:PRK12316 2384 rtgDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQ-DGASGKQLVAYVVPDDAAEDLLAEL 2462
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 501 KTlqdHVKATIAPFKYPRVVEFVTALPRTETGKLQRFKL--------RQAAATPQAEVKA 552
Cdd:PRK12316 2463 RA---WLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALpkpdvsqlRQAYVAPQEGLEQ 2519
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
30-540 |
5.39e-33 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 132.66 E-value: 5.39e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 30 PELQIPDQANL--VHALFDQAERAERAGNIDRpllrGPHRTYTYRDARTEAARIAEVLTQDHGLVPGNRVLLRGGNTVEM 107
Cdd:PLN02574 30 PPVPLPSDPNLdaVSFIFSHHNHNGDTALIDS----STGFSISYSELQPLVKSMAAGLYHVMGVRQGDVVLLLLPNSVYF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 108 ALAWLGTVYAGLIAVATMPLLRAGELANIIERAQPTLALCDGRLLAELAAAQDqhPVLTTIVPFH---TATDPADLLQRA 184
Cdd:PLN02574 106 PVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAFTSPENVEKLSPLGV--PVIGVPENYDfdsKRIEFPKFYELI 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 185 QGKPGSMQPCPTSADDIALMAFTSGTTGAPKAAVHTHRDVLAGCEAWPRH--VLKATP--DDIVAGSPPLAFTFGLGGLL 260
Cdd:PLN02574 184 KEDFDFVPKPVIKQDDVAAIMYSSGTTGASKGVVLTHRNLIAMVELFVRFeaSQYEYPgsDNVYLAALPMFHIYGLSLFV 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 261 VFPMWAGASVYFPDQpYTPETMVTLMRDAGVTISYTAPTFYRQMAPFAKKIGLPQLRICVSAGEGLPDATRQLWKD---- 336
Cdd:PLN02574 264 VGLLSLGSTIVVMRR-FDASDMVKVIDRFKVTHFPVVPPILMALTKKAKGVCGEVLKSLKQVSCGAAPLSGKFIQDfvqt 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 337 ATGIDMTDGIGATEmfhifiSSAGGE--------ARTGAIGKVVPGYTAKVVD-DDGNEVPRGTVGKLAVIGPTGCK-YL 406
Cdd:PLN02574 343 LPHVDFIQGYGMTE------STAVGTrgfnteklSKYSSVGLLAPNMQAKVVDwSTGCLLPPGNCGELWIQGPGVMKgYL 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 407 DDPR--QAKYVKDGWNYPGDAFTQDADGYFFYQARDDDMIITAGYNVGGPEVEDALLRHPAVAECGVIGVPDEERGMVVK 484
Cdd:PLN02574 417 NNPKatQSTIDKDGWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPV 496
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 496182614 485 AVCVLKPGHTGDAAMVktlQDHVKATIAPFKYPRVVEFVTALPRTETGKLQRFKLR 540
Cdd:PLN02574 497 AFVVRRQGSTLSQEAV---INYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRRELK 549
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
40-551 |
1.14e-32 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 134.31 E-value: 1.14e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 40 LVHALFdqAERAERagNIDRPLLRGPHRTYTYRDARTEAARIAEVLTQdHGLVPGNRVLLRGGNTVEMALAWLGTVYAGL 119
Cdd:PRK12316 4552 CVHQLV--AERARM--TPDAVAVVFDEEKLTYAELNRRANRLAHALIA-RGVGPEVLVGIAMERSAEMMVGLLAVLKAGG 4626
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 120 IAVATMPLLRAGELANIIERAQPTLALCDGRLLAELAAAQDQHPVlttivpfhtATDPADllqRAQGKPGSMQPCPTSAD 199
Cdd:PRK12316 4627 AYVPLDPEYPRERLAYMMEDSGAALLLTQSHLLQRLPIPDGLASL---------ALDRDE---DWEGFPAHDPAVRLHPD 4694
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 200 DIALMAFTSGTTGAPKAAVHTHRDVLAGCeAWPRHVLKATPDDIVAGSPPLAFTfGLGGLLVFPMWAGASVYF-PDQPYT 278
Cdd:PRK12316 4695 NLAYVIYTSGSTGRPKGVAVSHGSLVNHL-HATGERYELTPDDRVLQFMSFSFD-GSHEGLYHPLINGASVVIrDDSLWD 4772
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 279 PETMVTLMRDAGVTISYTAPTFYRQMAPFAKKIG-LPQLRICVSAGEGL-PDATRQLWKDATGIDMTDGIGATE--MFHI 354
Cdd:PRK12316 4773 PERLYAEIHEHRVTVLVFPPVYLQQLAEHAERDGePPSLRVYCFGGEAVaQASYDLAWRALKPVYLFNGYGPTEttVTVL 4852
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 355 FISSAGGEARTGA---IGKVVPGYTAKVVDDDGNEVPRGTVGKLaVIGPTGCK--YLDDP--RQAKYVKDGWNYP----- 422
Cdd:PRK12316 4853 LWKARDGDACGAAympIGTPLGNRSGYVLDGQLNPLPVGVAGEL-YLGGEGVArgYLERPalTAERFVPDPFGAPggrly 4931
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 423 --GDAFTQDADGYFFYQARDDDMIITAGYNVGGPEVEDALLRHPAVAECGVIGVP----DEERGMVVKAVCVLKPGHTGD 496
Cdd:PRK12316 4932 rtGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEgavgKQLVGYVVPQDPALADADEAQ 5011
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496182614 497 AAMVKTLQDHVKATIAPFKYPRVVEFVTALPRTETGKLQRFKL--------RQAAATPQAEVK 551
Cdd:PRK12316 5012 AELRDELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRKALpqpdasllQQAYVAPRSELE 5074
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
67-543 |
1.37e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 130.67 E-value: 1.37e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 67 RTYTYRDARTEAARIAEVLTQDHGLvpGNRVLLRGGNTVEMALAWLGTVYAGLIAVATMPLLRAGELANIIERAQPTLAL 146
Cdd:PRK07638 25 RVLTYKDWFESVCKVANWLNEKESK--NKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKERLAISNADMIV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 147 CDGRLLAELAAAQDqhPVLttivpfhtatdpadLLQRAQGKPGSMQPCPTSADDIAL----MAFTSGTTGAPKAAVHTHR 222
Cdd:PRK07638 103 TERYKLNDLPDEEG--RVI--------------EIDEWKRMIEKYLPTYAPIENVQNapfyMGFTSGSTGKPKAFLRAQQ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 223 DVLAG--CEAwprHVLKATPDD--IVAGSppLA---FTFGLggllVFPMWAGASVYFpDQPYTPETMVTLMRDAGVTISY 295
Cdd:PRK07638 167 SWLHSfdCNV---HDFHMKREDsvLIAGT--LVhslFLYGA----ISTLYVGQTVHL-MRKFIPNQVLDKLETENISVMY 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 296 TAPTFyrqMAPFAKKIGLPQ--LRICVSAGEGLPDATRQLWKDATGIDMTDGIGATEM-FHIFISSAGGEARTGAIGKVV 372
Cdd:PRK07638 237 TVPTM---LESLYKENRVIEnkMKIISSGAKWEAEAKEKIKNIFPYAKLYEFYGASELsFVTALVDEESERRPNSVGRPF 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 373 PGYTAKVVDDDGNEVPRGTVGKLAVIGP---TGckYLDDPRQAKYVK-DGWNYPGDAFTQDADGYFFYQARDDDMIITAG 448
Cdd:PRK07638 314 HNVQVRICNEAGEEVQKGEIGTVYVKSPqffMG--YIIGGVLARELNaDGWMTVRDVGYEDEEGFIYIVGREKNMILFGG 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 449 YNVGGPEVEDALLRHPAVAECGVIGVPDEERGMvvKAVCVLKpGHtgdaAMVKTLQDHVKATIAPFKYPRVVEFVTALPR 528
Cdd:PRK07638 392 INIFPEEIESVLHEHPAVDEIVVIGVPDSYWGE--KPVAIIK-GS----ATKQQLKSFCLQRLSSFKIPKEWHFVDEIPY 464
|
490
....*....|....*
gi 496182614 529 TETGKLQRFKLRQAA 543
Cdd:PRK07638 465 TNSGKIARMEAKSWI 479
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
58-542 |
1.76e-32 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 130.47 E-value: 1.76e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 58 DRPLLRGPHRTYTYRDARTEAARIAEVLTQdHGLVPGNRVLLRGGNTVEMALAWLGTVYAGLIAVATMPLLRAGELANII 137
Cdd:PRK03640 17 DRTAIEFEEKKVTFMELHEAVVSVAGKLAA-LGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 138 ERAQPTLALCDGRLLAELAAAQDQhpvlttivpfhtatDPADLLQRAQGKPGSMQPCPTsaDDIALMAFTSGTTGAPKAA 217
Cdd:PRK03640 96 DDAEVKCLITDDDFEAKLIPGISV--------------KFAELMNGPKEEAEIQEEFDL--DEVATIMYTSGTTGKPKGV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 218 VHTHRDvlagceawprHVLKA---------TPDDIVAGSPPLaftFGLGGL--LVFPMWAGASVYFPDQpYTPETMVTLM 286
Cdd:PRK03640 160 IQTYGN----------HWWSAvgsalnlglTEDDCWLAAVPI---FHISGLsiLMRSVIYGMRVVLVEK-FDAEKINKLL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 287 RDAGVTISYTAPTFYRQMAPFAKKIGLP-QLRiCVSAGEG-LPDATRQLWKdATGIDMTDGIGATEMFHIFISSAGGEAR 364
Cdd:PRK03640 226 QTGGVTIISVVSTMLQRLLERLGEGTYPsSFR-CMLLGGGpAPKPLLEQCK-EKGIPVYQSYGMTETASQIVTLSPEDAL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 365 T--GAIGKvvPGYTAKV-VDDDGNEVPRGTVGKLAVIGPTGCK-YLDDPRQ-AKYVKDGWNYPGDAFTQDADGYFFYQAR 439
Cdd:PRK03640 304 TklGSAGK--PLFPCELkIEKDGVVVPPFEEGEIVVKGPNVTKgYLNREDAtRETFQDGWFKTGDIGYLDEEGFLYVLDR 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 440 DDDMIITAGYNVGGPEVEDALLRHPAVAECGVIGVPDEERGMVVKAVCVLKPGHTGDAamvktLQDHVKATIAPFKYPRV 519
Cdd:PRK03640 382 RSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVKSGEVTEEE-----LRHFCEEKLAKYKVPKR 456
|
490 500
....*....|....*....|...
gi 496182614 520 VEFVTALPRTETGKLQRFKLRQA 542
Cdd:PRK03640 457 FYFVEELPRNASGKLLRHELKQL 479
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
177-545 |
2.12e-32 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 132.74 E-value: 2.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 177 PADLLQRAQGKPgsmqpcpTSADDIALMAFTSGTTGAPKAAVHTHRDVLAGCEAWpRHVLKATPDDIVAGSPPLAFTFGL 256
Cdd:PRK08633 767 PARLLKRLYGPT-------FKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQI-SDVFNLRNDDVILSSLPFFHSFGL 838
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 257 GGLLVFPMWAG-ASVYFPDqPYTPETMVTLMRDAGVTISYTAPTFYRQMA--PFAKKIGLPQLRICVSAGEGLPDATRQL 333
Cdd:PRK08633 839 TVTLWLPLLEGiKVVYHPD-PTDALGIAKLVAKHRATILLGTPTFLRLYLrnKKLHPLMFASLRLVVAGAEKLKPEVADA 917
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 334 WKDATGIDMTDGIGATEM-----------------FHIFissaggeARTGAIGKVVPGYTAKVVD-DDGNEVPRGTVGKL 395
Cdd:PRK08633 918 FEEKFGIRILEGYGATETspvasvnlpdvlaadfkRQTG-------SKEGSVGMPLPGVAVRIVDpETFEELPPGEDGLI 990
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 396 AVIGPTGCK-YLDDP-RQAKYVKD----GWNYPGDAFTQDADGYFFyqardddmiITAGYN----VGGpE------VEDA 459
Cdd:PRK08633 991 LIGGPQVMKgYLGDPeKTAEVIKDidgiGWYVTGDKGHLDEDGFLT---------ITDRYSrfakIGG-EmvplgaVEEE 1060
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 460 L---LRHPAVaECGVIGVPDEERGmvvKAVCVLkpgHTGDAAMVKTLQDHVKAT-IAPFKYPRVVEFVTALPRTETGKLQ 535
Cdd:PRK08633 1061 LakaLGGEEV-VFAVTAVPDEKKG---EKLVVL---HTCGAEDVEELKRAIKESgLPNLWKPSRYFKVEALPLLGSGKLD 1133
|
410
....*....|
gi 496182614 536 RFKLRQAAAT 545
Cdd:PRK08633 1134 LKGLKELALA 1143
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
133-541 |
8.55e-32 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 129.11 E-value: 8.55e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 133 LANIIERAQPTLALCDGRLLAELAAAQDQHPVLTTIVPFhTATDPADLLQRAQGKPGSMQPCPT--SADDIALmafTSGT 210
Cdd:PRK13382 132 LAEVVTREGVDTVIYDEEFSATVDRALADCPQATRIVAW-TDEDHDLTVEVLIAAHAGQRPEPTgrKGRVILL---TSGT 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 211 TGAPKAAVHTHRDVLAGCEAwprhVLKATP---DDIVAGSPPLAFTFGLGGLLVFPMWAGASVYfpDQPYTPETMVTLMR 287
Cdd:PRK13382 208 TGTPKGARRSGPGGIGTLKA----ILDRTPwraEEPTVIVAPMFHAWGFSQLVLAASLACTIVT--RRRFDPEATLDLID 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 288 DAGVTISYTAPTFYRQMAPFAKKI----GLPQLRICVSAGEGLPDATRQLWKDATGIDMTDGIGATEMFHIFISS-AGGE 362
Cdd:PRK13382 282 RHRATGLAVVPVMFDRIMDLPAEVrnrySGRSLRFAAASGSRMRPDVVIAFMDQFGDVIYNNYNATEAGMIATATpADLR 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 363 ARTGAIGKVVPGYTAKVVDDDGNEVPRGTVGKLAVIGPTgckyLDD---PRQAKYVKDGWNYPGDAFTQDADGYFFYQAR 439
Cdd:PRK13382 362 AAPDTAGRPAEGTEIRILDQDFREVPTGEVGTIFVRNDT----QFDgytSGSTKDFHDGFMASGDVGYLDENGRLFVVGR 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 440 DDDMIITAGYNVGGPEVEDALLRHPAVAECGVIGVPDEERGMVVKAVCVLKPghtGDAAMVKTLQDHVKATIAPFKYPRV 519
Cdd:PRK13382 438 DDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKP---GASATPETLKQHVRDNLANYKVPRD 514
|
410 420
....*....|....*....|..
gi 496182614 520 VEFVTALPRTETGKLQRFKLRQ 541
Cdd:PRK13382 515 IVVLDELPRGATGKILRRELQA 536
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
26-545 |
2.58e-31 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 127.79 E-value: 2.58e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 26 RYDLPELQIPDQANLVHALFdqaERAERAGniDRP-LLRGPH-RTYTYRDARTEAARIAEVLTQdHGLVPGNRVLLRGGN 103
Cdd:PLN02246 11 RSKLPDIYIPNHLPLHDYCF---ERLSEFS--DRPcLIDGATgRVYTYADVELLSRRVAAGLHK-LGIRQGDVVMLLLPN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 104 TVEMALAWLGTVYAGLIAVATMPLLRAGELANIIERAQPTLALCDGRLLAELAAAQDQHPVltTIVpfhTATDPAD---- 179
Cdd:PLN02246 85 CPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAKLIITQSCYVDKLKGLAEDDGV--TVV---TIDDPPEgclh 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 180 ---LLQRAQGkpgsmqPCPT---SADDIALMAFTSGTTGAPKAAVHTHRDvLAGCEAwpRHV------LKATPDDIVAGS 247
Cdd:PLN02246 160 fseLTQADEN------ELPEveiSPDDVVALPYSSGTTGLPKGVMLTHKG-LVTSVA--QQVdgenpnLYFHSDDVILCV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 248 PPLAFTFGLGGLLVFPMWAGASVYFPdQPYTPETMVTLMRDAGVTISYTAPTFYRQMA--PFAKKIGLPQLRICVSA--- 322
Cdd:PLN02246 231 LPMFHIYSLNSVLLCGLRVGAAILIM-PKFEIGALLELIQRHKVTIAPFVPPIVLAIAksPVVEKYDLSSIRMVLSGaap 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 323 -GEGLPDATRQLWKDAT---GIDMTDGiG---------ATEMFhifissaggEARTGAIGKVVPGYTAKVVD-DDGNEVP 388
Cdd:PLN02246 310 lGKELEDAFRAKLPNAVlgqGYGMTEA-GpvlamclafAKEPF---------PVKSGSCGTVVRNAELKIVDpETGASLP 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 389 RGTVGKLAVIGPTGCK-YLDDPRQAKYV--KDGWNYPGDAFTQDADGYFFYQARDDDMIITAGYNVGGPEVEDALLRHPA 465
Cdd:PLN02246 380 RNQPGEICIRGPQIMKgYLNDPEATANTidKDGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPS 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 466 VAECGVIGVPDEERGMVVKAVCVLKPGhtgdaamVKTLQDHVKATIAP----FKYPRVVEFVTALPRTETGKLQRFKLRQ 541
Cdd:PLN02246 460 IADAAVVPMKDEVAGEVPVAFVVRSNG-------SEITEDEIKQFVAKqvvfYKRIHKVFFVDSIPKAPSGKILRKDLRA 532
|
....
gi 496182614 542 AAAT 545
Cdd:PLN02246 533 KLAA 536
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
36-542 |
3.13e-31 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 127.81 E-value: 3.13e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 36 DQANLVHALfDQAERAERAGNI-DRpllRGP-HRTYTYRDARTEAARIAEVLTQdHGLVPGNRVLLRGGNTVEMALAWLG 113
Cdd:PRK09192 19 DFPTLVEAL-DYAALGEAGMNFyDR---RGQlEEALPYQTLRARAEAGARRLLA-LGLKPGDRVALIAETDGDFVEAFFA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 114 TVYAGLIAVAtMPLL-----RAG---ELANIIERAQPTLALCDGRLLAELAAAQDQHPVLTTIVP--FHTATDPADLLQR 183
Cdd:PRK09192 94 CQYAGLVPVP-LPLPmgfggRESyiaQLRGMLASAQPAAIITPDELLPWVNEATHGNPLLHVLSHawFKALPEADVALPR 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 184 AqgkpgsmqpcptSADDIALMAFTSGTTGAPKAAVHTHRDVLAGCEAWPRHVLKATPDDIVAGSPPLAFTFGLGGLLVFP 263
Cdd:PRK09192 173 P------------TPDDIAYLQYSSGSTRFPRGVIITHRALMANLRAISHDGLKVRPGDRCVSWLPFYHDMGLVGFLLTP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 264 MWAGASV-YFPDQPYT--PETMVTLMRDAGVTISYtAPTF---------------------YRQMAPFAKKIGLPQLRIC 319
Cdd:PRK09192 241 VATQLSVdYLPTRDFArrPLQWLDLISRNRGTISY-SPPFgyelcarrvnskdlaeldlscWRVAGIGADMIRPDVLHQF 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 320 V----SAG---------EGLPDATRQL--WKDATGI--DMTDgIGATEMFHIFISSAGGEARTGAI---GKVVPGYTAKV 379
Cdd:PRK09192 320 AeafaPAGfddkafmpsYGLAEATLAVsfSPLGSGIvvEEVD-RDRLEYQGKAVAPGAETRRVRTFvncGKALPGHEIEI 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 380 VDDDGNEVPRGTVGKLAVIGPT-GCKYLDDPRQAKYVK-DGWNYPGD-AFTqdADGYFFYQARDDDMIITAGYNVGGPEV 456
Cdd:PRK09192 399 RNEAGMPLPERVVGHICVRGPSlMSGYFRDEESQDVLAaDGWLDTGDlGYL--LDGYLYITGRAKDLIIINGRNIWPQDI 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 457 EDALLRHPAV--AECGVIGVPDEERGMVVkavcVLKPGHTGDAAMVKTLQDHVKATI-APFKYPRVVEFVT--ALPRTET 531
Cdd:PRK09192 477 EWIAEQEPELrsGDAAAFSIAQENGEKIV----LLVQCRISDEERRGQLIHALAALVrSEFGVEAAVELVPphSLPRTSS 552
|
570
....*....|.
