|
Name |
Accession |
Description |
Interval |
E-value |
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
45-529 |
0e+00 |
|
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: 569.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 45 MQICDTTGQELTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNSTYLTSVIIAALLRGIPINPLHPEFTEETVKYMYDI 124
Cdd:cd05911 1 AQIDADTGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 125 TEPKVIFCDVENYHIIKTVNGKLQNPAKIYLVNGKLEGVLDISEMLNDEDSITAAAYVPCPKLHGDHTAFIVCSSGTTGM 204
Cdd:cd05911 81 SKPKVIFTDPDGLEKVKEAAKELGPKDKIIVLDDKPDGVLSIEDLLSPTLGEEDEDLPPPLKDGKDDTAAILYSSGTTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 205 PKGVTRSHRSLLCNCKNPNTYT-----RDSVLLSFSPLYWISGTIILLASLLNGCRRIITNRPYSvEYLLQLVARHKVTF 279
Cdd:cd05911 161 PKGVCLSHRNLIANLSQVQTFLygndgSNDVILGFLPLYHIYGLFTTLASLLNGATVIIMPKFDS-ELFLDLIEKYKITF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 280 LFLASHQIALLSKHDSDVmelKAQLQSIRVLIGAGSKVCKAVCRRMYELIGNQRFVVGYGLSEMGG-LSKNVGGPV--GC 356
Cdd:cd05911 240 LYLVPPIAAALAKSPLLD---KYDLSSLRVILSGGAPLSKELQELLAKRFPNATIKQGYGMTETGGiLTVNPDGDDkpGS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 357 EGKVMRNVELRVLDKL-KMPLGINEVGIIYARLRFKWAGYYRNPEATRRALSSDGmWFRTGDIGYLDSEGYLYIQTRDTD 435
Cdd:cd05911 317 VGRLLPNVEAKIVDDDgKDSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDG-WLHTGDIGYFDEDGYLYIVDRKKE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 436 VFKFNNFQIYPEQIEEFILRLPGVSEACVFGIPDAVSTNLTACAVVRTKspeGERLTADHIRNIVEHHLSGAYHIRGGVY 515
Cdd:cd05911 396 LIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKP---GEKLTEKEVKDYVAKKVASYKQLRGGVV 472
|
490
....*....|....
gi 19922652 516 FIDSLPKTPNDKLQ 529
Cdd:cd05911 473 FVDEIPKSASGKIL 486
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
29-544 |
8.78e-95 |
|
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: 296.34 E-value: 8.78e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 29 LGEVIMRVLQINADQVMQICDttGQELTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNSTYLTSVIIAALLRGIPINP 108
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFG--GRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 109 LHPEFTEETVKYMYDITEPKVIFcdvenyhiiktvngklqnpakiylvngklegvldisemlndedsitaaayvpcpklh 188
Cdd:COG0318 79 LNPRLTAEELAYILEDSGARALV--------------------------------------------------------- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 189 gdhTAFIVCSSGTTGMPKGVTRSHRSLLCNCKNPNTY---TRDSVLLSFSPLYWISG-TIILLASLLNGCRrIITNRPYS 264
Cdd:COG0318 102 ---TALILYTSGTTGRPKGVMLTHRNLLANAAAIAAAlglTPGDVVLVALPLFHVFGlTVGLLAPLLAGAT-LVLLPRFD 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 265 VEYLLQLVARHKVTFLFLA-SHQIALLSKHDSDvmelKAQLQSIRVLIGAGSKVCKAVCRRMYELIGNqRFVVGYGLSEM 343
Cdd:COG0318 178 PERVLELIERERVTVLFGVpTMLARLLRHPEFA----RYDLSSLRLVVSGGAPLPPELLERFEERFGV-RIVEGYGLTET 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 344 GGLS-----KNVGGPVGCEGKVMRNVELRVLDKLKMPLGINEVGIIYAR--LRFKwaGYYRNPEATRRALSsDGmWFRTG 416
Cdd:COG0318 253 SPVVtvnpeDPGERRPGSVGRPLPGVEVRIVDEDGRELPPGEVGEIVVRgpNVMK--GYWNDPEATAEAFR-DG-WLRTG 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 417 DIGYLDSEGYLYIQTRDTDVFKFNNFQIYPEQIEEFILRLPGVSEACVFGIPDAVSTNlTACAVVRTKspEGERLTADHI 496
Cdd:COG0318 329 DLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGE-RVVAFVVLR--PGAELDAEEL 405
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 19922652 497 RNIVEHHLSGAYHIRgGVYFIDSLPKTPNDKLQRRKVLGLVQQLELKA 544
Cdd:COG0318 406 RAFLRERLARYKVPR-RVEFVDELPRTASGKIDRRALRERYAAGALEA 452
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
191-529 |
1.31e-76 |
|
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: 245.27 E-value: 1.31e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 191 HTAFIVCSSGTTGMPKGVTRSHRSLLCNCKNPNT---YTRDSVLLSFSPLYWISGTIILLASLLNGCRRIITNRPySVEY 267
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAAsggLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKF-DPEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 268 LLQLVARHKVTFLFLASHQIALLSKHDSdvmELKAQLQSIRVLIGAGSKVCKAVCRRMYELIGNqRFVVGYGLSEMGG-- 345
Cdd:cd04433 80 ALELIEREKVTILLGVPTLLARLLKAPE---SAGYDLSSLRALVSGGAPLPPELLERFEEAPGI-KLVNGYGLTETGGtv 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 346 ---LSKNVGGPVGCEGKVMRNVELRVLDKLKMPLGINEVGIIYARLRFKWAGYYRNPEATRRALSsDGmWFRTGDIGYLD 422
Cdd:cd04433 156 atgPPDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVDE-DG-WYRTGDLGRLD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 423 SEGYLYIQTRDTDVFKFNNFQIYPEQIEEFILRLPGVSEACVFGIPDAVSTNLTACAVVRTkspEGERLTADHIRNIVEH 502
Cdd:cd04433 234 EDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLR---PGADLDAEELRAHVRE 310
|
330 340
....*....|....*....|....*..
gi 19922652 503 HLSgAYHIRGGVYFIDSLPKTPNDKLQ 529
Cdd:cd04433 311 RLA-PYKVPRRVVFVDALPRTASGKID 336
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
42-530 |
7.00e-75 |
|
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: 244.06 E-value: 7.00e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 42 DQVMQICDttGQELTGAQLAQQSARIAQAFKRLGLRRGDVVGI-SANNSTYLTSVIIAALLRGIPiNPLHPEFTEETVKY 120
Cdd:cd17631 10 DRTALVFG--GRSLTYAELDERVNRLAHALRALGVAKGDRVAVlSKNSPEFLELLFAAARLGAVF-VPLNFRLTPPEVAY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 121 MYDITEPKVIFCDVenyhiiktvngklqnpakiylvngklegvldisemlndedsitaaayvpcpklhgdhtAFIVCSSG 200
Cdd:cd17631 87 ILADSGAKVLFDDL----------------------------------------------------------ALLMYTSG 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 201 TTGMPKGVTRSHRSLLCNCKNPNT---YTRDSVLLSFSPLYWISGT-IILLASLLNGCRRIITNRPySVEYLLQLVARHK 276
Cdd:cd17631 109 TTGRPKGAMLTHRNLLWNAVNALAaldLGPDDVLLVVAPLFHIGGLgVFTLPTLLRGGTVVILRKF-DPETVLDLIERHR 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 277 VTFLFLASHQIALLSKH-DSDvmelKAQLQSIRVLIGAGSKVCKAVCRRMYELigNQRFVVGYGLSEMGGL-----SKNV 350
Cdd:cd17631 188 VTSFFLVPTMIQALLQHpRFA----TTDLSSLRAVIYGGAPMPERLLRALQAR--GVKFVQGYGMTETSPGvtflsPEDH 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 351 GGPVGCEGKVMRNVELRVLDKLKMPLGINEVGIIYARLRFKWAGYYRNPEATRRALSsDGmWFRTGDIGYLDSEGYLYIQ 430
Cdd:cd17631 262 RRKLGSAGRPVFFVEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFR-DG-WFHTGDLGRLDEDGYLYIV 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 431 TRDTDVFKFNNFQIYPEQIEEFILRLPGVSEACVFGIPD-----AVstnltaCAVVRTKspEGERLTADHIRNIVEHHLs 505
Cdd:cd17631 340 DRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDekwgeAV------VAVVVPR--PGAELDEDELIAHCRERL- 410
|
490 500
....*....|....*....|....*
gi 19922652 506 GAYHIRGGVYFIDSLPKTPNDKLQR 530
Cdd:cd17631 411 ARYKIPKSVEFVDALPRNATGKILK 435
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
52-438 |
2.41e-74 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 241.83 E-value: 2.41e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 52 GQELTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNSTYLTSVIIAALLRGIPINPLHPEFTEETVKYMYDITEPKVIF 131
Cdd:pfam00501 19 GRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDSGAKVLI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 132 CDVEnyHIIKTVNGKLQNPAKIYLVNGKLEGVLDISEMLNDEDSITAAAYVPCPKLHGDHTAFIVCSSGTTGMPKGVTRS 211
Cdd:pfam00501 99 TDDA--LKLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVPPPPPPPPDPDDLAYIIYTSGTTGKPKGVMLT 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 212 HRSLLCNCKNPNT-------YTRDSVLLSFSPLYWISG-TIILLASLLNGCRRII--TNRPYSVEYLLQLVARHKVTFLF 281
Cdd:pfam00501 177 HRNLVANVLSIKRvrprgfgLGPDDRVLSTLPLFHDFGlSLGLLGPLLAGATVVLppGFPALDPAALLELIERYKVTVLY 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 282 LASHQIALLSKHDSdvmELKAQLQSIRVLIGAGSKVCKAVCRRMYELIGNQrFVVGYGLSEMGGLSKNVGGPVGCE---- 357
Cdd:pfam00501 257 GVPTLLNMLLEAGA---PKRALLSSLRLVLSGGAPLPPELARRFRELFGGA-LVNGYGLTETTGVVTTPLPLDEDLrslg 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 358 --GKVMRNVELRVLDKLKM-PLGINEVGIIYAR----LRfkwaGYYRNPEATRRALSSDGmWFRTGDIGYLDSEGYLYIQ 430
Cdd:pfam00501 333 svGRPLPGTEVKIVDDETGePVPPGEPGELCVRgpgvMK----GYLNDPELTAEAFDEDG-WYRTGDLGRRDEDGYLEIV 407
|
....*...
