|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
1-560 |
0e+00 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 1092.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 1 MANHSRPHICQCLTRLASVKRNAVVTVYGNRKRTGREFVDGVLSLAAGLIRLGLRNGDVVSIAAFNSDLFLEWLLAVALV 80
Cdd:PLN02860 1 MANHSQAHICQCLTRLATLRGNAVVTISGNRRRTGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 81 GGVVAPLNYRWSLKEAKMAMLLVEPVLLVTDETCVSWCIDVQNGDIPSLKWRVLMESTSTDFANELNQFLTTEMLKQRTL 160
Cdd:PLN02860 81 GGIVAPLNYRWSFEEAKSAMLLVRPVMLVTDETCSSWYEELQNDRLPSLMWQVFLESPSSSVFIFLNSFLTTEMLKQRAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 161 VPSLATYAWASDDAVVICFTSGTTGRPKGVTISHLAFITQSLAKIAIAGYGEDDVYLHTSPLVHIGGLSSAMAMLMVGAC 240
Cdd:PLN02860 161 GTTELDYAWAPDDAVLICFTSGTTGRPKGVTISHSALIVQSLAKIAIVGYGEDDVYLHTAPLCHIGGLSSALAMLMVGAC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 241 HVLLPKFDAKTALQVMEQNHITCFITVPAMMADLIRVNRTTKNGAENRGVRKILNGGGSLSSELLKEAVNIFPCARILSA 320
Cdd:PLN02860 241 HVLLPKFDAKAALQAIKQHNVTSMITVPAMMADLISLTRKSMTWKVFPSVRKILNGGGSLSSRLLPDAKKLFPNAKLFSA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 321 YGMTEACSSLTFMTLHDPTQESFKVT-------YPLLNQPKQGTCVGKPAPHIELMVKLDEdSSRVGKILTRGPHTMLRY 393
Cdd:PLN02860 321 YGMTEACSSLTFMTLHDPTLESPKQTlqtvnqtKSSSVHQPQGVCVGKPAPHVELKIGLDE-SSRVGRILTRGPHVMLGY 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 394 WGhqvaqENVETSESRSNEAWLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGVIDTR 473
Cdd:PLN02860 400 WG-----QNSETASVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSR 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 474 LGEMVVACVRLQEKWIWSDVE--NRKGSFQLSSETLKHHCRTQNLTGFKIPKRFVRWEKQFPLTTTGKVKRDEVRRQVLS 551
Cdd:PLN02860 475 LTEMVVACVRLRDGWIWSDNEkeNAKKNLTLSSETLRHHCREKNLSRFKIPKLFVQWRKPFPLTTTGKIRRDEVRREVLS 554
|
....*....
gi 22329863 552 HFQIMTSSL 560
Cdd:PLN02860 555 HLQSLPSNL 563
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
11-552 |
7.28e-115 |
|
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: 348.34 E-value: 7.28e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 11 QCLTRLASVKRNAVVTVYGNRKRTGREFVDGVLSLAAGLIRLGLRNGDVVSIAAFNSDLFLEWLLAVALVGGVVAPLNYR 90
Cdd:COG0318 3 DLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 91 WSLKEAKMAMLLVEPVLLVTdetcvswcidvqngdipslkwrvlmeststdfanelnqflttemlkqrtlvpslatyawa 170
Cdd:COG0318 83 LTAEELAYILEDSGARALVT------------------------------------------------------------ 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 171 sddaVVICFTSGTTGRPKGVTISHLAFITQSLAKIAIAGYGEDDVYLHTSPLVHIGGLS-SAMAMLMVGACHVLLPKFDA 249
Cdd:COG0318 103 ----ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTvGLLAPLLAGATLVLLPRFDP 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 250 KTALQVMEQNHITCFITVPAMMADLIRVNRttKNGAENRGVRKILNGGGSLSSELLKEAVNIFPCaRILSAYGMTEaCSS 329
Cdd:COG0318 179 ERVLELIERERVTVLFGVPTMLARLLRHPE--FARYDLSSLRLVVSGGAPLPPELLERFEERFGV-RIVEGYGLTE-TSP 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 330 LTFMTLHDPtqesfkvtypllnQPKQGTCVGKPAPHIELMVkLDEDSSRV-----GKILTRGPHTMLRYWGhqvaqeNVE 404
Cdd:COG0318 255 VVTVNPEDP-------------GERRPGSVGRPLPGVEVRI-VDEDGRELppgevGEIVVRGPNVMKGYWN------DPE 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 405 TSESRSNEAWLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGVIDTRLGEMVVACVRL 484
Cdd:COG0318 315 ATAEAFRDGWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVL 394
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22329863 485 qekwiwsdvenRKGSfQLSSETLKHHCRtQNLTGFKIPKRFVRWEkQFPLTTTGKVKRDEVRRQVLSH 552
Cdd:COG0318 395 -----------RPGA-ELDAEELRAFLR-ERLARYKVPRRVEFVD-ELPRTASGKIDRRALRERYAAG 448
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
173-541 |
4.61e-108 |
|
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: 326.93 E-value: 4.61e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 173 DAVVICFTSGTTGRPKGVTISHLAFITQSLAKIAIAGYGEDDVYLHTSPLVHIGGLSSAMAMLMVGACHVLLPKFDAKTA 252
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKFDPEAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 253 LQVMEQNHITCFITVPAMMADLIRVNRttKNGAENRGVRKILNGGGSLSSELLKEAVNIFPCaRILSAYGMTEACSSLTF 332
Cdd:cd04433 81 LELIEREKVTILLGVPTLLARLLKAPE--SAGYDLSSLRALVSGGAPLPPELLERFEEAPGI-KLVNGYGLTETGGTVAT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 333 MTLHDPtqesfkvtypllnqPKQGTCVGKPAPHIELMVkLDED-----SSRVGKILTRGPHTMLRYWGhqvaqeNVETSE 407
Cdd:cd04433 158 GPPDDD--------------ARKPGSVGRPVPGVEVRI-VDPDggelpPGEIGELVVRGPSVMKGYWN------NPEATA 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 408 SRSNEAWLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGVIDTRLGEMVVACVRLqek 487
Cdd:cd04433 217 AVDEDGWYRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVL--- 293
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 22329863 488 wiwsdvenrKGSFQLSSETLKHHCRtQNLTGFKIPkRFVRWEKQFPLTTTGKVK 541
Cdd:cd04433 294 ---------RPGADLDAEELRAHVR-ERLAPYKVP-RRVVFVDALPRTASGKID 336
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
11-549 |
3.82e-98 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 307.50 E-value: 3.82e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 11 QCLTRLASVKRNAVVTVYGNRKRTGREFVDGVLSLAAGLIRLGLRNGDVVSIAAFNSDLFLEWLLAVALVGGVVAPLNYR 90
Cdd:PRK06187 10 RILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPINIR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 91 -------WSLKEAKMAMLLVEPVLLVTdetcvswcIDVQNGDIPSLKWRVLMESTSTDFANELNQFLTtEMLKQRTlvps 163
Cdd:PRK06187 90 lkpeeiaYILNDAEDRVVLVDSEFVPL--------LAAILPQLPTVRTVIVEGDGPAAPLAPEVGEYE-ELLAAAS---- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 164 lATYAW---ASDDAVVICFTSGTTGRPKGVTISHLAFITQSLAKIAIAGYGEDDVYLHTSPLVHIGGLSSAMAMLMVGAC 240
Cdd:PRK06187 157 -DTFDFpdiDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVPMFHVHAWGLPYLALMAGAK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 241 HVLLPKFDAKTALQVMEQNHITCFITVPAMMADLIRVNRTtkNGAENRGVRKILNGGGSLSSELLKEAVNIFPCaRILSA 320
Cdd:PRK06187 236 QVIPRRFDPENLLDLIETERVTFFFAVPTIWQMLLKAPRA--YFVDFSSLRLVIYGGAALPPALLREFKEKFGI-DLVQG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 321 YGMTEACSSLTFMTLHDptQESFKVTYPLLnqpkqgtcVGKPAPHIEL-MVKLDE-----DSSRVGKILTRGPHTMLRYW 394
Cdd:PRK06187 313 YGMTETSPVVSVLPPED--QLPGQWTKRRS--------AGRPLPGVEArIVDDDGdelppDGGEVGEIIVRGPWLMQGYW 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 395 GHQvaqenvETSESRSNEAWLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGVIDTRL 474
Cdd:PRK06187 383 NRP------EATAETIDGGWLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKW 456
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22329863 475 GEMVVACVRLqekwiwsdvenRKGSfQLSSETLKHHCRTqNLTGFKIPKR--FVrweKQFPLTTTGKVKRDEVRRQV 549
Cdd:PRK06187 457 GERPVAVVVL-----------KPGA-TLDAKELRAFLRG-RLAKFKLPKRiaFV---DELPRTSVGKILKRVLREQY 517
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
13-540 |
5.25e-95 |
|
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: 296.83 E-value: 5.25e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 13 LTRLASVKRNAVVTVYGNRKRTGREFVDGVLSLAAGLIRLGLRNGDVVSIAAFNSDLFLEWLLAVALVGGVVAPLNYRWS 92
Cdd:cd17631 1 LRRRARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 93 LKEakMAMLLvepvllvtdETCVSwcidvqngdipslkwRVLMeststdfanelnqflttemlkqrtlvpslatyawasD 172
Cdd:cd17631 81 PPE--VAYIL---------ADSGA---------------KVLF------------------------------------D 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 173 DAVVICFTSGTTGRPKGVTISHLAFITQSLAKIAIAGYGEDDVYLHTSPLVHIGGLS-SAMAMLMVGACHVLLPKFDAKT 251
Cdd:cd17631 99 DLALLMYTSGTTGRPKGAMLTHRNLLWNAVNALAALDLGPDDVLLVVAPLFHIGGLGvFTLPTLLRGGTVVILRKFDPET 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 252 ALQVMEQNHITCFITVPAMMADLIRVNRTTKngAENRGVRKILnGGGSLSSELLKEAVNIFPCaRILSAYGMTEACSSLT 331
Cdd:cd17631 179 VLDLIERHRVTSFFLVPTMIQALLQHPRFAT--TDLSSLRAVI-YGGAPMPERLLRALQARGV-KFVQGYGMTETSPGVT 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 332 FMTlHDPTQEsfkvtypllnqpKQGTCvGKPAPHIELMVkLDEDSSRV-----GKILTRGPHTMLRYWGHQVAqenveTS 406
Cdd:cd17631 255 FLS-PEDHRR------------KLGSA-GRPVFFVEVRI-VDPDGREVppgevGEIVVRGPHVMAGYWNRPEA-----TA 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 407 ESRSNeAWLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGVIDTRLGEMVVACVRLQE 486
Cdd:cd17631 315 AAFRD-GWFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRP 393
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 22329863 487 kwiwsdvenrkGSfQLSSETLKHHCRTqNLTGFKIPKRFVRWEkQFPLTTTGKV 540
Cdd:cd17631 394 -----------GA-ELDEDELIAHCRE-RLARYKIPKSVEFVD-ALPRNATGKI 433
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
8-548 |
1.40e-87 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 279.87 E-value: 1.40e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 8 HICQCLTRLASVKRNAVVTVYGNRKRTGREFVDGVLSLAAGLIRLGLRNGDVVSIAAFNSDLFLEWLLAVALVGGVVAPL 87
Cdd:PRK07656 6 TLPELLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 88 NYRWSLKEA-------KMAMLLVEPVLLVTDEtcvswcidVQNGDIPSLKWRVLMESTSTDFANELN----QFLTTEMLK 156
Cdd:PRK07656 86 NTRYTADEAayilargDAKALFVLGLFLGVDY--------SATTRLPALEHVVICETEEDDPHTEKMktftDFLAAGDPA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 157 QRtlVPSLAtyawaSDDAVVICFTSGTTGRPKGVTISHLAFITQSLAKIAIAGYGEDDVYLHTSPLVHIGGLSSAM-AML 235
Cdd:PRK07656 158 ER--APEVD-----PDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLAANPFFHVFGYKAGVnAPL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 236 MVGACHVLLPKFDAKTALQVMEQNHITCFITVPAMMADLIRVNRttKNGAENRGVRKILNGGGSLSSELLKEAVNIFPCA 315
Cdd:PRK07656 231 MRGATILPLPVFDPDEVFRLIETERITVLPGPPTMYNSLLQHPD--RSAEDLSSLRLAVTGAASMPVALLERFESELGVD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 316 RILSAYGMTEACSSLTFMTLHDPtqesfKVTYPllnqpkqGTCvGKPAPHIELMVkLDEDSSR-----VGKILTRGPHTM 390
Cdd:PRK07656 309 IVLTGYGLSEASGVTTFNRLDDD-----RKTVA-------GTI-GTAIAGVENKI-VNELGEEvpvgeVGELLVRGPNVM 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 391 LRYWghqvaQENVETSESRSNEAWLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGVI 470
Cdd:PRK07656 375 KGYY-----DDPEATAAAIDADGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVP 449
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22329863 471 DTRLGEMVVACVrlqekwiwsdVenRKGSFQLSSETLKHHCRTQnLTGFKIPkRFVRWEKQFPLTTTGKVKRDEVRRQ 548
Cdd:PRK07656 450 DERLGEVGKAYV----------V--LKPGAELTEEELIAYCREH-LAKYKVP-RSIEFLDELPKNATGKVLKRALREK 513
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
24-442 |
5.89e-86 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 272.65 E-value: 5.89e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 24 VVTVYGNRKRTGREFVDGVLSLAAGLIRLGLRNGDVVSIAAFNSDLFLEWLLAVALVGGVVAPLNYRWSLKEAKMAMLLV 103
Cdd:pfam00501 13 ALEVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 104 EPVLLVTDETCVSWCIDVQNGDIPSLKWRVLMESTSTDFANELNQFLTTEMLKQRTLVPslatyaWASDDAVVICFTSGT 183
Cdd:pfam00501 93 GAKVLITDDALKLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVPPPPPPP------PDPDDLAYIIYTSGT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 184 TGRPKGVTISHLAFI----TQSLAKIAIAGYGEDDVYLHTSPLVHIGGLSSAM-AMLMVGACHVLLPKF---DAKTALQV 255
Cdd:pfam00501 167 TGKPKGVMLTHRNLVanvlSIKRVRPRGFGLGPDDRVLSTLPLFHDFGLSLGLlGPLLAGATVVLPPGFpalDPAALLEL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 256 MEQNHITCFITVPAMMADLIRVNRttKNGAENRGVRKILNGGGSLSSELLKEAVNIFPCArILSAYGMTEACSSLTFMTL 335
Cdd:pfam00501 247 IERYKVTVLYGVPTLLNMLLEAGA--PKRALLSSLRLVLSGGAPLPPELARRFRELFGGA-LVNGYGLTETTGVVTTPLP 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 336 HDPTQESFKvtypllnqpkqgtCVGKPAPHIELMVkLDEDSSR------VGKILTRGPHTMLRYWGHQVAqenveTSESR 409
Cdd:pfam00501 324 LDEDLRSLG-------------SVGRPLPGTEVKI-VDDETGEpvppgePGELCVRGPGVMKGYLNDPEL-----TAEAF 384
|
410 420 430
....*....|....*....|....*....|...
gi 22329863 410 SNEAWLDTGDIGAFDEFGNLWLIGRSNGRIKTG 442
Cdd:pfam00501 385 DEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
13-546 |
9.35e-81 |
|
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: 260.57 E-value: 9.35e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 13 LTRLASVKRNAVVTVYGNRKRTGREFVDGVLSLAAGLIRLGLRNGDVVSIAAFNSDLFLEWLLAVALVGGVVAPLNyrWS 92
Cdd:cd05936 5 LEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLN--PL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 93 LKEAKMAMLL--VEPVLLVTDETcvswcidvqngdipslkwrvlmeststdFANELNQFLTTEMLKQRTLvpslatyawa 170
Cdd:cd05936 83 YTPRELEHILndSGAKALIVAVS----------------------------FTDLLAAGAPLGERVALTP---------- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 171 sDDAVVICFTSGTTGRPKGVTISHLAFITQSLAKIAIAG--YGEDDVYLHTSPLVHIGGLSSAM-AMLMVGACHVLLPKF 247
Cdd:cd05936 125 -EDVAVLQYTSGTTGVPKGAMLTHRNLVANALQIKAWLEdlLEGDDVVLAALPLFHVFGLTVALlLPLALGATIVLIPRF 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 248 DAKTALQVMEQNHITCFITVPAMMADLirVNRTTKNGAENRGVRKILNGGGSLSSELLKEAVNIFPCaRILSAYGMTEAC 327
Cdd:cd05936 204 RPIGVLKEIRKHRVTIFPGVPTMYIAL--LNAPEFKKRDFSSLRLCISGGAPLPVEVAERFEELTGV-PIVEGYGLTETS 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 328 SSLTFMTLHDPtqesfkvtypllnqPKQGTcVGKPAPHIELMVkLDEDSS-----RVGKILTRGPHTMLRYWGHQVAQEN 402
Cdd:cd05936 281 PVVAVNPLDGP--------------RKPGS-IGIPLPGTEVKI-VDDDGEelppgEVGELWVRGPQVMKGYWNRPEETAE 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 403 VETSEsrsneaWLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGVIDTRLGEMVVACV 482
Cdd:cd05936 345 AFVDG------WLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFV 418
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22329863 483 RLqekwiwsdvenRKGSfQLSSETLKHHCRTQnLTGFKIPKR--FVrweKQFPLTTTGKVKRDEVR 546
Cdd:cd05936 419 VL-----------KEGA-SLTEEEIIAFCREQ-LAGYKVPRQveFR---DELPKSAVGKILRRELR 468
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
34-540 |
1.31e-79 |
|
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: 258.30 E-value: 1.31e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 34 TGREFVDGVLSLAAGLIRLGLRNGDVVSIAAFNSDLFLEWLLAVALVGGVVAPLNYRWSLKEAKMAMLLVEPVLLVTDET 113
Cdd:cd05911 12 TYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTDPD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 114 CVSWCIDVQNGDIPslKWRVLMESTSTDFANELNQFLTTEMLKQ-RTLVPSLATyawASDDAVVICFTSGTTGRPKGVTI 192
Cdd:cd05911 92 GLEKVKEAAKELGP--KDKIIVLDDKPDGVLSIEDLLSPTLGEEdEDLPPPLKD---GKDDTAAILYSSGTTGLPKGVCL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 193 SHLAFITQSLAKIAIAG--YGEDDVYLHTSPLVHIGGLSSAMAMLMVGACHVLLPKFDAKTALQVMEQNHITCFITVPAM 270
Cdd:cd05911 167 SHRNLIANLSQVQTFLYgnDGSNDVILGFLPLYHIYGLFTTLASLLNGATVIIMPKFDSELFLDLIEKYKITFLYLVPPI 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 271 MADLIRVNRTTKNGAENrgVRKILNGGGSLSSELLKEAVNIFPCARILSAYGMTEACSSLTFMTLHDPTQESfkvtypll 350
Cdd:cd05911 247 AAALAKSPLLDKYDLSS--LRVILSGGAPLSKELQELLAKRFPNATIKQGYGMTETGGILTVNPDGDDKPGS-------- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 351 nqpkqgtcVGKPAPHIELMVkLDEDSSR------VGKILTRGPHTMLRYWGHQVAqenveTSESRSNEAWLDTGDIGAFD 424
Cdd:cd05911 317 --------VGRLLPNVEAKI-VDDDGKDslgpnePGEICVRGPQVMKGYYNNPEA-----TKETFDEDGWLHTGDIGYFD 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 425 EFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGVIDTRLGEMVVACVRlqekwiwsdvenRKGSFQLSS 504
Cdd:cd05911 383 EDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVV------------RKPGEKLTE 450
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 22329863 505 ETLKHHCRtQNLTGFK-----IpkRFVrweKQFPLTTTGKV 540
Cdd:cd05911 451 KEVKDYVA-KKVASYKqlrggV--VFV---DEIPKSASGKI 485
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
172-546 |
4.40e-70 |
|
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: 229.09 E-value: 4.40e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 172 DDAVVICFTSGTTGRPKGVTISHLAFITQSlAKIAIA-GYGEDDVYLHTSPLVHIGGLS-SAMAMLMVGACHVLL-PKFD 248
Cdd:cd05917 2 DDVINIQFTSGTTGSPKGATLTHHNIVNNG-YFIGERlGLTEQDRLCIPVPLFHCFGSVlGVLACLTHGATMVFPsPSFD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 249 AKTALQVMEQNHITCFITVPAMMADLIRVNRTTKNGAENrgVRKILNGGGSLSSELLKEAVNIFPCARILSAYGMTEAcS 328
Cdd:cd05917 81 PLAVLEAIEKEKCTALHGVPTMFIAELEHPDFDKFDLSS--LRTGIMAGAPCPPELMKRVIEVMNMKDVTIAYGMTET-S 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 329 SLTFMTLHDPTQESFKVTypllnqpkqgtcVGKPAPHIELMVkLDEDSSRV------GKILTRGPHTMLRYWghqvaQEN 402
Cdd:cd05917 158 PVSTQTRTDDSIEKRVNT------------VGRIMPHTEAKI-VDPEGGIVppvgvpGELCIRGYSVMKGYW-----NDP 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 403 VETSESRSNEAWLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGVIDTRLGEMVVACV 482
Cdd:cd05917 220 EKTAEAIDGDGWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWI 299
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22329863 483 RLQEkwiwsdvenrkgSFQLSSETLKHHCRtQNLTGFKIPkRFVRWEKQFPLTTTGKVKRDEVR 546
Cdd:cd05917 300 RLKE------------GAELTEEDIKAYCK-GKIAHYKVP-RYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
34-542 |
4.74e-70 |
|
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: 233.36 E-value: 4.74e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 34 TGREFVDGVLSLAAGLIRLGLRNGDVVSIAAFNSDLFLEWLLAVALVGGVVAPLN-------YRWSLKEAKMAMLLVEPV 106
Cdd:cd05926 16 TYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNpaykkaeFEFYLADLGSKLVLTPKG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 107 LLVTD-ETCVSWCIDVQNgdipsLKWRVLMESTSTDfANELNQFLTTEMLKQRTLVPSlatyawaSDDAVVICFTSGTTG 185
Cdd:cd05926 96 ELGPAsRAASKLGLAILE-----LALDVGVLIRAPS-AESLSNLLADKKNAKSEGVPL-------PDDLALILHTSGTTG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 186 RPKGVTISHLAFITQslAKIAIAGY--GEDDVYLHTSPLVHIGGL-SSAMAMLMVGACHVLLPKFDAKTALQVMEQNHIT 262
Cdd:cd05926 163 RPKGVPLTHRNLAAS--ATNITNTYklTPDDRTLVVMPLFHVHGLvASLLSTLAAGGSVVLPPRFSASTFWPDVRDYNAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 263 CFITVPAMMADLIRvNRTTKNGAENRGVRKILNGGGSLSSELLKEAVNIFPcARILSAYGMTEACSSLTfmtlhdptqes 342
Cdd:cd05926 241 WYTAVPTIHQILLN-RPEPNPESPPPKLRFIRSCSASLPPAVLEALEATFG-APVLEAYGMTEAAHQMT----------- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 343 fkvTYPL-LNQPKQGTcVGKPApHIELMVkLDEDSS-----RVGKILTRGPHTMLRYwghqvaQENVE-TSESRSNEAWL 415
Cdd:cd05926 308 ---SNPLpPGPRKPGS-VGKPV-GVEVRI-LDEDGEilppgVVGEICLRGPNVTRGY------LNNPEaNAEAAFKDGWF 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 416 DTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGVIDTRLGEMVVACVRLQEKwiwsdven 495
Cdd:cd05926 376 RTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREG-------- 447
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 22329863 496 rkgsFQLSSETLKHHCRtQNLTGFKIPKRfVRWEKQFPLTTTGKVKR 542
Cdd:cd05926 448 ----ASVTEEELRAFCR-KHLAAFKVPKK-VYFVDELPKTATGKIQR 488
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
20-547 |
1.63e-68 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 229.08 E-value: 1.63e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 20 KRNAVVtvYGNRKRTGREFVDGVLSLAAGLIRLGLRNGDVVSIAAFNSDLFLEWLLAVALVGGVVAPLNYRWSLKEAKMA 99
Cdd:PRK03640 17 DRTAIE--FEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 100 MLLVEPVLLVTDEtcvswcidvqngdipslkwrvlmeststDFANELN---QFLTTEMLKQRTLVPSLATYaWASDDAVV 176
Cdd:PRK03640 95 LDDAEVKCLITDD----------------------------DFEAKLIpgiSVKFAELMNGPKEEAEIQEE-FDLDEVAT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 177 ICFTSGTTGRPKGVTIS---HLAFITQSLAKIaiaGYGEDDVYLHTSPLVHIGGLSSAMAMLMVGACHVLLPKFDAKTAL 253
Cdd:PRK03640 146 IMYTSGTTGKPKGVIQTygnHWWSAVGSALNL---GLTEDDCWLAAVPIFHISGLSILMRSVIYGMRVVLVEKFDAEKIN 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 254 QVMEQNHITCFITVPAMMADLIRVnrtTKNGAENRGVRKILNGGGSLSSELLKEAV--NIfPcarILSAYGMTEACSSLt 331
Cdd:PRK03640 223 KLLQTGGVTIISVVSTMLQRLLER---LGEGTYPSSFRCMLLGGGPAPKPLLEQCKekGI-P---VYQSYGMTETASQI- 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 332 fMTLhDPTqesFKVTypllnqpKQGTcVGKPAPHIELMVKLDED---SSRVGKILTRGPHTMLRYWgHQvAQENVETSES 408
Cdd:PRK03640 295 -VTL-SPE---DALT-------KLGS-AGKPLFPCELKIEKDGVvvpPFEEGEIVVKGPNVTKGYL-NR-EDATRETFQD 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 409 rsneAWLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGVIDTRLGEMVVACVRLQEKw 488
Cdd:PRK03640 360 ----GWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVKSGE- 434
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 22329863 489 iwsdvenrkgsfqLSSETLKHHCRTqNLTGFKIPKRFVRWEKqFPLTTTGKVKRDEVRR 547
Cdd:PRK03640 435 -------------VTEEELRHFCEE-KLAKYKVPKRFYFVEE-LPRNASGKLLRHELKQ 478
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
173-547 |
2.98e-68 |
|
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: 227.17 E-value: 2.98e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 173 DAVVICFTSGTTGRPKGVTISHLAFITQSLAKIAIAGYGEDDVYLHTSPLVHIGGLSSAMAM-LMVGACHVLLPKFDAKT 251
Cdd:cd05941 90 DPALILYTSGTTGRPKGVVLTHANLAANVRALVDAWRWTEDDVLLHVLPLHHVHGLVNALLCpLFAGASVEFLPKFDPKE 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 252 ALQVMEQNHITCFITVPAMMADLIRVNRTTKNGAEN------RGVRKILNGGGSLSSELLKEAVNIFPcARILSAYGMTE 325
Cdd:cd05941 170 VAISRLMPSITVFMGVPTIYTRLLQYYEAHFTDPQFaraaaaERLRLMVSGSAALPVPTLEEWEAITG-HTLLERYGMTE 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 326 acsslTFMTLhdptqesfkvTYPLLNQPKQGTcVGKPAPHIELMVKLDE-----DSSRVGKILTRGPHTMLRYWghqvaQ 400
Cdd:cd05941 249 -----IGMAL----------SNPLDGERRPGT-VGMPLPGVQARIVDEEtgeplPRGEVGEIQVRGPSVFKEYW-----N 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 401 ENVETSESRSNEAWLDTGDIGAFDEFGNLWLIGRSNGR-IKTGGENVYPEEVEAVLVEHPGIVSAVVIGVIDTRLGEMVV 479
Cdd:cd05941 308 KPEATKEEFTDDGWFKTGDLGVVDEDGYYWILGRSSVDiIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVV 387
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22329863 480 ACVRLqekwiwsdvenRKGSFQLSSETLKHHCRtQNLTGFKIPKRFVRWEKqFPLTTTGKVKRDEVRR 547
Cdd:cd05941 388 AVVVL-----------RAGAAALSLEELKEWAK-QRLAPYKRPRRLILVDE-LPRNAMGKVNKKELRK 442
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
21-546 |
7.64e-66 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 223.88 E-value: 7.64e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 21 RNAVVTVYGNRKRTGREFVDGVLSLAAGLIRLGLRNGDVVSIAAFNSdlfLEWLL---AVALVGGVVAPLN--YR----- 90
Cdd:PRK12583 34 REALVVRHQALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNC---AEWLLtqfATARIGAILVNINpaYRasele 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 91 WSLKEAKMAMLLVEPVLLVTD----------ETCVSWCIDVQNGDIPSLKWRVLMEststdfANELNQFLT-TEMLKQRT 159
Cdd:PRK12583 111 YALGQSGVRWVICADAFKTSDyhamlqellpGLAEGQPGALACERLPELRGVVSLA------PAPPPGFLAwHELQARGE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 160 LVPSLA----TYAWASDDAVVICFTSGTTGRPKGVTISH------LAFITQSLakiaiaGYGEDDVYLHTSPLVH-IGGL 228
Cdd:PRK12583 185 TVSREAlaerQASLDRDDPINIQYTSGTTGFPKGATLSHhnilnnGYFVAESL------GLTEHDRLCVPVPLYHcFGMV 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 229 SSAMAMLMVGAChVLLPK--FDAKTALQVMEQNHITCFITVPAM-MADLIRVNRTTKNGAEnrgVRKILNGGGSLSSELL 305
Cdd:PRK12583 259 LANLGCMTVGAC-LVYPNeaFDPLATLQAVEEERCTALYGVPTMfIAELDHPQRGNFDLSS---LRTGIMAGAPCPIEVM 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 306 KEAVNIFPCARILSAYGMTEAcSSLTFMTlhdptqesfKVTYPLlnqPKQGTCVGKPAPHIELMVkLDEDSSRV-----G 380
Cdd:PRK12583 335 RRVMDEMHMAEVQIAYGMTET-SPVSLQT---------TAADDL---ERRVETVGRTQPHLEVKV-VDPDGATVprgeiG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 381 KILTRGPHTMLRYWGHQVAqenveTSESRSNEAWLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPG 460
Cdd:PRK12583 401 ELCTRGYSVMKGYWNNPEA-----TAESIDEDGWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPA 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 461 IVSAVVIGVIDTRLGEMVVACVRLqekwiwsdvenRKGSfQLSSETLKHHCRTQnLTGFKIPkRFVRWEKQFPLTTTGKV 540
Cdd:PRK12583 476 VADVQVFGVPDEKYGEEIVAWVRL-----------HPGH-AASEEELREFCKAR-IAHFKVP-RYFRFVDEFPMTVTGKV 541
|
....*.
gi 22329863 541 KRDEVR 546
Cdd:PRK12583 542 QKFRMR 547
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
21-555 |
3.52e-65 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 221.99 E-value: 3.52e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 21 RNAVVTVYGNRKRTGREFVDGVLSLAAGLIRLGLRNGDVVSIAAFNSdlfLEWLL---AVALVGGVVAPLN--YRWS--- 92
Cdd:PRK08315 32 REALVYRDQGLRWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNV---PEWVLtqfATAKIGAILVTINpaYRLSele 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 93 --LKEAKMAMLL----------VEPVLLVTDETCVSWCIDVQNGDIPSLKWRVLMESTSTDFanelnqFLTTEMLKQRTL 160
Cdd:PRK08315 109 yaLNQSGCKALIaadgfkdsdyVAMLYELAPELATCEPGQLQSARLPELRRVIFLGDEKHPG------MLNFDELLALGR 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 161 VPSLATYAWAS-----DDAVVICFTSGTTGRPKGVTISHL------AFITQSLakiaiaGYGEDD-----VylhtsPLVH 224
Cdd:PRK08315 183 AVDDAELAARQatldpDDPINIQYTSGTTGFPKGATLTHRnilnngYFIGEAM------KLTEEDrlcipV-----PLYH 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 225 IGGLSSA-MAMLMVGACHVL-LPKFDAKTALQVMEQNHITCFITVPAM-----------MADLIRVnRTtkngaenrGVR 291
Cdd:PRK08315 252 CFGMVLGnLACVTHGATMVYpGEGFDPLATLAAVEEERCTALYGVPTMfiaeldhpdfaRFDLSSL-RT--------GIM 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 292 kilnGGGSLSSELLKEAVNIFPCARILSAYGMTEaCSSLTFMTL-HDPTQesfkvtypllnqpKQGTCVGKPAPHIElmV 370
Cdd:PRK08315 323 ----AGSPCPIEVMKRVIDKMHMSEVTIAYGMTE-TSPVSTQTRtDDPLE-------------KRVTTVGRALPHLE--V 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 371 KL-DEDSSRV------GKILTRGPHTMLRYWGHQVAqenveTSESRSNEAWLDTGDIGAFDEFGNLWLIGRSNGRIKTGG 443
Cdd:PRK08315 383 KIvDPETGETvprgeqGELCTRGYSVMKGYWNDPEK-----TAEAIDADGWMHTGDLAVMDEEGYVNIVGRIKDMIIRGG 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 444 ENVYPEEVEAVLVEHPGIVSAVVIGVIDTRLGEMVVACVRLqekwiwsdvenRKGSfQLSSETLKHHCRTQnLTGFKIPK 523
Cdd:PRK08315 458 ENIYPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIIL-----------RPGA-TLTEEDVRDFCRGK-IAHYKIPR 524
|
570 580 590
....*....|....*....|....*....|....
gi 22329863 524 --RFVrweKQFPLTTTGKVKRDEVRRQVLSHFQI 555
Cdd:PRK08315 525 yiRFV---DEFPMTVTGKIQKFKMREMMIEELGL 555
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
146-547 |
3.86e-62 |
|
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: 209.90 E-value: 3.86e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 146 LNQFLTT-EMLKQrtlvpsLATYAWASDDAVVICFTSGTTGRPKGVTIS---HLAFITQSLAKIaiaGYGEDDVYLHTSP 221
Cdd:cd05912 56 LNTRLTPnELAFQ------LKDSDVKLDDIATIMYTSGTTGKPKGVQQTfgnHWWSAIGSALNL---GLTEDDNWLCALP 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 222 LVHIGGLSSAMAMLMVGACHVLLPKFDAKTALQVMEQNHITCFITVPAMMADLIRVNrttkNGAENRGVRKILNGGGSLS 301
Cdd:cd05912 127 LFHISGLSILMRSVIYGMTVYLVDKFDAEQVLHLINSGKVTIISVVPTMLQRLLEIL----GEGYPNNLRCILLGGGPAP 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 302 SELLKEAV--NIfPcarILSAYGMTEACSSLtfmtlhdptqesfkVTYPLLNQPKQGTCVGKPAPHIEL-MVKLDEDSSR 378
Cdd:cd05912 203 KPLLEQCKekGI-P---VYQSYGMTETCSQI--------------VTLSPEDALNKIGSAGKPLFPVELkIEDDGQPPYE 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 379 VGKILTRGPHTMLRYWGhqvaqeNVETSESRSNEAWLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEH 458
Cdd:cd05912 265 VGEILLKGPNVTKGYLN------RPDATEESFENGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSH 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 459 PGIVSAVVIGVIDTRLGEMVVACVRLQEKwiwsdvenrkgsfqLSSETLKHHCRTqNLTGFKIPKRFVRWEKqFPLTTTG 538
Cdd:cd05912 339 PAIKEAGVVGIPDDKWGQVPVAFVVSERP--------------ISEEELIAYCSE-KLAKYKVPKKIYFVDE-LPRTASG 402
|
....*....
gi 22329863 539 KVKRDEVRR 547
Cdd:cd05912 403 KLLRHELKQ 411
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
42-545 |
6.02e-62 |
|
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 162605 [Multi-domain] Cd Length: 436 Bit Score: 210.38 E-value: 6.02e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 42 VLSLAAGLIRLGLRNGDVVSIAAFNSDLFLEWLLAVALVGGVVAPLNYRWSLKEAKMAMLLVEPVLLVTDEtcvswCIDV 121
Cdd:TIGR01923 9 AAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDS-----LLEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 122 QNGDIPSLkwrvlmESTSTDFANELNQFLTTEMlkqrtlvpslatyawasDDAVVICFTSGTTGRPKGVTIS---HLAFI 198
Cdd:TIGR01923 84 KDFQADSL------DRIEAAGRYETSLSASFNM-----------------DQIATLMFTSGTTGKPKAVPHTfrnHYASA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 199 TQSLAKIaiaGYGEDDVYLHTSPLVHIGGLSSAMAMLMVGACHVLLpkfDAKTALQVMEQNH-ITCFITVPAMMadlirv 277
Cdd:TIGR01923 141 VGSKENL---GFTEDDNWLLSLPLYHISGLSILFRWLIEGATLRIV---DKFNQLLEMIANErVTHISLVPTQL------ 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 278 NRTTKNGAENRGVRKILNGGGSLSSELLKEAVNI-FPcarILSAYGMTEACS-SLTFMTLHDPTQESfkvtypllnqpkq 355
Cdd:TIGR01923 209 NRLLDEGGHNENLRKILLGGSAIPAPLIEEAQQYgLP---IYLSYGMTETCSqVTTATPEMLHARPD------------- 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 356 gtcVGKPAPHIELMVKLDeDSSRVGKILTRGPHTMLRYWGhqvaqeNVETSESRSNEAWLDTGDIGAFDEFGNLWLIGRS 435
Cdd:TIGR01923 273 ---VGRPLAGREIKIKVD-NKEGHGEIMVKGANLMKGYLY------QGELTPAFEQQGWFNTGDIGELDGEGFLYVLGRR 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 436 NGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGVIDTRLGEMVVACVRLQEKWiwsdvenrkgsfqlSSETLKHHCrTQN 515
Cdd:TIGR01923 343 DDLIISGGENIYPEEIETVLYQHPGIQEAVVVPKPDAEWGQVPVAYIVSESDI--------------SQAKLIAYL-TEK 407
|
490 500 510
....*....|....*....|....*....|
gi 22329863 516 LTGFKIPKRFVRWEKQfPLTTTGKVKRDEV 545
Cdd:TIGR01923 408 LAKYKVPIAFEKLDEL-PYNASGKILRNQL 436
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
21-548 |
1.31e-60 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 209.02 E-value: 1.31e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 21 RNAVVtvYGNRKRTGREFVDGVLSLAAGLIRLGLRNGDVVSIAAFNSDLFLEWLLAVALVGGVVAPLNY-------RWSL 93
Cdd:PRK08316 27 KTALV--FGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFmltgeelAYIL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 94 KEAKMAMLLVEPVLLVTDETCVSWCIDVQngdipsLKWRVLMESTSTDfanelNQFLTTEMLKQRTLVPSLATYAwASDD 173
Cdd:PRK08316 105 DHSGARAFLVDPALAPTAEAALALLPVDT------LILSLVLGGREAP-----GGWLDFADWAEAGSVAEPDVEL-ADDD 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 174 AVVICFTSGTTGRPKGVTISHLAFITQSLAKIAIAGYGEDDVYLHTSPLVHIGGLSS-AMAMLMVGACHVLLPKFDAKTA 252
Cdd:PRK08316 173 LAQILYTSGTESLPKGAMLTHRALIAEYVSCIVAGDMSADDIPLHALPLYHCAQLDVfLGPYLYVGATNVILDAPDPELI 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 253 LQVMEQNHITCFITVPAMMADLIRvnRTTKNGAENRGVRKILNGGGSLSSELLKEAVNIFPCARILSAYGMTEACSSLTF 332
Cdd:PRK08316 253 LRTIEAERITSFFAPPTVWISLLR--HPDFDTRDLSSLRKGYYGASIMPVEVLKELRERLPGLRFYNCYGQTEIAPLATV 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 333 MTLHDptQESfkvtypllnqpKQGTCvGKPAPHIELMVkLDEDSSRV-----GKILTRGPHTMLRYWGhqvaqENVETSE 407
Cdd:PRK08316 331 LGPEE--HLR-----------RPGSA-GRPVLNVETRV-VDDDGNDVapgevGEIVHRSPQLMLGYWD-----DPEKTAE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 408 SRSNeAWLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGVIDTRLGEMVVACVRLqek 487
Cdd:PRK08316 391 AFRG-GWFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVP--- 466
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22329863 488 wiwsdvenrKGSFQLSSETLKHHCRtQNLTGFKIPKRfVRWEKQFPLTTTGKVKRDEVRRQ 548
Cdd:PRK08316 467 ---------KAGATVTEDELIAHCR-ARLAGFKVPKR-VIFVDELPRNPSGKILKRELRER 516
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
33-546 |
5.38e-60 |
|
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.
Pssm-ID: 341229 [Multi-domain] Cd Length: 437 Bit Score: 205.31 E-value: 5.38e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 33 RTGREFVDGVLSLAAGLIRLGLRNGDVVSIAAFNSDLFLEWLLAVALVGGVVAPLNYRWSLKEAKMAMLLVEP-VLLVTD 111
Cdd:cd05903 2 LTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAkVFVVPE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 112 EtcvswcidvqngdipslkWRvlmestSTDFANElnqflttemlkqrtlvpslatyawaSDDAVVICFTSGTTGRPKGVT 191
Cdd:cd05903 82 R------------------FR------QFDPAAM-------------------------PDAVALLLFTSGTTGEPKGVM 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 192 ISHLAFITQSLAKIAIAGYGEDDVYLHTSPLVHIGG-LSSAMAMLMVGACHVLLPKFDAKTALQVMEQNHITCFITVPAM 270
Cdd:cd05903 113 HSHNTLSASIRQYAERLGLGPGDVFLVASPMAHQTGfVYGFTLPLLLGAPVVLQDIWDPDKALALMREHGVTFMMGATPF 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 271 MADLIRVnrTTKNGAENRGVRKILNGGGSLSSELLKEAVNIFPcARILSAYGMTEACSSLTFMTLHDPTqesfkvtypll 350
Cdd:cd05903 193 LTDLLNA--VEEAGEPLSRLRTFVCGGATVPRSLARRAAELLG-AKVCSAYGSTECPGAVTSITPAPED----------- 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 351 nqpKQGTCVGKPAPHIElmVKLDEDSSR------VGKILTRGPHTMLRYWghqvaqENVETSESRSNEAWLDTGDIGAFD 424
Cdd:cd05903 259 ---RRLYTDGRPLPGVE--IKVVDDTGAtlapgvEGELLSRGPSVFLGYL------DRPDLTADAAPEGWFRTGDLARLD 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 425 EFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGVIDTRLGEMVVACVRLqekwiwsdvenrKGSFQLSS 504
Cdd:cd05903 328 EDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVT------------KSGALLTF 395
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 22329863 505 ETLKHHCRTQNLTGFKIPKRFVRWEKqFPLTTTGKVKRDEVR 546
Cdd:cd05903 396 DELVAYLDRQGVAKQYWPERLVHVDD-LPRTPSGKVQKFRLR 436
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
34-482 |
7.69e-60 |
|
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: 206.32 E-value: 7.69e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 34 TGR-----EFVDGVLSLAAGLIRLGLRNGDVVSIAAFNSDLFLEWLLAVALVGGVVAPLNYRWSLKEAKMAMLLVEPVLL 108
Cdd:cd05904 29 TGRaltyaELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 109 VTDETCVSwciDVQNGDIPSlkwrVLMESTSTDFA-NELNQFLTTEMLKQRTLVPSlatyawasDDAVVICFTSGTTGRP 187
Cdd:cd05904 109 FTTAELAE---KLASLALPV----VLLDSAEFDSLsFSDLLFEADEAEPPVVVIKQ--------DDVAALLYSSGTTGRS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 188 KGVTISHLAFIT---QSLAKIAIAGYGEDdVYLHTSPLVHIGGLSS-AMAMLMVGACHVLLPKFDAKTALQVMEQNHITC 263
Cdd:cd05904 174 KGVMLTHRNLIAmvaQFVAGEGSNSDSED-VFLCVLPMFHIYGLSSfALGLLRLGATVVVMPRFDLEELLAAIERYKVTH 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 264 FITVPAMMADLirvnrtTKNGAENRG----VRKILNGGGSLSSELLKEAVNIFPCARILSAYGMTEACSSLTFMtlhdPT 339
Cdd:cd05904 253 LPVVPPIVLAL------VKSPIVDKYdlssLRQIMSGAAPLGKELIEAFRAKFPNVDLGQGYGMTESTGVVAMC----FA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 340 QESFKVTYpllnqpkqGTCvGKPAPHIELMVkLDEDS------SRVGKILTRGPHTMLRYWGhqvaqeNVE-TSESRSNE 412
Cdd:cd05904 323 PEKDRAKY--------GSV-GRLVPNVEAKI-VDPETgeslppNQTGELWIRGPSIMKGYLN------NPEaTAATIDKE 386
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 413 AWLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGVIDTRLGEMVVACV 482
Cdd:cd05904 387 GWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFV 456
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
8-549 |
1.44e-59 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 205.40 E-value: 1.44e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 8 HICQCLTRLASVKRNAVVTVYGNRKRTGREFVDGVLSLAAGLIRLGLRNgDVVSIAAFNSDLFLEWLLAVALVGGVVAPL 87
Cdd:PRK07638 2 GITKEYKKHASLQPNKIAIKENDRVLTYKDWFESVCKVANWLNEKESKN-KTIAILLENRIEFLQLFAGAAMAGWTCVPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 88 NYRWSLKEAKMAMLLVEPVLLVTDETCVSWCIDVQNGDIPSLKWRVLMESTSTDFANELNqflttemlkqrtlvpslaty 167
Cdd:PRK07638 81 DIKWKQDELKERLAISNADMIVTERYKLNDLPDEEGRVIEIDEWKRMIEKYLPTYAPIEN-------------------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 168 awASDDAVVICFTSGTTGRPKGVTISHLAFITQSLAKIAIAGYGEDDVYLHTSPLVHIGGLSSAMAMLMVGACHVLLPKF 247
Cdd:PRK07638 141 --VQNAPFYMGFTSGSTGKPKAFLRAQQSWLHSFDCNVHDFHMKREDSVLIAGTLVHSLFLYGAISTLYVGQTVHLMRKF 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 248 DAKTALQVMEQNHITCFITVPAMMADLIRVNRTTKNgaenrgVRKILNGGGSLSSELLKEAVNIFPCARILSAYGMTEac 327
Cdd:PRK07638 219 IPNQVLDKLETENISVMYTVPTMLESLYKENRVIEN------KMKIISSGAKWEAEAKEKIKNIFPYAKLYEFYGASE-- 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 328 ssLTFMT-LHDPTQEsfkvtypllnqpKQGTCVGKPAPHIELMVKlDEDSSRV-----GKILTRGPHTMLRYWGHQVAQE 401
Cdd:PRK07638 291 --LSFVTaLVDEESE------------RRPNSVGRPFHNVQVRIC-NEAGEEVqkgeiGTVYVKSPQFFMGYIIGGVLAR 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 402 NVETSEsrsneaWLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGVIDTRLGEMVVAC 481
Cdd:PRK07638 356 ELNADG------WMTVRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAI 429
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22329863 482 VRLQEkwiwsdvenrkgsfqlSSETLKHHCRtQNLTGFKIPKRFVRWEkQFPLTTTGKVKRDEVRRQV 549
Cdd:PRK07638 430 IKGSA----------------TKQQLKSFCL-QRLSSFKIPKEWHFVD-EIPYTNSGKIARMEAKSWI 479
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
13-546 |
4.21e-59 |
|
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: 204.07 E-value: 4.21e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 13 LTRLASVKRNAVVTVYGNRKRTGREFVDGVLSLAAGLIRLGLRNGDVVSIAAFNSDLFLEWLLAVALVGGVVAPLNYRws 92
Cdd:cd12118 10 LERAAAVYPDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTR-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 93 LKEAKMAMLL--VEPVLLVTDEtcvswcidvqngdipSLKWRVLMESTSTDFANElnqflttemlkqrtlvpslatyaWA 170
Cdd:cd12118 88 LDAEEIAFILrhSEAKVLFVDR---------------EFEYEDLLAEGDPDFEWI-----------------------PP 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 171 SD--DAVVICFTSGTTGRPKGVTISHLAFITQSLAKIAIAGYGEDDVYLHTSPLVHIGGLSSAMAMLMVGACHVLLPKFD 248
Cdd:cd12118 130 ADewDPIALNYTSGTTGRPKGVVYHHRGAYLNALANILEWEMKQHPVYLWTLPMFHCNGWCFPWTVAAVGGTNVCLRKVD 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 249 AKTALQVMEQNHITCFITVPAMMADLIRVNRTTKNGAENRgVRkILNGGGSLSSELLKEAVNI-FpcaRILSAYGMTEAC 327
Cdd:cd12118 210 AKAIYDLIEKHKVTHFCGAPTVLNMLANAPPSDARPLPHR-VH-VMTAGAPPPAAVLAKMEELgF---DVTHVYGLTETY 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 328 SSLTFMTLHD-----PTQESFK------VTYPLLNqpkqGTCVGKPaphiELMVKLDEDSSRVGKILTRGPHTMLRYWGH 396
Cdd:cd12118 285 GPATVCAWKPewdelPTEERARlkarqgVRYVGLE----EVDVLDP----ETMKPVPRDGKTIGEIVFRGNIVMKGYLKN 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 397 QVAqenveTSESRSNeAWLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGVIDTRLGE 476
Cdd:cd12118 357 PEA-----TAEAFRG-GWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGE 430
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 477 MVVACVRLQEkwiwsdvenrkgSFQLSSETLKHHCRtQNLTGFKIPKRFVRWEkqFPLTTTGKVKRDEVR 546
Cdd:cd12118 431 VPCAFVELKE------------GAKVTEEEIIAFCR-EHLAGFMVPKTVVFGE--LPKTSTGKIQKFVLR 485
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
173-542 |
4.30e-59 |
|
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: 199.42 E-value: 4.30e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 173 DAVVICFTSGTTGRPKGVTISHLAFITQSLAKIAIAGYGEDDVYLHTSPLVHIGGLSSAMAMLMVGACHVLLPKFDAKTA 252
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPLFHIAGLNLALATFHAGGANVVMEKFDPAEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 253 LQVMEQNHITCFITVPAMMADLIrvNRTTKNGAENRGVRKILNGGGSLSSELLKEAVNifpcARILSAYGMTEACSSLTF 332
Cdd:cd17637 81 LELIEEEKVTLMGSFPPILSNLL--DAAEKSGVDLSSLRHVLGLDAPETIQRFEETTG----ATFWSLYGQTETSGLVTL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 333 MtlhdptqesfkvtyPLLNQPkqgTCVGKPAP--HIELMVKLDEDSSR--VGKILTRGPHTMLRYWghqvaqENVETSES 408
Cdd:cd17637 155 S--------------PYRERP---GSAGRPGPlvRVRIVDDNDRPVPAgeTGEIVVRGPLVFQGYW------NLPELTAY 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 409 RSNEAWLDTGDIGAFDEFGNLWLIGRSNGR--IKTGGENVYPEEVEAVLVEHPGIVSAVVIGVIDTRLGEMVVA-CVrlq 485
Cdd:cd17637 212 TFRNGWHHTGDLGRFDEDGYLWYAGRKPEKelIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAvCV--- 288
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 22329863 486 ekwiwsdvenRKGSFQLSSETLKHHCRTQnLTGFKIPkRFVRWEKQFPLTTTGKVKR 542
Cdd:cd17637 289 ----------LKPGATLTADELIEFVGSR-IARYKKP-RYVVFVEALPKTADGSIDR 333
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
45-546 |
6.80e-59 |
|
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: 201.75 E-value: 6.80e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 45 LAAGLIRLGLRNGDVVSIAAFNSDLFLEWLLAVALVGGVVAPLNYRwsLKEAKMAMLL--VEPVLLVTDETCvswcidvq 122
Cdd:cd05934 16 IAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTA--LRGDELAYIIdhSGAQLVVVDPAS-------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 123 ngdipslkwrvlmeststdfanelnqflttemlkqrtlvpslatyawasddavvICFTSGTTGRPKGVTISHLAFITQSL 202
Cdd:cd05934 86 ------------------------------------------------------ILYTSGTTGPPKGVVITHANLTFAGY 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 203 AKIAIAGYGEDDVYLHTSPLVHIGGLS-SAMAMLMVGACHVLLPKFDAKTALQVMEQNHITCFITVPAMMADLIRVNRTT 281
Cdd:cd05934 112 YSARRFGLGEDDVYLTVLPLFHINAQAvSVLAALSVGATLVLLPRFSASRFWSDVRRYGATVTNYLGAMLSYLLAQPPSP 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 282 KNgAENRgVRKIlnGGGSLSSELLKEAVNIFPCaRILSAYGMTEACssltFMTLHDPtqesfkvtypllNQPKQGTCVGK 361
Cdd:cd05934 192 DD-RAHR-LRAA--YGAPNPPELHEEFEERFGV-RLLEGYGMTETI----VGVIGPR------------DEPRRPGSIGR 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 362 PAPHIELMVKLDEDSS----RVGKILTR---GPHTMLRYWGHQVAqenveTSESRSNeAWLDTGDIGAFDEFGNLWLIGR 434
Cdd:cd05934 251 PAPGYEVRIVDDDGQElpagEPGELVIRglrGWGFFKGYYNMPEA-----TAEAMRN-GWFHTGDLGYRDADGFFYFVDR 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 435 SNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGVIDTRLGEMVVACVRLqekwiwsdvenRKGSfQLSSETLKHHCRtQ 514
Cdd:cd05934 325 KKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVL-----------RPGE-TLDPEELFAFCE-G 391
|
490 500 510
....*....|....*....|....*....|..