gi 496182614 532 GKLQRFKLRQA 542
Cdd:PRK09192 553 GKLSRAKAKKR 563
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
25-541 |
2.42e-30 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 124.71 E-value: 2.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 25 LRYDLPELQIPDQANLVHALFDQAER-AERAGNIDRplLRGphRTYTYRDARTEAARIAEVLTQdHGLVPGNRVLLRGGN 103
Cdd:PLN02330 15 FRSRYPSVPVPDKLTLPDFVLQDAELyADKVAFVEA--VTG--KAVTYGEVVRDTRRFAKALRS-LGLRKGQVVVVVLPN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 104 TVEMALAWLGTVYAGLIAVATMPLLRAGELANIIERAQPTLALCDGRLLAELAAAQDQHPVLTTiVPFHTATDPADLLQR 183
Cdd:PLN02330 90 VAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTNDTNYGKVKGLGLPVIVLGE-EKIEGAVNWKELLEA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 184 AQGKPGSMQPCPTSADDIALMAFTSGTTGAPKAAVHTHRDVLAG-CEAwprhVLKATPDDI----VAGSPPLAFTFGLGG 258
Cdd:PLN02330 169 ADRAGDTSDNEEILQTDLCALPFSSGTTGISKGVMLTHRNLVANlCSS----LFSVGPEMIgqvvTLGLIPFFHIYGITG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 259 LLVFPMWAGASVYFPDQpYTPETMVTLMRDAGVTISYTAPTFYRQMA--PFAKKIGLPQLR---ICVSAGEGLPDATRQL 333
Cdd:PLN02330 245 ICCATLRNKGKVVVMSR-FELRTFLNALITQEVSFAPIVPPIILNLVknPIVEEFDLSKLKlqaIMTAAAPLAPELLTAF 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 334 WKDATGIDMTDGIGATE-----MFHIFISSAGGEARTGAIGKVVPGYTAKVVD-DDGNEVPRGTVGKLAVigPTGC---- 403
Cdd:PLN02330 324 EAKFPGVQVQEAYGLTEhscitLTHGDPEKGHGIAKKNSVGFILPNLEVKFIDpDTGRSLPKNTPGELCV--RSQCvmqg 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 404 KYLDDPRQAKYV-KDGWNYPGDAFTQDADGYFFYQARDDDMIITAGYNVGGPEVEDALLRHPAVAECGVIGVPDEERGMV 482
Cdd:PLN02330 402 YYNNKEETDRTIdEDGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEI 481
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 496182614 483 VKAVCVLKPGHTGDAamvKTLQDHVKATIAPFKYPRVVEFVTALPRTETGKLQRFKLRQ 541
Cdd:PLN02330 482 PAACVVINPKAKESE---EDILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLKE 537
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
70-536 |
4.73e-30 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 123.84 E-value: 4.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 70 TYRDARTEAARIAEVLTQDhGLVPGNRVLLRGGNTVEMALAWLGTVYAGLIAVATMPLLRAGELANIIERAQPTLALCDG 149
Cdd:PRK05852 45 SYRDLARLVDDLAGQLTRS-GLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRSQAAGARVVLIDA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 150 RLLAELAAAQDQHPVLTTIVPFHTATDPADLLQR--AQGKPGSMQPCPTS-ADDIALMAFTSGTTGAPKAAVHTHRDVLA 226
Cdd:PRK05852 124 DGPHDRAEPTTRWWPLTVNVGGDSGPSGGTLSVHldAATEPTPATSTPEGlRPDDAMIMFTGGTTGLPKMVPWTHANIAS 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 227 G----CEAWprhvlKATPDDIVAGSPPLAFTFGLGGLLVFPMWAGASVYFPDQ-PYTPETMVTLMRDAGVTISYTAPTFY 301
Cdd:PRK05852 204 SvraiITGY-----RLSPRDATVAVMPLYHGHGLIAALLATLASGGAVLLPARgRFSAHTFWDDIKAVGATWYTAVPTIH 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 302 RQMAPFAK----KIGLPQLRICVSAGEGLPDATRQLWKDATGIDMTDGIGATEMFHIFISSAGGEARTGAIGKVVPGYTA 377
Cdd:PRK05852 279 QILLERAAtepsGRKPAALRFIRSCSAPLTAETAQALQTEFAAPVVCAFGMTEATHQVTTTQIEGIGQTENPVVSTGLVG 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 378 -------KVVDDDGNEVPRGTVGKLAVIGPTGCK-YLDDPR-QAKYVKDGWNYPGDAFTQDADGYFFYQARDDDMIITAG 448
Cdd:PRK05852 359 rstgaqiRIVGSDGLPLPAGAVGEVWLRGTTVVRgYLGDPTiTAANFTDGWLRTGDLGSLSAAGDLSIRGRIKELINRGG 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 449 YNVGGPEVEDALLRHPAVAECGVIGVPDEERGMVVKAVCVLKpghTGDAAMVKTLQDHVKATIAPFKYPRVVEFVTALPR 528
Cdd:PRK05852 439 EKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIVPR---ESAPPTAEELVQFCRERLAAFEIPASFQEASGLPH 515
|
....*...
gi 496182614 529 TETGKLQR 536
Cdd:PRK05852 516 TAKGSLDR 523
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
2-552 |
4.02e-29 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 123.35 E-value: 4.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 2 SVSSAQPDHFVHDRLPPQSAWPTLRydlpelqipdqanLVHALF-DQAERaeragNIDRPLLRGPHRTYTYRDARTEAAR 80
Cdd:PRK12467 3071 TLAAHERRQVLHAWNATAAAYPSER-------------LVHQLIeAQVAR-----TPEAPALVFGDQQLSYAELNRRANR 3132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 81 IAEVLTQdHGLVPGNRVLLRGGNTVEMALAWLGTVYAGLIAVATMPLLRAGELANIIERAQPTLALCDGRLLAELAAAqd 160
Cdd:PRK12467 3133 LAHRLIA-IGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLLTQAHLLEQLPAP-- 3209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 161 qhpvlttivpfhtATDPADLLQRaqGKPGSMQP-CPTS---ADDIALMAFTSGTTGAPKAAVHTHRDVLAGCEaWPRHVL 236
Cdd:PRK12467 3210 -------------AGDTALTLDR--LDLNGYSEnNPSTrvmGENLAYVIYTSGSTGKPKGVGVRHGALANHLC-WIAEAY 3273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 237 KATPDDIVAGSPPLAFTFGLGGLLVFPMWAGASVYFPDQPYTPETMVTLMRDAGVTISYTAPTFYRQMAPFAKKIGLPQL 316
Cdd:PRK12467 3274 ELDANDRVLLFMSFSFDGAQERFLWTLICGGCLVVRDNDLWDPEELWQAIHAHRISIACFPPAYLQQFAEDAGGADCASL 3353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 317 RICVSAGEGLPDATRQLWKDATG-IDMTDGIGATE-MFHIFISSAGGEARTGA----IGKVVPGYTAKVVDDDGNEVPRG 390
Cdd:PRK12467 3354 DIYVFGGEAVPPAAFEQVKRKLKpRGLTNGYGPTEaVVTVTLWKCGGDAVCEApyapIGRPVAGRSIYVLDGQLNPVPVG 3433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 391 TVGKLAVIGP------------TGCKYLDDPRQakyVKDGWNY-PGDAFTQDADGYFFYQARDDDMIITAGYNVGGPEVE 457
Cdd:PRK12467 3434 VAGELYIGGVglargyhqrpslTAERFVADPFS---GSGGRLYrTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIE 3510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 458 DALLRHPAVAECGVIGVpDEERGMVVKAVCVLkpgHTGDAAMVKTLQDHVKATIAPFKYPRVVEFVTALPRTETGKLQR- 536
Cdd:PRK12467 3511 ARLLQHPSVREAVVLAR-DGAGGKQLVAYVVP---ADPQGDWRETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRk 3586
|
570 580
....*....|....*....|..
gi 496182614 537 ------FKLRQAAATPQAEVKA 552
Cdd:PRK12467 3587 alpdpdAKGSREYVAPRSEVEQ 3608
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
58-536 |
2.52e-28 |
|
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: 118.14 E-value: 2.52e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 58 DRPLLRGPHRTYTYRDARTEAARIAEVLtQDHGLVPGNRVLLRGGNTVEMALAWLGTVYAGLIAVATMPLLRAGELANII 137
Cdd:cd12114 2 DATAVICGDGTLTYGELAERARRVAGAL-KAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 138 ERAQPTLALCDGrllaeLAAAQDQHPVLTTIVPFHTATDPADLLqraqgkpgsmqPCPTSADDIALMAFTSGTTGAPKAA 217
Cdd:cd12114 81 ADAGARLVLTDG-----PDAQLDVAVFDVLILDLDALAAPAPPP-----------PVDVAPDDLAYVIFTSGSTGTPKGV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 218 VHTHRDVLAGCEAWPRHvLKATPDDIVAGSPPLAF---TFGLGGLLVfpmwAGASVYFPD--QPYTPETMVTLMRDAGVT 292
Cdd:cd12114 145 MISHRAALNTILDINRR-FAVGPDDRVLALSSLSFdlsVYDIFGALS----AGATLVLPDeaRRRDPAHWAELIERHGVT 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 293 ISYTAPTfYRQM---APFAKKIGLPQLRICVSAGE----GLPDATRQLWKDATGIDMTdgiGATE--MFHIFISSAGGEA 363
Cdd:cd12114 220 LWNSVPA-LLEMlldVLEAAQALLPSLRLVLLSGDwiplDLPARLRALAPDARLISLG---GATEasIWSIYHPIDEVPP 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 364 RTGAI--GKVVPGYTAKVVDDDGNEVPRGTVGKLaVIGPTGCK--YLDDPR--QAKYVKDG----WNYPGDAFTQDADGY 433
Cdd:cd12114 296 DWRSIpyGRPLANQRYRVLDPRGRDCPDWVPGEL-WIGGRGVAlgYLGDPEltAARFVTHPdgerLYRTGDLGRYRPDGT 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 434 FFYQARDDDMIITAGYNVGGPEVEDALLRHPAVAECGVIGVPD-EERGMVVKAVCVLKPGHTGDAAMVKTLQDHVKATIA 512
Cdd:cd12114 375 LEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDpGGKRLAAFVVPDNDGTPIAPDALRAFLAQTLPAYMI 454
|
490 500
....*....|....*....|....
gi 496182614 513 PFKYPrvveFVTALPRTETGKLQR 536
Cdd:cd12114 455 PSRVI----ALEALPLTANGKVDR 474
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
35-553 |
5.82e-28 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 119.68 E-value: 5.82e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 35 PDQANLVHALFDQAERAERAgnidrPLLRGPHRTYTYRDARTEAARIAEVLtQDHGLVPGNRVLLRGGNTVEMALAWLGT 114
Cdd:PRK12316 508 PLQRGVHRLFEEQVERTPEA-----PALAFGEETLDYAELNRRANRLAHAL-IERGVGPDVLVGVAMERSIEMVVALLAI 581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 115 VYAGLIAVATMPLLRAGELANIIERAQPTLALCDGRLLAELA-AAQDQHPVLTTIVPFHTATDPADLLQRAQGkpgsmqp 193
Cdd:PRK12316 582 LKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQSHLGRKLPlAAGVQVLDLDRPAAWLEGYSEENPGTELNP------- 654
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 194 cptsaDDIALMAFTSGTTGAPKAAVHTHRdVLAGCEAWPRHVLKATPDDIVAGSPPLAFTFGLGGLLVfPMWAGAS--VY 271
Cdd:PRK12316 655 -----ENLAYVIYTSGSTGKPKGAGNRHR-ALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFW-PLMSGARlvVA 727
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 272 FPDQPYTPETMVTLMRDAGVTISYTAPTFYRQMAPFAKKIGLPQLRICVSAGEGLP-DATRQLWKDATGIDMTDGIGATE 350
Cdd:PRK12316 728 APGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVASCTSLRRIVCSGEALPaDAQEQVFAKLPQAGLYNLYGPTE 807
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 351 ----MFHIFISSAGGeaRTGAIGKVVPGYTAKVVDDDGNEVPRGTVGKLaVIGPTGCK--YLDDP--RQAKYVKDGWN-- 420
Cdd:PRK12316 808 aaidVTHWTCVEEGG--DSVPIGRPIANLACYILDANLEPVPVGVLGEL-YLAGRGLArgYHGRPglTAERFVPSPFVag 884
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 421 ----YPGDAFTQDADGYFFYQARDDDMIITAGYNVGGPEVEDALLRHPAVAECGVIGVpdeeRGMVVKAVCVLKpghTGD 496
Cdd:PRK12316 885 ermyRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV----DGKQLVGYVVLE---SEG 957
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 496182614 497 AAMVKTLQDHVKATIAPFKYPRVVEFVTALPRTETGKLQRFKLRQAAAT-PQAEVKAP 553
Cdd:PRK12316 958 GDWREALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKALPAPEASvAQQGYVAP 1015
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
191-552 |
4.73e-27 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 116.22 E-value: 4.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 191 MQPCPTSADDIALMAFTSGTTGAPKAAVHTHRDVLAGCeAWPRHVLKATPDDIVAGSPPLAFTFGLGGLLVFPMWAGASV 270
Cdd:PRK06814 785 VYFCNRDPDDPAVILFTSGSEGTPKGVVLSHRNLLANR-AQVAARIDFSPEDKVFNALPVFHSFGLTGGLVLPLLSGVKV 863
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 271 YFPDQP--Y--TPEtmvtLMRDAGVTISYTAPTFYRQMAPFAKKIGLPQLRICVSAGEGLPDATRQLWKDATGIDMTDGI 346
Cdd:PRK06814 864 FLYPSPlhYriIPE----LIYDTNATILFGTDTFLNGYARYAHPYDFRSLRYVFAGAEKVKEETRQTWMEKFGIRILEGY 939
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 347 GATEMFHIFISSAGGEARTGAIGKVVPGYTAKVVDDDGneVPRGtvGKLAVIGPT---GCKYLDDPRQAKYVKDGWNYPG 423
Cdd:PRK06814 940 GVTETAPVIALNTPMHNKAGTVGRLLPGIEYRLEPVPG--IDEG--GRLFVRGPNvmlGYLRAENPGVLEPPADGWYDTG 1015
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 424 DAFTQDADGYFFYQARDDDMIITAGYNVGGPEVEDALLRHPAVAECGVIGVPDEERGmvvKAVCVLKPGHTGDAAmvkTL 503
Cdd:PRK06814 1016 DIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELWPDALHAAVSIPDARKG---ERIILLTTASDATRA---AF 1089
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 496182614 504 QDHVKATIAPFKY-PRVVEFVTALPRTETGKLQRFKLRQAAATPQAEVKA 552
Cdd:PRK06814 1090 LAHAKAAGASELMvPAEIITIDEIPLLGTGKIDYVAVTKLAEEAAAKPEA 1139
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
58-548 |
5.08e-27 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 114.70 E-value: 5.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 58 DRPLLRGPHRTYTYRDARTEAARIAEVLTQdHGLVPGNRVLLRGGNTVEMALAWLGTVYAGLIAVATMPLLRAGELANII 137
Cdd:PRK10946 38 DAIAVICGERQFSYRELNQASDNLACSLRR-QGIKPGDTALVQLGNVAEFYITFFALLKLGVAPVNALFSHQRSELNAYA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 138 ERAQPTLALCD--------GRLLAELaaaQDQHPVLTTIVpFHTATDPADLLQRAQGKPGSMQPCPTSADDIALMAFTSG 209
Cdd:PRK10946 117 SQIEPALLIADrqhalfsdDDFLNTL---VAEHSSLRVVL-LLNDDGEHSLDDAINHPAEDFTATPSPADEVAFFQLSGG 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 210 TTGAPKAAVHTHRD----VLAGCEawprhVLKATPDDIVAGSPPLAFTFGL---GGLLVFpMWAGASVYFPDqpytPE-- 280
Cdd:PRK10946 193 STGTPKLIPRTHNDyyysVRRSVE-----ICGFTPQTRYLCALPAAHNYPMsspGALGVF-LAGGTVVLAPD----PSat 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 281 -----------TMVTLMRDAgVTI---SYTAPTFYRQM----------APF----AKKIglP-----QLRICVSAGEGLP 327
Cdd:PRK10946 263 lcfpliekhqvNVTALVPPA-VSLwlqAIAEGGSRAQLaslkllqvggARLsetlARRI--PaelgcQLQQVFGMAEGLV 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 328 DATRqlwkdatgIDMTDGigatemfHIFISSaggeartgaiGK-VVPGYTAKVVDDDGNEVPRGTVGKLAVIGP-TGCKY 405
Cdd:PRK10946 340 NYTR--------LDDSDE-------RIFTTQ----------GRpMSPDDEVWVADADGNPLPQGEVGRLMTRGPyTFRGY 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 406 LDDPRQAKYV--KDGWNYPGDAFTQDADGYFFYQARDDDMIITAGYNVGGPEVEDALLRHPAVAECGVIGVPDEERGMVV 483
Cdd:PRK10946 395 YKSPQHNASAfdANGFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKS 474
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496182614 484 KAVCV----LKPghtgdAAMVKTLQDHvkaTIAPFKYPRVVEFVTALPRTETGKLQRFKLRQAAATPQA 548
Cdd:PRK10946 475 CAFLVvkepLKA-----VQLRRFLREQ---GIAEFKLPDRVECVDSLPLTAVGKVDKKQLRQWLASRAS 535
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
198-544 |
1.21e-26 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 114.61 E-value: 1.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 198 ADDIALMAFTSGTTGAPKAAVHTHRDVLAGCEAWPRHVLKATPDDIVAGSPPLAFTFGLGGLLVFPMWAGASVY-FPDQP 276
Cdd:PLN02654 274 AEDPLFLLYTSGSTGKPKGVLHTTGGYMVYTATTFKYAFDYKPTDVYWCTADCGWITGHSYVTYGPMLNGATVLvFEGAP 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 277 YTPET--MVTLMRDAGVTISYTAPTFYRQMA----PFAKKIGLPQLRICVSAGEGL-PDATRQLWkDATG---IDMTDGI 346
Cdd:PLN02654 354 NYPDSgrCWDIVDKYKVTIFYTAPTLVRSLMrdgdEYVTRHSRKSLRVLGSVGEPInPSAWRWFF-NVVGdsrCPISDTW 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 347 GATEMFHIFISSAGG--EARTGAIGKVVPGYTAKVVDDDGNEVPRGTVGKLAVI----GPTGCKYLDDPR-QAKYVK--D 417
Cdd:PLN02654 433 WQTETGGFMITPLPGawPQKPGSATFPFFGVQPVIVDEKGKEIEGECSGYLCVKkswpGAFRTLYGDHERyETTYFKpfA 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 418 GWNYPGDAFTQDADGYFFYQARDDDMIITAGYNVGGPEVEDALLRHPAVAECGVIGVPDEERGMVVKAVCVLKPGHTGDA 497
Cdd:PLN02654 513 GYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEVKGQGIYAFVTLVEGVPYSE 592
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 496182614 498 AMVKTLQDHVKATIAPFKYPRVVEFVTALPRTETGKLQRFKLRQAAA 544
Cdd:PLN02654 593 ELRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRKIAS 639
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
52-550 |
1.17e-25 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 110.89 E-value: 1.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 52 ERAGNiDRPLLRGPHRTYTYRDARTEAARIAEVLT--QDHGLVPGNRVLLrgGNTVEMALAWLGTVYAGLIAVATMPLLR 129
Cdd:PRK13388 11 DRAGD-DTIAVRYGDRTWTWREVLAEAAARAAALIalADPDRPLHVGVLL--GNTPEMLFWLAAAALGGYVLVGLNTTRR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 130 AGELANIIERAQPTLALCD--GR-LLAELAAAQDqhPVLTTIVPFHtatdpADLLQRAqgkpGSMQPCPT-SADDIALMA 205
Cdd:PRK13388 88 GAALAADIRRADCQLLVTDaeHRpLLDGLDLPGV--RVLDVDTPAY-----AELVAAA----GALTPHREvDAMDPFMLI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 206 FTSGTTGAPKAAVHTH-RDVLAGCEAWPRHVLkaTPDDIVAGSPPL----------AFTFGLGGLLVFPMWAGASVYFPD 274
Cdd:PRK13388 157 FTSGTTGAPKAVRCSHgRLAFAGRALTERFGL--TRDDVCYVSMPLfhsnavmagwAPAVASGAAVALPAKFSASGFLDD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 275 qpyTPETMVTLMRDAGVTISYTAPTfyrqmaPFAKKIGLPQLRicVSAGEGLPDATRQLWKDATGIDMTDGIGATEMFHI 354
Cdd:PRK13388 235 ---VRRYGATYFNYVGKPLAYILAT------PERPDDADNPLR--VAFGNEASPRDIAEFSRRFGCQVEDGYGSSEGAVI 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 355 FISSAGgeARTGAIGKVVPGYTakVVD-DDGNEVPRG-------------TVGKLAVIGPTG---CKYLDDPRQAKYVKD 417
Cdd:PRK13388 304 VVREPG--TPPGSIGRGAPGVA--IYNpETLTECAVArfdahgallnadeAIGELVNTAGAGffeGYYNNPEATAERMRH 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 418 GWNYPGDAFTQDADGYFFYQARDDDMIITAGYNVGGPEVEDALLRHPAVAECGVIGVPDEERGMVVKAVCVLKPGHTGD- 496
Cdd:PRK13388 380 GMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVGDQVMAALVLRDGATFDp 459
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 496182614 497 AAMVKTLqdHVKATIAPFKYPRVVEFVTALPRTETGKLQRFKLR-QAAATPQAEV 550
Cdd:PRK13388 460 DAFAAFL--AAQPDLGTKAWPRYVRIAADLPSTATNKVLKRELIaQGWATGDPVT 512
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
41-539 |
1.30e-25 |
|
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: 109.71 E-value: 1.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 41 VHALFD-QAERaeragNIDRPLLRGPHRTYTYRDARTEAARIAEVLTQdHGLVPGNRVLLRGGNTVEMALAWLGTVYAGL 119
Cdd:cd12115 1 LHDLVEaQAAR-----TPDAIALVCGDESLTYAELNRRANRLAARLRA-AGVGPESRVGVCLERTPDLVVALLAVLKAGA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 120 IAVATMPLLRAGELANIIERAQPTLALcdgrllaelaaaqdqhpvlttivpfhtaTDPADLlqraqgkpgsmqpcptsad 199
Cdd:cd12115 75 AYVPLDPAYPPERLRFILEDAQARLVL----------------------------TDPDDL------------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 200 diALMAFTSGTTGAPKAAVHTHRDVLA---------GCEAWpRHVLKATPddivagspplaFTFGLGGLLVF-PMWAGAS 269
Cdd:cd12115 108 --AYVIYTSGSTGRPKGVAIEHRNAAAflqwaaaafSAEEL-AGVLASTS-----------ICFDLSVFELFgPLATGGK 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 270 VYFPDqpyTPETMVTLMRDAGVTISYTAPTfyrQMAPFAKKIGLPQ-LRICVSAGEGLP-DATRQLWKDATGIDMTDGIG 347