gi 19922652 431 TRDTDVFK 438
Cdd:pfam00501 408 GRKKDQIK 415
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
22-533 |
3.52e-73 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 243.10 E-value: 3.52e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 22 FYGPEMTLGE-VIMRVLQINADQV-MQICDTTG--QELTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNSTYLTSVII 97
Cdd:COG0365 3 FVGGRLNIAYnCLDRHAEGRGDKVaLIWEGEDGeeRTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAML 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 98 AALLRGIPINPLHPEFTEETVKYMYDITEPKVIFCDVENYHIIKTVNGK---------LQNPAKIYLVNG-----KLEGV 163
Cdd:COG0365 83 ACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADGGLRGGKVIDLKekvdealeeLPSLEHVIVVGRtgadvPMEGD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 164 LDISEMLNDedsitAAAYVPCPKLHGDHTAFIVCSSGTTGMPKGVTRSHRSLLCNCKNPNTY----TRDSVLLSFSPLYW 239
Cdd:COG0365 163 LDWDELLAA-----ASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYvldlKPGDVFWCTADIGW 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 240 ISG-TIILLASLLNGCRRII---TNRPYSVEYLLQLVARHKVTFLFLASHQIALLSKHDSDVMElKAQLQSIRVLIGAGS 315
Cdd:COG0365 238 ATGhSYIVYGPLLNGATVVLyegRPDFPDPGRLWELIEKYGVTVFFTAPTAIRALMKAGDEPLK-KYDLSSLRLLGSAGE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 316 KVCKAVCRRMYELIGnQRFVVGYGLSEMGG--LSKNVGGPV--GCEGKVMRNVELRVLDKLKMPLGINEVGIIYARLrfK 391
Cdd:COG0365 317 PLNPEVWEWWYEAVG-VPIVDGWGQTETGGifISNLPGLPVkpGSMGKPVPGYDVAVVDEDGNPVPPGEEGELVIKG--P 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 392 W----AGYYRNPEATRRALSSDGM-WFRTGDIGYLDSEGYLYIQTRDTDVFKFNNFQIYPEQIEEFILRLPGVSEACVFG 466
Cdd:COG0365 394 WpgmfRGYWNDPERYRETYFGRFPgWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVG 473
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19922652 467 IPDAVSTNLTACAVVRTKSPEGERLTADHIRNIVEHHLsGAYHIRGGVYFIDSLPKTPNDKLQRRKV 533
Cdd:COG0365 474 VPDEIRGQVVKAFVVLKPGVEPSDELAKELQAHVREEL-GPYAYPREIEFVDELPKTRSGKIMRRLL 539
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
29-531 |
4.46e-69 |
|
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: 229.76 E-value: 4.46e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 29 LGEVIMRVLQINADQVMQICDttGQELTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNSTYLTSVIIAALLRG---IP 105
Cdd:cd05936 1 LADLLEEAARRFPDKTALIFM--GRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGavvVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 106 INPLhpeFTEETVKYMYDITEPKVIFCDVENYHIIKTvngklqnpakiylvngklegvldisemlndedsitAAAYVPCP 185
Cdd:cd05936 79 LNPL---YTPRELEHILNDSGAKALIVAVSFTDLLAA-----------------------------------GAPLGERV 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 186 KLHGDHTAFIVCSSGTTGMPKGVTRSHRSLLCN---CKN--PNTYTRDSVLLSFSPLYWISG-TIILLASLLNGCRRIIT 259
Cdd:cd05936 121 ALTPEDVAVLQYTSGTTGVPKGAMLTHRNLVANalqIKAwlEDLLEGDDVVLAALPLFHVFGlTVALLLPLALGATIVLI 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 260 NRPySVEYLLQLVARHKVTFLFLASHQIALLSKHDSDvmeLKAQLQSIRVLIGAGSKVCKAVCRRMYELIGNqRFVVGYG 339
Cdd:cd05936 201 PRF-RPIGVLKEIRKHRVTIFPGVPTMYIALLNAPEF---KKRDFSSLRLCISGGAPLPVEVAERFEELTGV-PIVEGYG 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 340 LSEMGglsknvggPVGCE------------GKVMRNVELRVLDKLKMPLGINEVGIIYARLRFKWAGYYRNPEATRRALS 407
Cdd:cd05936 276 LTETS--------PVVAVnpldgprkpgsiGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFV 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 408 sDGmWFRTGDIGYLDSEGYLYIQTRDTDVFKFNNFQIYPEQIEEFILRLPGVSEACVFGIPDAVSTNlTACAVVRTKspE 487
Cdd:cd05936 348 -DG-WLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGE-AVKAFVVLK--E 422
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 19922652 488 GERLTADHIRNIVEHHLSGaYHIRGGVYFIDSLPKTPNDKLQRR 531
Cdd:cd05936 423 GASLTEEEIIAFCREQLAG-YKVPRQVEFRDELPKSAVGKILRR 465
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
21-533 |
1.01e-68 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 230.07 E-value: 1.01e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 21 DFYGPeMTLGEVIMRVLQINADQVmqICDTTGQELTGAQLAQQSARIAQAFKRLGLRRGDVVG-ISANNSTYLTSVIIAA 99
Cdd:PRK06187 1 MQDYP-LTIGRILRHGARKHPDKE--AVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAvFDWNSHEYLEAYFAVP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 100 LLRGI--PIN-PLHPEfteeTVKYMYDITEPKVIFCDVENYHIIKTVNGKLQNPAKIYLVN-----GKLEGVLDISEMLN 171
Cdd:PRK06187 78 KIGAVlhPINiRLKPE----EIAYILNDAEDRVVLVDSEFVPLLAAILPQLPTVRTVIVEGdgpaaPLAPEVGEYEELLA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 172 DedsitAAAYVPCPKLHGDHTAFIVCSSGTTGMPKGVTRSHRSLLCN---CKNPNTYTRDSVLLSFSPLYWISGTIILLA 248
Cdd:PRK06187 154 A-----ASDTFDFPDIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHslaVCAWLKLSRDDVYLVIVPMFHVHAWGLPYL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 249 SLLNGCRRIITNRpYSVEYLLQLVARHKVTFLFL--ASHQIALLSKHDSDVmelkaQLQSIRVLIGAGSKVCKAVCRRMY 326
Cdd:PRK06187 229 ALMAGAKQVIPRR-FDPENLLDLIETERVTFFFAvpTIWQMLLKAPRAYFV-----DFSSLRLVIYGGAALPPALLREFK 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 327 ELIGnQRFVVGYGLSEMGGL------SKNVGGPV---GCEGKVMRNVELRVLDKLKMPL--GINEVG-IIyarLRFKW-- 392
Cdd:PRK06187 303 EKFG-IDLVQGYGMTETSPVvsvlppEDQLPGQWtkrRSAGRPLPGVEARIVDDDGDELppDGGEVGeII---VRGPWlm 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 393 AGYYRNPEATRRALssDGMWFRTGDIGYLDSEGYLYIQTRDTDVFKFNNFQIYPEQIEEFILRLPGVSEACVFGIPD--- 469
Cdd:PRK06187 379 QGYWNRPEATAETI--DGGWLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDekw 456
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19922652 470 --AVstnltaCAVVRTKspEGERLTADHIRNIVEHHLSGaYHIRGGVYFIDSLPKTPNDKLQRRKV 533
Cdd:PRK06187 457 geRP------VAVVVLK--PGATLDAKELRAFLRGRLAK-FKLPKRIAFVDELPRTSVGKILKRVL 513
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
50-531 |
2.10e-67 |
|
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: 226.35 E-value: 2.10e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 50 TTGQELTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNSTYLTSVIIAALLRGIPINPLHPEFTEETVKYMYDITEPKV 129
Cdd:cd05904 28 ATGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 130 IFCDVENYHIIKTVNgklqnpAKIYLVNGKLEGVLDISEMLNDEDSitaaAYVPCPKLHGDHTAFIVCSSGTTGMPKGVT 209
Cdd:cd05904 108 AFTTAELAEKLASLA------LPVVLLDSAEFDSLSFSDLLFEADE----AEPPVVVIKQDDVAALLYSSGTTGRSKGVM 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 210 RSHRSLLCNCK-----NPNTYTRDSVLLSFSPLYWISG-TIILLASLLNGCRRIITNRpYSVEYLLQLVARHKVTFLFLA 283
Cdd:cd05904 178 LTHRNLIAMVAqfvagEGSNSDSEDVFLCVLPMFHIYGlSSFALGLLRLGATVVVMPR-FDLEELLAAIERYKVTHLPVV 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 284 SHQIALLSKHDsdvMELKAQLQSIRVLIGAGSKVCKAVCRRMYELIGNQRFVVGYGLSEMGGLS-------KNVGGPVGC 356
Cdd:cd05904 257 PPIVLALVKSP---IVDKYDLSSLRQIMSGAAPLGKELIEAFRAKFPNVDLGQGYGMTESTGVVamcfapeKDRAKYGSV 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 357 eGKVMRNVELRVLD-KLKMPLGINEVGIIYARLRFKWAGYYRNPEATRRALSSDGmWFRTGDIGYLDSEGYLYIQTRDTD 435
Cdd:cd05904 334 -GRLVPNVEAKIVDpETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDKEG-WLHTGDLCYIDEDGYLFIVDRLKE 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 436 VFKFNNFQIYPEQIEEFILRLPGVSEACVFGIPDAVSTNLTACAVVRtkSPEGErLTADHIRNIVEHHLSGAYHIRgGVY 515
Cdd:cd05904 412 LIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVR--KPGSS-LTEDEIMDFVAKQVAPYKKVR-KVA 487
|
490
....*....|....*.
gi 19922652 516 FIDSLPKTPNDKLQRR 531
Cdd:cd05904 488 FVDAIPKSPSGKILRK 503
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
51-533 |
6.44e-66 |
|
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: 223.17 E-value: 6.44e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 51 TGQELTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNSTYLTSVIIAALLRGIPINPLHPEFTEETVKYMYDITEPKVI 130
Cdd:cd17642 41 TGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 131 FCDVENYHIIKTVNGKLQNPAKIYLVNGK--LEGVLDISEML--NDEDSITAAAYVPCPKLHGDHTAFIVCSSGTTGMPK 206
Cdd:cd17642 121 FCSKKGLQKVLNVQKKLKIIKTIIILDSKedYKGYQCLYTFItqNLPPGFNEYDFKPPSFDRDEQVALIMNSSGSTGLPK 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 207 GVTRSHRSLLC---NCKNP---NTYTRDSVLLSFSPLYWISGTIILLASLLNGCRRIITNRpYSVEYLLQLVARHKVTFL 280
Cdd:cd17642 201 GVQLTHKNIVArfsHARDPifgNQIIPDTAILTVIPFHHGFGMFTTLGYLICGFRVVLMYK-FEEELFLRSLQDYKVQSA 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 281 FLASHQIALLSKHDsdvMELKAQLQSIRVLIGAGSKVCKAVCRRMYELIGNQRFVVGYGLSEMGG--LSKNVG--GPvGC 356
Cdd:cd17642 280 LLVPTLFAFFAKST---LVDKYDLSNLHEIASGGAPLSKEVGEAVAKRFKLPGIRQGYGLTETTSaiLITPEGddKP-GA 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 357 EGKVMRNVELRVLD-KLKMPLGINEVGIIYARLRFKWAGYYRNPEATRRALSSDGmWFRTGDIGYLDSEGYLYIQTRDTD 435
Cdd:cd17642 356 VGKVVPFFYAKVVDlDTGKTLGPNERGELCVKGPMIMKGYVNNPEATKALIDKDG-WLHSGDIAYYDEDGHFFIVDRLKS 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 436 VFKFNNFQIYPEQIEEFILRLPGVSEACVFGIPDAVSTNLTACAVVRTkspEGERLTADHIRNIVEHHLSGAYHIRGGVY 515
Cdd:cd17642 435 LIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVVLE---AGKTMTEKEVMDYVASQVSTAKRLRGGVK 511
|
490
....*....|....*...
gi 19922652 516 FIDSLPKTPNDKLQRRKV 533
Cdd:cd17642 512 FVDEVPKGLTGKIDRRKI 529
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
47-533 |
3.87e-61 |
|
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: 209.48 E-value: 3.87e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 47 ICDTTGQELTGAQLAQQSARIAQAFKRLGLRRGDVVGIS-ANNSTYLTSVIIAALLRGIpINPLHPEFTEETVKYMYDIT 125
Cdd:cd05926 7 VVPGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIAlPNGLEFVVAFLAAARAGAV-VAPLNPAYKKAEFEFYLADL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 126 EPKVIFCD-VENYHIIK---TVNGKLQNPAKIYLVNGklegVLDISEMLNDEDSITAAAYvPCPKLHGDHTAFIVCSSGT 201
Cdd:cd05926 86 GSKLVLTPkGELGPASRaasKLGLAILELALDVGVLI----RAPSAESLSNLLADKKNAK-SEGVPLPDDLALILHTSGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 202 TGMPKGVTRSHRSLLCNCKN-PNTY--TRDSVLLSFSPLYWISGTII-LLASLLNGCRRIITNRpYSVEYLLQLVARHKV 277
Cdd:cd05926 161 TGRPKGVPLTHRNLAASATNiTNTYklTPDDRTLVVMPLFHVHGLVAsLLSTLAAGGSVVLPPR-FSASTFWPDVRDYNA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 278 TFlFLAS---HQIaLLSKHDSDVMELKAQLQSIRvliGAGSKVCKAVCRRMYELIGNQrfVV-GYGLSEMGGLS------ 347
Cdd:cd05926 240 TW-YTAVptiHQI-LLNRPEPNPESPPPKLRFIR---SCSASLPPAVLEALEATFGAP--VLeAYGMTEAAHQMtsnplp 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 348 ------KNVGGPVGcegkvmrnVELRVLDKLKMPLGINEVGIIYARLRFKWAGYYRNPEATRRALSSDGmWFRTGDIGYL 421
Cdd:cd05926 313 pgprkpGSVGKPVG--------VEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDG-WFRTGDLGYL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 422 DSEGYLYIQTRDTDVFKFNNFQIYPEQIEEFILRLPGVSEACVFGIPDAVSTNLTACAVVRTkspEGERLTADHIRNIVE 501
Cdd:cd05926 384 DADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLR---EGASVTEEELRAFCR 460
|
490 500 510
....*....|....*....|....*....|..