gi 22329863 515 NLTGFKIPkRFVRWEKQFPLTTTGKVKRDEVR 546
Cdd:cd05934 392 QLAYFKVP-RYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
21-542 |
3.05e-57 |
|
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: 199.27 E-value: 3.05e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 21 RNAVVTVYGNRKRTGREFVDGVLSLAAGLIRLGLRNGDVVSIAAFNSDLFLEWLLAVALVGGVVAPLNyrWSLKEAKMAM 100
Cdd:cd05923 17 ACAIADPARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALIN--PRLKAAELAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 101 LLVEpvllvtDETC-VSWCIDVQNGD-IPSLKWRVLMESTSTDfANELNQFltTEMLKQRTLVPSlatyawasDDAVVIc 178
Cdd:cd05923 95 LIER------GEMTaAVIAVDAQVMDaIFQSGVRVLALSDLVG-LGEPESA--GPLIEDPPREPE--------QPAFVF- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 179 FTSGTTGRPKGVTISHLAFITQSLAKIAIAG--YGEDDVYLHTSPLVHIGGLSSAMAM-LMVGACHVLLPKFDAKTALQV 255
Cdd:cd05923 157 YTSGTTGLPKGAVIPQRAAESRVLFMSTQAGlrHGRHNVVLGLMPLYHVIGFFAVLVAaLALDGTYVVVEEFDPADALKL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 256 MEQNHITCFITVPAMMADLirVNRTTKNGAENRGVRKILNGGGSLSSELLKEaVNIFPCARILSAYGMTEACSSLtFMtl 335
Cdd:cd05923 237 IEQERVTSLFATPTHLDAL--AAAAEFAGLKLSSLRHVTFAGATMPDAVLER-VNQHLPGEKVNIYGTTEAMNSL-YM-- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 336 HDPTQESfkVTYPLLNQPKQGTCVGKPAPHI-------ELMVKLDEDSsrvgkiltrgphTMLRYWGHQVAqenveTSES 408
Cdd:cd05923 311 RDARTGT--EMRPGFFSEVRIVRIGGSPDEAlangeegELIVAAAADA------------AFTGYLNQPEA-----TAKK 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 409 RSnEAWLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGVIDTRLGEMVVACVRLQEKw 488
Cdd:cd05923 372 LQ-DGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREG- 449
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 22329863 489 iwsdvenrkgsfQLSSETLKHHCRTQNLTGFKIPKRFVrWEKQFPLTTTGKVKR 542
Cdd:cd05923 450 ------------TLSADELDQFCRASELADFKRPRRYF-FLDELPKNAMNKVLR 490
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
177-542 |
5.75e-57 |
|
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain
Pssm-ID: 341288 [Multi-domain] Cd Length: 320 Bit Score: 193.39 E-value: 5.75e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 177 ICFTSGTTGRPKGVTISH---LAFITQSLAKIAIAGygeDDVYLHTSPLVHIGGLSSAMAMLMVGACHVLLPKFDAKTAL 253
Cdd:cd17633 5 IGFTSGTTGLPKAYYRSErswIESFVCNEDLFNISG---EDAILAPGPLSHSLFLYGAISALYLGGTFIGQRKFNPKSWI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 254 QVMEQNHITCFITVPAMMADLIRVNRTTKNgaenrgVRKILNGGGSLSSELLKEAVNIFPCARILSAYGMTEAcssltfm 333
Cdd:cd17633 82 RKINQYNATVIYLVPTMLQALARTLEPESK------IKSIFSSGQKLFESTKKKLKNIFPKANLIEFYGTSEL------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 334 tlhdptqeSFkVTYPLLNQPKQGTCVGKPAPHIELMVkLDEDSSRVGKILTRGPhtmLRYWGHQVAQENVETSesrsnea 413
Cdd:cd17633 149 --------SF-ITYNFNQESRPPNSVGRPFPNVEIEI-RNADGGEIGKIFVKSE---MVFSGYVRGGFSNPDG------- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 414 WLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGVIDTRLGEMVVACVrlqekwiwsdv 493
Cdd:cd17633 209 WMSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALY----------- 277
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 22329863 494 enrKGSfQLSSETLKHHCRtQNLTGFKIPKRFVRWEKqFPLTTTGKVKR 542
Cdd:cd17633 278 ---SGD-KLTYKQLKRFLK-QKLSRYEIPKKIIFVDS-LPYTSSGKIAR 320
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
6-549 |
6.04e-57 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 199.62 E-value: 6.04e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 6 RPHICQCLTRLASVKRNAVVTVYGNRKRTGREFVDGVLSLAAGLIRLGLRNGDVVSIAAFNSDLFLEWLLAVALVGGVVA 85
Cdd:PRK07786 16 RQNWVNQLARHALMQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 86 PLNYRWSLKEAKMAMLLVEPVLLVTDETCVSWCIDVQNgDIPSLKWRVLMESTSTDFANELNQFLTTEMlkqrtlvPSLA 165
Cdd:PRK07786 96 PVNFRLTPPEIAFLVSDCGAHVVVTEAALAPVATAVRD-IVPLLSTVVVAGGSSDDSVLGYEDLLAEAG-------PAHA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 166 TYAWASDDAVVICFTSGTTGRPKGVTISHLAFITQSLAKIAIAGYG-EDDVYLHTSPLVHIGGLSSAMAMLMVGACHVLL 244
Cdd:PRK07786 168 PVDIPNDSPALIMYTSGTTGRPKGAVLTHANLTGQAMTCLRTNGADiNSDVGFVGVPLFHIAGIGSMLPGLLLGAPTVIY 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 245 P--KFDAKTALQVMEQNHITCFITVPAMMADLIRVNRttkngAENRGVR-KILNGGGSLSSE-LLKEAVNIFPCARILSA 320
Cdd:PRK07786 248 PlgAFDPGQLLDVLEAEKVTGIFLVPAQWQAVCAEQQ-----ARPRDLAlRVLSWGAAPASDtLLRQMAATFPEAQILAA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 321 YGMTEAcSSLTFMTLHDPTQEsfkvtypllnqpKQGTcVGKPAPHIELMVkLDEDSS-----RVGKILTRGPHTMLRYWG 395
Cdd:PRK07786 323 FGQTEM-SPVTCMLLGEDAIR------------KLGS-VGKVIPTVAARV-VDENMNdvpvgEVGEIVYRAPTLMSGYWN 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 396 HQVAqenveTSESRSNeAWLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGVIDTRLG 475
Cdd:PRK07786 388 NPEA-----TAEAFAG-GWFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWG 461
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22329863 476 EMVVACVRLqekwiwsdvenRKGSFQLSSETLKHHCrTQNLTGFKIPKrFVRWEKQFPLTTTGKVKRDEVRRQV 549
Cdd:PRK07786 462 EVPVAVAAV-----------RNDDAALTLEDLAEFL-TDRLARYKHPK-ALEIVDALPRNPAGKVLKTELRERY 522
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
25-548 |
1.68e-56 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 197.39 E-value: 1.68e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 25 VTVYGNRKR-TGREFVDGVLSLAAGLI-RLGLRNGDVVSIAAFNSDLFLEWLLAVALVGGVVAPLNYR-------WSLKE 95
Cdd:PRK06839 19 IAIITEEEEmTYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRlteneliFQLKD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 96 AKMAMLLVEPVLLVTdetcvswcidvqngdIPSLKWRVLMESTS--TDFANELNQflttemlKQRTLVPSlatyawASDD 173
Cdd:PRK06839 99 SGTTVLFVEKTFQNM---------------ALSMQKVSYVQRVIsiTSLKEIEDR-------KIDNFVEK------NESA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 174 AVVICFTSGTTGRPKGVTISHLAFITQSLAKIAIAGYGEDDVYLHTSPLVHIGGLS-SAMAMLMVGACHVLLPKFDAKTA 252
Cdd:PRK06839 151 SFIICYTSGTTGKPKGAVLTQENMFWNALNNTFAIDLTMHDRSIVLLPLFHIGGIGlFAFPTLFAGGVIIVPRKFEPTKA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 253 LQVMEQNHITCFITVPAMMADLIRVNRTTKNGAENrgVRKILNGGGSLSSELLKEAVNI-FPCARilsAYGMTEAcSSLT 331
Cdd:PRK06839 231 LSMIEKHKVTVVMGVPTIHQALINCSKFETTNLQS--VRWFYNGGAPCPEELMREFIDRgFLFGQ---GFGMTET-SPTV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 332 FMTLHDPTQEsfkvtypllnqpKQGTcVGKPAPHIELMVkLDEDSSRV-----GKILTRGPHTMLRYWghqvaqENVETS 406
Cdd:PRK06839 305 FMLSEEDARR------------KVGS-IGKPVLFCDYEL-IDENKNKVevgevGELLIRGPNVMKEYW------NRPDAT 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 407 ESRSNEAWLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGVIDTRLGEMVVACVRLqe 486
Cdd:PRK06839 365 EETIQDGWLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVK-- 442
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22329863 487 kwiwsdvenrKGSFQLSSETLKHHCRtQNLTGFKIPKRFVrWEKQFPLTTTGKVKRDEVRRQ 548
Cdd:PRK06839 443 ----------KSSSVLIEKDVIEHCR-LFLAKYKIPKEIV-FLKELPKNATGKIQKAQLVNQ 492
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
4-546 |
3.15e-56 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 197.13 E-value: 3.15e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 4 HSRPHICQCLTRLASVKRNAVVTVYGNRKRTGREFVDGVLSLAAGLIRLGLRNGDVVSIAAFNSDLFLEWLLAVALVGGV 83
Cdd:PRK06188 9 HSGATYGHLLVSALKRYPDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 84 VAPL-------NYRWSLKEAKMAMLLVEPVLLVTD-----ETCvswcidvqngdiPSLKwRVLMESTSTDFANELNQFLT 151
Cdd:PRK06188 89 RTALhplgsldDHAYVLEDAGISTLIVDPAPFVERalallARV------------PSLK-HVLTLGPVPDGVDLLAAAAK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 152 TEmlkQRTLVPslatyAWASDDAVVICFTSGTTGRPKGVTISHLAFITQSLAKIAIAGYGEDDVYLHTSPLVHIGGLSsA 231
Cdd:PRK06188 156 FG---PAPLVA-----AALPPDIAGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLSHAGGAF-F 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 232 MAMLMVGACHVLLPKFDAKTALQVMEQNHITCFITVPAMMADLI---RVNRTTKNGAENrgvrkILNGGGSLSSELLKEA 308
Cdd:PRK06188 227 LPTLLRGGTVIVLAKFDPAEVLRAIEEQRITATFLVPTMIYALLdhpDLRTRDLSSLET-----VYYGASPMSPVRLAEA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 309 VNIFpcARILS-AYGMTEACSSLTFMTL--HDPTQesfkvtypllnqPKQGTCVGKPAPHIELMVkLDEDSSRV-----G 380
Cdd:PRK06188 302 IERF--GPIFAqYYGQTEAPMVITYLRKrdHDPDD------------PKRLTSCGRPTPGLRVAL-LDEDGREVaqgevG 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 381 KILTRGPHTMLRYWGhqvaqENVETSESRSNeAWLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPG 460
Cdd:PRK06188 367 EICVRGPLVMDGYWN-----RPEETAEAFRD-GWLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPA 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 461 IVSAVVIGVIDTRLGEMVVACVRLQEKW------IWSDVENRKGSFQlssetlkhhcrtqnltgfkIPKR--FVrweKQF 532
Cdd:PRK06188 441 VAQVAVIGVPDEKWGEAVTAVVVLRPGAavdaaeLQAHVKERKGSVH-------------------APKQvdFV---DSL 498
|
570
....*....|....
gi 22329863 533 PLTTTGKVKRDEVR 546
Cdd:PRK06188 499 PLTALGKPDKKALR 512
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
27-544 |
3.87e-56 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 196.26 E-value: 3.87e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 27 VYGNRKRTGREFVDGVLSLAAGLIRLGLRNGDVVSIAAFNSDLFLEWLLAVALVGGVVAPLNYRWSLKEAKMAMLLVEPV 106
Cdd:PRK06145 22 VYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYILGDAGAK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 107 LLVTDETcvswcIDVQNGDIPSLKwrVLMESTSTDfanelnqfltTEMLKQRTLvPSLATYAWASDDAVVICFTSGTTGR 186
Cdd:PRK06145 102 LLLVDEE-----FDAIVALETPKI--VIDAAAQAD----------SRRLAQGGL-EIPPQAAVAPTDLVRLMYTSGTTDR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 187 PKGVTISHLAFITQSLAKIAIAGYGEDDVYLHTSPLVHIGGLS-SAMAMLMVGACHVLLPKFDAKTALQVMEQNHITCFI 265
Cdd:PRK06145 164 PKGVMHSYGNLHWKSIDHVIALGLTASERLLVVGPLYHVGAFDlPGIAVLWVGGTLRIHREFDPEAVLAAIERHRLTCAW 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 266 TVPAMMADLIRVnrTTKNGAENRGVRKILNGGGSLSSELLKEAVNIFPCARILSAYGMTEACSSLTFMtlhDPTQESFKV 345
Cdd:PRK06145 244 MAPVMLSRVLTV--PDRDRFDLDSLAWCIGGGEKTPESRIRDFTRVFTRARYIDAYGLTETCSGDTLM---EAGREIEKI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 346 typllnqpkqGTcVGKPAPHIELMVKLDED----SSRVGKILTRGPHTMLRYWghqvaQENVETSESRSNEaWLDTGDIG 421
Cdd:PRK06145 319 ----------GS-TGRALAHVEIRIADGAGrwlpPNMKGEICMRGPKVTKGYW-----KDPEKTAEAFYGD-WFRSGDVG 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 422 AFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGVIDTRLGEMVVACVRLQEkwiwsdvenrkgSFQ 501
Cdd:PRK06145 382 YLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNP------------GAT 449
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 22329863 502 LSSETLKHHCRtQNLTGFKIPKRFVrWEKQFPLTTTGK----VKRDE 544
Cdd:PRK06145 450 LTLEALDRHCR-QRLASFKVPRQLK-VRDELPRNPSGKvlkrVLRDE 494
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
31-543 |
7.66e-56 |
|
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: 195.93 E-value: 7.66e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 31 RKRTGREFVDGVLSLAAGLIRLGLRNGDVVSIAAFNSDLFLEWLLAVALVGGVVAPLNYR-------WSLKEAKMAMLLV 103
Cdd:cd12119 24 HRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRlfpeqiaYIINHAEDRVVFV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 104 EPVLLVTdetcvswcIDVQNGDIPSLKWRVLMESTSTDFANELNQFLTTEMLkqrtLVPSLATYAWAS---DDAVVICFT 180
Cdd:cd12119 104 DRDFLPL--------LEAIAPRLPTVEHVVVMTDDAAMPEPAGVGVLAYEEL----LAAESPEYDWPDfdeNTAAAICYT 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 181 SGTTGRPKGVTISHLAFITQSLA---KIAIaGYGEDDVYLHTSPLVHIGGLSSAMAMLMVGACHVLL-PKFDAKTALQVM 256
Cdd:cd12119 172 SGTTGNPKGVVYSHRSLVLHAMAallTDGL-GLSESDVVLPVVPMFHVNAWGLPYAAAMVGAKLVLPgPYLDPASLAELI 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 257 EQNHITCFITVPAMMADLIrvNRTTKNGAENRGVRKILNGGG----SLSSELLKEAVnifpcaRILSAYGMTEACSSLTF 332
Cdd:cd12119 251 EREGVTFAAGVPTVWQGLL--DHLEANGRDLSSLRRVVIGGSavprSLIEAFEERGV------RVIHAWGMTETSPLGTV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 333 MTL---HDPTQESFKVTYpllnQPKQGtcvgKPAPHIEL------MVKLDEDSSRVGKILTRGPHTMLRYWGhqvaqeNV 403
Cdd:cd12119 323 ARPpseHSNLSEDEQLAL----RAKQG----RPVPGVELrivdddGRELPWDGKAVGELQVRGPWVTKSYYK------ND 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 404 ETSESRSNEAWLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGVIDTRLGEMVVACVR 483
Cdd:cd12119 389 EESEALTEDGWLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVV 468
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22329863 484 LqekwiwsdvenRKGSfQLSSETLKHHCRTQnLTGFKIPKRFVRWEkQFPLTTTGKV-KRD 543
Cdd:cd12119 469 L-----------KEGA-TVTAEELLEFLADK-VAKWWLPDDVVFVD-EIPKTSTGKIdKKA 515
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
36-468 |
1.44e-54 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 194.55 E-value: 1.44e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 36 REFVDGVLSLAAGLIRLGLRNGDVVSIAAFNSdlfLEWL---LAVALVGGVVAPL-------NYRWSLKEAKMAMLLVEp 105
Cdd:COG1022 44 AEFAERVRALAAGLLALGVKPGDRVAILSDNR---PEWViadLAILAAGAVTVPIyptssaeEVAYILNDSGAKVLFVE- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 106 vllvtDETCVSWCIDVQnGDIPSLKWRVLME---STSTDFANELNQFLTT-EMLKQRTLVPSLATyAWASDDAVVICFTS 181
Cdd:COG1022 120 -----DQEQLDKLLEVR-DELPSLRHIVVLDprgLRDDPRLLSLDELLALgREVADPAELEARRA-AVKPDDLATIIYTS 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 182 GTTGRPKGVTISHLAFITQSLAKIAIAGYGEDDVYLhtS--PLVHIGGLSSAMAMLMVGACHVLLPkfDAKTALQVMEQN 259
Cdd:COG1022 193 GTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTL--SflPLAHVFERTVSYYALAAGATVAFAE--SPDTLAEDLREV 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 260 HITCFITVP-----------AMMADL---------------IRVNRTTKNGAENRGV-------------RKILN----- 295
Cdd:COG1022 269 KPTFMLAVPrvwekvyagiqAKAEEAgglkrklfrwalavgRRYARARLAGKSPSLLlrlkhaladklvfSKLREalggr 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 296 ------GGGSLSSELLK--EAVNIfpcaRILSAYGMTEACSSLTFMTLHDPtqesfkvtypllnqpKQGTcVGKPAPHIE 367
Cdd:COG1022 349 lrfavsGGAALGPELARffRALGI----PVLEGYGLTETSPVITVNRPGDN---------------RIGT-VGPPLPGVE 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 368 lmVKLDEDssrvGKILTRGPHTMLRYWGHQVAqenveTSESRSNEAWLDTGDIGAFDEFGNLWLIGRSNGRIKT-GGENV 446
Cdd:COG1022 409 --VKIAED----GEILVRGPNVMKGYYKNPEA-----TAEAFDADGWLHTGDIGELDEDGFLRITGRKKDLIVTsGGKNV 477
|
490 500
....*....|....*....|..
gi 22329863 447 YPEEVEAVLVEHPGIVSAVVIG 468
Cdd:COG1022 478 APQPIENALKASPLIEQAVVVG 499
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
34-545 |
9.65e-54 |
|
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: 188.57 E-value: 9.65e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 34 TGREFVDGVLSLAAGLIRLGLRNGDVVSIAAFNSdlfLEWL---LAVALVGGVVAPLnYRwSLKEAKMAMLL--VEPVLL 108
Cdd:cd05907 7 TWAEFAEEVRALAKGLIALGVEPGDRVAILSRNR---PEWTiadLAILAIGAVPVPI-YP-TSSAEQIAYILndSEAKAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 109 VTDETcvswcidvqngdipslkwrvlmeststdfanelnqflttemlkqrtlvpslatyawasDDAVVICFTSGTTGRPK 188
Cdd:cd05907 82 FVEDP----------------------------------------------------------DDLATIIYTSGTTGRPK 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 189 GVTISHLAFITQSLAKIAIAGYGEDDVYLHTSPLVHI-GGLSSAMAMLMVGACHVLLPkfDAKTALQVMEQNHITCFITV 267
Cdd:cd05907 104 GVMLSHRNILSNALALAERLPATEGDRHLSFLPLAHVfERRAGLYVPLLAGARIYFAS--SAETLLDDLSEVRPTVFLAV 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 268 PAM---MADLIRVnrttKNGAENRG----------VRKILNGGGSLSSELLK--EAVNIfPcarILSAYGMTEACSSLTF 332
Cdd:cd05907 182 PRVwekVYAAIKV----KAVPGLKRklfdlavggrLRFAASGGAPLPAELLHffRALGI-P---VYEGYGLTETSAVVTL 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 333 MTLHDptqesfkvtypllnqPKQGTcVGKPAPHIElmVKLDEDssrvGKILTRGPHTMLRYWGHQVAqenveTSESRSNE 412
Cdd:cd05907 254 NPPGD---------------NRIGT-VGKPLPGVE--VRIADD----GEILVRGPNVMLGYYKNPEA-----TAEALDAD 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 413 AWLDTGDIGAFDEFGNLWLIGRSNGRIKT-GGENVYPEEVEAVLVEHPGIVSAVVIGviDTRlgEMVVACVRLQEKwIWS 491
Cdd:cd05907 307 GWLHTGDLGEIDEDGFLHITGRKKDLIITsGGKNISPEPIENALKASPLISQAVVIG--DGR--PFLVALIVPDPE-ALE 381
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22329863 492 DVENRKGSFQLSSETLKHHCRT------------QNLTGFKIPKRFVRWEKQFP-----LTTTGKVKRDEV 545
Cdd:cd05907 382 AWAEEHGIAYTDVAELAANPAVraeieaaveaanARLSRYEQIKKFLLLPEPFTiengeLTPTLKLKRPVI 452
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
14-554 |
3.91e-52 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 187.13 E-value: 3.91e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 14 TRLASVKRNAVVTvYGNR--------KRTGREFVDGVLSLAAGLIRLGLRNGDVVSIAAFNSDLFLEWLLAVALVGGVVA 85
Cdd:PRK05605 32 TTLVDLYDNAVAR-FGDRpaldffgaTTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 86 ---PLnYR------------------WSlKEAKMAMLLVEPVLLvtdETCVSwcIDVQNG-----------DIPSLK--- 130
Cdd:PRK05605 111 ehnPL-YTahelehpfedhgarvaivWD-KVAPTVERLRRTTPL---ETIVS--VNMIAAmpllqrlalrlPIPALRkar 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 131 ------------WRVLMESTstdfanelnqfltteMLKQRTLVPSLATyawASDDAVVICFTSGTTGRPKGVTISHL--- 195
Cdd:PRK05605 184 aaltgpapgtvpWETLVDAA---------------IGGDGSDVSHPRP---TPDDVALILYTSGTTGKPKGAQLTHRnlf 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 196 AFITQSLAkiAIAGYGEDD-VYLHTSPLVHIGGLSSAMAM-LMVGACHVLLPKFDAKTALQVMEQNHITCFITVPAMMAD 273
Cdd:PRK05605 246 ANAAQGKA--WVPGLGDGPeRVLAALPMFHAYGLTLCLTLaVSIGGELVLLPAPDIDLILDAMKKHPPTWLPGVPPLYEK 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 274 LIRVNRttKNGAENRGVRKILNGGGSL---SSELLKEAVNifpcARILSAYGMTEaCSSLTfmtlhdptqesfkVTYPLL 350
Cdd:PRK05605 324 IAEAAE--ERGVDLSGVRNAFSGAMALpvsTVELWEKLTG----GLLVEGYGLTE-TSPII-------------VGNPMS 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 351 NQPKQGTcVGKPAPHIELMVKLDEDSSRV------GKILTRGPHTMLRYWGHQVAQENVETsesrsnEAWLDTGDIGAFD 424
Cdd:PRK05605 384 DDRRPGY-VGVPFPDTEVRIVDPEDPDETmpdgeeGELLVRGPQVFKGYWNRPEETAKSFL------DGWFRTGDVVVME 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 425 EFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGVIDTRLGEMVVACVRLQEkwiwsdvenrkGSfQLSS 504
Cdd:PRK05605 457 EDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEP-----------GA-ALDP 524
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 22329863 505 ETLKHHCRtQNLTGFKIPKRFVRWEKqFPLTTTGKVKRDEVRRQVLSHFQ 554
Cdd:PRK05605 525 EGLRAYCR-EHLTRYKVPRRFYHVDE-LPRDQLGKVRRREVREELLEKLG 572
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
174-547 |
7.85e-52 |
|
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: 180.22 E-value: 7.85e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 174 AVVIcFTSGTTGRPKGVTISHLAFITQSLAKIAIAGYGEDDVYLHTSPLVHIGGLSSAMAMLMVGACHVLLPKFDAktAL 253
Cdd:cd17630 3 ATVI-LTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLYHVGGLAILVRSLLAGAELVLLERNQA--LA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 254 QVMEQNHITCFITVPAMmadLIRVNRTTKNGAENRGVRKILNGGGSLSSELLKEAVnifpCARI--LSAYGMTEACSSLT 331
Cdd:cd17630 80 EDLAPPGVTHVSLVPTQ---LQRLLDSGQGPAALKSLRAVLLGGAPIPPELLERAA----DRGIplYTTYGMTETASQVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 332 FMTLHDPTQESfkvtypllnqpkqgtcVGKPAPHIELmvKLDEDssrvGKILTRGPHTMLRYWGHQVAQENvetsesrSN 411
Cdd:cd17630 153 TKRPDGFGRGG----------------VGVLLPGREL--RIVED----GEIWVGGASLAMGYLRGQLVPEF-------NE 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 412 EAWLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGVIDTRLGEMVVACVRLQEKWiws 491
Cdd:cd17630 204 DGWFTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRGPA--- 280
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 22329863 492 dvenrkgsfqlSSETLKHHCRTQnLTGFKIPKRFVRWeKQFPLTTTGKVKRDEVRR 547
Cdd:cd17630 281 -----------DPAELRAWLKDK-LARFKLPKRIYPV-PELPRTGGGKVDRRALRA 323
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
21-549 |
6.24e-51 |
|
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: 183.04 E-value: 6.24e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 21 RNAVVTvyGNRKRTGREFVDGVLSLAAGLIRLGLRNGDVVSIAAFNSDLFLEWLLAVALVGgvVAPLNYRWSLKEAKMAM 100
Cdd:COG1021 41 RIAVVD--GERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAG--AIPVFALPAHRRAEISH 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 101 L--LVEPVLLVTDetcvswciDVQNG------------DIPSLKwRVLMESTSTDFAnELNQFLTTEMlkqrtlvpSLAT 166
Cdd:COG1021 117 FaeQSEAVAYIIP--------DRHRGfdyralarelqaEVPSLR-HVLVVGDAGEFT-SLDALLAAPA--------DLSE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 167 YAWASDDAVVICFTSGTTGRPKGVTISHLAFITQSLAKIAIAGYGEDDVYLHTSPLVHIGGLSS--AMAMLMVGACHVLL 244
Cdd:COG1021 179 PRPDPDDVAFFQLSGGTTGLPKLIPRTHDDYLYSVRASAEICGLDADTVYLAALPAAHNFPLSSpgVLGVLYAGGTVVLA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 245 PKFDAKTALQVMEQNHITCFITVPAMMADLIrvnrttkNGAENRGV-----RKILNGGGSLSSELLKEAVNIFPCaRILS 319
Cdd:COG1021 259 PDPSPDTAFPLIERERVTVTALVPPLALLWL-------DAAERSRYdlsslRVLQVGGAKLSPELARRVRPALGC-TLQQ 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 320 AYGMTEAcsSLTFMTLHDPTQESFkvtypllnqpkqgTCVGKP-APHIELMVkLDEDSSRV-----GKILTRGPHTMLRY 393
Cdd:COG1021 331 VFGMAEG--LVNYTRLDDPEEVIL-------------TTQGRPiSPDDEVRI-VDEDGNPVppgevGELLTRGPYTIRGY 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 394 wgHQVAQENvetSESRSNEAWLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGVIDTR 473
Cdd:COG1021 395 --YRAPEHN---ARAFTPDGFYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEY 469
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22329863 474 LGEMVVACVRLQEKwiwsdvenrkgsfQLSSETLKHHCRTQNLTGFKIPKRFVRWEKqFPLTTTGKVKRDEVRRQV 549
Cdd:COG1021 470 LGERSCAFVVPRGE-------------PLTLAELRRFLRERGLAAFKLPDRLEFVDA-LPLTAVGKIDKKALRAAL 531
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
177-542 |
2.17e-50 |
|
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: 176.54 E-value: 2.17e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 177 ICFTSGTTGRPKGVTISHLAFITQSLAKIAIAGYGEDDVYLHTSPLVHIGGLSSA-MAMLMVGACHVLLPKFDAKTALQV 255
Cdd:cd17638 5 IMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIINPFFHTFGYKAGiVACLLTGATVVPVAVFDVDAILEA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 256 MEQNHITCFITVPAMMADLIRVNRTTKngAENRGVRKILNGGGSLSSELLKEAVNIFPCARILSAYGMTEAcsslTFMTL 335
Cdd:cd17638 85 IERERITVLPGPPTLFQSLLDHPGRKK--FDLSSLRAAVTGAATVPVELVRRMRSELGFETVLTAYGLTEA----GVATM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 336 HDPTQESFKVTypllnqpkqgTCVGKPAPHIElmVKLDEDssrvGKILTRGPHTMLRYWGHQVAqenveTSESRSNEAWL 415
Cdd:cd17638 159 CRPGDDAETVA----------TTCGRACPGFE--VRIADD----GEVLVRGYNVMQGYLDDPEA-----TAEAIDADGWL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 416 DTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGVIDTRLGEMVVACVRLQEkwiwsdven 495
Cdd:cd17638 218 HTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARP--------- 288
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 22329863 496 rkgSFQLSSETLKHHCRtQNLTGFKIPkRFVRWEKQFPLTTTGKVKR 542
Cdd:cd17638 289 ---GVTLTEEDVIAWCR-ERLANYKVP-RFVRFLDELPRNASGKVMK 330
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
22-542 |
1.32e-49 |
|
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: 177.33 E-value: 1.32e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 22 NAVVTVYGNRKRTGREFVDGVLSLAAGLIRLGLRNGDVVSIAAFNSdlfLEW---LLAVALVGGVVAPLNYRWSlkEAKM 98
Cdd:cd05930 2 DAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERS---LEMvvaILAVLKAGAAYVPLDPSYP--AERL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 99 AMLL--VEPVLLVTDetcvswcidvqngdipslkwrvlmeststdfanelnqflttemlkqrtlvpslatyawASDDAVV 176
Cdd:cd05930 77 AYILedSGAKLVLTD----------------------------------------------------------PDDLAYV 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 177 IcFTSGTTGRPKGVTISHLAFITQSLAKIAIAGYGEDDVYLHTSPLVHIGGLSSAMAMLMVGACHVLLPK---FDAKTAL 253
Cdd:cd05930 99 I-YTSGSTGKPKGVMVEHRGLVNLLLWMQEAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEevrKDPEALA 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 254 QVMEQNHITCFITVPAMMADLIRVNRTtkngAENRGVRKILNGGGSLSSELLKEAVNIFPCARILSAYGMTEACSSLTFM 333
Cdd:cd05930 178 DLLAEEGITVLHLTPSLLRLLLQELEL----AALPSLRLVLVGGEALPPDLVRRWRELLPGARLVNLYGPTEATVDATYY 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 334 TLHDPTQESFKVTypllnqpkqgtcVGKPAPHIELMVkLDEDSSRV-----------GKILTRGphtmlrYWGhqvaqen 402
Cdd:cd05930 254 RVPPDDEEDGRVP------------IGRPIPNTRVYV-LDENLRPVppgvpgelyigGAGLARG------YLN------- 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 403 vetSESRSNEAWLD-----------TGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGVID 471
Cdd:cd05930 308 ---RPELTAERFVPnpfgpgermyrTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVARED 384
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22329863 472 TRLGEMVVACVRLQEKWiwsdvenrkgsfQLSSETLKHHCRtQNLTGFKIPKRFVRWEkQFPLTTTGKVKR 542
Cdd:cd05930 385 GDGEKRLVAYVVPDEGG------------ELDEEELRAHLA-ERLPDYMVPSAFVVLD-ALPLTPNGKVDR 441
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
42-547 |
1.42e-49 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 180.04 E-value: 1.42e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 42 VLSLAAGLIR-LGLRNGDVVSIAAFNSDLFLEWLLAVALVGGVVAPLNYRWSLKEAKMAMLLVEPVLLVTDETCVswcid 120
Cdd:PLN02574 76 VKSMAAGLYHvMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAFTSPENV----- 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 121 vqnGDIPSLKWRVLMESTSTDFANELNQFLTTEMLKQRTLVPSLATYAwASDDAVVICFTSGTTGRPKGVTISHLAFIT- 199
Cdd:PLN02574 151 ---EKLSPLGVPVIGVPENYDFDSKRIEFPKFYELIKEDFDFVPKPVI-KQDDVAAIMYSSGTTGASKGVVLTHRNLIAm 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 200 -QSLAKIAIAGY---GEDDVYLHTSPLVHIGGLS-SAMAMLMVGACHVLLPKFDAKTALQVMEQNHITCFITVPAMMADL 274
Cdd:PLN02574 227 vELFVRFEASQYeypGSDNVYLAALPMFHIYGLSlFVVGLLSLGSTIVVMRRFDASDMVKVIDRFKVTHFPVVPPILMAL 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 275 IRvnrTTKNGAEN--RGVRKILNGGGSLSSELLKEAVNIFPCARILSAYGMTEACSSLT--FMTlhdptqesfkvtypll 350
Cdd:PLN02574 307 TK---KAKGVCGEvlKSLKQVSCGAAPLSGKFIQDFVQTLPHVDFIQGYGMTESTAVGTrgFNT---------------- 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 351 NQPKQGTCVGKPAPHIELMVkLDEDSSRV------GKILTRGPHTMLRYWGHQVAqenveTSESRSNEAWLDTGDIGAFD 424
Cdd:PLN02574 368 EKLSKYSSVGLLAPNMQAKV-VDWSTGCLlppgncGELWIQGPGVMKGYLNNPKA-----TQSTIDKDGWLRTGDIAYFD 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 425 EFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGVIDTRLGEMVVACvrlqekwiwsdVENRKGSfQLSS 504
Cdd:PLN02574 442 EDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAF-----------VVRRQGS-TLSQ 509
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 22329863 505 ETLKHHCRTQNLTGFKIPKrfVRWEKQFPLTTTGKVKRDEVRR 547
Cdd:PLN02574 510 EAVINYVAKQVAPYKKVRK--VVFVQSIPKSPAGKILRRELKR 550
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
12-560 |
2.16e-49 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 179.54 E-value: 2.16e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 12 CLTRLASVKRNAVVTVYGN-----RKRTGREFVDGVLSLAAGLIRLGLRNGDVVSIAAFNSdlfLEW---LLAVALVGGV 83
Cdd:COG0365 14 CLDRHAEGRGDKVALIWEGedgeeRTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNI---PEAviaMLACARIGAV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 84 VAPLNYRWSLKEAKMAMLLVEPVLLVTDETCVSWCIDVQNGDI--------PSLKWRVLMESTSTDFANELNQFLTTEML 155
Cdd:COG0365 91 HSPVFPGFGAEALADRIEDAEAKVLITADGGLRGGKVIDLKEKvdealeelPSLEHVIVVGRTGADVPMEGDLDWDELLA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 156 KQRTLVPSLATyawASDDAVVICFTSGTTGRPKGVTISHLAFITQsLAKIA--IAGYGEDDVYLHTSPLVHIGGLSSAM- 232
Cdd:COG0365 171 AASAEFEPEPT---DADDPLFILYTSGTTGKPKGVVHTHGGYLVH-AATTAkyVLDLKPGDVFWCTADIGWATGHSYIVy 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 233 AMLMVGACHVLL---PKF-DAKTALQVMEQNHITCFITVPAMMADLIRVNRTTKNGAENRGVRKILNGGGSLSSELL--- 305
Cdd:COG0365 247 GPLLNGATVVLYegrPDFpDPGRLWELIEKYGVTVFFTAPTAIRALMKAGDEPLKKYDLSSLRLLGSAGEPLNPEVWeww 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 306 KEAVNIfpcaRILSAYGMTEACSsltFMTLHDPTQEsfkvtypllnqPKQGTCvGKPAPHIELMVkLDEDSSRV-----G 380
Cdd:COG0365 327 YEAVGV----PIVDGWGQTETGG---IFISNLPGLP-----------VKPGSM-GKPVPGYDVAV-VDEDGNPVppgeeG 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 381 KILTRGPHT--MLRYWGhqvaqenvetSESRSNEAWLD-------TGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEV 451
Cdd:COG0365 387 ELVIKGPWPgmFRGYWN----------DPERYRETYFGrfpgwyrTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEI 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 452 EAVLVEHPGIVSAVVIGVIDTRLGEMVVACVRLQEKWIWSDvenrkgsfQLSSEtLKHHCRtQNLTGFKIPKRfVRWEKQ 531
Cdd:COG0365 457 ESALVSHPAVAEAAVVGVPDEIRGQVVKAFVVLKPGVEPSD--------ELAKE-LQAHVR-EELGPYAYPRE-IEFVDE 525
|
570 580
....*....|....*....|....*....
gi 22329863 532 FPLTTTGKVKRDEVRRQVLSHFQIMTSSL 560
Cdd:COG0365 526 LPKTRSGKIMRRLLRKIAEGRPLGDTSTL 554
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
14-548 |
7.01e-48 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 173.91 E-value: 7.01e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 14 TRLASVKRNAVVTVYGnRKRTGREFVDGVLSLAAGLIRLGLRNGDVV------SIAAfnsdLFLewLLAVALVGGVVAPL 87
Cdd:PRK07514 11 AAFADRDAPFIETPDG-LRYTYGDLDAASARLANLLVALGVKPGDRVavqvekSPEA----LAL--YLATLRAGAVFLPL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 88 NYRWSLKEakMAMLLV--EPVLLVTDETCVSWCidvqngdipslkwRVLMESTSTDFANELNQFLTTEMLK-QRTLVPSL 164
Cdd:PRK07514 84 NTAYTLAE--LDYFIGdaEPALVVCDPANFAWL-------------SKIAAAAGAPHVETLDADGTGSLLEaAAAAPDDF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 165 ATYAWASDDAVVICFTSGTTGRPKGVTISHLAFITQSLAKIAIAGYGEDDVYLHTSPLVHIGGLSSAM-AMLMVGACHVL 243
Cdd:PRK07514 149 ETVPRGADDLAAILYTSGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPDDVLIHALPIFHTHGLFVATnVALLAGASMIF 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 244 LPKFDAKTALQVMEQNhiTCFITVPAMMADLIRVNRTTKNGAenRGVRKILNGggslSSELLKEAVNIFPcAR----ILS 319
Cdd:PRK07514 229 LPKFDPDAVLALMPRA--TVMMGVPTFYTRLLQEPRLTREAA--AHMRLFISG----SAPLLAETHREFQ-ERtghaILE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 320 AYGMTEacsslTFMTlhdptqesfkVTYPLLNQPKQGTcVGKPAPHIELMVkLDEDSSR------VGKILTRGPHTMLRY 393
Cdd:PRK07514 300 RYGMTE-----TNMN----------TSNPYDGERRAGT-VGFPLPGVSLRV-TDPETGAelppgeIGMIEVKGPNVFKGY 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 394 WghqvaQENVETSESRSNEAWLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGVIDTR 473
Cdd:PRK07514 363 W-----RMPEKTAEEFRADGFFITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPD 437
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22329863 474 LGEMVVACVrlqekwiwsdVenRKGSFQLSSETLKHHCRTQnLTGFKIPKRfVRWEKQFPLTTTGKVKRDEVRRQ 548
Cdd:PRK07514 438 FGEGVTAVV----------V--PKPGAALDEAAILAALKGR-LARFKQPKR-VFFVDELPRNTMGKVQKNLLREQ 498
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
22-547 |
1.66e-47 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 173.53 E-value: 1.66e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 22 NAVVTVYGNRKRTGREFVDGVLSLAAGLIRLGLRNGDVVSIAAFNSDLFLEWLLAVALVGGVVAPLNYRWslKEAKMAML 101
Cdd:PRK07798 18 DRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRY--VEDELRYL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 102 L--VEPVLLVTdETCVSWCIDVQNGDIPSLKWRVLMESTSTD----FANELNQFLTTEMLKQRTLVPSlatyawaSDDAV 175
Cdd:PRK07798 96 LddSDAVALVY-EREFAPRVAEVLPRLPKLRTLVVVEDGSGNdllpGAVDYEDALAAGSPERDFGERS-------PDDLY 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 176 VICfTSGTTGRPKGVTISH----------LAFIT-------QSLAKIAIAGYGEddVYLHTSPLVHIGGLSSAMAMLMVG 238
Cdd:PRK07798 168 LLY-TGGTTGMPKGVMWRQedifrvllggRDFATgepiedeEELAKRAAAGPGM--RRFPAPPLMHGAGQWAAFAALFSG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 239 ACHVLLP--KFDAKTALQVMEQNHIT-CFITVPAM---MADLIRvnrtTKNGAENRGVRKILNGGGSLSSELLKEAVNIF 312
Cdd:PRK07798 245 QTVVLLPdvRFDADEVWRTIEREKVNvITIVGDAMarpLLDALE----ARGPYDLSSLFAIASGGALFSPSVKEALLELL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 313 PCARILSAYGMTEACSSLTFMTLHDPTQE-SFKVTypllnqPKQGTCVgkpaphielmvkLDEDSSRV------GKILTR 385
Cdd:PRK07798 321 PNVVLTDSIGSSETGFGGSGTVAKGAVHTgGPRFT------IGPRTVV------------LDEDGNPVepgsgeIGWIAR 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 386 GPHTMLRYWGHQVAQEnvETSESRSNEAWLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAV 465
Cdd:PRK07798 383 RGHIPLGYYKDPEKTA--ETFPTIDGVRYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADAL 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 466 VIGVIDTRLGEMVVACVRLQEkwiwsdvenrkGSfQLSSETLKHHCRTQnLTGFKIPKRFVRwekqfpltttgkvkRDEV 545
Cdd:PRK07798 461 VVGVPDERWGQEVVAVVQLRE-----------GA-RPDLAELRAHCRSS-LAGYKVPRAIWF--------------VDEV 513
|
..
gi 22329863 546 RR 547
Cdd:PRK07798 514 QR 515
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
44-550 |
7.56e-47 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 172.24 E-value: 7.56e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 44 SLAAGLIRLGLRNGDVVsiaAFNSDLFLEWL---LAVALVGGVVAPLNYRWSLKEAKMAMLLVEPVLLVT-----DETCV 115
Cdd:PRK06087 61 RLANWLLAKGIEPGDRV---AFQLPGWCEFTiiyLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFAptlfkQTRPV 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 116 SWCIDVQNgDIPSLKWRVLME----STSTDfanELNQFLTTEmlkqrtlvPSLATYAWA-SDDAVVICFTSGTTGRPKGV 190
Cdd:PRK06087 138 DLILPLQN-QLPQLQQIVGVDklapATSSL---SLSQIIADY--------EPLTTAITThGDELAAVLFTSGTEGLPKGV 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 191 TISHLAFITQSLAKIAIAGYGEDDVYLHTSPLVHIGG-LSSAMAMLMVGACHVLLPKFDAKTALQVMEQNHITCFITVPA 269
Cdd:PRK06087 206 MLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGfLHGVTAPFLIGARSVLLDIFTPDACLALLEQQRCTCMLGATP 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 270 MMADLIrvNRTTKNGAENRGVRKILNGGGSLSSELLKEAV--NIfpcaRILSAYGMTEACSSlTFMTLHDPTqesfkvty 347
Cdd:PRK06087 286 FIYDLL--NLLEKQPADLSALRFFLCGGTTIPKKVARECQqrGI----KLLSVYGSTESSPH-AVVNLDDPL-------- 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 348 pllnqPKQGTCVGKPAPHIELMVkLDEDSSRV-----GKILTRGPHTMLRYWGhqvaqENVETSESRSNEAWLDTGDIGA 422
Cdd:PRK06087 351 -----SRFMHTDGYAAAGVEIKV-VDEARKTLppgceGEEASRGPNVFMGYLD-----EPELTARALDEEGWYYSGDLCR 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 423 FDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGVIDTRLGEMVVACVRLQEKwiwsdvENRkgsfqL 502
Cdd:PRK06087 420 MDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVVLKAP------HHS-----L 488
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 22329863 503 SSETLKHHCRTQNLTGFKIPKRFVRWEKqFPLTTTGKVKRDEVRRQVL 550
Cdd:PRK06087 489 TLEEVVAFFSRKRVAKYKYPEHIVVIDK-LPRTASGKIQKFLLRKDIM 535
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
31-549 |
2.81e-45 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 167.92 E-value: 2.81e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 31 RKRTGREFVDGVLSLAAGLIRLGLRNGDVVSIAAFNSDLFLEWLLAVALVGGVVAPL-------NYRWSLKEAKMAMLLV 103
Cdd:PRK13295 54 RRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLmpifrerELSFMLKHAESKVLVV 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 104 EPVLLVTDETCVSWCIdvqNGDIPSLKWRVLMEStstDFANELNQFLTT-EMLKQRTLVPSLATYAWASDDAVVICFTSG 182
Cdd:PRK13295 134 PKTFRGFDHAAMARRL---RPELPALRHVVVVGG---DGADSFEALLITpAWEQEPDAPAILARLRPGPDDVTQLIYTSG 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 183 TTGRPKGVTISHLAFITQSLAKIAIAGYGEDDVYLHTSPLVHIGGLSSAMAM-LMVGACHVLLPKFDAKTALQVMEQNHI 261
Cdd:PRK13295 208 TTGEPKGVMHTANTLMANIVPYAERLGLGADDVILMASPMAHQTGFMYGLMMpVMLGATAVLQDIWDPARAAELIRTEGV 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 262 TCFITVPAMMADLIRVnrTTKNGAENRGVRKILNGGGSLSSELLKEAVNIFPcARILSAYGMTEaCSSLTFMTLHDPTQE 341
Cdd:PRK13295 288 TFTMASTPFLTDLTRA--VKESGRPVSSLRTFLCAGAPIPGALVERARAALG-AKIVSAWGMTE-NGAVTLTKLDDPDER 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 342 SFkvtypllnqpkqgTCVGKPAPHIELMVkLDEDSSRV-----GKILTRGPHTMLRYWGHQvaQENvetseSRSNEAWLD 416
Cdd:PRK13295 364 AS-------------TTDGCPLPGVEVRV-VDADGAPLpagqiGRLQVRGCSNFGGYLKRP--QLN-----GTDADGWFD 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 417 TGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGVIDTRLGEMVVACVRLqekwiwsdvenR 496
Cdd:PRK13295 423 TGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVP-----------R 491
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 22329863 497 KGSfQLSSETLKHHCRTQNLTGFKIPKRFVRWEkQFPLTTTGKVKRDEVRRQV 549
Cdd:PRK13295 492 PGQ-SLDFEEMVEFLKAQKVAKQYIPERLVVRD-ALPRTPSGKIQKFRLREML 542
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
21-551 |
3.18e-45 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 166.52 E-value: 3.18e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 21 RNAVVTVYGNRKRTGREFVDGVLSLAAGLIRLGLRNGDVVSIAAFNSDLFLEWLLAVALVGGVVAPLNYRWSLKEAKMAM 100
Cdd:PRK09088 11 RLAAVDLALGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 101 LLVEPVLLVTDETcvswcidVQNGdipslkwRVLMESTStDFANELNQFlttemlkqrtlvpSLATYAWASDDAV-VICF 179
Cdd:PRK09088 91 QDAEPRLLLGDDA-------VAAG-------RTDVEDLA-AFIASADAL-------------EPADTPSIPPERVsLILF 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 180 TSGTTGRPKGVTISHlafitQSLAKIAI-----AGYGEDDVYLHTSPLVHIGGL-SSAMAMLMVGACHVLLPKFDAKTAL 253
Cdd:PRK09088 143 TSGTSGQPKGVMLSE-----RNLQQTAHnfgvlGRVDAHSSFLCDAPMFHIIGLiTSVRPVLAVGGSILVSNGFEPKRTL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 254 QVMEQNH--ITCFITVPAMMaDLIRvNRTTKNGAENRGVRKILNGGGSLSSE----LLKEAVnifpcaRILSAYGMTEAC 327
Cdd:PRK09088 218 GRLGDPAlgITHYFCVPQMA-QAFR-AQPGFDAAALRHLTALFTGGAPHAAEdilgWLDDGI------PMVDGFGMSEAG 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 328 SSLTfMTLhDPTqesfkvtyplLNQPKQGTcVGKPAPHIELMVkLDEDSSRV-----GKILTRGPHTMLRYWghqvaQEN 402
Cdd:PRK09088 290 TVFG-MSV-DCD----------VIRAKAGA-AGIPTPTVQTRV-VDDQGNDCpagvpGELLLRGPNLSPGYW-----RRP 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 403 VETSESRSNEAWLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGVIDTRLGEMVVACV 482
Cdd:PRK09088 351 QATARAFTGDGWFRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAI 430
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22329863 483 RLQEkwiwsdvenrkgSFQLSSETLKHHCRTQnLTGFKIPKRFvRWEKQFPLTTTGKVKRDEVRRQVLS 551
Cdd:PRK09088 431 VPAD------------GAPLDLERIRSHLSTR-LAKYKVPKHL-RLVDALPRTASGKLQKARLRDALAA 485
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
11-550 |
6.20e-45 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 166.37 E-value: 6.20e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 11 QCLTRLASVKRNAVVTVYGNRKRTGREFVDGVLSLAAGLIRLGLRNGDVVSIAAFNSDLFLEWLLAVALVGGVVAPLNYR 90
Cdd:PRK07470 11 HFLRQAARRFPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 91 WS------LKEAKMAMLLV------EPVLLVTDETcvswcidvqngdiPSLKWRVLMESTstDFANELnqflttEMLKQR 158
Cdd:PRK07470 91 QTpdevayLAEASGARAMIchadfpEHAAAVRAAS-------------PDLTHVVAIGGA--RAGLDY------EALVAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 159 TLVPSLATYAWASDDAVVICFTSGTTGRPKGVTISH--LAF-ITQSLAKIaIAGYGEDDVYLHTSPLVHIGGLSsAMAML 235
Cdd:PRK07470 150 HLGARVANAAVDHDDPCWFFFTSGTTGRPKAAVLTHgqMAFvITNHLADL-MPGTTEQDASLVVAPLSHGAGIH-QLCQV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 236 MVGACHVLLP--KFDAKTALQVMEQNHITCFITVPA---MMADLIRVNRttkngAENRGVRKILNGGGSLSSELLKEAVN 310
Cdd:PRK07470 228 ARGAATVLLPseRFDPAEVWALVERHRVTNLFTVPTilkMLVEHPAVDR-----YDHSSLRYVIYAGAPMYRADQKRALA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 311 IFpcARILSAY-GMTEACSSLTFMT--LHDPTQESfkvtypllnQPKQGTCvGKPAPHIELMVKLDE----DSSRVGKIL 383
Cdd:PRK07470 303 KL--GKVLVQYfGLGEVTGNITVLPpaLHDAEDGP---------DARIGTC-GFERTGMEVQIQDDEgrelPPGETGEIC 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 384 TRGPHTMLRYWghqvaqENVETSESRSNEAWLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVS 463
Cdd:PRK07470 371 VIGPAVFAGYY------NNPEANAKAFRDGWFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSE 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 464 AVVIGVIDTRLGEMVVA-CVrlqekwiwsdvenRKGSFQLSSETLKHHCRTqNLTGFKIPKRFVRWEkQFPLTTTGKVKR 542
Cdd:PRK07470 445 VAVLGVPDPVWGEVGVAvCV-------------ARDGAPVDEAELLAWLDG-KVARYKLPKRFFFWD-ALPKSGYGKITK 509
|
....*...