Cdd:cd12115 174 VVLAD---NVLALPDLPAAAEVTLINTVPS---AAAELLRHDALPAsVRVVNLAGEPLPrDLVQRLYARLQVERVVNLYG 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 348 ATE-----MFHIFISSAGGEArtgAIGKVVPGYTAKVVDDDGNEVPRGTVGKLAVIGPTGCK-YLDDPRQ--AKYVKDGW 419
Cdd:cd12115 248 PSEdttysTVAPVPPGASGEV---SIGRPLANTQAYVLDRALQPVPLGVPGELYIGGAGVARgYLGRPGLtaERFLPDPF 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 420 NYP------GDAFTQDADGYFFYQARDDDMIITAGYNVGGPEVEDALLRHPAVAECGVIGVPDEERGMVVKAVCVLKPGH 493
Cdd:cd12115 325 GPGarlyrtGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEPGA 404
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 496182614 494 TGDaamVKTLQDHVKATIAPFKYPRVVEFVTALPRTETGKLQRFKL 539
Cdd:cd12115 405 AGL---VEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
194-548 |
2.19e-25 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 110.57 E-value: 2.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 194 CPTSADDIALMAFTSGTTGAPKAAVHTHRDVLAGCEAWpRHVLKATPDDIVAGSPPLAFTFGLGGLLVFPMWAGASVYFP 273
Cdd:PRK08043 360 VKQQPEDAALILFTSGSEGHPKGVVHSHKSLLANVEQI-KTIADFTPNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLY 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 274 DQPYTPETMVTLMRDAGVTISYTAPTFYRQMAPFAKKIGLPQLRICVSAGEGLPDATRQLWKDATGIDMTDGIGATEMFH 353
Cdd:PRK08043 439 PSPLHYRIVPELVYDRNCTVLFGTSTFLGNYARFANPYDFARLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAP 518
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 354 IFISSAGGEARTGAIGKVVPGYTAKVVDDDGNEvpRGtvGKLAVIGPTGCK-YLD-------DPRQAKYVKD----GWNY 421
Cdd:PRK08043 519 VVSINVPMAAKPGTVGRILPGMDARLLSVPGIE--QG--GRLQLKGPNIMNgYLRvekpgvlEVPTAENARGemerGWYD 594
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 422 PGDAFTQDADGYFFYQARDDDMIITAGYNVGGPEVEDALLRHPAVAECGVIGVPDEERGMVVkavcVLkpgHTGDAAMVK 501
Cdd:PRK08043 595 TGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKQHATAIKSDASKGEAL----VL---FTTDSELTR 667
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 496182614 502 -TLQDHVKATIAP-FKYPRVVEFVTALPRTETGKLQRFKLRQAAATPQA 548
Cdd:PRK08043 668 eKLQQYAREHGVPeLAVPRDIRYLKQLPLLGSGKPDFVTLKSMVDEPEQ 716
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
58-539 |
2.39e-25 |
|
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: 108.88 E-value: 2.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 58 DRPLLRGPHRTYTYRDARTEAARIAEVLtQDHGLVPGNRVLLRGGNTVEMALAWLGTVYAGLIAVATMPLLRAGELANII 137
Cdd:cd17652 2 DAPAVVFGDETLTYAELNARANRLARLL-AARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 138 ERAQPTLALcdgrllaelaaaqdqhpvlttivpfhtatdpadllqraqgkpgsmqpcpTSADDIALMAFTSGTTGAPKAA 217
Cdd:cd17652 81 ADARPALLL-------------------------------------------------TTPDNLAYVIYTSGSTGRPKGV 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 218 VHTHRDVLAGCEAWPRHvLKATPDDIV---------AGSPPLAFTFGLGGLLVFPmwaGASVYFPDQPYTpetmvTLMRD 288
Cdd:cd17652 112 VVTHRGLANLAAAQIAA-FDVGPGSRVlqfaspsfdASVWELLMALLAGATLVLA---PAEELLPGEPLA-----DLLRE 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 289 AGVTISYTAPTFYRQMAPfakkIGLPQLRICVSAGEGLPDATRQLWkdATGIDMTDGIGATEmfhIFISSAGGEARTGA- 367
Cdd:cd17652 183 HRITHVTLPPAALAALPP----DDLPDLRTLVVAGEACPAELVDRW--APGRRMINAYGPTE---TTVCATMAGPLPGGg 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 368 ---IGKVVPGYTAKVVDDDGNEVPRGTVGKLAVIGPTGCK-YLDDPRQA--KYVKDGWNYP-------GDAFTQDADGYF 434
Cdd:cd17652 254 vppIGRPVPGTRVYVLDARLRPVPPGVPGELYIAGAGLARgYLNRPGLTaeRFVADPFGAPgsrmyrtGDLARWRADGQL 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 435 FYQARDDDMIITAGYNVGGPEVEDALLRHPAVAECGVIGVPDEERGMVVKAVCVLKPGHTGDAAmvkTLQDHVKATIAPF 514
Cdd:cd17652 334 EFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAPGAAPTAA---ELRAHLAERLPGY 410
|
490 500
....*....|....*....|....*
gi 496182614 515 KYPRVVEFVTALPRTETGKLQRFKL 539
Cdd:cd17652 411 MVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
455-533 |
3.76e-25 |
|
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: 98.77 E-value: 3.76e-25
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496182614 455 EVEDALLRHPAVAECGVIGVPDEERGMVVKAVCVLKPGHTgdaAMVKTLQDHVKATIAPFKYPRVVEFVTALPRTETGK 533
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVE---LLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
44-539 |
1.23e-24 |
|
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: 107.03 E-value: 1.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 44 LFdqAERAERAGniDRPLLRGPHRTYTYRDARTEAARIAEVLTQDhGLVPGNRVLLRGGNTVEMALAWLGTVYAGliaVA 123
Cdd:cd17655 2 LF--EEQAEKTP--DHTAVVFEDQTLTYRELNERANQLARTLREK-GVGPDTIVGIMAERSLEMIVGILGILKAG---GA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 124 TMPLlragELANIIERAQPTLALCDGRLLaeLAAAQDQHPVLttivpfHTATDPADLLQRAQGKPGSMQPCPTSADDIAL 203
Cdd:cd17655 74 YLPI----DPDYPEERIQYILEDSGADIL--LTQSHLQPPIA------FIGLIDLLDEDTIYHEESENLEPVSKSDDLAY 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 204 MAFTSGTTGAPKAAVHTHRDVLAGCEAWPRHVLKATPDDIVAGSPplaFTFGLGGLLVF-PMWAGASVY-FPDQPYTP-E 280
Cdd:cd17655 142 VIYTSGSTGKPKGVMIEHRGVVNLVEWANKVIYQGEHLRVALFAS---ISFDASVTEIFaSLLSGNTLYiVRKETVLDgQ 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 281 TMVTLMRDAGVTISYTAPTfYRQMAPFAKKIGLPQLRICVSAGEGLPDATRQLWKD--ATGIDMTDGIGATE-----MFH 353
Cdd:cd17655 219 ALTQYIRQNRITIIDLTPA-HLKLLDAADDSEGLSLKHLIVGGEALSTELAKKIIElfGTNPTITNAYGPTEttvdaSIY 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 354 IFISSAGGEARTgAIGKVVPGYTAKVVDDDGNEVPRGTVGKLAVIG----------P--TGCKYLDDPrqakYVKDGWNY 421
Cdd:cd17655 298 QYEPETDQQVSV-PIGKPLGNTRIYILDQYGRPQPVGVAGELYIGGegvargylnrPelTAEKFVDDP----FVPGERMY 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 422 -PGDAFTQDADGYFFYQARDDDMIITAGYNVGGPEVEDALLRHPAVAECGVIGVPDEERGMVVKAVCVLKPGHTgdaamV 500
Cdd:cd17655 373 rTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEKELP-----V 447
|
490 500 510
....*....|....*....|....*....|....*....
gi 496182614 501 KTLQDHVKATIAPFKYPRVVEFVTALPRTETGKLQRFKL 539
Cdd:cd17655 448 AQLREFLARELPDYMIPSYFIKLDEIPLTPNGKVDRKAL 486
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
68-546 |
2.06e-24 |
|
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: 106.99 E-value: 2.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 68 TYTYRDARTEAARIAEVLTQDHGLVPGNRVLLRGGNTVEMALAWLGTVYAGLIAVATMPLLRAGELANIIERaqptlalC 147
Cdd:cd05938 5 TYTYRDVDRRSNQAARALLAHAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRC-------C 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 148 DGRLL---AELAAAQDqhPVLTTI------VPFHTATDPAD----LLQRAQGKPGsmQPCPTSA------DDIALMAFTS 208
Cdd:cd05938 78 GAKVLvvaPELQEAVE--EVLPALradgvsVWYLSHTSNTEgvisLLDKVDAASD--EPVPASLrahvtiKSPALYIYTS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 209 GTTGAPKAAVHTHRDVLAGCEAWprHVLKATPDDIVAGSPPL----AFTFGLGGLLVfpmwAGASVY---------FPD- 274
Cdd:cd05938 154 GTTGLPKAARISHLRVLQCSGFL--SLCGVTADDVIYITLPLyhssGFLLGIGGCIE----LGATCVlkpkfsasqFWDd 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 275 -QPYTpetmVTLMRDAGVTISYTAPTfyrqmapfAKKIGLPQLRICVSAGEGL-PDATRQLWKDATGIDMTDGIGATEMF 352
Cdd:cd05938 228 cRKHN----VTVIQYIGELLRYLCNQ--------PQSPNDRDHKVRLAIGNGLrADVWREFLRRFGPIRIREFYGSTEGN 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 353 HIFISSAGgeaRTGAIGKVvpGYTAK-----------------VVDDDGN--EVPRGTVGKLavIGPTGCK-----YLDD 408
Cdd:cd05938 296 IGFFNYTG---KIGAVGRV--SYLYKllfpfelikfdvekeepVRDAQGFciPVAKGEPGLL--VAKITQQspflgYAGD 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 409 PRQA--KYVKD----GWNY--PGDAFTQDADGYFFYQARDDDMIITAGYNVGGPEVEDALLRHPAVAECGVIGV--PDEE 478
Cdd:cd05938 369 KEQTekKLLRDvfkkGDVYfnTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVYGVtvPGHE 448
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496182614 479 rGMVVKAVCVLKPGHTGDAamvKTLQDHVKATIAPFKYPRVVEFVTALPRTETGKLQRFKLRQAAATP 546
Cdd:cd05938 449 -GRIGMAAVKLKPGHEFDG---KKLYQHVREYLPAYARPRFLRIQDSLEITGTFKQQKVRLVEEGFNP 512
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
35-553 |
3.45e-24 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 106.50 E-value: 3.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 35 PDQANLVHALFDQAerAERAGniDRPLLRGPHRTYTYRDARTEAARIAEVLtQDHGLVPGNRVLLRGGNTVEMALAWLGT 114
Cdd:PRK08279 33 PDSKRSLGDVFEEA--AARHP--DRPALLFEDQSISYAELNARANRYAHWA-AARGVGKGDVVALLMENRPEYLAAWLGL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 115 VYAGliAVATMpL---LRAGELANIIERAQPTLALCDGRLLAELAAAQdQHPVLTTIVPFH---TATDP---ADLLQRAQ 185
Cdd:PRK08279 108 AKLG--AVVAL-LntqQRGAVLAHSLNLVDAKHLIVGEELVEAFEEAR-ADLARPPRLWVAggdTLDDPegyEDLAAAAA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 186 GKPgsmQPCPTS-----ADDIALMAFTSGTTGAPKAAVHTHRDVLAGCeAWPRHVLKATPDDIVAGSPPL----AFTFGL 256
Cdd:PRK08279 184 GAP---TTNPASrsgvtAKDTAFYIYTSGTTGLPKAAVMSHMRWLKAM-GGFGGLLRLTPDDVLYCCLPLyhntGGTVAW 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 257 GGLLVfpmwAGASV----------YFPDqpytpetmvtlmrdagvTISYTAPTF--------YRQMAPFAKKIGLPQLRI 318
Cdd:PRK08279 260 SSVLA----AGATLalrrkfsasrFWDD-----------------VRRYRATAFqyigelcrYLLNQPPKPTDRDHRLRL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 319 CVsaGEGL-PDATRQlWKDATGID-MTDGIGATE----MFHIFissaggeARTGAIGKvVPGYTAK-------------- 378
Cdd:PRK08279 319 MI--GNGLrPDIWDE-FQQRFGIPrILEFYAASEgnvgFINVF-------NFDGTVGR-VPLWLAHpyaivkydvdtgep 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 379 VVDDDGN--EVPRGTVGKLavIGPTGCK-----YLDDPR-QAKYVKDG------WNYPGDAFTQDADGYFFYQARDDDMI 444
Cdd:PRK08279 388 VRDADGRciKVKPGEVGLL--IGRITDRgpfdgYTDPEAsEKKILRDVfkkgdaWFNTGDLMRDDGFGHAQFVDRLGDTF 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 445 ITAGYNVGGPEVEDALLRHPAVAECGVIGVP----DEERGMVvkAVcVLKPGHTGD-AAMVKTLQDHVKATIAPFkYPRV 519
Cdd:PRK08279 466 RWKGENVATTEVENALSGFPGVEEAVVYGVEvpgtDGRAGMA--AI-VLADGAEFDlAALAAHLYERLPAYAVPL-FVRL 541
|
570 580 590
....*....|....*....|....*....|....
gi 496182614 520 VEfvtALPRTETGKLQRFKLRQAAATPqAEVKAP 553
Cdd:PRK08279 542 VP---ELETTGTFKYRKVDLRKEGFDP-SKVDDP 571
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
197-545 |
1.08e-23 |
|
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: 104.16 E-value: 1.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 197 SADDIALMAFTSGTTGAPKAAVHTHRDVLAGCEAWPRhVLKATPDDIVagsppLAF---TFGLGGLLVFPMW-AGASVYF 272
Cdd:cd05918 104 SPSDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGR-ALGLTSESRV-----LQFasyTFDVSILEIFTTLaAGGCLCI 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 273 PDQPYTPETMVTLMRDAGVTISYTAPTFYRQMAPfakkIGLPQLRICVSAGEGLPDATRQLWkdATGIDMTDGIGATE-- 350
Cdd:cd05918 178 PSEEDRLNDLAGFINRLRVTWAFLTPSVARLLDP----EDVPSLRTLVLGGEALTQSDVDTW--ADRVRLINAYGPAEct 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 351 -MFHIFISSAGGEARTgaIGKVVPGyTAKVVDDDGNE--VPRGTVGKLAVIGPTGCK-YLDDPRQ--AKYVKD-GWNYP- 422
Cdd:cd05918 252 iAATVSPVVPSTDPRN--IGRPLGA-TCWVVDPDNHDrlVPIGAVGELLIEGPILARgYLNDPEKtaAAFIEDpAWLKQe 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 423 -----------GDAFTQDADGYFFYQARDDDMIITAGYNVGGPEVEDALLRHPAVAECGVIGV----PDEERGMVVkAVC 487
Cdd:cd05918 329 gsgrgrrlyrtGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSLPGAKEVVVEVvkpkDGSSSPQLV-AFV 407
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496182614 488 VLKPGHTGDA--------------AMVKTLQDHVKATIAPFKYPRVVEFVTALPRTETGKLQRFKLRQAAAT 545
Cdd:cd05918 408 VLDGSSSGSGdgdslflepsdefrALVAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRALRELAES 479
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
70-550 |
3.87e-23 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 103.32 E-value: 3.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 70 TYRDARTEAARIAEVLTQDHGLVPGNRVLLRGGNTVE-----MALAWLGTVYAgliavatmPL---LRAGELANIIERAQ 141
Cdd:PRK05620 40 TFAAIGARAAALAHALHDELGITGDQRVGSMMYNCAEhlevlFAVACMGAVFN--------PLnkqLMNDQIVHIINHAE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 142 PTLALCDGRLLAELAAAQDQHPVLTTIVpfHTATDPADllQRAQGKPGSMQPCPTSA----------------DDIALMA 205
Cdd:PRK05620 112 DEVIVADPRLAEQLGEILKECPCVRAVV--FIGPSDAD--SAAAHMPEGIKVYSYEAlldgrstvydwpeldeTTAAAIC 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 206 FTSGTTGAPKAAVHTHRDVLAGCEAwprhvLKATPDdivagsppLAFTFGLGGLLVFPMW-------------AGASVYF 272
Cdd:PRK05620 188 YSTGTTGAPKGVVYSHRSLYLQSLS-----LRTTDS--------LAVTHGESFLCCVPIYhvlswgvplaafmSGTPLVF 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 273 PDQPYTPETMVTLMRDAGVTISYTAPTFYRQ-MAPFAKKIglPQ---LRICVSAGEGLPDATRQLWKDATGIDMTDGIGA 348
Cdd:PRK05620 255 PGPDLSAPTLAKIIATAMPRVAHGVPTLWIQlMVHYLKNP--PErmsLQEIYVGGSAVPPILIKAWEERYGVDVVHVWGM 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 349 TEMFHIFI-----SSAGGEARTG---AIGKVVPGYTAKVVDDDgnEVPRGT---VGKLAVIGPT-GCKYLDDPRQ----- 411
Cdd:PRK05620 333 TETSPVGTvarppSGVSGEARWAyrvSQGRFPASLEYRIVNDG--QVMESTdrnEGEIQVRGNWvTASYYHSPTEeggga 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 412 -------------AKYVKDGWNYPGDAFTQDADGYFFYQARDDDMIITAGYNVGGPEVEDALLRHPAVAECGVIGVPDEE 478
Cdd:PRK05620 411 astfrgedvedanDRFTADGWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDK 490
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496182614 479 RGMVVKAVCVLKPGHTGDAAMVKTLQDHVKATIAPFKYPRVVEFVTALPRTETGKLQRFKLRQAAATPQAEV 550
Cdd:PRK05620 491 WGERPLAVTVLAPGIEPTRETAERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDLRQHLADGDFEI 562
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
69-473 |
4.27e-23 |
|
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: 102.55 E-value: 4.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 69 YTYRDARTEAARIAEVLtQDHGLVPGNRVLLRGGNTVEMALAWLGTVYAGLIAVATMPLLRAGELANIIERAQptlalCD 148
Cdd:cd05932 7 FTWGEVADKARRLAAAL-RALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSE-----SK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 149 GRLLAELAAAQDQHPVL-----TTIVPFHTATDPADLLQR--AQGKPGSMQPcPTSADDIALMAFTSGTTGAPKAAVHTH 221
Cdd:cd05932 81 ALFVGKLDDWKAMAPGVpegliSISLPPPSAANCQYQWDDliAQHPPLEERP-TRFPEQLATLIYTSGTTGQPKGVMLTF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 222 RDVLAGCEAWPRHvLKATPDDIVAGSPPLAF----TFGLGGLLvfpmWAGASVYFPDqpyTPETMVTLMRDAGVTISYTA 297
Cdd:cd05932 160 GSFAWAAQAGIEH-IGTEENDRMLSYLPLAHvterVFVEGGSL----YGGVLVAFAE---SLDTFVEDVQRARPTLFFSV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 298 PTFYR--QMA----------------PF---------AKKIGLPQLRICVSAGEGLPDATrQLWKDATGIDMTDGIGATE 350
Cdd:cd05932 232 PRLWTkfQQGvqdkipqqklnlllkiPVvnslvkrkvLKGLGLDQCRLAGCGSAPVPPAL-LEWYRSLGLNILEAYGMTE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 351 MFHIFISSAGGEARTGAIGKVVPGYTAKVVDDdgnevprgtvGKLAVIGP-TGCKYLDDPRQ--AKYVKDGWNYPGDAFT 427
Cdd:cd05932 311 NFAYSHLNYPGRDKIGTVGNAGPGVEVRISED----------GEILVRSPaLMMGYYKDPEAtaEAFTADGFLRTGDKGE 380
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 496182614 428 QDADGYFFYQARDDDMIITA-GYNVGGPEVEDALLRHPAVAECGVIG 473
Cdd:cd05932 381 LDADGNLTITGRVKDIFKTSkGKYVAPAPIENKLAEHDRVEMVCVIG 427
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
23-553 |
1.35e-22 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 102.43 E-value: 1.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 23 PTLRYDLPELQIPDQANLVHALFDQAE-----------RAERAGNIDRPLLRGPHRTYTYRDARTEAARIAEVLTQdHGL 91
Cdd:PRK10252 427 PALLCGDVDILLPGEYAQLAQVNATAVeipettlsalvAQQAAKTPDAPALADARYQFSYREMREQVVALANLLRE-RGV 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 92 VPGNRVLLRGGNTVEMALAWLGTVYAGliaVATMPLLRA---GELANIIERAQPTLalcdgrllaeLAAAQDQHPVLTTI 168
Cdd:PRK10252 506 KPGDSVAVALPRSVFLTLALHAIVEAG---AAWLPLDTGypdDRLKMMLEDARPSL----------LITTADQLPRFADV 572
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 169 vPFHTATDPADLLQRAQGKP-GSMQPcptsaDDIALMAFTSGTTGAPKAAVHTHRDVLAGCEaWPRHVLKATPDDIVAGS 247
Cdd:PRK10252 573 -PDLTSLCYNAPLAPQGAAPlQLSQP-----HHTAYIIFTSGSTGRPKGVMVGQTAIVNRLL-WMQNHYPLTADDVVLQK 645
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 248 PPLAFTFGLGGLLvFPMWAGASVYF--PDQPYTPETMVTLMRDAGVTISYTAPT----FYRQMAPFAKKIGLPQLRICVS 321
Cdd:PRK10252 646 TPCSFDVSVWEFF-WPFIAGAKLVMaePEAHRDPLAMQQFFAEYGVTTTHFVPSmlaaFVASLTPEGARQSCASLRQVFC 724
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 322 AGEGLPDATRQLWKDATGIDMTDGIGATEMfHIFIS--SAGGEARTGAIGKVVP-GY----TA-KVVDDDGNEVPRGTVG 393
Cdd:PRK10252 725 SGEALPADLCREWQQLTGAPLHNLYGPTEA-AVDVSwyPAFGEELAAVRGSSVPiGYpvwnTGlRILDARMRPVPPGVAG 803
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 394 KLAVIG----------P--TGCKYLDDPrqakYVKDGWNY-PGDAFTQDADGYFFYQARDDDMIITAGYNVGGPEVEDAL 460
Cdd:PRK10252 804 DLYLTGiqlaqgylgrPdlTASRFIADP----FAPGERMYrTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAM 879
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 461 LRHPAVAECGVIGV--------PDEERGMVvkAVCVLKPGHTGDAAMvktLQDHVKATIAPFKYPRVVEFVTALPRTETG 532
Cdd:PRK10252 880 QALPDVEQAVTHACvinqaaatGGDARQLV--GYLVSQSGLPLDTSA---LQAQLRERLPPHMVPVVLLQLDQLPLSANG 954
|
570 580
....*....|....*....|.