gi 19922652 502 HHLsGAYHIRGGVYFIDSLPKTPNDKLQRRKV 533
Cdd:cd05926 461 KHL-AAFKVPKKVYFVDELPKTATGKIQRRKV 491
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
27-531 |
1.60e-59 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 205.52 E-value: 1.60e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 27 MTLGEVIMRVLQINADQVMQIcdTTGQELTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNSTYLTSVIIAALLRGIPI 106
Cdd:PRK07656 5 MTLPELLARAARRFGDKEAYV--FGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 107 NPLHPEFTEETVKYMYDITEPKVIFC----------------DVENYHIIKTVNGKlqnpakiylvnGKLEGVLDISEML 170
Cdd:PRK07656 83 VPLNTRYTADEAAYILARGDAKALFVlglflgvdysattrlpALEHVVICETEEDD-----------PHTEKMKTFTDFL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 171 NDEDSITAAayvpcPKLHGDHTAFIVCSSGTTGMPKGVTRSHRSLLCNCKNPNTY---TRDSVLLSFSPLYWISG-TIIL 246
Cdd:PRK07656 152 AAGDPAERA-----PEVDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYlglTEGDRYLAANPFFHVFGyKAGV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 247 LASLLNGCRrIITNRPYSVEYLLQLVARHKVTFL--------FLASHqiALLSKHDsdvmelkaqLQSIRVLIGAGSKVC 318
Cdd:PRK07656 227 NAPLMRGAT-ILPLPVFDPDEVFRLIETERITVLpgpptmynSLLQH--PDRSAED---------LSSLRLAVTGAASMP 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 319 KAVCRRMYELIGNQRFVVGYGLSEMGGLS---------KNVGGPVGcegKVMRNVELRVLDKLKMPLGINEVGIIYARLR 389
Cdd:PRK07656 295 VALLERFESELGVDIVLTGYGLSEASGVTtfnrldddrKTVAGTIG---TAIAGVENKIVNELGEEVPVGEVGELLVRGP 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 390 FKWAGYYRNPEATRRALSSDGmWFRTGDIGYLDSEGYLYIQTRDTDVFKFNNFQIYPEQIEEFILRLPGVSEACVFGIPD 469
Cdd:PRK07656 372 NVMKGYYDDPEATAAAIDADG-WLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPD 450
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19922652 470 AVSTNLTACAVVRTkspEGERLTADHIRNIVEHHLSGaYHIRGGVYFIDSLPKTPNDKLQRR 531
Cdd:PRK07656 451 ERLGEVGKAYVVLK---PGAELTEEELIAYCREHLAK-YKVPRSIEFLDELPKNATGKVLKR 508
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
51-531 |
2.38e-54 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 192.12 E-value: 2.38e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 51 TGQELTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNSTYLTSVIIAALLRGIPINPLHPEFTEETVKYMYDITEPKVI 130
Cdd:PLN02246 47 TGRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAKLI 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 131 FcdVENYHIIKTVNGKLQNPAKIYLVNGKLEGVLDISEMLNDEDSItaaayVPCPKLHGDHTAFIVCSSGTTGMPKGVTR 210
Cdd:PLN02246 127 I--TQSCYVDKLKGLAEDDGVTVVTIDDPPEGCLHFSELTQADENE-----LPEVEISPDDVVALPYSSGTTGLPKGVML 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 211 SHRSLLCNC------KNPNTY-TRDSVLLSFSPLYWI-SGTIILLASLLNGCRrIITNRPYSVEYLLQLVARHKVTFLFL 282
Cdd:PLN02246 200 THKGLVTSVaqqvdgENPNLYfHSDDVILCVLPMFHIySLNSVLLCGLRVGAA-ILIMPKFEIGALLELIQRHKVTIAPF 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 283 ASHQIALLSKhdSDVMElKAQLQSIR-VLIGA---GSKVCKAVCRRmyelIGNQRFVVGYGLSEMGG-LSKNVG-----G 352
Cdd:PLN02246 279 VPPIVLAIAK--SPVVE-KYDLSSIRmVLSGAaplGKELEDAFRAK----LPNAVLGQGYGMTEAGPvLAMCLAfakepF 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 353 PV--GCEGKVMRNVELRVLD-KLKMPLGINEVGIIYARLRFKWAGYYRNPEATRRALSSDGmWFRTGDIGYLDSEGYLYI 429
Cdd:PLN02246 352 PVksGSCGTVVRNAELKIVDpETGASLPRNQPGEICIRGPQIMKGYLNDPEATANTIDKDG-WLHTGDIGYIDDDDELFI 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 430 QTRDTDVFKFNNFQIYPEQIEEFILRLPGVSEACVFGIPDAVSTNLTACAVVRTkspEGERLTADHIRNIVEHHLSGAYH 509
Cdd:PLN02246 431 VDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVVRS---NGSEITEDEIKQFVAKQVVFYKR 507
|
490 500
....*....|....*....|..
gi 19922652 510 IRgGVYFIDSLPKTPNDKLQRR 531
Cdd:PLN02246 508 IH-KVFFVDSIPKAPSGKILRK 528
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
28-531 |
6.49e-52 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 185.14 E-value: 6.49e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 28 TLGEVIMRVLQINADQVMQICDttGQELTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNS-----TYLTSVIIAALLr 102
Cdd:PRK08316 12 TIGDILRRSARRYPDKTALVFG--DRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSdayalLWLACARAGAVH- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 103 gIPINPLhpeFTEETVKYMYDITEPKVIFCDVENYHIIKTVNGKLQNPAKIYLVNGKL----EGVLDISEMLNdedsiTA 178
Cdd:PRK08316 89 -VPVNFM---LTGEELAYILDHSGARAFLVDPALAPTAEAALALLPVDTLILSLVLGGreapGGWLDFADWAE-----AG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 179 AAYVPCPKLHGDHTAFIVCSSGTTGMPKGVTRSHRSLLCN---CKNPNTYTRDSVLLSFSPLYWISGT-IILLASLLNGC 254
Cdd:PRK08316 160 SVAEPDVELADDDLAQILYTSGTESLPKGAMLTHRALIAEyvsCIVAGDMSADDIPLHALPLYHCAQLdVFLGPYLYVGA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 255 RRIITNRPySVEYLLQLVARHKVTFLFLA-SHQIALLSKHDSDvmelKAQLQSIR-VLIGAgSKVCKAVCRRMYELIGNQ 332
Cdd:PRK08316 240 TNVILDAP-DPELILRTIEAERITSFFAPpTVWISLLRHPDFD----TRDLSSLRkGYYGA-SIMPVEVLKELRERLPGL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 333 RFVVGYGLSEMGGLSkNVGGP------VGCEGKVMRNVELRVLDKLKMPLGINEVGIIYARLRFKWAGYYRNPEATRRAL 406
Cdd:PRK08316 314 RFYNCYGQTEIAPLA-TVLGPeehlrrPGSAGRPVLNVETRVVDDDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEAF 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 407 SsdGMWFRTGDIGYLDSEGYLYIQTRDTDVFKFNNFQIYPEQIEEFILRLPGVSEACVFGIPD-----AVstnlTACAVV 481
Cdd:PRK08316 393 R--GGWFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDpkwieAV----TAVVVP 466
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 19922652 482 RtkspEGERLTADhirNIVEH---HLSGaYHIRGGVYFIDSLPKTPNDKLQRR 531
Cdd:PRK08316 467 K----AGATVTED---ELIAHcraRLAG-FKVPKRVIFVDELPRNPSGKILKR 511
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
47-532 |
7.56e-51 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 181.64 E-value: 7.56e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 47 ICDTTGQELTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNSTYLTSVIIAALLRGIPINPLHPEFTEETVKYMYDITE 126
Cdd:PRK08276 4 IMAPSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 127 PKVIFCDVENYHIIKTVNGKLQNPAKI-YLVNGKLEGVLDISEMLNDEdsitaAAYVPCPKLHGDHTAFivcSSGTTGMP 205
Cdd:PRK08276 84 AKVLIVSAALADTAAELAAELPAGVPLlLVVAGPVPGFRSYEEALAAQ-----PDTPIADETAGADMLY---SSGTTGRP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 206 KGVTR--SHRSLLcncKNPNTYTR----------DSVLLSFSPLY------WiSGTIILLASLLngcrrIITNRpYSVEY 267
Cdd:PRK08276 156 KGIKRplPGLDPD---EAPGMMLAllgfgmyggpDSVYLSPAPLYhtaplrF-GMSALALGGTV-----VVMEK-FDAEE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 268 LLQLVARHKVTFL-FLASHQIALLsKHDSDVMElKAQLQSIRVLIGAGSKVCKAVCRRMYELIGNqrfVVG--YGLSEMG 344
Cdd:PRK08276 226 ALALIERYRVTHSqLVPTMFVRML-KLPEEVRA-RYDVSSLRVAIHAAAPCPVEVKRAMIDWWGP---IIHeyYASSEGG 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 345 G---------LSK--NVGGPVGCegkvmrnvELRVLDKLKMPLGINEVGIIYarlrFKWAGY---YRN-PEATRRALSSD 409
Cdd:PRK08276 301 GvtvitsedwLAHpgSVGKAVLG--------EVRILDEDGNELPPGEIGTVY----FEMDGYpfeYHNdPEKTAAARNPH 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 410 GmWFRTGDIGYLDSEGYLYIQTRDTDVFKFNNFQIYPEQIEEFILRLPGVSEACVFGIPDA-----VStnltacAVVRTK 484
Cdd:PRK08276 369 G-WVTVGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEemgerVK------AVVQPA 441
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 19922652 485 SP--EGERLTADhIRNIVEHHLSGaYHIRGGVYFIDSLPKTPNDKLQRRK 532
Cdd:PRK08276 442 DGadAGDALAAE-LIAWLRGRLAH-YKCPRSIDFEDELPRTPTGKLYKRR 489
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
55-533 |
3.40e-50 |
|
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: 178.34 E-value: 3.40e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 55 LTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNSTYLTSVIIAALLRGIPINPLHPEFTEETVKYMYDITEPKVIFcdv 134
Cdd:cd05903 2 LTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFV--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 135 enyhiIKTVNGKLqnpakiylvngklegvlDISEMlndedsitaaayvpcpklhGDHTAFIVCSSGTTGMPKGVTRSHRS 214
Cdd:cd05903 79 -----VPERFRQF-----------------DPAAM-------------------PDAVALLLFTSGTTGEPKGVMHSHNT 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 215 LLCN----CKNPNTYTRDSVLLSfSPLYWISGTI-ILLASLLNGCRRIITNRpYSVEYLLQLVARHKVTFLFLASHQIAL 289
Cdd:cd05903 118 LSASirqyAERLGLGPGDVFLVA-SPMAHQTGFVyGFTLPLLLGAPVVLQDI-WDPDKALALMREHGVTFMMGATPFLTD 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 290 LSKHdsdVMELKAQLQSIRVLIGAGSKVCKAVCRRMYELIGNqrFVVG-YGLSEMGGLSKN-----VGGPVGCEGKVMRN 363
Cdd:cd05903 196 LLNA---VEEAGEPLSRLRTFVCGGATVPRSLARRAAELLGA--KVCSaYGSTECPGAVTSitpapEDRRLYTDGRPLPG 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 364 VELRVLDKLKMPLGINEVGIIYARLRFKWAGYYRNPEATRRALssDGMWFRTGDIGYLDSEGYLYIQTRDTDVFKFNNFQ 443
Cdd:cd05903 271 VEIKVVDDTGATLAPGVEGELLSRGPSVFLGYLDRPDLTADAA--PEGWFRTGDLARLDEDGYLRITGRSKDIIIRGGEN 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 444 IYPEQIEEFILRLPGVSEACVFGIPDAvSTNLTACAVVRTKSpeGERLTADHIRNIVEHHLSGAYHIRGGVYFIDSLPKT 523
Cdd:cd05903 349 IPVLEVEDLLLGHPGVIEAAVVALPDE-RLGERACAVVVTKS--GALLTFDELVAYLDRQGVAKQYWPERLVHVDDLPRT 425
|
490
....*....|
gi 19922652 524 PNDKLQRRKV 533
Cdd:cd05903 426 PSGKVQKFRL 435
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
23-466 |
9.32e-49 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 177.98 E-value: 9.32e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 23 YGPEMTLGEVIMRVLQINADQVMQICDTTG--QELTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNSTYLTSVIIAAL 100
Cdd:COG1022 7 VPPADTLPDLLRRRAARFPDRVALREKEDGiwQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAIL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 101 -LRGIPInPLHPEFTEETVKYMYDITEPKVIFC-DVENYHIIKTVNGKLQNPAKIYLVNGK----LEGVLDISEMLNDED 174
Cdd:COG1022 87 aAGAVTV-PIYPTSSAEEVAYILNDSGAKVLFVeDQEQLDKLLEVRDELPSLRHIVVLDPRglrdDPRLLSLDELLALGR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 175 SITAAAYVP--CPKLHGDHTAFIVCSSGTTGMPKGVTRSHRSLLCNCKNPNTY---TRDSVLLSFSPLYWISGTIILLAS 249
Cdd:COG1022 166 EVADPAELEarRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERlplGPGDRTLSFLPLAHVFERTVSYYA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 250 LLNGC--------RRIITN----RP-------------YS------------------------VEYLLQLVARHKVTFL 280
Cdd:COG1022 246 LAAGAtvafaespDTLAEDlrevKPtfmlavprvwekvYAgiqakaeeagglkrklfrwalavgRRYARARLAGKSPSLL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 281 FLASHQIA---LLSKhdsdvmeLKAQLQS-IRVLIGAGSKVCKAVCrRMYELIGnqrfV---VGYGLSEMGGLSkNVGGP 353
Cdd:COG1022 326 LRLKHALAdklVFSK-------LREALGGrLRFAVSGGAALGPELA-RFFRALG----IpvlEGYGLTETSPVI-TVNRP 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 354 ----VGCEGKVMRNVELRvldklkmplgINEVGIIYAR--LRFKwaGYYRNPEATRRALSSDGmWFRTGDIGYLDSEGYL 427
Cdd:COG1022 393 gdnrIGTVGPPLPGVEVK----------IAEDGEILVRgpNVMK--GYYKNPEATAEAFDADG-WLHTGDIGELDEDGFL 459
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 19922652 428 YIQTRDTDVFKFN---NfqIYPEQIEEFILRLPGVSEACVFG 466
Cdd:COG1022 460 RITGRKKDLIVTSggkN--VAPQPIENALKASPLIEQAVVVG 499
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
54-531 |
7.23e-48 |
|
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: 171.89 E-value: 7.23e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 54 ELTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNSTYLTSVIIAALLRG---IPINPLHPEFteetvkymyditEPKVI 130
Cdd:cd05935 1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANavvVPINPMLKER------------ELEYI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 131 FCDVEnyhiiktvngklqnpAKIYLVNGKLEGVldisemlndedsitaaayvpcpklhgdhtAFIVCSSGTTGMPKGVTR 210
Cdd:cd05935 69 LNDSG---------------AKVAVVGSELDDL-----------------------------ALIPYTSGTTGLPKGCMH 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 211 SHRSLLCNCKNP---NTYTRDSVLLSFSPLYWISGTIILLASLLNGCRRIITNRPYSVEYLLQLVARHKVTFLFLASHQI 287
Cdd:cd05935 105 THFSAAANALQSavwTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMARWDRETALELIEKYKVTFWTNIPTML 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 288 ALLSkhdSDVMELKAQLQSIRVLIGAGSKVCKAVCRRMYELIGnQRFVVGYGLSEMggLSKNVGGPVG-----CEGKVMR 362
Cdd:cd05935 185 VDLL---ATPEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTG-LRFVEGYGLTET--MSQTHTNPPLrpklqCLGIP*F 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 363 NVELRVLD-KLKMPLGINEVGIIYARLRFKWAGYYRNPEATRRALSSDG--MWFRTGDIGYLDSEGYLYIQTRDTDVFKF 439
Cdd:cd05935 259 GVDARVIDiETGRELPPNEVGEIVVRGPQIFKGYWNRPEETEESFIEIKgrRFFRTGDLGYMDEEGYFFFVDRVKRMINV 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 440 NNFQIYPEQIEEFILRLPGVSEACVFGIPDAVSTNLTACAVVRTKSPEGErLTADHIRNIVEHHLSGAYHIRgGVYFIDS 519
Cdd:cd05935 339 SGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEYRGK-VTEEDIIEWAREQMAAYKYPR-EVEFVDE 416
|
490
....*....|..