gi 22329863 543 DEVRRQVL 550
Cdd:PRK07470 510 KMVREELE 517
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
173-540 |
4.97e-44 |
|
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: 159.39 E-value: 4.97e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 173 DAVVICFTSGTTGRPKGVTISHLAFITQSLAKIAIAGYGEDDVYLHTSPLVHIGGLSSAMAMLMVGACHVLLPKFDAKTA 252
Cdd:cd17636 1 DPVLAIYTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTVFLNSGPLFHIGTLMFTLATFHAGGTNVFVRRVDAEEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 253 LQVMEQNHITCFITVPAMMADLIRVNRTTKNGAEnrgvrkilngggSLSSELLKE------AVNIFPCARILSAYGMTEA 326
Cdd:cd17636 81 LELIEAERCTHAFLLPPTIDQIVELNADGLYDLS------------SLRSSPAAPewndmaTVDTSPWGRKPGGYGQTEV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 327 CSSLTFMTLHDPTQESFkvtypllnqpkqgtcvGKPAPHIELMVkLDED-----SSRVGKILTRGPHTMLRYWGHQvaQE 401
Cdd:cd17636 149 MGLATFAALGGGAIGGA----------------GRPSPLVQVRI-LDEDgrevpDGEVGEIVARGPTVMAGYWNRP--EV 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 402 NVEtsesRSNEAWLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGVIDTRLGEMVVAC 481
Cdd:cd17636 210 NAR----RTRGGWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAI 285
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 22329863 482 VRLQEkwiwsdvenrkGSfQLSSETLKHHCRTQnLTGFKIPKrFVRWEKQFPLTTTGKV 540
Cdd:cd17636 286 VVLKP-----------GA-SVTEAELIEHCRAR-IASYKKPK-SVEFADALPRTAGGAD 330
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
37-542 |
1.68e-43 |
|
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: 160.34 E-value: 1.68e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 37 EFVDGVLSLAAGLIRLGLRNGDVVSIAAFNSDLFLEWLLAVALVGGVVAPLNyrwslkeakmamllvepvllvtdetcvs 116
Cdd:cd05935 6 ELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPIN---------------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 117 wcidvqngdiPSLKWRvlmeststdfanELNQFLTTEMLKQRTLVPSLatyawasDDAVVICFTSGTTGRPKGVTISHLA 196
Cdd:cd05935 58 ----------PMLKER------------ELEYILNDSGAKVAVVGSEL-------DDLALIPYTSGTTGLPKGCMHTHFS 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 197 FITQSLAKIAIAGYGEDDVYLHTSPLVHIGGL-SSAMAMLMVGACHVLLPKFDAKTALQVMEQNHITCFITVPAMMADLI 275
Cdd:cd05935 109 AAANALQSAVWTGLTPSDVILACLPLFHVTGFvGSLNTAVYVGGTYVLMARWDRETALELIEKYKVTFWTNIPTMLVDLL 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 276 RvnrTTKNGAENRGVRKILNGGGSLSSELLKEAVNIFPCARILSAYGMTEACSSLTfmtlhdptqesfkvTYPLLNQPKQ 355
Cdd:cd05935 189 A---TPEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTETMSQTH--------------TNPPLRPKLQ 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 356 gtCVGKPAPHIELMVkLDEDSSR------VGKILTRGPHTMLRYWghQVAQENVETSESRSNEAWLDTGDIGAFDEFGNL 429
Cdd:cd05935 252 --CLGIP*FGVDARV-IDIETGRelppneVGEIVVRGPQIFKGYW--NRPEETEESFIEIKGRRFFRTGDLGYMDEEGYF 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 430 WLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGVIDTRLGEMVVACVRLQEkwiwsdvENRKgsfQLSSETLKH 509
Cdd:cd05935 327 FFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRP-------EYRG---KVTEEDIIE 396
|
490 500 510
....*....|....*....|....*....|...
gi 22329863 510 HCRTQnLTGFKIPkRFVRWEKQFPLTTTGKVKR 542
Cdd:cd05935 397 WAREQ-MAAYKYP-REVEFVDELPRSASGKILW 427
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
37-486 |
6.86e-43 |
|
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341297 [Multi-domain] Cd Length: 532 Bit Score: 160.77 E-value: 6.86e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 37 EFVDGVLSLAAGLIRLGLRNGDVVSIAAFNSDLFLEWLLAVALVGGVVAPLNYRWSLKEAKMAMLLVEPVLLVTDETCVS 116
Cdd:cd17642 49 EYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFCSKKGLQ 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 117 WCIDVQNgDIPSLKWRVLMESTStdfanELNQFLTTEMLKQRTLVPSLATYAWAS------DDAVVICFTSGTTGRPKGV 190
Cdd:cd17642 129 KVLNVQK-KLKIIKTIIILDSKE-----DYKGYQCLYTFITQNLPPGFNEYDFKPpsfdrdEQVALIMNSSGSTGLPKGV 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 191 TISHLAFITQ-SLAKIAIAGYG--EDDVYLHTSPLVHIGGLSSAMAMLMVGACHVLLPKFDAKTALQVMEQNHITCFITV 267
Cdd:cd17642 203 QLTHKNIVARfSHARDPIFGNQiiPDTAILTVIPFHHGFGMFTTLGYLICGFRVVLMYKFEEELFLRSLQDYKVQSALLV 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 268 PAMMADLIRVNRTTKNGAENrgVRKILNGGGSLSSELLKEAVNIFPCARILSAYGMTEACSSLTFmtlhdpTQESFKvty 347
Cdd:cd17642 283 PTLFAFFAKSTLVDKYDLSN--LHEIASGGAPLSKEVGEAVAKRFKLPGIRQGYGLTETTSAILI------TPEGDD--- 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 348 pllnqpKQGTCvGKPAPHIELMVkLDEDSSRV------GKILTRGPHTMLRYWGHQVAqenveTSESRSNEAWLDTGDIG 421
Cdd:cd17642 352 ------KPGAV-GKVVPFFYAKV-VDLDTGKTlgpnerGELCVKGPMIMKGYVNNPEA-----TKALIDKDGWLHSGDIA 418
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22329863 422 AFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGVIDTRLGEMVVACVRLQE 486
Cdd:cd17642 419 YYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVVLEA 483
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
33-547 |
1.11e-42 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 160.48 E-value: 1.11e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 33 RTGREFVDGVLSLAAGLIRLGLRNGDVVSIAAFNSDLFLEWLLAVALVGGVVAPLNYRWS---LKEAkMAMLLVEpVLLV 109
Cdd:PRK07788 75 LTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSgpqLAEV-AAREGVK-ALVY 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 110 TDE-------------TCVSWCIDVQNGDIPSLKWRVLMESTSTDfanelnqflTTEMLKqrtlvpslatyAWASDDAVV 176
Cdd:PRK07788 153 DDEftdllsalppdlgRLRAWGGNPDDDEPSGSTDETLDDLIAGS---------STAPLP-----------KPPKPGGIV 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 177 IcFTSGTTGRPKGVTISH---LAFITQSLAKIAiagYGEDDVYLHTSPLVHIGGLSSAMAMLMVGACHVLLPKFDAKTAL 253
Cdd:PRK07788 213 I-LTSGTTGTPKGAPRPEpspLAPLAGLLSRVP---FRAGETTLLPAPMFHATGWAHLTLAMALGSTVVLRRRFDPEATL 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 254 QVMEQNHITCFITVPAMMADLIRVNRTTKNGAENRGVRKILNGGGSLSSELLKEAVNIF-PcaRILSAYGMTEAcsslTF 332
Cdd:PRK07788 289 EDIAKHKATALVVVPVMLSRILDLGPEVLAKYDTSSLKIIFVSGSALSPELATRALEAFgP--VLYNLYGSTEV----AF 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 333 MTLHDPtQEsfkvtypLLNQPkqgTCVGKPAP--HIELmvkLDEDSSRV-----GKILTRGPHTMLRYWGhqvaqenvet 405
Cdd:PRK07788 363 ATIATP-ED-------LAEAP---GTVGRPPKgvTVKI---LDENGNEVprgvvGRIFVGNGFPFEGYTD---------- 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 406 seSRSNE---AWLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGVID----TRLGEMV 478
Cdd:PRK07788 419 --GRDKQiidGLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDeefgQRLRAFV 496
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22329863 479 VAcvrlqekwiwsdvenRKGSfQLSSETLKHHCRTqNLTGFKIPkRFVRWEKQFPLTTTGKVKRDEVRR 547
Cdd:PRK07788 497 VK---------------APGA-ALDEDAIKDYVRD-NLARYKVP-RDVVFLDELPRNPTGKVLKRELRE 547
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
36-548 |
1.49e-42 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 160.05 E-value: 1.49e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 36 REFVDGVLSLAAGLIRLGLRNGDVVSIAAFNSDLFLEWLLAVALVGGVVAPLNYRWSLKE--AKMAMLLVEPVLLVTDET 113
Cdd:PRK05852 47 RDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEqrVRSQAAGARVVLIDADGP 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 114 CvswcidvqNGDIPSLKWRVLMESTSTDFANELNqflTTEMLKQRTLVPSLATYA---WASDDAVvICFTSGTTGRPKGV 190
Cdd:PRK05852 127 H--------DRAEPTTRWWPLTVNVGGDSGPSGG---TLSVHLDAATEPTPATSTpegLRPDDAM-IMFTGGTTGLPKMV 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 191 TISHlAFITQSLAKIaIAGY--GEDDVYLHTSPLVHIGGLSSAMAMLMVGACHVLLP---KFDAKTALQVMEQNHITCFI 265
Cdd:PRK05852 195 PWTH-ANIASSVRAI-ITGYrlSPRDATVAVMPLYHGHGLIAALLATLASGGAVLLPargRFSAHTFWDDIKAVGATWYT 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 266 TVPAMMADLIRVNRTTKNGAENRGVRKILNGGGSLSSELLKEAVNIFpCARILSAYGMTEACSSLT------FMTLHDPT 339
Cdd:PRK05852 273 AVPTIHQILLERAATEPSGRKPAALRFIRSCSAPLTAETAQALQTEF-AAPVVCAFGMTEATHQVTttqiegIGQTENPV 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 340 QESFKVTYPLLNQPKQGTCVGKPAPhielmvkldedSSRVGKILTRGPHTMLRYWGhqvaqeNVETSESRSNEAWLDTGD 419
Cdd:PRK05852 352 VSTGLVGRSTGAQIRIVGSDGLPLP-----------AGAVGEVWLRGTTVVRGYLG------DPTITAANFTDGWLRTGD 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 420 IGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGVIDTRLGEMVVACVRLQEkwiwsdvenrkgS 499
Cdd:PRK05852 415 LGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIVPRE------------S 482
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 22329863 500 FQLSSETLKHHCRTQnLTGFKIPKRFVRWEkQFPLTTTGKVKRDEVRRQ 548
Cdd:PRK05852 483 APPTAEELVQFCRER-LAAFEIPASFQEAS-GLPHTAKGSLDRRAVAEQ 529
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
52-542 |
2.04e-42 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 159.08 E-value: 2.04e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 52 LGLRNGDVVSIAAFNSDLFLEWLLAVALVGGVVAPLNYRWSLKEAKMAMLLVEPVLLVTDETCVSWCIDVQNGDIPSLKW 131
Cdd:PRK08008 57 LGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASLLVTSAQFYPMYRQIQQEDATPLRH 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 132 RVLMESTS------TDFANELNQfLTTEMLKQRTLvpslatyawASDDAVVICFTSGTTGRPKGVTISHlafitqslAKI 205
Cdd:PRK08008 137 ICLTRVALpaddgvSSFTQLKAQ-QPATLCYAPPL---------STDDTAEILFTSGTTSRPKGVVITH--------YNL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 206 AIAGY--------GEDDVYLHTSPLVHIG-GLSSAMAMLMVGACHVLLPKFDAKTALQVMEQNHITCFITVPAMMADLIR 276
Cdd:PRK08008 199 RFAGYysawqcalRDDDVYLTVMPAFHIDcQCTAAMAAFSAGATFVLLEKYSARAFWGQVCKYRATITECIPMMIRTLMV 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 277 vnRTTKNGAENRGVRKI---LNgggslSSELLKEAVNIFPCARILSAYGMTEACSSLtfmtLHDPTQEsfKVTYPLLNQP 353
Cdd:PRK08008 279 --QPPSANDRQHCLREVmfyLN-----LSDQEKDAFEERFGVRLLTSYGMTETIVGI----IGDRPGD--KRRWPSIGRP 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 354 kqGTCV--------GKPAPHIElmvkldedssrVGKILTRG-P-HTMLR-YWGHQVAqenveTSESRSNEAWLDTGDIGA 422
Cdd:PRK08008 346 --GFCYeaeirddhNRPLPAGE-----------IGEICIKGvPgKTIFKeYYLDPKA-----TAKVLEADGWLHTGDTGY 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 423 FDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGVIDTRLGEMVVACVRLQEkwiwsdvenrkgSFQL 502
Cdd:PRK08008 408 VDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNE------------GETL 475
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 22329863 503 SSETLKHHCRtQNLTGFKIPKrFVRWEKQFPLTTTGKVKR 542
Cdd:PRK08008 476 SEEEFFAFCE-QNMAKFKVPS-YLEIRKDLPRNCSGKIIK 513
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
179-546 |
2.79e-42 |
|
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: 157.92 E-value: 2.79e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 179 FTSGTTGRPKGVTISHLAFITQSLAKIAIA---GYGEDDVYLHTSPLVHIGGLSSAMAMLMVGACHVLLPKFDAKTALQV 255
Cdd:cd05929 132 YSGGTTGRPKGIKRGLPGGPPDNDTLMAAAlgfGPGADSVYLSPAPLYHAAPFRWSMTALFMGGTLVLMEKFDPEEFLRL 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 256 MEQNHITCFITVPAMMADLIRVNRTTKNgAENRGVRKILNGGGSLSSELLKEAVNIFPCARILSAYGMTEaCSSLTFMTL 335
Cdd:cd05929 212 IERYRVTFAQFVPTMFVRLLKLPEAVRN-AYDLSSLKRVIHAAAPCPPWVKEQWIDWGGPIIWEYYGGTE-GQGLTIING 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 336 HDptqesfKVTYPllnqpkqGTcVGKPAP---HIelmvkLDEDSSRV-----GKILTRGPHTMLrywghqVAQENVETSE 407
Cdd:cd05929 290 EE------WLTHP-------GS-VGRAVLgkvHI-----LDEDGNEVppgeiGEVYFANGPGFE------YTNDPEKTAA 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 408 SRSNEAWLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGVIDTRLGEMVVACvrlqek 487
Cdd:cd05929 345 ARNEGGWSTLGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAV------ 418
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22329863 488 wiwsdVENRKGSF--QLSSETLKHHCRtQNLTGFKIPKRFvRWEKQFPLTTTGKVKRDEVR 546
Cdd:cd05929 419 -----VQPAPGADagTALAEELIAFLR-DRLSRYKCPRSI-EFVAELPRDDTGKLYRRLLR 472
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
29-548 |
4.43e-42 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 157.94 E-value: 4.43e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 29 GNRKRTGREFVDGVLSLAAGLIRLGLRNGDVVSIAAFNSDLFLEWLLAVALVGGVVAPLNY-------RWSLKEAKMAML 101
Cdd:PRK12406 8 GDRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWhfkpeeiAYILEDSGARVL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 102 -----LVEPVLLVTDETCVSWCIDVQnGDIPSlKWRVLMESTST-DFANELNQFLTTEMLKQRTLVPSLATyawasddav 175
Cdd:PRK12406 88 iahadLLHGLASALPAGVTVLSVPTP-PEIAA-AYRISPALLTPpAGAIDWEGWLAQQEPYDGPPVPQPQS--------- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 176 vICFTSGTTGRPKGV-----TISHLAfitqSLAKIAIAGYG--EDDVYLHTSPLVHIGGLSSAMAMLMVGACHVLLPKFD 248
Cdd:PRK12406 157 -MIYTSGTTGHPKGVrraapTPEQAA----AAEQMRALIYGlkPGIRALLTGPLYHSAPNAYGLRAGRLGGVLVLQPRFD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 249 AKTALQVMEQNHITCFITVPAMMADLIRVNRTTKNGAENRGVRKILNGGGSLSSELlKEAVNIFPCARILSAYGMTEAcS 328
Cdd:PRK12406 232 PEELLQLIERHRITHMHMVPTMFIRLLKLPEEVRAKYDVSSLRHVIHAAAPCPADV-KRAMIEWWGPVIYEYYGSTES-G 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 329 SLTFMTLHDptqesfkvtypLLNQPkqGTcVGKPAPHIELMVkLDED-----SSRVGKILTRGP-HTMLRYWGHQVAQEN 402
Cdd:PRK12406 310 AVTFATSED-----------ALSHP--GT-VGKAAPGAELRF-VDEDgrplpQGEIGEIYSRIAgNPDFTYHNKPEKRAE 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 403 VEtsesrsNEAWLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGVIDTRLGEMVVACV 482
Cdd:PRK12406 375 ID------RGGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVV 448
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22329863 483 RLQEkwiwsdvenrkgSFQLSSETLKHHCRTQnLTGFKIPKRfVRWEKQFPLTTTGKVKRDEVRRQ 548
Cdd:PRK12406 449 EPQP------------GATLDEADIRAQLKAR-LAGYKVPKH-IEIMAELPREDSGKIFKRRLRDP 500
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
170-547 |
8.86e-42 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 154.08 E-value: 8.86e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 170 ASDDAVVICFTSGTTGRPKGVTISH------------LAFITQSLAKIAI--AGYGEDDVYLHTSPLVHIGGLSSAMAML 235
Cdd:cd05924 1 RSADDLYILYTGGTTGMPKGVMWRQedifrmlmggadFGTGEFTPSEDAHkaAAAAAGTVMFPAPPLMHGTGSWTAFGGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 236 MVGACHVLL-PKFDAKTALQVMEQNHITC-FITVPAMMADLIRVNRTTkNGAENRGVRKILNGGGSLSSELLKEAVNIFP 313
Cdd:cd05924 81 LGGQTVVLPdDRFDPEEVWRTIEKHKVTSmTIVGDAMARPLIDALRDA-GPYDLSSLFAISSGGALLSPEVKQGLLELVP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 314 CARILSAYGMTEACSSLTFMT-LHDPTQESFKVTYPllnqpkqGTCVGKPAPHIelmvkLDEDSSRVGKILTRGpHTMLR 392
Cdd:cd05924 160 NITLVDAFGSSETGFTGSGHSaGSGPETGPFTRANP-------DTVVLDDDGRV-----VPPGSGGVGWIARRG-HIPLG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 393 YWGHqvAQENVETSESRSNEAWLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGVIDT 472
Cdd:cd05924 227 YYGD--EAKTAETFPEVDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDE 304
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22329863 473 RLGEMVVACVRLQEkwiwsdvenrkgSFQLSSETLKHHCRTQnLTGFKIPKRFVRwekqfpltttgkvkRDEVRR 547
Cdd:cd05924 305 RWGQEVVAVVQLRE------------GAGVDLEELREHCRTR-IARYKLPKQVVF--------------VDEIER 352
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
150-546 |
1.56e-41 |
|
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: 154.80 E-value: 1.56e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 150 LTTEMLKQR--TLVPSLATYAwaSDDAVVICFTSGTTGRPKGVTISHLAFITQSLAKIAIAGYGEDDVYLHTSPLVHIGG 227
Cdd:cd05972 59 LGPKDIEYRleAAGAKAIVTD--AEDPALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGLRPDDIHWNIADPGWAKG 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 228 LSSA-MAMLMVGACHVL--LPKFDAKTALQVMEQNHITCFITVPAMMADLIRVNrttkngaENRGVRKILNGGGSLSSEL 304
Cdd:cd05972 137 AWSSfFGPWLLGATVFVyeGPRFDAERILELLERYGVTSFCGPPTAYRMLIKQD-------LSSYKFSHLRLVVSAGEPL 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 305 LKEAVNIFPCA---RILSAYGMTEacsslTFMTLHD-PTQEsfkvtypllnqPKQGTcVGKPAPHIELMVkLDEDS---- 376
Cdd:cd05972 210 NPEVIEWWRAAtglPIRDGYGQTE-----TGLTVGNfPDMP-----------VKPGS-MGRPTPGYDVAI-IDDDGrelp 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 377 -SRVGKI-LTRGPHTMLR-YWGhqvaqeNVETSESRSNEAWLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEA 453
Cdd:cd05972 272 pGEEGDIaIKLPPPGLFLgYVG------DPEKTEASIRGDYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVES 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 454 VLVEHPGIVSAVVIGVIDTRLGEMVVACVRLQEKWIWSDvenrkgsfQLSSEtLKHHCRTQnLTGFKIPKR--FVrweKQ 531
Cdd:cd05972 346 ALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYEPSE--------ELAEE-LQGHVKKV-LAPYKYPREieFV---EE 412
|
410
....*....|....*
gi 22329863 532 FPLTTTGKVKRDEVR 546
Cdd:cd05972 413 LPKTISGKIRRVELR 427
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
13-546 |
5.21e-41 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 156.33 E-value: 5.21e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 13 LTRLASVKRNAVVTVYGNRKRTGREFVDGVLSLAAGLIRLGLRNGDVVSIAAFNSDLFLEWLLAVALVGGVVAPLNYRWS 92
Cdd:PLN03102 20 LKRASECYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 93 LKEAKMAMLLVEPVLLVTD---ETCVSWCIDVQNGDIPSLKWRVLM----ESTSTDFANELNQflttEMLKQR-TLVPSL 164
Cdd:PLN03102 100 ATSIAAILRHAKPKILFVDrsfEPLAREVLHLLSSEDSNLNLPVIFiheiDFPKRPSSEELDY----ECLIQRgEPTPSL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 165 ATYAWA---SDDAVVICFTSGTTGRPKGVTISHLAFITQSLAKIAIAGYGEDDVYLHTSPLVHIGGLSSAMAMLMVGACH 241
Cdd:PLN03102 176 VARMFRiqdEHDPISLNYTSGTTADPKGVVISHRGAYLSTLSAIIGWEMGTCPVYLWTLPMFHCNGWTFTWGTAARGGTS 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 242 VLLPKFDAKTALQVMEQNHITCFITVPAMMADLIRVNRTtkNGAENRGVRKILNGGGSLSSELLKEAVNI-FpcaRILSA 320
Cdd:PLN03102 256 VCMRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLKGNSL--DLSPRSGPVHVLTGGSPPPAALVKKVQRLgF---QVMHA 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 321 YGMTEACSSLTFMTLHD-----PTQESFKVtypllnQPKQG----TCVGKPAPHIELMVKLDEDSSRVGKILTRGPHTML 391
Cdd:PLN03102 331 YGLTEATGPVLFCEWQDewnrlPENQQMEL------KARQGvsilGLADVDVKNKETQESVPRDGKTMGEIVIKGSSIMK 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 392 RYWGHQVAqenveTSESRSNeAWLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGVID 471
Cdd:PLN03102 405 GYLKNPKA-----TSEAFKH-GWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPH 478
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22329863 472 TRLGEMVVACVRLQEKwiWSDVENRKGSFQLSSETLKHHCRtQNLTGFKIPKRFVRWEkQFPLTTTGKVKRDEVR 546
Cdd:PLN03102 479 PTWGETPCAFVVLEKG--ETTKEDRVDKLVTRERDLIEYCR-ENLPHFMCPRKVVFLQ-ELPKNGNGKILKPKLR 549
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
172-546 |
5.22e-41 |
|
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: 154.14 E-value: 5.22e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 172 DDAVVICFTSGTTGRPKGVTISHLAFITQSLAKIAIAGYGEDDVYLHTSPLVHIGGLSSAMAMLMVGACHVLLPKF--DA 249
Cdd:cd05922 117 EDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADDRALTVLPLSYDYGLSVLNTHLLRGATLVLTNDGvlDD 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 250 KTALQVMEQNhITCFITVPAMMADLIRVNRTTkngAENRGVRKILNGGGSLSSELLKEAVNIFPCARILSAYGMTEACSS 329
Cdd:cd05922 197 AFWEDLREHG-ATGLAGVPSTYAMLTRLGFDP---AKLPSLRYLTQAGGRLPQETIARLRELLPGAQVYVMYGQTEATRR 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 330 LTFMtlhDPTQEsfkvtyplLNQPkqgTCVGKPAPHIELMVkLDEDSSR-----VGKILTRGPHTMLRYWGhqvaQENVE 404
Cdd:cd05922 273 MTYL---PPERI--------LEKP---GSIGLAIPGGEFEI-LDDDGTPtppgePGEIVHRGPNVMKGYWN----DPPYR 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 405 TSESRSNEAwLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGVIDTrLGEMVVACVRL 484
Cdd:cd05922 334 RKEGRGGGV-LHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDP-LGEKLALFVTA 411
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22329863 485 QEKWIWSDVenrkgsfqlssetlKHHCRTQnLTGFKIPKRfVRWEKQFPLTTTGKVKRDEVR 546
Cdd:cd05922 412 PDKIDPKDV--------------LRSLAER-LPPYKVPAT-VRVVDELPLTASGKVDYAALR 457
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
36-466 |
5.36e-41 |
|
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: 152.80 E-value: 5.36e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 36 REFVDGVLSLAAGLI-RLGLRNGDVVSIAAFNSDLFLEWLLAVALVGGVVAPLNyrWSLKEAKMAMLL--VEPVLLVTDE 112
Cdd:TIGR01733 3 RELDERANRLARHLRaAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLD--PAYPAERLAFILedAGARLLLTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 113 TCVSwcidvqngdipslkwrVLMESTSTDFANELNQFLTTEmlkQRTLVPSLATYAWASDDAVVIcFTSGTTGRPKGVTI 192
Cdd:TIGR01733 81 ALAS----------------RLAGLVLPVILLDPLELAALD---DAPAPPPPDAPSGPDDLAYVI-YTSGSTGRPKGVVV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 193 SHLAFITQSLAKIAIAGYGEDDVYLHTSPLVHIGGLSSAMAMLMVGACHVLLP----KFDAKTALQVMEQNHITCFITVP 268
Cdd:TIGR01733 141 THRSLVNLLAWLARRYGLDPDDRVLQFASLSFDASVEEIFGALLAGATLVVPPedeeRDDAALLAALIAEHPVTVLNLTP 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 269 AMMADLIRVNRTtkngaENRGVRKILNGGGSLSSELLKEAVNIFPCARILSAYGMTEACSSLTfMTLHDPTQESFKVTYP 348
Cdd:TIGR01733 221 SLLALLAAALPP-----ALASLRLVILGGEALTPALVDRWRARGPGARLINLYGPTETTVWST-ATLVDPDDAPRESPVP 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 349 llnqpkqgtcVGKPAPHIELMVkLDEDSSRV-----GKILTRGPHTMLRYWGH--QVAQENVE-TSESRSNEAWLDTGDI 420
Cdd:TIGR01733 295 ----------IGRPLANTRLYV-LDDDLRPVpvgvvGELYIGGPGVARGYLNRpeLTAERFVPdPFAGGDGARLYRTGDL 363
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 22329863 421 GAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVV 466
Cdd:TIGR01733 364 VRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
2-551 |
8.55e-41 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 155.10 E-value: 8.55e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 2 ANHsrphicQCLTRLASVKRNAVV------TVYGNRKRTGREFVDGVLSLAAGLIRLGLRNGDVVSIAAFNSDLFLEWLL 75
Cdd:PRK08162 13 ANY------VPLTPLSFLERAAEVypdrpaVIHGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 76 AVALVGGVVAPLNYRwsLKEAKMAMLL--VEPVLLVTDE---TCVSWCIDVQNGDIPSLKWRVLMESTSTDFANELN--Q 148
Cdd:PRK08162 87 GVPMAGAVLNTLNTR--LDAASIAFMLrhGEAKVLIVDTefaEVAREALALLPGPKPLVIDVDDPEYPGGRFIGALDyeA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 149 FLTTemlkqrtlvpSLATYAWA--SD--DAVVICFTSGTTGRPKGVTISHLAFITQSLAKIAIAGYGEDDVYLHTSPLVH 224
Cdd:PRK08162 165 FLAS----------GDPDFAWTlpADewDAIALNYTSGTTGNPKGVVYHHRGAYLNALSNILAWGMPKHPVYLWTLPMFH 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 225 IGGLSSAMAMLMVGACHVLLPKFDAKTALQVMEQNHITCFITVPAMMADLIRVNRTTKNGAENRgVRKILNGGGSLSSEL 304
Cdd:PRK08162 235 CNGWCFPWTVAARAGTNVCLRKVDPKLIFDLIREHGVTHYCGAPIVLSALINAPAEWRAGIDHP-VHAMVAGAAPPAAVI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 305 LK-EAVNIfpcaRILSAYGMTEACSSLT-------FMTLHDPTQESFK----VTYPLLnqpkQGTCVGKPaphiELMVKL 372
Cdd:PRK08162 314 AKmEEIGF----DLTHVYGLTETYGPATvcawqpeWDALPLDERAQLKarqgVRYPLQ----EGVTVLDP----DTMQPV 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 373 DEDSSRVGKILTRGPHTMLRYWghqvaqENVETSESRSNEAWLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVE 452
Cdd:PRK08162 382 PADGETIGEIMFRGNIVMKGYL------KNPKATEEAFAGGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVE 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 453 AVLVEHPGIVSAVVIGVIDTRLGEMVVACVRLQEkwiwsdvenrkgSFQLSSETLKHHCRtQNLTGFKIPKRFVRWEkqF 532
Cdd:PRK08162 456 DVLYRHPAVLVAAVVAKPDPKWGEVPCAFVELKD------------GASATEEEIIAHCR-EHLAGFKVPKAVVFGE--L 520
|
570
....*....|....*....
gi 22329863 533 PLTTTGKVKRDEVRRQVLS 551
Cdd:PRK08162 521 PKTSTGKIQKFVLREQAKS 539
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
23-542 |
3.49e-40 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 152.75 E-value: 3.49e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 23 AVVTVYGNRKRTGREFVDGVLSLAAGLIRLGLRNGDVVSIAAFNSDLFLEWLLAVALVGGVVAPLNyrWSLKEAKMAMLL 102
Cdd:PRK08276 2 AVIMAPSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPIN--WHLTAAEIAYIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 103 VEP---VLLVT---DETCVSWCIDVQNGdipsLKWRVLMESTST---DFANELNQFLTTEMLKQrtlvpslatyaWASDD 173
Cdd:PRK08276 80 DDSgakVLIVSaalADTAAELAAELPAG----VPLLLVVAGPVPgfrSYEEALAAQPDTPIADE-----------TAGAD 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 174 AVvicFTSGTTGRPKGV--TISHLAFITQSLAKIAIAGY----GEDDVYLHTSPLVHIGGLSSAMAMLMVGACHVLLPKF 247
Cdd:PRK08276 145 ML---YSSGTTGRPKGIkrPLPGLDPDEAPGMMLALLGFgmygGPDSVYLSPAPLYHTAPLRFGMSALALGGTVVVMEKF 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 248 DAKTALQVMEQNHITCFITVPAMMADLIRVNRTTKNGAENRGVRKILNGGGSLSSELLKEAVNIF-PCarILSAYGMTEA 326
Cdd:PRK08276 222 DAEEALALIERYRVTHSQLVPTMFVRMLKLPEEVRARYDVSSLRVAIHAAAPCPVEVKRAMIDWWgPI--IHEYYASSEG 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 327 CSSlTFMTLHDptqesfkvtypLLNQPkqGTcVGKPAP---HIelmvkLDEDSSR-----VGKILTRGPHTMLRYWGHQV 398
Cdd:PRK08276 300 GGV-TVITSED-----------WLAHP--GS-VGKAVLgevRI-----LDEDGNElppgeIGTVYFEMDGYPFEYHNDPE 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 399 AqenveTSESRSNEAWLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGVIDTRLGEMV 478
Cdd:PRK08276 360 K-----TAAARNPHGWVTVGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERV 434
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22329863 479 VACVRLQEkwiWSDvenrkGSFQLSSEtLKHHCRtQNLTGFKIPKRFVrWEKQFPLTTTGK-VKR 542
Cdd:PRK08276 435 KAVVQPAD---GAD-----AGDALAAE-LIAWLR-GRLAHYKCPRSID-FEDELPRTPTGKlYKR 488
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
13-542 |
3.54e-40 |
|
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: 152.10 E-value: 3.54e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 13 LTRLASVKRNAVVTVYGNRKRTGREFVDGVLSLAAGLIRLGLRNGDVVSIAAFNSDLFLEWLLAVALVGgvVAPLNYRWS 92
Cdd:cd05920 21 LARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLG--AVPVLALPS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 93 LKEAKMAML--LVEPVLLVTDETcvswcidvqngdipslkwrvlmeststdFANELNQFLTTEMlkqrtlvpslatyawA 170
Cdd:cd05920 99 HRRSELSAFcaHAEAVAYIVPDR----------------------------HAGFDHRALAREL---------------A 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 171 SDDAVVICF--TSGTTGRPKGVTISHLAFITQSLAKIAIAGYGEDDVYLHTSPLVHIGGLSS--AMAMLMVGACHVLLPK 246
Cdd:cd05920 136 ESIPEVALFllSGGTTGTPKLIPRTHNDYAYNVRASAEVCGLDQDTVYLAVLPAAHNFPLACpgVLGTLLAGGRVVLAPD 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 247 FDAKTALQVMEQNHITCFITVPAMMadLIRVNRTTKNGAENRGVRKILNGGGSLSSELLKEAVNIFPCaRILSAYGMTEA 326
Cdd:cd05920 216 PSPDAAFPLIEREGVTVTALVPALV--SLWLDAAASRRADLSSLRLLQVGGARLSPALARRVPPVLGC-TLQQVFGMAEG 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 327 CssLTFMTLHDP------TQesfkvtypllnqpkqgtcvGKPA-PHIELMVkLDEDSSRV-----GKILTRGPHTMLRYW 394
Cdd:cd05920 293 L--LNYTRLDDPdeviihTQ-------------------GRPMsPDDEIRV-VDEEGNPVppgeeGELLTRGPYTIRGYY 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 395 ghQVAQENvetSESRSNEAWLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGVIDTRL 474
Cdd:cd05920 351 --RAPEHN---ARAFTPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELL 425
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22329863 475 GEMVVACVRLQEKwiwsdvenrkgsfQLSSETLKHHCRTQNLTGFKIPKRFVRWEkQFPLTTTGKVKR 542
Cdd:cd05920 426 GERSCAFVVLRDP-------------PPSAAQLRRFLRERGLAAYKLPDRIEFVD-SLPLTAVGKIDK 479
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
21-542 |
1.23e-39 |
|
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: 150.09 E-value: 1.23e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 21 RNAVVTVYGNRKRTGREFVDGVLSLAAGLIRLGLRNGDVVSIAAFNSDLFLEWLLAVALVGGVVAPLNYRWSLKEAKMAM 100
Cdd:cd05945 5 PDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERIREIL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 101 LLVEPVLLVTDEtcvswcidvqngdipslkwrvlmeststdfanelnqflttemlkqrtlvpslatyawasDDAVVICFT 180
Cdd:cd05945 85 DAAKPALLIADG-----------------------------------------------------------DDNAYIIFT 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 181 SGTTGRPKGVTISH---LAFITQSLAKIAIagyGEDDVYLHTSPlvhiggLS---SAMAM---LMVGACHVLLPKFDAKT 251
Cdd:cd05945 106 SGSTGRPKGVQISHdnlVSFTNWMLSDFPL---GPGDVFLNQAP------FSfdlSVMDLypaLASGATLVPVPRDATAD 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 252 ALQVMEQNH---ITCFITVPAMMADLIRvnRTTKNGAENRGVRKILNGGGSLSSELLKEAVNIFPCARILSAYGMTEACS 328
Cdd:cd05945 177 PKQLFRFLAehgITVWVSTPSFAAMCLL--SPTFTPESLPSLRHFLFCGEVLPHKTARALQQRFPDARIYNTYGPTEATV 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 329 SLTFmtlHDPTQESFKVTYPLlnqPkqgtcVGKPAPHIELMVkLDEDSSRV-----GKILTRGPHTMLRYWGhqVAQENV 403
Cdd:cd05945 255 AVTY---IEVTPEVLDGYDRL---P-----IGYAKPGAKLVI-LDEDGRPVppgekGELVISGPSVSKGYLN--NPEKTA 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 404 ETSESRSNEAWLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGVIDTRLGEMVVACVR 483
Cdd:cd05945 321 AAFFPDEGQRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVV 400
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 22329863 484 LQEkwiwsdvenrKGSFQLSSEtLKHHCRtQNLTGFKIPKRFVrWEKQFPLTTTGKVKR 542
Cdd:cd05945 401 PKP----------GAEAGLTKA-IKAELA-ERLPPYMIPRRFV-YLDELPLNANGKIDR 446
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
170-547 |
4.30e-39 |
|
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: 148.35 E-value: 4.30e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 170 ASDDAVVICFTSGTTGRPKG------VTISHLA--FITQSLAKiaiagyGEDDVYLHTSPLVHIGGLSSamamLMVGACH 241
Cdd:cd05971 86 GSDDPALIIYTSGTTGPPKGalhahrVLLGHLPgvQFPFNLFP------RDGDLYWTPADWAWIGGLLD----VLLPSLY 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 242 VLLP-------KFDAKTALQVMEQNHIT-CFItvPAMMADLIRVNRTTKNGAENRgVRKILNGGGSLSSELL---KEAVN 310
Cdd:cd05971 156 FGVPvlahrmtKFDPKAALDLMSRYGVTtAFL--PPTALKMMRQQGEQLKHAQVK-LRAIATGGESLGEELLgwaREQFG 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 311 IfpcaRILSAYGMTEA------CSSLtfmtlhdptqesfkvtYPllnqPKQGTcVGKPAP-HIelmVKLDEDSSR----- 378
Cdd:cd05971 233 V----EVNEFYGQTECnlvignCSAL----------------FP----IKPGS-MGKPIPgHR---VAIVDDNGTplppg 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 379 -VGKILTRGPH--TMLRYWghqvaqENVETSESRSNEAWLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVL 455
Cdd:cd05971 285 eVGEIAVELPDpvAFLGYW------NNPSATEKKMAGDWLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECL 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 456 VEHPGIVSAVVIGVIDTRLGEMVVACVRLQEKWIWSDvenrkgsfQLSSEtLKHHCRTQnLTGFKIPkRFVRWEKQFPLT 535
Cdd:cd05971 359 LKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGETPSD--------ALARE-IQELVKTR-LAAHEYP-REIEFVNELPRT 427
|
410
....*....|..
gi 22329863 536 TTGKVKRDEVRR 547
Cdd:cd05971 428 ATGKIRRRELRA 439
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
13-548 |
8.36e-39 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 149.52 E-value: 8.36e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 13 LTRLASVKRNAVVTVYGNRKRTGREFVDGVLSLAAGLIRLGLRNGDVVSIAAFNSDLFLEWLLAVALVGGVVAPLN--YR 90
Cdd:PRK06155 27 LARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINtaLR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 91 -----WSLKEAKMAMLLVEPVLLVTDETCVS--------WCIDVQNGDIPSLKWRvlmeststdfanelnqflTTEMlkq 157
Cdd:PRK06155 107 gpqleHILRNSGARLLVVEAALLAALEAADPgdlplpavWLLDAPASVSVPAGWS------------------TAPL--- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 158 rtlvPSLATYAWASD----DAVVICFTSGTTGRPKGVTISHLAFITQSLAKIAIAGYGEDDVYLHTSPLVHIGGLSSAMA 233
Cdd:PRK06155 166 ----PPLDAPAPAAAvqpgDTAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADDVLYTTLPLFHTNALNAFFQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 234 MLMVGACHVLLPKFDAKTALQVMEQNHITCFITVPAMMAdlIRVNRTTknGAENRG--VRKILNGGGSlsSELLKEAVNI 311
Cdd:PRK06155 242 ALLAGATYVLEPRFSASGFWPAVRRHGATVTYLLGAMVS--ILLSQPA--RESDRAhrVRVALGPGVP--AALHAAFRER 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 312 FPCArILSAYGMTEacssltfmtlhdpTQESFKVTYPllnQPKQGTcVGKPAPHIELMVkLDEDSSRV-----GKILTRG 386
Cdd:PRK06155 316 FGVD-LLDGYGSTE-------------TNFVIAVTHG---SQRPGS-MGRLAPGFEARV-VDEHDQELpdgepGELLLRA 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 387 --PHTMLR-YWGhqVAQENVETSesrsNEAWLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVS 463
Cdd:PRK06155 377 dePFAFATgYFG--MPEKTVEAW----RNLWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAA 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 464 AVVIGViDTRLGEMVVACVrlqekwiwsdVENRKGSfQLSSETLKHHCRTQnLTGFKIPkRFVRWEKQFPLTTTGKVKRD 543
Cdd:PRK06155 451 AAVFPV-PSELGEDEVMAA----------VVLRDGT-ALEPVALVRHCEPR-LAYFAVP-RYVEFVAALPKTENGKVQKF 516
|
....*
gi 22329863 544 EVRRQ 548
Cdd:PRK06155 517 VLREQ 521
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
45-544 |
1.52e-38 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 149.04 E-value: 1.52e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 45 LAAGLIRLGLRNGDVVSIAAFNSDLFLEWLLAVALVGGVVAPLN-------YRWSLKEAKMAMLLVEPVLL-----VTDE 112
Cdd:PRK06178 71 FAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSplfreheLSYELNDAGAEVLLALDQLApvveqVRAE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 113 TCVSWCIDVQNGDI----PSLKWRVLMESTSTDFANELNQFLTTEMLKQRTLVPSLATyawasDDAVVICFTSGTTGRPK 188
Cdd:PRK06178 151 TSLRHVIVTSLADVlpaePTLPLPDSLRAPRLAAAGAIDLLPALRACTAPVPLPPPAL-----DALAALNYTGGTTGMPK 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 189 GV--TISHLAFITQSLAKIAIAGyGEDDVYLHTSPLVHIGGLSSAMAM-LMVGACHVLLPKFDAKTALQVMEQNHIT-CF 264
Cdd:PRK06178 226 GCehTQRDMVYTAAAAYAVAVVG-GEDSVFLSFLPEFWIAGENFGLLFpLFSGATLVLLARWDAVAFMAAVERYRVTrTV 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 265 ITV---------PAMMA-DLirvnRTTKNGAENRGVRKI----------LNGGgslsseLLKEAvnifpcarilsAYGMT 324
Cdd:PRK06178 305 MLVdnavelmdhPRFAEyDL----SSLRQVRVVSFVKKLnpdyrqrwraLTGS------VLAEA-----------AWGMT 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 325 EACSSLTFMTlhdptqeSFKV-TYPLLNQPkqgTCVGKPAPHIELMVkLDEDSSRV------GKILTRGPHTMLRYWGHQ 397
Cdd:PRK06178 364 ETHTCDTFTA-------GFQDdDFDLLSQP---VFVGLPVPGTEFKI-CDFETGELlplgaeGEIVVRTPSLLKGYWNKP 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 398 VAqenveTSESRsNEAWLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGVIDTRLGEM 477
Cdd:PRK06178 433 EA-----TAEAL-RDGWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQV 506
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22329863 478 VVACVRLqekwiwsdvenrKGSFQLSSETLKHHCRtQNLTGFKIPKrfVRWEKQFPLTTTGKVKRDE 544
Cdd:PRK06178 507 PVAFVQL------------KPGADLTAAALQAWCR-ENMAVYKVPE--IRIVDALPMTATGKVRKQD 558
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
150-542 |
1.76e-38 |
|
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: 146.88 E-value: 1.76e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 150 LTTEMLKQRTlvpslatyawASDDAVVICFTSGTTGRPKGVTISHLAFITQSLAKIAIAGYGEDDVYLHTSPLVHIGGLS 229
Cdd:cd05969 77 ITTEELYERT----------DPEDPTLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLDLHPDDIYWCTADPGWVTGTV 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 230 SAM-AMLMVGACHVLLP-KFDAKTALQVMEQNHITCFITVPAMMADLIRVNRTTKNGAENRGVRKILNGGGSLSSELLKE 307
Cdd:cd05969 147 YGIwAPWLNGVTNVVYEgRFDAESWYGIIERVKVTVWYTAPTAIRMLMKEGDELARKYDLSSLRFIHSVGEPLNPEAIRW 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 308 AVNIFPcARILSAYGMTEACSSLTfmtlhdptqesfkVTYPllNQPKQGTCVGKPAPHIELMVkLDEDSS-----RVGKI 382
Cdd:cd05969 227 GMEVFG-VPIHDTWWQTETGSIMI-------------ANYP--CMPIKPGSMGKPLPGVKAAV-VDENGNelppgTKGIL 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 383 -LTRGPHTMLR-YWGhqvaqeNVETSESRSNEAWLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPG 460
Cdd:cd05969 290 aLKPGWPSMFRgIWN------DEERYKNSFIDGWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPA 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 461 IVSAVVIGVIDTRLGEMVVACVRLQEKWIWSDvenrkgsfQLSSETLKHhcRTQNLTGFKIPkRFVRWEKQFPLTTTGKV 540
Cdd:cd05969 364 VAEAGVIGKPDPLRGEIIKAFISLKEGFEPSD--------ELKEEIINF--VRQKLGAHVAP-REIEFVDNLPKTRSGKI 432
|
..