gi 496182614 533 KLQRFKLRQAAATPQAEVKAP 553
Cdd:PRK10252 955 KLDRKALPLPELKAQVPGRAP 975
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
94-550 |
4.28e-22 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 99.70 E-value: 4.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 94 GNRVLLRGGNTVEMALAWLGTVYAGLIAVATMPLLRAGELANIIERAQPTLAL------CDGRLLAELAAAQDQHPVLTT 167
Cdd:PRK05857 66 GSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLPIAAIERFCQITDPAAALvapgskMASSAVPEALHSIPVIAVDIA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 168 IVPFHTATDPAdlLQRAQGKPGSmqpcptSADDIALMAFTSGTTGAPKAAVHTHRDVLAGCEAWPRHVLKATpdDIVAGS 247
Cdd:PRK05857 146 AVTRESEHSLD--AASLAGNADQ------GSEDPLAMIFTSGTTGEPKAVLLANRTFFAVPDILQKEGLNWV--TWVVGE 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 248 ---PPLAFTF--GLGGLLVFPMWAGASVYFPDQPytpETMVTLMRDAGVTISYTAPTFYRQMAPFAKKIG--LPQLRICV 320
Cdd:PRK05857 216 ttySPLPATHigGLWWILTCLMHGGLCVTGGENT---TSLLEILTTNAVATTCLVPTLLSKLVSELKSANatVPSLRLVG 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 321 SAGEGLPDATRQlWKDATGIDMTDGIGATEMFHIFI---SSAGGEAR--TGAIGKVVPGYTAKVVDDDG------NEVPR 389
Cdd:PRK05857 293 YGGSRAIAADVR-FIEATGVRTAQVYGLSETGCTALclpTDDGSIVKieAGAVGRPYPGVDVYLAATDGigptapGAGPS 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 390 GTVGKLAVIGPTG-CKYLDDP-RQAKYVKDGWNYPGDAFTQDADGYFFYQARDDDMIITAGYNVGGPEVEDALLRHPAVA 467
Cdd:PRK05857 372 ASFGTLWIKSPANmLGYWNNPeRTAEVLIDGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVR 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 468 ECGVIGVPDEERGMVV--KAVCVLKPGHTGDAAMVKTLQDHVKATIAPFKYPRVVEFVTALPRTETGKLQRFKLRQAAAT 545
Cdd:PRK05857 452 EAACYEIPDEEFGALVglAVVASAELDESAARALKHTIAARFRRESEPMARPSTIVIVTDIPRTQSGKVMRASLAAAATA 531
|
....*
gi 496182614 546 PQAEV 550
Cdd:PRK05857 532 DKARV 536
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
68-541 |
4.37e-22 |
|
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: 98.92 E-value: 4.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 68 TYTYRDARTEAarIAEVLtQDHGLVPGNRVLLRGGNTVEMALAWLGTVYAGLIAVatmPLlragELANIIERAQPTLALC 147
Cdd:cd17653 24 TYGELDAASNA--LANRL-LQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYV---PL----DAKLPSARIQAILRTS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 148 DGRLLAelaaaqdqhpvlttivpfhtatdpadllqraqgkpgsmqpCPTSADDIALMAFTSGTTGAPKAAVHTHRDVLAG 227
Cdd:cd17653 94 GATLLL----------------------------------------TTDSPDDLAYIIFTSGSTGIPKGVMVPHRGVLNY 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 228 CEaWPRHVLKATPDDIVAGSPPLAFTFGLGGLLVFPMWaGASVYFPDqpyTPETMVTLMRDagVTISYTAPTFYRQMAPf 307
Cdd:cd17653 134 VS-QPPARLDVGPGSRVAQVLSIAFDACIGEIFSTLCN-GGTLVLAD---PSDPFAHVART--VDALMSTPSILSTLSP- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 308 akkIGLPQLRICVSAGEGLPDATRQLWkdATGIDMTDGIGATEmfhIFISSAGGEARTG---AIGKVVPGYTAKVVDDDG 384
Cdd:cd17653 206 ---QDFPNLKTIFLGGEAVPPSLLDRW--SPGRRLYNAYGPTE---CTISSTMTELLPGqpvTIGKPIPNSTCYILDADL 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 385 NEVPRGTVGKLAVIGPT-GCKYLDDPRQA--KYVKDGWNYP------GDAFTQDADGYFFYQARDDDMIITAGYNVGGPE 455
Cdd:cd17653 278 QPVPEGVVGEICISGVQvARGYLGNPALTasKFVPDPFWPGsrmyrtGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEE 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 456 VEDALLRHPAVAECGVIGVpdeERGMVVKAVcvlkpghTGDAAMVKTLQDHVKATIAPFKYPRVVEFVTALPRTETGKLQ 535
Cdd:cd17653 358 IEEVVLQSQPEVTQAAAIV---VNGRLVAFV-------TPETVDVDGLRSELAKHLPSYAVPDRIIALDSFPLTANGKVD 427
|
....*.
gi 496182614 536 RFKLRQ 541
Cdd:cd17653 428 RKALRE 433
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
28-552 |
1.21e-21 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 99.86 E-value: 1.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 28 DLPELQIPDQANLV----------------HALFdqAERAERAGniDRPLLRGPHRTYTYRDARTEAARIAEVLtQDHGL 91
Cdd:PRK05691 2161 ELPLLAAAEQQQLLdslageagearldqtlHGLF--AAQAARTP--QAPALTFAGQTLSYAELDARANRLARAL-RERGV 2235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 92 VPGNRVLLRGGNTVEMALAWLGTVYAGLIAVATMPLLRAGELANIIERAQPTLALCDGRL---LAELAAA------QDQH 162
Cdd:PRK05691 2236 GPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHYMIEDSGIGLLLSDRALfeaLGELPAGvarwclEDDA 2315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 163 PVLTtivpfHTATDPADLLQRAQGKpgsmqpcptsaddiALMAFTSGTTGAPKAAVHTHRDVLAGCEAwprhVLKA---T 239
Cdd:PRK05691 2316 AALA-----AYSDAPLPFLSLPQHQ--------------AYLIYTSGSTGKPKGVVVSHGEIAMHCQA----VIERfgmR 2372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 240 PDDIVAGSPPLAFTFGLGGLLVfPMWAGASVYFPDQ-PYTPETMVTLMRDAGVTISYTAPTFYRQMAPFAKKIG--LPqL 316
Cdd:PRK05691 2373 ADDCELHFYSINFDAASERLLV-PLLCGARVVLRAQgQWGAEEICQLIREQQVSILGFTPSYGSQLAQWLAGQGeqLP-V 2450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 317 RICVSAGEGLP----DATRQLWKDATgidMTDGIGATEMFHIFISSAGGEA-RTGA----IGKVVPGYTAKVVDDDGNEV 387
Cdd:PRK05691 2451 RMCITGGEALTgehlQRIRQAFAPQL---FFNAYGPTETVVMPLACLAPEQlEEGAasvpIGRVVGARVAYILDADLALV 2527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 388 PRGTVGKLAVIGP------------TGCKYLDDPRQAKyvkDGWNY-PGDAFTQDADGYFFYQARDDDMIITAGYNVGGP 454
Cdd:PRK05691 2528 PQGATGELYVGGAglaqgyhdrpglTAERFVADPFAAD---GGRLYrTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELG 2604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 455 EVEDALLRHPAVAECGVIGVpDEERG--MVVKAVC-VLKPGHTGDAAMVKTLQDHVKATIAPFKYPRVVEFVTALPRTET 531
Cdd:PRK05691 2605 EIESRLLEHPAVREAVVLAL-DTPSGkqLAGYLVSaVAGQDDEAQAALREALKAHLKQQLPDYMVPAHLILLDSLPLTAN 2683
|
570 580
....*....|....*....|....*....
gi 496182614 532 GKLQRFKL--------RQAAATPQAEVKA 552
Cdd:PRK05691 2684 GKLDRRALpapdpelnRQAYQAPRSELEQ 2712
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
41-553 |
1.99e-21 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 99.26 E-value: 1.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 41 VHALF-DQAERAEragniDRPLLRGPHRTYTYRDARTEAARIAEVLTQdHGLVPGNRVLLRGGNTVEMALAWLGTVYAGL 119
Cdd:PRK12316 3059 VHRLFeEQVERTP-----DAVALAFGEQRLSYAELNRRANRLAHRLIE-RGVGPDVLVGVAVERSLEMVVGLLAILKAGG 3132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 120 IAVATMPLLRAGELANIIERAQPTLALCDGRLLaelaaaqdqhpvlttiVPFHTATDPADLLQRAQGKPGSMQPCPTSAD 199
Cdd:PRK12316 3133 AYVPLDPEYPEERLAYMLEDSGAQLLLSQSHLR----------------LPLAQGVQVLDLDRGDENYAEANPAIRTMPE 3196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 200 DIALMAFTSGTTGAPKAAVHTHRdVLAGCEAWPRHVLKATPDDIVAGSPPLAFTFGLGGLLVfPMWAGASVYF--PDQPY 277
Cdd:PRK12316 3197 NLAYVIYTSGSTGKPKGVGIRHS-ALSNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFW-PLMSGARVVLagPEDWR 3274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 278 TPETMVTLMRDAGVTISYTAPTFYRQMAPFAKKIGLPQLRICVSAGEGLPDATRQLWKDATGIDMTDGIGATEMFHIFIS 357
Cdd:PRK12316 3275 DPALLVELINSEGVDVLHAYPSMLQAFLEEEDAHRCTSLKRIVCGGEALPADLQQQVFAGLPLYNLYGPTEATITVTHWQ 3354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 358 SAGGEARTGAIGKVVPGYTAKVVDDDGNEVPRGTVGKLAVIGPTGCK-YLDDPRQAK-------YVKDGWNY-PGDAFTQ 428
Cdd:PRK12316 3355 CVEEGKDAVPIGRPIANRACYILDGSLEPVPVGALGELYLGGEGLARgYHNRPGLTAerfvpdpFVPGERLYrTGDLARY 3434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 429 DADGYFFYQARDDDMIITAGYNVGGPEVEDALLRHPAVAECGVIGVpdEERGMVVKAVCVLKPGHTGDAamvktLQDHVK 508
Cdd:PRK12316 3435 RADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLAV--DGRQLVAYVVPEDEAGDLREA-----LKAHLK 3507
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 496182614 509 ATIAPFKYPRVVEFVTALPRTETGKLQRFKL-RQAAATPQAEVKAP 553
Cdd:PRK12316 3508 ASLPEYMVPAHLLFLERMPLTPNGKLDRKALpRPDAALLQQDYVAP 3553
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
64-479 |
4.04e-21 |
|
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: 96.27 E-value: 4.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 64 GPHRTYTYRDARTEAARIAEVLtQDHGLVPGNRVLLRGGNTVEMALAWLGTVYAGLIAVATMPLLRAGELANIIERAQPT 143
Cdd:cd17640 1 KPPKRITYKDLYQEILDFAAGL-RSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 144 LALCDgrllaelaaaqdqhpvlttivpfhtatdpadllqraqgkpgsmqpcpTSADDIALMAFTSGTTGAPKAAVHTHRD 223
Cdd:cd17640 80 ALVVE-----------------------------------------------NDSDDLATIIYTSGTTGNPKGVMLTHAN 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 224 VLAGCeawpRHVLkatpdDIVAGSPPLAFtfglggLLVFPMW-------------AGAS------VYFPD--QPYTPETM 282
Cdd:cd17640 113 LLHQI----RSLS-----DIVPPQPGDRF------LSILPIWhsyersaeyfifaCGCSqaytsiRTLKDdlKRVKPHYI 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 283 VTLMR-----DAGVTISYTAPTFYRQM-APFAKKIGlpQLRICVSAGEGLPDATRQLWKdATGIDMTDGIGATEmfhifi 356
Cdd:cd17640 178 VSVPRlweslYSGIQKQVSKSSPIKQFlFLFFLSGG--IFKFGISGGGALPPHVDTFFE-AIGIEVLNGYGLTE------ 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 357 SSAGGEART------GAIGKVVPGYTAKVVDDDGNEV-PRGTVGKLAVIGPTGCK-YLDDPRQAKYV--KDGWNYPGDAF 426
Cdd:cd17640 249 TSPVVSARRlkcnvrGSVGRPLPGTEIKIVDPEGNVVlPPGEKGIVWVRGPQVMKgYYKNPEATSKVldSDGWFNTGDLG 328
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496182614 427 TQDADGYFFYQARDDDMII-TAGYNVGGPEVEDALLRHPAVAECGVIG----------VPDEER 479
Cdd:cd17640 329 WLTCGGELVLTGRAKDTIVlSNGENVEPQPIEEALMRSPFIEQIMVVGqdqkrlgaliVPNFEE 392
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
66-546 |
9.77e-21 |
|
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: 95.19 E-value: 9.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 66 HRTYTYRDARTEAARIAEVLTQDHGLVPGNRVLLRGGNTVEMALAWLGTVYAGLIAVATMPLLRAGELANiieraqpTLA 145
Cdd:cd05937 3 GKTWTYSETYDLVLRYAHWLHDDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIH-------CLK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 146 LCDGRLLaelaaaqdqhpvlttIVpfhtatDPadllqraqgkpgsmqpcptsaDDIALMAFTSGTTGAPKAAVHTHRDVL 225
Cdd:cd05937 76 LSGSRFV---------------IV------DP---------------------DDPAILIYTSGTTGLPKAAAISWRRTL 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 226 AGCeaWPR-HVLKATPDDIVAGSPPL----AFTFGL------GGLLVFPMWAGASVYFPDqpyTPETMVTLMRDAGVTIS 294
Cdd:cd05937 114 VTS--NLLsHDLNLKNGDRTYTCMPLyhgtAAFLGAcnclmsGGTLALSRKFSASQFWKD---VRDSGATIIQYVGELCR 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 295 Y---TAPTFYRQMApfakkiglpqlRICVSAGEGL-PDatrqLW---KDATGIDM-------TDGIGATEMFHIFISSAG 360
Cdd:cd05937 189 YllsTPPSPYDRDH-----------KVRVAWGNGLrPD----IWerfRERFNVPEigefyaaTEGVFALTNHNVGDFGAG 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 361 GEARTGAIGKVVPGYTAKVVDDDGN--------------EVPRGTVGKLAVIGPTGCK-----YL--DDPRQAKYVK--- 416
Cdd:cd05937 254 AIGHHGLIRRWKFENQVVLVKMDPEtddpirdpktgfcvRAPVGEPGEMLGRVPFKNReafqgYLhnEDATESKLVRdvf 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 417 ---DGWNYPGDAFTQDADGYFFYQARDDDMIITAGYNVGGPEVEDALLRHPAVAECGVIGV--PDEErGMVVKAVCVLKP 491
Cdd:cd05937 334 rkgDIYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGVkvPGHD-GRAGCAAITLEE 412
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 496182614 492 GHTGDAAMVKTLQD-HVKATIAPFKYPRVVEFVTALPRTETGKLQRFKLRQAAATP 546
Cdd:cd05937 413 SSAVPTEFTKSLLAsLARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVLRDEGVDP 468
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
46-476 |
5.90e-20 |
|
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: 93.27 E-value: 5.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 46 DQAERAERAGNidrpllrGPHRTYTYRDARTEAARIAEVLtQDHGLVPGNRVLLRGGNTVEMALAWLGTVYAGLIAVATM 125
Cdd:cd05921 10 DRTWLAEREGN-------GGWRRVTYAEALRQVRAIAQGL-LDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 126 P---LLRA--GELANIIERAQPTLALCD-----GRLLAELAAAQDQHPVLTTIVPFHTATDPADLLQRAQGKPGSMQPCP 195
Cdd:cd05921 82 PaysLMSQdlAKLKHLFELLKPGLVFAQdaapfARALAAIFPLGTPLVVSRNAVAGRGAISFAELAATPPTAAVDAAFAA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 196 TSADDIALMAFTSGTTGAPKAAVHTHRDV------LAGCEAWPRHvlkatPDDIVAGSPPLAFTFGLGGLLVFPMWAGAS 269
Cdd:cd05921 162 VGPDTVAKFLFTSGSTGLPKAVINTQRMLcanqamLEQTYPFFGE-----EPPVLVDWLPWNHTFGGNHNFNLVLYNGGT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 270 VYFPDQPYTP---ETMVTLMRDAGVTISYTAPTFYRQMAPFAKKIG------LPQLRICVSAGEGLP----DATRQLWKD 336
Cdd:cd05921 237 LYIDDGKPMPggfEETLRNLREISPTVYFNVPAGWEMLVAALEKDEalrrrfFKRLKLMFYAGAGLSqdvwDRLQALAVA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 337 ATG--IDMTDGIGATEMFHIFISSAGGEARTGAIGKVVPGYTAKVvdddgneVPRGTVGKLAVIGPT-GCKYLDDPRQ-- 411
Cdd:cd05921 317 TVGerIPMMAGLGATETAPTATFTHWPTERSGLIGLPAPGTELKL-------VPSGGKYEVRVKGPNvTPGYWRQPELta 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 412 AKYVKDGWNYPGDA--FTQDAD---GYFFYQARDDDMIITAGYNV------------GGPEVEDALLRHPAVAECGVIGV 474
Cdd:cd05921 390 QAFDEEGFYCLGDAakLADPDDpakGLVFDGRVAEDFKLASGTWVsvgplraravaaCAPLVHDAVVAGEDRAEVGALVF 469
|
..