gi 19922652 520 LPKTPNDKLQRR 531
Cdd:cd05935 417 LPRSASGKILWR 428
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
51-531 |
1.36e-47 |
|
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: 171.46 E-value: 1.36e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 51 TGQELTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNSTYLTSVIIAALLRGIPINPLHPEFTEETVKYMYDITEPKVI 130
Cdd:cd05971 3 TPEKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 131 fcdvenyhiiktvngklqnpakiylvngklegVLDISemlndedsitaaayvpcpklhgDHTAFIVCSSGTTGMPKGVTR 210
Cdd:cd05971 83 --------------------------------VTDGS----------------------DDPALIIYTSGTTGPPKGALH 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 211 SHRSLLCNckNPNTYT-------RDSVLLSFSPLYWISGTI-ILLASLLNG-----CRRiitnRPYSVEYLLQLVARHKV 277
Cdd:cd05971 109 AHRVLLGH--LPGVQFpfnlfprDGDLYWTPADWAWIGGLLdVLLPSLYFGvpvlaHRM----TKFDPKAALDLMSRYGV 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 278 TFLFLASHQIALLSKHDSdvmELKAQLQSIRVLIGAGSKVCKavcrrmyELIGNQRFVVG------YGLSEMGGLSKN-- 349
Cdd:cd05971 183 TTAFLPPTALKMMRQQGE---QLKHAQVKLRAIATGGESLGE-------ELLGWAREQFGvevnefYGQTECNLVIGNcs 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 350 VGGPV--GCEGKVMRNVELRVLDKLKMPLGINEVGIIYARL--RFKWAGYYRNPEATRRALSSDgmWFRTGDIGYLDSEG 425
Cdd:cd05971 253 ALFPIkpGSMGKPIPGHRVAIVDDNGTPLPPGEVGEIAVELpdPVAFLGYWNNPSATEKKMAGD--WLLTGDLGRKDSDG 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 426 YLYIQTRDTDVFKFNNFQIYPEQIEEFILRLPGVSEACVFGIPDAVSTNLTACAVVRTKSPEGERLTADHIRNIVEHHLs 505
Cdd:cd05971 331 YFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGETPSDALAREIQELVKTRL- 409
|
490 500
....*....|....*....|....*.
gi 19922652 506 GAYHIRGGVYFIDSLPKTPNDKLQRR 531
Cdd:cd05971 410 AAHEYPREIEFVNELPRTATGKIRRR 435
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
64-534 |
1.51e-47 |
|
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: 171.85 E-value: 1.51e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 64 SARIAQAFKRLGLRRGD-VVGISANNSTYLTS---VIIAALLRGIPINPLHPEFTEETVKYMYDITEPKVIFCDVenyhi 139
Cdd:cd05922 3 VSAAASALLEAGGVRGErVVLILPNRFTYIELsfaVAYAGGRLGLVFVPLNPTLKESVLRYLVADAGGRIVLADA----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 140 iktvngKLQNPAKIYLVngklegVLDISEMLNDEDSITAA-AYVPCPKLHGDHTAFIVCSSGTTGMPKGVTRSHRSLLCN 218
Cdd:cd05922 78 ------GAADRLRDALP------ASPDPGTVLDADGIRAArASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLAN 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 219 CKNPNTY---TRDSVLLSFSPLYWISGTIILLASLLNGCRRIITNRPYSVEYLLQLVARHKVTFLFLASHQIALLSKHDS 295
Cdd:cd05922 146 ARSIAEYlgiTADDRALTVLPLSYDYGLSVLNTHLLRGATLVLTNDGVLDDAFWEDLREHGATGLAGVPSTYAMLTRLGF 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 296 DvmelKAQLQSIRVLIGAGSKVCKAVCRRMYELIGNQRFVVGYGLSE----MGGL-SKNVGGPVGCEGKVMRNVELRVLD 370
Cdd:cd05922 226 D----PAKLPSLRYLTQAGGRLPQETIARLRELLPGAQVYVMYGQTEatrrMTYLpPERILEKPGSIGLAIPGGEFEILD 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 371 KLKMPLGINEVGIIYARLRFKWAGYYRNPeATRRALSSDGMWFRTGDIGYLDSEGYLYIQTRDTDVFKFNNFQIYPEQIE 450
Cdd:cd05922 302 DDGTPTPPGEPGEIVHRGPNVMKGYWNDP-PYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIE 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 451 EFILRLPGVSEACVFGIPDAVSTNLTACAVvrtkSPEGERLTA--DHIRNIVEHHLSGAYhirggVYFIDSLPKTPNDKL 528
Cdd:cd05922 381 AAARSIGLIIEAAAVGLPDPLGEKLALFVT----APDKIDPKDvlRSLAERLPPYKVPAT-----VRVVDELPLTASGKV 451
|
....*.
gi 19922652 529 QRRKVL 534
Cdd:cd05922 452 DYAALR 457
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
199-532 |
1.88e-47 |
|
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: 168.61 E-value: 1.88e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 199 SGTTGMPKGVTRSHRSLLCNCKN---PNTYTRDSVLLSFSPLYWISGTII-LLASLLNGCRRIITNRPYSVEYLLQLVAR 274
Cdd:cd05917 11 SGTTGSPKGATLTHHNIVNNGYFigeRLGLTEQDRLCIPVPLFHCFGSVLgVLACLTHGATMVFPSPSFDPLAVLEAIEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 275 HKVTFLF-LASHQIALLSKHDSDVMELKaqlqSIRVLIGAGSKVCKAVCRRMYELIGNQRFVVGYGLSE------MGGLS 347
Cdd:cd05917 91 EKCTALHgVPTMFIAELEHPDFDKFDLS----SLRTGIMAGAPCPPELMKRVIEVMNMKDVTIAYGMTEtspvstQTRTD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 348 KNVGGPVGCEGKVMRNVELRVLDKL-KMPLGINEVGIIYARLRFKWAGYYRNPEATRRALSSDGmWFRTGDIGYLDSEGY 426
Cdd:cd05917 167 DSIEKRVNTVGRIMPHTEAKIVDPEgGIVPPVGVPGELCIRGYSVMKGYWNDPEKTAEAIDGDG-WLHTGDLAVMDEDGY 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 427 LYIQTRDTDVFKFNNFQIYPEQIEEFILRLPGVSEACVFGIPDAvSTNLTACAVVRTKspEGERLTADHIRNIVEHHLSg 506
Cdd:cd05917 246 CRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDE-RYGEEVCAWIRLK--EGAELTEEDIKAYCKGKIA- 321
|
330 340
....*....|....*....|....*.
gi 19922652 507 AYHIRGGVYFIDSLPKTPNDKLQRRK 532
Cdd:cd05917 322 HYKVPRYVFFVDEFPLTVSGKIQKFK 347
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
52-531 |
2.55e-47 |
|
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: 171.61 E-value: 2.55e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 52 GQELTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNSTYLTSVIIAALLRGIPINPLHPEFTEETVKYMYDITEPKVIF 131
Cdd:cd12117 20 DRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAERLAFMLADAGAKVLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 132 CDvenyhiiKTVNGKLQNPAKIYLVngklegvldisemlnDEDSITAAAYVPCPKLHGDHTAFIVCSSGTTGMPKGVTRS 211
Cdd:cd12117 100 TD-------RSLAGRAGGLEVAVVI---------------DEALDAGPAGNPAVPVSPDDLAYVMYTSGSTGRPKGVAVT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 212 HRSLLCNCKNPN--TYTRDSVLLSFSPLYWISGTIILLASLLNGCRRIITNR--PYSVEYLLQLVARHKVTFLFLASHQI 287
Cdd:cd12117 158 HRGVVRLVKNTNyvTLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKgtLLDPDALGALIAEEGVTVLWLTAALF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 288 ALLSKHDSDVMElkaqlqSIRVLIGAGSKVCKAVCRRMYELIGNQRFVVGYGLSE--------------MGGLSKNVGGP 353
Cdd:cd12117 238 NQLADEDPECFA------GLRELLTGGEVVSPPHVRRVLAACPGLRLVNGYGPTEnttfttshvvteldEVAGSIPIGRP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 354 VGcegkvmrNVELRVLDKLKMPLGINEVGIIY------ARlrfkwaGYYRNPEATRRALSSD-----GMWFRTGDIGYLD 422
Cdd:cd12117 312 IA-------NTRVYVLDEDGRPVPPGVPGELYvggdglAL------GYLNRPALTAERFVADpfgpgERLYRTGDLARWL 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 423 SEGYL-YIQTRDTDVfKFNNFQIYPEQIEEFILRLPGVSEACVFGIPDAVSTNLTACAVVRTkspegERLTADHIRNIVE 501
Cdd:cd12117 379 PDGRLeFLGRIDDQV-KIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVVAE-----GALDAAELRAFLR 452
|
490 500 510
....*....|....*....|....*....|
gi 19922652 502 HHLSgAYHIRGGVYFIDSLPKTPNDKLQRR 531
Cdd:cd12117 453 ERLP-AYMVPAAFVVLDELPLTANGKVDRR 481
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
28-534 |
3.45e-47 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 172.09 E-value: 3.45e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 28 TLGEVIMRVLQINADQVMQICDTTgqELTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNSTYLTSVIIAALLRGIPIN 107
Cdd:PRK06188 13 TYGHLLVSALKRYPDRPALVLGDT--RLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 108 PLHPEFTEETVKYMYDITEPKVIFCD----VENYHIIKTVNGKLQNpakiYLVNGKLEGVLDISEMlndedsitAAAYVP 183
Cdd:PRK06188 91 ALHPLGSLDDHAYVLEDAGISTLIVDpapfVERALALLARVPSLKH----VLTLGPVPDGVDLLAA--------AAKFGP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 184 CPKLHGDHT---AFIVCSSGTTGMPKGVTRSHRSLLcncknpnTYT----------RDSVLLSFSPLYWISGTIILLASL 250
Cdd:PRK06188 159 APLVAAALPpdiAGLAYTGGTTGKPKGVMGTHRSIA-------TMAqiqlaewewpADPRFLMCTPLSHAGGAFFLPTLL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 251 LNGCrrIITNRPYSVEYLLQLVARHKVTFLFLASHQI-ALLSKHDSDvmelKAQLQSIRVLIGAGSKVCKAVCRRMYELI 329
Cdd:PRK06188 232 RGGT--VIVLAKFDPAEVLRAIEEQRITATFLVPTMIyALLDHPDLR----TRDLSSLETVYYGASPMSPVRLAEAIERF 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 330 GNQrFVVGYGLSEMGG----LSK------NVGGPVGCeGKVMRNVELRVLDKLKMPLGINEVGIIYARLRFKWAGYYRNP 399
Cdd:PRK06188 306 GPI-FAQYYGQTEAPMvityLRKrdhdpdDPKRLTSC-GRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRP 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 400 EATRRALSSDgmWFRTGDIGYLDSEGYLYIQTRDTDVFKFNNFQIYPEQIEEFILRLPGVSEACVFGIPD-----AVstn 474
Cdd:PRK06188 384 EETAEAFRDG--WLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDekwgeAV--- 458
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 475 lTACAVVRTkspeGERLTADHIRNIVEHHlSGAYHIRGGVYFIDSLPKTPNDKLQrRKVL 534
Cdd:PRK06188 459 -TAVVVLRP----GAAVDAAELQAHVKER-KGSVHAPKQVDFVDSLPLTALGKPD-KKAL 511
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
26-531 |
1.50e-46 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 170.93 E-value: 1.50e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 26 EMTLGEVIMRVLQINADQVMQICDTTGQELTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNSTYLTSVIIAALLRGIP 105
Cdd:PLN02330 27 KLTLPDFVLQDAELYADKVAFVEAVTGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 106 INPLHPEFTEETVKYMYDITEPKVIFCDVENYHIIKTvngkLQNPAkIYLVNGKLEGVLDISEMLNDEDSitAAAYVPCP 185
Cdd:PLN02330 107 FSGANPTALESEIKKQAEAAGAKLIVTNDTNYGKVKG----LGLPV-IVLGEEKIEGAVNWKELLEAADR--AGDTSDNE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 186 KLHGDHTAFIVCSSGTTGMPKGVTRSHRSLLCN-CKNPNTYTRDSV-------LLSFSPLYWISGtiILLASLLNGCRRI 257
Cdd:PLN02330 180 EILQTDLCALPFSSGTTGISKGVMLTHRNLVANlCSSLFSVGPEMIgqvvtlgLIPFFHIYGITG--ICCATLRNKGKVV 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 258 ITNRpYSVEYLLQLVARHKVTFLFLASHQIALLSKhDSDVMELKAQLQSIRVLIGAGSKVCKAVCRRMYELIGNQRFVVG 337