gi 22329863 541 KR 542
Cdd:cd05969 433 MR 434
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
34-542 |
3.48e-38 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 147.15 E-value: 3.48e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 34 TGREFVDGVLSLAAGLIRLGLRNGDVVSIAAFNSDLFLEWLLAVALVGGVVAPLNyrWSLKEAKMAMLLV--EPVLLVTD 111
Cdd:PRK13391 26 TYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVN--SHLTPAEAAYIVDdsGARALITS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 112 ETCVSWCIDVQnGDIPSLKWRVLMESTST-----DFANELNQFLTTEMLKQRTLVPSLatyawasddavvicFTSGTTGR 186
Cdd:PRK13391 104 AAKLDVARALL-KQCPGVRHRLVLDGDGElegfvGYAEAVAGLPATPIADESLGTDML--------------YSSGTTGR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 187 PKGV-------TISHLAFITQSLAKIAiaGYGEDDVYLHTSPLVHIGGLSSAMAMLMVGACHVLLPKFDAKTALQVMEQN 259
Cdd:PRK13391 169 PKGIkrplpeqPPDTPLPLTAFLQRLW--GFRSDMVYLSPAPLYHSAPQRAVMLVIRLGGTVIVMEHFDAEQYLALIEEY 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 260 HITCFITVPAMMADLIRVNRTTKNGAENRGVRKILNGGGSLSSELlKEAVNIFPCARILSAYGMTEAcSSLTFMTLHDpt 339
Cdd:PRK13391 247 GVTHTQLVPTMFSRMLKLPEEVRDKYDLSSLEVAIHAAAPCPPQV-KEQMIDWWGPIIHEYYAATEG-LGFTACDSEE-- 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 340 qesfkvtypLLNQPkqGTcVGKP---APHIelmvkLDEDssrvGKILTRG-PHTMlrYW--GHQVAQEN--VETSESRSN 411
Cdd:PRK13391 323 ---------WLAHP--GT-VGRAmfgDLHI-----LDDD----GAELPPGePGTI--WFegGRPFEYLNdpAKTAEARHP 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 412 EA-WLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGVIDTRLGEMVVACVRLqekwiw 490
Cdd:PRK13391 380 DGtWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQP------ 453
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 22329863 491 sdVENRKGSFQLSSETLKhHCRtQNLTGFKIPkRFVRWEKQFPLTTTGK-VKR 542
Cdd:PRK13391 454 --VDGVDPGPALAAELIA-FCR-QRLSRQKCP-RSIDFEDELPRLPTGKlYKR 501
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
34-542 |
9.68e-38 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 146.72 E-value: 9.68e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 34 TGREFVDGVLSLAAGLIRLGLRNGDVVSIAAFNSDLFLEWLLAVALVGGVVAPLNYRWSLKEAK-----------MAMLL 102
Cdd:PRK06710 51 TFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEyqlhdsgakviLCLDL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 103 VEP-VLLVTDETCVSWCIDVQNGDIPSLKWRVLMESTSTDFANELNQFLTTEMLK-----QRTLVPSLATYAWASDDAVV 176
Cdd:PRK06710 131 VFPrVTNVQSATKIEHVIVTRIADFLPFPKNLLYPFVQKKQSNLVVKVSESETIHlwnsvEKEVNTGVEVPCDPENDLAL 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 177 ICFTSGTTGRPKGVTISHLAFITQSLAKI-----AIAGygeDDVYLHTSPLVHIGGLSSAMAM-LMVGACHVLLPKFDAK 250
Cdd:PRK06710 211 LQYTGGTTGFPKGVMLTHKNLVSNTLMGVqwlynCKEG---EEVVLGVLPFFHVYGMTAVMNLsIMQGYKMVLIPKFDMK 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 251 TALQVMEQNHITCFITVPAMMADLIrvNRTTKNGAENRGVRKILNGGGSLSSELlKEAVNIFPCARILSAYGMTEAcssl 330
Cdd:PRK06710 288 MVFEAIKKHKVTLFPGAPTIYIALL--NSPLLKEYDISSIRACISGSAPLPVEV-QEKFETVTGGKLVEGYGLTES---- 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 331 tfmtlhDPTQESfkvtyPLLNQPKQGTCVGKPAPHIELMVKLDEDSS-----RVGKILTRGPHTMLRYWGHQvaqenvET 405
Cdd:PRK06710 361 ------SPVTHS-----NFLWEKRVPGSIGVPWPDTEAMIMSLETGEalppgEIGEIVVKGPQIMKGYWNKP------EE 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 406 SESRSNEAWLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGVIDTRLGEMVVACVRLQ 485
Cdd:PRK06710 424 TAAVLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVLK 503
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 22329863 486 EKWIWSDvenrkgsfqlssETLKHHCRtQNLTGFKIPKRFvRWEKQFPLTTTGKVKR 542
Cdd:PRK06710 504 EGTECSE------------EELNQFAR-KYLAAYKVPKVY-EFRDELPKTTVGKILR 546
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
15-546 |
1.07e-37 |
|
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: 145.59 E-value: 1.07e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 15 RLASVKRNAVVTVYGNRKRTGREFVDGVLSLAAGLIRLGLRNGDVVSIAAFNSDLFLEWLLAVALVGGVVAPLN------ 88
Cdd:cd05959 12 NLNEGRGDKTAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNtlltpd 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 89 -YRWSLKEAKMAMLLVEPVLLVTDEtcvswciDVQNGDIPSLkwRVLMesTSTDFANELNQFLTTEMLkqRTLVPSLATY 167
Cdd:cd05959 92 dYAYYLEDSRARVVVVSGELAPVLA-------AALTKSEHTL--VVLI--VSGGAGPEAGALLLAELV--AAEAEQLKPA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 168 AWASDDAVVICFTSGTTGRPKGVTISH--LAFITQSLAKiAIAGYGEDDVYLHTSPLVHIGGLSSAMAMLM-VGACHVLL 244
Cdd:cd05959 159 ATHADDPAFWLYSSGSTGRPKGVVHLHadIYWTAELYAR-NVLGIREDDVCFSAAKLFFAYGLGNSLTFPLsVGATTVLM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 245 PKF-DAKTALQVMEQNHITCFITVPAMMADLIRVNRTTKNGAENrgVRKILNGGGSLSSELLKEAVNIFPCaRILSAYGM 323
Cdd:cd05959 238 PERpTPAAVFKRIRRYRPTVFFGVPTLYAAMLAAPNLPSRDLSS--LRLCVSAGEALPAEVGERWKARFGL-DILDGIGS 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 324 TEAcssltfmtLHdptqesfkvTYpLLNQP--KQGTCVGKPAPHIElmVKL-DEDSSRV-----GKILTRGPHTMLRYWG 395
Cdd:cd05959 315 TEM--------LH---------IF-LSNRPgrVRYGTTGKPVPGYE--VELrDEDGGDVadgepGELYVRGPSSATMYWN 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 396 hqvaqeNVETSESRSNEAWLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGVIDTRLG 475
Cdd:cd05959 375 ------NRDKTRDTFQGEWTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGL 448
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22329863 476 EMVVACVRLQEKWIWSDVenrkgsfqlSSETLKHHCRtQNLTGFKIPkRFVRWEKQFPLTTTGKVKRDEVR 546
Cdd:cd05959 449 TKPKAFVVLRPGYEDSEA---------LEEELKEFVK-DRLAPYKYP-RWIVFVDELPKTATGKIQRFKLR 508
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
28-540 |
4.08e-37 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 144.72 E-value: 4.08e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 28 YGNRKrTGREFVDGVLSLAAGLIR-LGLRNGDVVSIAAFNSDLFLEWLLAVALVGGVVAPLNYRWSLKE---------AK 97
Cdd:PRK08314 32 YGRAI-SYRELLEEAERLAGYLQQeCGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEElahyvtdsgAR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 98 MAML---LVEPVLLVTDETCVSWCIDVQNGDI----PSLKWRVLMESTSTDFANELNQFLT-TEMLKQRTLVPSLATyaw 169
Cdd:PRK08314 111 VAIVgseLAPKVAPAVGNLRLRHVIVAQYSDYlpaePEIAVPAWLRAEPPLQALAPGGVVAwKEALAAGLAPPPHTA--- 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 170 ASDDAVVICFTSGTTGRPKGVTISHLAFITQSLAKIAIAGYGEDDVYLHTSPLVHIGGLSSAM-AMLMVGACHVLLPKFD 248
Cdd:PRK08314 188 GPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVLPLFHVTGMVHSMnAPIYAGATVVLMPRWD 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 249 AKTALQVMEQNHITCFITVPAMMADLIRVNRTTKngAENRGVRKILNGGGSLS---SELLKEAVNIfpcaRILSAYGMTE 325
Cdd:PRK08314 268 REAAARLIERYRVTHWTNIPTMVVDFLASPGLAE--RDLSSLRYIGGGGAAMPeavAERLKELTGL----DYVEGYGLTE 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 326 ACSSltfmTLHDPtqesfkvtyplLNQPKQGtCVGKPAPHIELMVkLDEDS------SRVGKILTRGPHTMLRYWGHQva 399
Cdd:PRK08314 342 TMAQ----THSNP-----------PDRPKLQ-CLGIPTFGVDARV-IDPETleelppGEVGEIVVHGPQVFKGYWNRP-- 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 400 QENVETSESRSNEAWLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGVIDTRLGEMVV 479
Cdd:PRK08314 403 EATAEAFIEIDGKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPDPRRGETVK 482
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22329863 480 ACVRLQEKWiwsdvenrKGsfQLSSETLKHHCRtQNLTGFKIPkRFVRWEKQFPLTTTGKV 540
Cdd:PRK08314 483 AVVVLRPEA--------RG--KTTEEEIIAWAR-EHMAAYKYP-RIVEFVDSLPKSGSGKI 531
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
12-549 |
7.26e-37 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 143.97 E-value: 7.26e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 12 CLTRLASVKRNAVVtVYGNrkrTGREFVDG---VLS--LAAGLIRLGLRNGDVVSIAAFNSDLFLEWLLAVALVGGVVAP 86
Cdd:PLN02246 29 CFERLSEFSDRPCL-IDGA---TGRVYTYAdveLLSrrVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 87 LNYRWSLKE-AKMA------MLLVEPVL------LVTDETCVSWCIDvQNGDIpSLKWRVLMESTSTDfanelnqfltte 153
Cdd:PLN02246 105 ANPFYTPAEiAKQAkasgakLIITQSCYvdklkgLAEDDGVTVVTID-DPPEG-CLHFSELTQADENE------------ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 154 mlkqrtlvpsLATYAWASDDAVVICFTSGTTGRPKGVTISHLAFITqSLAKiAIAG------YGEDDVYLHTSPLVHIGG 227
Cdd:PLN02246 171 ----------LPEVEISPDDVVALPYSSGTTGLPKGVMLTHKGLVT-SVAQ-QVDGenpnlyFHSDDVILCVLPMFHIYS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 228 LSSAM-AMLMVGACHVLLPKFDAKTALQVMEQNHITCFITVPAMMADLIRVNRTTKNGAENrgVRKILNGGGSLSSELlK 306
Cdd:PLN02246 239 LNSVLlCGLRVGAAILIMPKFEIGALLELIQRHKVTIAPFVPPIVLAIAKSPVVEKYDLSS--IRMVLSGAAPLGKEL-E 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 307 EAVNI-FPCARILSAYGMTEA----CSSLTFmtlhdpTQESFKVtypllnqpKQGTCvGKPAPHIELMVkLDEDS----- 376
Cdd:PLN02246 316 DAFRAkLPNAVLGQGYGMTEAgpvlAMCLAF------AKEPFPV--------KSGSC-GTVVRNAELKI-VDPETgaslp 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 377 -SRVGKILTRGPHTMLRYWGhqvaqeNVE-TSESRSNEAWLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAV 454
Cdd:PLN02246 380 rNQPGEICIRGPQIMKGYLN------DPEaTANTIDKDGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEAL 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 455 LVEHPGIVSAVVIGVIDTRLGEMVVACVRlqekwiwsdvenRKGSFQLSSETLKHHCRTQNLTGFKIPKRFvrWEKQFPL 534
Cdd:PLN02246 454 LISHPSIADAAVVPMKDEVAGEVPVAFVV------------RSNGSEITEDEIKQFVAKQVVFYKRIHKVF--FVDSIPK 519
|
570
....*....|....*
gi 22329863 535 TTTGKVKRDEVRRQV 549
Cdd:PLN02246 520 APSGKILRKDLRAKL 534
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
34-547 |
1.25e-35 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 140.28 E-value: 1.25e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 34 TGREFVDGVLSLAAGLIRLGLRNGDVVSIAAFNSDLFLEWLLAVALVGGVVAPLNYRWSlKEAKMAMLLVEPV-LLVTDE 112
Cdd:PRK13382 70 TWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFA-GPALAEVVTREGVdTVIYDE 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 113 ---TCVSWCIDVQNGDIPSLKWrvlmesTSTDfANELNQFLTTEMLKQRtlVPSlatyawASDDAVVICFTSGTTGRPKG 189
Cdd:PRK13382 149 efsATVDRALADCPQATRIVAW------TDED-HDLTVEVLIAAHAGQR--PEP------TGRKGRVILLTSGTTGTPKG 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 190 VtiSHLAFITQSLAKiAIAGY----GEDDVYLhTSPLVHIGGLSS-AMAMLMvgACHVLLP-KFDAKTALQVMEQNHITC 263
Cdd:PRK13382 214 A--RRSGPGGIGTLK-AILDRtpwrAEEPTVI-VAPMFHAWGFSQlVLAASL--ACTIVTRrRFDPEATLDLIDRHRATG 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 264 FITVPAMMADLIRVNRTTKNGAENRGVRKILNGGGSLSSELLKEAVNIFPCArILSAYGMTEAcSSLTFMTLHDptqesf 343
Cdd:PRK13382 288 LAVVPVMFDRIMDLPAEVRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFGDV-IYNNYNATEA-GMIATATPAD------ 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 344 kvtypLLNQPKQGtcvGKPAPHIELMVkLDED-----SSRVGKILTRGPHTMLRYwghqvaqenveTSESRSN--EAWLD 416
Cdd:PRK13382 360 -----LRAAPDTA---GRPAEGTEIRI-LDQDfrevpTGEVGTIFVRNDTQFDGY-----------TSGSTKDfhDGFMA 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 417 TGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGVIDTRLGEMVVACVRLqekwiwsdvenr 496
Cdd:PRK13382 420 SGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVL------------ 487
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 22329863 497 KGSFQLSSETLKHHCRtQNLTGFKIPKRFVRWEKqFPLTTTGKVKRDEVRR 547
Cdd:PRK13382 488 KPGASATPETLKQHVR-DNLANYKVPRDIVVLDE-LPRGATGKILRRELQA 536
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
173-542 |
1.14e-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: 133.93 E-value: 1.14e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 173 DAVVICFTSGTTGRPKGVTISH-LAFITQSLAKIAIAGYGEDDVYLHTSPLVHIGGLS-SAMAMLMVGACHVLLPKFDAK 250
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANkTFFAVPDILQKEGLNWVVGDVTYLPLPATHIGGLWwILTCLIHGGLCVTGGENTTYK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 251 TALQVMEQNHITCFITVPAMMADLirVNRTTKNGAENRGVRKILNGGgSLSSELLKEAVNIFPCARILSAYGMTEAcSSL 330
Cdd:cd17635 82 SLFKILTTNAVTTTCLVPTLLSKL--VSELKSANATVPSLRLIGYGG-SRAIAADVRFIEATGLTNTAQVYGLSET-GTA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 331 TFMTLHDPTQESfkvtypllnqpkqgTCVGKPAPHIELMVKlDEDSSRV-----GKILTRGPHTMLRYWghqvaqENVET 405
Cdd:cd17635 158 LCLPTDDDSIEI--------------NAVGRPYPGVDVYLA-ATDGIAGpsasfGTIWIKSPANMLGYW------NNPER 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 406 SESRSNEAWLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGVIDTRLGEMVVACVRLQ 485
Cdd:cd17635 217 TAEVLIDGWVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVAS 296
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 22329863 486 EkwiWSDvENRkgsfqlsSETLKHHCRTQnLTGFKIPKRFVRWEkQFPLTTTGKVKR 542
Cdd:cd17635 297 A---ELD-ENA-------IRALKHTIRRE-LEPYARPSTIVIVT-DIPRTQSGKVKR 340
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
163-546 |
1.87e-34 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 137.32 E-value: 1.87e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 163 SLATYAWASDDAVVICFTSGTTGRPKGVTISH---LAFITQSLAKIAIAGYGED--DVYLHTSPLVHIGGLSSAMAMLM- 236
Cdd:PRK08751 199 SMPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHrnlVANMQQAHQWLAGTGKLEEgcEVVITALPLYHIFALTANGLVFMk 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 237 VGAC-HVLLPKFDAKTALQVMEQNHITCFITVPAMMADLIrvNRTTKNGAENRGVRKILNGGGSLS---SELLKEAVNIf 312
Cdd:PRK08751 279 IGGCnHLISNPRDMPGFVKELKKTRFTAFTGVNTLFNGLL--NTPGFDQIDFSSLKMTLGGGMAVQrsvAERWKQVTGL- 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 313 pcaRILSAYGMTEACSSLTFmtlhDPtqesfkvtyplLNQPKQGTCVGKPAPHIELMVKLDEDSS----RVGKILTRGPH 388
Cdd:PRK08751 356 ---TLVEAYGLTETSPAACI----NP-----------LTLKEYNGSIGLPIPSTDACIKDDAGTVlaigEIGELCIKGPQ 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 389 TMLRYWghqvaQENVETSESRSNEAWLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIG 468
Cdd:PRK08751 418 VMKGYW-----KRPEETAKVMDADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVG 492
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22329863 469 VIDTRLGEMVVACVrlqekwiwsdvenRKGSFQLSSETLKHHCRTqNLTGFKIPkRFVRWEKQFPLTTTGKVKRDEVR 546
Cdd:PRK08751 493 VPDEKSGEIVKVVI-------------VKKDPALTAEDVKAHARA-NLTGYKQP-RIIEFRKELPKTNVGKILRRELR 555
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
23-542 |
7.51e-34 |
|
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: 134.25 E-value: 7.51e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 23 AVVTVYGNRKRTGREFVDGVLSLAAGLIRLGLRNGDVVSIAAFNSDLFLEWLLAVALVGGVVAPLNYRWSlkEAKMAMLL 102
Cdd:cd12117 13 AVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELP--AERLAFML 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 103 --VEPVLLVTDEtcvswcidvqngdipSLKWRVLMESTSTDFANELNQFLTtemlkqrtlvPSLATYAWASDDAVVIcFT 180
Cdd:cd12117 91 adAGAKVLLTDR---------------SLAGRAGGLEVAVVIDEALDAGPA----------GNPAVPVSPDDLAYVM-YT 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 181 SGTTGRPKGVTISHLAFItqSLAKIA-IAGYGEDDVYLHTSPLVhigglSSAMAM-----LMVGACHVLLPK---FDAKT 251
Cdd:cd12117 145 SGSTGRPKGVAVTHRGVV--RLVKNTnYVTLGPDDRVLQTSPLA-----FDASTFeiwgaLLNGARLVLAPKgtlLDPDA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 252 ALQVMEQNHITC-FIT----------VPAMMAdlirvnrttkngaenrGVRKILNGGGSLSSELLKEAVNIFPCARILSA 320
Cdd:cd12117 218 LGALIAEEGVTVlWLTaalfnqladeDPECFA----------------GLRELLTGGEVVSPPHVRRVLAACPGLRLVNG 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 321 YGMTEacsSLTFMTLHdPTQESFKVTYPLLnqpkqgtcVGKPAPHIELMVkLDEDSS-----RVGKILTRGPHTMLRYWG 395
Cdd:cd12117 282 YGPTE---NTTFTTSH-VVTELDEVAGSIP--------IGRPIANTRVYV-LDEDGRpvppgVPGELYVGGDGLALGYLN 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 396 H-QVAQENVETSESRSNEAWLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIgVIDTRL 474
Cdd:cd12117 349 RpALTAERFVADPFGPGERLYRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVV-VREDAG 427
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22329863 475 GE-MVVACVRLQEKwiwsdvenrkgsfqLSSETLKHHCRtQNLTGFKIPKRFVRWEkQFPLTTTGKVKR 542
Cdd:cd12117 428 GDkRLVAYVVAEGA--------------LDAAELRAFLR-ERLPAYMVPAAFVVLD-ELPLTANGKVDR 480
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
172-546 |
7.81e-34 |
|
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: 133.36 E-value: 7.81e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 172 DDAVVICFTSGTTGRPKGVTISH--LAFITQSLAKIAIaGYGEDDVYLHTSPLVHIGGL-SSAMAMLMVGACHVLLPKF- 247
Cdd:cd05919 91 DDIAYLLYSSGTTGPPKGVMHAHrdPLLFADAMAREAL-GLTPGDRVFSSAKMFFGYGLgNSLWFPLAVGASAVLNPGWp 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 248 DAKTALQVMEQNHITCFITVPAMMADLIRVNRTTKngAENRGVRKILNGGGSLSSELLKEAVNIFPCArILSAYGMTEac 327
Cdd:cd05919 170 TAERVLATLARFRPTVLYGVPTFYANLLDSCAGSP--DALRSLRLCVSAGEALPRGLGERWMEHFGGP-ILDGIGATE-- 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 328 ssltfmTLHdptqeSFkvtypLLNQPKQ---GTCvGKPAPHIELMVkLDED-----SSRVGKILTRGPHTMLRYWghqva 399
Cdd:cd05919 245 ------VGH-----IF-----LSNRPGAwrlGST-GRPVPGYEIRL-VDEEghtipPGEEGDLLVRGPSAAVGYW----- 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 400 qENVETSESRSNEAWLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGVID----TRLG 475
Cdd:cd05919 302 -NNPEKSRATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPEstglSRLT 380
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22329863 476 EMVVAcvrlqekwiwsdvENRKGSFQLSSETLKHHCRTQnLTGFKIPKRFVRWEkQFPLTTTGKVKRDEVR 546
Cdd:cd05919 381 AFVVL-------------KSPAAPQESLARDIHRHLLER-LSAHKVPRRIAFVD-ELPRTATGKLQRFKLR 436
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
170-546 |
9.79e-34 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 135.28 E-value: 9.79e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 170 ASDDAVVICFTSGTTGRPKGVTISH---LAFITQSLAKIAiAGYGED-DVYLHTSPLVHIGGLS-SAMAMLMVGACHVLL 244
Cdd:PRK05677 205 QADDVAVLQYTGGTTGVAKGAMLTHrnlVANMLQCRALMG-SNLNEGcEILIAPLPLYHIYAFTfHCMAMMLIGNHNILI 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 245 PK-FDAKTALQVMEQNHITCFITVPAMMADLirVNRTTKNGAENRGVRKILNGGGSLSSELLKEAVNIFPCArILSAYGM 323
Cdd:PRK05677 284 SNpRDLPAMVKELGKWKFSGFVGLNTLFVAL--CNNEAFRKLDFSALKLTLSGGMALQLATAERWKEVTGCA-ICEGYGM 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 324 TEACSSLTFmtlhDPTQEsfkvtypllNQPkqGTcVGKPAPHIelMVKLDEDSSR------VGKILTRGPHTMLRYWghq 397
Cdd:PRK05677 361 TETSPVVSV----NPSQA---------IQV--GT-IGIPVPST--LCKVIDDDGNelplgeVGELCVKGPQVMKGYW--- 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 398 vaQENVETSESRSNEAWLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGVIDTRLGEM 477
Cdd:PRK05677 420 --QRPEATDEILDSDGWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEA 497
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22329863 478 VVACVRLqekwiwsdvenrKGSFQLSSETLKHHCRtQNLTGFKIPKrFVRWEKQFPLTTTGKVKRDEVR 546
Cdd:PRK05677 498 IKVFVVV------------KPGETLTKEQVMEHMR-ANLTGYKVPK-AVEFRDELPTTNVGKILRRELR 552
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
34-545 |
1.61e-33 |
|
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: 133.25 E-value: 1.61e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 34 TGREFVDGVLSLAAGLIRLGLRNGDVVSIAAFNSdlfLEWLLA-VALV--GGVVAPLNYRWSLKEAKMAMLLVEPVLLVt 110
Cdd:cd17640 7 TYKDLYQEILDFAAGLRSLGVKAGEKVALFADNS---PRWLIAdQGIMalGAVDVVRGSDSSVEELLYILNHSESVALV- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 111 detcvswcidVQNGdipslkwrvlmeststdfanelnqflttemlkqrtlvpslatyawaSDDAVVICFTSGTTGRPKGV 190
Cdd:cd17640 83 ----------VEND----------------------------------------------SDDLATIIYTSGTTGNPKGV 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 191 TISHLAFITQ--SLAKIAIAGYGedDVYLHTSPLVHIGGLSSAMAMLMVGACHvllpkfdAKTALQVMEQNHITCfitVP 268
Cdd:cd17640 107 MLTHANLLHQirSLSDIVPPQPG--DRFLSILPIWHSYERSAEYFIFACGCSQ-------AYTSIRTLKDDLKRV---KP 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 269 AMMADLIRVNRTTKNG------AENRGVRKI-------------LNGGGSLSSELLK--EAVNIfpcaRILSAYGMTEAc 327
Cdd:cd17640 175 HYIVSVPRLWESLYSGiqkqvsKSSPIKQFLflfflsggifkfgISGGGALPPHVDTffEAIGI----EVLNGYGLTET- 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 328 ssltfmtlhdptqeSFKVTYPLLNQPKQGTCvGKPAPHIELMVkLDEDSSRV------GKILTRGPHTMLRYWghqvaQE 401
Cdd:cd17640 250 --------------SPVVSARRLKCNVRGSV-GRPLPGTEIKI-VDPEGNVVlppgekGIVWVRGPQVMKGYY-----KN 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 402 NVETSESRSNEAWLDTGDIGAFDEFGNLWLIGRSNGRIK-TGGENVYPEEVEAVLVEHPGIVSAVVIGVIDTRLGEMVVA 480
Cdd:cd17640 309 PEATSKVLDSDGWFNTGDLGWLTCGGELVLTGRAKDTIVlSNGENVEPQPIEEALMRSPFIEQIMVVGQDQKRLGALIVP 388
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 481 CVRLQEKW-------IWSDVENRKGSFQ-LSSETLKHHCRTQNLTGFKIPKR---FVRWEKQFP----LTTTGKVKRDEV 545
Cdd:cd17640 389 NFEELEKWakesgvkLANDRSQLLASKKvLKLYKNEIKDEISNRPGFKSFEQiapFALLEEPFIengeMTQTMKIKRNVV 468
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
33-547 |
1.98e-33 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 134.70 E-value: 1.98e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 33 RTGREFVDGVLSLAAGLIRLGLRNGDVVSIAAFN-SDLFleWLLAVALVGGVVAPLNYRWS-------LKEAKMAMLL-- 102
Cdd:PRK07529 59 WTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNlPETH--FALWGGEAAGIANPINPLLEpeqiaelLRAAGAKVLVtl 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 103 -----------VEPVL--LVTDETCVswCIDVQNGDIPSLKWRVLMesTSTDFANELNQFLTtEMLKQRTLVPSLATYAW 169
Cdd:PRK07529 137 gpfpgtdiwqkVAEVLaaLPELRTVV--EVDLARYLPGPKRLAVPL--IRRKAHARILDFDA-ELARQPGDRLFSGRPIG 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 170 ASDDAVVICfTSGTTGRPKGVTISHLAFITQSLAKIAIAGYGEDDVYLHTSPLVHIGGL-SSAMAMLMVGAcHVLLPK-- 246
Cdd:PRK07529 212 PDDVAAYFH-TGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPGDTVFCGLPLFHVNALlVTGLAPLARGA-HVVLATpq 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 247 -FDAKTALQ----VMEQNHITCFITVPAMMADLIRVNRttkNGAENRGVRKILNGGGSLSSELL---KEAVNIfpcaRIL 318
Cdd:PRK07529 290 gYRGPGVIAnfwkIVERYRINFLSGVPTVYAALLQVPV---DGHDISSLRYALCGAAPLPVEVFrrfEAATGV----RIV 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 319 SAYGMTEA-CSSltfmtlhdptqesfKVTYPllNQPKQGTCVGKPAPHIEL-MVKLDEDSSR--------VGKILTRGPH 388
Cdd:PRK07529 363 EGYGLTEAtCVS--------------SVNPP--DGERRIGSVGLRLPYQRVrVVILDDAGRYlrdcavdeVGVLCIAGPN 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 389 TMLRYWghQVAQENVETSESRsneaWLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIG 468
Cdd:PRK07529 427 VFSGYL--EAAHNKGLWLEDG----WLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAAVG 500
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 469 VIDTRLGEMVVACVRLQEkwiwsdvenrkGSfQLSSETLKHHCRTQNLTGFKIPKRfVRWEKQFPLTTTGKV-----KRD 543
Cdd:PRK07529 501 RPDAHAGELPVAYVQLKP-----------GA-SATEAELLAFARDHIAERAAVPKH-VRILDALPKTAVGKIfkpalRRD 567
|
....
gi 22329863 544 EVRR 547
Cdd:PRK07529 568 AIRR 571
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
23-548 |
5.03e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 132.94 E-value: 5.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 23 AVVTVYGNRKRTGREFVDGVLSLAAGLIRLGLRNGDVVSIAAFNSDLFLEWLLAVALVGGVVAPLNYRWS-------LKE 95
Cdd:PRK06164 26 AVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRshevahiLGR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 96 AKMAMLLVEPVLLVTDetCVSWCIDVQNGDIPSLKWRVLMESTSTDFANELnQFLTTEMLKQRTLVPSLATYAWASD-DA 174
Cdd:PRK06164 106 GRARWLVVWPGFKGID--FAAILAAVPPDALPPLRAIAVVDDAADATPAPA-PGARVQLFALPDPAPPAAAGERAADpDA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 175 VVICF-TSGTTGRPKGVTISHLAFITQSLAKIAIAGYGEDDVYLHTSPLVHIGGLSSAMAMLMVGACHVLLPKFDAKTAL 253
Cdd:PRK06164 183 GALLFtTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFGFSTLLGALAGGAPLVCEPVFDAARTA 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 254 QVMEQNHITCFITVPAMMAdliRVNRTTKNGAENRGVRkiLNGGGSLS---SELLKEAvnifpCARILSAYGMTEACSSL 330
Cdd:PRK06164 263 RALRRHRVTHTFGNDEMLR---RILDTAGERADFPSAR--LFGFASFApalGELAALA-----RARGVPLTGLYGSSEVQ 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 331 TFMTLHDptqesfkVTYPLLNQPKQGtcvGKPA-PHIELMVKlDEDSSRV------GKILTRGPHTMLRYWGHQVAqenv 403
Cdd:PRK06164 333 ALVALQP-------ATDPVSVRIEGG---GRPAsPEARVRAR-DPQDGALlpdgesGEIEIRAPSLMRGYLDNPDA---- 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 404 eTSESRSNEAWLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGVidTRLGEMV-VACV 482
Cdd:PRK06164 398 -TARALTDDGYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGA--TRDGKTVpVAFV 474
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22329863 483 RLQEkwiwsdvenrkgSFQLSSETLKHHCRtQNLTGFKIPKRFVRWEkQFPLTTTG---KVKRDEVRRQ 548
Cdd:PRK06164 475 IPTD------------GASPDEAGLMAACR-EALAGFKVPARVQVVE-AFPVTESAngaKIQKHRLREM 529
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
11-486 |
1.69e-32 |
|
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: 133.44 E-value: 1.69e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 11 QCLTRL--ASVKRN--AVVTVYGNRKRTGREFVDGVLSLAAGLIRLGLRNGDVVSIAAFNSDLFLEWLLAVALVGGVVAP 86
Cdd:COG1020 476 ATLHELfeAQAARTpdAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVP 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 87 L--NYRwslkEAKMAMLL--VEPVLLVTDETCVSWcidvqngdIPSLKWRVLmestSTDfanelnqflTTEMLKQRTLVP 162
Cdd:COG1020 556 LdpAYP----AERLAYMLedAGARLVLTQSALAAR--------LPELGVPVL----ALD---------ALALAAEPATNP 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 163 SLATyawASDD-AVVIcFTSGTTGRPKGVTISHLAFITQSLAKIAIAGYGEDDVYLHTSPL---VHIGGLSSAmamLMVG 238
Cdd:COG1020 611 PVPV---TPDDlAYVI-YTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFASLsfdASVWEIFGA---LLSG 683
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 239 ACHVLLPKFDAKTA---LQVMEQNHITCFITVPAMMADLIRVNRttkngAENRGVRKILNGGGSLSSELLKEAVNIFPCA 315
Cdd:COG1020 684 ATLVLAPPEARRDPaalAELLARHRVTVLNLTPSLLRALLDAAP-----EALPSLRLVLVGGEALPPELVRRWRARLPGA 758
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 316 RILSAYGMTEA--CSSLTFMTLHDPTQESfkVTYpllnqpkqgtcvGKPAPHIELMVkLDEDSSRV-----------GKI 382
Cdd:COG1020 759 RLVNLYGPTETtvDSTYYEVTPPDADGGS--VPI------------GRPIANTRVYV-LDAHLQPVpvgvpgelyigGAG 823
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 383 LTRGphtmlrYWGHQVAqenveTSE-------SRSNEAWLDTGDIGAFDEFGNLWLIGRS------NG-RIKTGgenvyp 448
Cdd:COG1020 824 LARG------YLNRPEL-----TAErfvadpfGFPGARLYRTGDLARWLPDGNLEFLGRAddqvkiRGfRIELG------ 886
|
490 500 510
....*....|....*....|....*....|....*...
gi 22329863 449 eEVEAVLVEHPGIVSAVVIGVIDTRLGEMVVACVRLQE 486
Cdd:COG1020 887 -EIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEA 923
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
33-463 |
2.77e-32 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 130.48 E-value: 2.77e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 33 RTGREFVDGVLSLAAGLIRLGLRNGDVVsIAAFNSDL-FLEWLLAVALVGGVVAPL----NYR-WSLKEAKMA---MLLV 103
Cdd:cd05906 40 QSYQDLLEDARRLAAGLRQLGLRPGDSV-ILQFDDNEdFIPAFWACVLAGFVPAPLtvppTYDePNARLRKLRhiwQLLG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 104 EPVLLVTDETCVSwcIDVQNGDIPSLKWRVLMESTSTDFANELNqflttemlkqrtLVPSLAtyawasDDAVVICFTSGT 183
Cdd:cd05906 119 SPVVLTDAELVAE--FAGLETLSGLPGIRVLSIEELLDTAADHD------------LPQSRP------DDLALLMLTSGS 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 184 TGRPKGVTISHLAFITQSLAKIAIAGYGEDDVYLHTSPLVHIGGLSSAMAMLMVGACHvllpKFDAKTALQVMEqnhitc 263
Cdd:cd05906 179 TGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVPLDHVGGLVELHLRAVYLGCQ----QVHVPTEEILAD------ 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 264 fitvPAMMADLI---RVNRT-TKNGA---ENRGVRKILNGGGSLSSelLK------EAVNIFPCARILS----------- 319
Cdd:cd05906 249 ----PLRWLDLIdryRVTITwAPNFAfalLNDLLEEIEDGTWDLSS--LRylvnagEAVVAKTIRRLLRllepyglppda 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 320 ---AYGMTEACSSLTFmTLHDPTQES-----FkvtypllnqpkqgTCVGKPAPHIELMVKLDEDSS----RVGKILTRGP 387
Cdd:cd05906 323 irpAFGMTETCSGVIY-SRSFPTYDHsqaleF-------------VSLGRPIPGVSMRIVDDEGQLlpegEVGRLQVRGP 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22329863 388 HTMLRYWGHQVAqenveTSESRSNEAWLDTGDIGAFDEfGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVS 463
Cdd:cd05906 389 VVTKGYYNNPEA-----NAEAFTEDGWFRTGDLGFLDN-GNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEP 458
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
21-546 |
3.83e-31 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 126.66 E-value: 3.83e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 21 RNAVVTVYGNRKRTGREFVDGVLSLAAGLIRLGLRNGDVVSIAAFNSDLFLEWLLAVALVGGVVAPLNYRWSLKEAKMAM 100
Cdd:PRK13390 13 RPAVIVAETGEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYIV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 101 LLVEPVLLVTDETCVSWCIDVqNGDIPslkwrvlmesTSTDFANELNQFLTTEmlkqRTLV---PSLATYAWASddavVI 177
Cdd:PRK13390 93 GDSGARVLVASAALDGLAAKV-GADLP----------LRLSFGGEIDGFGSFE----AALAgagPRLTEQPCGA----VM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 178 CFTSGTTGRPKGVT--ISHLAFITQSLAKIAIAG--YG--EDDVYLHTSPLVHIGGLSSAMAMLMVGACHVLLPKFDAKT 251
Cdd:PRK13390 154 LYSSGTTGFPKGIQpdLPGRDVDAPGDPIVAIARafYDisESDIYYSSAPIYHAAPLRWCSMVHALGGTVVLAKRFDAQA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 252 ALQVMEQNHITCFITVPAMMADLIRVNRTTKNGAENRGVRKILNGGGSLSSELlKEAVNIFPCARILSAYGMTEAcSSLT 331
Cdd:PRK13390 234 TLGHVERYRITVTQMVPTMFVRLLKLDADVRTRYDVSSLRAVIHAAAPCPVDV-KHAMIDWLGPIVYEYYSSTEA-HGMT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 332 FMTLHDPTQESFKVTYPLLnqpkqGTCvgkpapHIelmvkLDED-----SSRVGKILTRGPHTMLRYWGhqvAQENVETS 406
Cdd:PRK13390 312 FIDSPDWLAHPGSVGRSVL-----GDL------HI-----CDDDgnelpAGRIGTVYFERDRLPFRYLN---DPEKTAAA 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 407 ESRSNEAWLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGVIDTRLGEMVVACVRLqe 486
Cdd:PRK13390 373 QHPAHPFWTTVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQL-- 450
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 487 kwiwsdVENRKGSFQLSSEtLKHHCRTQnLTGFKIPkRFVRWEKQFPLTTTGKVKRDEVR 546
Cdd:PRK13390 451 ------VEGIRGSDELARE-LIDYTRSR-IAHYKAP-RSVEFVDELPRTPTGKLVKGLLR 501
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
172-542 |
4.96e-31 |
|
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: 126.02 E-value: 4.96e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 172 DDAVVICFTSGTTGRPKGVTISHLAFITQSLAKIAIAGYGEDDVYLHTSPLVHIGGLSSAMAM-LMVGACHVLLPKF-DA 249
Cdd:cd05914 89 DDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLLGKGDKILSILPLHHIYPLTFTLLLpLLNGAHVVFLDKIpSA 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 250 KTALQVMEQNHITCFITVPAMMADLIR---VNRTTKNGAENRGVRKILN------------------------GGGSLSS 302
Cdd:cd05914 169 KIIALAFAQVTPTLGVPVPLVIEKIFKmdiIPKLTLKKFKFKLAKKINNrkirklafkkvheafggnikefviGGAKINP 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 303 ELLKEAVNI-FPcarILSAYGMTEaCSSLtfmtlhdptqesfkVTYPLLNQPKQGTCvGKPAPHIELMVKLDEDSSRVGK 381
Cdd:cd05914 249 DVEEFLRTIgFP---YTIGYGMTE-TAPI--------------ISYSPPNRIRLGSA-GKVIDGVEVRIDSPDPATGEGE 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 382 ILTRGPHTMLRYWGHQVAqenveTSESRSNEAWLDTGDIGAFDEFGNLWLIGRSNGRIKTG-GENVYPEEVEAVLVEHPG 460
Cdd:cd05914 310 IIVRGPNVMKGYYKNPEA-----TAEAFDKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSsGKNIYPEEIEAKINNMPF 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 461 IVSAVVIgVIDTRLGEMVVacvrlqekwIWSDVENRKGSFQLSS-ETLKHHCR---TQNLTGFKIPKRFVRWEKQFPLTT 536
Cdd:cd05914 385 VLESLVV-VQEKKLVALAY---------IDPDFLDVKALKQRNIiDAIKWEVRdkvNQKVPNYKKISKVKIVKEEFEKTP 454
|
....*.
gi 22329863 537 TGKVKR 542
Cdd:cd05914 455 KGKIKR 460
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
171-551 |
1.02e-30 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 126.32 E-value: 1.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 171 SDDAVVICFTSGTTGRPKGVTISHLAFITQSLAKIAIAG----YGEDDVYLhTSPLVHIGGLS-SAMAMLMVGACHVLlp 245
Cdd:PRK08974 205 PEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQAKAAYGpllhPGKELVVT-ALPLYHIFALTvNCLLFIELGGQNLL-- 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 246 kfdaktalqvmeqnhITCFITVPAMMADLIR--------VNrTTKNGAENR---------GVRKILNGGGSLSSELLKEA 308
Cdd:PRK08974 282 ---------------ITNPRDIPGFVKELKKypftaitgVN-TLFNALLNNeefqeldfsSLKLSVGGGMAVQQAVAERW 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 309 VNIFPCaRILSAYGMTEaCSSLTFMTLHDPTQESfkvtypllnqpkqGTcVGKPAPHIELMVKLDEDS----SRVGKILT 384
Cdd:PRK08974 346 VKLTGQ-YLLEGYGLTE-CSPLVSVNPYDLDYYS-------------GS-IGLPVPSTEIKLVDDDGNevppGEPGELWV 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 385 RGPHTMLRYWghqvaQENVETSESRSNeAWLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSA 464
Cdd:PRK08974 410 KGPQVMLGYW-----QRPEATDEVIKD-GWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEV 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 465 VVIGVIDTRLGEMVVACVRLQEKwiwsdvenrkgsfQLSSETLKHHCRtQNLTGFKIPKrFVRWEKQFPLTTTGKVKRDE 544
Cdd:PRK08974 484 AAVGVPSEVSGEAVKIFVVKKDP-------------SLTEEELITHCR-RHLTGYKVPK-LVEFRDELPKSNVGKILRRE 548
|
....*..
gi 22329863 545 VRRQVLS 551
Cdd:PRK08974 549 LRDEARA 555
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
9-469 |
1.41e-30 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 126.14 E-value: 1.41e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 9 ICQCLTRLASVKRNAVVTVYGNRKRTGREFVDGVLSLAAGLIRLGLRNGDVVSIAAFNS-DLFLEWLlAVALVGGVVAPL 87
Cdd:PRK08279 39 LGDVFEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRpEYLAAWL-GLAKLGAVVALL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 88 NYrwSLKEAKMA--MLLVEPVLLVTDETCVSWCIDVQNGDIPSLKWRVL--MESTSTDFANELNQFLTTemlkQRTLVPS 163
Cdd:PRK08279 118 NT--QQRGAVLAhsLNLVDAKHLIVGEELVEAFEEARADLARPPRLWVAggDTLDDPEGYEDLAAAAAG----APTTNPA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 164 LATYAWASDDAVVIcFTSGTTGRPKGVTISHLAFITQSLAKIAIAGYGEDDVYLHTSPLVH-IGGLSSAMAMLMVGACHV 242
Cdd:PRK08279 192 SRSGVTAKDTAFYI-YTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLTPDDVLYCCLPLYHnTGGTVAWSSVLAAGATLA 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 243 LLPKFDAKTALQVMEQNHITCFITVpammADLIR--VNRTTKNGAENRGVRKIL-NGggsLSSELLKEAVNIFPCARILS 319
Cdd:PRK08279 271 LRRKFSASRFWDDVRRYRATAFQYI----GELCRylLNQPPKPTDRDHRLRLMIgNG---LRPDIWDEFQQRFGIPRILE 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 320 AYGMTEACSSLtfmtlhdptqesfkvtYPLLNQPKQ-GTCVGKPAPHIELmVKLDEDSSR-------------------- 378
Cdd:PRK08279 344 FYAASEGNVGF----------------INVFNFDGTvGRVPLWLAHPYAI-VKYDVDTGEpvrdadgrcikvkpgevgll 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 379 VGKILTRGPhtmlrYWGHQVAQEnvetSES-------RSNEAWLDTGDIGAFDEFGNLWLIGRSnG---RIKtgGENVYP 448
Cdd:PRK08279 407 IGRITDRGP-----FDGYTDPEA----SEKkilrdvfKKGDAWFNTGDLMRDDGFGHAQFVDRL-GdtfRWK--GENVAT 474
|
490 500
....*....|....*....|.