gi 496182614 475 PD 476
Cdd:cd05921 470 PD 471
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
67-546 |
6.00e-20 |
|
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: 92.42 E-value: 6.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 67 RTYTYRDARTEAARIAEVLtQDHGLVPGNRVLLRGGNTVEMALAWLGTVYAGLIAVatmpllrageLANIIERAQPtLAL 146
Cdd:cd05940 2 EALTYAELDAMANRYARWL-KSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAA----------LINYNLRGES-LAH 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 147 CdgrllaelaaaqdqhpvLTTIVPFHTATDPAdllqraqgkpgsmqpcptsaddiaLMAFTSGTTGAPKAAVHTHRDVLA 226
Cdd:cd05940 70 C-----------------LNVSSAKHLVVDAA------------------------LYIYTSGTTGLPKAAIISHRRAWR 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 227 GCeAWPRHVLKATPDDIVAGSPPL----AFTFGLGGLLVfpmwAGASVY----FPDQPYTPETM---VTLMRDAGVTISY 295
Cdd:cd05940 109 GG-AFFAGSGGALPSDVLYTCLPLyhstALIVGWSACLA----SGATLVirkkFSASNFWDDIRkyqATIFQYIGELCRY 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 296 TAPTfyrQMAPFAKKiglPQLR-ICvsaGEGL-PDatrqLWKDATG----IDMTDGIGATEMFHIFISSAGgeaRTGAIG 369
Cdd:cd05940 184 LLNQ---PPKPTERK---HKVRmIF---GNGLrPD----IWEEFKErfgvPRIAEFYAATEGNSGFINFFG---KPGAIG 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 370 KVVP----GYTAKVV-----------DDDG--NEVPRGTVGKL-AVIGP----TGckYLDDPRQAKYVK-------DGWN 420
Cdd:cd05940 248 RNPSllrkVAPLALVkydlesgepirDAEGrcIKVPRGEPGLLiSRINPlepfDG--YTDPAATEKKILrdvfkkgDAWF 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 421 YPGDAFTQDADGYFFYQARDDDMIITAGYNVGGPEVEDALLRHPAVAECGVIGVP----DEERGMvvkAVCVLKPGHTGD 496
Cdd:cd05940 326 NTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQvpgtDGRAGM---AAIVLQPNEEFD 402
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 496182614 497 aamVKTLQDHVKATIAPFKYPRVVEFVTALPRTETGKLQRFKLRQAAATP 546
Cdd:cd05940 403 ---LSALAAHLEKNLPGYARPLFLRLQPEMEITGTFKQQKVDLRNEGFDP 449
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
39-539 |
1.11e-19 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 92.27 E-value: 1.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 39 NLVHALFDQAERaeragNIDRPLLRGPHRTYTYRDARTEAARIAEVLtQDHGLVPGNRVLLRGGNTVEMALAWLGTVYAG 118
Cdd:PRK04813 3 DIIETIEEFAQT-----QPDFPAYDYLGEKLTYGQLKEDSDALAAFI-DSLKLPDKSPIIVFGHMSPEMLATFLGAVKAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 119 --LIAVAT-MPLLRageLANIIERAQPTLALCdgrlLAELAAAQDQHPVLTtivpfhtatdpADLLQRAQGKPGSMQPC- 194
Cdd:PRK04813 77 haYIPVDVsSPAER---IEMIIEVAKPSLIIA----TEELPLEILGIPVIT-----------LDELKDIFATGNPYDFDh 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 195 PTSADDIALMAFTSGTTGAPKAAVHTHRDVLAGCEaWprhvlkATPDDIVAGSPP-LA---FTFGLGGLLVFPMWAGASV 270
Cdd:PRK04813 139 AVKGDDNYYIIFTSGTTGKPKGVQISHDNLVSFTN-W------MLEDFALPEGPQfLNqapYSFDLSVMDLYPTLASGGT 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 271 YFPdqpyTPETMVTLMRD---------AGVTISytAPTFYrQMAPFAKKIG---LPQLRICVSAGEGLPDATRQLWKDAt 338
Cdd:PRK04813 212 LVA----LPKDMTANFKQlfetlpqlpINVWVS--TPSFA-DMCLLDPSFNeehLPNLTHFLFCGEELPHKTAKKLLER- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 339 gidmtdgigatemF---HIFISSAGGEArTGA------------------IGKVVPGYTAKVVDDDGNEVPRGTVGKLAV 397
Cdd:PRK04813 284 -------------FpsaTIYNTYGPTEA-TVAvtsieitdemldqykrlpIGYAKPDSPLLIIDEEGTKLPDGEQGEIVI 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 398 IGPTGCK-YLDDPR---QAKYVKDG-WNY-PGDAFTQDaDGYFFYQARDDDMIITAGYNVGGPEVEDALLRHPAVAECGV 471
Cdd:PRK04813 350 SGPSVSKgYLNNPEktaEAFFTFDGqPAYhTGDAGYLE-DGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVV 428
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496182614 472 igVPDEERGMVVK--AVCVLKPGH-TGDAAMVKTLQDHVKATIAPFKYPRVVEFVTALPRTETGKLQRFKL 539
Cdd:PRK04813 429 --VPYNKDHKVQYliAYVVPKEEDfEREFELTKAIKKELKERLMEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
49-543 |
4.88e-19 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 90.67 E-value: 4.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 49 ERAERAGNIDRPLLRGPHRtYTYRDARTEAARIAEVLTQdHGLVPGNRVLLRGGNTVEMALAWLGTVYAGLIAVATMPLL 128
Cdd:PLN02479 27 ERAAVVHPTRKSVVHGSVR-YTWAQTYQRCRRLASALAK-RSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 129 RAGELANIIERAQPTLALCDG----------RLLAELAAAQDQHPVLttIVPFHTATDPADLlQRAQGKpGSM------- 191
Cdd:PLN02479 105 NAPTIAFLLEHSKSEVVMVDQefftlaeealKILAEKKKSSFKPPLL--IVIGDPTCDPKSL-QYALGK-GAIeyekfle 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 192 --------QPCPTSADDIALmAFTSGTTGAPKAAVHTHRDvlagceawprhvlkatpddivagspplAFTFGLGGLLVFP 263
Cdd:PLN02479 181 tgdpefawKPPADEWQSIAL-GYTSGTTASPKGVVLHHRG---------------------------AYLMALSNALIWG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 264 MWAGAsVYFPDQPY-------------------------TPETMVTLMRDAGVTISYTAPTFYRQM--APFAKKI-GLPQ 315
Cdd:PLN02479 233 MNEGA-VYLWTLPMfhcngwcftwtlaalcgtniclrqvTAKAIYSAIANYGVTHFCAAPVVLNTIvnAPKSETIlPLPR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 316 LRICVSAGEGlPDATRQLWKDATGIDMTDGIGATEMFHI--------------FISSAGGEARTGA--IG----KVVPGY 375
Cdd:PLN02479 312 VVHVMTAGAA-PPPSVLFAMSEKGFRVTHTYGLSETYGPstvcawkpewdslpPEEQARLNARQGVryIGleglDVVDTK 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 376 TAKVVDDDGNevprgTVGKLAVIGPTGCK-YLDDPR-QAKYVKDGWNYPGDAFTQDADGYFFYQARDDDMIITAGYNVGG 453
Cdd:PLN02479 391 TMKPVPADGK-----TMGEIVMRGNMVMKgYLKNPKaNEEAFANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISS 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 454 PEVEDALLRHPAVAECGVIGVPDEERGMVVKAVCVLKPG--HTGDAAMVKTLQDHVKATIAPFKYPRVVEFvTALPRTET 531
Cdd:PLN02479 466 LEVENVVYTHPAVLEASVVARPDERWGESPCAFVTLKPGvdKSDEAALAEDIMKFCRERLPAYWVPKSVVF-GPLPKTAT 544
|
570
....*....|..
gi 496182614 532 GKLQRFKLRQAA 543
Cdd:PLN02479 545 GKIQKHVLRAKA 556
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
179-540 |
6.86e-19 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 89.86 E-value: 6.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 179 DLLQRAQGKPGSMQPCpTSADDIALMAFTSGTTGAPKAAVHTHRDVLAGCEAwPRHVLKATPDDIVAGSPPLAFTFGLGG 258
Cdd:PLN02860 153 EMLKQRALGTTELDYA-WAPDDAVLICFTSGTTGRPKGVTISHSALIVQSLA-KIAIVGYGEDDVYLHTAPLCHIGGLSS 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 259 LLVFPMWAGASVYFPDqpYTPETMVTLMRDAGVTISYTAPTFYRQM-APFAKKI---GLPQLRICVSAGEGLP----DAT 330
Cdd:PLN02860 231 ALAMLMVGACHVLLPK--FDAKAALQAIKQHNVTSMITVPAMMADLiSLTRKSMtwkVFPSVRKILNGGGSLSsrllPDA 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 331 RQLWKDA---TGIDMTDG-----------------IGATEMFHIFISSAGGEARTGAIGKVVPGYTAKVVDDDGNevprg 390
Cdd:PLN02860 309 KKLFPNAklfSAYGMTEAcssltfmtlhdptlespKQTLQTVNQTKSSSVHQPQGVCVGKPAPHVELKIGLDESS----- 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 391 TVGKLAVIGP-TGCKYLDDP--RQAKYVKDGWNYPGDAFTQDADGYFFYQARDDDMIITAGYNVGGPEVEDALLRHPAVA 467
Cdd:PLN02860 384 RVGRILTRGPhVMLGYWGQNseTASVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVA 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 468 ECGVIGVPDEERGMVVKAVCVLKPG---------HTGDAAMV--KTLQDHV-KATIAPFKYPR-VVEFVTALPRTETGKL 534
Cdd:PLN02860 464 SVVVVGVPDSRLTEMVVACVRLRDGwiwsdnekeNAKKNLTLssETLRHHCrEKNLSRFKIPKlFVQWRKPFPLTTTGKI 543
|
....*.
gi 496182614 535 QRFKLR 540
Cdd:PLN02860 544 RRDEVR 549
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
169-537 |
1.17e-18 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 88.28 E-value: 1.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 169 VPFhtaTDPADLLQRaqgkpgsmQP---CPTSADDIALMAFTSGTTGAPKAAVHTHRD--VLAGCEAwprHVLKA---TP 240
Cdd:COG1541 61 LPF---TTKEDLRDN--------YPfglFAVPLEEIVRIHASSGTTGKPTVVGYTRKDldRWAELFA---RSLRAagvRP 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 241 DDIVAgsppLAFTFGL--GGL-----------LVFPMWAGasvyfpdqpyTPETMVTLMRDAGVTISYTAPTFYRQMAPF 307
Cdd:COG1541 127 GDRVQ----NAFGYGLftGGLglhygaerlgaTVIPAGGG----------NTERQLRLMQDFGPTVLVGTPSYLLYLAEV 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 308 AKKIGL----PQLRICVSAGEGLPDATRQLWKDATGIDMTDGIGATEM-FHIFISSaggEARTGAI---GKVVPgytaKV 379
Cdd:COG1541 193 AEEEGIdprdLSLKKGIFGGEPWSEEMRKEIEERWGIKAYDIYGLTEVgPGVAYEC---EAQDGLHiweDHFLV----EI 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 380 VDDDGNE-VPRGTVGKLAV--IGPTG-----------CKYLDDPRqakyvKDGWNYP------GdaftqdadgyffyqaR 439
Cdd:COG1541 266 IDPETGEpVPEGEEGELVVttLTKEAmpliryrtgdlTRLLPEPC-----PCGRTHPrigrilG---------------R 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 440 DDDMIITAGYNVGGPEVEDALLRHPAVAECGVIGVPDEERGMVVKAVCVLKPGHTgDAAMVKTLQDHVKATIapfKYPRV 519
Cdd:COG1541 326 ADDMLIIRGVNVFPSQIEEVLLRIPEVGPEYQIVVDREGGLDELTVRVELAPGAS-LEALAEAIAAALKAVL---GLRAE 401
|
410 420
....*....|....*....|
gi 496182614 520 VEFVTA--LPRTEtGKLQRF 537
Cdd:COG1541 402 VELVEPgsLPRSE-GKAKRV 420
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
69-541 |
1.45e-18 |
|
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: 88.64 E-value: 1.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 69 YTYRDARTEAARIAEVLTqDHGLVPGNRVLLRGGNTVEMALAWLGTVYAGLIAVATMPLLRAGELANIIERAQPTLALCD 148
Cdd:cd05915 25 TTYAEVYQRARRLMGGLR-ALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVLLFD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 149 GRLLAelaAAQDQHPVLTTIVPFHTATDPADLLQR--AQGKPGSMQPCPTSADDIALMAFTSGTTGAPKAAVHTHRDV-L 225
Cdd:cd05915 104 PNLLP---LVEAIRGELKTVQHFVVMDEKAPEGYLayEEALGEEADPVRVPERAACGMAYTTGTTGLPKGVVYSHRALvL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 226 AGCEAWPRHVLKATPDDIVAGSPPLAFTFGLGGLLVFPMWAGASVYFPDQPYTPETMVTLMRDAGVTISYTAPTFyrQMA 305
Cdd:cd05915 181 HSLAASLVDGTALSEKDVVLPVVPMFHVNAWCLPYAATLVGAKQVLPGPRLDPASLVELFDGEGVTFTAGVPTVW--LAL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 306 PFAK---KIGLPQLRICVSAGEGLPDATRQLwKDATGIDMTDGIGATEMFHIFIS--------------SAGGEARTG-- 366
Cdd:cd05915 259 ADYLestGHRLKTLRRLVVGGSAAPRSLIAR-FERMGVEVRQGYGLTETSPVVVQnfvkshleslseeeKLTLKAKTGlp 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 367 ----AIGKVVPgyTAKVVDDDGNevprgTVGKLAVIGPTGCK-YLDDPR--QAKYVKDGWNYPGDAFTQDADGYFFYQAR 439
Cdd:cd05915 338 iplvRLRVADE--EGRPVPKDGK-----ALGEVQLKGPWITGgYYGNEEatRSALTPDGFFRTGDIAVWDEEGYVEIKDR 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 440 DDDMIITAGYNVGGPEVEDALLRHPAVAECGVIGVPDEERGMVVKAVCVLKPGHTGDAAMVktlqDHVKATIAPFKY-PR 518
Cdd:cd05915 411 LKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVVVPRGEKPTPEELN----EHLLKAGFAKWQlPD 486
|
490 500
....*....|....*....|...
gi 496182614 519 VVEFVTALPRTETGKLQRFKLRQ 541
Cdd:cd05915 487 AYVFAEEIPRTSAGKFLKRALRE 509
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
67-500 |
1.70e-18 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 88.80 E-value: 1.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 67 RTYTYRDARTEAARIAEVLTQdHGLVPGNRVLLR---GGNTVEMALAWLGtvyAGLIAVATMPLLRAGELANIIERAQP- 142
Cdd:PRK09274 40 DELSFAELDARSDAIAHGLNA-AGIGRGMRAVLMvtpSLEFFALTFALFK---AGAVPVLVDPGMGIKNLKQCLAEAQPd 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 143 -----TLALCdGRLLAELAAAQDQHPVLTTIVPFHTATDPADLLQRAQGKPGSMQPcpTSADDIALMAFTSGTTGAPKAA 217
Cdd:PRK09274 116 afigiPKAHL-ARRLFGWGKPSVRRLVTVGGRLLWGGTTLATLLRDGAAAPFPMAD--LAPDDMAAILFTSGSTGTPKGV 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 218 VHTHRDVLAGCEAWpRHVLKATPDDI-VAGSPPLAFtFG--LGGLLVFPmwagasvYF-PDQPYT--PETMVTLMRDAGV 291
Cdd:PRK09274 193 VYTHGMFEAQIEAL-REDYGIEPGEIdLPTFPLFAL-FGpaLGMTSVIP-------DMdPTRPATvdPAKLFAAIERYGV 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 292 TISYTAPTFYRQMAPF--AKKIGLPQLRICVSAGEglPdATRQLWKDATGIdMTDGI------GATEMFHifISSAGGEA 363
Cdd:PRK09274 264 TNLFGSPALLERLGRYgeANGIKLPSLRRVISAGA--P-VPIAVIERFRAM-LPPDAeiltpyGATEALP--ISSIESRE 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 364 ---------RTGA---IGKVVPGYTAKVVD---------DDGNEVPRGTVGKLAVIGPTGCK-YLDDP---RQAKyVKDG 418
Cdd:PRK09274 338 ilfatraatDNGAgicVGRPVDGVEVRIIAisdapipewDDALRLATGEIGEIVVAGPMVTRsYYNRPeatRLAK-IPDG 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 419 ----WNYPGDAFTQDADGYFFYQARDDDMIITAGYNVGGPEVEDALLRHPAVAECGVIGVPdeERGMVVKAVCV-LKPGH 493
Cdd:PRK09274 417 qgdvWHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGVKRSALVGVG--VPGAQRPVLCVeLEPGV 494
|
....*..
gi 496182614 494 TGDAAMV 500
Cdd:PRK09274 495 ACSKSAL 501
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
53-536 |
2.09e-18 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 88.51 E-value: 2.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 53 RAGNIDRPLLRG-PH--RTYTYRDARTEAARIAEVLtQDHGLVPGNRVLLRGGNTVEMALAWLGTVYAGliAVATM---P 126
Cdd:PRK07768 11 NARTSPRGMVTGePDapVRHTWGEVHERARRIAGGL-AAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRG--ASLTMlhqP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 127 LLRAgELANIIERAQPTLALCDGRLLA------ELAAAQDQHPVLTTIVPFHTATDPADllqraqgkpgsmqPCPTSADD 200
Cdd:PRK07768 88 TPRT-DLAVWAEDTLRVIGMIGAKAVVvgepflAAAPVLEEKGIRVLTVADLLAADPID-------------PVETGEDD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 201 IALMAFTSGTTGAPKAAVHTHRDVLAGCEAWpRHVLKATPD-DIVAGSPPLAFTFGLGGLLVFPMWAGASVYF--P-DQP 276
Cdd:PRK07768 154 LALMQLTSGSTGSPKAVQITHGNLYANAEAM-FVAAEFDVEtDVMVSWLPLFHDMGMVGFLTVPMYFGAELVKvtPmDFL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 277 YTPETMVTLMRDAGVTISyTAPTF-Y----RQMAPFAK--KIGLPQLRICVSAGEGLPDATRQLWKDATG---------- 339
Cdd:PRK07768 233 RDPLLWAELISKYRGTMT-AAPNFaYallaRRLRRQAKpgAFDLSSLRFALNGAEPIDPADVEDLLDAGArfglrpeail 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 340 ----------------------IDMTDGiGATEMFHIFISSAGGEARTGA-IGKVVPGYTAKVVDDDGNEVPRGTVGKLA 396
Cdd:PRK07768 312 paygmaeatlavsfspcgaglvVDEVDA-DLLAALRRAVPATKGNTRRLAtLGPPLPGLEVRVVDEDGQVLPPRGVGVIE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 397 VIGPTGCKYLDDPRQAKYVKD--GWNYPGDAFTQDADGYFFYQARDDDMIITAGYNVGGPEVEDALLRHPAVAECGVIGV 474
Cdd:PRK07768 391 LRGESVTPGYLTMDGFIPAQDadGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVRPGNAVAV 470
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 475 ----PDEERGMVVkavcVLKPGHTGDAAMVKTLQDHVKATI--APFKYPRVVEFVTA--LPRTETGKLQR 536
Cdd:PRK07768 471 rldaGHSREGFAV----AVESNAFEDPAEVRRIRHQVAHEVvaEVGVRPRNVVVLGPgsIPKTPSGKLRR 536
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
414-545 |
2.74e-18 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 87.36 E-value: 2.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 414 YVKDGWNYPGDAFTQD-----ADGYFFYQARDDDMIITAGYNVGGPEVEDALLRHPAVAECGVIGVPDEERGMVVKAVCV 488
Cdd:PRK07445 315 YYPQILDSQGIFETDDlgyldAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYV 394
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 496182614 489 LKPGHTGdaamVKTLQDHVKATIAPFKYPRVVEFVTALPRTETGKLQRFKLRQAAAT 545
Cdd:PRK07445 395 PKDPSIS----LEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQQIAVQ 447
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
48-384 |
6.40e-18 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 87.24 E-value: 6.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 48 AERAERAGniDRPLL-----RGPHRTYTYRDARTEAARIAEVLTqDHGLVPGNRVLLRGGNTVEMALAWLGTVYAGLIAV 122
Cdd:PRK08180 46 VHWAQEAP--DRVFLaergaDGGWRRLTYAEALERVRAIAQALL-DRGLSAERPLMILSGNSIEHALLALAAMYAGVPYA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 123 ATMP---LLRA--GELANIIERAQPTLALCD--GRLLAELAAAQDQH-PVLTT--IVPFHTATDPADLLQRAQGKPGSMQ 192
Cdd:PRK08180 123 PVSPaysLVSQdfGKLRHVLELLTPGLVFADdgAAFARALAAVVPADvEVVAVrgAVPGRAATPFAALLATPPTAAVDAA 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 193 PCPTSADDIALMAFTSGTTGAPKAAVHTHRDVLAG----CEAWPrhVLKATPDDIVaGSPPLAFTFglGGLLVFPM--WA 266
Cdd:PRK08180 203 HAAVGPDTIAKFLFTSGSTGLPKAVINTHRMLCANqqmlAQTFP--FLAEEPPVLV-DWLPWNHTF--GGNHNLGIvlYN 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 267 GASVYFPDQPYTP---ETMVTLMRDAGVTISYTAPTFYRQMAP-------FAKKIgLPQLRICVSAGEGLPDATR----Q 332
Cdd:PRK08180 278 GGTLYIDDGKPTPggfDETLRNLREISPTVYFNVPKGWEMLVPalerdaaLRRRF-FSRLKLLFYAGAALSQDVWdrldR 356
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 496182614 333 LWKDATG--IDMTDGIGATEMFHIFISSAGGEARTGAIGKVVPGYTAKVVDDDG 384
Cdd:PRK08180 357 VAEATCGerIRMMTGLGMTETAPSATFTTGPLSRAGNIGLPAPGCEVKLVPVGG 410
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
198-483 |
1.98e-17 |
|
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: 84.82 E-value: 1.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 198 ADDIALMAFTSGTTGAPKAAVHTHRDVLAGCEAWprhvlkATPDDIVAGSPPLAfTFGLGGLLVFPMwaGASVYFPDQPY 277
Cdd:cd05910 84 ADEPAAILFTSGSTGTPKGVVYRHGTFAAQIDAL------RQLYGIRPGEVDLA-TFPLFALFGPAL--GLTSVIPDMDP 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 278 T------PETMVTLMRDAGVTISYTAPTFYRQMAPFAKKIG--LPQLRICVSAGEGLPDATRQLWKDAT--GIDMTDGIG 347
Cdd:cd05910 155 TrparadPQKLVGAIRQYGVSIVFGSPALLERVARYCAQHGitLPSLRRVLSAGAPVPIALAARLRKMLsdEAEILTPYG 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 348 ATEMFHI-FISSAGGEARTGA---------IGKVVPGYTAKVVD---------DDGNEVPRGTVGKLAVIGPT-GCKYLD 407
Cdd:cd05910 235 ATEALPVsSIGSRELLATTTAatsggagtcVGRPIPGVRVRIIEiddepiaewDDTLELPRGEIGEITVTGPTvTPTYVN 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 408 DPRQAKYVK--DG----WNYPGDAFTQDADGYFFYQARDDDMIITAGYNVGGPEVEDALLRHPAVAECGVIGV--PDEER 479
Cdd:cd05910 315 RPVATALAKidDNsegfWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVGVgkPGCQL 394
|
....