Cdd:PLN02330 258 VMSR-FELRTFLNALITQEVSFAPIVPPIILNLVK-NPIVEEFDLSKLKLQAIMTAAAPLAPELLTAFEAKFPGVQVQEA 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 338 YGLSEMGGLSKNVGGPVGCEGKVMRN--------VELRVLD-KLKMPLGINEVGIIYARLRFKWAGYYRNPEATRRALSS 408
Cdd:PLN02330 336 YGLTEHSCITLTHGDPEKGHGIAKKNsvgfilpnLEVKFIDpDTGRSLPKNTPGELCVRSQCVMQGYYNNKEETDRTIDE 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 409 DGmWFRTGDIGYLDSEGYLYIQTRDTDVFKFNNFQIYPEQIEEFILRLPGVSEACVFGIPDAVSTNL-TACAVVRTKSPE 487
Cdd:PLN02330 416 DG-WLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIpAACVVINPKAKE 494
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 19922652 488 GErltaDHIRNIVEHHLSGAYHIRgGVYFIDSLPKTPNDKLQRR 531
Cdd:PLN02330 495 SE----EDILNFVAANVAHYKKVR-VVQFVDSIPKSLSGKIMRR 533
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
53-533 |
4.85e-46 |
|
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: 167.39 E-value: 4.85e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 53 QELTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNSTYLTSVIIAALLRGIPINPLHPEFTEETVKYMYDITEPKVIFC 132
Cdd:cd05907 4 QPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 133 DvenyhiiktvngklqnpakiylvngklegvldisemlndedsitaaayvpcpklHGDHTAFIVCSSGTTGMPKGVTRSH 212
Cdd:cd05907 84 E------------------------------------------------------DPDDLATIIYTSGTTGRPKGVMLSH 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 213 RSLLCNCKNPNTYTR---DSVLLSFSPLYWISGTI-ILLASLLNGCRriiTNRPYSVEYLLQLVARHKVTFLFL------ 282
Cdd:cd05907 110 RNILSNALALAERLPateGDRHLSFLPLAHVFERRaGLYVPLLAGAR---IYFASSAETLLDDLSEVRPTVFLAvprvwe 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 283 ---ASHQIALLSKHDSdVMELKAQLQSIRVLIGAGSKVCKAVCRrMYELIGNQrFVVGYGLSEMGG-LSKNVGG--PVGC 356
Cdd:cd05907 187 kvyAAIKVKAVPGLKR-KLFDLAVGGRLRFAASGGAPLPAELLH-FFRALGIP-VYEGYGLTETSAvVTLNPPGdnRIGT 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 357 EGKVMRNVELRvldklkmplgINEVGIIYARLRFKWAGYYRNPEATRRALSSDGmWFRTGDIGYLDSEGYLYIQTRDTDV 436
Cdd:cd05907 264 VGKPLPGVEVR----------IADDGEILVRGPNVMLGYYKNPEATAEALDADG-WLHTGDLGEIDEDGFLHITGRKKDL 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 437 FKFNNFQ-IYPEQIEEFILRLPGVSEACVFG----------IPDAVSTNLTACAVVRTKSPEGERLTADHIRNIVEHHLS 505
Cdd:cd05907 333 IITSGGKnISPEPIENALKASPLISQAVVIGdgrpflvaliVPDPEALEAWAEEHGIAYTDVAELAANPAVRAEIEAAVE 412
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 19922652 506 GA------------YHIRGGVYFIDSLPKTPNDKLQRRKV 533
Cdd:cd05907 413 AAnarlsryeqikkFLLLPEPFTIENGELTPTLKLKRPVI 452
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
52-532 |
3.68e-45 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 167.06 E-value: 3.68e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 52 GQELTGAQLAQQSARIA---QAfkRLGLRRGDVVGISANNSTYLtsvIIA--ALLRG----IPINPLHpefTEETVKYMY 122
Cdd:PRK08314 33 GRAISYRELLEEAERLAgylQQ--ECGVRKGDRVLLYMQNSPQF---VIAyyAILRAnavvVPVNPMN---REEELAHYV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 123 DITEPKVIFCDVENYHIIKTVNGKLQnpakiylvngkLEGVL--DISEMLNDEDSIT----------------------- 177
Cdd:PRK08314 105 TDSGARVAIVGSELAPKVAPAVGNLR-----------LRHVIvaQYSDYLPAEPEIAvpawlraepplqalapggvvawk 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 178 ---AAAYVPCP-KLHGDHTAFIVCSSGTTGMPKGVTRSHRSLLCNCKNP---NTYTRDSVLLSFSPLYWISGTI-ILLAS 249
Cdd:PRK08314 174 ealAAGLAPPPhTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSvlwSNSTPESVVLAVLPLFHVTGMVhSMNAP 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 250 LLNGCRRIITNRpYSVEYLLQLVARHKVTFL---------FLASHQIAllskhdsdvmelKAQLQSIRVLIGAGSKVCKA 320
Cdd:PRK08314 254 IYAGATVVLMPR-WDREAAARLIERYRVTHWtniptmvvdFLASPGLA------------ERDLSSLRYIGGGGAAMPEA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 321 VCRRMYELIGnQRFVVGYGLSE-MGGLSKNvggP-----VGCEGKVMRNVELRVLD--KLKmPLGINEVG--IIYARLRF 390
Cdd:PRK08314 321 VAERLKELTG-LDYVEGYGLTEtMAQTHSN---PpdrpkLQCLGIPTFGVDARVIDpeTLE-ELPPGEVGeiVVHGPQVF 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 391 KwaGYYRNPEATRRA-LSSDGM-WFRTGDIGYLDSEGYLYIQTRDTDVFKFNNFQIYPEQIEEFILRLPGVSEACVFGIP 468
Cdd:PRK08314 396 K--GYWNRPEATAEAfIEIDGKrFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATP 473
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19922652 469 DAvSTNLTACAVVRTKSPEGERLTADHIRNIVEHHLSgAYHIRGGVYFIDSLPKTPNDKLQRRK 532
Cdd:PRK08314 474 DP-RRGETVKAVVVLRPEARGKTTEEEIIAWAREHMA-AYKYPRIVEFVDSLPKSGSGKILWRQ 535
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
32-532 |
3.34e-44 |
|
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: 163.96 E-value: 3.34e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 32 VIMRVLQINADQVMQICDTTGQ--ELTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNS-----TYLTSVIIAALLRgi 104
Cdd:cd12119 1 LLEHAARLHGDREIVSRTHEGEvhRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNThrhleLYYAVPGMGAVLH-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 105 PINP-LHPEFTEETVKYMYDitepKVIFCD------VENYH-IIKTVNGKLQNPAKIYLVNGKLEGVLDISEMLNDEDSI 176
Cdd:cd12119 79 TINPrLFPEQIAYIINHAED----RVVFVDrdflplLEAIApRLPTVEHVVVMTDDAAMPEPAGVGVLAYEELLAAESPE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 177 TAAayvpcPKLHGDHTAFIVCSSGTTGMPKGVTRSHRSL------LCNCKNPNTYTRDSVLLsFSPLYWISGTIILLASL 250
Cdd:cd12119 155 YDW-----PDFDENTAAAICYTSGTTGNPKGVVYSHRSLvlhamaALLTDGLGLSESDVVLP-VVPMFHVNAWGLPYAAA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 251 LNGCRRIITNRPYSVEYLLQLVARHKVTF--------LFLASHqialLSKHDSDVMELKaqlqsiRVLIGaGSKVCKAVC 322
Cdd:cd12119 229 MVGAKLVLPGPYLDPASLAELIEREGVTFaagvptvwQGLLDH----LEANGRDLSSLR------RVVIG-GSAVPRSLI 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 323 RRMYELIgnQRFVVGYGLSEMGGL-------SKNVGGPVGCE-------GKVMRNVELRVLDK--LKMPLGINEVGIIYA 386
Cdd:cd12119 298 EAFEERG--VRVIHAWGMTETSPLgtvarppSEHSNLSEDEQlalrakqGRPVPGVELRIVDDdgRELPWDGKAVGELQV 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 387 RLRFKWAGYYRNPEATRrALSSDGmWFRTGDIGYLDSEGYLYIQTRDTDVFKFNNFQIYPEQIEEFILRLPGVSEACVFG 466
Cdd:cd12119 376 RGPWVTKSYYKNDEESE-ALTEDG-WLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIG 453
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19922652 467 IPDA------VstnltACAVVRtkspEGERLTADHIRniveHHLSGA---YHIRGGVYFIDSLPKTPNDKLQRRK 532
Cdd:cd12119 454 VPHPkwgerpL-----AVVVLK----EGATVTAEELL----EFLADKvakWWLPDDVVFVDEIPKTSTGKIDKKA 515
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
58-464 |
4.49e-44 |
|
amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.
Pssm-ID: 273779 [Multi-domain] Cd Length: 409 Bit Score: 161.28 E-value: 4.49e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 58 AQLAQQSARIAQAFK-RLGLRRGDVVGISANNSTYLTSVIIAALLRG---IPINPLHPEfteETVKYMYDITEPKVIFCD 133
Cdd:TIGR01733 3 RELDERANRLARHLRaAGGVGPGDRVAVLLERSAELVVAILAVLKAGaayVPLDPAYPA---ERLAFILEDAGARLLLTD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 134 VENYHiiktvngklqnpakiyLVNGKLEGVLDISEMLNDEDSITAAAYVPCPKLHGDHTAFIVCSSGTTGMPKGVTRSHR 213
Cdd:TIGR01733 80 SALAS----------------RLAGLVLPVILLDPLELAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 214 SLLCNC---KNPNTYTRDSVLLSFSPLYWISGTIILLASLLNGCRRII---TNRPYSVEYLLQLVARHKVTFLFLASHQI 287
Cdd:TIGR01733 144 SLVNLLawlARRYGLDPDDRVLQFASLSFDASVEEIFGALLAGATLVVppeDEERDDAALLAALIAEHPVTVLNLTPSLL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 288 ALLskhdsdVMELKAQLQSIRVLIGAGSKVCKAVCRRMYELIGNQRFVVGYGLSE---------------MGGLSKNVGG 352
Cdd:TIGR01733 224 ALL------AAALPPALASLRLVILGGEALTPALVDRWRARGPGARLINLYGPTEttvwstatlvdpddaPRESPVPIGR 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 353 PVGcegkvmrNVELRVLDKLKMPLGINEVGIIY------ARlrfkwaGYYRNPEATRR-------ALSSDGMWFRTGDIG 419
Cdd:TIGR01733 298 PLA-------NTRLYVLDDDLRPVPVGVVGELYiggpgvAR------GYLNRPELTAErfvpdpfAGGDGARLYRTGDLV 364
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 19922652 420 YLDSEGYLYIQTR-DTDVfKFNNFQIYPEQIEEFILRLPGVSEACV 464
Cdd:TIGR01733 365 RYLPDGNLEFLGRiDDQV-KIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
52-532 |
4.87e-43 |
|
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: 158.61 E-value: 4.87e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 52 GQELTGAQLAQQSARIAQAFKRLGLRRGDVVGISA-NNSTYLTSVIIAALLRGIPInPLHPEFTEETVKYMYDITEPKVI 130
Cdd:cd05934 1 GRRWTYAELLRESARIAAALAALGIRPGDRVALMLdNCPEFLFAWFALAKLGAVLV-PINTALRGDELAYIIDHSGAQLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 131 FCDvenyhiiktvngklqnpakiylvngklegvldisemlndedsitaaayvpcpklhgdhTAFIVCSSGTTGMPKGVTR 210
Cdd:cd05934 80 VVD----------------------------------------------------------PASILYTSGTTGPPKGVVI 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 211 SHRSLLCNCKNPNTY---TRDSVLLSFSPLYWISGTII-LLASLLNGCRRIITNRpYSVEYLLQLVARHKVTFLFLASHQ 286
Cdd:cd05934 102 THANLTFAGYYSARRfglGEDDVYLTVLPLFHINAQAVsVLAALSVGATLVLLPR-FSASRFWSDVRRYGATVTNYLGAM 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 287 IALLSKHDSDVMELKAQLqsiRVLIGAG--SKVCKAVCRRMyeligNQRFVVGYGLSEMG-GLSKNVGGPV--GCEGKVM 361
Cdd:cd05934 181 LSYLLAQPPSPDDRAHRL---RAAYGAPnpPELHEEFEERF-----GVRLLEGYGMTETIvGVIGPRDEPRrpGSIGRPA 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 362 RNVELRVLDKLKMPLGINEVGIIYARLRFKWA---GYYRNPEATRRALSsdGMWFRTGDIGYLDSEGYLYIQTRDTDVFK 438
Cdd:cd05934 253 PGYEVRIVDDDGQELPAGEPGELVIRGLRGWGffkGYYNMPEATAEAMR--NGWFHTGDLGYRDADGFFYFVDRKKDMIR 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 439 FNNFQIYPEQIEEFILRLPGVSEACVFGIPDAVSTN-LTACAVVRtkspEGERLTADHIRNIVEHHLSgAYHIRGGVYFI 517