gi 22329863 449 EEVEAVLVEHPGIVSAVVIGV 469
Cdd:PRK08279 475 TEVENALSGFPGVEEAVVYGV 495
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
22-542 |
1.55e-30 |
|
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: 124.70 E-value: 1.55e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 22 NAVVTVYGNRKRTGREFVDGVLSLAAGLIRLGLRNGDVVSIAAFNSDLFLEWLLAVALVGGVVAPLNYRWSlkEAKMAML 101
Cdd:cd17646 13 DAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYP--ADRLAYM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 102 L--VEPVLLVTDETCVSWCidVQNGDIPSLKWRVLMESTSTDfanelnqflttemlKQRTLVPSLATYawasddavVIcF 179
Cdd:cd17646 91 LadAGPAVVLTTADLAARL--PAGGDVALLGDEALAAPPATP--------------PLVPPRPDNLAY--------VI-Y 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 180 TSGTTGRPKGVTISHLAFITQSLAKIAIAGYGEDDVYLHTSPLvhigglSSAMAM------LMVGACHVLLP---KFDAK 250
Cdd:cd17646 146 TSGSTGRPKGVMVTHAGIVNRLLWMQDEYPLGPGDRVLQKTPL------SFDVSVwelfwpLVAGARLVVARpggHRDPA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 251 TALQVMEQNHITCFITVPAMMADLIRVNRttknGAENRGVRKILNGGGSLSSELlkeavnifpCARILSAYGMTeacssl 330
Cdd:cd17646 220 YLAALIREHGVTTCHFVPSMLRVFLAEPA----AGSCASLRRVFCSGEALPPEL---------AARFLALPGAE------ 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 331 tFMTLHDPTQESFKVTYPLLNQPKQGTCV--GKPAPHIELMVkLDEDSSRV-----------GKILTRGPH-----TMLR 392
Cdd:cd17646 281 -LHNLYGPTEAAIDVTHWPVRGPAETPSVpiGRPVPNTRLYV-LDDALRPVpvgvpgelylgGVQLARGYLgrpalTAER 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 393 YWGHQVAQEnvetseSRSNEawldTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGVIDT 472
Cdd:cd17646 359 FVPDPFGPG------SRMYR----TGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAP 428
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 473 RLGEMVVACVRLQEkwiwsdvenrkGSFQLSSETLKHHCRTQnLTGFKIPKRFVRWEkQFPLTTTGKVKR 542
Cdd:cd17646 429 AGAARLVGYVVPAA-----------GAAGPDTAALRAHLAER-LPEYMVPAAFVVLD-ALPLTANGKLDR 485
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
170-546 |
3.05e-30 |
|
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: 123.36 E-value: 3.05e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 170 ASDDAVVICFTSGTTGRPKGVTISHLAFI-TQSLAKIAIAGYGEDDVYLHTSPLVHIGGLSS-AMAMLMVGACHVLLPKF 247
Cdd:cd05958 95 ASDDICILAFTSGTTGAPKATMHFHRDPLaSADRYAVNVLRLREDDRFVGSPPLAFTFGLGGvLLFPFGVGASGVLLEEA 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 248 DAKTALQVMEQNHITCFITVPAMMADLIRVNRTTknGAENRGVRKILNGGGSLSSELL---KEAVNIfpcaRILSAYGMT 324
Cdd:cd05958 175 TPDLLLSAIARYKPTVLFTAPTAYRAMLAHPDAA--GPDLSSLRKCVSAGEALPAALHrawKEATGI----PIIDGIGST 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 325 EAcssltfmtLHdptqeSFKVTYPLLNQPkqGTcVGKPAPHIELMVkLDEDSSRV-----GKILTRGPhTMLRYWGHQVA 399
Cdd:cd05958 249 EM--------FH-----IFISARPGDARP--GA-TGKPVPGYEAKV-VDDEGNPVpdgtiGRLAVRGP-TGCRYLADKRQ 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 400 QENVEtsesrsnEAWLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGVIDTRLGEMVV 479
Cdd:cd05958 311 RTYVQ-------GGWNITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVK 383
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22329863 480 ACVRLQEKWIWSDVENRKgsfqlssetLKHHCrTQNLTGFKIPkRFVRWEKQFPLTTTGKVKRDEVR 546
Cdd:cd05958 384 AFVVLRPGVIPGPVLARE---------LQDHA-KAHIAPYKYP-RAIEFVTELPRTATGKLQRFALR 439
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
34-540 |
4.30e-30 |
|
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: 123.60 E-value: 4.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 34 TGREFVDGVLSLAAgLIRLGLRNGDVVSIAAFNSDLFLEWLLAVALVGGVVAPLNYRWSLKEAKMAMLLVE--------- 104
Cdd:cd05909 9 TYRKLLTGAIALAR-KLAKMTKEGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGiktvltskq 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 105 ------PVLLVTDETCVSWCI--DVQNGDIPSLKWRVLMESTstdfanelnqFLTTEMLKQRTLVPSLatyawaSDDAVV 176
Cdd:cd05909 88 fieklkLHHLFDVEYDARIVYleDLRAKISKADKCKAFLAGK----------FPPKWLLRIFGVAPVQ------PDDPAV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 177 ICFTSGTTGRPKGVTISHLAFITQSLAKIAIAGYGEDDVYLHTSPLVHIGGLSSAMAM-LMVGACHVLLPK-FDAKTALQ 254
Cdd:cd05909 152 ILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPFFHSFGLTGCLWLpLLSGIKVVFHPNpLDYKKIPE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 255 VMEQNHITCFITVPAMMADLIRvnrtTKNGAENRGVRKILNGGGSLSSELLKEAVNIFPcARILSAYGMTEACSSLTfmt 334
Cdd:cd05909 232 LIYDKKATILLGTPTFLRGYAR----AAHPEDFSSLRLVVAGAEKLKDTLRQEFQEKFG-IRILEGYGTTECSPVIS--- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 335 lhdptqesfkVTYPllNQPKQGTCVGKPAPHIElmVKLDEDSSRV-------GKILTRGPHTMLRYWGhqvaqeNVETSE 407
Cdd:cd05909 304 ----------VNTP--QSPNKEGTVGRPLPGME--VKIVSVETHEevpigegGLLLVRGPNVMLGYLN------EPELTS 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 408 SRSNEAWLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAV-VIGVIDTRLGEMVVACVRLQE 486
Cdd:cd05909 364 FAFGDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEILPEDNEVaVVSVPDGRKGEKIVLLTTTTD 443
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 22329863 487 kwiwsdvenrkgsfqLSSETLKHHCRTQNLTGFKIPKRfVRWEKQFPLTTTGKV 540
Cdd:cd05909 444 ---------------TDPSSLNDILKNAGISNLAKPSY-IHQVEEIPLLGTGKP 481
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
22-545 |
4.99e-30 |
|
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: 123.15 E-value: 4.99e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 22 NAVVTVYGNRKRTGREFVDGVLSLAAGLIRLGLRNGDVVSIAAFNSDLFLEWLLAVALVGGVVAPLNYRWSlkEAKMAML 101
Cdd:cd12114 2 DATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQP--AARREAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 102 LVEP--VLLVTDETCVSWCIDVqngdIPSLKWRVLMESTSTDFAnelnqflttemlkqrtlvPSLAtyawASDDAVVICF 179
Cdd:cd12114 80 LADAgaRLVLTDGPDAQLDVAV----FDVLILDLDALAAPAPPP------------------PVDV----APDDLAYVIF 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 180 TSGTTGRPKGVTISHLAFITQSLAKIAIAGYGEDDVYLHTSPLVH-------IGGLSSAMAMLMVGACHVLlpkfDAKTA 252
Cdd:cd12114 134 TSGSTGTPKGVMISHRAALNTILDINRRFAVGPDDRVLALSSLSFdlsvydiFGALSAGATLVLPDEARRR----DPAHW 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 253 LQVMEQNHITCFITVPAMMaDLIrVNRTTKNGAENRGVRKILNGGGSLSSELLKEAVNIFPCARILSAYGMTEACSSLTF 332
Cdd:cd12114 210 AELIERHGVTLWNSVPALL-EML-LDVLEAAQALLPSLRLVLLSGDWIPLDLPARLRALAPDARLISLGGATEASIWSIY 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 333 MTLHDPTQESFKVTY--PLLNQpkqgtcvgkpAPHIelmvkLDEDSSR-----VGKILTRGPHTMLRYWGHQvaqenvET 405
Cdd:cd12114 288 HPIDEVPPDWRSIPYgrPLANQ----------RYRV-----LDPRGRDcpdwvPGELWIGGRGVALGYLGDP------EL 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 406 SESR-----SNEAWLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIgVIDTRLGEMVVA 480
Cdd:cd12114 347 TAARfvthpDGERLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVV-VLGDPGGKRLAA 425
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22329863 481 CVrlqekwiwsdVENRKGSfQLSSETLKHHcRTQNLTGFKIPKRFVrWEKQFPLTTTGKVKRDEV 545
Cdd:cd12114 426 FV----------VPDNDGT-PIAPDALRAF-LAQTLPAYMIPSRVI-ALEALPLTANGKVDRAAL 477
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
172-546 |
5.68e-30 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 124.16 E-value: 5.68e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 172 DDAVVICFTSGTTGRPKGVTISH---LAFITQSLAkiAIAGYGED---------DVYLHTSPLVHIGGLSS-AMAMLMVG 238
Cdd:PRK12492 207 DDIAVLQYTGGTTGLAKGAMLTHgnlVANMLQVRA--CLSQLGPDgqplmkegqEVMIAPLPLYHIYAFTAnCMCMMVSG 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 239 ACHVLL--PKfDAKTALQVMEQNHITCFITVPAMMADLIrvnrttkNGAENRGVR----KILNGGGS-LSSELLKEAVNI 311
Cdd:PRK12492 285 NHNVLItnPR-DIPGFIKELGKWRFSALLGLNTLFVALM-------DHPGFKDLDfsalKLTNSGGTaLVKATAERWEQL 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 312 FPCaRILSAYGMTEACSSLTfmtlhdptqesfkvTYPLLNQPKQGTcVGKPAPHIELMVkLDEDSSRV-----GKILTRG 386
Cdd:PRK12492 357 TGC-TIVEGYGLTETSPVAS--------------TNPYGELARLGT-VGIPVPGTALKV-IDDDGNELplgerGELCIKG 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 387 PHTMLRYWghqvaQENVETSESRSNEAWLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVV 466
Cdd:PRK12492 420 PQVMKGYW-----QQPEATAEALDAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAA 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 467 IGVIDTRLGEMVVACVRLQEKwiwsdvenrkgsfQLSSETLKHHCRtQNLTGFKIPKRFVRWEkQFPLTTTGKVKRDEVR 546
Cdd:PRK12492 495 IGVPDERSGEAVKLFVVARDP-------------GLSVEELKAYCK-ENFTGYKVPKHIVLRD-SLPMTPVGKILRRELR 559
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
171-547 |
1.04e-29 |
|
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: 120.28 E-value: 1.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 171 SDDAVVICFTSGTTGRPKGVTISHLAFITQSLAKIAIAGYGEDDVYLHTSPLVHIGG-LSSAMAMLMVGAcHVLLPK--- 246
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFHVNGsVVTLLTPLASGA-HVVLAGpag 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 247 FDAKTALQ----VMEQNHITCFITVPAMMADLIRVnrttKNGAENRGVRKILNGGGSLSSELLK--EAVNIFPcarILSA 320
Cdd:cd05944 80 YRNPGLFDnfwkLVERYRITSLSTVPTVYAALLQV----PVNADISSLRFAMSGAAPLPVELRArfEDATGLP---VVEG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 321 YGMTEACSSLTfmtlhdptqesfkVTYPllNQPKQGTCVGKPAPHIELMVKLDEDSSR---------VGKILTRGPHTml 391
Cdd:cd05944 153 YGLTEATCLVA-------------VNPP--DGPKRPGSVGLRLPYARVRIKVLDGVGRllrdcapdeVGEICVAGPGV-- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 392 rYWGHQVAQENvetSESRSNEAWLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGVID 471
Cdd:cd05944 216 -FGGYLYTEGN---KNAFVADGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPD 291
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22329863 472 TRLGEMVVACVRLqekwiwsdvenrKGSFQLSSETLKHHCRTQNLTGFKIPKRFVRWEkQFPLTTTGKVKRDEVRR 547
Cdd:cd05944 292 AHAGELPVAYVQL------------KPGAVVEEEELLAWARDHVPERAAVPKHIEVLE-ELPVTAVGKVFKPALRA 354
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
23-551 |
1.48e-29 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 122.78 E-value: 1.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 23 AVVTVYGNRKRTGREFVDGVLSLAAGLIRLGLRNGDVVSIAAFNSDLFLEWLLAVALVGGVVAPLNYRWSLKEAKMAMLL 102
Cdd:PLN02330 46 AFVEAVTGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 103 VEPVLLVTDetcvswciDVQNGDIPSLKWRVLMEStSTDFANELNQfltTEMLKQRTLVPSLATYAWA-SDDAVVICFTS 181
Cdd:PLN02330 126 AGAKLIVTN--------DTNYGKVKGLGLPVIVLG-EEKIEGAVNW---KELLEAADRAGDTSDNEEIlQTDLCALPFSS 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 182 GTTGRPKGVTISH---LAFITQSLAKIAIAGYGEDdVYLHTSPLVHIGGLSS-AMAMLMVGACHVLLPKFDAKTALQVME 257
Cdd:PLN02330 194 GTTGISKGVMLTHrnlVANLCSSLFSVGPEMIGQV-VTLGLIPFFHIYGITGiCCATLRNKGKVVVMSRFELRTFLNALI 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 258 QNHITCFITVPAMMADLIRVNRTTKNGAENRGVRKILNGGGSLSSELLKEAVNIFPCARILSAYGMTE-ACSSLTfmtlH 336
Cdd:PLN02330 273 TQEVSFAPIVPPIILNLVKNPIVEEFDLSKLKLQAIMTAAAPLAPELLTAFEAKFPGVQVQEAYGLTEhSCITLT----H 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 337 -DPTQEsfkvtypllNQPKQGTCVGKPAPHIELMVkLDEDSSRV------GKILTRGPHTMLRYWGHQVaqenvETSESR 409
Cdd:PLN02330 349 gDPEKG---------HGIAKKNSVGFILPNLEVKF-IDPDTGRSlpkntpGELCVRSQCVMQGYYNNKE-----ETDRTI 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 410 SNEAWLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGVIDTRLGEMVVACVRLQEKwi 489
Cdd:PLN02330 414 DEDGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVVINPK-- 491
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22329863 490 wsDVENRKGSFQLSSETLKHHCRTqnltgfkipkRFVRWEKQFPLTTTGKVKRDEVRRQVLS 551
Cdd:PLN02330 492 --AKESEEDILNFVAANVAHYKKV----------RVVQFVDSIPKSLSGKIMRRLLKEKMLS 541
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
21-546 |
3.24e-29 |
|
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: 121.45 E-value: 3.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 21 RNAVVTV--YGNRKR-TGREFVDGVLSLAAGLIRLGLRNGDVVSIAAFNSDLFLEWLLAVALVGGVVAP---------LN 88
Cdd:cd05970 33 KLALVWCddAGEERIfTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPathqltakdIV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 89 YRWSLKEAKMAMLLVEPVLL----VTDETCVSWCIDVQNGDIPSLKW---RVLMESTSTDFAnelnqflttemlkqrtlv 161
Cdd:cd05970 113 YRIESADIKMIVAIAEDNIPeeieKAAPECPSKPKLVWVGDPVPEGWidfRKLIKNASPDFE------------------ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 162 PSLATYAWASDDAVVICFTSGTTGRPKGVTISHlafiTQSLAKIAIAGYGED--DVYLHTSplVHIGGLSSAMAMLMVG- 238
Cdd:cd05970 175 RPTANSYPCGEDILLVYFSSGTTGMPKMVEHDF----TYPLGHIVTAKYWQNvrEGGLHLT--VADTGWGKAVWGKIYGq 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 239 ---ACHVLL---PKFDAKTALQVMEQNHITCFITVPAMMADLIRVNRTTKNGAenrGVRKILNGGGSLSSELL---KEAV 309
Cdd:cd05970 249 wiaGAAVFVydyDKFDPKALLEKLSKYGVTTFCAPPTIYRFLIREDLSRYDLS---SLRYCTTAGEALNPEVFntfKEKT 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 310 NIfpcaRILSAYGMTEacSSLTFMTLhdPTQEsfkvtypllnqPKQGTcVGKPAP--HIELMvklDEDSSRV-----GKI 382
Cdd:cd05970 326 GI----KLMEGFGQTE--TTLTIATF--PWME-----------PKPGS-MGKPAPgyEIDLI---DREGRSCeageeGEI 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 383 LTR----GPHTMLRYWGhqvaqENVEtsesRSNEAWLD----TGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAV 454
Cdd:cd05970 383 VIRtskgKPVGLFGGYY-----KDAE----KTAEVWHDgyyhTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESA 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 455 LVEHPGIVSAVVIGVIDTRLGEMVVACVRLQEKWIWSDVenrkgsfqLSSEtLKHHCRtQNLTGFKIPkRFVRWEKQFPL 534
Cdd:cd05970 454 LIQHPAVLECAVTGVPDPIRGQVVKATIVLAKGYEPSEE--------LKKE-LQDHVK-KVTAPYKYP-RIVEFVDELPK 522
|
570
....*....|..
gi 22329863 535 TTTGKVKRDEVR 546
Cdd:cd05970 523 TISGKIRRVEIR 534
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
170-546 |
6.40e-29 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 120.90 E-value: 6.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 170 ASDDAVVICFTSGTTGRPKGVTISH---LAFITQSLA--KIAIAGYGEDD--VYLHTSPLVHIGGLSSAMAMLM-VGACH 241
Cdd:PRK07059 202 GPDDVAFLQYTGGTTGVSKGATLLHrniVANVLQMEAwlQPAFEKKPRPDqlNFVCALPLYHIFALTVCGLLGMrTGGRN 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 242 VLLPK-FDAKTALQVMEQNHITCFitvPAmmadlirVNrTTKNG-AENRGVRK-------ILNGGGSLSSELLKEA-VNI 311
Cdd:PRK07059 282 ILIPNpRDIPGFIKELKKYQVHIF---PA-------VN-TLYNAlLNNPDFDKldfskliVANGGGMAVQRPVAERwLEM 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 312 FPCArILSAYGMTEACSSLTfmtLHDPTQESFkvtypllnqpkQGTcVGKPAPHIELMVKLDEDSS----RVGKILTRGP 387
Cdd:PRK07059 351 TGCP-ITEGYGLSETSPVAT---CNPVDATEF-----------SGT-IGLPLPSTEVSIRDDDGNDlplgEPGEICIRGP 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 388 HTMLRYWghqvaQENVETSESRSNEAWLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVI 467
Cdd:PRK07059 415 QVMAGYW-----NRPDETAKVMTADGFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAV 489
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22329863 468 GVIDTRLGEMVVACVRlqekwiwsdvenRKGSfQLSSETLKHHCRTQnLTGFKIPkRFVRWEKQFPLTTTGKVKRDEVR 546
Cdd:PRK07059 490 GVPDEHSGEAVKLFVV------------KKDP-ALTEEDVKAFCKER-LTNYKRP-KFVEFRTELPKTNVGKILRRELR 553
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
31-542 |
1.03e-28 |
|
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: 120.22 E-value: 1.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 31 RKRTGREFVDGVLSLAAGLIRLGLRNGDVVSIAAFNSDLFLEWLLAVALVGGVVAPLnYRWSLKEaKMAMLLV---EPVL 107
Cdd:cd17641 10 QEFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGI-YQDSMAE-EVAYLLNytgARVV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 108 LVTDETCVSWCIDVQNgDIPSLKWRVL-----MESTSTDFANELNQFLTTEMLKQRTLvPSLATYAWAS---DDAVVICF 179
Cdd:cd17641 88 IAEDEEQVDKLLEIAD-RIPSVRYVIYcdprgMRKYDDPRLISFEDVVALGRALDRRD-PGLYEREVAAgkgEDVAVLCT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 180 TSGTTGRPKGVTISHLAFITQSLAKIAIAGYGEDDVYLHTSPLVHIGGLSSAMAMLMVGACHVLLPKfDAKTALQVMEQN 259
Cdd:cd17641 166 TSGTTGKPKLAMLSHGNFLGHCAAYLAADPLGPGDEYVSVLPLPWIGEQMYSVGQALVCGFIVNFPE-EPETMMEDLREI 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 260 HITCFITVP-----------AMMADLIRVNR-------TTKNGAENRGVRKILNGGGSLSSELLKEAVNIFPC------A 315
Cdd:cd17641 245 GPTFVLLPPrvwegiaadvrARMMDATPFKRfmfelgmKLGLRALDRGKRGRPVSLWLRLASWLADALLFRPLrdrlgfS 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 316 RILSA-------------------------YGMTEACSSLTFMTLHDPTQESfkvtypllnqpkqgtcVGKPAPHIElmV 370
Cdd:cd17641 325 RLRSAatggaalgpdtfrffhaigvplkqlYGQTELAGAYTVHRDGDVDPDT----------------VGVPFPGTE--V 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 371 KLDEdssrVGKILTRGPHTMLRYWGHQVAqenveTSESRSNEAWLDTGDIGAFDEFGNLWLIGRSNGRIKTG-GENVYPE 449
Cdd:cd17641 387 RIDE----VGEILVRSPGVFVGYYKNPEA-----TAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDVGTTSdGTRFSPQ 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 450 EVEAVLVEHPGIVSAVVIGVIDTRLGEMVvaCVRLQ--EKWiwsdVENRKGSF----QLSS-----ETLKHHCRTQNLT- 517
Cdd:cd17641 458 FIENKLKFSPYIAEAVVLGAGRPYLTAFI--CIDYAivGKW----AEQRGIAFttytDLASrpevyELIRKEVEKVNASl 531
|
570 580 590
....*....|....*....|....*....|..
gi 22329863 518 --GFKIpKRFVRWEKQF-----PLTTTGKVKR 542
Cdd:cd17641 532 peAQRI-RRFLLLYKELdaddgELTRTRKVRR 562
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
24-548 |
1.96e-28 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 119.09 E-value: 1.96e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 24 VVT--VYGNRKRTG-REFVDGVLSLAAGLIRLGLRNGDVVSIAAFNSDLFLEWLLAVALVGGVVAPLNYR-------WSL 93
Cdd:PRK06018 28 VVTrsVEGPIVRTTyAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRlfpeqiaWII 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 94 KEAkmamllvEPVLLVTDETCVSwCIDVQNGDIPSLKWRVLMESTSTDFANEL-NQFLTTEMLKQRTlvpslATYAWASD 172
Cdd:PRK06018 108 NHA-------EDRVVITDLTFVP-ILEKIADKLPSVERYVVLTDAAHMPQTTLkNAVAYEEWIAEAD-----GDFAWKTF 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 173 D---AVVICFTSGTTGRPKGVTISHLAFITQSLAKIA--IAGYGEDDVYLHTSPLVHIGGLSSAMAMLMVGACHVLL-PK 246
Cdd:PRK06018 175 DentAAGMCYTSGTTGDPKGVLYSHRSNVLHALMANNgdALGTSAADTMLPVVPLFHANSWGIAFSAPSMGTKLVMPgAK 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 247 FDAKTALQVMEQNHITCFITVPAMMadLIRVNRTTKNGAENRGVRKILNGGGSLSSELLKE----AVNIFPcarilsAYG 322
Cdd:PRK06018 255 LDGASVYELLDTEKVTFTAGVPTVW--LMLLQYMEKEGLKLPHLKMVVCGGSAMPRSMIKAfedmGVEVRH------AWG 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 323 MTEACSSLTFMTLHDPTQEsFKVTYPLLNQPKQGtcvgKPAPHIELMVKLDE------DSSRVGKILTRGPHTMLRYWGh 396
Cdd:PRK06018 327 MTEMSPLGTLAALKPPFSK-LPGDARLDVLQKQG----YPPFGVEMKITDDAgkelpwDGKTFGRLKVRGPAVAAAYYR- 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 397 qvaqenvETSESRSNEAWLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGVIDTRLGE 476
Cdd:PRK06018 401 -------VDGEILDDDGFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDE 473
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22329863 477 MVVACVRLQEkwiwsdvenrkGSFQLSSETLKHhcrtqnLTGfKIPKRF----VRWEKQFPLTTTGKVKRDEVRRQ 548
Cdd:PRK06018 474 RPLLIVQLKP-----------GETATREEILKY------MDG-KIAKWWmpddVAFVDAIPHTATGKILKTALREQ 531
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
23-542 |
3.91e-28 |
|
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: 117.08 E-value: 3.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 23 AVVTVYGNRKRTGREFVDGVLSLAAGLIRLGLRNGDVVSIAAFNSDLFLEWLLAVALVGGVVAPL--NY-----RWSLKE 95
Cdd:cd17649 3 AVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLdpEYpaerlRYMLED 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 96 AKMAMLLVepvllvtdetcvswcidvQNGDIPslkwrvlmeststdfanelnqflttemlkqrtlvpslatyawasddAV 175
Cdd:cd17649 83 SGAGLLLT------------------HHPRQL----------------------------------------------AY 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 176 VIcFTSGTTGRPKGVTISHLAFITQSLAKIAIAGYGEDDVYLHTSPLVHIGGLSSAMAMLMVGACHVLLPK---FDAKTA 252
Cdd:cd17649 99 VI-YTSGSTGTPKGVAVSHGPLAAHCQATAERYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDelwASADEL 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 253 LQVMEQNHITCFITVPAMMADLIRVNRTTKNGAENRgVRKILNGGGSLSSELLKEAvniFPCA-RILSAYGMTEAcsSLT 331
Cdd:cd17649 178 AEMVRELGVTVLDLPPAYLQQLAEEADRTGDGRPPS-LRLYIFGGEALSPELLRRW---LKAPvRLFNAYGPTEA--TVT 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 332 FMTLHDPTQESFKVTYPLLnqpkqGTCVGKPAPHIelmvkLDED-----SSRVGKILTRGPHTMLRYWGH--QVAQENVE 404
Cdd:cd17649 252 PLVWKCEAGAARAGASMPI-----GRPLGGRSAYI-----LDADlnpvpVGVTGELYIGGEGLARGYLGRpeLTAERFVP 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 405 TSESRSNEAWLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGViDTRLGEMVVACVRL 484
Cdd:cd17649 322 DPFGAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVAL-DGAGGKQLVAYVVL 400
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 22329863 485 QEkwiwsdvenrKGSFQLSSETLKHHCRTQnLTGFKIPKRFVRWEKqFPLTTTGKVKR 542
Cdd:cd17649 401 RA----------AAAQPELRAQLRTALRAS-LPDYMVPAHLVFLAR-LPLTPNGKLDR 446
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
73-548 |
1.38e-27 |
|
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: 116.41 E-value: 1.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 73 WLLAVALV--GGVVAP---------LNYRWSLKEAKMamllvepvlLVTDETcVSWCIDVQNGDIPSLKWRVLMESTSTD 141
Cdd:cd05928 81 WLVNVACIrtGLVFIPgtiqltakdILYRLQASKAKC---------IVTSDE-LAPEVDSVASECPSLKTKLLVSEKSRD 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 142 ----FaNELNQFLTTEMLKQRTlvpslatyawASDDAVVICFTSGTTGRPKGVTISHLAF-ITQSLAKIAIAGYGEDDVY 216
Cdd:cd05928 151 gwlnF-KELLNEASTEHHCVET----------GSQEPMAIYFTSGTTGSPKMAEHSHSSLgLGLKVNGRYWLDLTASDIM 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 217 LHTSPLVHI-GGLSSAMAMLMVGAC---HvLLPKFDAKTALQVMEQNHITCFITVPAMMADLIRVNRTTkngAENRGVRK 292
Cdd:cd05928 220 WNTSDTGWIkSAWSSLFEPWIQGACvfvH-HLPRFDPLVILKTLSSYPITTFCGAPTVYRMLVQQDLSS---YKFPSLQH 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 293 ILNGGGSLSSELL---KEAVNIfpcaRILSAYGMTEacSSLTFMTlhdptQESFKVtypllnqpKQGTcVGKPAPHIELM 369
Cdd:cd05928 296 CVTGGEPLNPEVLekwKAQTGL----DIYEGYGQTE--TGLICAN-----FKGMKI--------KPGS-MGKASPPYDVQ 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 370 VkLDEDSSRV-----GKILTR-GPHTMLRYWGHQVaQENVETSESRSNEAWLdTGDIGAFDEFGNLWLIGRSNGRIKTGG 443
Cdd:cd05928 356 I-IDDNGNVLppgteGDIGIRvKPIRPFGLFSGYV-DNPEKTAATIRGDFYL-TGDRGIMDEDGYFWFMGRADDVINSSG 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 444 ENVYPEEVEAVLVEHPGIVSAVVIGVIDTRLGEMVVACVRLQEKWIWSDVEnrkgsfQLSSETLKHhcrTQNLTG-FKIP 522
Cdd:cd05928 433 YRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLAPQFLSHDPE------QLTKELQQH---VKSVTApYKYP 503
|
490 500
....*....|....*....|....*.
gi 22329863 523 KRfVRWEKQFPLTTTGKVKRDEVRRQ 548
Cdd:cd05928 504 RK-VEFVQELPKTVTGKIQRNELRDK 528
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
149-469 |
1.88e-27 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 116.15 E-value: 1.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 149 FLTTEMLKQRTLVPSLAtyAWASDDAVVICFTSGTTGRPKGVTISHLAFitqsLAKIAIAG--YGE--DDVYLHTSPLVH 224
Cdd:PRK09274 153 TLATLLRDGAAAPFPMA--DLAPDDMAAILFTSGSTGTPKGVVYTHGMF----EAQIEALRedYGIepGEIDLPTFPLFA 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 225 IGGLSSAMAMLmvgachvlLPKFDA-KTA-------LQVMEQNHITCFITVPAMMadlirvNRTTKNGAENR----GVRK 292
Cdd:PRK09274 227 LFGPALGMTSV--------IPDMDPtRPAtvdpaklFAAIERYGVTNLFGSPALL------ERLGRYGEANGiklpSLRR 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 293 ILNGGGSLSSELLKEAVNIFP-CARILSAYGMTEA--CSSLTFMTLHDPTQEsfkvtyplLNQPKQGTCVGKPAPHIEL- 368
Cdd:PRK09274 293 VISAGAPVPIAVIERFRAMLPpDAEILTPYGATEAlpISSIESREILFATRA--------ATDNGAGICVGRPVDGVEVr 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 369 MVKLDE-------DSSR-----VGKILTRGPHTMLRYWGHQVAQENVETSESRSNeAWLDTGDIGAFDEFGNLWLIGRSN 436
Cdd:PRK09274 365 IIAISDapipewdDALRlatgeIGEIVVAGPMVTRSYYNRPEATRLAKIPDGQGD-VWHRMGDLGYLDAQGRLWFCGRKA 443
|
330 340 350
....*....|....*....|....*....|....
gi 22329863 437 GRIKTGGENVYPEEVEAVLVEHPGIV-SAVViGV 469
Cdd:PRK09274 444 HRVETAGGTLYTIPCERIFNTHPGVKrSALV-GV 476
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
45-546 |
3.31e-27 |
|
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: 115.13 E-value: 3.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 45 LAAGLIRLGLRNGDVVSIAAFNSDLFLEWLLAVALVGGVVAPLNYRWSlKEAKMAMLL-VEPVLLVTDEtcvswciDVQN 123
Cdd:cd17651 33 LAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP-AERLAFMLAdAGPVLVLTHP-------ALAG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 124 gdipslkwrvlmeststDFANELNQFLTTEMLKQRTLVPSLATYAWASDDAVVICFTSGTTGRPKGVTISH--LAFITQS 201
Cdd:cd17651 105 -----------------ELAVELVAVTLLDQPGAAAGADAEPDPALDADDLAYVIYTSGSTGRPKGVVMPHrsLANLVAW 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 202 LAKIAIAGYGEddvylHTSPLVhigGLSSAMAM------LMVGACHVLLP---KFDAKTALQVMEQNHIT-CFitVPAMM 271
Cdd:cd17651 168 QARASSLGPGA-----RTLQFA---GLGFDVSVqeifstLCAGATLVLPPeevRTDPPALAAWLDEQRISrVF--LPTVA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 272 ADLIrVNRTTKNGAENRGVRKILNGGGSLS-SELLKEAVNIFPCARILSAYGMTEAcsslTFMTLHDPTQESfkVTYPLL 350
Cdd:cd17651 238 LRAL-AEHGRPLGVRLAALRYLLTGGEQLVlTEDLREFCAGLPGLRLHNHYGPTET----HVVTALSLPGDP--AAWPAP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 351 NQpkqgtcVGKPAPHIELMVkLDEDSSRV-----------GKILTRGphtmLRYWGHQVAQENVETSESRSNEAWLdTGD 419
Cdd:cd17651 311 PP------IGRPIDNTRVYV-LDAALRPVppgvpgelyigGAGLARG----YLNRPELTAERFVPDPFVPGARMYR-TGD 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 420 IGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGVIDTRLGEMVVACVRLQEkwiwsdvenrkgS 499
Cdd:cd17651 379 LARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDP------------E 446
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 22329863 500 FQLSSETLKHHCRTQnLTGFKIPKRFVRWEKqFPLTTTGKVKRDEVR 546
Cdd:cd17651 447 APVDAAELRAALATH-LPEYMVPSAFVLLDA-LPLTPNGKLDRRALP 491
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
13-546 |
3.87e-27 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 115.33 E-value: 3.87e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 13 LTRLASVKRNAVVTVYGNRKRTGREFVDGVLSLAAGLIRLGLRNGDVVSIAAFNSDLFLEWLLAVALVGGVVAPLNYRws 92
Cdd:PLN02479 26 LERAAVVHPTRKSVVHGSVRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIR-- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 93 LKEAKMAMLL---VEPVLLVTDE--TCVSwcidvqngdiPSLKwrVLMESTSTDFANELNQFLTTEMLKQRTLVPSLA-- 165
Cdd:PLN02479 104 LNAPTIAFLLehsKSEVVMVDQEffTLAE----------EALK--ILAEKKKSSFKPPLLIVIGDPTCDPKSLQYALGkg 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 166 -------------TYAWASD----DAVVICFTSGTTGRPKGVTISHLAFITQSLAKIAIAGYGEDDVYLHTSPLVHIGGL 228
Cdd:PLN02479 172 aieyekfletgdpEFAWKPPadewQSIALGYTSGTTASPKGVVLHHRGAYLMALSNALIWGMNEGAVYLWTLPMFHCNGW 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 229 SSAMAMLMVGACHVLLPKFDAKTALQVMEQNHITCFITVPAMMADLIRVNRTTKNGAENRGVRKILNGGGSLSSELLKEA 308
Cdd:PLN02479 252 CFTWTLAALCGTNICLRQVTAKAIYSAIANYGVTHFCAAPVVLNTIVNAPKSETILPLPRVVHVMTAGAAPPPSVLFAMS 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 309 VNIFpcaRILSAYGMTEACSSLTFMTLHdPTQESFkvtyPLLNQPK----QG-------------TCVGKPAPhielmvk 371
Cdd:PLN02479 332 EKGF---RVTHTYGLSETYGPSTVCAWK-PEWDSL----PPEEQARlnarQGvryiglegldvvdTKTMKPVP------- 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 372 ldEDSSRVGKILTRGPHTMLRYWghqvaqENVETSESRSNEAWLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEV 451
Cdd:PLN02479 397 --ADGKTMGEIVMRGNMVMKGYL------KNPKANEEAFANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEV 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 452 EAVLVEHPGIVSAVVIGVIDTRLGEMVVACVRLQEKWIWSDvENRkgsfqLSSETLKhHCRtQNLTGFKIPKRFVRweKQ 531
Cdd:PLN02479 469 ENVVYTHPAVLEASVVARPDERWGESPCAFVTLKPGVDKSD-EAA-----LAEDIMK-FCR-ERLPAYWVPKSVVF--GP 538
|
570
....*....|....*
gi 22329863 532 FPLTTTGKVKRDEVR 546
Cdd:PLN02479 539 LPKTATGKIQKHVLR 553
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
221-546 |
4.39e-27 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 114.32 E-value: 4.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 221 PLVHIGGLSSAMAMLMVGACHVLLPKFDAKTAlQVMEQNHITCFIT-VPAMMADLIrvnrtTKNGAENRGVRKILNGGGS 299
Cdd:PRK07445 168 PLYHVSGLMQFMRSFLTGGKLVILPYKRLKSG-QELPPNPSDFFLSlVPTQLQRLL-----QLRPQWLAQFRTILLGGAP 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 300 LSSELLKEA----VNIFPCarilsaYGMTEACSSLTfmTLhdpTQESFkvtyplLNQpkqGTCVGKPAPHielmVKLDED 375
Cdd:PRK07445 242 AWPSLLEQArqlqLRLAPT------YGMTETASQIA--TL---KPDDF------LAG---NNSSGQVLPH----AQITIP 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 376 SSRVGKILTRGPHTMLRYWGHQVAQENVetsesrsneawLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVL 455
Cdd:PRK07445 298 ANQTGNITIQAQSLALGYYPQILDSQGI-----------FETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAI 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 456 VEHPGIVSAVVIGVIDTRLGEMVVACVRLQEkwiwsdvenrkgsFQLSSETLKHHCRTQnLTGFKIPKRFVrWEKQFPLT 535
Cdd:PRK07445 367 LATGLVQDVCVLGLPDPHWGEVVTAIYVPKD-------------PSISLEELKTAIKDQ-LSPFKQPKHWI-PVPQLPRN 431
|
330
....*....|.
gi 22329863 536 TTGKVKRDEVR 546
Cdd:PRK07445 432 PQGKINRQQLQ 442
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
158-482 |
8.14e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 113.55 E-value: 8.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 158 RTLVPSLATYAWASDDAV-VICFTSGTTGRPKGVTISHLAfITQSLAKIAIA-GYGEDDVYLHTSPLVHIGGLS-SAMAM 234
Cdd:PRK07787 113 RLHARSWHRYPEPDPDAPaLIVYTSGTTGPPKGVVLSRRA-IAADLDALAEAwQWTADDVLVHGLPLFHVHGLVlGVLGP 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 235 LMVGACHVLLPKFDAKTALQVMEQNHiTCFITVPAMMAdliRVNRTTKNGAENRGVRKILNGGGSLSS---ELLKEAVNI 311
Cdd:PRK07787 192 LRIGNRFVHTGRPTPEAYAQALSEGG-TLYFGVPTVWS---RIAADPEAARALRGARLLVSGSAALPVpvfDRLAALTGH 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 312 FPCARilsaYGMTEacsslTFMTLhdptqeSFKVTYPllnqPKQGTcVGKPAPHIELMVKLDE------DSSRVGKILTR 385
Cdd:PRK07787 268 RPVER----YGMTE-----TLITL------STRADGE----RRPGW-VGLPLAGVETRLVDEDggpvphDGETVGELQVR 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 386 GPHTMLRYWGHQVAqenveTSESRSNEAWLDTGDIGAFDEFGNLWLIGR-SNGRIKTGGENVYPEEVEAVLVEHPGIVSA 464
Cdd:PRK07787 328 GPTLFDGYLNRPDA-----TAAAFTADGWFRTGDVAVVDPDGMHRIVGReSTDLIKSGGYRIGAGEIETALLGHPGVREA 402
|
330
....*....|....*...
gi 22329863 465 VVIGVIDTRLGEMVVACV 482
Cdd:PRK07787 403 AVVGVPDDDLGQRIVAYV 420
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
171-545 |
1.50e-26 |
|
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: 113.08 E-value: 1.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 171 SDDAVVICFTSGTTGRPKGVTISHLAFI--TQSLAKIAIAGYGEDDVYLHTSPLVHIGGLSSAMAMLMVGAC------HV 242
Cdd:cd17639 87 PDDLACIMYTSGSTGNPKGVMLTHGNLVagIAGLGDRVPELLGPDDRYLAYLPLAHIFELAAENVCLYRGGTigygspRT 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 243 LLPKFDAKTALQVMEQNHiTCFITVPAMMaDLIR------------VNRT-------TKNGAENRG-------------- 289
Cdd:cd17639 167 LTDKSKRGCKGDLTEFKP-TLMVGVPAIW-DTIRkgvlaklnpmggLKRTlfwtayqSKLKALKEGpgtplldelvfkkv 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 290 -------VRKILNGGGSLSSELlKEAVNIFpCARILSAYGMTEACSSLTFMTLHDPTQEsfkvtypllnqpkqgtCVGKP 362
Cdd:cd17639 245 raalggrLRYMLSGGAPLSADT-QEFLNIV-LCPVIQGYGLTETCAGGTVQDPGDLETG----------------RVGPP 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 363 APHIElmVKL----------DEDSSRvGKILTRGPHTMLRYWGHQVaqenvETSESRSNEAWLDTGDIGAFDEFGNLWLI 432
Cdd:cd17639 307 LPCCE--IKLvdweeggystDKPPPR-GEILIRGPNVFKGYYKNPE-----KTKEAFDGDGWFHTGDIGEFHPDGTLKII 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 433 GRSNGRIKT-GGENVYPEEVEAVLVEHPgIVSAV----------VIGVIDTRLGE-MVVAcvrlQEKWI----WSDVENR 496
Cdd:cd17639 379 DRKKDLVKLqNGEYIALEKLESIYRSNP-LVNNIcvyadpdksyPVAIVVPNEKHlTKLA----EKHGVinseWEELCED 453
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 22329863 497 KGSFQLSSETLKHHCRTQNLTGFKIPKRFV----RW--EKQFpLTTTGKVKRDEV 545
Cdd:cd17639 454 KKLQKAVLKSLAETARAAGLEKFEIPQGVVlldeEWtpENGL-VTAAQKLKRKEI 507
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
45-552 |
6.46e-26 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 111.72 E-value: 6.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 45 LAAGLIRLGLRNGDVVSIAAFNSDLFLEWLLAVALVGGVVAPLNYR-------WSLKEAKMAMLLVEPVLLVTDETCVSW 117
Cdd:PRK07008 52 LAQALAALGVEPGDRVGTLAWNGYRHLEAYYGVSGSGAVCHTINPRlfpeqiaYIVNHAEDRYVLFDLTFLPLVDALAPQ 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 118 CidvqngdiPSLKWRVLMestsTDFANELNQflTTEMLKQRTLVPSL-ATYAWASDD---AVVICFTSGTTGRPKGVTIS 193
Cdd:PRK07008 132 C--------PNVKGWVAM----TDAAHLPAG--STPLLCYETLVGAQdGDYDWPRFDenqASSLCYTSGTTGNPKGALYS 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 194 HLAFITQSLAKIA--IAGYGEDDVYLHTSPLVHIGGLSSAMAMLMVGACHVLL-PKFDAKTALQVMEQNHITCFITVPAM 270
Cdd:PRK07008 198 HRSTVLHAYGAALpdAMGLSARDAVLPVVPMFHVNAWGLPYSAPLTGAKLVLPgPDLDGKSLYELIEAERVTFSAGVPTV 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 271 MADLIrvNRTTKNGAENRGVRKILNGGGSLSSELLKEAVNIFPcARILSAYGMTE-----ACSSLTFMTLHDPTQESFKV 345
Cdd:PRK07008 278 WLGLL--NHMREAGLRFSTLRRTVIGGSACPPAMIRTFEDEYG-VEVIHAWGMTEmsplgTLCKLKWKHSQLPLDEQRKL 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 346 typllnQPKQGTCV-----------GKPAPHielmvkldeDSSRVGKILTRGPHTMLRYWGhqvaqenveTSESRSNEAW 414
Cdd:PRK07008 355 ------LEKQGRVIygvdmkivgddGRELPW---------DGKAFGDLQVRGPWVIDRYFR---------GDASPLVDGW 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 415 LDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGVIDTRLGE---MVVAcvrlqekwiws 491
Cdd:PRK07008 411 FPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDErplLVVV----------- 479
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22329863 492 dvenRKGSFQLSSETLKHHCRTQnLTGFKIPKRFVrWEKQFPLTTTGKVKRDEVRRQVLSH 552
Cdd:PRK07008 480 ----KRPGAEVTREELLAFYEGK-VAKWWIPDDVV-FVDAIPHTATGKLQKLKLREQFRDY 534
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
22-542 |
9.42e-26 |
|
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: 110.46 E-value: 9.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 22 NAVVTVYGNRKRTGREFVDGVLSLAAGLIRLGLRNGDVVSIAAFNSDLFLEWLLAVALVGGVVAPLNYRwsLKEAKMAML 101
Cdd:cd12116 2 DATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPD--YPADRLRYI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 102 L--VEPVLLVTDETC---VSWCIDVQNGDIPSLKWRVLMESTSTDFAnelnqflttemlkqrtlvpslatyawasDDAVV 176
Cdd:cd12116 80 LedAEPALVLTDDALpdrLPAGLPVLLLALAAAAAAPAAPRTPVSPD----------------------------DLAYV 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 177 IcFTSGTTGRPKGVTISHLAFITQSLAKIAIAGYGEDDVYLH-TSPLVHIGGLSSAMAmLMVGACHVLLPKFDAKTA--- 252
Cdd:cd12116 132 I-YTSGSTGRPKGVVVSHRNLVNFLHSMRERLGLGPGDRLLAvTTYAFDISLLELLLP-LLAGARVVIAPRETQRDPeal 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 253 LQVMEQNHITCFITVPA---MMADlirvnrttkNGAENR-GVRkILNGGGSLSSELLKEAvnifpCARILSA---YGMTE 325
Cdd:cd12116 210 ARLIEAHSITVMQATPAtwrMLLD---------AGWQGRaGLT-ALCGGEALPPDLAARL-----LSRVGSLwnlYGPTE 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 326 AC--SSLTFMTLHDPtqesfKVTypllnqpkqgtcVGKPAPHIELMVkLDEDSSRV-----GKILTRGPHTMLRYWGHQV 398
Cdd:cd12116 275 TTiwSTAARVTAAAG-----PIP------------IGRPLANTQVYV-LDAALRPVppgvpGELYIGGDGVAQGYLGRPA 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 399 --AQENVETSESRSNEAWLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIgVIDTRLGE 476
Cdd:cd12116 337 ltAERFVPDPFAGPGSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVV-VREDGGDR 415
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22329863 477 MVVACVRLqekwiwsdvenrKGSFQLSSETLKHHCRTQnLTGFKIPKRFVRWEkQFPLTTTGKVKR 542
Cdd:cd12116 416 RLVAYVVL------------KAGAAPDAAALRAHLRAT-LPAYMVPSAFVRLD-ALPLTANGKLDR 467
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
29-550 |
1.31e-25 |
|
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: 110.79 E-value: 1.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 29 GNRKRTGREFVDGVLSLAAGLIRLGLRnGDVVSIAAFNSDLFLEWLLAVALVGGVVAPLNYRWSLKEAKMAMLLV---EP 105
Cdd:cd05931 21 REETLTYAELDRRARAIAARLQAVGKP-GDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPPTPGRHAERLAAILadaGP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 106 VLLVTDEtcvswcidvqnGDIPSLKwrvlmESTSTDFANELNQFLTTEmlkqrtLVPSLATYAW-----ASDDAVVICFT 180
Cdd:cd05931 100 RVVLTTA-----------AALAAVR-----AFAASRPAAGTPRLLVVD------LLPDTSAADWpppspDPDDIAYLQYT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 181 SGTTGRPKGVTISHLAFITQSLAKIAIAGYGEDDV---YLhtsPLVH----IGGLssaMAMLMVGACHVLLP--KFDAKT 251
Cdd:cd05931 158 SGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVvvsWL---PLYHdmglIGGL---LTPLYSGGPSVLMSpaAFLRRP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 252 A--LQVMEQNHITcFITVPAMMADLIrVNRTTKNGAEN---RGVRKILNGGGSLSSELLKEAVNIF-----PCARILSAY 321
Cdd:cd05931 232 LrwLRLISRYRAT-ISAAPNFAYDLC-VRRVRDEDLEGldlSSWRVALNGAEPVRPATLRRFAEAFapfgfRPEAFRPSY 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 322 GMTEACSSLTFMTLHDPTQESFkVTYPLLNQPKQG-----------TCVGKPAPHIELMVkLDEDSSR------VGKILT 384
Cdd:cd05931 310 GLAEATLFVSGGPPGTGPVVLR-VDRDALAGRAVAvaaddpaarelVSCGRPLPDQEVRI-VDPETGRelpdgeVGEIWV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 385 RGPHTMLRYWGHQVAQEnvETSESRSNEA---WLDTGDIGAFDEfGNLWLIGRSNGRIKTGGENVYPEEVEAVLVE-HPG 460
Cdd:cd05931 388 RGPSVASGYWGRPEATA--ETFGALAATDeggWLRTGDLGFLHD-GELYITGRLKDLIIVRGRNHYPQDIEATAEEaHPA 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 461 IV--SAVVIGVIDTRLGEMVVACvrlqekwiwsDVENRKGSFQLSSetLKHHCRTQNLTGFKIPKR---FVRwEKQFPLT 535
Cdd:cd05931 465 LRpgCVAAFSVPDDGEERLVVVA----------EVERGADPADLAA--IAAAIRAAVAREHGVAPAdvvLVR-PGSIPRT 531
|
570
....*....|....*
gi 22329863 536 TTGKVKRDEVRRQVL 550
Cdd:cd05931 532 SSGKIQRRACRAAYL 546
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
36-554 |
2.00e-25 |
|
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: 110.00 E-value: 2.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 36 REFVDGVLSLAAGLIRLGLR--NGDVVSIAAFNSdlfLEWLL---AVALVGGVVAPLnY--------RWSLKEAKMAMLL 102
Cdd:cd05927 9 KEVAERADNIGSALRSLGGKpaPASFVGIYSINR---PEWIIselACYAYSLVTVPL-YdtlgpeaiEYILNHAEISIVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 103 VEPvllvtDETCVSWcidvqngdipslkwrvlmeststdfanelNQFLTTEMLKQRTLVPSlatyawASDDAVVICFTSG 182
Cdd:cd05927 85 CDA-----GVKVYSL-----------------------------EEFEKLGKKNKVPPPPP------KPEDLATICYTSG 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 183 TTGRPKGVTISHLAFITQSLAKIAIAG----YGEDDVYLHTSPLVHIGGLSSAMAMLMVGAC--------HVLLPkfDAK 250
Cdd:cd05927 125 TTGNPKGVMLTHGNIVSNVAGVFKILEilnkINPTDVYISYLPLAHIFERVVEALFLYHGAKigfysgdiRLLLD--DIK 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 251 tALQVmeqnhiTCFITVP--------AMMADLIR---VNRTTKNGAENR------------------------------G 289
Cdd:cd05927 203 -ALKP------TVFPGVPrvlnriydKIFNKVQAkgpLKRKLFNFALNYklaelrsgvvraspfwdklvfnkikqalggN 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 290 VRKILNGGGSLSSELLKEAVNIFpCARILSAYGMTEaCSSLTFMTLHDPTQEsfkvtypllnqpkqgTCVGKPAPHIElm 369
Cdd:cd05927 276 VRLMLTGSAPLSPEVLEFLRVAL-GCPVLEGYGQTE-CTAGATLTLPGDTSV---------------GHVGGPLPCAE-- 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 370 VKLDE---------DSSRVGKILTRGPHTMLRYWghqvaQENVETSESRSNEAWLDTGDIGAFDEFGNLWLIGRSNGRIK 440
Cdd:cd05927 337 VKLVDvpemnydakDPNPRGEVCIRGPNVFSGYY-----KDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIFK 411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 441 -TGGENVYPEEVEAVLVEHPGIVSAVVIGviDTrLGEMVVACVRLQEKWI--WSDVENR-KGSFQ--LSSETLKHH---- 510
Cdd:cd05927 412 lSQGEYVAPEKIENIYARSPFVAQIFVYG--DS-LKSFLVAIVVPDPDVLkeWAASKGGgTGSFEelCKNPEVKKAiled 488
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 22329863 511 ----CRTQNLTGFKIPKRFVRWEKQFP-----LTTTGKVKRDEVRrqvlSHFQ 554
Cdd:cd05927 489 lvrlGKENGLKGFEQVKAIHLEPEPFSvenglLTPTFKLKRPQLK----KYYK 537
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
37-468 |
3.81e-25 |
|
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: 109.10 E-value: 3.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 37 EFVDGVLSLAAGLIRLGLRNGDVVSIAAFNSdlfLEWL---LAVALVGGVVAPL-------NYRWSLKEAKMAMLLVEPV 106
Cdd:cd05932 11 EVADKARRLAAALRALGLEPGSKIALISKNC---AEWFitdLAIWMAGHISVPLyptlnpdTIRYVLEHSESKALFVGKL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 107 llvtDEtcvsWCiDVQNGDIPSLKWRVLMESTSTDFANELNQFLTTEMLKQRTLVPslatyawASDDAVVICFTSGTTGR 186
Cdd:cd05932 88 ----DD----WK-AMAPGVPEGLISISLPPPSAANCQYQWDDLIAQHPPLEERPTR-------FPEQLATLIYTSGTTGQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 187 PKGVTISHLAFITQSLAKIAIAGYGEDDVYLHTSPLVHI--------GGLSSAMAMLMVGAChvllpkfdaKTALQVMEQ 258
Cdd:cd05932 152 PKGVMLTFGSFAWAAQAGIEHIGTEENDRMLSYLPLAHVtervfvegGSLYGGVLVAFAESL---------DTFVEDVQR 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 259 NHITCFITVPAM-------MADLI---RVNRTTKNGAENRGV-RKILNGGGSLSSELLKEAVNIFPCA----------RI 317
Cdd:cd05932 223 ARPTLFFSVPRLwtkfqqgVQDKIpqqKLNLLLKIPVVNSLVkRKVLKGLGLDQCRLAGCGSAPVPPAllewyrslglNI 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 318 LSAYGMTEACSsltfmtlhdptqesfkvtYPLLNQP---KQGTcVGKPAPHIElmVKLDEDssrvGKILTRGPHTMLRYW 394
Cdd:cd05932 303 LEAYGMTENFA------------------YSHLNYPgrdKIGT-VGNAGPGVE--VRISED----GEILVRSPALMMGYY 357
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22329863 395 ghqvaQENVETSESRSNEAWLDTGDIGAFDEFGNLWLIGRSNGRIKTG-GENVYPEEVEAVLVEHPGIVSAVVIG 468
Cdd:cd05932 358 -----KDPEATAEAFTADGFLRTGDKGELDADGNLTITGRVKDIFKTSkGKYVAPAPIENKLAEHDRVEMVCVIG 427
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
13-555 |
3.97e-25 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 109.31 E-value: 3.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 13 LTRLASVKRNAVVtvYGNRKRTGREFVDGVLSLAAGLIRLGLRNGDVV-----SIAAFNSDLFlewllavALVGGVVAPL 87
Cdd:PRK10946 31 LTRHAASDAIAVI--CGERQFSYRELNQASDNLACSLRRQGIKPGDTAlvqlgNVAEFYITFF-------ALLKLGVAPV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 88 NYRWSLKEAKMA--MLLVEPVLLVTDETCVSWC----IDVQNGDIPSLKwRVLMESTSTDFAnelnqfLTTEMLKQRTLV 161
Cdd:PRK10946 102 NALFSHQRSELNayASQIEPALLIADRQHALFSdddfLNTLVAEHSSLR-VVLLLNDDGEHS------LDDAINHPAEDF 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 162 PSLATyawASDDAVVICFTSGTTGRPKGVTISHLAFITQSLAKIAIAGYGEDDVYLHTSPLVHIGGLSS--AMAMLMVGA 239
Cdd:PRK10946 175 TATPS---PADEVAFFQLSGGSTGTPKLIPRTHNDYYYSVRRSVEICGFTPQTRYLCALPAAHNYPMSSpgALGVFLAGG 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 240 CHVLLPKFDAKTALQVMEQNHITCFITVPAMMADLIRVNRTTKNGAENRGVRKILNGGGSLSSELLKEAVNIFPCaRILS 319
Cdd:PRK10946 252 TVVLAPDPSATLCFPLIEKHQVNVTALVPPAVSLWLQAIAEGGSRAQLASLKLLQVGGARLSETLARRIPAELGC-QLQQ 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 320 AYGMTEACSSLTfmTLHDPTQESFkvtypllnqpkqgTCVGKP-APHIELMVkLDEDSSRV-----GKILTRGPHTMLRY 393
Cdd:PRK10946 331 VFGMAEGLVNYT--RLDDSDERIF-------------TTQGRPmSPDDEVWV-ADADGNPLpqgevGRLMTRGPYTFRGY 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 394 WghQVAQENvetSESRSNEAWLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGVIDTR 473
Cdd:PRK10946 395 Y--KSPQHN---ASAFDANGFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDEL 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 474 LGEMVVACVRLQEKwiwsdvenrkgsfqLSSETLKHHCRTQNLTGFKIPKRFVRWEkQFPLTTTGKVKRDEVrRQVLSHF 553
Cdd:PRK10946 470 MGEKSCAFLVVKEP--------------LKAVQLRRFLREQGIAEFKLPDRVECVD-SLPLTAVGKVDKKQL-RQWLASR 533
|
..