gi 496182614 480 GMVV 483
Cdd:cd05910 395 PVLC 398
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
177-540 |
5.15e-17 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 82.79 E-value: 5.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 177 PADLLQRAQGKPGSMQPCPTSADDIALMAFTSGTTGAPKAAVHTHRDVLAGCEA----------W-----PRHV--LKAT 239
Cdd:PRK07824 13 PAQDERRAALLRDALRVGEPIDDDVALVVATSGTTGTPKGAMLTAAALTASADAthdrlggpgqWllalpAHHIagLQVL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 240 PDDIVAGSPPLAFTFGlGGLLVFPMWAGASVYFPDQPYT---PETMVTLMRDAGVTISytaptfyrqmapfakkigLPQL 316
Cdd:PRK07824 93 VRSVIAGSEPVELDVS-AGFDPTALPRAVAELGGGRRYTslvPMQLAKALDDPAATAA------------------LAEL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 317 RICVSAGEGLPDATRQLWKDAtGIDMTDGIGATEmfhifisSAGGEARTGaigKVVPGYTAKVVDddgnevprgtvGKLA 396
Cdd:PRK07824 154 DAVLVGGGPAPAPVLDAAAAA-GINVVRTYGMSE-------TSGGCVYDG---VPLDGVRVRVED-----------GRIA 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 397 VIGPTGCK-YLDDPRQAKYVKDGWNYPGDAFTQDaDGYFFYQARDDDMIITAGYNVGGPEVEDALLRHPAVAECGVIGVP 475
Cdd:PRK07824 212 LGGPTLAKgYRNPVDPDPFAEPGWFRTDDLGALD-DGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLP 290
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496182614 476 DEERGMVVKAVCVlkpGHTGDAAMVKTLQDHVKATIAPFKYPRVVEFVTALPRTETGKLQRFKLR 540
Cdd:PRK07824 291 DDRLGQRVVAAVV---GDGGPAPTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALV 352
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
67-536 |
6.05e-17 |
|
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: 83.29 E-value: 6.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 67 RTYTYRDARTEAARIAEVLtQDHGLVPGNRVLLRGGNTVEMALAWLGTVYAGLIAVATMPLLRAGELANIIERAQPTLAL 146
Cdd:cd17650 11 RQLTYRELNERANQLARTL-RGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYMLEDSGAKLLL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 147 cdgrllaelaaaqdqhpvlttivpfhtaTDPadllqraqgkpgsmqpcptsaDDIALMAFTSGTTGAPKAAVHTHRDVLA 226
Cdd:cd17650 90 ----------------------------TQP---------------------EDLAYVIYTSGTTGKPKGVMVEHRNVAH 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 227 GCEAWPRHV-LKATPD----------DIVAGSPPLAFTFGlGGLLVFPmwagasvyfPDQPYTPETMVTLMRDAGVTISY 295
Cdd:cd17650 121 AAHAWRREYeLDSFPVrllqmasfsfDVFAGDFARSLLNG-GTLVICP---------DEVKLDPAALYDLILKSRITLME 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 296 TAPTFYRQMAPFA--KKIGLPQLRICVSAGEGLP-----DATRQLwkdATGIDMTDGIGATEMF---HIFISSAG--GEA 363
Cdd:cd17650 191 STPALIRPVMAYVyrNGLDLSAMRLLIVGSDGCKaqdfkTLAARF---GQGMRIINSYGVTEATidsTYYEEGRDplGDS 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 364 RTGAIGKVVPGYTAKVVDDDGNEVPRGTVGKLAVIGPTGCK-YLDDPRQAK-------YVKDGWNY-PGDAFTQDADGYF 434
Cdd:cd17650 268 ANVPIGRPLPNTAMYVLDERLQPQPVGVAGELYIGGAGVARgYLNRPELTAerfvenpFAPGERMYrTGDLARWRADGNV 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 435 FYQARDDDMIITAGYNVGGPEVEDALLRHPAVAECGVIGVPDEERGMVVKAVCVlkPGHTGD-AAMVKTLQDHVKATIAP 513
Cdd:cd17650 348 ELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVREDKGGEARLCAYVV--AAATLNtAELRAFLAKELPSYMIP 425
|
490 500
....*....|....*....|...
gi 496182614 514 FKYPRVVefvtALPRTETGKLQR 536
Cdd:cd17650 426 SYYVQLD----ALPLTPNGKVDR 444
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
48-533 |
6.23e-17 |
|
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: 84.24 E-value: 6.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 48 AERAERAGNIDRPLL-----RGPHRTYTYRDARTEAARIAEVLtQDHGLVPGNRVLLRGGNTVEMALAWLGTVYAGLIAV 122
Cdd:cd05943 73 AENLLRHADADDPAAiyaaeDGERTEVTWAELRRRVARLAAAL-RALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWS 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 123 ATMPLLRAgelANIIER---AQPTLAL-CDG--------RLLAELAAAQDQHPVL--TTIVPFHTATDPADLLQR----- 183
Cdd:cd05943 152 SCSPDFGV---PGVLDRfgqIEPKVLFaVDAytyngkrhDVREKVAELVKGLPSLlaVVVVPYTVAAGQPDLSKIakalt 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 184 -----AQGKPGSMQPCPTSADDIALMAFTSGTTGAPKAAVHTHRDVLagCEAWPRHVLKAtpdDIVAGSPPLAFT----- 253
Cdd:cd05943 229 ledflATGAAGELEFEPLPFDHPLYILYSSGTTGLPKCIVHGAGGTL--LQHLKEHILHC---DLRPGDRLFYYTtcgwm 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 254 ---FGLGGLLVfpmwaGASVYFPD-QPYTPETMVtLMRDA---GVTISYTAPTFY----RQMAPFAKKIGLPQLRICVSA 322
Cdd:cd05943 304 mwnWLVSGLAV-----GATIVLYDgSPFYPDTNA-LWDLAdeeGITVFGTSAKYLdaleKAGLKPAETHDLSSLRTILST 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 323 GEGLPDATRQLWKDATGIDM--------TDGIGAtemfhifisSAGG----EARTGAIGKVVPGYTAKVVDDDGNEVpRG 390
Cdd:cd05943 378 GSPLKPESFDYVYDHIKPDVllasisggTDIISC---------FVGGnpllPVYRGEIQCRGLGMAVEAFDEEGKPV-WG 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 391 TVGKLAVIGPTGC---KYLDDPRQAKYvKDGW--NYP-----GDAFTQDADGYFFYQARDDDMIITAGYNVGGPEVEDAL 460
Cdd:cd05943 448 EKGELVCTKPFPSmpvGFWNDPDGSRY-RAAYfaKYPgvwahGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVV 526
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496182614 461 LRHPAVAECGVIGVPDEERGMVVKAVCVLKPGHTGDAAMVKTLQDHVKATIAPFKYPRVVEFVTALPRTETGK 533
Cdd:cd05943 527 EKIPEVEDSLVVGQEWKDGDERVILFVKLREGVELDDELRKRIRSTIRSALSPRHVPAKIIAVPDIPRTLSGK 599
|
|
| PaaK |
cd05913 |
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic ... |
193-537 |
1.08e-16 |
|
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: 82.29 E-value: 1.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 193 PCPTSADDIALMAFTSGTTGAPKAAVHTHRDVLAGCEAWPRhVLKA---TPDDIVAGSPPLA-FTFGLG--------GLL 260
Cdd:cd05913 72 LFAVPREKVVRIHASSGTTGKPTVVGYTKNDLDVWAELVAR-CLDAagvTPGDRVQNAYGYGlFTGGLGfhygaerlGAL 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 261 VFPMWAGASvyfpdqpytpETMVTLMRDAGVTISYTAPTFYRQMAPFAKKIGLP----QLRICVSAGEGLPDATRQLWKD 336
Cdd:cd05913 151 VIPAGGGNT----------ERQLQLIKDFGPTVLCCTPSYALYLAEEAEEEGIDprelSLKVGIFGAEPWTEEMRKRIER 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 337 ATGIDMTDGIGATEMFHifISSAGGEARTGAIGKVVPGYTAKVVDDDGNE-VPRGTVGKLAV--IGPTG----------- 402
Cdd:cd05913 221 RLGIKAYDIYGLTEIIG--PGVAFECEEKDGLHIWEDHFIPEIIDPETGEpVPPGEVGELVFttLTKEAmpliryrtrdi 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 403 CKYLDDP----RQAKYVkDGWnyPGdaftqdadgyffyqaRDDDMIITAGYNVGGPEVEDALLRHPAV-AECGVIGVPDE 477
Cdd:cd05913 299 TRLLPGPcpcgRTHRRI-DRI--TG---------------RSDDMLIIRGVNVFPSQIEDVLLKIPGLgPHYQLILTRQE 360
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496182614 478 ERG-MVVK-AVCVLKPGHTGDAAMVKTLQDHVKATIapfkypRV---VEFVT--ALPRTEtGKLQRF 537
Cdd:cd05913 361 HLDeLTIKvEVRPEADDDEKLEALKQRLERHIKSVL------GVtveVELVEpgSLPRSE-GKAKRV 420
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
196-534 |
3.36e-16 |
|
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: 80.91 E-value: 3.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 196 TSADDIALMAFTSGTTGAPKAAVHTHRDVLAGCEAW-PRHVLKATPDDIVAGSPPLAFTFGLGGLLVFPMWAGASVYFPD 274
Cdd:cd17648 91 TNSTDLAYAIYTSGTTGKPKGVLVEHGSVVNLRTSLsERYFGRDNGDEAVLFFSNYVFDFFVEQMTLALLNGQKLVVPPD 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 275 Q-PYTPETMVTLMRDAGVTISYTAPTFYrQMAPFAKkigLPQLRICVSAGEGLPDATRQLWKDATGIDMTDGIGATE--M 351
Cdd:cd17648 171 EmRFDPDRFYAYINREKVTYLSGTPSVL-QQYDLAR---LPHLKRVDAAGEEFTAPVFEKLRSRFAGLIINAYGPTEttV 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 352 FHIFISSAGGEARTGAIGKVVPGYTAKVVDDDGNEVPRGTVGKLAVIGP------------TGCKYLDDPRQAKYVKDGW 419
Cdd:cd17648 247 TNHKRFFPGDQRFDKSLGRPVRNTKCYVLNDAMKRVPVGAVGELYLGGDgvargylnrpelTAERFLPNPFQTEQERARG 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 420 NYP-----GDAFTQDADGYFFYQARDDDMIITAGYNVGGPEVEDALLRHPAVAECGVIGVPDEERGMVVKA---VC--VL 489
Cdd:cd17648 327 RNArlyktGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAKEDASQAQSRIQkylVGyyLP 406
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 496182614 490 KPGHTGDAAmvktLQDHVKATIAPFKYPRVVEFVTALPRTETGKL 534
Cdd:cd17648 407 EPGHVPESD----LLSFLRAKLPRYMVPARLVRLEGIPVTINGKL 447
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
199-439 |
4.92e-16 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 81.02 E-value: 4.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 199 DDIALMAFTSGTTGAPKAAVHTHRDVLAGCEAWPRHVLKATPDDIVAGSPPL-AFTFGLGGLlvFPMWAGASVYFPDQPY 277
Cdd:PRK06334 183 EDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSFLPPFhAYGFNSCTL--FPLLSGVPVVFAYNPL 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 278 TPETMVTLMRDAGVTISYTAPTFYRQMAPFAKKIG--LPQLRICVSAGEGLPDATRQ-LWKDATGIDMTDGIGATEMFH- 353
Cdd:PRK06334 261 YPKKIVEMIDEAKVTFLGSTPVFFDYILKTAKKQEscLPSLRFVVIGGDAFKDSLYQeALKTFPHIQLRQGYGTTECSPv 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 354 IFISSAGGEARTGAIGKVVPGYTAKVVDDDGN-EVPRGTVGKLAVIGPTGCK-YL-DDPRQAKYVKDG--WNYPGDAFTQ 428
Cdd:PRK06334 341 ITINTVNSPKHESCVGMPIRGMDVLIVSEETKvPVSSGETGLVLTRGTSLFSgYLgEDFGQGFVELGGetWYVTGDLGYV 420
|
250
....*....|.
gi 496182614 429 DADGYFFYQAR 439
Cdd:PRK06334 421 DRHGELFLKGR 431
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
387-543 |
4.95e-16 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 81.22 E-value: 4.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 387 VPRG--TVGKLAVIGPTGCK-YLDDPR-QAKYVKDGWNYPGDAFTQDADGYFFYQARDDDMIITAGYNVGGPEVEDALLR 462
Cdd:PLN03102 385 VPRDgkTMGEIVIKGSSIMKgYLKNPKaTSEAFKHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYK 464
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 463 HPAVAECGVIGVPDEERGMVVKAVCVLKPGHTGDAAMVKTLQ-------DHVKATIAPFKYPRVVEFVTALPRTETGKLQ 535
Cdd:PLN03102 465 YPKVLETAVVAMPHPTWGETPCAFVVLEKGETTKEDRVDKLVtrerdliEYCRENLPHFMCPRKVVFLQELPKNGNGKIL 544
|
....*...
gi 496182614 536 RFKLRQAA 543
Cdd:PLN03102 545 KPKLRDIA 552
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
42-539 |
1.18e-15 |
|
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: 79.14 E-value: 1.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 42 HALFD-QAERAEragniDRPLLRGPHRTYTYRDARTEAARIAEVLtQDHGLVPGNRVLLRGGNTVEMALAWLGTVYAGLI 120
Cdd:cd17645 1 HQLFEeQVERTP-----DHVAVVDRGQSLTYKQLNEKANQLARHL-RGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 121 AVATMPLLRAGELANIIERAQPTLALcdgrllaelaaaqdqhpvlttivpfhtatdpadllqraqgkpgsmqpcpTSADD 200
Cdd:cd17645 75 YVPIDPDYPGERIAYMLADSSAKILL-------------------------------------------------TNPDD 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 201 IALMAFTSGTTGAPKAAVHTHRDVLAGCEaWPRHVLKATPDDivAGSPPLAFTFGLGGLLVFPMW-AGASVYFPDQP--Y 277
Cdd:cd17645 106 LAYVIYTSGSTGLPKGVMIEHHNLVNLCE-WHRPYFGVTPAD--KSLVYASFSFDASAWEIFPHLtAGAALHVVPSErrL 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 278 TPETMVTLMRDAGVTISYTaPTfyrQMAPFAKKIGLPQLRICVSAGEGLPDATRQLWKDATGIDMTDGIGATEMFHIFIS 357
Cdd:cd17645 183 DLDALNDYFNQEGITISFL-PT---GAAEQFMQLDNQSLRVLLTGGDKLKKIERKGYKLVNNYGPTENTVVATSFEIDKP 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 358 SAggearTGAIGKVVPGYTAKVVDDDGNEVPRGTVGKLAVIGP-TGCKYLDDPRQA--KYVKDGWnYPGDAFTQDAD--- 431
Cdd:cd17645 259 YA-----NIPIGKPIDNTRVYILDEALQLQPIGVAGELCIAGEgLARGYLNRPELTaeKFIVHPF-VPGERMYRTGDlak 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 432 ----GYFFYQARDDDMIITAGYNVGGPEVEDALLRHPAVAECGVIGVPDEERGMVVKAVCVLKpghtgDAAMVKTLQDHV 507
Cdd:cd17645 333 flpdGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTAP-----EEIPHEELREWL 407
|
490 500 510
....*....|....*....|....*....|..
gi 496182614 508 KATIAPFKYPRVVEFVTALPRTETGKLQRFKL 539
Cdd:cd17645 408 KNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
196-536 |
1.25e-15 |
|
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: 79.40 E-value: 1.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 196 TSADDIALMAFTSGTTGAPKAAVHTHRDVLAGCEAWPRHVLKATPDDIVAGSpplAFTFGLGGLLVFPMW-AGASVYF-P 273
Cdd:cd17644 103 TQPENLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEYGITSSDRVLQFA---SIAFDVAAEEIYVTLlSGATLVLrP 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 274 DQPY-TPETMVTLMRDAGVTISYTAPTFYRQMAP--FAKKIGLPQ-LRICVSAGEGLPDATRQLWKDATG--IDMTDGIG 347
Cdd:cd17644 180 EEMRsSLEDFVQYIQQWQLTVLSLPPAYWHLLVLelLLSTIDLPSsLRLVIVGGEAVQPELVRQWQKNVGnfIQLINVYG 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 348 ATE-----MFHIFISSAGGEARTGAIGKVVPGYTAKVVDDDGNEVPRGTVGKLaVIGPTGCK--YLDDPR--QAKYVKDG 418
Cdd:cd17644 260 PTEatiaaTVCRLTQLTERNITSVPIGRPIANTQVYILDENLQPVPVGVPGEL-HIGGVGLArgYLNRPEltAEKFISHP 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 419 WNYP--------GDAFTQDADGYFFYQARDDDMIITAGYNVGGPEVEDALLRHPAVAECGVIGVPDEERGMVVKAVCVlk 490
Cdd:cd17644 339 FNSSeserlyktGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIV-- 416
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 496182614 491 pGHTGDAAMVKTLQDHVKATIAPFKYPRVVEFVTALPRTETGKLQR 536
Cdd:cd17644 417 -PHYEESPSTVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDR 461
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
40-541 |
2.32e-15 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 79.83 E-value: 2.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 40 LVHALfdqAERAERAGniDRPLLR------GPHRTYTYRDARTEAARIAEVLtQDHGlVPGNRVLLRGGNTVEMALAWLG 113
Cdd:PRK05691 11 LVQAL---QRRAAQTP--DRLALRfladdpGEGVVLSYRDLDLRARTIAAAL-QARA-SFGDRAVLLFPSGPDYVAAFFG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 114 TVYAGLIAVATMPLLRAGE-----LANIIERAQPTL-----ALCDGRLLAELAAAQDQHPVLTTivpfhTATDPAdLLQR 183
Cdd:PRK05691 84 CLYAGVIAVPAYPPESARRhhqerLLSIIADAEPRLlltvaDLRDSLLQMEELAAANAPELLCV-----DTLDPA-LAEA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 184 AQGKpgSMQPcptsaDDIALMAFTSGTTGAPKAAVHTHRDVLAGcEAWPRH--VLKATPDDIVAGSPPLAFTFGLGGLLV 261
Cdd:PRK05691 158 WQEP--ALQP-----DDIAFLQYTSGSTALPKGVQVSHGNLVAN-EQLIRHgfGIDLNPDDVIVSWLPLYHDMGLIGGLL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 262 FPMWAG------ASVYFPDQPYtpeTMVTLMRDAGVTISyTAPTF-YRQMAPFAKKIGLPQL-----RICVSAGE----- 324
Cdd:PRK05691 230 QPIFSGvpcvlmSPAYFLERPL---RWLEAISEYGGTIS-GGPDFaYRLCSERVSESALERLdlsrwRVAYSGSEpirqd 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 325 -----------------------GLPDATrqLWkdATGIDMTDGIGATEMFHIFISSAGGEARTGAI----GKVVPGYTA 377
Cdd:PRK05691 306 slerfaekfaacgfdpdsffasyGLAEAT--LF--VSGGRRGQGIPALELDAEALARNRAEPGTGSVlmscGRSQPGHAV 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 378 KVVD-DDGNEVPRGTVGKLAVIGPT-GCKYLDDPR-QAK-YVK-DG--WNYPGD-AFTQdaDGYFFYQARDDDMIITAGY 449
Cdd:PRK05691 382 LIVDpQSLEVLGDNRVGEIWASGPSiAHGYWRNPEaSAKtFVEhDGrtWLRTGDlGFLR--DGELFVTGRLKDMLIVRGH 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 450 NVGGPEVEDALLRHPAVAECGVIGV----PDEERGMVVKAVC------VLKPghtgdAAMVKTLQDHVKAtiAPFKYPRV 519
Cdd:PRK05691 460 NLYPQDIEKTVEREVEVVRKGRVAAfavnHQGEEGIGIAAEIsrsvqkILPP-----QALIKSIRQAVAE--ACQEAPSV 532
|
570 580
....*....|....*....|....
gi 496182614 520 VEFVT--ALPRTETGKLQRFKLRQ 541
Cdd:PRK05691 533 VLLLNpgALPKTSSGKLQRSACRL 556
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
62-226 |
4.83e-15 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 77.60 E-value: 4.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 62 LRGPHRTYTYRDARTEAARIAEVLTQdHGLVPGNRVLLRGGNTVEMALAWLGTVYAGLIAVATMPLLRAGELANIIERAQ 141
Cdd:PRK09029 22 LRLNDEVLTWQQLCARIDQLAAGFAQ-QGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLLEELLPSLT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 142 PTLALCDgrllaelaaaqDQHPVLTTIVPFHTATDPAdllqraqgkpgsMQPCPTSADDIALMAFTSGTTGAPKAAVHTH 221
Cdd:PRK09029 101 LDFALVL-----------EGENTFSALTSLHLQLVEG------------AHAVAWQPQRLATMTLTSGSTGLPKAAVHTA 157
|
....*
gi 496182614 222 RDVLA 226
Cdd:PRK09029 158 QAHLA 162
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
67-473 |
6.94e-15 |
|
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: 77.46 E-value: 6.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 67 RTYTYRDARTEAARIAEVLtQDHGLVPGNRVLLRGGNTVEmalaWL-GTVYAGLIAVATMPLLR---AGELANIIERAQP 142
Cdd:cd17641 10 QEFTWADYADRVRAFALGL-LALGVGRGDVVAILGDNRPE----WVwAELAAQAIGALSLGIYQdsmAEEVAYLLNYTGA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 143 TLALC-DGRLLAELAAAQDQHPVLTTIVPF-------------------------HTATDPaDLLQR--AQGKPgsmqpc 194
Cdd:cd17641 85 RVVIAeDEEQVDKLLEIADRIPSVRYVIYCdprgmrkyddprlisfedvvalgraLDRRDP-GLYERevAAGKG------ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 195 ptsaDDIALMAFTSGTTGAPKAAVHTHRDVLAGCEAW----PRHvlkatPDDIVAGSPPLAFTFGLGGLLVFPMWAGASV 270
Cdd:cd17641 158 ----EDVAVLCTTSGTTGKPKLAMLSHGNFLGHCAAYlaadPLG-----PGDEYVSVLPLPWIGEQMYSVGQALVCGFIV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 271 YFPDQpytPETMVTLMRDAGVTISYTAPTFYRQMA-----------PFAKKI---------------------------- 311
Cdd:cd17641 229 NFPEE---PETMMEDLREIGPTFVLLPPRVWEGIAadvrarmmdatPFKRFMfelgmklglraldrgkrgrpvslwlrla 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 312 ----------------GLPQLRICVSAGEGL-PDATRQLwkDATGIDMTDGIGATEMFHIFISSAGGEARTGAIGkvvpg 374
Cdd:cd17641 306 swladallfrplrdrlGFSRLRSAATGGAALgPDTFRFF--HAIGVPLKQLYGQTELAGAYTVHRDGDVDPDTVG----- 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 375 ytakvVDDDGNEVPRGTVGKLAVIGPTGCK-YLDDPR--QAKYVKDGWNYPGDAFTQDADGYFFYQARDDDMIITAGYNV 451
Cdd:cd17641 379 -----VPFPGTEVRIDEVGEILVRSPGVFVgYYKNPEatAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDVGTTSDGTR 453
|
490 500
....*....|....*....|...