Cdd:cd05934 331 RRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDeVKAVVVLR----PGETLDPEELFAFCEGQLA-YFKVPRYIRFV 405
|
490
....*....|....*
gi 19922652 518 DSLPKTPNDKLQRRK 532
Cdd:cd05934 406 DDLPKTPTEKVAKAQ 420
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
52-532 |
5.63e-43 |
|
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: 158.85 E-value: 5.63e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 52 GQELTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNSTYLTSVIIAALLRG---IPINPLHPEfteETVKYMYDITEPK 128
Cdd:cd05930 10 DQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGaayVPLDPSYPA---ERLAYILEDSGAK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 129 VIFCDvenyhiiktvngklqnpakiylvngklegvldisemlndedsitaaayvpcpklhGDHTAFIVCSSGTTGMPKGV 208
Cdd:cd05930 87 LVLTD-------------------------------------------------------PDDLAYVIYTSGSTGKPKGV 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 209 TRSHRSLLCNCKNPNTY----TRDSVLLSFSPLYWISGTIILLAsLLNGCRRIITNR--PYSVEYLLQLVARHKVTFLFL 282
Cdd:cd05930 112 MVEHRGLVNLLLWMQEAypltPGDRVLQFTSFSFDVSVWEIFGA-LLAGATLVVLPEevRKDPEALADLLAEEGITVLHL 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 283 -ASHQIALLSkhdsdvMELKAQLQSIRVLIGAGSKVCKAVCRRMYELIGNQRFVVGYGLSE--MGGLSKNVGGPVGCEGK 359
Cdd:cd05930 191 tPSLLRLLLQ------ELELAALPSLRLVLVGGEALPPDLVRRWRELLPGARLVNLYGPTEatVDATYYRVPPDDEEDGR 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 360 V-----MRNVELRVLDKLKMPLGINEVGIIY------ARlrfkwaGYYRNPEATRRA----LSSDGMW-FRTGDIGYLDS 423
Cdd:cd05930 265 VpigrpIPNTRVYVLDENLRPVPPGVPGELYiggaglAR------GYLNRPELTAERfvpnPFGPGERmYRTGDLVRWLP 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 424 EGYL-YIQTRDTDVfKFNNFQIYPEQIEEFILRLPGVSEACVFGIPDAVSTNLTACAVVrtkSPEGERLTADHIRNIVEH 502
Cdd:cd05930 339 DGNLeFLGRIDDQV-KIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVV---PDEGGELDEEELRAHLAE 414
|
490 500 510
....*....|....*....|....*....|
gi 19922652 503 HLSgAYHIRGGVYFIDSLPKTPNDKLQRRK 532
Cdd:cd05930 415 RLP-DYMVPSAFVVLDALPLTPNGKVDRKA 443
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
49-532 |
5.88e-43 |
|
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: 160.23 E-value: 5.88e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 49 DTTGqELTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNSTYLTSVIIAALLRGI---PINPLhpeFTEETVKYMYDIT 125
Cdd:cd05959 25 DDAG-SLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIvpvPVNTL---LTPDDYAYYLEDS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 126 EPKVIFCDVENYHIIKTVNGKLQnPAKIYLV----NGKLEGVLDISEMLNDEDSITAAAyvpcpKLHGDHTAFIVCSSGT 201
Cdd:cd05959 101 RARVVVVSGELAPVLAAALTKSE-HTLVVLIvsggAGPEAGALLLAELVAAEAEQLKPA-----ATHADDPAFWLYSSGS 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 202 TGMPKGVTRSHRSLLCNCknpNTYTR-------DSVLLSFSPLY-------------WISGTIILLASllngcrriitnR 261
Cdd:cd05959 175 TGRPKGVVHLHADIYWTA---ELYARnvlgireDDVCFSAAKLFfayglgnsltfplSVGATTVLMPE-----------R 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 262 PySVEYLLQLVARHKVTFLFLASHQIALLSKhdSDVMElKAQLQSIRVLIGAGSKVCKAVCRRMYELIGNQrFVVGYGLS 341
Cdd:cd05959 241 P-TPAAVFKRIRRYRPTVFFGVPTLYAAMLA--APNLP-SRDLSSLRLCVSAGEALPAEVGERWKARFGLD-ILDGIGST 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 342 EMGG--LSkNVGGPV--GCEGKVMRNVELRVLDKLKMPLGINEVGIIYARLRFKWAGYYRNPEATRRALssDGMWFRTGD 417
Cdd:cd05959 316 EMLHifLS-NRPGRVryGTTGKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTF--QGEWTRTGD 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 418 IGYLDSEGYLYIQTRDTDVFKFNNFQIYPEQIEEFILRLPGVSEACVFGIPDAVS-TNLTACAVVRTKSPEGERLTADhI 496
Cdd:cd05959 393 KYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGlTKPKAFVVLRPGYEDSEALEEE-L 471
|
490 500 510
....*....|....*....|....*....|....*.
gi 19922652 497 RNIVEHHLsGAYHIRGGVYFIDSLPKTPNDKLQRRK 532
Cdd:cd05959 472 KEFVKDRL-APYKYPRWIVFVDELPKTATGKIQRFK 506
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
28-530 |
1.02e-42 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 160.32 E-value: 1.02e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 28 TLGEVIMRVLQINADQVMQICDTTGQELTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNS-----TYLTSVIIAALLr 102
Cdd:PRK12583 19 TIGDAFDATVARFPDREALVVRHQALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCaewllTQFATARIGAIL- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 103 gIPINPlhpEFTEETVKYMYDITEPKVIFC----DVENYHII---------KTVNGKLQNP------AKIYLVNGKLEGV 163
Cdd:PRK12583 98 -VNINP---AYRASELEYALGQSGVRWVICadafKTSDYHAMlqellpglaEGQPGALACErlpelrGVVSLAPAPPPGF 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 164 LDISEMLNDEDSITAAAYVP-CPKLHGDHTAFIVCSSGTTGMPKGVTRSHRSLLCN---CKNPNTYTRDSVLLSFSPLYW 239
Cdd:PRK12583 174 LAWHELQARGETVSREALAErQASLDRDDPINIQYTSGTTGFPKGATLSHHNILNNgyfVAESLGLTEHDRLCVPVPLYH 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 240 ISGTIIL-LASLLNGCRRIITNRPYSVEYLLQLVARHKVTFLF-LASHQIALLSKHDSDVMELkaqlQSIRVLIGAGSKV 317
Cdd:PRK12583 254 CFGMVLAnLGCMTVGACLVYPNEAFDPLATLQAVEEERCTALYgVPTMFIAELDHPQRGNFDL----SSLRTGIMAGAPC 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 318 CKAVCRRMYELIGNQRFVVGYGLSEMGGLSKNVGGP------VGCEGKVMRNVELRVLDKLKMPLGINEVGIIYARLRFK 391
Cdd:PRK12583 330 PIEVMRRVMDEMHMAEVQIAYGMTETSPVSLQTTAAddlerrVETVGRTQPHLEVKVVDPDGATVPRGEIGELCTRGYSV 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 392 WAGYYRNPEATRRALSSDGmWFRTGDIGYLDSEGYLYIQTRDTDVFKFNNFQIYPEQIEEFILRLPGVSEACVFGIPDAV 471
Cdd:PRK12583 410 MKGYWNNPEATAESIDEDG-WMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEK 488
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 19922652 472 STNLTaCAVVRTKSpeGERLTADHIRNIVEHHLSgAYHIRGGVYFIDSLPKTPNDKLQR 530
Cdd:PRK12583 489 YGEEI-VAWVRLHP--GHAASEEELREFCKARIA-HFKVPRYFRFVDEFPMTVTGKVQK 543
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
55-532 |
1.06e-42 |
|
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: 157.88 E-value: 1.06e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 55 LTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNSTYLTSVIIAALLRGIPINPLHPEFTEETVKYMYDITEPKVIFCDv 134
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 135 enyhiiktvngklqnpakiylvngklegvldisemlnDEDsitaaayvpcpklhgdhTAFIVCSSGTTGMPKGVTRSHRS 214
Cdd:cd05972 80 -------------------------------------AED-----------------PALIYFTSGTTGLPKGVLHTHSY 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 215 LLCNCKNPNTYT---RDSVLLSFSPLYWISGTII-LLASLLNGCRRIITN-RPYSVEYLLQLVARHKVTFLFLASHQIAL 289
Cdd:cd05972 106 PLGHIPTAAYWLglrPDDIHWNIADPGWAKGAWSsFFGPWLLGATVFVYEgPRFDAERILELLERYGVTSFCGPPTAYRM 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 290 LSKHDSDVMELKaqlqSIRVLIGAGSKVCKAVCRRMYELIGnQRFVVGYGLSEMGGLSKNVGG-PV--GCEGKVMRNVEL 366
Cdd:cd05972 186 LIKQDLSSYKFS----HLRLVVSAGEPLNPEVIEWWRAATG-LPIRDGYGQTETGLTVGNFPDmPVkpGSMGRPTPGYDV 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 367 RVLDKLKMPLGINEVGIIYARLrfKW----AGYYRNPEATRRALSSDgmWFRTGDIGYLDSEGYLYIQTRDTDVFKFNNF 442
Cdd:cd05972 261 AIIDDDGRELPPGEEGDIAIKL--PPpglfLGYVGDPEKTEASIRGD--YYLTGDRAYRDEDGYFWFVGRADDIIKSSGY 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 443 QIYPEQIEEFILRLPGVSEACVFGIPDAVSTNLTACAVVRTKSPEGERLTADHIRNIVEHHLsGAYHIRGGVYFIDSLPK 522
Cdd:cd05972 337 RIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYEPSEELAEELQGHVKKVL-APYKYPREIEFVEELPK 415
|
490
....*....|
gi 19922652 523 TPNDKLQRRK 532
Cdd:cd05972 416 TISGKIRRVE 425
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
25-533 |
2.25e-41 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 157.08 E-value: 2.25e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 25 PEMTLGEVIMRVLQINADQVMqiCDTTGQELTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNSTYLTSVIIAAL-LRG 103
Cdd:PRK05605 30 GDTTLVDLYDNAVARFGDRPA--LDFFGATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLrLGA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 104 IPI--NPLhpeFTEETVKYMYDITEPKV-IFCDVENYHIIKTVNGKlqNPAKIYLVN--------GKLEGVLDISEMLND 172
Cdd:PRK05605 108 VVVehNPL---YTAHELEHPFEDHGARVaIVWDKVAPTVERLRRTT--PLETIVSVNmiaampllQRLALRLPIPALRKA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 173 EDSITAAA-------------------YVPCPKLHGDHTAFIVCSSGTTGMPKGVTRSHRSLLCNCKN-----PNTYTRD 228
Cdd:PRK05605 183 RAALTGPApgtvpwetlvdaaiggdgsDVSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFANAAQgkawvPGLGDGP 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 229 SVLLSFSPLYWISG-TIILLASLLNGCRRIITNRPySVEYLLQLVARHKVTFL----FLASHQIALLSKHDSDvmelkaq 303
Cdd:PRK05605 263 ERVLAALPMFHAYGlTLCLTLAVSIGGELVLLPAP-DIDLILDAMKKHPPTWLpgvpPLYEKIAEAAEERGVD------- 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 304 LQSIRVLIGAGSKVCKAVCRRMYELIGNqRFVVGYGLSEMGGLSknVGGPVGCE------GKVMRNVELRVLDK----LK 373
Cdd:PRK05605 335 LSGVRNAFSGAMALPVSTVELWEKLTGG-LLVEGYGLTETSPII--VGNPMSDDrrpgyvGVPFPDTEVRIVDPedpdET 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 374 MPLGinEVGIIYARLRFKWAGYYRNPEATRRALSSDgmWFRTGDIGYLDSEGYLYIQTRDTDVFKFNNFQIYPEQIEEFI 453
Cdd:PRK05605 412 MPDG--EEGELLVRGPQVFKGYWNRPEETAKSFLDG--WFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVL 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 454 LRLPGVSEACVFGIP-DAVSTNLTACAVVRtkspEGERLTADHIRNIVEHHLSgAYHIRGGVYFIDSLPKTPNDKLQRRK 532
Cdd:PRK05605 488 REHPGVEDAAVVGLPrEDGSEEVVAAVVLE----PGAALDPEGLRAYCREHLT-RYKVPRRFYHVDELPRDQLGKVRRRE 562
|
.