gi 22329863 554 QI 555
Cdd:PRK10946 534 AS 535
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
171-482 |
4.38e-25 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 109.14 E-value: 4.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 171 SDDAVVICFTSGTTGRPKGVTISHLAFITQSLAKIAIAGYGEDDVYLHTSPLVHIGGLSSAMAMLMVGACHVLLP--KFD 248
Cdd:PRK06334 182 PEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSFLPPFHAYGFNSCTLFPLLSGVPVVFAynPLY 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 249 AKTALQVMEQNHITCFITVPAMMaDLIrVNRTTKNGAENRGVRKILNGGGSLSSELLKEAVNIFPCARILSAYGMTEaCS 328
Cdd:PRK06334 262 PKKIVEMIDEAKVTFLGSTPVFF-DYI-LKTAKKQESCLPSLRFVVIGGDAFKDSLYQEALKTFPHIQLRQGYGTTE-CS 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 329 SLtfmtlhdptqesfkVTYPLLNQPKQGTCVGKPAPHIELMVKLDE-----DSSRVGKILTRGPHTMLRYWGHQVAQENV 403
Cdd:PRK06334 339 PV--------------ITINTVNSPKHESCVGMPIRGMDVLIVSEEtkvpvSSGETGLVLTRGTSLFSGYLGEDFGQGFV 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 404 ETSesrsNEAWLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEH------PGIVSAVVIGVIdtrlGEM 477
Cdd:PRK06334 405 ELG----GETWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEGfgqnaaDHAGPLVVCGLP----GEK 476
|
....*
gi 22329863 478 VVACV 482
Cdd:PRK06334 477 VRLCL 481
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
49-492 |
7.33e-25 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 108.44 E-value: 7.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 49 LIRLGLRNGDVVSIAAFNSDLFLEWLLAVALVGGVVAPLNyrwslkEAKMA------MLLVEPVLLVTDETCVSwciDVQ 122
Cdd:PRK04319 90 LKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLF------EAFMEeavrdrLEDSEAKVLITTPALLE---RKP 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 123 NGDIPSLKWRVLMESTSTDFANELNqfLTTEMlkqRTLVPSLATYAWASDDAVVICFTSGTTGRPKGVTISHLAFITQSL 202
Cdd:PRK04319 161 ADDLPSLKHVLLVGEDVEEGPGTLD--FNALM---EQASDEFDIEWTDREDGAILHYTSGSTGKPKGVLHVHNAMLQHYQ 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 203 -AKIAIaGYGEDDVYLHT--------------SPLVHigGLSSamamLMVGAchvllpKFDAKTALQVMEQNHITCFITV 267
Cdd:PRK04319 236 tGKYVL-DLHEDDVYWCTadpgwvtgtsygifAPWLN--GATN----VIDGG------RFSPERWYRILEDYKVTVWYTA 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 268 PAMMADLIRVNRTTKNGAENRGVRKILNGGGSLSSELLKEAVNIFPcARILSAYGMTEacssltfmtlhdpTQESFKVTY 347
Cdd:PRK04319 303 PTAIRMLMGAGDDLVKKYDLSSLRHILSVGEPLNPEVVRWGMKVFG-LPIHDNWWMTE-------------TGGIMIANY 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 348 PLLNQpKQGTcVGKPAPHIELMVKLDEDSS----RVGKI-LTRGPHTMLR-YWGhqvaqeNVETSESRSNEAWLDTGDIG 421
Cdd:PRK04319 369 PAMDI-KPGS-MGKPLPGIEAAIVDDQGNElppnRMGNLaIKKGWPSMMRgIWN------NPEKYESYFAGDWYVSGDSA 440
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22329863 422 AFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGVIDTRLGEMVVACVRLQEKWIWSD 492
Cdd:PRK04319 441 YMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVALRPGYEPSE 511
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
155-551 |
1.70e-24 |
|
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: 106.80 E-value: 1.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 155 LKQRTLVPSLATYAWASDDAVVICFTSGTTGRPKGVTISHLAFITQSLAKIAIAGYGEDDVYLHTSPLVHIGGLSSA-MA 233
Cdd:cd05908 89 LKNPYLITEEEVLCELADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAFhLA 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 234 MLMVGACHVLLPK--FDAKTAL---QVMEqnHITCFITVPAMMADLI--RVNRTTKNGAENRGVRKILNGGGSLSSELLK 306
Cdd:cd05908 169 PLIAGMNQYLMPTrlFIRRPILwlkKASE--HKATIVSSPNFGYKYFlkTLKPEKANDWDLSSIRMILNGAEPIDYELCH 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 307 E---AVNIFPCAR--ILSAYGMTEACSSLTFmtlhDPTQESFKVTYPLlnqpKQGTCVGKPAPHI-----------ELMV 370
Cdd:cd05908 247 EfldHMSKYGLKRnaILPVYGLAEASVGASL----PKAQSPFKTITLG----RRHVTHGEPEPEVdkkdsecltfvEVGK 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 371 KLDEDSSR-------------VGKILTRGPHTMLRYWGHQVAQENVETSesrsnEAWLDTGDIGaFDEFGNLWLIGRSNG 437
Cdd:cd05908 319 PIDETDIRicdednkilpdgyIGHIQIRGKNVTPGYYNNPEATAKVFTD-----DGWLKTGDLG-FIRNGRLVITGREKD 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 438 RIKTGGENVYPEEVEAVLVEHPGIVSA--VVIGVIDTRLGEMVVACVRLQEKwiwsdVENRkgsFQLSSETLKHHCRTQn 515
Cdd:cd05908 393 IIFVNGQNVYPHDIERIAEELEGVELGrvVACGVNNSNTRNEEIFCFIEHRK-----SEDD---FYPLGKKIKKHLNKR- 463
|
410 420 430
....*....|....*....|....*....|....*.
gi 22329863 516 lTGFKIPKrfVRWEKQFPLTTTGKVKRDEVRRQVLS 551
Cdd:cd05908 464 -GGWQINE--VLPIRRIPKTTSGKVKRYELAQRYQS 496
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
11-557 |
5.74e-24 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 106.02 E-value: 5.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 11 QCLTRLASVKRNAVVTVYGNRKRTGREFVDgVLSLAAGLIR-----LGLRNGDVVSIAAFNSDLFLEWLLAVALVGGVVA 85
Cdd:PRK05620 14 RILEYGSTVHGDTTVTTWGGAEQEQTTFAA-IGARAAALAHalhdeLGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 86 PLNYRWSLKEAKMAMLLVEPVLLVTDETCVSWCIDVQNgDIPSLKWRVLmesTSTDFANELNQFLTT--EMLKQRTLVPS 163
Cdd:PRK05620 93 PLNKQLMNDQIVHIINHAEDEVIVADPRLAEQLGEILK-ECPCVRAVVF---IGPSDADSAAAHMPEgiKVYSYEALLDG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 164 LAT-YAWA---SDDAVVICFTSGTTGRPKGVTISHLAFITQSLAKIAIAGYG--EDDVYLHTSPLVHIGGLSSAMAMLMV 237
Cdd:PRK05620 169 RSTvYDWPeldETTAAAICYSTGTTGAPKGVVYSHRSLYLQSLSLRTTDSLAvtHGESFLCCVPIYHVLSWGVPLAAFMS 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 238 GACHVLL-PKFDAKTALQVMEQNHITCFITVPAMMADLIrvNRTTKNGAENRGVRKILNGGGSLSSELLKE-----AVNI 311
Cdd:PRK05620 249 GTPLVFPgPDLSAPTLAKIIATAMPRVAHGVPTLWIQLM--VHYLKNPPERMSLQEIYVGGSAVPPILIKAweeryGVDV 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 312 FPCarilsaYGMTEacsSLTFMTLHDP--------------TQESFKVT--YPLLNQPkqgtcvgkpaphiELMVKLDED 375
Cdd:PRK05620 327 VHV------WGMTE---TSPVGTVARPpsgvsgearwayrvSQGRFPASleYRIVNDG-------------QVMESTDRN 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 376 SsrvGKILTRGPHTMLRYW----------GHQVAQENVETSESR-SNEAWLDTGDIGAFDEFGNLWLIGRSNGRIKTGGE 444
Cdd:PRK05620 385 E---GEIQVRGNWVTASYYhspteegggaASTFRGEDVEDANDRfTADGWLRTGDVGSVTRDGFLTIHDRARDVIRSGGE 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 445 NVYPEEVEAVLVEHPGIVSAVVIGVIDTRLGEMVVACVRLQEKWIWSdvenrkgsfQLSSETLKHHCRTQnLTGFKIPKR 524
Cdd:PRK05620 462 WIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLAVTVLAPGIEPT---------RETAERLRDQLRDR-LPNWMLPEY 531
|
570 580 590
....*....|....*....|....*....|....
gi 22329863 525 FVrWEKQFPLTTTGKVKRDEVRRQVLS-HFQIMT 557
Cdd:PRK05620 532 WT-FVDEIDKTSVGKFDKKDLRQHLADgDFEIIK 564
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
13-547 |
8.83e-24 |
|
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: 104.82 E-value: 8.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 13 LTRLASVKRNAVV---TVYGNRKRTGREFVDGVLSLAAGLIRLGLRNGDVVSIAAFNSDLFLEWLLAVALVGGVVAPLNY 89
Cdd:cd05915 2 ERAAALFGRKEVVsrlHTGEVHRTTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 90 RWSLKEAKMAMLLVEPVLLVTDETCVSwcidVQNGDIpSLKWRVLMESTSTDFANELNQFLTTEMLKQRTLVPSLATyaw 169
Cdd:cd05915 82 RLSPKEIAYILNHAEDKVLLFDPNLLP----LVEAIR-GELKTVQHFVVMDEKAPEGYLAYEEALGEEADPVRVPER--- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 170 asdDAVVICFTSGTTGRPKGVTISHL-AFITQSLAKIAIAGYGED-DVYLHTSPLVHIGGLSSAMAMLMVGACHVLLPK- 246
Cdd:cd05915 154 ---AACGMAYTTGTTGLPKGVVYSHRaLVLHSLAASLVDGTALSEkDVVLPVVPMFHVNAWCLPYAATLVGAKQVLPGPr 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 247 FDAKTALQVMEQNHITCFITVPAMMADLIRVNRTTKNGAEnrGVRKILNGGGSLSSELLK-------EAVNIFPCARIls 319
Cdd:cd05915 231 LDPASLVELFDGEGVTFTAGVPTVWLALADYLESTGHRLK--TLRRLVVGGSAAPRSLIArfermgvEVRQGYGLTET-- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 320 aYGMTEACSSL-TFMTLhdPTQESFKV-TYPLLNQPKQGTCVGKPAphielMVKLDEDSSRVGKILTRGPHTMLRYWGHQ 397
Cdd:cd05915 307 -SPVVVQNFVKsHLESL--SEEEKLTLkAKTGLPIPLVRLRVADEE-----GRPVPKDGKALGEVQLKGPWITGGYYGNE 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 398 vaqENVETSESRSNEAWldTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGVIDTRLGEM 477
Cdd:cd05915 379 ---EATRSALTPDGFFR--TGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQER 453
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 478 VVACVRLQEkwiwsdVENRKgsfqlssETLKHHCRtQNLTGFKIPKRFVRWEKQFPLTTTGKVKRDEVRR 547
Cdd:cd05915 454 PLAVVVPRG------EKPTP-------EELNEHLL-KAGFAKWQLPDAYVFAEEIPRTSAGKFLKRALRE 509
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
174-542 |
1.86e-23 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 105.63 E-value: 1.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 174 AVVIcFTSGTTGRPKGVTISHLAfITQSLAKIAIA-GYGEDDVYLHTSPLVHIGGLSSAMAMLMVGACHVLLPK---FDA 249
Cdd:PRK12467 659 AYVI-YTSGSTGQPKGVAISHGA-LANYVCVIAERlQLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLPPdcaRDA 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 250 KTALQVMEQNHITCFITVPAMMADLIRVNRTtkngAENRGVRKILNGGGSLSSELLKEAVNIFPCARILSAYGMTEACSS 329
Cdd:PRK12467 737 EAFAALMADQGVTVLKIVPSHLQALLQASRV----ALPRPQRALVCGGEALQVDLLARVRALGPGARLINHYGPTETTVG 812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 330 LTFMTLHDptqesfkvtyplLNQPKQGTCVGKPAPHIELMVkLDEDSSRV-----------GKILTRGPHTMlrywGHQV 398
Cdd:PRK12467 813 VSTYELSD------------EERDFGNVPIGQPLANLGLYI-LDHYLNPVpvgvvgelyigGAGLARGYHRR----PALT 875
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 399 AQENVETSESRSNEAWLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGVIDTRLGEMV 478
Cdd:PRK12467 876 AERFVPDPFGADGGRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAGLQLV 955
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22329863 479 VACVrlqekwiwSDVENRKGSFQLSSETLKHHCRTQnLTGFKIPKRFVrWEKQFPLTTTGKVKR 542
Cdd:PRK12467 956 AYLV--------PAAVADGAEHQATRDELKAQLRQV-LPDYMVPAHLL-LLDSLPLTPNGKLDR 1009
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
5-548 |
3.07e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 103.22 E-value: 3.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 5 SRPHICQCLTRLASVKRNAVVtvYGNRKRTGREFVDGVLSLAAGLIRLGLRNGDV-VSIAAFNSDLFLEWLLAVALVGGV 83
Cdd:PRK07867 3 SAPTVAELLLPLAEDDDRGLY--FEDSFTSWREHIRGSAARAAALRARLDPTRPPhVGVLLDNTPEFSLLLGAAALSGIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 84 VAPLNYRWSLKEAKMAMLLVEPVLLVTDETCVSWCIDVQNGDipslkwRVLmESTSTDFANELNQFLTTEmlkqrtlvPS 163
Cdd:PRK07867 81 PVGLNPTRRGAALARDIAHADCQLVLTESAHAELLDGLDPGV------RVI-NVDSPAWADELAAHRDAE--------PP 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 164 LATYAwaSDDAVVICFTSGTTGRPKGVTISH--LAFITQSLAkiAIAGYGEDDVYLHTSPLVH----IGGLSSAMAmlmV 237
Cdd:PRK07867 146 FRVAD--PDDLFMLIFTSGTSGDPKAVRCTHrkVASAGVMLA--QRFGLGPDDVCYVSMPLFHsnavMAGWAVALA---A 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 238 GACHVLLPKFDAKTALQVMEQNHITCFITVPAMMADLIrvnrTTK---NGAENrgVRKIL--NGGGSLSSELLKEAvniF 312
Cdd:PRK07867 219 GASIALRRKFSASGFLPDVRRYGATYANYVGKPLSYVL----ATPerpDDADN--PLRIVygNEGAPGDIARFARR---F 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 313 PCaRILSAYGMTEACSSLTfmtlhdptqesfkvtypllnqPKQGT---CVGKPAPHIELmvkLDEDSSR----------- 378
Cdd:PRK07867 290 GC-VVVDGFGSTEGGVAIT---------------------RTPDTppgALGPLPPGVAI---VDPDTGTecppaedadgr 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 379 -------VGKIL-TRGPHTMLRYWGhqvaqeNVETSESRSNEAWLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEE 450
Cdd:PRK07867 345 llnadeaIGELVnTAGPGGFEGYYN------DPEADAERMRGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAP 418
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 451 VEAVLVEHPGIVSAVVIGVIDTRLGEMVVACVRLQEkwiwsdvenrkgSFQLSSETLKHHCRTQNLTGFKIPKRFVRWEK 530
Cdd:PRK07867 419 IERILLRYPDATEVAVYAVPDPVVGDQVMAALVLAP------------GAKFDPDAFAEFLAAQPDLGPKQWPSYVRVCA 486
|
570
....*....|....*...
gi 22329863 531 QFPLTTTGKVKRDEVRRQ 548
Cdd:PRK07867 487 ELPRTATFKVLKRQLSAE 504
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
172-548 |
3.61e-23 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 101.28 E-value: 3.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 172 DDAVVICFTSGTTGRPKGVTISHLAFITQSLAKIA-IAGYGEddvYLHTSPLVHIGGLSSAMAMLMVGAchvllpkfdAK 250
Cdd:PRK07824 35 DDVALVVATSGTTGTPKGAMLTAAALTASADATHDrLGGPGQ---WLLALPAHHIAGLQVLVRSVIAGS---------EP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 251 TALQVMEQNHITCFITVPAMM-----------ADLIRVNRTTKNGAENRGVRKILNGGGSLSSELLKEAVNIfpCARILS 319
Cdd:PRK07824 103 VELDVSAGFDPTALPRAVAELgggrrytslvpMQLAKALDDPAATAALAELDAVLVGGGPAPAPVLDAAAAA--GINVVR 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 320 AYGMTEACssltfmtlhdptqesfkvtypllnqpkqGTCV--GKPAPHIELMVkldEDssrvGKILTRGPhtmlrywghQ 397
Cdd:PRK07824 181 TYGMSETS----------------------------GGCVydGVPLDGVRVRV---ED----GRIALGGP---------T 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 398 VAQ--ENVETSESRSNEAWLDTGDIGAFDEfGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGVIDTRLG 475
Cdd:PRK07824 217 LAKgyRNPVDPDPFAEPGWFRTDDLGALDD-GVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLG 295
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22329863 476 EMVVACVRLQEKWiwsdvenrkgsfqlsSETL----KHHCRTqnLTGFKIPKRFVRWEkQFPLTTTGKVKRDEVRRQ 548
Cdd:PRK07824 296 QRVVAAVVGDGGP---------------APTLealrAHVART--LDRTAAPRELHVVD-ELPRRGIGKVDRRALVRR 354
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
174-542 |
2.32e-22 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 102.34 E-value: 2.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 174 AVVIcFTSGTTGRPKGVTISHLAFITQSLAKIAIAGYGEDDVYLHTSPLVHIGGLSSAMAMLMVGAChVLLPK---FDAK 250
Cdd:PRK12316 4697 AYVI-YTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLINGAS-VVIRDdslWDPE 4774
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 251 TALQVMEQNHITCFITVPAMMADLIrvnrttkNGAENRG----VRKILNGGGSLSSELLKEAVNIFPCARILSAYGMTEA 326
Cdd:PRK12316 4775 RLYAEIHEHRVTVLVFPPVYLQQLA-------EHAERDGeppsLRVYCFGGEAVAQASYDLAWRALKPVYLFNGYGPTET 4847
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 327 CSSLTFMTLHDPTQESfKVTYPLlnqpkqGTCVGKPAPHIeLMVKLDEDSSRVGKILTRGPHTMLR-YWGHQ--VAQENV 403
Cdd:PRK12316 4848 TVTVLLWKARDGDACG-AAYMPI------GTPLGNRSGYV-LDGQLNPLPVGVAGELYLGGEGVARgYLERPalTAERFV 4919
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 404 ETSESRSNEAWLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGViDTRLGEMVVACVR 483
Cdd:PRK12316 4920 PDPFGAPGGRLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQ-EGAVGKQLVGYVV 4998
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 22329863 484 LQEKWIWSDVENRKGSFQlsseTLKHHCRTqNLTGFKIPKRFVRWEKqFPLTTTGKVKR 542
Cdd:PRK12316 4999 PQDPALADADEAQAELRD----ELKAALRE-RLPEYMVPAHLVFLAR-MPLTPNGKLDR 5051
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
171-482 |
3.47e-22 |
|
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: 99.46 E-value: 3.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 171 SDDAVVICFTSGTTGRPKGVTISHLAFITQSLAKIAIAGYGEDDVYLHTSPLVHIggLSSAMAMLMVgachvlLPKFDAK 250
Cdd:cd05910 84 ADEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGEVDLATFPLFAL--FGPALGLTSV------IPDMDPT 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 251 TALQV--------MEQNHITCFITVPAMMADLIRVNRTtkNGAENRGVRKILNGGGSL---SSELLKEAVNifPCARILS 319
Cdd:cd05910 156 RPARAdpqklvgaIRQYGVSIVFGSPALLERVARYCAQ--HGITLPSLRRVLSAGAPVpiaLAARLRKMLS--DEAEILT 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 320 AYGMTEAcssLTFMTLHDPTQESFKVTYPllnQPKQGTCVGKPAPHIELMV-------------KLDEDSSRVGKILTRG 386
Cdd:cd05910 232 PYGATEA---LPVSSIGSRELLATTTAAT---SGGAGTCVGRPIPGVRVRIieiddepiaewddTLELPRGEIGEITVTG 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 387 PHTMLRYWGHQVAQENVETSESrSNEAWLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVV 466
Cdd:cd05910 306 PTVTPTYVNRPVATALAKIDDN-SEGFWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSAL 384
|
330
....*....|....*.
gi 22329863 467 IGViDTRLGEMVVACV 482
Cdd:cd05910 385 VGV-GKPGCQLPVLCV 399
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
31-548 |
5.69e-22 |
|
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: 98.97 E-value: 5.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 31 RKRTGREFVDGVLSLAAGLIRLGLRNGDVVSIAAFNSDLFLEWLLAVALVGGVVAPLNYRWSLKEAKMAMLLVEPVLLVT 110
Cdd:cd05940 2 EALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 111 DetcvswcidvqngdipslkwrvlmeststdfanelnqflttemlkqrtlvpslatyawasddAVVICFTSGTTGRPKGV 190
Cdd:cd05940 82 D--------------------------------------------------------------AALYIYTSGTTGLPKAA 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 191 TISHLAFITQSLAKIAIAGYGEDDVYLHTSPLVHIGGLSSAM-AMLMVGACHVLLPKFDAKTALQVMEQNHITCFITVpa 269
Cdd:cd05940 100 IISHRRAWRGGAFFAGSGGALPSDVLYTCLPLYHSTALIVGWsACLASGATLVIRKKFSASNFWDDIRKYQATIFQYI-- 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 270 mmADLIRVNRTTKNGAENRG--VRKILngGGSLSSELLKEAVNIFPCARILSAYGMTEACSSLTfmtlhdptqesfkvty 347
Cdd:cd05940 178 --GELCRYLLNQPPKPTERKhkVRMIF--GNGLRPDIWEEFKERFGVPRIAEFYAATEGNSGFI---------------- 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 348 PLLNQPkqGTCVGKPAPHIELM----VKLDEDSSR--------------------VGKILTRGPHTmlRYWGHQVAQENV 403
Cdd:cd05940 238 NFFGKP--GAIGRNPSLLRKVAplalVKYDLESGEpirdaegrcikvprgepgllISRINPLEPFD--GYTDPAATEKKI 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 404 ETSESRSNEAWLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGV----IDTRLGemvV 479
Cdd:cd05940 314 LRDVFKKGDAWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVqvpgTDGRAG---M 390
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22329863 480 ACVRLQEkwiwsdvenrKGSFQLSSetLKHHCrTQNLTGFKIPkRFVRWEKQFPLTTTGKVKRDEVRRQ 548
Cdd:cd05940 391 AAIVLQP----------NEEFDLSA--LAAHL-EKNLPGYARP-LFLRLQPEMEITGTFKQQKVDLRNE 445
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
170-547 |
1.22e-21 |
|
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: 97.64 E-value: 1.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 170 ASDDAVVICFTSGTTGRPKGVTISHLAFITQSLAKIAIAGYGEDDVYLH-TSPLVHIGGLSSAMAMLMVGACHVLL--PK 246
Cdd:cd05974 83 HADDPMLLYFTSGTTSKPKLVEHTHRSYPVGHLSTMYWIGLKPGDVHWNiSSPGWAKHAWSCFFAPWNAGATVFLFnyAR 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 247 FDAKTALQVMEQNHITCFITVPAMMADLIRVNRTTKNgaenRGVRKILNGGGSLSSELLkEAVNIFPCARILSAYGMTEA 326
Cdd:cd05974 163 FDAKRVLAALVRYGVTTLCAPPTVWRMLIQQDLASFD----VKLREVVGAGEPLNPEVI-EQVRRAWGLTIRDGYGQTET 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 327 csslTFMTLHDPtqesfkvtypllNQPKQGTCVGKPAPHIELMVkLDEDSSRV--GKIL-----TRGPHTMLRYWGHQVA 399
Cdd:cd05974 238 ----TALVGNSP------------GQPVKAGSMGRPLPGYRVAL-LDPDGAPAteGEVAldlgdTRPVGLMKGYAGDPDK 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 400 qenveTSESRSNeAWLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGVIDTRLGEMVV 479
Cdd:cd05974 301 -----TAHAMRG-GYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPK 374
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22329863 480 ACVRLQEKWIWSDvENRKGSFQLSSETLKHHCRTQNLTGFKIPKrfvrwekqfplTTTGKVKRDEVRR 547
Cdd:cd05974 375 AFIVLRAGYEPSP-ETALEIFRFSRERLAPYKRIRRLEFAELPK-----------TISGKIRRVELRR 430
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
171-542 |
1.50e-21 |
|
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: 97.39 E-value: 1.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 171 SDDAVVICFTSGTTGRPKGVTISH---LAFItqslaKIAIAGYGEDD---VYLHTSplvhIG-GLS--SAMAMLMVGACH 241
Cdd:cd12115 104 PDDLAYVIYTSGSTGRPKGVAIEHrnaAAFL-----QWAAAAFSAEElagVLASTS----ICfDLSvfELFGPLATGGKV 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 242 VL----LPKFDAKTALQVMEQNhitcfiTVPAMMADLIRVNrttkngAENRGVRKILNGGGSLSSELLKEAVNIFPCARI 317
Cdd:cd12115 175 VLadnvLALPDLPAAAEVTLIN------TVPSAAAELLRHD------ALPASVRVVNLAGEPLPRDLVQRLYARLQVERV 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 318 LSAYGMTEACsslTFMTLHdptqesfkvtyPLLNQPKQGTCVGKPAPHIELMVkLDEDSSRV-----GKILTRGPHTMLR 392
Cdd:cd12115 243 VNLYGPSEDT---TYSTVA-----------PVPPGASGEVSIGRPLANTQAYV-LDRALQPVplgvpGELYIGGAGVARG 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 393 YWGHQVAqenveTSES------RSNEAWLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVV 466
Cdd:cd12115 308 YLGRPGL-----TAERflpdpfGPGARLYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVV 382
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22329863 467 IGVIDTRLGEMVVACVRLqekwiwsdvenrKGSFQLSSETLKHHCRTQnLTGFKIPKRFVRWEkQFPLTTTGKVKR 542
Cdd:cd12115 383 VAIGDAAGERRLVAYIVA------------EPGAAGLVEDLRRHLGTR-LPAYMVPSRFVRLD-ALPLTPNGKIDR 444
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
8-542 |
2.48e-21 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 98.88 E-value: 2.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 8 HICQCLTRLASVKRNAVVTVYGNRKRTGREFVDGVLSLAAGLIRLGLRNGDVVSIAAFNSDLFLEWLLAVALVGGVVAPL 87
Cdd:PRK12316 3058 GVHRLFEEQVERTPDAVALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPL 3137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 88 NYRWS-------LKEAKMAMLLVEPVLLVTDETCVswcidvqngdipslkwRVLMESTSTDFANELNqflttemLKQRTL 160
Cdd:PRK12316 3138 DPEYPeerlaymLEDSGAQLLLSQSHLRLPLAQGV----------------QVLDLDRGDENYAEAN-------PAIRTM 3194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 161 VPSLAtyawasddavVICFTSGTTGRPKGVTISHLAFITQSLAKIAIAGYGEDDVYLHTSPLVHIGGLSSAMAMLMVGAC 240
Cdd:PRK12316 3195 PENLA----------YVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGAR 3264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 241 HVLLPKFDAKTALQVMEQNHITCfITVPAMMADLIRVNRTTKNGAENRGVRKILNGGGSLSSELLKEAVNIFPcarILSA 320
Cdd:PRK12316 3265 VVLAGPEDWRDPALLVELINSEG-VDVLHAYPSMLQAFLEEEDAHRCTSLKRIVCGGEALPADLQQQVFAGLP---LYNL 3340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 321 YGMTEACSSLTFMTLHDPTQESFKVTYP-------LLNQPKQGTCVGKPAphiELMVKldedssrvGKILTRGPHTMlry 393
Cdd:PRK12316 3341 YGPTEATITVTHWQCVEEGKDAVPIGRPianracyILDGSLEPVPVGALG---ELYLG--------GEGLARGYHNR--- 3406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 394 wgHQVAQENVETSESRSNEAWLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGVIDTR 473
Cdd:PRK12316 3407 --PGLTAERFVPDPFVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLAVDGRQ 3484
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22329863 474 LGEMVVAcvrlqekwiwsdvENRKGSFQlssETLKHHCRtQNLTGFKIPKRFVRWEKqFPLTTTGKVKR 542
Cdd:PRK12316 3485 LVAYVVP-------------EDEAGDLR---EALKAHLK-ASLPEYMVPAHLLFLER-MPLTPNGKLDR 3535
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
171-551 |
4.12e-21 |
|
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: 96.46 E-value: 4.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 171 SDDAVVICFTSGTTGRPKGVTISHLAFITQSLAKIAIAGYGEDDVYLHTSPL---VHIGglsSAMAMLMVGACHVLLPKF 247
Cdd:cd05918 105 PSDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRALGLTSESRVLQFASYtfdVSIL---EIFTTLAAGGCLCIPSEE 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 248 DAKTALQ-VMEQNHIT-CFITvPAmMADLIrvnrttkNGAENRGVRKILNGGgslssELLKEA-VNIF-PCARILSAYGM 323
Cdd:cd05918 182 DRLNDLAgFINRLRVTwAFLT-PS-VARLL-------DPEDVPSLRTLVLGG-----EALTQSdVDTWaDRVRLINAYGP 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 324 TEACsslTFMTLHDPTQESfkvTYPLLNQPKQGTC-VGKPAPHIELmVKLDEdssrVGKILTRGPhtmlrywghQVAQE- 401
Cdd:cd05918 248 AECT---IAATVSPVVPST---DPRNIGRPLGATCwVVDPDNHDRL-VPIGA----VGELLIEGP---------ILARGy 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 402 ---NVETSESR-SNEAWLD------------TGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAV 465
Cdd:cd05918 308 lndPEKTAAAFiEDPAWLKqegsgrgrrlyrTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSLPGAKEV 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 466 VIGVI---DTRLGEMVVACVRLQEkwiwSDVENRKGS---------FQLSSETLKHHCRtQNLTGFKIPKRFVRWeKQFP 533
Cdd:cd05918 388 VVEVVkpkDGSSSPQLVAFVVLDG----SSSGSGDGDslflepsdeFRALVAELRSKLR-QRLPSYMVPSVFLPL-SHLP 461
|
410
....*....|....*...
gi 22329863 534 LTTTGKVKRDEVRRQVLS 551
Cdd:cd05918 462 LTASGKIDRRALRELAES 479
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
17-534 |
8.73e-21 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 95.32 E-value: 8.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 17 ASVKRNAVVTVYGNRKRTGREFVDGVLSLAAGLIRLGLRNGDVVSIAAFNS-DLFLEWLLAVALvGGVVAPLNYrwSLKE 95
Cdd:PRK09029 13 AQVRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSpETLLAYLALLQC-GARVLPLNP--QLPQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 96 AKMAMLLvepvllvtdetcvswcidvqngdiPSLkwrvlmestSTDFANELNQFLTTEMLKQRTLVPSLATYA--WASDD 173
Cdd:PRK09029 90 PLLEELL------------------------PSL---------TLDFALVLEGENTFSALTSLHLQLVEGAHAvaWQPQR 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 174 AVVICFTSGTTGRPKGV--TIS-HLAFITQSLAKIAiagYGEDDVYLHTSPLVHIGGLSSAMAMLMVGACHVLLPKFDAK 250
Cdd:PRK09029 137 LATMTLTSGSTGLPKAAvhTAQaHLASAEGVLSLMP---FTAQDSWLLSLPLFHVSGQGIVWRWLYAGATLVVRDKQPLE 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 251 TALQVMeqNHitcfitvpammADLI--RVNRTTKNGAENRGVRKILNGGGSLSSELLKEAV--NIfpcaRILSAYGMTEA 326
Cdd:PRK09029 214 QALAGC--TH-----------ASLVptQLWRLLDNRSEPLSLKAVLLGGAAIPVELTEQAEqqGI----RCWCGYGLTEM 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 327 CSSLTfmtlhdptqesfkvtyPLLNQPKQGtcVGKPAPHIELMVKLDEdssrvgkILTRGPHTMLRYW--GHQVAQENve 404
Cdd:PRK09029 277 ASTVC----------------AKRADGLAG--VGSPLPGREVKLVDGE-------IWLRGASLALGYWrqGQLVPLVN-- 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 405 tsesrsNEAWLDTGDIGAFDEfGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGVIDTRLGEMVVACVRL 484
Cdd:PRK09029 330 ------DEGWFATRDRGEWQN-GELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVPVADAEFGQRPVAVVES 402
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 22329863 485 qekwiwsdvenrkgSFQLSSETLKHHCRTQnLTGFKIPkrfVRWekqFPL 534
Cdd:PRK09029 403 --------------DSEAAVVNLAEWLQDK-LARFQQP---VAY---YLL 431
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
34-468 |
1.33e-20 |
|
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: 95.50 E-value: 1.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 34 TGREFVDGVLSLAAGLIRLGLRNGDVVSIAAFNSDlflEWLLA---VALVGGVVA-------PLNYRWSLKEAKMAMLLV 103
Cdd:cd05933 10 TYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSP---EWFIAavgAIFAGGIAVgiyttnsPEACQYVAETSEANILVV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 104 E------PVLLVTD-----ETCVSWCIDVQNGDIPSLKWRVLMESTSTDFANELNQFLTTEMLKQrtlvpslatyawasd 172
Cdd:cd05933 87 EnqkqlqKILQIQDklphlKAIIQYKEPLKEKEPNLYSWDEFMELGRSIPDEQLDAIISSQKPNQ--------------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 173 dAVVICFTSGTTGRPKGVTISH--LAFITQSLAK---IAIAGYGEDDV--YLhtsPLVHIGG-LSSAMAMLMVGAChVLL 244
Cdd:cd05933 152 -CCTLIYTSGTTGMPKGVMLSHdnITWTAKAASQhmdLRPATVGQESVvsYL---PLSHIAAqILDIWLPIKVGGQ-VYF 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 245 PKFDA--KTALQVMEQNHITCFITVP---------------------------AMMADLiRVNRTTKNGAEN-------- 287
Cdd:cd05933 227 AQPDAlkGTLVKTLREVRPTAFMGVPrvwekiqekmkavgaksgtlkrkiaswAKGVGL-ETNLKLMGGESPsplfyrla 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 288 -----RGVRKIL---------NGGGSLSSELLK--EAVNIfpcaRILSAYGMTEaCSSLTFMTLhdptQESFKVTyplln 351
Cdd:cd05933 306 kklvfKKVRKALgldrcqkffTGAAPISRETLEffLSLNI----PIMELYGMSE-TSGPHTISN----PQAYRLL----- 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 352 qpkqgTCvGKPAPHIELMVkLDEDSSRVGKILTRGPHTMLRYWGHQVaqenvETSESRSNEAWLDTGDIGAFDEFGNLWL 431
Cdd:cd05933 372 -----SC-GKALPGCKTKI-HNPDADGIGEICFWGRHVFMGYLNMED-----KTEEAIDEDGWLHSGDLGKLDEDGFLYI 439
|
490 500 510
....*....|....*....|....*....|....*....
gi 22329863 432 IGRSNGRIKT-GGENVYPEEVE-AVLVEHPGIVSAVVIG 468
Cdd:cd05933 440 TGRIKELIITaGGENVPPVPIEdAVKKELPIISNAMLIG 478
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
36-545 |
1.34e-20 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 95.06 E-value: 1.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 36 REFVDGVLSLAAGLIRLGLRNGDVVSIAAFNSDLFLEWLLAVALVGGVVAPLNYRWSLKEAKMAMLLVEPVLLVTDETCV 115
Cdd:PRK13383 64 RELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAALRAHHISTVVADNEFA 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 116 SwcidvqngDIPSLKWRVLMESTSTDFANElnqflttemlkqrtlvpSLATYAWASDDAVVIcFTSGTTGRPKGVTIShl 195
Cdd:PRK13383 144 E--------RIAGADDAVAVIDPATAGAEE-----------------SGGRPAVAAPGRIVL-LTSGTTGKPKGVPRA-- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 196 afiTQSLAKIAIAGYGEDDVYLHT-------SPLVHigGLSSAMAMLMVGACHVLLPK--FDAKTALQVMEQNHITCFIT 266
Cdd:PRK13383 196 ---PQLRSAVGVWVTILDRTRLRTgsrisvaMPMFH--GLGLGMLMLTIALGGTVLTHrhFDAEAALAQASLHRADAFTA 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 267 VPAMMADLIRVNRTTKNGAENRGVRKILNGGGSLSSELLKEAVNIFpcARIL-SAYGMTEacssLTFMTLHDPTQesfkv 345
Cdd:PRK13383 271 VPVVLARILELPPRVRARNPLPQLRVVMSSGDRLDPTLGQRFMDTY--GDILyNGYGSTE----VGIGALATPAD----- 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 346 typLLNQPKQgtcVGKPAPHIELMVkLDEDSSRV-----GKILTRGPHTMLRYWGHqvaqenvetsesrSNEAWLD---- 416
Cdd:PRK13383 340 ---LRDAPET---VGKPVAGCPVRI-LDRNNRPVgprvtGRIFVGGELAGTRYTDG-------------GGKAVVDgmts 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 417 TGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGVIDTRLGEMVVACVRLqekwiwsdvenR 496
Cdd:PRK13383 400 TGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVL-----------H 468
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 22329863 497 KGSfQLSSETLKHHCRTQnLTGFKIPkRFVRWEKQFPLTTTGKVKRDEV 545
Cdd:PRK13383 469 PGS-GVDAAQLRDYLKDR-VSRFEQP-RDINIVSSIPRNPTGKVLRKEL 514
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
45-542 |
2.63e-20 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 95.79 E-value: 2.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 45 LAAGLIRLGLRNGDVVSIAAFNSDLFLEWLLAVALVGGVVAPLNYRWS-------LKEAKMAMLLVEPVLLvtDETCVSW 117
Cdd:PRK12316 549 LAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPaerlaymLEDSGVQLLLSQSHLG--RKLPLAA 626
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 118 CIDVQNGDIPSLkWrvlMESTSTdfaNELNQFLTTEMLkqrtlvpslatyawasddAVVIcFTSGTTGRPKGVTISHLAF 197
Cdd:PRK12316 627 GVQVLDLDRPAA-W---LEGYSE---ENPGTELNPENL------------------AYVI-YTSGSTGKPKGAGNRHRAL 680
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 198 ITQSLAKIAIAGYGEDDVYLHTSPLVHIGGLSSAMAMLMVGACHVLLPKFDAKTAL---QVMEQNHITCFITVPAMMADL 274
Cdd:PRK12316 681 SNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAklvELINREGVDTLHFVPSMLQAF 760
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 275 IRVNRTtkngAENRGVRKILNGGGSLSSELLKEAVNIFPCARILSAYGMTEACSSLTFMTLHDPTQESFKVTYPLLN--- 351
Cdd:PRK12316 761 LQDEDV----ASCTSLRRIVCSGEALPADAQEQVFAKLPQAGLYNLYGPTEAAIDVTHWTCVEEGGDSVPIGRPIANlac 836
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 352 -------QPKQGTCVGkpaphiELMVkldedssrVGKILTRGPH-----TMLRYwghqVAqenvetSESRSNEAWLDTGD 419
Cdd:PRK12316 837 yildanlEPVPVGVLG------ELYL--------AGRGLARGYHgrpglTAERF----VP------SPFVAGERMYRTGD 892
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 420 IGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGVIDTRLGEMVVAcvrlqekwiwsdvENRKGS 499
Cdd:PRK12316 893 LARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDGKQLVGYVVL-------------ESEGGD 959
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 22329863 500 FQlssETLKHHCRtQNLTGFKIPKRFVRWEkQFPLTTTGKVKR 542
Cdd:PRK12316 960 WR---EALKAHLA-ASLPEYMVPAQWLALE-RLPLTPNGKLDR 997
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
44-468 |
3.23e-20 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 94.40 E-value: 3.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 44 SLAAGLIRLGLRNGDVVSIAAFNSDlflEWLL---AVALVGGVVAPLnY--------RWSLKEAKMAMLLVEPVLLVTDE 112
Cdd:PLN02736 90 AIGSGLVQHGIPKGACVGLYFINRP---EWLIvdhACSAYSYVSVPL-YdtlgpdavKFIVNHAEVAAIFCVPQTLNTLL 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 113 TCVSwcidvqngDIPSLKWRV-------LMESTSTDFANEL---NQFLTTEMLKQRTLVPSlatyawASDDAVVICFTSG 182
Cdd:PLN02736 166 SCLS--------EIPSVRLIVvvggadePLPSLPSGTGVEIvtySKLLAQGRSSPQPFRPP------KPEDVATICYTSG 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 183 TTGRPKGVTISHLAFITQSLAKIAIAGYGEDDVYLHTSPLVHIGGLSSAMAMLMVGAChVLLPKFDAKTALQVMEQNHIT 262
Cdd:PLN02736 232 TTGTPKGVVLTHGNLIANVAGSSLSTKFYPSDVHISYLPLAHIYERVNQIVMLHYGVA-VGFYQGDNLKLMDDLAALRPT 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 263 CFITVP--------AMMA----------DLIRVNRTTKNGAENRG----------------------VRKILNGGGSLSS 302
Cdd:PLN02736 311 IFCSVPrlynriydGITNavkesgglkeRLFNAAYNAKKQALENGknpspmwdrlvfnkikaklggrVRFMSSGASPLSP 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 303 ELLkEAVNIFPCARILSAYGMTEACSSLTFMTLHDPTQESfkvtypllnqpkqgtcVGKPAPHIElmVKL---------- 372
Cdd:PLN02736 391 DVM-EFLRICFGGRVLEGYGMTETSCVISGMDEGDNLSGH----------------VGSPNPACE--VKLvdvpemnyts 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 373 -DEDSSRvGKILTRGPHTMLRYWghqvaQENVETSESRSNEAWLDTGDIGAFDEFGNLWLIGRSNGRIKTG-GENVYPEE 450
Cdd:PLN02736 452 eDQPYPR-GEICVRGPIIFKGYY-----KDEVQTREVIDEDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLAqGEYIAPEK 525
|
490
....*....|....*...
gi 22329863 451 VEAVLVEHPGIVSAVVIG 468
Cdd:PLN02736 526 IENVYAKCKFVAQCFVYG 543
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
28-548 |
3.89e-20 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 93.94 E-value: 3.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 28 YGNRKRTGREFVDGVLSLAAGLIrlGLRNGDV---VSIAAFNSDLFLEWLLAVALVGGVVAPLNYRWSLKEAKMAMLLVE 104
Cdd:PRK13388 22 YGDRTWTWREVLAEAAARAAALI--ALADPDRplhVGVLLGNTPEMLFWLAAAALGGYVLVGLNTTRRGAALAADIRRAD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 105 PVLLVTDETCVSWCIDVqngDIPSLkwRVLMesTSTDFANELnqfltteMLKQRTLVPSLATYAwasDDAVVICFTSGTT 184
Cdd:PRK13388 100 CQLLVTDAEHRPLLDGL---DLPGV--RVLD--VDTPAYAEL-------VAAAGALTPHREVDA---MDPFMLIFTSGTT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 185 GRPKGVTISH--LAFITQSLAkiaiAGYG--EDDVYLHTSPLVHIGGLSSAMA-MLMVGACHVLLPKFDAKTALQVMEQN 259
Cdd:PRK13388 163 GAPKAVRCSHgrLAFAGRALT----ERFGltRDDVCYVSMPLFHSNAVMAGWApAVASGAAVALPAKFSASGFLDDVRRY 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 260 HITCFITVPAMMAdLIRVNRTTKNGAENRGVRKIlngGGSLSSELLKEAVNIFPCaRILSAYGMTEACSSLTfmtlHDPt 339
Cdd:PRK13388 239 GATYFNYVGKPLA-YILATPERPDDADNPLRVAF---GNEASPRDIAEFSRRFGC-QVEDGYGSSEGAVIVV----REP- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 340 qesfkvtypllNQPKqgTCVGKPAPHIELM----------VKLDED------SSRVGKIL-TRGPHTMLRYWGHQVAqen 402
Cdd:PRK13388 309 -----------GTPP--GSIGRGAPGVAIYnpetltecavARFDAHgallnaDEAIGELVnTAGAGFFEGYYNNPEA--- 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 403 veTSEsRSNEAWLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGVIDTRLGEMVVACV 482
Cdd:PRK13388 373 --TAE-RMRHGMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVGDQVMAAL 449
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22329863 483 RLQEKwiwsdvenrkGSFqlSSETLKHHCRTQNLTGFKIPKRFVRWEKQFPLTTTGKVKRDEVRRQ 548
Cdd:PRK13388 450 VLRDG----------ATF--DPDAFAAFLAAQPDLGTKAWPRYVRIAADLPSTATNKVLKRELIAQ 503
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
172-543 |
4.60e-20 |
|
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: 93.14 E-value: 4.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 172 DDAVVICFTSGTTGRPKGVTISHLAFITQSLAKIAIAGYGEDDVYL--HTS-----------PLVHIGGLssamamlmvg 238
Cdd:cd17643 93 DDLAYVIYTSGSTGRPKGVVVSHANVLALFAATQRWFGFNEDDVWTlfHSYafdfsvweiwgALLHGGRL---------- 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 239 achVLLPKFDAKTA---LQVMEQNHITCFITVPAMMADLIRVNRttKNGAENRGVRKILNGGGSLSSELLKEAVNIF--P 313
Cdd:cd17643 163 ---VVVPYEVARSPedfARLLRDEGVTVLNQTPSAFYQLVEAAD--RDGRDPLALRYVIFGGEALEAAMLRPWAGRFglD 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 314 CARILSAYGMTEACSSLTFmtlhdptqesfkvtYPLLNQ---PKQGTCVGKPAPHIELMVkLDED-----SSRVGKILTR 385
Cdd:cd17643 238 RPQLVNMYGITETTVHVTF--------------RPLDAAdlpAAAASPIGRPLPGLRVYV-LDADgrpvpPGVVGELYVS 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 386 GPhtmlrywghQVAQ----ENVETSES-RSNEAWLD------TGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAV 454
Cdd:cd17643 303 GA---------GVARgylgRPELTAERfVANPFGGPgsrmyrTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAA 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 455 LVEHPGIVSAVVIGVIDTRLGEMVVACVRLQEkwiwsdvenrkGSFQLSSEtLKHHCRTqNLTGFKIPKRFVRWEkQFPL 534
Cdd:cd17643 374 LATHPSVRDAAVIVREDEPGDTRLVAYVVADD-----------GAAADIAE-LRALLKE-LLPDYMVPARYVPLD-ALPL 439
|
....*....
gi 22329863 535 TTTGKVKRD 543
Cdd:cd17643 440 TVNGKLDRA 448
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
22-554 |
1.26e-19 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 93.69 E-value: 1.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 22 NAVVTVYGNRKRTGREFVDGVLSLAAGLIRLGLRNGDVVSIAAFNSDLFLEWLLAVALVGGVVAPLNYRWS-------LK 94
Cdd:PRK12467 1589 EAVALVFGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPrerlaymIE 1668
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 95 EAKMAMLLVEPVLLVTdetcvswcIDVQNGdIPSLkwrvlmeststdFANELNQFLTTEMLKQRTLVPSLATYAWasdda 174
Cdd:PRK12467 1669 DSGIELLLTQSHLQAR--------LPLPDG-LRSL------------VLDQEDDWLEGYSDSNPAVNLAPQNLAY----- 1722
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 175 vVIcFTSGTTGRPKGVTISHLAFITQSLAKIAIAGYGEDDVYLHTSPLVHIGGLSSAMAMLMVGACHVLLP---KFDAKT 251
Cdd:PRK12467 1723 -VI-YTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTSFAFDVSVWELFWPLINGARLVIAPpgaHRDPEQ 1800
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 252 ALQVMEQNHITCFITVPAMMADLIRVNRTTkngAENRGVRKILNGGGSLSSELLKEAVNIFPCARILSAYGMTEACSSLT 331
Cdd:PRK12467 1801 LIQLIERQQVTTLHFVPSMLQQLLQMDEQV---EHPLSLRRVVCGGEALEVEALRPWLERLPDTGLFNLYGPTETAVDVT 1877
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 332 FMTLHdptqesfkvtyplLNQPKQGTCV--GKPAPHIELMVkLDEDSSRV-----------GKILTRGPH-----TMLRY 393
Cdd:PRK12467 1878 HWTCR-------------RKDLEGRDSVpiGQPIANLSTYI-LDASLNPVpigvagelylgGVGLARGYLnrpalTAERF 1943
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 394 wghqvaqenVETSESRSNEAWLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIgVIDTR 473
Cdd:PRK12467 1944 ---------VADPFGTVGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVI-AQDGA 2013
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 474 LGEMVVA-CVRLQEKWIWSDVenRKGSFQlssETLKHHCRTQnLTGFKIPKRFVRWEKqFPLTTTGKVKRDEVRRQVLSH 552
Cdd:PRK12467 2014 NGKQLVAyVVPTDPGLVDDDE--AQVALR---AILKNHLKAS-LPEYMVPAHLVFLAR-MPLTPNGKLDRKALPAPDASE 2086
|
..