gi 496182614 452 GGPE-VEDALLRHPAVAECGVIG 473
Cdd:cd17641 454 FSPQfIENKLKFSPYIAEAVVLG 476
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
194-432 |
4.29e-14 |
|
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: 74.94 E-value: 4.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 194 CPTSADDIALMAFTSGTTGAPKAAVHTHRDVLAGCEAWPRHVLKA-TPDDIVAGSPPLAFTFGLGGLLVFPMWAGASVYF 272
Cdd:cd17639 83 TDGKPDDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDRVPELlGPDDRYLAYLPLAHIFELAAENVCLYRGGTIGYG 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 273 PDQPYTPETMV-----------TLMrdAGV-----TISY-------TAPTFYRQM-----------------APFA---- 308
Cdd:cd17639 163 SPRTLTDKSKRgckgdltefkpTLM--VGVpaiwdTIRKgvlaklnPMGGLKRTLfwtayqsklkalkegpgTPLLdelv 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 309 -KKI-----GlpQLRICVSAGEGLPDATrQLWKDATGIDMTDGIGATEmfhifiSSAGG------EARTGAIGKVVPGYT 376
Cdd:cd17639 241 fKKVraalgG--RLRYMLSGGAPLSADT-QEFLNIVLCPVIQGYGLTE------TCAGGtvqdpgDLETGRVGPPLPCCE 311
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496182614 377 AKVVD-DDGNEV-----PRGTVgklAVIGPTGCK-YLDDPRQAK--YVKDGWNYPGDAFTQDADG 432
Cdd:cd17639 312 IKLVDwEEGGYStdkppPRGEI---LIRGPNVFKgYYKNPEKTKeaFDGDGWFHTGDIGEFHPDG 373
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
68-536 |
7.84e-14 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 75.20 E-value: 7.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 68 TYTYRDARTEAARIAEVLtQDHGLVPGNRVLLRGGNTVEMALAWLGTVYAGLIAVATMPLLRAGELANIIERAQPTLALC 147
Cdd:PRK05691 1156 SLDYAELHAQANRLAHYL-RDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELLLT 1234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 148 DGRLLAELAAAqdqhPVLTTIvpfhtATDPADLLQRAQGKPGsmqpCPTSADDIALMAFTSGTTGAPKAAVHTHRdVLAG 227
Cdd:PRK05691 1235 QSHLLERLPQA----EGVSAI-----ALDSLHLDSWPSQAPG----LHLHGDNLAYVIYTSGSTGQPKGVGNTHA-ALAE 1300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 228 CEAWPRHVLKATPDDIVAGSPPLAFTFGLGGLLvFPMWAGASVYF--PDQPYTPETMVTLMRDAGVTISYTAPTFYRQMA 305
Cdd:PRK05691 1301 RLQWMQATYALDDSDVLMQKAPISFDVSVWECF-WPLITGCRLVLagPGEHRDPQRIAELVQQYGVTTLHFVPPLLQLFI 1379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 306 PFAKKIGLPQLRICVSAGEGLPDATR-QLWKDATGIDMTDGIGATE----MFHIFISSAGGEarTGAIGKVVPGYTAKVV 380
Cdd:PRK05691 1380 DEPLAAACTSLRRLFSGGEALPAELRnRVLQRLPQVQLHNRYGPTEtainVTHWQCQAEDGE--RSPIGRPLGNVLCRVL 1457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 381 DDDGNEVPRGTVGKLaVIGPTGCK--YLDDPRQA--KYVKDGWNYP-------GDAFTQDADGYFFYQARDDDMIITAGY 449
Cdd:PRK05691 1458 DAELNLLPPGVAGEL-CIGGAGLArgYLGRPALTaeRFVPDPLGEDgarlyrtGDRARWNADGALEYLGRLDQQVKLRGF 1536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 450 NVGGPEVEDALLRHPAVAECGVIgVPDEERGMVVKAVCVLKPGHTGDAAMVKT-LQDHVKATIAPFKYPRvvefVTALPR 528
Cdd:PRK05691 1537 RVEPEEIQARLLAQPGVAQAAVL-VREGAAGAQLVGYYTGEAGQEAEAERLKAaLAAELPEYMVPAQLIR----LDQMPL 1611
|
....*...
gi 496182614 529 TETGKLQR 536
Cdd:PRK05691 1612 GPSGKLDR 1619
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
71-473 |
1.72e-13 |
|
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: 73.16 E-value: 1.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 71 YRDARTEA-ARIAEVLTQDHGlvpgnrVLLRGGNTVEMALAWLGTVYAGLIAVATMPLLRAGELANIIERAQPTLALCDG 149
Cdd:cd05933 15 YEACRQAAkAFLKLGLERFHG------VGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSEANILVVEN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 150 -RLLAELAAAQDQHPVLTTIVPFHTATDPA--------DLLQRAQGKPGS--MQPCPT-SADDIALMAFTSGTTGAPKAA 217
Cdd:cd05933 89 qKQLQKILQIQDKLPHLKAIIQYKEPLKEKepnlyswdEFMELGRSIPDEqlDAIISSqKPNQCCTLIYTSGTTGMPKGV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 218 VHTHRDVLAGCEAWPRHVLKATPDD---IVAGSPPLAFTfglgGLLVFPMWA----GASVYFPDQPYTPETMVTLMRDA- 289
Cdd:cd05933 169 MLSHDNITWTAKAASQHMDLRPATVgqeSVVSYLPLSHI----AAQILDIWLpikvGGQVYFAQPDALKGTLVKTLREVr 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 290 -----GV------------TISYTAPTFYRQMAPFAKKIGLPQLRICVSAGEGLPDATR-------QLWKDATGID---- 341
Cdd:cd05933 245 ptafmGVprvwekiqekmkAVGAKSGTLKRKIASWAKGVGLETNLKLMGGESPSPLFYRlakklvfKKVRKALGLDrcqk 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 342 ---MTDGIGAtEMFHIFIS-------------SAG-------GEARTGAIGKVVPGYTAKVV--DDDGNevprGTV---G 393
Cdd:cd05933 325 fftGAAPISR-ETLEFFLSlnipimelygmseTSGphtisnpQAYRLLSCGKALPGCKTKIHnpDADGI----GEIcfwG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 394 KLAVIGptgckYLDDPRQAKYV--KDGWNYPGDAFTQDADGYFFYQARDDDMIITA-GYNVGGPEVEDAL-LRHPAVAEC 469
Cdd:cd05933 400 RHVFMG-----YLNMEDKTEEAidEDGWLHSGDLGKLDEDGFLYITGRIKELIITAgGENVPPVPIEDAVkKELPIISNA 474
|
....
gi 496182614 470 GVIG 473
Cdd:cd05933 475 MLIG 478
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
39-425 |
7.40e-13 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 71.23 E-value: 7.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 39 NLVHALfdqAERAERAGniDRPLL------RGPHRTYTYRDARteaaRIAEVLTQ---DHGLVPGNRVLLRGGNTVEMAL 109
Cdd:PRK12582 50 SIPHLL---AKWAAEAP--DRPWLaqrepgHGQWRKVTYGEAK----RAVDALAQallDLGLDPGRPVMILSGNSIEHAL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 110 AWLGTVYAGLIAVATMP---LLRAG--ELANIIERAQPTLALCD-----GRLLAELAAAQDQHPVLTTIVPFHTATDPAD 179
Cdd:PRK12582 121 MTLAAMQAGVPAAPVSPaysLMSHDhaKLKHLFDLVKPRVVFAQsgapfARALAALDLLDVTVVHVTGPGEGIASIAFAD 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 180 LLQRAQGKPGSMQPCPTSADDIALMAFTSGTTGAPKAAVHTHRdVLAGCEAWPRHVLKATPDDIVAGS---PPLAFTFG- 255
Cdd:PRK12582 201 LAATPPTAAVAAAIAAITPDTVAKYLFTSGSTGMPKAVINTQR-MMCANIAMQEQLRPREPDPPPPVSldwMPWNHTMGg 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 256 ---LGGLLvfpmWAGASVYFPDQPYTP---ETMVTLMRDAGVTISYTAPTFYRQMAP-----------FAKKiglpqLRI 318
Cdd:PRK12582 280 nanFNGLL----WGGGTLYIDDGKPLPgmfEETIRNLREISPTVYGNVPAGYAMLAEamekddalrrsFFKN-----LRL 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 319 CVSAGEGLPDATRQ----LWKDATG--IDMTDGIGATEMFHIFISSAGGEARTGAIGKVVPGYTAKVvdddgneVPRGTV 392
Cdd:PRK12582 351 MAYGGATLSDDLYErmqaLAVRTTGhrIPFYTGYGATETAPTTTGTHWDTERVGLIGLPLPGVELKL-------APVGDK 423
|
410 420 430
....*....|....*....|....*....|....*.
gi 496182614 393 GKLAVIGPTGCK-YLDDPRQAKYVKD--GWNYPGDA 425
Cdd:PRK12582 424 YEVRVKGPNVTPgYHKDPELTAAAFDeeGFYRLGDA 459
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
196-536 |
2.71e-12 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 70.20 E-value: 2.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 196 TSADDIALMAFTSGTTGAPKAAVHTHRDVLagceawpRHVLKATP------DDIVAGSPPLAFTFGLGGLLVFPMWAGAS 269
Cdd:PRK05691 3866 SGPDNLAYVIYTSGSTGLPKGVMVEQRGML-------NNQLSKVPylalseADVIAQTASQSFDISVWQFLAAPLFGARV 3938
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 270 VYFP-DQPYTPETMVTLMRDAGVTISYTAPTFYRQMAPfAKKIGLPQLRICVSAGEGLP-DATRQLWKDATGIDMTDGIG 347
Cdd:PRK05691 3939 EIVPnAIAHDPQGLLAHVQAQGITVLESVPSLIQGMLA-EDRQALDGLRWMLPTGEAMPpELARQWLQRYPQIGLVNAYG 4017
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 348 ATE------MFHIFISSAGGEARtgAIGKVVPGYTAKVVDDDGNEVPRGTVGKLAVIGP-TGCKYLDDP-RQAK-YVKDG 418
Cdd:PRK05691 4018 PAEcsddvaFFRVDLASTRGSYL--PIGSPTDNNRLYLLDEALELVPLGAVGELCVAGTgVGRGYVGDPlRTALaFVPHP 4095
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 419 WNYPG-------DAFTQDADGYFFYQARDDDMIITAGYNVGGPEVEDALLRHPAVAEcGVIGVPDEERGMVVKAVCVLKP 491
Cdd:PRK05691 4096 FGAPGerlyrtgDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVRE-AAVAVQEGVNGKHLVGYLVPHQ 4174
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 496182614 492 GHTGDAAMVKTLQDHVKATIAPFKYPRVVEFVTALPRTETGKLQR 536
Cdd:PRK05691 4175 TVLAQGALLERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDR 4219
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
104-540 |
3.33e-12 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 68.69 E-value: 3.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 104 TVEMALAWLGTVYAGLIAVATMPLLRAGELA--------------NIIERAQPTLALCD-------GRLLAELAAAQDQH 162
Cdd:PLN03051 4 TVDAVIIYLAIVLAGCVVVSVADSFSAKEIAtrldisgakgvftqDVVLRGGRALPLYSkvveaapAKAIVLPAAGEPVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 163 PVLTTIVPFHtatdpADLLQRA--QGKPGSMQPCPTSADDIALMA--FTSGTTGAPKAAVHTHRDVL-AGCEAWPrHVlk 237
Cdd:PLN03051 84 VPLREQDLSW-----CDFLGVAaaQGSVGGNEYSPVYAPVESVTNilFSSGTTGEPKAIPWTHLSPLrCASDGWA-HM-- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 238 atpdDIVAGSP---PLAFTFGLGGLLVFPMWA-GASV-YFPDQPYTPEtMVTLMRDAGVTISYTAPTFYRQM----APFA 308
Cdd:PLN03051 156 ----DIQPGDVvcwPTNLGWMMGPWLLYSAFLnGATLaLYGGAPLGRG-FGKFVQDAGVTVLGLVPSIVKAWrhtgAFAM 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 309 KKIGLPQLRICVSAGEGlPDATRQLWKDATGIDMTDGI---GATEMFHIFISSAGGEART-GAIGKVVPGYTAKVVDDDG 384
Cdd:PLN03051 231 EGLDWSKLRVFASTGEA-SAVDDVLWLSSVRGYYKPVIeycGGTELASGYISSTLLQPQApGAFSTASLGTRFVLLNDNG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 385 NEVPRGT--VGKLAVIGP---TGCKYLDDPRQAKYVKDGWNYP---------GDAFTQDADGYFFYQARDDDMIITAGYN 450
Cdd:PLN03051 310 VPYPDDQpcVGEVALAPPmlgASDRLLNADHDKVYYKGMPMYGskgmplrrhGDIMKRTPGGYFCVQGRADDTMNLGGIK 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 451 VGGPEVEDALLR-HPAVAECGVIGVPDE----ERGMVVKAVCVLKPGHTG--DAAMVKTLQDHVKATIAP-FKYPRVVeF 522
Cdd:PLN03051 390 TSSVEIERACDRaVAGIAETAAVGVAPPdggpELLVIFLVLGEEKKGFDQarPEALQKKFQEAIQTNLNPlFKVSRVK-I 468
|
490
....*....|....*...
gi 496182614 523 VTALPRTETGKLQRFKLR 540
Cdd:PLN03051 469 VPELPRNASNKLLRRVLR 486
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
206-536 |
1.55e-11 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 67.07 E-value: 1.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 206 FTSGTTGAPKAAVHTHRDVLAGCE-AWPRHVLKATPDDIVAGSPP--LAFTFGLGGLLV----FPMWAGASVyfPDQPYT 278
Cdd:PTZ00237 261 YTSGTTGNSKAVVRSNGPHLVGLKyYWRSIIEKDIPTVVFSHSSIgwVSFHGFLYGSLSlgntFVMFEGGII--KNKHIE 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 279 PETMVTLMRDAgVTISYTAPTFYR---QMAPFAKKI----GLPQLRICVSAGEGLPDATRQLWKDATGIDMTDGIGATEM 351
Cdd:PTZ00237 339 DDLWNTIEKHK-VTHTLTLPKTIRyliKTDPEATIIrskyDLSNLKEIWCGGEVIEESIPEYIENKLKIKSSRGYGQTEI 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 352 FHIFISSAGGEART-GAIGKVVPGYTAKVVDDDGNEVPRGTVGKLAVIGP-----TGCKYLDDPRQAKYVKD--GWNYPG 423
Cdd:PTZ00237 418 GITYLYCYGHINIPyNATGVPSIFIKPSILSEDGKELNVNEIGEVAFKLPmppsfATTFYKNDEKFKQLFSKfpGYYNSG 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 424 DAFTQDADGYFFYQARDDDMIITAGYNVGGPEVEDALLRHPAVAECGVIGVPDEERGMVVKAVCVLKPGHTGDAAMVKTL 503
Cdd:PTZ00237 498 DLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPIGLLVLKQDQSNQSIDLNKL 577
|
330 340 350
....*....|....*....|....*....|....*..
gi 496182614 504 QDH----VKATIAPFKYPRVVEFVTALPRTETGKLQR 536
Cdd:PTZ00237 578 KNEinniITQDIESLAVLRKIIIVNQLPKTKTGKIPR 614
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
67-546 |
2.34e-11 |
|
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: 65.91 E-value: 2.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 67 RTYTYRDARTEAARIAEVLtQDHGLVPGNRVLLRGGNTVEMALAWLGTVYAGLIAVATMPLLRAGELANIIeraqpTLAL 146
Cdd:cd05939 2 RHWTFRELNEYSNKVANFF-QAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCI-----TVSK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 147 CDG---RLLAELAAAQDQHPVLTTIVPFHtatdpadllqraqgkpgsmqpcptsadDIALMAFTSGTTGAPKAAVHTHRD 223
Cdd:cd05939 76 AKAlifNLLDPLLTQSSTEPPSQDDVNFR---------------------------DKLFYIYTSGTTGLPKAAVIVHSR 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 224 VLAgCEAWPRHVLKATPDDIVAGSPPLAFT----FGLGGLLVFPMWA------GASVYFPD-QPYTpetmVTLMRDAGVT 292
Cdd:cd05939 129 YYR-IAAGAYYAFGMRPEDVVYDCLPLYHSaggiMGVGQALLHGSTVvirkkfSASNFWDDcVKYN----CTIVQYIGEI 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 293 ISYTAPTFYRqmaPFAKKiglPQLRICVsaGEGLpdaTRQLWKDAT---GIDMTDGI-GATEMfhifISSAGG-EARTGA 367
Cdd:cd05939 204 CRYLLAQPPS---EEEQK---HNVRLAV--GNGL---RPQIWEQFVrrfGIPQIGEFyGATEG----NSSLVNiDNHVGA 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 368 IGkVVPGYTAKV-------VDDDGNEVPRGTVGKLAVIGP--TGC---------------KYLDDPRQA-KYVKDGWNY- 421
Cdd:cd05939 269 CG-FNSRILPSVypirlikVDEDTGELIRDSDGLCIPCQPgePGLlvgkiiqndplrrfdGYVNEGATNkKIARDVFKKg 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 422 -----PGDAFTQDADGYFFYQARDDDMIITAGYNVGGPEVEDALLRHPAVAECGVIGV--PDEErgmvvkavcvlkpGHT 494
Cdd:cd05939 348 dsaflSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVYGVevPGVE-------------GRA 414
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 495 GDAAMV----KTLQDHVKATIA----PFKYPRVVEFVTALPRTETGKLQRFKLRQAAATP 546
Cdd:cd05939 415 GMAAIVdperKVDLDRFSAVLAkslpPYARPQFIRLLPEVDKTGTFKLQKTDLQKEGYDP 474
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
74-541 |
2.44e-11 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 65.94 E-value: 2.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 74 ARTEAarIAEVLTqDHGlvPGNRVLLRGGNTVEMALAWLGTVYAGlIAVATMPLLRAGelANIIERAQPTLALC------ 147
Cdd:PRK05851 39 GRAEN--VAARLL-DRD--RPGAVGLVGEPTVELVAAIQGAWLAG-AAVSILPGPVRG--ADDGRWADATLTRFagigvr 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 148 ----DGRLLAELAAAQdqhpvltTIVPFHTatdpadlLQRAQGKPGSMQPCPTSADDIALMAFTSGTTGAPKAAVHTHRD 223
Cdd:PRK05851 111 tvlsHGSHLERLRAVD-------SSVTVHD-------LATAAHTNRSASLTPPDSGGPAVLQGTAGSTGTPRTAILSPGA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 224 VLAGCEAWPRHVLKATPDDIVAGSPPLAFTFGLGGLLVfPMWAGASVYF-PDQPYT--PETMVTLMRDAGVTISyTAPTF 300
Cdd:PRK05851 177 VLSNLRGLNARVGLDAATDVGCSWLPLYHDMGLAFLLT-AALAGAPLWLaPTTAFSasPFRWLSWLSDSRATLT-AAPNF 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 301 -YRQMAPFAKKIG---LPQLRICVSAGEGLPDATRQLWKDAT---GID-----------------MTDGIGATEMFHIFI 356
Cdd:PRK05851 255 aYNLIGKYARRVSdvdLGALRVALNGGEPVDCDGFERFATAMapfGFDagaaapsyglaestcavTVPVPGIGLRVDEVT 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 357 SSAGGEARTGAI-GKVVPGYTAKVVDDDGN-EVPRGTVGKLAVIGP---TGckYL-DDPRQAkyvkDGWNYPGDAftqda 430
Cdd:PRK05851 335 TDDGSGARRHAVlGNPIPGMEVRISPGDGAaGVAGREIGEIEIRGAsmmSG--YLgQAPIDP----DDWFPTGDL----- 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 431 dGYFFYQA-----RDDDMIITAGYNVGGPEVEDALLRHPAVAECGVIGVPDEER----GMVVKAVCVLKPGHTGDAAMVK 501
Cdd:PRK05851 404 -GYLVDGGlvvcgRAKELITVAGRNIFPTEIERVAAQVRGVREGAVVAVGTGEGsarpGLVIAAEFRGPDEAGARSEVVQ 482
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 496182614 502 TLQDHVKATiapfkyPRVVEFVT--ALPRTETGKLQRFKLRQ 541
Cdd:PRK05851 483 RVASECGVV------PSDVVFVApgSLPRTSSGKLRRLAVKR 518
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
30-253 |
7.66e-11 |
|
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.