gi 19922652 533 V 533
Cdd:PRK05605 563 V 563
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
56-533 |
2.31e-41 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 156.35 E-value: 2.31e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 56 TGAQLAQQSARIAQAFKRLGLRRGDVVGISANNSTYLTSVIIAALLRGIPINPLHPEFTEETVKYMYDITEPKVIFCDVE 135
Cdd:PRK07470 34 TWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPDEVAYLAEASGARAMICHAD 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 136 NYHIIKTVNGklqnpakiylVNGKLEGVLDI--SEMLNDEDSITAA---AYVPCPKLHGDHTAFIVCSSGTTGMPKGVTR 210
Cdd:PRK07470 114 FPEHAAAVRA----------ASPDLTHVVAIggARAGLDYEALVARhlgARVANAAVDHDDPCWFFFTSGTTGRPKAAVL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 211 SHRSL-------LCNCKnPNTyTRDSVLLSFSPLYWISGtIILLASLLNGCRRIIT-NRPYSVEYLLQLVARHKVTFLFL 282
Cdd:PRK07470 184 THGQMafvitnhLADLM-PGT-TEQDASLVVAPLSHGAG-IHQLCQVARGAATVLLpSERFDPAEVWALVERHRVTNLFT 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 283 ASHQIALLSKHDS-DvmelKAQLQSIRVLIGAGSKVCKAVCRRMYELIGNqRFVVGYGLSEMGG--------LSKNVGGP 353
Cdd:PRK07470 261 VPTILKMLVEHPAvD----RYDHSSLRYVIYAGAPMYRADQKRALAKLGK-VLVQYFGLGEVTGnitvlppaLHDAEDGP 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 354 ---VGCEGKVMRNVELRVLDKLKMPLGINEVGIIYARLRFKWAGYYRNPEATRRALSsDGmWFRTGDIGYLDSEGYLYIQ 430
Cdd:PRK07470 336 darIGTCGFERTGMEVQIQDDEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAFR-DG-WFRTGDLGHLDARGFLYIT 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 431 TRDTDVFKFNNFQIYPEQIEEFILRLPGVSEACVFGIPDAVSTNL-TACAVVRtkspEGERLTADHIRNIVEHHLSgAYH 509
Cdd:PRK07470 414 GRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVgVAVCVAR----DGAPVDEAELLAWLDGKVA-RYK 488
|
490 500
....*....|....*....|....
gi 19922652 510 IRGGVYFIDSLPKTPNDKLQRRKV 533
Cdd:PRK07470 489 LPKRFFFWDALPKSGYGKITKKMV 512
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
55-532 |
5.79e-41 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 154.86 E-value: 5.79e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 55 LTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNSTYLTSVIIAALLRGIPINPLHPEFTEETVKYMYDITEPKVIfcdV 134
Cdd:PRK12406 12 RSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVL---I 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 135 ENYHIIKTVNGKL---------QNPAKI---YLVNGKL----EGVLDISEMLNDEDSITAAAyVPCPklhgdhtAFIVCS 198
Cdd:PRK12406 89 AHADLLHGLASALpagvtvlsvPTPPEIaaaYRISPALltppAGAIDWEGWLAQQEPYDGPP-VPQP-------QSMIYT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 199 SGTTGMPKGVTRshrsllcnckNPNT----------------YTRDSVLLSFSPLYWISGTIILLASLLNGCRRIITNRp 262
Cdd:PRK12406 161 SGTTGHPKGVRR----------AAPTpeqaaaaeqmraliygLKPGIRALLTGPLYHSAPNAYGLRAGRLGGVLVLQPR- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 263 YSVEYLLQLVARHKVTFLFLASHQIALLSKHDSDVMElKAQLQSIRVLIGAGSKVCKAVCRRMYELIGNqrfVVG--YGL 340
Cdd:PRK12406 230 FDPEELLQLIERHRITHMHMVPTMFIRLLKLPEEVRA-KYDVSSLRHVIHAAAPCPADVKRAMIEWWGP---VIYeyYGS 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 341 SEMG---------GLSKnvggPvGCEGKVMRNVELRVLDKLKMPLGINEVGIIYARLrfkwAGY----YRNPEATRRALS 407
Cdd:PRK12406 306 TESGavtfatsedALSH----P-GTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRI----AGNpdftYHNKPEKRAEID 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 408 SDGmWFRTGDIGYLDSEGYLYIQTRDTDVFKFNNFQIYPEQIEEFILRLPGVSEACVFGIPDAvSTNLTACAVVRTKspE 487
Cdd:PRK12406 377 RGG-FITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDA-EFGEALMAVVEPQ--P 452
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 19922652 488 GERLTADHIRNIVEHHLSGaYHIRGGVYFIDSLPKTPNDKLQRRK 532
Cdd:PRK12406 453 GATLDEADIRAQLKARLAG-YKVPKHIEIMAELPREDSGKIFKRR 496
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
52-532 |
1.74e-40 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 152.81 E-value: 1.74e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 52 GQELTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNSTYLTSVIIAALLRGIPINPLHPEFTEETVKYMYDITEPKVIF 131
Cdd:PRK03640 25 EKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDDAEVKCLI 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 132 CDvENYhiiktvngklqnPAKIYLvngklEGVLDISEMLNDEDSITaaayVPCPKLHGDHTAFIVCSSGTTGMPKGVTRS 211
Cdd:PRK03640 105 TD-DDF------------EAKLIP-----GISVKFAELMNGPKEEA----EIQEEFDLDEVATIMYTSGTTGKPKGVIQT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 212 HR----SLLCNCKNPNTYTRDSVLLSFsPLYWISGTIILLASLLNGCRrIITNRPYSVEYLLQLVARHKVTFLFLAShqi 287
Cdd:PRK03640 163 YGnhwwSAVGSALNLGLTEDDCWLAAV-PIFHISGLSILMRSVIYGMR-VVLVEKFDAEKINKLLQTGGVTIISVVS--- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 288 ALLSKhdsdvmeLKAQLQ------SIR-VLIGAG--SKVCKAVCRRmyelignQRFVV--GYGLSEMGglSKNVGGP--- 353
Cdd:PRK03640 238 TMLQR-------LLERLGegtypsSFRcMLLGGGpaPKPLLEQCKE-------KGIPVyqSYGMTETA--SQIVTLSped 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 354 ----VGCEGKVMRNVELRVLDKLKmPLGINEVGIIYARLRFKWAGYYRNPEATRRALSsDGmWFRTGDIGYLDSEGYLYI 429
Cdd:PRK03640 302 altkLGSAGKPLFPCELKIEKDGV-VVPPFEEGEIVVKGPNVTKGYLNREDATRETFQ-DG-WFKTGDIGYLDEEGFLYV 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 430 QTRDTDVFKFNNFQIYPEQIEEFILRLPGVSEACVFGIPDAVSTNLTACAVVRtkspeGERLTADHIRNIVEHHLSGaYH 509
Cdd:PRK03640 379 LDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVK-----SGEVTEEELRHFCEEKLAK-YK 452
|
490 500
....*....|....*....|...
gi 19922652 510 IRGGVYFIDSLPKTPNDKLQRRK 532
Cdd:PRK03640 453 VPKRFYFVEELPRNASGKLLRHE 475
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
47-532 |
2.98e-40 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 153.54 E-value: 2.98e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 47 ICDTTGqELTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNSTYLTSVIIAALLRGIPINPLHPEFTEETVKYMYDITE 126
Cdd:PRK07788 68 LIDERG-TLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQLAEVAAREG 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 127 PKVIFCDVENYHIIktvnGKLQNPAKIYLVNG----KLEGVLDISEMLNDEDSITAAAYVPCPKLHGdhtAFIVCSSGTT 202
Cdd:PRK07788 147 VKALVYDDEFTDLL----SALPPDLGRLRAWGgnpdDDEPSGSTDETLDDLIAGSSTAPLPKPPKPG---GIVILTSGTT 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 203 GMPKGVTRSHrsllcncknPNTYT------------RDSVLLSFSPLYWISGTIILLASLLNGCrRIITNRPYSVEYLLQ 270
Cdd:PRK07788 220 GTPKGAPRPE---------PSPLAplagllsrvpfrAGETTLLPAPMFHATGWAHLTLAMALGS-TVVLRRRFDPEATLE 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 271 LVARHKVTFL-----FLaSHQIALLSKHDSdvmelKAQLQSIRVLIGAGSKVCKAVCRRMYELIGNqrfVVG--YGLSE- 342
Cdd:PRK07788 290 DIAKHKATALvvvpvML-SRILDLGPEVLA-----KYDTSSLKIIFVSGSALSPELATRALEAFGP---VLYnlYGSTEv 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 343 -------MGGLSKNvggPvGCEGKVMRNVELRVLDKLKMPLGINEVGIIYARLRFKWAGYY--RNPEatrralSSDGMwF 413
Cdd:PRK07788 361 afatiatPEDLAEA---P-GTVGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFPFEGYTdgRDKQ------IIDGL-L 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 414 RTGDIGYLDSEGYLYIQTRDTDVFKFNNFQIYPEQIEEFILRLPGVSEACVFGIPDAVSTNLTACAVVRTkspEGERLTA 493
Cdd:PRK07788 430 SSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKA---PGAALDE 506
|
490 500 510
....*....|....*....|....*....|....*....
gi 19922652 494 DHIRNIVEHHLSgAYHIRGGVYFIDSLPKTPNDKLQRRK 532
Cdd:PRK07788 507 DAIKDYVRDNLA-RYKVPRDVVFLDELPRNPTGKVLKRE 544
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
50-531 |
9.74e-40 |
|
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: 150.13 E-value: 9.74e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 50 TTGQELTGAQLAQQSARIAQAFKRLG-LRRGDVVGISANNSTYLTSVIIAALLRGIPINPLHPEFTEETVKYMYDITEPK 128
Cdd:cd05941 7 DDGDSITYADLVARAARLANRLLALGkDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITDSEPS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 129 VifcdvenyhiiktvngklqnpakiylvngklegVLDIsemlndedsitaaayvpcpklhgdhtAFIVCSSGTTGMPKGV 208
Cdd:cd05941 87 L---------------------------------VLDP--------------------------ALILYTSGTTGRPKGV 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 209 TRSHRSLLCNCK---NPNTYTRDSVLLSFSPLYWISGTI-ILLASLLNGCRRIITnRPYSVEYLLQLVARHKVTFLF--- 281
Cdd:cd05941 108 VLTHANLAANVRalvDAWRWTEDDVLLHVLPLHHVHGLVnALLCPLFAGASVEFL-PKFDPKEVAISRLMPSITVFMgvp 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 282 -LASHQIALLSKHDSDV-MELKAQLQSIRVLIgAGSKVCKAVCRRMYELIGNQRFVVGYGLSEMG-GLSKNVGGP--VGC 356
Cdd:cd05941 187 tIYTRLLQYYEAHFTDPqFARAAAAERLRLMV-SGSAALPVPTLEEWEAITGHTLLERYGMTEIGmALSNPLDGErrPGT 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 357 EGKVMRNVELRVLDKL-KMPLGINEVGIIYAR--LRFKwaGYYRNPEATRRALSSDGmWFRTGDIGYLDSEGYLYIQTRD 433
Cdd:cd05941 266 VGMPLPGVQARIVDEEtGEPLPRGEVGEIQVRgpSVFK--EYWNKPEATKEEFTDDG-WFKTGDLGVVDEDGYYWILGRS 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 434 -TDVFKFNNFQIYPEQIEEFILRLPGVSEACVFGIPDAVSTNLTACAVVRtkSPEGERLTADHIRNIVEHHLSgAYHIRG 512
Cdd:cd05941 343 sVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVL--RAGAAALSLEELKEWAKQRLA-PYKRPR 419
|
490
....*....|....*....
gi 19922652 513 GVYFIDSLPKTPNDKLQRR 531
Cdd:cd05941 420 RLILVDELPRNAMGKVNKK 438
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
28-541 |
1.24e-39 |
|
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: 151.45 E-value: 1.24e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 28 TLGEVIMRVLQINADQVMQICDttGQELTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNSTYLTSVIIAALLRG-IPI 106
Cdd:COG1021 26 TLGDLLRRRAERHPDRIAVVDG--ERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGaIPV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 107 N--PLHPEfTEetVKYMYDITEPK-VIFCDVenyH-------IIKTVNGKLQNPAKIyLVNGKLEGVLDISEMLNDEdsi 176
Cdd:COG1021 104 FalPAHRR-AE--ISHFAEQSEAVaYIIPDR---HrgfdyraLARELQAEVPSLRHV-LVVGDAGEFTSLDALLAAP--- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 177 tAAAYVPCPklHGDHTAFIVCSSGTTGMPKGVTRSHRSLLCN-------CKnpntYTRDSVLL-------SF---SPlyw 239
Cdd:COG1021 174 -ADLSEPRP--DPDDVAFFQLSGGTTGLPKLIPRTHDDYLYSvrasaeiCG----LDADTVYLaalpaahNFplsSP--- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 240 isGtiiLLASLLNGCRRIITNRPySVEYLLQLVARHKVTFLFLA-SHQIALLSKHDSDvmelKAQLQSIRVLIGAGSKVC 318
Cdd:COG1021 244 --G---VLGVLYAGGTVVLAPDP-SPDTAFPLIERERVTVTALVpPLALLWLDAAERS----RYDLSSLRVLQVGGAKLS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 319 KAVCRRMYELIG---NQRFvvgyGLSEmgGL-------------SKNVGGPVgCEGKvmrnvELRVLDKLKMPLGINEVG 382
Cdd:COG1021 314 PELARRVRPALGctlQQVF----GMAE--GLvnytrlddpeeviLTTQGRPI-SPDD-----EVRIVDEDGNPVPPGEVG 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 383 IIYAR----LRfkwaGYYRNPEATRRALSSDGmWFRTGDIGYLDSEGYLYIQTRDTDVF-----KfnnfqIYPEQIEEFI 453
Cdd:COG1021 382 ELLTRgpytIR----GYYRAPEHNARAFTPDG-FYRTGDLVRRTPDGYLVVEGRAKDQInrggeK-----IAAEEVENLL 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 454 LRLPGVSEACVFGIPDAVstnL--TACAVVrtkSPEGERLTADHIRniveHHLSG----AYHIRGGVYFIDSLPKTPNDK 527
Cdd:COG1021 452 LAHPAVHDAAVVAMPDEY---LgeRSCAFV---VPRGEPLTLAELR----RFLRErglaAFKLPDRLEFVDALPLTAVGK 521
|
570
....*....|....