gi 22329863 553 FQ 554
Cdd:PRK12467 2087 LQ 2088
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
31-486 |
1.62e-19 |
|
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: 92.38 E-value: 1.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 31 RKRTGREFVDGVLSLAAGLIRLGLRNGDVVSI-------AAFNsdlflewLLAVALVGGVVAPLNYRWSLKEAKMAMLLV 103
Cdd:cd05967 81 RTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIympmipeAAIA-------MLACARIGAIHSVVFGGFAAKELASRIDDA 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 104 EPVLLVT-----------------DE--TCVSW----CIDVQNGDIPSLKWRVLmesTSTDFAnelnqflttEMLKQRTL 160
Cdd:cd05967 154 KPKLIVTascgiepgkvvpykpllDKalELSGHkphhVLVLNRPQVPADLTKPG---RDLDWS---------ELLAKAEP 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 161 VPslatYAW-ASDDAVVICFTSGTTGRPKGV---TISHLAFITQSLAKIAiaGYGEDDVYLHTSPLVHIGGLS-SAMAML 235
Cdd:cd05967 222 VD----CVPvAATDPLYILYTSGTTGKPKGVvrdNGGHAVALNWSMRNIY--GIKPGDVWWAASDVGWVVGHSyIVYGPL 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 236 MVGACHVL---LPKF--DAKTALQVMEQNHITCFITVP-AMMAdlIRvnRTTKNGAENRGV-----RKILNGGGSLSSEL 304
Cdd:cd05967 296 LHGATTVLyegKPVGtpDPGAFWRVIEKYQVNALFTAPtAIRA--IR--KEDPDGKYIKKYdlsslRTLFLAGERLDPPT 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 305 LKEAVNIFPCArILSAYGMTEACSSLTfmtlhdptqESFKVTYPLlnQPKQGTcVGKPAPHIELMVkLDEDSSRV----- 379
Cdd:cd05967 372 LEWAENTLGVP-VIDHWWQTETGWPIT---------ANPVGLEPL--PIKAGS-PGKPVPGYQVQV-LDEDGEPVgpnel 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 380 GKILTRGP---HTMLRYWGHQVAQENVETSESRsneAWLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLV 456
Cdd:cd05967 438 GNIVIKLPlppGCLLTLWKNDERFKKLYLSKFP---GYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVL 514
|
490 500 510
....*....|....*....|....*....|
gi 22329863 457 EHPGIVSAVVIGVIDTRLGEMVVACVRLQE 486
Cdd:cd05967 515 SHPAVAECAVVGVRDELKGQVPLGLVVLKE 544
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
158-547 |
4.05e-19 |
|
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: 89.88 E-value: 4.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 158 RTLVPSLATYAWASDDAVVICFTSGTTGRPKGVTI---SHLAFitQSLAKIAIaGYGEDDVYLHTSPLVHIGGLSSAM-A 233
Cdd:cd05973 74 RLVVTDAANRHKLDSDPFVMMFTSGTTGLPKGVPVplrALAAF--GAYLRDAV-DLRPEDSFWNAADPGWAYGLYYAItG 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 234 MLMVGACHVLLP-KFDAKTALQVMEQNHITCFITVPAMMADLIRVNRTTKNGAENRgVRKILNGGGSLSSELLKEAVNIF 312
Cdd:cd05973 151 PLALGHPTILLEgGFSVESTWRVIERLGVTNLAGSPTAYRLLMAAGAEVPARPKGR-LRRVSSAGEPLTPEVIRWFDAAL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 313 PCArILSAYGMTEacssltfmtLHDPTQESFKVTYPLlnqpKQGTcVGKPAPHIELMVkLDEDSSRVGK------ILTRG 386
Cdd:cd05973 230 GVP-IHDHYGQTE---------LGMVLANHHALEHPV----HAGS-AGRAMPGWRVAV-LDDDGDELGPgepgrlAIDIA 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 387 PHTMLRYWGHQvaqeNVETSESRSNeaWLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVV 466
Cdd:cd05973 294 NSPLMWFRGYQ----LPDTPAIDGG--YYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAV 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 467 IGVIDTRLGEMVVACVRLQekwiwsdvENRKGSFQLSSEtLKHHCRTQnLTGFKIPkRFVRWEKQFPLTTTGKVKRDEVR 546
Cdd:cd05973 368 IGVPDPERTEVVKAFVVLR--------GGHEGTPALADE-LQLHVKKR-LSAHAYP-RTIHFVDELPKTPSGKIQRFLLR 436
|
.
gi 22329863 547 R 547
Cdd:cd05973 437 R 437
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
171-478 |
4.18e-19 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 90.84 E-value: 4.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 171 SDDAVVICFTSGTTGRPKGVTISHLAFIT-------QSLAKIA-IAGygeDDVYlhtSPL--VHIGGLSSAMAMLMVGAC 240
Cdd:PRK05857 168 SEDPLAMIFTSGTTGEPKAVLLANRTFFAvpdilqkEGLNWVTwVVG---ETTY---SPLpaTHIGGLWWILTCLMHGGL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 241 HVLLPKFDAkTALQVMEQNHITCFITVPAMMADLirVNRTTKNGAENRGVRKILNGGgslsSELLKEAVNIFPCARILSA 320
Cdd:PRK05857 242 CVTGGENTT-SLLEILTTNAVATTCLVPTLLSKL--VSELKSANATVPSLRLVGYGG----SRAIAADVRFIEATGVRTA 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 321 --YGMTE-ACSSLTFmtlhdPTQESFkvtyplLNQPKQGTcVGKPAPHIELMVKlDED-----------SSRVGKILTRG 386
Cdd:PRK05857 315 qvYGLSEtGCTALCL-----PTDDGS------IVKIEAGA-VGRPYPGVDVYLA-ATDgigptapgagpSASFGTLWIKS 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 387 PHTMLRYWGhqvaqeNVETSESRSNEAWLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVV 466
Cdd:PRK05857 382 PANMLGYWN------NPERTAEVLIDGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAAC 455
|
330
....*....|..
gi 22329863 467 IGVIDTRLGEMV 478
Cdd:PRK05857 456 YEIPDEEFGALV 467
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
22-542 |
4.73e-19 |
|
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: 90.23 E-value: 4.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 22 NAVVTVYGNRKRTGREFVDGVLSLAAGLIRLGLRNGDVVSIAAFNSDLFLEWLLAVALVGGVVAPLNYRWSLKEAKMAML 101
Cdd:cd17656 3 DAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIML 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 102 LVEPVLLVTDETCVSwcIDVQNGDIPSLKWrvlmESTSTDFANELNqflttemlkqrtlvpslatYAWASDDAVVICFTS 181
Cdd:cd17656 83 DSGVRVVLTQRHLKS--KLSFNKSTILLED----PSISQEDTSNID-------------------YINNSDDLLYIIYTS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 182 GTTGRPKGVTISH------LAF-ITQSLAKIaiagygEDDVYLHTSPLVHIGGLSSAMAMLMVGACHVLlpkfDAKTALQ 254
Cdd:cd17656 138 GTTGKPKGVQLEHknmvnlLHFeREKTNINF------SDKVLQFATCSFDVCYQEIFSTLLSGGTLYII----REETKRD 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 255 VME-----QNHITCFITVPAMMADLIRVNRTTKNGAENrGVRKILNGGGSLS-SELLKEAVNIFPCArILSAYGMTEAcS 328
Cdd:cd17656 208 VEQlfdlvKRHNIEVVFLPVAFLKFIFSEREFINRFPT-CVKHIITAGEQLViTNEFKEMLHEHNVH-LHNHYGPSET-H 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 329 SLTFMTLH--DPTQEsfkvtYPllnqPkqgtcVGKPAPHIELMVkLDEDSS-----RVGKILTRGPHTMLRYWGHQ-VAQ 400
Cdd:cd17656 285 VVTTYTINpeAEIPE-----LP----P-----IGKPISNTWIYI-LDQEQQlqpqgIVGELYISGASVARGYLNRQeLTA 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 401 ENVETSESRSNEAWLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGVIDTRLGEMVVA 480
Cdd:cd17656 350 EKFFPDPFDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCA 429
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22329863 481 -CVRLQEkwiwsdvenrkgsfqLSSETLKHHCRTQnLTGFKIPKRFVrWEKQFPLTTTGKVKR 542
Cdd:cd17656 430 yFVMEQE---------------LNISQLREYLAKQ-LPEYMIPSFFV-PLDQLPLTPNGKVDR 475
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
31-485 |
5.92e-19 |
|
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: 90.33 E-value: 5.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 31 RKRTGREFVDGVLSLAAGLIRLGLRNGDVVSI-------AAFNsdlflewLLAVALVGGVVAPLNYRWSLKEAKMAMLLV 103
Cdd:cd17634 83 RTISYRELHREVCRFAGTLLDLGVKKGDRVAIympmipeAAVA-------MLACARIGAVHSVIFGGFAPEAVAGRIIDS 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 104 EPVLLVTDETCV---------SWCIDVQNGDIPSLKWRVLMESTSTDFA-NELNQFLTTEMLKQRTlvPSLATYAWASDD 173
Cdd:cd17634 156 SSRLLITADGGVragrsvplkKNVDDALNPNVTSVEHVIVLKRTGSDIDwQEGRDLWWRDLIAKAS--PEHQPEAMNAED 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 174 AVVICFTSGTTGRPKGV---TISHLAFITQSLAKIAiaGYGEDDVYLHTSPLVHIGGLSSAM-AMLMVGACHVLL---PK 246
Cdd:cd17634 234 PLFILYTSGTTGKPKGVlhtTGGYLVYAATTMKYVF--DYGPGDIYWCTADVGWVTGHSYLLyGPLACGATTLLYegvPN 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 247 FDAKTAL-QVMEQNHITCFITVPAMMADLIRVNRTTKNGAENRGVRKILNGGGSLSSELLKEAVNIFPCAR--ILSAYGM 323
Cdd:cd17634 312 WPTPARMwQVVDKHGVNILYTAPTAIRALMAAGDDAIEGTDRSSLRILGSVGEPINPEAYEWYWKKIGKEKcpVVDTWWQ 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 324 TEACSsltFMTLHDPTQESFKVTYPLLNQPKQGTCV----GKPAPhielmvkldedSSRVGKILTRGP---HTMLRYWGH 396
Cdd:cd17634 392 TETGG---FMITPLPGAIELKAGSATRPVFGVQPAVvdneGHPQP-----------GGTEGNLVITDPwpgQTRTLFGDH 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 397 QvaqENVETSESRSNEAWLdTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGVIDTRLGE 476
Cdd:cd17634 458 E---RFEQTYFSTFKGMYF-SGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQ 533
|
....*....
gi 22329863 477 MVVACVRLQ 485
Cdd:cd17634 534 APYAYVVLN 542
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
37-459 |
6.77e-19 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 90.56 E-value: 6.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 37 EFVDGVLSLAAGLIRLGLRNGDVVSIAAfnsDLFLEWLLAVA-------LVGGVVAplnyrwSLKEAKMAMLL--VEPVL 107
Cdd:PLN02387 111 QVFERVCNFASGLVALGHNKEERVAIFA---DTRAEWLIALQgcfrqniTVVTIYA------SLGEEALCHSLneTEVTT 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 108 LVTDETCVSWCIDVQnGDIPSLKWRVLMESTSTDFANELNQ--------FLTTEML-KQRTLVPSLATyawaSDDAVVIC 178
Cdd:PLN02387 182 VICDSKQLKKLIDIS-SQLETVKRVIYMDDEGVDSDSSLSGssnwtvssFSEVEKLgKENPVDPDLPS----PNDIAVIM 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 179 FTSGTTGRPKGVTISHLAFI-TQSLAKIAIAGYGEDDVYLHTSPLVHIGGLSSAMAMLMVGAC------HVLL------- 244
Cdd:PLN02387 257 YTSGSTGLPKGVMMTHGNIVaTVAGVMTVVPKLGKNDVYLAYLPLAHILELAAESVMAAVGAAigygspLTLTdtsnkik 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 245 --PKFDAkTALQVmeqnhiTCFITVPAMMaDLIR--VNRT--TKNGAENR------------------------------ 288
Cdd:PLN02387 337 kgTKGDA-SALKP------TLMTAVPAIL-DRVRdgVRKKvdAKGGLAKKlfdiaykrrlaaiegswfgawglekllwda 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 289 ------------GVRKILNGGGSLSSElLKEAVNIFPCARILSAYGMTEACSSLTFMTLHDPTQESfkvtypllnqpkqg 356
Cdd:PLN02387 409 lvfkkiravlggRIRFMLSGGAPLSGD-TQRFINICLGAPIGQGYGLTETCAGATFSEWDDTSVGR-------------- 473
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 357 tcVGKPAPH--IELmVKLDEDSSRV-------GKILTRGPHTMLRYWGHQVAQENVETSESRSNEaWLDTGDIGAFDEFG 427
Cdd:PLN02387 474 --VGPPLPCcyVKL-VSWEEGGYLIsdkpmprGEIVIGGPSVTLGYFKNQEKTDEVYKVDERGMR-WFYTGDIGQFHPDG 549
|
490 500 510
....*....|....*....|....*....|...
gi 22329863 428 NLWLIGRSNGRIK-TGGENVYPEEVEAVLVEHP 459
Cdd:PLN02387 550 CLEIIDRKKDIVKlQHGEYVSLGKVEAALSVSP 582
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
158-547 |
9.65e-19 |
|
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: 88.91 E-value: 9.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 158 RTLVPSLATYAWASDDAVVICFTSGTTGRPKGVTISHlafitQSLAkiAIAGYGEDDvyLHTSPlvhigglSSAMAmlmv 237
Cdd:cd17653 91 RTSGATLLLTTDSPDDLAYIIFTSGSTGIPKGVMVPH-----RGVL--NYVSQPPAR--LDVGP-------GSRVA---- 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 238 gacHVLLPKFDAKTA--LQVMEQNHITCFITVPAMMADLIR-VNRT--------TKNGAENRGVRKILNGGGSLSSELLK 306
Cdd:cd17653 151 ---QVLSIAFDACIGeiFSTLCNGGTLVLADPSDPFAHVARtVDALmstpsilsTLSPQDFPNLKTIFLGGEAVPPSLLD 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 307 EAVnifPCARILSAYGMTEaCSSLTFMTLhdptqesfkvtypLLnqPKQGTCVGKPAPHIElMVKLDEDSSRV-----GK 381
Cdd:cd17653 228 RWS---PGRRLYNAYGPTE-CTISSTMTE-------------LL--PGQPVTIGKPIPNST-CYILDADLQPVpegvvGE 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 382 ILTRGPHTMLRYWGHQVaqenvETSESRSNEAWLD------TGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVL 455
Cdd:cd17653 288 ICISGVQVARGYLGNPA-----LTASKFVPDPFWPgsrmyrTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEVV 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 456 VEHPGIVSAVVIGVIDTRLgemvVACVRLQEkwiwSDVEnrkgsfQLSSETLKHhcrtqnLTGFKIPKRFVRWEkQFPLT 535
Cdd:cd17653 363 LQSQPEVTQAAAIVVNGRL----VAFVTPET----VDVD------GLRSELAKH------LPSYAVPDRIIALD-SFPLT 421
|
410
....*....|..
gi 22329863 536 TTGKVKRDEVRR 547
Cdd:cd17653 422 ANGKVDRKALRE 433
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
43-497 |
1.05e-18 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 89.68 E-value: 1.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 43 LSLAAGLIRLGLRNGDVVSIAAFNSDLFLEWLLAVALVGGVVAPLNYRWSL--KEAKMAMLLV-----EPVLLVTDETCV 115
Cdd:PRK09192 60 EAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPLPLPMGFggRESYIAQLRGmlasaQPAAIITPDELL 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 116 SWcidvqngdipslkwrvLMESTStdfANELNQFLTTEMLKQRTlVPSLATYAWASDDAVVICFTSGTTGRPKGVTISHL 195
Cdd:PRK09192 140 PW----------------VNEATH---GNPLLHVLSHAWFKALP-EADVALPRPTPDDIAYLQYSSGSTRFPRGVIITHR 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 196 AFITqSLAKIAIAG--YGEDDVYLHTSPLVHIGGLssamamlmVG------ACHV---LLPKFD-AKTALQ---VMEQNH 260
Cdd:PRK09192 200 ALMA-NLRAISHDGlkVRPGDRCVSWLPFYHDMGL--------VGflltpvATQLsvdYLPTRDfARRPLQwldLISRNR 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 261 ITcfITV-PAMMADLI--RVNRTTKNGAENRGVRKILNGGGSLSSELLKEAVNIFPCA-----RILSAYGMTEACSSLTF 332
Cdd:PRK09192 271 GT--ISYsPPFGYELCarRVNSKDLAELDLSCWRVAGIGADMIRPDVLHQFAEAFAPAgfddkAFMPSYGLAEATLAVSF 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 333 M---------TLHDPTQESFKVTYPLLNQPKQGT----CvGKPAPHIELMVKlDEDSS-----RVGKILTRGPHTMLRYW 394
Cdd:PRK09192 349 SplgsgivveEVDRDRLEYQGKAVAPGAETRRVRtfvnC-GKALPGHEIEIR-NEAGMplperVVGHICVRGPSLMSGYF 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 395 GHQvaqenvETSESRSNEAWLDTGDIGaFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIG-VIDTR 473
Cdd:PRK09192 427 RDE------ESQDVLAADGWLDTGDLG-YLLDGYLYITGRAKDLIIINGRNIWPQDIEWIAEQEPELRSGDAAAfSIAQE 499
|
490 500
....*....|....*....|....*.
gi 22329863 474 LGEMVVACV--RLqekwiwSDVENRK 497
Cdd:PRK09192 500 NGEKIVLLVqcRI------SDEERRG 519
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
5-554 |
1.16e-18 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 90.40 E-value: 1.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 5 SRPHICQCLTRLASVKRNAVVTVYGNRKRTGREFVDGVLSLAAGLIRLGLRNGDVVSIAAFNSDLFLEWLLAVALVGGVV 84
Cdd:PRK12316 2001 RGPGVHQRIAEQAARAPEAIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAY 2080
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 85 APL--NY-----RWSLKEAKMAMLLVEPVL---LVTDETCVSWCIDvqngdiPSLKWRvlmESTSTDFANELnqflttem 154
Cdd:PRK12316 2081 VPLdpNYpaerlAYMLEDSGAALLLTQRHLlerLPLPAGVARLPLD------RDAEWA---DYPDTAPAVQL-------- 2143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 155 lkqrtlvpslatyawASDDAVVICFTSGTTGRPKGVTISHLAFITQSLAKIAIAGYGEDDVYLHTSPLVHIGGLSSAMAM 234
Cdd:PRK12316 2144 ---------------AGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPADCELQFMSFSFDGAHEQWFHP 2208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 235 LMVGACHVLLPK--FDAKTALQVMEQNHITCFITVPAMMADLIRVNRTTKNGAEnrgVRKILNGGGSLSSELLKEAVNIF 312
Cdd:PRK12316 2209 LLNGARVLIRDDelWDPEQLYDEMERHGVTILDFPPVYLQQLAEHAERDGRPPA---VRVYCFGGEAVPAASLRLAWEAL 2285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 313 PCARILSAYGMTEAcsSLTFMTLHDPTQESFKVTYPLLnqpkqGTCVGKPAPHIelmvkLDED-----SSRVGKILTRGP 387
Cdd:PRK12316 2286 RPVYLFNGYGPTEA--VVTPLLWKCRPQDPCGAAYVPI-----GRALGNRRAYI-----LDADlnllaPGMAGELYLGGE 2353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 388 HTMLRYWGH--QVAQENVETSESRSNEAWLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAV 465
Cdd:PRK12316 2354 GLARGYLNRpgLTAERFVPDPFSASGERLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAV 2433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 466 VIGvIDTRLGEMVVACVRLQEKwiwsdvenRKGSFQLSSETLKhhcrtQNLTGFKIPKRFVRWEKqFPLTTTGKVKRDEV 545
Cdd:PRK12316 2434 VVA-QDGASGKQLVAYVVPDDA--------AEDLLAELRAWLA-----ARLPAYMVPAHWVVLER-LPLNPNGKLDRKAL 2498
|
....*....
gi 22329863 546 RRQVLSHFQ 554
Cdd:PRK12316 2499 PKPDVSQLR 2507
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
172-542 |
1.40e-18 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 88.80 E-value: 1.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 172 DDAVVICFTSGTTGRPKGVTISH---LAFITQSLAKIAIagyGEDDVYLHTSPLvhigglS---SAMAM---LMVGACHV 242
Cdd:PRK04813 143 DDNYYIIFTSGTTGKPKGVQISHdnlVSFTNWMLEDFAL---PEGPQFLNQAPY------SfdlSVMDLyptLASGGTLV 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 243 LLPK---FDAKTALQVMEQNHITCFITVP-----AMMADlirvnrtTKNGAENRGVRKILNGGGSLSSELLKEAVNIFPC 314
Cdd:PRK04813 214 ALPKdmtANFKQLFETLPQLPINVWVSTPsfadmCLLDP-------SFNEEHLPNLTHFLFCGEELPHKTAKKLLERFPS 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 315 ARILSAYGMTEACSSLTfmtlhdptqeSFKVTYPLLNQ----PkqgtcVGKPAPHIELMVkLDEDSSRV-----GKILTR 385
Cdd:PRK04813 287 ATIYNTYGPTEATVAVT----------SIEITDEMLDQykrlP-----IGYAKPDSPLLI-IDEEGTKLpdgeqGEIVIS 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 386 GPHTMLRYWGhqvaqenvetSESRSNEAWLD--------TGDIGAFDEfgNLWLI-GRSNGRIKTGGENVYPEEVEAVLV 456
Cdd:PRK04813 351 GPSVSKGYLN----------NPEKTAEAFFTfdgqpayhTGDAGYLED--GLLFYqGRIDFQIKLNGYRIELEEIEQNLR 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 457 EHPGIVSAVVIGVIDTRLGEMVVACVRLQEKwiwsdveNRKGSFQLSS---ETLKhhcrtQNLTGFKIPKRFVrWEKQFP 533
Cdd:PRK04813 419 QSSYVESAVVVPYNKDHKVQYLIAYVVPKEE-------DFEREFELTKaikKELK-----ERLMEYMIPRKFI-YRDSLP 485
|
....*....
gi 22329863 534 LTTTGKVKR 542
Cdd:PRK04813 486 LTPNGKIDR 494
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
170-542 |
2.13e-18 |
|
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: 87.69 E-value: 2.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 170 ASDDAVVIcFTSGTTGRPKGVTISHLAFITQSLAKIAIAGYGEDDVYL-HTSPLVHIGGLSSAMAmLMVGACHVLLPKFD 248
Cdd:cd17652 92 PDNLAYVI-YTSGSTGRPKGVVVTHRGLANLAAAQIAAFDVGPGSRVLqFASPSFDASVWELLMA-LLAGATLVLAPAEE 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 249 AKTA---LQVMEQNHITCFITVPAMMADLirvnrttkNGAENRGVRKILNGGGSLSSELLKEAVnifPCARILSAYGMTE 325
Cdd:cd17652 170 LLPGeplADLLREHRITHVTLPPAALAAL--------PPDDLPDLRTLVVAGEACPAELVDRWA---PGRRMINAYGPTE 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 326 A--CSsltfmTLHDPTQESFKVTypllnqpkqgtcVGKPAPHIELMVkLDEDSSRV-----------GKILTRGphtmlr 392
Cdd:cd17652 239 TtvCA-----TMAGPLPGGGVPP------------IGRPVPGTRVYV-LDARLRPVppgvpgelyiaGAGLARG------ 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 393 YWGH--QVAQENVETSESRSNEAWLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGVI 470
Cdd:cd17652 295 YLNRpgLTAERFVADPFGAPGSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRD 374
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22329863 471 DTRLGEMVVACVrlqekwiwsdveNRKGSFQLSSETLKHHCRTQnLTGFKIPKRFVRWEKqFPLTTTGKVKR 542
Cdd:cd17652 375 DRPGDKRLVAYV------------VPAPGAAPTAAELRAHLAER-LPGYMVPAAFVVLDA-LPLTPNGKLDR 432
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
22-542 |
3.73e-18 |
|
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: 87.14 E-value: 3.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 22 NAVVTVYGNRKRTGREFVDGVLSLAAGLIRLGLRNGDVVSIAAFNSDLFLEWLLAVALVGGVVAPLNyrwslkeakmaml 101
Cdd:cd17650 2 DAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPID------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 102 lvepvllvtdetcvswcidvqnGDIPSLKWRVLMESTSTDFanelnqfLTTEmlkqrtlvpslatyawaSDDAVVICFTS 181
Cdd:cd17650 69 ----------------------PDYPAERLQYMLEDSGAKL-------LLTQ-----------------PEDLAYVIYTS 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 182 GTTGRPKGVTISHlafitqslAKIAIAGYGEDDVY-LHTSPLVHIGGLSSAMAM--------LMVGACHVLLP---KFDA 249
Cdd:cd17650 103 GTTGKPKGVMVEH--------RNVAHAAHAWRREYeLDSFPVRLLQMASFSFDVfagdfarsLLNGGTLVICPdevKLDP 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 250 KTALQVMEQNHITCFITVPAmmadLIR--VNRTTKNGAENRGVRKILNGGGSLSSELLKEAVNIF-PCARILSAYGMTEA 326
Cdd:cd17650 175 AALYDLILKSRITLMESTPA----LIRpvMAYVYRNGLDLSAMRLLIVGSDGCKAQDFKTLAARFgQGMRIINSYGVTEA 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 327 C-SSLTFMTLHDPTQESFKVTypllnqpkqgtcVGKPAPHIELMVkLDED-----SSRVGKILTRGPHTMLRYWGH-QVA 399
Cdd:cd17650 251 TiDSTYYEEGRDPLGDSANVP------------IGRPLPNTAMYV-LDERlqpqpVGVAGELYIGGAGVARGYLNRpELT 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 400 QENVETSESRSNEAWLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGVIDTRLGEMVV 479
Cdd:cd17650 318 AERFVENPFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVREDKGGEARLC 397
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22329863 480 ACVRLQEKWIWSDvenrkgsfqlssetLKHHCrTQNLTGFKIPKRFVRWEKqFPLTTTGKVKR 542
Cdd:cd17650 398 AYVVAAATLNTAE--------------LRAFL-AKELPSYMIPSYYVQLDA-LPLTPNGKVDR 444
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
179-545 |
4.01e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 86.63 E-value: 4.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 179 FTSGTTGRPKgvtishlaFITQSLAKI--AIAGYGE------DDVYLHTSPLVHIGGL-SSAMAMLMVGACHVLLPKFDA 249
Cdd:PRK08308 108 YSSGTTGEPK--------LIRRSWTEIdrEIEAYNEalnceqDETPIVACPVTHSYGLiCGVLAALTRGSKPVIITNKNP 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 250 KTALQVMEQNHITCFITVPAMMADLIRVNRTTKNgaenrgVRKILNGGGSLSSELLKEAVNIfpCARILSAYGMTEA-CS 328
Cdd:PRK08308 180 KFALNILRNTPQHILYAVPLMLHILGRLLPGTFQ------FHAVMTSGTPLPEAWFYKLRER--TTYMMQQYGCSEAgCV 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 329 SLTfMTLHDPTQesfkvtypllnqpkqgtcVGKPAPHIELMVKLDEDSSRvgKILtrgphtmlrywghqvaqenVETSES 408
Cdd:PRK08308 252 SIC-PDMKSHLD------------------LGNPLPHVSVSAGSDENAPE--EIV-------------------VKMGDK 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 409 RSNeawldTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGVIDTRLGEMVVACVRLQEkw 488
Cdd:PRK08308 292 EIF-----TKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVISHE-- 364
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 22329863 489 iwsdvenrkgsfQLSSETLKHHCRtQNLTGFKIPKRFVRwEKQFPLTTTGKVKRDEV 545
Cdd:PRK08308 365 ------------EIDPVQLREWCI-QHLAPYQVPHEIES-VTEIPKNANGKVSRKLL 407
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
172-549 |
5.54e-18 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 88.10 E-value: 5.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 172 DDAVVICFTSGTTGRPKGVTISH---LAFITQSLAKIAiagYGEDDVYLHTSPLVHIGGLSSAMAMLMVGACHVLL-Pkf 247
Cdd:PRK06814 793 DDPAVILFTSGSEGTPKGVVLSHrnlLANRAQVAARID---FSPEDKVFNALPVFHSFGLTGGLVLPLLSGVKVFLyP-- 867
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 248 dakTALQVmeqnHItcfitVPAMMADlirVNRT--------------TKNGAENRGVRKILNGggslsSELLKEA----- 308
Cdd:PRK06814 868 ---SPLHY----RI-----IPELIYD---TNATilfgtdtflngyarYAHPYDFRSLRYVFAG-----AEKVKEEtrqtw 927
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 309 VNIFPcARILSAYGMTEACSSLTFMTlhdptqesfkvtyPLLNQPkqGTcVGKPAPHIElmVKLD--EDSSRVGKILTRG 386
Cdd:PRK06814 928 MEKFG-IRILEGYGVTETAPVIALNT-------------PMHNKA--GT-VGRLLPGIE--YRLEpvPGIDEGGRLFVRG 988
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 387 PHTMLRYwghqVAQENVETSESRSnEAWLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVE-HPGIVSAV 465
Cdd:PRK06814 989 PNVMLGY----LRAENPGVLEPPA-DGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAElWPDALHAA 1063
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 466 ViGVIDTRLGEMVVACVRLQekwiwsdvenrkgsfQLSSETLKHHCRTQNLTGFKIPKRFVRWEKqFPLTTTGKVKRDEV 545
Cdd:PRK06814 1064 V-SIPDARKGERIILLTTAS---------------DATRAAFLAHAKAAGASELMVPAEIITIDE-IPLLGTGKIDYVAV 1126
|
....
gi 22329863 546 RRQV 549
Cdd:PRK06814 1127 TKLA 1130
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
22-542 |
5.71e-18 |
|
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: 87.00 E-value: 5.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 22 NAVVTVYGNRKRTGREFVDGVLSLAAGLIRLGLRNGDVVSIAAFNSDLFLEWLLAVALVGGVVAPLN--Y-----RWSLK 94
Cdd:cd17655 12 DHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDpdYpeeriQYILE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 95 EAKMAMLLvepvllvTDETCVSWCIDVqnGDIPSLKWRVLMESTSTDFANELNqflttemlkqrtlvpslatyawASDDA 174
Cdd:cd17655 92 DSGADILL-------TQSHLQPPIAFI--GLIDLLDEDTIYHEESENLEPVSK----------------------SDDLA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 175 VVIcFTSGTTGRPKGVTISHLAFITQSLAKIAIAGYGEDDVYLHTSPLVHIGGLSSAMAMLMVGACHVLLPK---FDAKT 251
Cdd:cd17655 141 YVI-YTSGSTGKPKGVMIEHRGVVNLVEWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVRKetvLDGQA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 252 ALQVMEQNHITcFITVPAMMADLIRVNrttkNGAENRGVRKILNGGGSLSSELLKEAVNIFPCAR-ILSAYGMTEA--CS 328
Cdd:cd17655 220 LTQYIRQNRIT-IIDLTPAHLKLLDAA----DDSEGLSLKHLIVGGEALSTELAKKIIELFGTNPtITNAYGPTETtvDA 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 329 SLTFMTLHDPTQESFKVTYPLLN-------QPKQGTCVGKPAphiELMVKldedssrvGKILTRGphtmlrYWGH-QVAQ 400
Cdd:cd17655 295 SIYQYEPETDQQVSVPIGKPLGNtriyildQYGRPQPVGVAG---ELYIG--------GEGVARG------YLNRpELTA 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 401 ENVETSESRSNEAWLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGVIDTRlGEMVVA 480
Cdd:cd17655 358 EKFVDDPFVPGERMYRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQ-GQNYLC 436
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22329863 481 CVRLQEKwiwsdvenrkgsfQLSSETLKHHCrTQNLTGFKIPKRFVRWEKqFPLTTTGKVKR 542
Cdd:cd17655 437 AYIVSEK-------------ELPVAQLREFL-ARELPDYMIPSYFIKLDE-IPLTPNGKVDR 483
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
172-540 |
7.17e-18 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 87.67 E-value: 7.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 172 DDAVVICFTSGTTGRPKGVTISHLAFITQSLAKIAIAGYGEDDVYLHTSPLVHIGGLSSAMAM-LMVGACHVLLPK-FDA 249
Cdd:PRK08633 782 DDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSSLPFFHSFGLTVTLWLpLLEGIKVVYHPDpTDA 861
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 250 KTALQVMEQNHITCFITVPAMMADLIRVNRTTKngAENRGVRKILNGGGSLSSEL---LKEAVNIfpcaRILSAYGMTEa 326
Cdd:PRK08633 862 LGIAKLVAKHRATILLGTPTFLRLYLRNKKLHP--LMFASLRLVVAGAEKLKPEVadaFEEKFGI----RILEGYGATE- 934
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 327 CSSLTFMTLHDptqeSFKVTYPLLNQPKQGTcVGKPAPHIELMVkLDEDSSRV------GKILTRGPHTMLRYWGH--QV 398
Cdd:PRK08633 935 TSPVASVNLPD----VLAADFKRQTGSKEGS-VGMPLPGVAVRI-VDPETFEElppgedGLILIGGPQVMKGYLGDpeKT 1008
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 399 AQENVETSESRsneaWLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVyP-----EEVEAVLVEHPGIVsaVVIGVIDTR 473
Cdd:PRK08633 1009 AEVIKDIDGIG----WYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMV-PlgaveEELAKALGGEEVVF--AVTAVPDEK 1081
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22329863 474 LGEMVVACVRLQEkwiwsdvenrkgsfqLSSETLKHHCRTQNLTGFKIPKRFVRWEkQFPLTTTGKV 540
Cdd:PRK08633 1082 KGEKLVVLHTCGA---------------EDVEELKRAIKESGLPNLWKPSRYFKVE-ALPLLGSGKL 1132
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
31-550 |
1.35e-17 |
|
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: 86.00 E-value: 1.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 31 RKRTGREFVDGVLSLAAGLIRLGLRNGDVVSIAAFNSDLFLEWLLAVALVGGVVAPL-------NYRWSLKEAKMAMLLV 103
Cdd:cd05968 90 RTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIfsgfgkeAAATRLQDAEAKALIT 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 104 --------EPV-LLVTDETCVSWCidvqngdiPSLKWRVLMESTSTDFANELNQFLTTEMLKQRTLVPSLATYawaSDDA 174
Cdd:cd05968 170 adgftrrgREVnLKEEADKACAQC--------PTVEKVVVVRHLGNDFTPAKGRDLSYDEEKETAGDGAERTE---SEDP 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 175 VVICFTSGTTGRPKGVTISHLAFITQSLAKIAIA-GYGEDDVYLHTSPLVHIGGLSSAMAMLMVGACHVL---LPKFDAK 250
Cdd:cd05968 239 LMIIYTSGTTGKPKGTVHVHAGFPLKAAQDMYFQfDLKPGDLLTWFTDLGWMMGPWLIFGGLILGATMVLydgAPDHPKA 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 251 TALQVMEQNHitcFITVPAMMADLIRVNRTTKNGAENRGVRKILNGGGSLSSELLKEAVNIFPCAR------ILSAYGMT 324
Cdd:cd05968 319 DRLWRMVEDH---EITHLGLSPTLIRALKPRGDAPVNAHDLSSLRVLGSTGEPWNPEPWNWLFETVgkgrnpIINYSGGT 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 325 EACSSLTFMTLHDPTQE-SFkvtypllNQPKQGTCVgkpaphielmVKLDEDSSR----VGKILTRGPHT-MLR-YWGHQ 397
Cdd:cd05968 396 EISGGILGNVLIKPIKPsSF-------NGPVPGMKA----------DVLDESGKParpeVGELVLLAPWPgMTRgFWRDE 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 398 vaQENVETSESRSNEAWLDtGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGVIDTRLGEM 477
Cdd:cd05968 459 --DRYLETYWSRFDNVWVH-GDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEA 535
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22329863 478 VVACVRLQEKWIWSDvENRKGSFQLSSETLKHHCRtqnltgfkiPKRfVRWEKQFPLTTTGKVKRDEVRRQVL 550
Cdd:cd05968 536 IVCFVVLKPGVTPTE-ALAEELMERVADELGKPLS---------PER-ILFVKDLPKTRNAKVMRRVIRAAYL 597
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
23-542 |
1.76e-17 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 86.75 E-value: 1.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 23 AVVTVYGNRKRTGREFVDGVLSLAAGLIRLGLRNGDVVSIAAFNSDLFLEWLLAVALVGGVVAPLN-------YRWSLKE 95
Cdd:PRK12467 3111 APALVFGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDpeyprerLAYMIED 3190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 96 AKMAMLLVEPVLLvtdetcvswcidvQNGDIPSLKWRVLMESTSTDFANELNqflttemlkqrtlvpsLATYAWASDDAV 175
Cdd:PRK12467 3191 SGVKLLLTQAHLL-------------EQLPAPAGDTALTLDRLDLNGYSENN----------------PSTRVMGENLAY 3241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 176 VIcFTSGTTGRPKGVTISHLAFITQSLAKIAIAGYGEDDVYLHTSPLVHIGGLSSAMAMLMVGACHVLLPK--FDAKTAL 253
Cdd:PRK12467 3242 VI-YTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDRVLLFMSFSFDGAQERFLWTLICGGCLVVRDNdlWDPEELW 3320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 254 QVMEQNHITCFITVPAMMADLIRvnrtTKNGAENRGVRKILNGGGSLSSELLKEAVNIFPCARILSAYGMTEACssltfm 333
Cdd:PRK12467 3321 QAIHAHRISIACFPPAYLQQFAE----DAGGADCASLDIYVFGGEAVPPAAFEQVKRKLKPRGLTNGYGPTEAV------ 3390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 334 tlhdptqesfkVTYPLLNQPKQGTC------VGKPAPHIELMVkLDEDSSRV-----------GKILTRGPHtmlrywgH 396
Cdd:PRK12467 3391 -----------VTVTLWKCGGDAVCeapyapIGRPVAGRSIYV-LDGQLNPVpvgvagelyigGVGLARGYH-------Q 3451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 397 Q---VAQENVETSESRSNEAWLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGViDTR 473
Cdd:PRK12467 3452 RpslTAERFVADPFSGSGGRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLAR-DGA 3530
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22329863 474 LGEMVVACVRL---QEKWiwsdvenrkgsfqlsSETLKHHCRTQnLTGFKIPKRFVRWEkQFPLTTTGKVKR 542
Cdd:PRK12467 3531 GGKQLVAYVVPadpQGDW---------------RETLRDHLAAS-LPDYMVPAQLLVLA-AMPLGPNGKVDR 3585
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
177-542 |
2.36e-17 |
|
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: 84.79 E-value: 2.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 177 ICFTSGTTGRPKGVTISHLAFITQSLAKIAIAGYGEDDvylHTSPLVHIGGLSSA---MAMLMVGACHVLLPK---FDAK 250
Cdd:cd17644 111 VIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEYGITSSD---RVLQFASIAFDVAAeeiYVTLLSGATLVLRPEemrSSLE 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 251 TALQVMEQNHITCFITVPAMMADLIRVNRTTKNGAENRgVRKILNGGGSLSSEL---LKEAVNIFPcaRILSAYGMTEAC 327
Cdd:cd17644 188 DFVQYIQQWQLTVLSLPPAYWHLLVLELLLSTIDLPSS-LRLVIVGGEAVQPELvrqWQKNVGNFI--QLINVYGPTEAT 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 328 SSLTFMTLHDPTQEsfKVTYPLlnqpkqgtcVGKPAPHIELMVkLDEDSSRV-----------GKILTRG----PH-TML 391
Cdd:cd17644 265 IAATVCRLTQLTER--NITSVP---------IGRPIANTQVYI-LDENLQPVpvgvpgelhigGVGLARGylnrPElTAE 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 392 RYWGHQVAQenveTSESRsneaWLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGVID 471
Cdd:cd17644 333 KFISHPFNS----SESER----LYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVRED 404
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22329863 472 TRLGEMVVACVRLQEKWIWSDVENRkgsfqlssETLKhhcrtQNLTGFKIPKRFVRWEkQFPLTTTGKVKR 542
Cdd:cd17644 405 QPGNKRLVAYIVPHYEESPSTVELR--------QFLK-----AKLPDYMIPSAFVVLE-ELPLTPNGKIDR 461
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
172-465 |
6.71e-17 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 83.89 E-value: 6.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 172 DDAVVICFTSGTTGRPKGVTISHLAFITQSLAKIAIAGYG-EDDVYLHTSPLVHigglssamAMLMVGAchVLLPKFDAK 250
Cdd:PRK07768 152 DDLALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEFDvETDVMVSWLPLFH--------DMGMVGF--LTVPMYFGA 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 251 TALQV--MEqnhitcFITVPAMMADLIRVNRTTKNGAEN--------RGVRKILNGGGSLSSelLKEAVN----IFPC-- 314
Cdd:PRK07768 222 ELVKVtpMD------FLRDPLLWAELISKYRGTMTAAPNfayallarRLRRQAKPGAFDLSS--LRFALNgaepIDPAdv 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 315 -------AR-------ILSAYGMTEACSSLTFmtlhDPTQESFKVTYP---LLNQPKQGT-----------CVGKPAPHI 366
Cdd:PRK07768 294 edlldagARfglrpeaILPAYGMAEATLAVSF----SPCGAGLVVDEVdadLLAALRRAVpatkgntrrlaTLGPPLPGL 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 367 ELMVkLDED-----SSRVGKILTRGPHTMLRYW---GHQVAQENvetsesrsnEAWLDTGDIGAFDEFGNLWLIGRSNGR 438
Cdd:PRK07768 370 EVRV-VDEDgqvlpPRGVGVIELRGESVTPGYLtmdGFIPAQDA---------DGWLDTGDLGYLTEEGEVVVCGRVKDV 439
|
330 340 350
....*....|....*....|....*....|.
gi 22329863 439 IKTGGENVYPEEVE--AVLVE--HPGIVSAV 465
Cdd:PRK07768 440 IIMAGRNIYPTDIEraAARVEgvRPGNAVAV 470
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
173-555 |
1.86e-16 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 82.56 E-value: 1.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 173 DAVVICFTSGTTGRPKGVTISHLA----------FITQSLAKIAIagygeDDVYLHTSPLVHI----------------- 225
Cdd:PLN02430 221 DICTIMYTSGTSGDPKGVVLTHEAvatfvrgvdlFMEQFEDKMTH-----DDVYLSFLPLAHIldrmieeyffrkgasvg 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 226 ---GGLSSAMAMLM-------VGACHVLLPKFDA-KTALQvmEQNHITCFI------------------TVPAMMADLIR 276
Cdd:PLN02430 296 yyhGDLNALRDDLMelkptllAGVPRVFERIHEGiQKALQ--ELNPRRRLIfnalykyklawmnrgyshKKASPMADFLA 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 277 VnRTTKNGAENRgVRKILNGGGSLSSELlKEAVNIFPCARILSAYGMTEACSsltfmtlhdPTQESFKVTYPLLnqpkqG 356
Cdd:PLN02430 374 F-RKVKAKLGGR-LRLLISGGAPLSTEI-EEFLRVTSCAFVVQGYGLTETLG---------PTTLGFPDEMCML-----G 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 357 TcVGKPAPHIELmvKLDE----------DSSRvGKILTRGPHTMLRYWghqvaqENVETSESRSNEAWLDTGDIGAFDEF 426
Cdd:PLN02430 437 T-VGAPAVYNEL--RLEEvpemgydplgEPPR-GEICVRGKCLFSGYY------KNPELTEEVMKDGWFHTGDIGEILPN 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 427 GNLWLIGRSNGRIK-TGGENVYPEEVEAVLVEHPgIVSAvvIGVIDTRLGEMVVACVRLQEKWI--WSDVENRKGSFQ-- 501
Cdd:PLN02430 507 GVLKIIDRKKNLIKlSQGEYVALEYLENVYGQNP-IVED--IWVYGDSFKSMLVAVVVPNEENTnkWAKDNGFTGSFEel 583
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22329863 502 LSSETLKHHCRTQ--------NLTGFKIPKRFVRWEKQFPL-----TTTGKVKRDevrrQVLSHFQI 555
Cdd:PLN02430 584 CSLPELKEHILSElkstaeknKLRGFEYIKGVILETKPFDVerdlvTATLKKRRN----NLLKYYQV 646
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
160-539 |
4.77e-16 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 81.29 E-value: 4.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 160 LVPSLATYAWASDDAVVICFTSGTTGRPKGVTISH---LAFITQslakI-AIAGYGEDDVYLHTSPLVHIGGLS-SAMAM 234
Cdd:PRK08043 353 LMPRLAQVKQQPEDAALILFTSGSEGHPKGVVHSHkslLANVEQ----IkTIADFTPNDRFMSALPLFHSFGLTvGLFTP 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 235 LMVGACHVLLPkfdakTALQ-------VMEQNHITCFITVP-----AMMA---DLIRVnRTTKNGAEnrgvrKILNGggs 299
Cdd:PRK08043 429 LLTGAEVFLYP-----SPLHyrivpelVYDRNCTVLFGTSTflgnyARFAnpyDFARL-RYVVAGAE-----KLQES--- 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 300 lSSELLKEAVNIfpcaRILSAYGMTEaCSSLTfmtlhdptqesfkvtypLLNQP---KQGTcVGKPAPHIE---LMVKLD 373
Cdd:PRK08043 495 -TKQLWQDKFGL----RILEGYGVTE-CAPVV-----------------SINVPmaaKPGT-VGRILPGMDarlLSVPGI 550
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 374 EDSsrvGKILTRGPHTMLRYWghQVAQENV------ETSESRSNEAWLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVY 447
Cdd:PRK08043 551 EQG---GRLQLKGPNIMNGYL--RVEKPGVlevptaENARGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVS 625
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 448 PEEVEAV-LVEHPGIVSAVVIgVIDTRLGEMVVACVrlqekwiwSDVEnrkgsfqLSSETLKHHCRTQNLTGFKIPkRFV 526
Cdd:PRK08043 626 LEMVEQLaLGVSPDKQHATAI-KSDASKGEALVLFT--------TDSE-------LTREKLQQYAREHGVPELAVP-RDI 688
|
410
....*....|...
gi 22329863 527 RWEKQFPLTTTGK 539
Cdd:PRK08043 689 RYLKQLPLLGSGK 701
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
60-542 |
6.82e-15 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 78.67 E-value: 6.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 60 VSIAAFNSDLFLEWLLAVALVGGVVAPLN-------YRWSLKEAKMAMLLVEPVLLvtdetcvswcidvqnGDIPSLKWR 132
Cdd:PRK05691 1184 VAIAAERSPQLLVGLLAILKAGGAYVPLDpdypaerLAYMLADSGVELLLTQSHLL---------------ERLPQAEGV 1248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 133 VLMESTSTDFANELNQflttemlkqrtlVPSLATYAwasDDAVVICFTSGTTGRPKGVTISHLAFITQSLAKIAIAGYGE 212
Cdd:PRK05691 1249 SAIALDSLHLDSWPSQ------------APGLHLHG---DNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYALDD 1313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 213 DDVYLHTSPLVHIGGLSSAMAMLMVGaCHVLLP----KFDAKTALQVMEQNHITCFITVPAMMADLIRVNRTtkngAENR 288
Cdd:PRK05691 1314 SDVLMQKAPISFDVSVWECFWPLITG-CRLVLAgpgeHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDEPLA----AACT 1388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 289 GVRKILNGGGSLSSELLKEAVNIFPCARILSAYGMTEACSSLTFMTLHDPTQESFKVTYPL-------LNQPKQGTCVGK 361
Cdd:PRK05691 1389 SLRRLFSGGEALPAELRNRVLQRLPQVQLHNRYGPTETAINVTHWQCQAEDGERSPIGRPLgnvlcrvLDAELNLLPPGV 1468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 362 PAphiELMVKldedssrvGKILTRGphtmlrYWGH--QVAQENVETSESRSNEAWLDTGDIGAFDEFGNLWLIGRSNGRI 439
Cdd:PRK05691 1469 AG---ELCIG--------GAGLARG------YLGRpaLTAERFVPDPLGEDGARLYRTGDRARWNADGALEYLGRLDQQV 1531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 440 KTGGENVYPEEVEAVLVEHPGIVSAVVIgVIDTRLGEMVVACVRLQekwiwsdvenrkGSFQLSSETLKhHCRTQNLTGF 519
Cdd:PRK05691 1532 KLRGFRVEPEEIQARLLAQPGVAQAAVL-VREGAAGAQLVGYYTGE------------AGQEAEAERLK-AALAAELPEY 1597
|
490 500
....*....|....*....|...