Pssm-ID: 341287 [Multi-domain] Cd Length: 588 Bit Score: 64.78 E-value: 7.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 30 PELQIPDQANLVHALF-DQAERAERAGNIDRPLLRG-------PHR-TYTYRDARTEAARIAEVLTQDHGLVPGNRVLLR 100
Cdd:cd17632 20 PGLRLAQIIATVMTGYaDRPALGQRATELVTDPATGrttlrllPRFeTITYAELWERVGAVAAAHDPEQPVRPGDFVAVL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 101 GGNTVEMALAWLGTVYAGLIAVATMPLLRAGELANIIERAQPTLALCDGRLLAELAAAQDQHPVLTTIVPF--------H 172
Cdd:cd17632 100 GFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLAVSAEHLDLAVEAVLEGGTPPRLVVFdhrpevdaH 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 173 TA-----------------TDPADLLQRAQGKPGSMQPCPTSADDIALMAFTSGTTGAPKAAVHTHRDVlagCEAWprhv 235
Cdd:cd17632 180 RAalesarerlaavgipvtTLTLIAVRGRDLPPAPLFRPEPDDDPLALLIYTSGSTGTPKGAMYTERLV---ATFW---- 252
|
250
....*....|....*...
gi 496182614 236 LKATPddIVAGSPPLAFT 253
Cdd:cd17632 253 LKVSS--IQDIRPPASIT 268
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
48-535 |
1.08e-10 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 64.43 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 48 AERAERAGNIDRPLL-----RGPHRTYTYRDARTEAARIAEVLtQDHGLVPGNRVLLRGGNTVE-----MALAWLGTVYA 117
Cdd:PRK03584 89 AENLLRHRRDDRPAIifrgeDGPRRELSWAELRRQVAALAAAL-RALGVGPGDRVAAYLPNIPEtvvamLATASLGAIWS 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 118 ------GLIAVatmpLLRAGELAniieraqPTLAL-CDG--------RLLAELAAAQDQHPVL--TTIVPFHTATDPADL 180
Cdd:PRK03584 168 scspdfGVQGV----LDRFGQIE-------PKVLIaVDGyryggkafDRRAKVAELRAALPSLehVVVVPYLGPAAAAAA 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 181 LQRAQ--------GKPGSMQPCPTSADDIALMAFTSGTTGAPKAAVHTHRDVLAgcEAWPRHVLKAtpdDIVAGSPPLAF 252
Cdd:PRK03584 237 LPGALlwedflapAEAAELEFEPVPFDHPLWILYSSGTTGLPKCIVHGHGGILL--EHLKELGLHC---DLGPGDRFFWY 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 253 T--------FGLGGLLVfpmwaGASVYFPD-QPYTPeTMVTLMR---DAGVTISYTAPTFYRQMAPF----AKKIGLPQL 316
Cdd:PRK03584 312 TtcgwmmwnWLVSGLLV-----GATLVLYDgSPFYP-DPNVLWDlaaEEGVTVFGTSAKYLDACEKAglvpGETHDLSAL 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 317 RICVSAGEGLPDATrQLW-KDATGIDM--------TDGIGAtemfhiFIssaGGEA----RTGAIGKVVPGYTAKVVDDD 383
Cdd:PRK03584 386 RTIGSTGSPLPPEG-FDWvYEHVKADVwlasisggTDICSC------FV---GGNPllpvYRGEIQCRGLGMAVEAWDED 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 384 GNEVpRGTVGKLAVIGPTGC---KYLDDPRQAKYVKDGWN-YP-----GDAFTQDADGYFFYQARDDDMIITAGYNVGGP 454
Cdd:PRK03584 456 GRPV-VGEVGELVCTKPFPSmplGFWNDPDGSRYRDAYFDtFPgvwrhGDWIEITEHGGVVIYGRSDATLNRGGVRIGTA 534
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 455 EVEDALLRHPAVAECGVIGVPDEERGMVVKAVCVLKPGHTGDAAMVKTLQDHVKATIAPFKYPRVVEFVTALPRTETGKL 534
Cdd:PRK03584 535 EIYRQVEALPEVLDSLVIGQEWPDGDVRMPLFVVLAEGVTLDDALRARIRTTIRTNLSPRHVPDKIIAVPDIPRTLSGKK 614
|
.
gi 496182614 535 Q 535
Cdd:PRK03584 615 V 615
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
203-546 |
1.39e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 60.05 E-value: 1.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 203 LMAFTSGTTGAPKAAVHTHRDVLAGCEAWprHVLKATPDD---IVAGspPLAFTFGL-GGLLVfPMWAGASVYFPDQPyT 278
Cdd:PRK08308 105 LLQYSSGTTGEPKLIRRSWTEIDREIEAY--NEALNCEQDetpIVAC--PVTHSYGLiCGVLA-ALTRGSKPVIITNK-N 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 279 PETMVTLMRDAGVTISYTAPTFYRQMAPFAKkiGLPQLRICVSAGEGLPDATRQLWKDATGIdMTDGIGATEMFHIFISS 358
Cdd:PRK08308 179 PKFALNILRNTPQHILYAVPLMLHILGRLLP--GTFQFHAVMTSGTPLPEAWFYKLRERTTY-MMQQYGCSEAGCVSICP 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 359 AGGEArtGAIGKVVPGYTAKVVDDDGNevPRGTVGKLAvigptgckylddpRQAKYVKD-GWnypgdaftQDADGYFFYQ 437
Cdd:PRK08308 256 DMKSH--LDLGNPLPHVSVSAGSDENA--PEEIVVKMG-------------DKEIFTKDlGY--------KSERGTLHFM 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 438 ARDDDMIITAGYNVGGPEVEDALLRHPAVAECGVIGVPDEERGMVVKAVCVLKpgHTGDAAmvkTLQDHVKATIAPFKYP 517
Cdd:PRK08308 311 GRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVISH--EEIDPV---QLREWCIQHLAPYQVP 385
|
330 340
....*....|....*....|....*....
gi 496182614 518 RVVEFVTALPRTETGKLQRfKLRQAAATP 546
Cdd:PRK08308 386 HEIESVTEIPKNANGKVSR-KLLELGEVT 413
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
68-539 |
2.44e-09 |
|
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: 59.80 E-value: 2.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 68 TYTYRDARTEAARIAEVLtQDHGLVPGNRVLLRGGNTVEMALAWLGTVYAGLIAVATMPLLRAGELANIIERAQptlalc 147
Cdd:cd17656 13 KLTYRELNERSNQLARFL-REKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSG------ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 148 dgrllAELAAAQDQHPVLTTIVPFHTATDPADLLQRAqgkpGSMQPCPTSADDIALMAFTSGTTGAPKAAVHTHRDVLAG 227
Cdd:cd17656 86 -----VRVVLTQRHLKSKLSFNKSTILLEDPSISQED----TSNIDYINNSDDLLYIIYTSGTTGKPKGVQLEHKNMVNL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 228 CEAWPRHVLKATPDDIVAGSpplAFTFGLGGLLVFPMW-AGASVYFPDQPYTPET--MVTLMRDAGVTISYTAPTFYRQM 304
Cdd:cd17656 157 LHFEREKTNINFSDKVLQFA---TCSFDVCYQEIFSTLlSGGTLYIIREETKRDVeqLFDLVKRHNIEVVFLPVAFLKFI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 305 apFAKKIGLPQLRICV----SAGEGL--PDATRQLWKDaTGIDMTDGIGATEMfHIF----ISSAGGEARTGAIGKVVPG 374
Cdd:cd17656 234 --FSEREFINRFPTCVkhiiTAGEQLviTNEFKEMLHE-HNVHLHNHYGPSET-HVVttytINPEAEIPELPPIGKPISN 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 375 YTAKVVDDDGNEVPRGTVGKLAVIGPT-GCKYLDDPR--QAKYVKDGWN------YPGDAFTQDADGYFFYQARDDDMII 445
Cdd:cd17656 310 TWIYILDQEQQLQPQGIVGELYISGASvARGYLNRQEltAEKFFPDPFDpnermyRTGDLARYLPDGNIEFLGRADHQVK 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 446 TAGYNVGGPEVEDALLRHPAVAECGVIGVPDEERGMVVKA-VCVLKPGHTGDaamvktLQDHVKATIAPFKYPRVVEFVT 524
Cdd:cd17656 390 IRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAyFVMEQELNISQ------LREYLAKQLPEYMIPSFFVPLD 463
|
490
....*....|....*
gi 496182614 525 ALPRTETGKLQRFKL 539
Cdd:cd17656 464 QLPLTPNGKVDRKAL 478
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
64-251 |
1.65e-08 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 57.42 E-value: 1.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 64 GPHRTYTYRDARTEAARIAEVLTQdHGLVPGNRVLLRGGNT-----VEMALAWLGTV----YAGLIAVATMPLLRAGELA 134
Cdd:PLN02736 74 GEYKWMTYGEAGTARTAIGSGLVQ-HGIPKGACVGLYFINRpewliVDHACSAYSYVsvplYDTLGPDAVKFIVNHAEVA 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 135 NIIERAQ--PTLALC-----DGRLLAELAAAQDQHPVLTT-----IVPFhtatdpADLLqrAQGKPGSMQPCPTSADDIA 202
Cdd:PLN02736 153 AIFCVPQtlNTLLSClseipSVRLIVVVGGADEPLPSLPSgtgveIVTY------SKLL--AQGRSSPQPFRPPKPEDVA 224
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 496182614 203 LMAFTSGTTGAPKAAVHTHRDVLAGCeAWPRHVLKATPDDIVAGSPPLA 251
Cdd:PLN02736 225 TICYTSGTTGTPKGVVLTHGNLIANV-AGSSLSTKFYPSDVHISYLPLA 272
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
179-541 |
2.10e-08 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 57.01 E-value: 2.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 179 DLLQRAQG--KPGSMQPCPTSADDIALMAFTSGTTGAPKAAVHTHRDVL-AGCEAWPRHVLKatPDDIVAGspPLAFTFG 255
Cdd:PLN03052 334 DFLARANGlrRPDEYKAVEQPVEAFTNILFSSGTTGEPKAIPWTQLTPLrAAADAWAHLDIR--KGDIVCW--PTNLGWM 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 256 LGGLLVFP-MWAGASVYFPDQPYTPETMVTLMRDAGVTISYTAPTFYR--QMAPFAKKIGLPQLRICVSAGEGlPDATRQ 332
Cdd:PLN03052 410 MGPWLVYAsLLNGATLALYNGSPLGRGFAKFVQDAKVTMLGTVPSIVKtwKNTNCMAGLDWSSIRCFGSTGEA-SSVDDY 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 333 LWKDATG--IDMTDGIGATEMFHIFISsaGGEARTGAIGKV-VPGYTAKVV--DDDGNEVPRGT--VGKLAvIGPT--GC 403
Cdd:PLN03052 489 LWLMSRAgyKPIIEYCGGTELGGGFVT--GSLLQPQAFAAFsTPAMGCKLFilDDSGNPYPDDApcTGELA-LFPLmfGA 565
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 404 KY--LDDPRQAKYVKdG---WN-----YPGDAFTQDADGYFFYQARDDDMIITAGYNVGGPEVEDALLR-HPAVAECGVI 472
Cdd:PLN03052 566 SStlLNADHYKVYFK-GmpvFNgkilrRHGDIFERTSGGYYRAHGRADDTMNLGGIKVSSVEIERVCNAaDESVLETAAI 644
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496182614 473 GVPDEERG---MVVKAVCVLKPGHTGDAAMVK-TLQDHVKATIAP-FKYPRVVeFVTALPRTETGKLQRFKLRQ 541
Cdd:PLN03052 645 GVPPPGGGpeqLVIAAVLKDPPGSNPDLNELKkIFNSAIQKKLNPlFKVSAVV-IVPSFPRTASNKVMRRVLRQ 717
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
198-541 |
2.24e-08 |
|
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: 56.73 E-value: 2.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 198 ADDIALMAFTSGTTGAPKAAVHTHRDVLAGCEAWpRHVLKATPDDIVAGSPPLAFTFGLGGLLVFPMWAGASVYF----- 272
Cdd:cd05908 105 ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAI-LNSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGMNQYLmptrl 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 273 ----------------------PD-------QPYTPETM-------VTLMRDAGVTISYT-APTFYRQMAPFAKK----- 310
Cdd:cd05908 184 firrpilwlkkasehkativssPNfgykyflKTLKPEKAndwdlssIRMILNGAEPIDYElCHEFLDHMSKYGLKrnail 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 311 --IGLPQlricVSAGEGLPDATRQLWKDATGID-MTDGIGATEMfhifISSAGGEARTGAIGKVVPGYTAKVVDDDGNEV 387
Cdd:cd05908 264 pvYGLAE----ASVGASLPKAQSPFKTITLGRRhVTHGEPEPEV----DKKDSECLTFVEVGKPIDETDIRICDEDNKIL 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 388 PRGTVGKLAVIGPTGCK-YLDDPRQAKYV--KDGWNYPGD-AFTQDADGYFFyqARDDDMIITAGYNV-------GGPEV 456
Cdd:cd05908 336 PDGYIGHIQIRGKNVTPgYYNNPEATAKVftDDGWLKTGDlGFIRNGRLVIT--GREKDIIFVNGQNVyphdierIAEEL 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 457 EDALLRHpaVAECGVIGVPDEERGMVVKAVCVLKPGHTgdAAMVKTLQDHVKAtiapFKYPRVVEFV--TALPRTETGKL 534
Cdd:cd05908 414 EGVELGR--VVACGVNNSNTRNEEIFCFIEHRKSEDDF--YPLGKKIKKHLNK----RGGWQINEVLpiRRIPKTTSGKV 485
|
....*..
gi 496182614 535 QRFKLRQ 541
Cdd:cd05908 486 KRYELAQ 492
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
64-226 |
1.09e-07 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 54.82 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 64 GPHRTYTYRDARTEAARIAEVLtQDHGLVPGNRVLLRGGNTVEMALAWLGTVYAGLIAVATMPLLRAGELANIIERAQPT 143
Cdd:PLN02430 72 GPYMWKTYKEVYEEVLQIGSAL-RASGAEPGSRVGIYGSNCPQWIVAMEACAAHSLICVPLYDTLGPGAVDYIVDHAEID 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 144 LALCDGRLLAEL-----AAAQDqhpvLTTIVPFHTATDPA---------------DLLQRAQGKPGsmQPCPTSADDIAL 203
Cdd:PLN02430 151 FVFVQDKKIKELlepdcKSAKR----LKAIVSFTSVTEEEsdkasqigvktyswiDFLHMGKENPS--ETNPPKPLDICT 224
|
170 180
....*....|....*....|...
gi 496182614 204 MAFTSGTTGAPKAAVHTHRDVLA 226
Cdd:PLN02430 225 IMYTSGTSGDPKGVVLTHEAVAT 247
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
195-272 |
1.67e-07 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 54.21 E-value: 1.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 195 PTSADDIALMAFTSGTTGAPKAAVHTHRDVLAGCEA---WPRHVL-KATPDDIVAGSPPLAFTFGLGGLLVFpMWAGASV 270
Cdd:PTZ00216 260 PENNDDLALIMYTSGTTGDPKGVMHTHGSLTAGILAledRLNDLIgPPEEDETYCSYLPLAHIMEFGVTNIF-LARGALI 338
|
..
gi 496182614 271 YF 272
Cdd:PTZ00216 339 GF 340
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
64-254 |
1.71e-07 |
|
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: 53.76 E-value: 1.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 64 GPHRTYTYRDARTEAARIAEVLTQdHGLVPGN--RVLLRGGNTVEMALAWLGTVYAGLIAVATMPLLRAGELANIIERAQ 141
Cdd:cd05927 1 GPYEWISYKEVAERADNIGSALRS-LGGKPAPasFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 142 PTLALCDGRLlaelaaaqdqhpvltTIVPFhtatdpADLLQraQGKPGSMQPCPTSADDIALMAFTSGTTGAPKAAVHTH 221
Cdd:cd05927 80 ISIVFCDAGV---------------KVYSL------EEFEK--LGKKNKVPPPPPKPEDLATICYTSGTTGNPKGVMLTH 136
|
170 180 190
....*....|....*....|....*....|....*.
gi 496182614 222 RDV---LAGCEAWPRHVLKATPDDIVAGSPPLAFTF 254
Cdd:cd05927 137 GNIvsnVAGVFKILEILNKINPTDVYISYLPLAHIF 172
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
68-271 |
3.32e-07 |
|
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: 53.12 E-value: 3.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 68 TYTYRDARTEAARIAEVLTQDHGLVPGNRVLLRGGNTVEMALAWLGTVYAGLIAVATMPLLRAGELANIIERAQPTLALC 147
Cdd:cd05905 14 TLTWGKLLSRAEKIAAVLQKKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLGFLLGTCKVRVALT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 148 DGRLLAELAAAQDQHPVLTTIVPFHTA-----TDPADLLQRAQGKPGSMQPcPTSADDIALMAFTSGTTGAPKAAVHTHR 222
Cdd:cd05905 94 VEACLKGLPKKLLKSKTAAEIAKKKGWpkildFVKIPKSKRSKLKKWGPHP-PTRDGDTAYIEYSFSSDGSLSGVAVSHS 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 496182614 223 DVLAGCeawprHVLKA----TPDDIVAGSppLAFTFGLGgllvFPMWAGASVY 271
Cdd:cd05905 173 SLLAHC-----RALKEacelYESRPLVTV--LDFKSGLG----LWHGCLLSVY 214
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
114-270 |
9.17e-07 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 51.66 E-value: 9.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 114 TVYAGLiavatmpllraGE--LANIIERAQPTLALCDGRLLAELAAAQDQHPVLTTIVPFHTATDPADLLQRAQ------ 185
Cdd:PLN02387 160 TIYASL-----------GEeaLCHSLNETEVTTVICDSKQLKKLIDISSQLETVKRVIYMDDEGVDSDSSLSGSsnwtvs 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 186 --------GKPGSMQPCPTSADDIALMAFTSGTTGAPKAAVHTHRDVLAGCEAWPRHVLKATPDDIVAGSPPLAFTFGLG 257
Cdd:PLN02387 229 sfseveklGKENPVDPDLPSPNDIAVIMYTSGSTGLPKGVMMTHGNIVATVAGVMTVVPKLGKNDVYLAYLPLAHILELA 308
|
170
....*....|...
gi 496182614 258 GLLVFpMWAGASV 270
Cdd:PLN02387 309 AESVM-AAVGAAI 320
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
58-229 |
3.13e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 46.86 E-value: 3.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 58 DRPLLRGPHRTYTYRDARTEAARIAEVLT---------------QDHGlVPGNRVLLRGGNTVEMALAWLGTVYAGLIAV 122
Cdd:PRK05850 9 ERASLQPDDAAFTFIDYEQDPAGVAETLTwsqlyrrtlnvaeelRRHG-STGDRAVILAPQGLEYIVAFLGALQAGLIAV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 123 A-TMPLLRAGElaniiERAqpTLALCDGRLLAELAAAQDQHPVLTTIVPFHTATDPA----DLLQRAQgkPGSMQPCPTS 197
Cdd:PRK05850 88 PlSVPQGGAHD-----ERV--SAVLRDTSPSVVLTTSAVVDDVTEYVAPQPGQSAPPvievDLLDLDS--PRGSDARPRD 158
|
170 180 190
....*....|....*....|....*....|..
gi 496182614 198 ADDIALMAFTSGTTGAPKAAVHTHRDVLAGCE 229
Cdd:PRK05850 159 LPSTAYLQYTSGSTRTPAGVMVSHRNVIANFE 190
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
64-254 |
7.48e-05 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 45.60 E-value: 7.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 64 GPHRTYTYRDARTEAARIAEVLtQDHGLVPGNRVLLRGGNTVEMALAWLGTVYAGLIAVATMPLLRAGELANIIERAQPT 143
Cdd:PLN02861 73 GPYVWLTYKEVYDAAIRIGSAI-RSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVS 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 144 LALC-DGRLLAELAAAQDQHPVLTTIVPFHTATDPADLLQRAQGKP----------GSmQPC---PTSADDIALMAFTSG 209
Cdd:PLN02861 152 IAFVqESKISSILSCLPKCSSNLKTIVSFGDVSSEQKEEAEELGVScfsweefslmGS-LDCelpPKQKTDICTIMYTSG 230
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 496182614 210 TTGAPKAAVHTHRDVLAGCEAwPRHVLK-----ATPDDIVAGSPPLAFTF 254
Cdd:PLN02861 231 TTGEPKGVILTNRAIIAEVLS-TDHLLKvtdrvATEEDSYFSYLPLAHVY 279
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
75-224 |
1.55e-03 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 41.25 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 75 RTEAARIAEVlTQdhglvPGNRVLLRGGNTVEMALAWLGTVYAGLIAVatmPLLragelaniieraQPTLALCDGRLLAE 154
Cdd:PRK07769 66 RAVGARLQQV-TK-----PGDRVAILAPQNLDYLIAFFGALYAGRIAV---PLF------------DPAEPGHVGRLHAV 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 155 LAaaqDQHPvlTTIVpfhTATDPADLLQR------AQGKP------------GSM-QPCPTSADDIALMAFTSGTTGAPK 215
Cdd:PRK07769 125 LD---DCTP--SAIL---TTTDSAEGVRKffrarpAKERPrviavdavpdevGATwVPPEANEDTIAYLQYTSGSTRIPA 196
|
....*....
gi 496182614 216 AAVHTHRDV 224
Cdd:PRK07769 197 GVQITHLNL 205
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
68-224 |
2.25e-03 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 40.88 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 68 TYTYRDARTEA--ARIAEVLTqdhglvPGNRVLLRGGNTVEMALAWLGTVYAGLIAVatmPLLrAGELANIIER------ 139
Cdd:PRK12476 70 TWTQLGVRLRAvgARLQQVAG------PGDRVAILAPQGIDYVAGFFAAIKAGTIAV---PLF-APELPGHAERldtalr 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 140 -AQPTLALCDG-------RLLAELAAAQDQHPVLTTIVPFHTATDpadllqraqgkpgsMQPCPTSADDIALMAFTSGTT 211
Cdd:PRK12476 140 dAEPTVVLTTTaaaeaveGFLRNLPRLRRPRVIAIDAIPDSAGES--------------FVPVELDTDDVSHLQYTSGST 205
|
170
....*....|...
gi 496182614 212 GAPKAAVHTHRDV 224
Cdd:PRK12476 206 RPPVGVEITHRAV 218
|
|
| PRK07868 |
PRK07868 |
acyl-CoA synthetase; Validated |
363-531 |
8.08e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236121 [Multi-domain] Cd Length: 994 Bit Score: 39.32 E-value: 8.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 363 ARTGAIGKVVPGyTAKV-------------VDDDG--NEVPRGTVGKL--AVIGPTgckyldDPRQAkyVKDGWNYPGDA 425
Cdd:PRK07868 766 AKIGSKGRPLPG-AGRVelaaydpehdlilEDDRGfvRRAEVNEVGVLlaRARGPI------DPTAS--VKRGVFAPADT 836
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496182614 426 -------FTQDADGYFFYQARDDDMIITAGYNVGGPEVEDALLRHPAVAECGVIGVPDEERGMVVKAVCvLKPGHTGDAA 498
Cdd:PRK07868 837 wisteylFRRDDDGDYWLVDRRGSVIRTARGPVYTEPVTDALGRIGGVDLAVTYGVEVGGRQLAVAAVT-LRPGAAITAA 915
|
170 180 190
....*....|....*....|....*....|...
gi 496182614 499 mvkTLQDHVkATIAPFKYPRVVEFVTALPRTET 531
Cdd:PRK07868 916 ---DLTEAL-ASLPVGLGPDIVHVVPEIPLSAT 944
|
|
| |