gi 22329863 520 KIPKRFVRWEkQFPLTTTGKVKR 542
Cdd:PRK05691 1598 MVPAQLIRLD-QMPLGPSGKLDR 1619
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
25-459 |
7.09e-15 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 77.71 E-value: 7.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 25 VTVYGNRKR-TGREFVDGVLSLAAGLIRLGLRNGDVVSIAafnSDLFLEWLLAV-------ALVGGVVAPLN---YRWSL 93
Cdd:PTZ00216 113 VTHFNETRYiTYAELWERIVNFGRGLAELGLTKGSNVAIY---EETRWEWLASIygiwsqsMVAATVYANLGedaLAYAL 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 94 KEAKMAMLL-----VEPVLLVTDETCVSWCIDVQNGDIPSlkwrvlmestSTDfANELNQFLTTEMLKQRTLVPSLATYA 168
Cdd:PTZ00216 190 RETECKAIVcngknVPNLLRLMKSGGMPNTTIIYLDSLPA----------SVD-TEGCRLVAWTDVVAKGHSAGSHHPLN 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 169 WAS--DDAVVICFTSGTTGRPKGVTISHLAfITQSLAKIA------IAGYGEDDVYLHTSPLVHIGGLSSAMAMLMVGaC 240
Cdd:PTZ00216 259 IPEnnDDLALIMYTSGTTGDPKGVMHTHGS-LTAGILALEdrlndlIGPPEEDETYCSYLPLAHIMEFGVTNIFLARG-A 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 241 HV-------LL-----PKFDAKTALQVMeqnhitcFITVP--------AMMADLIRVN---------------RTTKNGA 285
Cdd:PTZ00216 337 LIgfgsprtLTdtfarPHGDLTEFRPVF-------LIGVPrifdtikkAVEAKLPPVGslkrrvfdhayqsrlRALKEGK 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 286 EN----------------RGVRKILNGGGSLSSElLKEAVNI-FpcARILSAYGMTEACSSltfmtlhDPTQESFKVTYp 348
Cdd:PTZ00216 410 DTpywnekvfsapravlgGRVRAMLSGGGPLSAA-TQEFVNVvF--GMVIQGWGLTETVCC-------GGIQRTGDLEP- 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 349 llnqpkqgTCVGKPAPHIELmvKL---------DEDSSRvGKILTRGPHTMLRYWghqvAQENVeTSESRSNEAWLDTGD 419
Cdd:PTZ00216 479 --------NAVGQLLKGVEM--KLldteeykhtDTPEPR-GEILLRGPFLFKGYY----KQEEL-TREVLDEDGWFHTGD 542
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 22329863 420 IGAFDEFGNLWLIGRSNGRIKTG-GENVYPEEVEAVLVEHP 459
Cdd:PTZ00216 543 VGSIAANGTLRIIGRVKALAKNClGEYIALEALEALYGQNE 583
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
173-468 |
2.73e-14 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 75.83 E-value: 2.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 173 DAVVICFTSGTTGRPKGVTISHLAFIT-----QSLAKIAIAGYGEDDVYLHTSPLVHIGGLSSAMAMLMVGAChVLLPKF 247
Cdd:PLN02614 224 DICTIMYTSGTTGDPKGVMISNESIVTliagvIRLLKSANAALTVKDVYLSYLPLAHIFDRVIEECFIQHGAA-IGFWRG 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 248 DAKTALQVMEQNHITCFITVPAMM------------------ADLIRVNRTTKNGAENRG-------------------- 289
Cdd:PLN02614 303 DVKLLIEDLGELKPTIFCAVPRVLdrvysglqkklsdggflkKFVFDSAFSYKFGNMKKGqshveasplcdklvfnkvkq 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 290 -----VRKILNGGGSLSSELlKEAVNIFPCARILSAYGMTEACSSlTFMTLHDPTQesfkvtypllnqpKQGTcVGKPAP 364
Cdd:PLN02614 383 glggnVRIILSGAAPLASHV-ESFLRVVACCHVLQGYGLTESCAG-TFVSLPDELD-------------MLGT-VGPPVP 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 365 HIELMV----KLDED---SSRVGKILTRGPHTMLRYWGHQVAQENVETsesrsnEAWLDTGDIGAFDEFGNLWLIGRSNG 437
Cdd:PLN02614 447 NVDIRLesvpEMEYDalaSTPRGEICIRGKTLFSGYYKREDLTKEVLI------DGWLHTGDVGEWQPNGSMKIIDRKKN 520
|
330 340 350
....*....|....*....|....*....|..
gi 22329863 438 RIK-TGGENVYPEEVEAVLVEHPGIVSAVVIG 468
Cdd:PLN02614 521 IFKlSQGEYVAVENIENIYGEVQAVDSVWVYG 552
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
40-548 |
9.07e-14 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 74.30 E-value: 9.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 40 DGVLSLAAGLIRLGLRNGDVVSIAAFNSDLFLEWLLAvALVGGVVA----PLNYR--WSLKEAKMAMLLVepvllvtdet 113
Cdd:PRK06060 38 DGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLA-CLARGVMAflanPELHRddHALAARNTEPALV---------- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 114 cvswcidVQNGdipSLKWRvLMESTSTDFAnelnqflttEMLKQRTLVPSlATYAWASDDAVVIC-FTSGTTGRPKGVTI 192
Cdd:PRK06060 107 -------VTSD---ALRDR-FQPSRVAEAA---------ELMSEAARVAP-GGYEPMGGDALAYAtYTSGTTGPPKAAIH 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 193 SH---LAFItQSLAKIAIAgYGEDDVYLHTSPLVHIGGLSSAMAM-LMVGACHVLLP-KFDAKTALQVMEQNHITCFITV 267
Cdd:PRK06060 166 RHadpLTFV-DAMCRKALR-LTPEDTGLCSARMYFAYGLGNSVWFpLATGGSAVINSaPVTPEAAAILSARFGPSVLYGV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 268 PAMMADLIrvnrTTKNGAENRGVRKILNGGGSLSSELLKEAVNIFPCARILSAYGMTEACSSLTFMTLHDPtqesfkvty 347
Cdd:PRK06060 244 PNFFARVI----DSCSPDSFRSLRCVVSAGEALELGLAERLMEFFGGIPILDGIGSTEVGQTFVSNRVDEW--------- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 348 pllnqpKQGTcVGKPAPHIELMVKLDEDSSR----VGKILTRGPHTMLRYWGHqvaqenveTSESRSNEAWLDTGDIGAF 423
Cdd:PRK06060 311 ------RLGT-LGRVLPPYEIRVVAPDGTTAgpgvEGDLWVRGPAIAKGYWNR--------PDSPVANEGWLDTRDRVCI 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 424 DEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGVIDtrlgemVVACVRLQEKWIWSDVENRKGSfqls 503
Cdd:PRK06060 376 DSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRE------STGASTLQAFLVATSGATIDGS---- 445
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 22329863 504 seTLKH-HCR--TQnLTGFKIPKRFVRWEKqFPLTTTGKVKRDEVRRQ 548
Cdd:PRK06060 446 --VMRDlHRGllNR-LSAFKVPHRFAVVDR-LPRTPNGKLVRGALRKQ 489
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
171-542 |
9.26e-14 |
|
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: 73.36 E-value: 9.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 171 SDDAVVICFTSGTTGRPKGVTISHLAFI------------TQSLAKIAIAGYGEDDVYLHTSPLVHIGglssamamlmvG 238
Cdd:cd17645 103 PDDLAYVIYTSGSTGLPKGVMIEHHNLVnlcewhrpyfgvTPADKSLVYASFSFDASAWEIFPHLTAG-----------A 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 239 ACHVL--LPKFDAKTALQVMEQNHITcfIT-VPAMMADLIrvnrttkNGAENRGVRKILNGGgslssELLKEAVNifPCA 315
Cdd:cd17645 172 ALHVVpsERRLDLDALNDYFNQEGIT--ISfLPTGAAEQF-------MQLDNQSLRVLLTGG-----DKLKKIER--KGY 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 316 RILSAYGmteacssltfmtlhdPTQESFKVTYPLLNQPKQGTCVGKPAPHIELMVkLDEDSSR-----------VGKILT 384
Cdd:cd17645 236 KLVNNYG---------------PTENTVVATSFEIDKPYANIPIGKPIDNTRVYI-LDEALQLqpigvagelciAGEGLA 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 385 RG-----PHTMLRYWGH-QVAQENVetsesrsneawLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEH 458
Cdd:cd17645 300 RGylnrpELTAEKFIVHpFVPGERM-----------YRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNH 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 459 PGIVSAVVIGVIDTRLGEMVVACVRLQEKwiwSDVENRKgsfqlssETLKhhcrtQNLTGFKIPKRFVRWeKQFPLTTTG 538
Cdd:cd17645 369 PLIELAAVLAKEDADGRKYLVAYVTAPEE---IPHEELR-------EWLK-----NDLPDYMIPTYFVHL-KALPLTANG 432
|
....
gi 22329863 539 KVKR 542
Cdd:cd17645 433 KVDR 436
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
172-484 |
2.85e-13 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 71.72 E-value: 2.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 172 DDAVVICFTSGTTGRPKGV--TISHLAFITQSLAKI-AIAGYGEDDVYLHTSPL-VHIGGLSSAMAMLMVGAchVLLPKF 247
Cdd:COG1541 83 EEIVRIHASSGTTGKPTVVgyTRKDLDRWAELFARSlRAAGVRPGDRVQNAFGYgLFTGGLGLHYGAERLGA--TVIPAG 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 248 DAKTALQV--MEQNHITCFITVPAMMADLIRVnrttkngAENRG-------VRKILNGGGSLSSEL---LKEAVNIfpca 315
Cdd:COG1541 161 GGNTERQLrlMQDFGPTVLVGTPSYLLYLAEV-------AEEEGidprdlsLKKGIFGGEPWSEEMrkeIEERWGI---- 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 316 RILSAYGMTEA-------CSSLTFMTLHdptQESFkvtYPLLNQPkqGTcvGKPAPHIElmvkldedssrVGKI----LT 384
Cdd:COG1541 230 KAYDIYGLTEVgpgvayeCEAQDGLHIW---EDHF---LVEIIDP--ET--GEPVPEGE-----------EGELvvttLT 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 385 RGPHTMLRYWghqvaqenvetsesrsneawldTGDIGAFDE-----------FGNlwLIGRSNGRIKTGGENVYPEEVEA 453
Cdd:COG1541 289 KEAMPLIRYR----------------------TGDLTRLLPepcpcgrthprIGR--ILGRADDMLIIRGVNVFPSQIEE 344
|
330 340 350
....*....|....*....|....*....|.
gi 22329863 454 VLVEHPGIVSAVVIGVidTRLGEMVVACVRL 484
Cdd:COG1541 345 VLLRIPEVGPEYQIVV--DREGGLDELTVRV 373
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
450-539 |
4.19e-13 |
|
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: 64.49 E-value: 4.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 450 EVEAVLVEHPGIVSAVVIGVIDTRLGEMVVACVRLqekwiwsdvenrKGSFQLSSETLKHHCRtQNLTGFKIPKRFVRWE 529
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVL------------KPGVELLEEELVAHVR-EELGPYAVPKEVVFVD 67
|
90
....*....|
gi 22329863 530 kQFPLTTTGK 539
Cdd:pfam13193 68 -ELPKTRSGK 76
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
171-547 |
5.73e-13 |
|
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: 70.89 E-value: 5.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 171 SDDAVVIcFTSGTTGRPKGVTISH---LAFITqSLAKIAIAGYGEDDVYLHTSPLVHIGGLSSAMAMLMVGACHVLLP-- 245
Cdd:cd17648 94 TDLAYAI-YTSGTTGKPKGVLVEHgsvVNLRT-SLSERYFGRDNGDEAVLFFSNYVFDFFVEQMTLALLNGQKLVVPPde 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 246 -KFDAKTALQVMEQNHITCFITVPAM--MADLIRVNRttkngaenrgVRKILNGGGSLSSELLKEAVNIFPcARILSAYG 322
Cdd:cd17648 172 mRFDPDRFYAYINREKVTYLSGTPSVlqQYDLARLPH----------LKRVDAAGEEFTAPVFEKLRSRFA-GLIINAYG 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 323 MTEacSSLTfmtlhdptqeSFKVTYPllNQPKQGTCVGKPAPHIELMVkLDEDSSRV-----------GKILTRGPH--- 388
Cdd:cd17648 241 PTE--TTVT----------NHKRFFP--GDQRFDKSLGRPVRNTKCYV-LNDAMKRVpvgavgelylgGDGVARGYLnrp 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 389 --TMLRYWGH--QVAQENVETSESRSNEawldTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSA 464
Cdd:cd17648 306 elTAERFLPNpfQTEQERARGRNARLYK----TGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVREC 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 465 VVIGvidtrlgemvvacvRLQEKWIWSDVENRKGSFQLSSE------TLKHHCRTQnLTGFKIPKRFVRWEkQFPLTTTG 538
Cdd:cd17648 382 AVVA--------------KEDASQAQSRIQKYLVGYYLPEPghvpesDLLSFLRAK-LPRYMVPARLVRLE-GIPVTING 445
|
....*....
gi 22329863 539 KVkrdEVRR 547
Cdd:cd17648 446 KL---DVRA 451
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
30-548 |
9.28e-13 |
|
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: 70.53 E-value: 9.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 30 NRKRTGREFVDGVLSLAAGLIRLGLRNGDVVSIAAFNSDLFLEWLLAVALVGGVVAPLNYRwslkeakmamLLVEPVLlv 109
Cdd:cd05939 1 DRHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSN----------LRLESLL-- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 110 tdetcvsWCIDVQNgdipslkwrvlmesTSTDFANELNQFLTTEMLKQRTLVPSLATyawasdDAVVICFTSGTTGRPKG 189
Cdd:cd05939 69 -------HCITVSK--------------AKALIFNLLDPLLTQSSTEPPSQDDVNFR------DKLFYIYTSGTTGLPKA 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 190 VTISHLAFItqSLAKIAIAGYG--EDDVYLHTSPLVH-IGGLSSAMAMLMVGACHVLLPKFDA-KTALQVMEQNhitcfI 265
Cdd:cd05939 122 AVIVHSRYY--RIAAGAYYAFGmrPEDVVYDCLPLYHsAGGIMGVGQALLHGSTVVIRKKFSAsNFWDDCVKYN-----C 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 266 TVPAMMADLIRVNRTTKNGAENRGVRKILNGGGSLSSELLKEAVNIFPCARILSAYGMTEACSSLT----------FMTL 335
Cdd:cd05939 195 TIVQYIGEICRYLLAQPPSEEEQKHNVRLAVGNGLRPQIWEQFVRRFGIPQIGEFYGATEGNSSLVnidnhvgacgFNSR 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 336 HDPTQESFKV------TYPLLNQPKqGTCV----GKPAphieLMvkldedssrVGKILTRGPhtMLRYWGH----QVAQE 401
Cdd:cd05939 275 ILPSVYPIRLikvdedTGELIRDSD-GLCIpcqpGEPG----LL---------VGKIIQNDP--LRRFDGYvnegATNKK 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 402 NVETSESRSNEAWLdTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGV-IDTRLGEMVVA 480
Cdd:cd05939 339 IARDVFKKGDSAFL-SGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVYGVeVPGVEGRAGMA 417
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22329863 481 CVrlqekwiwSDVENRKGSFQLSSETLKhhcrtqNLTGFKIPKrFVRWEKQFPLTTTGKVKRDEVRRQ 548
Cdd:cd05939 418 AI--------VDPERKVDLDRFSAVLAK------SLPPYARPQ-FIRLLPEVDKTGTFKLQKTDLQKE 470
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
6-547 |
1.60e-12 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 70.31 E-value: 1.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 6 RPHIC-QCLTRLASVKRNAVVTVY--GNR-----KRTGREFVDGVLSLAAGLIRLGLRNGDVVSIAAfnsDLFLEW---L 74
Cdd:PLN02654 86 KTNICyNCLDRNVEAGNGDKIAIYweGNEpgfdaSLTYSELLDRVCQLANYLKDVGVKKGDAVVIYL---PMLMELpiaM 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 75 LAVALVGGVVAPLNYRWSLKEAKMAMLLVEPVLLVTdetcvswCIDVQNGDIP-SLKWRV---LMESTSTDFANELnqFL 150
Cdd:PLN02654 163 LACARIGAVHSVVFAGFSAESLAQRIVDCKPKVVIT-------CNAVKRGPKTiNLKDIVdaaLDESAKNGVSVGI--CL 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 151 TTE----MLKQRT------------LVPSLAT---YAWA-SDDAVVICFTSGTTGRPKGVTISHLAFITQSLAKIAIA-G 209
Cdd:PLN02654 234 TYEnqlaMKREDTkwqegrdvwwqdVVPNYPTkceVEWVdAEDPLFLLYTSGSTGKPKGVLHTTGGYMVYTATTFKYAfD 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 210 YGEDDVYLHTSPLVHIGGLSSAMAMLMVGACHVLL----PKF-DAKTALQVMEQNHITCFITVPAMMADLIRvnrttkNG 284
Cdd:PLN02654 314 YKPTDVYWCTADCGWITGHSYVTYGPMLNGATVLVfegaPNYpDSGRCWDIVDKYKVTIFYTAPTLVRSLMR------DG 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 285 AE--NRGVRKILNGGGSLSSELLKEA----VNIFPCAR--ILSAYGMTEACSsltFMTLHDP---TQESFKVTYPLLN-Q 352
Cdd:PLN02654 388 DEyvTRHSRKSLRVLGSVGEPINPSAwrwfFNVVGDSRcpISDTWWQTETGG---FMITPLPgawPQKPGSATFPFFGvQ 464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 353 PK---------QGTCVGKpaphieLMVKldedSSRVGKILT-RGPHTmlRYwghqvaqenvETSESRSNEAWLDTGDIGA 422
Cdd:PLN02654 465 PVivdekgkeiEGECSGY------LCVK----KSWPGAFRTlYGDHE--RY----------ETTYFKPFAGYYFSGDGCS 522
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 423 FDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGVIDTRLGEMVVACVRLQEKWIWSDvENRKgsfql 502
Cdd:PLN02654 523 RDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEVKGQGIYAFVTLVEGVPYSE-ELRK----- 596
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 22329863 503 sseTLKHHCRTQnLTGFKIPKRfVRWEKQFPLTTTGKVKRDEVRR 547
Cdd:PLN02654 597 ---SLILTVRNQ-IGAFAAPDK-IHWAPGLPKTRSGKIMRRILRK 636
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
177-544 |
2.76e-12 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341309 [Multi-domain] Cd Length: 449 Bit Score: 69.04 E-value: 2.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 177 ICFTSGTTGRPKGVTISH---LAFITQSLAKIAIAgygEDDVYLHTSPLVHIGGLSSAMAMLMVGACHVLLP----KFDA 249
Cdd:cd17654 123 VIHTSGTTGTPKIVAVPHkciLPNIQHFRSLFNIT---SEDILFLTSPLTFDPSVVEIFLSLSSGATLLIVPtsvkVLPS 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 250 KTALQVMEQNHITCFITVPAMMADLIRVNRTTKNGAENRGVRKILNGGGSL-SSELLKEAVNIFPCARILSAYGMTEACS 328
Cdd:cd17654 200 KLADILFKRHRITVLQATPTLFRRFGSQSIKSTVLSATSSLRVLALGGEPFpSLVILSSWRGKGNRTRIFNIYGITEVSC 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 329 -SLTFmtlHDPTQES-FKVTYPLLNQPKQGTCVGKPAPHIELMVKLdedSSRVGkiLTRGPHTmlrywghqvaqenvets 406
Cdd:cd17654 280 wALAY---KVPEEDSpVQLGSPLLGTVIEVRDQNGSEGTGQVFLGG---LNRVC--ILDDEVT----------------- 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 407 esRSNEAWLDTGDIGAFDEfGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGVIDtrlgEMVVACVRLQE 486
Cdd:cd17654 335 --VPKGTMRATGDFVTVKD-GELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGVESCAVTLSDQ----QRLIAFIVGES 407
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 22329863 487 KwiwsdvenrkgsfqlsSETLKHHCRTQNLTGFKIPKRFVRWEKqFPLTTTGKVKRDE 544
Cdd:cd17654 408 S----------------SSRIHKELQLTLLSSHAIPDTFVQIDK-LPLTSHGKVDKSE 448
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
36-542 |
3.86e-12 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 69.30 E-value: 3.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 36 REFVDGVLSLAAGLIRLGLRNGDVVSIAAFNSdLFLEW-LLAVALVGGVVAPLNYRWSlkEAKMAMLLVE--PVLLVTDE 112
Cdd:PRK10252 487 REMREQVVALANLLRERGVKPGDSVAVALPRS-VFLTLaLHAIVEAGAAWLPLDTGYP--DDRLKMMLEDarPSLLITTA 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 113 tcvswciDVQN--GDIPSLKwrvlmeststdfanelnqFLTTEMLKQRTLVPSLATYAwASDDAVVIcFTSGTTGRPKGV 190
Cdd:PRK10252 564 -------DQLPrfADVPDLT------------------SLCYNAPLAPQGAAPLQLSQ-PHHTAYII-FTSGSTGRPKGV 616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 191 TISHLAFITQSLAKIAIAGYGEDDVYLHTSPLVHIGGLSSAMAMLMVGACHVLLPKfDAK---TALQ-VMEQNHITCFIT 266
Cdd:PRK10252 617 MVGQTAIVNRLLWMQNHYPLTADDVVLQKTPCSFDVSVWEFFWPFIAGAKLVMAEP-EAHrdpLAMQqFFAEYGVTTTHF 695
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 267 VPAMMAdlIRVNRTTKNGAEN--RGVRKILNGGGSLSSELLKE---AVNifpcARILSAYGMTEACSSLTFmtlhdptqe 341
Cdd:PRK10252 696 VPSMLA--AFVASLTPEGARQscASLRQVFCSGEALPADLCREwqqLTG----APLHNLYGPTEAAVDVSW--------- 760
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 342 sfkvtYP-----LLNQPKQGTCVGKPAPHIELMVkLDEDSSRVgkiltrgPHTM---LRYWGHQVAQ---ENVETSESR- 409
Cdd:PRK10252 761 -----YPafgeeLAAVRGSSVPIGYPVWNTGLRI-LDARMRPV-------PPGVagdLYLTGIQLAQgylGRPDLTASRf 827
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 410 ------SNEAWLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVvigvidtrlgemVVACVR 483
Cdd:PRK10252 828 iadpfaPGERMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAV------------THACVI 895
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22329863 484 LQekwiwsDVENRKGSFQL------------SSETLKHHCRTQnLTGFKIPKRFVRWEkQFPLTTTGKVKR 542
Cdd:PRK10252 896 NQ------AAATGGDARQLvgylvsqsglplDTSALQAQLRER-LPPHMVPVVLLQLD-QLPLSANGKLDR 958
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
162-542 |
1.24e-11 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 67.89 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 162 PSLATYAWASDDAV-------VICFTSGTTGRPKGVTISHLAFITQSLAKIAIAGYGEDDVYLHTSPLVHIGGLSSAMAM 234
Cdd:PRK05691 2316 AALAAYSDAPLPFLslpqhqaYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIERFGMRADDCELHFYSINFDAASERLLVP 2395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 235 LMVGACHVLLP--KFDAKTALQVMEQNHITCFITVPAMMADLIRVNRTTkngAENRGVRKILNGGGSLSSELLKEAVNIF 312
Cdd:PRK05691 2396 LLCGARVVLRAqgQWGAEEICQLIREQQVSILGFTPSYGSQLAQWLAGQ---GEQLPVRMCITGGEALTGEHLQRIRQAF 2472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 313 PCARILSAYGMTEAcsslTFMTLHDPTQESFK---VTYPLlnqpkqGTCVGKPAPHIelmvkLDEDSSRV---------- 379
Cdd:PRK05691 2473 APQLFFNAYGPTET----VVMPLACLAPEQLEegaASVPI------GRVVGARVAYI-----LDADLALVpqgatgelyv 2537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 380 -GKILTRGPHTMLRYwghqVAQENVETSESRSNEAWLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEH 458
Cdd:PRK05691 2538 gGAGLAQGYHDRPGL----TAERFVADPFAADGGRLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEH 2613
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 459 PGIVSAVVIGViDTRLGEMVVAcvrlqekWIWSDVENRKGSFQLS-SETLKHHCRTQnLTGFKIPKRFVRWEKqFPLTTT 537
Cdd:PRK05691 2614 PAVREAVVLAL-DTPSGKQLAG-------YLVSAVAGQDDEAQAAlREALKAHLKQQ-LPDYMVPAHLILLDS-LPLTAN 2683
|
....*
gi 22329863 538 GKVKR 542
Cdd:PRK05691 2684 GKLDR 2688
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
52-469 |
2.30e-11 |
|
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: 66.16 E-value: 2.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 52 LGLRNGDVVSIAAFNSDLFLEWLLAVALVGGVVAPLNYRW-------SLKEAKMAMLLVEPVLLVTDETcvswcidvqng 124
Cdd:cd05938 26 AGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIrsksllhCFRCCGAKVLVVAPELQEAVEE----------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 125 DIPSLK-----WRVLMESTSTDFANELNQFLTTEmlkQRTLVP-SLATYAWASDDAVVIcFTSGTTGRPKGVTISHLAfI 198
Cdd:cd05938 95 VLPALRadgvsVWYLSHTSNTEGVISLLDKVDAA---SDEPVPaSLRAHVTIKSPALYI-YTSGTTGLPKAARISHLR-V 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 199 TQSLAKIAIAGYGEDDVYLHTSPLVH-IGGLSSAMAMLMVGACHVLLPKFDAktalqvmeqnhiTCF--------ITVPA 269
Cdd:cd05938 170 LQCSGFLSLCGVTADDVIYITLPLYHsSGFLLGIGGCIELGATCVLKPKFSA------------SQFwddcrkhnVTVIQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 270 MMADLIR--VNRTTKNGAENRGVRKILngGGSLSSELLKEAVNIFPCARILSAYGMTEAcsSLTFMT------------- 334
Cdd:cd05938 238 YIGELLRylCNQPQSPNDRDHKVRLAI--GNGLRADVWREFLRRFGPIRIREFYGSTEG--NIGFFNytgkigavgrvsy 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 335 LH-----------DPTQESfkvtyPLLNqpKQGTCVgkpaphielMVKLDEDSSRVGKILTRGPhtMLRYWGHQvaqenv 403
Cdd:cd05938 314 LYkllfpfelikfDVEKEE-----PVRD--AQGFCI---------PVAKGEPGLLVAKITQQSP--FLGYAGDK------ 369
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22329863 404 ETSES-------RSNEAWLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGV 469
Cdd:cd05938 370 EQTEKkllrdvfKKGDVYFNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVYGV 442
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
138-464 |
4.84e-11 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 65.52 E-value: 4.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 138 TSTDFANELNQFLTTEMLKQRT------LVPSLATYAWA-----SDDAVVICFTSGTTGRPKGVTISHLAFITQSLAKIA 206
Cdd:PRK07769 135 TTTDSAEGVRKFFRARPAKERPrviavdAVPDEVGATWVppeanEDTIAYLQYTSGSTRIPAGVQITHLNLPTNVLQVID 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 207 IAGYGEDDVYLHTSPLVHIGGLSSAMAMLMVG--------ACHVLLPKFDAKtALQVMEQNHITCFITVPAMMADLIRVN 278
Cdd:PRK07769 215 ALEGQEGDRGVSWLPFFHDMGLITVLLPALLGhyitfmspAAFVRRPGRWIR-ELARKPGGTGGTFSAAPNFAFEHAAAR 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 279 RTTKNGAEN---RGVRKILNGGGSLSSELLKEAVNIF-----PCARILSAYGMTEAcsslTFMTLHDPTQESFKVTYPLL 350
Cdd:PRK07769 294 GLPKDGEPPldlSNVKGLLNGSEPVSPASMRKFNEAFapyglPPTAIKPSYGMAEA----TLFVSTTPMDEEPTVIYVDR 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 351 NQPKQGTCVGKPA------PHI--------ELMVKLDEDSS------RVGKILTRGPHTMLRYWGHqvAQENVET----- 405
Cdd:PRK07769 370 DELNAGRFVEVPAdapnavAQVsagkvgvsEWAVIVDPETAselpdgQIGEIWLHGNNIGTGYWGK--PEETAATfqnil 447
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22329863 406 ----SESRSNEA-----WLDTGDIGAFDEfGNLWLIGRSNGRIKTGGENVYPEEVEAVLVE-----HPGIVSA 464
Cdd:PRK07769 448 ksrlSESHAEGApddalWVRTGDYGVYFD-GELYITGRVKDLVIIDGRNHYPQDLEYTAQEatkalRTGYVAA 519
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
28-548 |
5.49e-11 |
|
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: 64.76 E-value: 5.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 28 YGNRKRTGREFVDGVLSLAAGLI-RLGLRNGDVVSIAAFNSDLFLEWLLAVALVGGVVAPLNYRwslkeakmamllvepv 106
Cdd:cd05937 1 FEGKTWTYSETYDLVLRYAHWLHdDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYN---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 107 llVTDETCVSwCIDVqngdipslkwrvlmeSTSTdfanelnQFLTTEmlkqrtlvpslatyawasDDAVVICFTSGTTGR 186
Cdd:cd05937 65 --LSGDPLIH-CLKL---------------SGSR-------FVIVDP------------------DDPAILIYTSGTTGL 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 187 PKGVTISHLAFITQSLAKIAIAGYGEDDVYLHTSPLVH-IGGLSSAMAMLMVGACHVLLPKFDAKTALQVMEQNHITCFI 265
Cdd:cd05937 102 PKAAAISWRRTLVTSNLLSHDLNLKNGDRTYTCMPLYHgTAAFLGACNCLMSGGTLALSRKFSASQFWKDVRDSGATIIQ 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 266 TVpammADLIRVNRTTKNGAENRGVRKILNGGGSLSSELLKEAVNIFPCARILSAYGMTEACSSLT-------------- 331
Cdd:cd05937 182 YV----GELCRYLLSTPPSPYDRDHKVRVAWGNGLRPDIWERFRERFNVPEIGEFYAATEGVFALTnhnvgdfgagaigh 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 332 -------------FMTLHDPTQESfkvtypLLNQPKQGTCVgkpaphielMVKLDEDSSRVGKILTRGPHTMLRYWGHQV 398
Cdd:cd05937 258 hglirrwkfenqvVLVKMDPETDD------PIRDPKTGFCV---------RAPVGEPGEMLGRVPFKNREAFQGYLHNED 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 399 A-QENVETSESRSNEAWLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGVI----DTR 473
Cdd:cd05937 323 AtESKLVRDVFRKGDIYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGVKvpghDGR 402
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22329863 474 LGemvVACVRLQEKWIWSDVENrkgsFQLssetLKHHCRtQNLTGFKIPkRFVRWEKQFPLTTTGKVKRDEVRRQ 548
Cdd:cd05937 403 AG---CAAITLEESSAVPTEFT----KSL----LASLAR-KNLPSYAVP-LFLRLTEEVATTDNHKQQKGVLRDE 464
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
172-508 |
7.01e-10 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 61.78 E-value: 7.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 172 DDAVVICFTSGTTGRPKGVTISHLAFI-----TQSLAKIAIAGYGEDDVYLHTSPLVHIGGLSSAMAMLMVGAChVLLPK 246
Cdd:PLN02861 220 TDICTIMYTSGTTGEPKGVILTNRAIIaevlsTDHLLKVTDRVATEEDSYFSYLPLAHVYDQVIETYCISKGAS-IGFWQ 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 247 FDAKTALQVMEQNHITCFITVP---------AMM----ADLIR-------------------------------VNRTTK 282
Cdd:PLN02861 299 GDIRYLMEDVQALKPTIFCGVPrvydriytgIMQkissGGMLRkklfdfaynyklgnlrkglkqeeasprldrlVFDKIK 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 283 NGAENRgVRKILNGGGSLSSELlKEAVNIFPCARILSAYGMTEACSSlTFMTLHDptqesfkvTYPLLnqpkqGTcVGKP 362
Cdd:PLN02861 379 EGLGGR-VRLLLSGAAPLPRHV-EEFLRVTSCSVLSQGYGLTESCGG-CFTSIAN--------VFSMV-----GT-VGVP 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 363 APHIELMV----KLDEDS-SRV--GKILTRGpHTMLR-YWGHQvaqenvETSESRSNEAWLDTGDIGAFDEFGNLWLIGR 434
Cdd:PLN02861 442 MTTIEARLesvpEMGYDAlSDVprGEICLRG-NTLFSgYHKRQ------DLTEEVLIDGWFHTGDIGEWQPNGAMKIIDR 514
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22329863 435 SNGRIK-TGGENVYPEEVEAVLVEHPGIVSAVVIGvidTRLGEMVVACVRLQEKWI--WSDVENRKGSFQLSSETLK 508
Cdd:PLN02861 515 KKNIFKlSQGEYVAVENLENTYSRCPLIASIWVYG---NSFESFLVAVVVPDRQALedWAANNNKTGDFKSLCKNLK 588
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
180-549 |
1.86e-09 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 60.16 E-value: 1.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 180 TSGTTGRPKGVTISHLAFITQSLAKIAIAGYGED-DVYLHTSPLVHIGGLSSAMAMLMVGACHVLLPKfDAKTA-----L 253
Cdd:PRK05851 160 TAGSTGTPRTAILSPGAVLSNLRGLNARVGLDAAtDVGCSWLPLYHDMGLAFLLTAALAGAPLWLAPT-TAFSAspfrwL 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 254 QVMEQNHITcFITVPAMMADLI-----RVNrttknGAENRGVRKILNGGGSL---SSELLKEAVNIF---PCArILSAYG 322
Cdd:PRK05851 239 SWLSDSRAT-LTAAPNFAYNLIgkyarRVS-----DVDLGALRVALNGGEPVdcdGFERFATAMAPFgfdAGA-AAPSYG 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 323 MTEACSSLTFMTLHDPTQESfKVTYPLLNQPKQGTCVGKPAPHIELMVKLDEDSS-----RVGKILTRGPHTMLRYWGHQ 397
Cdd:PRK05851 312 LAESTCAVTVPVPGIGLRVD-EVTTDDGSGARRHAVLGNPIPGMEVRISPGDGAAgvagrEIGEIEIRGASMMSGYLGQA 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 398 vaqenvetseSRSNEAWLDTGDIGAFDEfGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGI----VSAVVIGVIDTR 473
Cdd:PRK05851 391 ----------PIDPDDWFPTGDLGYLVD-GGLVVCGRAKELITVAGRNIFPTEIERVAAQVRGVregaVVAVGTGEGSAR 459
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22329863 474 LGEMVVACVRlqekwiWSDVENRKgsfqlsSETLKhhcRTQNLTGFkIPKRFVRWEK-QFPLTTTGKVKRDEVRRQV 549
Cdd:PRK05851 460 PGLVIAAEFR------GPDEAGAR------SEVVQ---RVASECGV-VPSDVVFVAPgSLPRTSSGKLRRLAVKRSL 520
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
153-455 |
4.94e-08 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 56.33 E-value: 4.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 153 EMLKQRTLVPSLATyAW-----ASDDAVVICFTSGTTGRPKGVTISHLAFITQSLakIAIAGYG----EDDVYLHTSPLV 223
Cdd:PRK05691 143 ELLCVDTLDPALAE-AWqepalQPDDIAFLQYTSGSTALPKGVQVSHGNLVANEQ--LIRHGFGidlnPDDVIVSWLPLY 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 224 H----IGGLssamamlmvgachvLLPKFDAktalqvmeqnhITCFITVPAMMadLIRVNRTTKNGAENRGVrkiLNGGGS 299
Cdd:PRK05691 220 HdmglIGGL--------------LQPIFSG-----------VPCVLMSPAYF--LERPLRWLEAISEYGGT---ISGGPD 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 300 LSSELLKEAVNIFPCARI-LS----AYGMTEACSSLTFMTLHDP------TQESFKVTY------------------PLL 350
Cdd:PRK05691 270 FAYRLCSERVSESALERLdLSrwrvAYSGSEPIRQDSLERFAEKfaacgfDPDSFFASYglaeatlfvsggrrgqgiPAL 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 351 N-----------QPKQGT---CVGKPAP-HIELMV---KLDE-DSSRVGKILTRGPHTMLRYWGHqvAQENVETSESRSN 411
Cdd:PRK05691 350 EldaealarnraEPGTGSvlmSCGRSQPgHAVLIVdpqSLEVlGDNRVGEIWASGPSIAHGYWRN--PEASAKTFVEHDG 427
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 22329863 412 EAWLDTGDIGaFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVL 455
Cdd:PRK05691 428 RTWLRTGDLG-FLRDGELFVTGRLKDMLIVRGHNLYPQDIEKTV 470
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
417-560 |
5.88e-08 |
|
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: 55.65 E-value: 5.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 417 TGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGVIDTRLGEMVVACVRLQEKWIWSDvenr 496
Cdd:cd05966 473 TGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGEEPSD---- 548
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22329863 497 kgsfQLSSEtLKHHCRTQnLTGFKIPKRfVRWEKQFPLTTTGKVKRdEVRRQVLSHFQIM--TSSL 560
Cdd:cd05966 549 ----ELRKE-LRKHVRKE-IGPIATPDK-IQFVPGLPKTRSGKIMR-RILRKIAAGEEELgdTSTL 606
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
31-484 |
1.33e-07 |
|
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: 54.36 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 31 RKRTGREFVDGVLSLAAGLIRLGLRNGDVVSIAAFNSDLFLEWLLAVALVGGVVAPLNYRWSLKEAKMAML-----LVEP 105
Cdd:cd05921 24 RRVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSPAYSLMSQDLAKLkhlfeLLKP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 106 -VLLVTDETCVSWCID-VQNGDIPSLKWRVLMES-TSTDFANELNQFLTTEmlkqrtlVPSLATyAWASDDAVVICFTSG 182
Cdd:cd05921 104 gLVFAQDAAPFARALAaIFPLGTPLVVSRNAVAGrGAISFAELAATPPTAA-------VDAAFA-AVGPDTVAKFLFTSG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 183 TTGRPKGVTISH--LAFITQSLAKIAIAGYGEDDVYLHTSPLVHIGGLSSAMAMLMVGACHVLLPkfDAKTALQVMEQN- 259
Cdd:cd05921 176 STGLPKAVINTQrmLCANQAMLEQTYPFFGEEPPVLVDWLPWNHTFGGNHNFNLVLYNGGTLYID--DGKPMPGGFEETl 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 260 ------HITCFITVPAMMADLIRVNRTTKNGAEN--RGVRKILNGGGSLSSELLK--EAVNIFPCA---RILSAYGMTEA 326
Cdd:cd05921 254 rnlreiSPTVYFNVPAGWEMLVAALEKDEALRRRffKRLKLMFYAGAGLSQDVWDrlQALAVATVGeriPMMAGLGATET 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 327 CSSLTFMtlHDPTQESfkvtypllnqpkqGTcVGKPAPHIElmVKLDEDSSRVgKILTRGPHTMLRYWGhqvAQEnvETS 406
Cdd:cd05921 334 APTATFT--HWPTERS-------------GL-IGLPAPGTE--LKLVPSGGKY-EVRVKGPNVTPGYWR---QPE--LTA 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 407 ESRSNEAWLDTGDIGAF----DEFGNLWLIGR--SNGRIKTGG-ENVYPEEVEAVLVEHPGIVSAVVIGVIDTRLGEMVV 479
Cdd:cd05921 390 QAFDEEGFYCLGDAAKLadpdDPAKGLVFDGRvaEDFKLASGTwVSVGPLRARAVAACAPLVHDAVVAGEDRAEVGALVF 469
|
....*....
gi 22329863 480 ----ACVRL 484
Cdd:cd05921 470 pdllACRRL 478
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
174-542 |
1.38e-07 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 54.79 E-value: 1.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 174 AVVIcFTSGTTGRPKGVTISHLAFITQSLAKIAIAGYGEDDVYLHTSPLVHIGGLSSAMAMLMVGACHVLLPK---FDAK 250
Cdd:PRK05691 3872 AYVI-YTSGSTGLPKGVMVEQRGMLNNQLSKVPYLALSEADVIAQTASQSFDISVWQFLAAPLFGARVEIVPNaiaHDPQ 3950
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 251 TALQVMEQNHITCFITVPAMMADLIRVNRTTKNgaenrGVRKILNGGGSLSSELLKEAVNIFPCARILSAYGMTEACSSL 330
Cdd:PRK05691 3951 GLLAHVQAQGITVLESVPSLIQGMLAEDRQALD-----GLRWMLPTGEAMPPELARQWLQRYPQIGLVNAYGPAECSDDV 4025
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 331 TFMTLhdpTQESFKVTY-PllnqpkqgtcVGKPAPHIELMVkLDEDSS-----RVGKILTRGPHTMLRYWGHQV--AQEN 402
Cdd:PRK05691 4026 AFFRV---DLASTRGSYlP----------IGSPTDNNRLYL-LDEALElvplgAVGELCVAGTGVGRGYVGDPLrtALAF 4091
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 403 VETSESRSNEAWLDTGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVViGVIDTRLGEMVVA-- 480
Cdd:PRK05691 4092 VPHPFGAPGERLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAV-AVQEGVNGKHLVGyl 4170
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22329863 481 ----CVRLQEKWIwsdvenrkgsfqlssETLKHHCRTQnLTGFKIPKRFVrWEKQFPLTTTGKVKR 542
Cdd:PRK05691 4171 vphqTVLAQGALL---------------ERIKQRLRAE-LPDYMVPLHWL-WLDRLPLNANGKLDR 4219
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
179-487 |
2.19e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 50.33 E-value: 2.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 179 FTSGTTGRPKGVTISHLAFIT--QSLAKIAIAGYG----EDDVYLHTSPLVHIGGLSSAMAMLMVGACHVLL--P-KFDA 249
Cdd:PRK05850 167 YTSGSTRTPAGVMVSHRNVIAnfEQLMSDYFGDTGgvppPDTTVVSWLPFYHDMGLVLGVCAPILGGCPAVLtsPvAFLQ 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 250 KTA--LQVMeQNHITCFITVPAMMADLIrVNRTTK---NGAENRGVRKILNGGGSLSSELLKEAVNIFpcAR-------I 317
Cdd:PRK05850 247 RPArwMQLL-ASNPHAFSAAPNFAFELA-VRKTSDddmAGLDLGGVLGIISGSERVHPATLKRFADRF--APfnlretaI 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 318 LSAYGMTEAcssltfmTL--------HDPTQ-----ESFKVTYPLLNQPKQGT-CVGKPAPHIELMVKLDEDSSR----- 378
Cdd:PRK05850 323 RPSYGLAEA-------TVyvatrepgQPPESvrfdyEKLSAGHAKRCETGGGTpLVSYGSPRSPTVRIVDPDTCIecpag 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 379 -VGKILTRGPHTMLRYWgHQVAQEN-------VETSESRSNEAWLDTGDIGAFDEfGNLWLIGRSNGRIKTGGENVYPEE 450
Cdd:PRK05850 396 tVGEIWVHGDNVAAGYW-QKPEETErtfgatlVDPSPGTPEGPWLRTGDLGFISE-GELFIVGRIKDLLIVDGRNHYPDD 473
|
330 340 350
....*....|....*....|....*....|....*...
gi 22329863 451 VEAVLVE-HPGIVSAVVIGVIDTrlgEMVVACVRLQEK 487
Cdd:PRK05850 474 IEATIQEiTGGRVAAISVPDDGT---EKLVAIIELKKR 508
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
31-423 |
2.68e-06 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 50.26 E-value: 2.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 31 RKRTGREFVDGVLSLAAGLIRLGLRNGDVVSIAAFNSdlfLE-WLLAVA--LVGGVVAPLNYRWSLKEAKMAML-----L 102
Cdd:PRK08180 68 RRLTYAEALERVRAIAQALLDRGLSAERPLMILSGNS---IEhALLALAamYAGVPYAPVSPAYSLVSQDFGKLrhvleL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 103 VEPVLLVTDET---------CVSWCIDV--QNGDIPSlkwrvlmeSTSTDFAnelnqflttEMLKQRTLVPSLATYAWAS 171
Cdd:PRK08180 145 LTPGLVFADDGaafaralaaVVPADVEVvaVRGAVPG--------RAATPFA---------ALLATPPTAAVDAAHAAVG 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 172 DDAVV-ICFTSGTTGRPKGVTISHL------AFITQSLAKIAIagygEDDVYLHTSPLVHIGGLSSAMAM-LMVGACHVL 243
Cdd:PRK08180 208 PDTIAkFLFTSGSTGLPKAVINTHRmlcanqQMLAQTFPFLAE----EPPVLVDWLPWNHTFGGNHNLGIvLYNGGTLYI 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 244 -----LPKFDAKTALQVMEqnhI--TCFITVPAMMADLIRVNRTTKNGAEN--RGVRKILNGGGSLSSELLK--EAVNIF 312
Cdd:PRK08180 284 ddgkpTPGGFDETLRNLRE---IspTVYFNVPKGWEMLVPALERDAALRRRffSRLKLLFYAGAALSQDVWDrlDRVAEA 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 313 PC---ARILSAYGMTEACSSLTFmtlhdptqesfkVTYPLlnqPKQGtCVGKPAPHIEL-MVKLDedssrvGK--ILTRG 386
Cdd:PRK08180 361 TCgerIRMMTGLGMTETAPSATF------------TTGPL---SRAG-NIGLPAPGCEVkLVPVG------GKleVRVKG 418
|
410 420 430
....*....|....*....|....*....|....*..
gi 22329863 387 PHTMLRYWGHQVAqenveTSESRSNEAWLDTGDIGAF 423
Cdd:PRK08180 419 PNVTPGYWRAPEL-----TAEAFDEEGYYRSGDAVRF 450
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
417-542 |
2.58e-05 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 47.06 E-value: 2.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 417 TGDiGA-FDEFGNLWLIGR-------SNGRIKTGgenvypeEVEAVLVEHPGIVSAVVIGVIDTRLGEMVVACVRLQekw 488
Cdd:PRK00174 487 TGD-GArRDEDGYYWITGRvddvlnvSGHRLGTA-------EIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLK--- 555
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 22329863 489 iwsdvENRKGSFQLSSEtLKHHCRTQnlTGfKIPK-RFVRWEKQFPLTTTGKVKR 542
Cdd:PRK00174 556 -----GGEEPSDELRKE-LRNWVRKE--IG-PIAKpDVIQFAPGLPKTRSGKIMR 601
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
54-461 |
4.97e-05 |
|
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: 46.29 E-value: 4.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 54 LRNGDVVSIAAFNSDLFLEWLLAVALVGGVVAPLNYrwSLKEAKMAMLL--VEPVLLVTDETCVSWCID-VQNGDIPSlk 130
Cdd:cd17632 90 VRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQA--GASAAQLAPILaeTEPRLLAVSAEHLDLAVEaVLEGGTPP-- 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 131 wRVL--------------MESTSTDFAN--ELNQFLTTEMLKQRTLVPSLATYAWASDDAVV-ICFTSGTTGRPKGVTIS 193
Cdd:cd17632 166 -RLVvfdhrpevdahraaLESARERLAAvgIPVTTLTLIAVRGRDLPPAPLFRPEPDDDPLAlLIYTSGSTGTPKGAMYT 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 194 HLAFITQSL-AKIAIAGYGEDDVYLHTSPLVHIGGLSSAMAMLMVGACHVLLPKFDAKTALQVMEQNHITCFITVPaMMA 272
Cdd:cd17632 245 ERLVATFWLkVSSIQDIRPPASITLNFMPMSHIAGRISLYGTLARGGTAYFAAASDMSTLFDDLALVRPTELFLVP-RVC 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 273 DLI------RVNRTTKNGAENRGV--------RKILNGG-------GS--LSSElLKEAVNIFPCARILSAYGMTEACSS 329
Cdd:cd17632 324 DMLfqryqaELDRRSVAGADAETLaervkaelRERVLGGrllaavcGSapLSAE-MKAFMESLLDLDLHDGYGSTEAGAV 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 330 LTFMTLHDPtqesfKVT-YPLLNQPKQGTCV-GKPAPHIELMVKLDEdssrvgkiLTRGphtmlrYWghqvaQENVETSE 407
Cdd:cd17632 403 ILDGVIVRP-----PVLdYKLVDVPELGYFRtDRPHPRGELLVKTDT--------LFPG------YY-----KRPEVTAE 458
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 22329863 408 SRSNEAWLDTGDIGAfdEFG--NLWLIGRSNGRIK-TGGENVYPEEVEAVLVEHPGI 461
Cdd:cd17632 459 VFDEDGFYRTGDVMA--ELGpdRLVYVDRRNNVLKlSQGEFVTVARLEAVFAASPLV 513
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
12-492 |
6.00e-05 |
|
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: 45.72 E-value: 6.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 12 CLTRLASVKRNAVVTVYGNRKR---TGREFVDGVLSLAAGLIRLGLRNGD-VVSIAAfNSDLFLEWLLAVALVGGVvapl 87
Cdd:cd05943 75 NLLRHADADDPAAIYAAEDGERtevTWAELRRRVARLAAALRALGVKPGDrVAGYLP-NIPEAVVAMLATASIGAI---- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 88 nyrWSLKEAKMAMLLV-------EPVLLVTDETCVSW-----CID----VQNGdIPSLKWRVLMESTSTDFANEL---NQ 148
Cdd:cd05943 150 ---WSSCSPDFGVPGVldrfgqiEPKVLFAVDAYTYNgkrhdVREkvaeLVKG-LPSLLAVVVVPYTVAAGQPDLskiAK 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 149 FLTTEMLKQRTLVPSLATYAWASDDAVVICFTSGTTGRPKGVTISHLAFITQSLAKIAI-AGYGEDDVYLHtsplvhigg 227
Cdd:cd05943 226 ALTLEDFLATGAAGELEFEPLPFDHPLYILYSSGTTGLPKCIVHGAGGTLLQHLKEHILhCDLRPGDRLFY--------- 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 228 LSSAMAM--------LMVGACHVLL---PKFDAKTAL-QVMEQNHITCFITVPAMMADLIRVNRTTKNGAENRGVRKILN 295
Cdd:cd05943 297 YTTCGWMmwnwlvsgLAVGATIVLYdgsPFYPDTNALwDLADEEGITVFGTSAKYLDALEKAGLKPAETHDLSSLRTILS 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 296 GGGSLSSELLKEAV-NIFPCARILSAYGMTEACSSltFMtLHDPTQesfkvtyPLLNQPKQGTCVGkpaphiELMVKLDE 374
Cdd:cd05943 377 TGSPLKPESFDYVYdHIKPDVLLASISGGTDIISC--FV-GGNPLL-------PVYRGEIQCRGLG------MAVEAFDE 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 375 DSSRV----GKILTRGPH-TM-LRYWGhqvaqenvETSESRSNEAWLDT-------GDIGAFDEFGNLWLIGRSNGRIKT 441
Cdd:cd05943 441 EGKPVwgekGELVCTKPFpSMpVGFWN--------DPDGSRYRAAYFAKypgvwahGDWIEITPRGGVVILGRSDGTLNP 512
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 22329863 442 GGENVYPEEVEAVLVEHPGIVSAVVIGVIDTRLGEMVVACVRLQEKWIWSD 492
Cdd:cd05943 513 GGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDERVILFVKLREGVELDD 563
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
417-542 |
2.17e-04 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 44.17 E-value: 2.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329863 417 TGDIGAFDEFGNLWLIGRSNGRIKTGGENVYPEEVEAVLVEHPGIVSAVVIGVIDTRLGEMVVACVRLQEKwiwSDVENR 496
Cdd:PRK10524 477 TFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPKDS---DSLADR 553
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 22329863 497 KGSFQLSSETLKHhcRTQNLTGFKIPKRfVRWEKQFPLTTTGKVKR 542
Cdd:PRK10524 554 EARLALEKEIMAL--VDSQLGAVARPAR-VWFVSALPKTRSGKLLR 596
|
|
| |