gi 19922652 528 LQRRKvlgLVQQLE 541
Cdd:COG1021 522 IDKKA---LRAALA 532
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
54-532 |
1.28e-39 |
|
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: 149.03 E-value: 1.28e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 54 ELTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNSTYLTSVIIAALLRGIPINPLHPEFTEETVKYMyditepkvifcd 133
Cdd:cd05912 1 SYTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQ------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 134 venyhiiktvngklqnpakiylvngklegvldisemLNDEDSITaaayvpcpklhgDHTAFIVCSSGTTGMPKGVTRSHR 213
Cdd:cd05912 69 ------------------------------------LKDSDVKL------------DDIATIMYTSGTTGKPKGVQQTFG 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 214 SLLCN---CKNPNTYTRDSVLLSFSPLYWISGTIILLASLLNGCRRIITNRpYSVEYLLQLVARHKVTFLFLASHQIA-L 289
Cdd:cd05912 101 NHWWSaigSALNLGLTEDDNWLCALPLFHISGLSILMRSVIYGMTVYLVDK-FDAEQVLHLINSGKVTIISVVPTMLQrL 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 290 LSKHDSDVMElkaqlqSIR-VLIGAG--SKVCKAVCRRMyeligNQRFVVGYGLSEMGglSKNVGGP-------VGCEGK 359
Cdd:cd05912 180 LEILGEGYPN------NLRcILLGGGpaPKPLLEQCKEK-----GIPVYQSYGMTETC--SQIVTLSpedalnkIGSAGK 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 360 VMRNVELRVLDKLKMPLGINEVGIIYARLRfkwAGYYRNPEATRRALSSDgmWFRTGDIGYLDSEGYLYIQTRDTDVFKF 439
Cdd:cd05912 247 PLFPVELKIEDDGQPPYEVGEILLKGPNVT---KGYLNRPDATEESFENG--WFKTGDIGYLDEEGFLYVLDRRSDLIIS 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 440 NNFQIYPEQIEEFILRLPGVSEACVFGIPDAVSTNLTACAVVRTKSpegerLTADHIRNIVEHHLSGaYHIRGGVYFIDS 519
Cdd:cd05912 322 GGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSERP-----ISEEELIAYCSEKLAK-YKVPKKIYFVDE 395
|
490
....*....|...
gi 19922652 520 LPKTPNDKLQRRK 532
Cdd:cd05912 396 LPRTASGKLLRHE 408
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
52-531 |
1.64e-39 |
|
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: 150.35 E-value: 1.64e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 52 GQELTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNSTYLTSVIIAALLRGIPINPLHPEFTEETVKYMyditepkvif 131
Cdd:cd05923 26 GLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAEL---------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 132 cdVENYHIIKTV--NGKLQNPAkiylVNGKLEGVLDISEMLNDEDSITAAAYVPCPKLHGDHTAFIVCSSGTTGMPKGV- 208
Cdd:cd05923 96 --IERGEMTAAViaVDAQVMDA----IFQSGVRVLALSDLVGLGEPESAGPLIEDPPREPEQPAFVFYTSGTTGLPKGAv 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 209 ----TRSHRSLLCNCKNPNTYTRDSVLLSFSPLYWISGTIILLASLLNGCRRIITNRPYSVEYLLQLVARHKVTFLFLA- 283
Cdd:cd05923 170 ipqrAAESRVLFMSTQAGLRHGRHNVVLGLMPLYHVIGFFAVLVAALALDGTYVVVEEFDPADALKLIEQERVTSLFATp 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 284 SHQIALLSKhdsdVMELKAQLQSIRVLIGAGSKVCKAVCRRMYELIGNqRFVVGYGLSEMGGLSKNVGGPVGCEGKVMRN 363
Cdd:cd05923 250 THLDALAAA----AEFAGLKLSSLRHVTFAGATMPDAVLERVNQHLPG-EKVNIYGTTEAMNSLYMRDARTGTEMRPGFF 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 364 VELRVLDKLKMPLGINEVG-----IIYARLRFKWAGYYRNPEATRRALSsDGmWFRTGDIGYLDSEGYLYIQTRDTDVFK 438
Cdd:cd05923 325 SEVRIVRIGGSPDEALANGeegelIVAAAADAAFTGYLNQPEATAKKLQ-DG-WYRTGDVGYVDPSGDVRILGRVDDMII 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 439 FNNFQIYPEQIEEFILRLPGVSEACVFGIPDAV-STNLTACAVVRTKSPEGERLT--------ADHIRnivehhlSGAYh 509
Cdd:cd05923 403 SGGENIHPSEIERVLSRHPGVTEVVVIGVADERwGQSVTACVVPREGTLSADELDqfcraselADFKR-------PRRY- 474
|
490 500
....*....|....*....|..
gi 19922652 510 irggvYFIDSLPKTPNDKLQRR 531
Cdd:cd05923 475 -----FFLDELPKNAMNKVLRR 491
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
50-533 |
2.62e-39 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 150.01 E-value: 2.62e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 50 TTGQELTGAQLAQQSARIAQAFK-RLGLRRGDVVGISANNSTYLTSVIIAALLRGIPINPLHPEFTEETVKYMYDITEPK 128
Cdd:PRK06839 23 TEEEEMTYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 129 VIFCDVENYHIIKTVNGK--LQNPAKIYlvngKLEGVLDiSEMLNDEDSitaaayvpcpklhGDHTAFIVC-SSGTTGMP 205
Cdd:PRK06839 103 VLFVEKTFQNMALSMQKVsyVQRVISIT----SLKEIED-RKIDNFVEK-------------NESASFIICyTSGTTGKP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 206 KGVTRSHRSLLCNCKNpNTY----TRDSVLLSFSPLYWISGT-IILLASLLNGcRRIITNRPYSVEYLLQLVARHKVTFL 280
Cdd:PRK06839 165 KGAVLTQENMFWNALN-NTFaidlTMHDRSIVLLPLFHIGGIgLFAFPTLFAG-GVIIVPRKFEPTKALSMIEKHKVTVV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 281 F--LASHQiALLSKHDSdvmeLKAQLQSIRVLIGAGSKVCKAVCRRMYELigNQRFVVGYGLSEMGG-----LSKNVGGP 353
Cdd:PRK06839 243 MgvPTIHQ-ALINCSKF----ETTNLQSVRWFYNGGAPCPEELMREFIDR--GFLFGQGFGMTETSPtvfmlSEEDARRK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 354 VGCEGKVMRNVELRVLDKLKMPLGINEVGIIYARLRFKWAGYYRNPEATRRALSsDGmWFRTGDIGYLDSEGYLYIQTRD 433
Cdd:PRK06839 316 VGSIGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEETIQ-DG-WLCTGDLARVDEDGFVYIVGRK 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 434 TDVFKFNNFQIYPEQIEEFILRLPGVSEACVFGIPDAVSTNLTACAVVRtKSpeGERLTADHIRNIVEHHLsGAYHIRGG 513
Cdd:PRK06839 394 KEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVK-KS--SSVLIEKDVIEHCRLFL-AKYKIPKE 469
|
490 500
....*....|....*....|
gi 19922652 514 VYFIDSLPKTPNDKLQRRKV 533
Cdd:PRK06839 470 IVFLKELPKNATGKIQKAQL 489
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
23-530 |
8.44e-39 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 149.13 E-value: 8.44e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 23 YGPEMTLGEVIMRVLQINADQVMqICDTTGQELTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNSTYLTSVIIAALLR 102
Cdd:PRK06087 19 YWGDASLADYWQQTARAMPDKIA-VVDNHGASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 103 GIPINPLHPEFTEETVKYMYDITEPKVIFC-----DVENYHIIKTVNGKLQNPAKIYLV--NGKLEGVLDISEMLNDEDS 175
Cdd:PRK06087 98 GAVSVPLLPSWREAELVWVLNKCQAKMFFAptlfkQTRPVDLILPLQNQLPQLQQIVGVdkLAPATSSLSLSQIIADYEP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 176 ITAAayvpcPKLHGDHTAFIVCSSGTTGMPKGVTRSHRSLLCN----CKNPNTyTRDSVLLSFSPLYWISGTII-LLASL 250
Cdd:PRK06087 178 LTTA-----ITTHGDELAAVLFTSGTEGLPKGVMLTHNNILASerayCARLNL-TWQDVFMMPAPLGHATGFLHgVTAPF 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 251 LNGCRRIITNRpYSVEYLLQLVARHKVTFLFLASHQIALLSKHdsdVMELKAQLQSIRVLIGAGSKVCKAVCRRMYEliG 330
Cdd:PRK06087 252 LIGARSVLLDI-FTPDACLALLEQQRCTCMLGATPFIYDLLNL---LEKQPADLSALRFFLCGGTTIPKKVARECQQ--R 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 331 NQRFVVGYGLSE-----MGGLSKNVGGPVGCEGKVMRNVELRVLDKLKMPLGINEVGIIYARLRFKWAGYYRNPEATRRA 405
Cdd:PRK06087 326 GIKLLSVYGSTEssphaVVNLDDPLSRFMHTDGYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYLDEPELTARA 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 406 LSSDGmWFRTGDIGYLDSEGYLYIQTRDTDVFKFNNFQIYPEQIEEFILRLPGVSEACVFGIPDAVSTNLTaCAVVRTKS 485
Cdd:PRK06087 406 LDEEG-WYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERS-CAYVVLKA 483
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 19922652 486 PEGERLTADHIRNIVEHHLSGAYHIRGGVYfIDSLPKTPNDKLQR 530
Cdd:PRK06087 484 PHHSLTLEEVVAFFSRKRVAKYKYPEHIVV-IDKLPRTASGKIQK 527
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
54-539 |
1.03e-38 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 149.05 E-value: 1.03e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 54 ELTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNSTYLTSVIIAALLRGIPINPLHPEFTEETVKYMYDITEPKVI--- 130
Cdd:PRK13295 55 RFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERELSFMLKHAESKVLvvp 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 131 --FCDVENYHIIKTVNGKLQNPAKIYLVNGklEGVLDISEMLND---EDSITAAAYVPCPKLHGDHTAFIVCSSGTTGMP 205
Cdd:PRK13295 135 ktFRGFDHAAMARRLRPELPALRHVVVVGG--DGADSFEALLITpawEQEPDAPAILARLRPGPDDVTQLIYTSGTTGEP 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 206 KGVTRSHRSLLCN---CKNPNTYTRDSVLLSFSPLYWISGTII-LLASLLNGCRRIITNRpYSVEYLLQLVARHKVTFLF 281
Cdd:PRK13295 213 KGVMHTANTLMANivpYAERLGLGADDVILMASPMAHQTGFMYgLMMPVMLGATAVLQDI-WDPARAAELIRTEGVTFTM 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 282 LASHQIALLSKHdsdVMELKAQLQSIRVLIGAGSKVCKAVCRRMYELIGnQRFVVGYGLSEMGGLSknVGGP-------V 354
Cdd:PRK13295 292 ASTPFLTDLTRA---VKESGRPVSSLRTFLCAGAPIPGALVERARAALG-AKIVSAWGMTENGAVT--LTKLddpderaS 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 355 GCEGKVMRNVELRVLDKLKMPLGINEVGIIYARLRFKWAGYYRNPEATRraLSSDGmWFRTGDIGYLDSEGYLYIQTRDT 434
Cdd:PRK13295 366 TTDGCPLPGVEVRVVDADGAPLPAGQIGRLQVRGCSNFGGYLKRPQLNG--TDADG-WFDTGDLARIDADGYIRISGRSK 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 435 DVFKFNNFQIYPEQIEEFILRLPGVSEACVFGIPDAvstNL--TACAVVRTKSpeGERLT-ADHIRNIVEHHLSGAYhIR 511
Cdd:PRK13295 443 DVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDE---RLgeRACAFVVPRP--GQSLDfEEMVEFLKAQKVAKQY-IP 516
|
490 500
....*....|....*....|....*...
gi 19922652 512 GGVYFIDSLPKTPNDKLQRRKVLGLVQQ 539
Cdd:PRK13295 517 ERLVVRDALPRTPSGKIQKFRLREMLRG 544
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
52-531 |
1.68e-38 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 147.72 E-value: 1.68e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 52 GQELTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNSTYLTSVIIAALLRGIPINPLHPEFTEETVKYMYDITEPKVIF 131
Cdd:PRK06145 25 DQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYILGDAGAKLLL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 132 CDVENYHIIKTVNGKLqnpakiylvngklegVLDisEMLNDEDSITAAAYVPCPKLHG---DHTAFIVCSSGTTGMPKGV 208
Cdd:PRK06145 105 VDEEFDAIVALETPKI---------------VID--AAAQADSRRLAQGGLEIPPQAAvapTDLVRLMYTSGTTDRPKGV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 209 TRSHRSLLCNCKNPNT---YTRDSVLLSFSPLYWIsGTIIL--LASLLNGcRRIITNRPYSVEYLLQLVARHKVTFLFLA 283
Cdd:PRK06145 168 MHSYGNLHWKSIDHVIalgLTASERLLVVGPLYHV-GAFDLpgIAVLWVG-GTLRIHREFDPEAVLAAIERHRLTCAWMA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 284 SHQI-ALLSKHDSDvmelKAQLQSIRVLIGAGSKVCKAVCRRMYELIGNQRFVVGYGLSE-MGGLSKNVGG----PVGCE 357
Cdd:PRK06145 246 PVMLsRVLTVPDRD----RFDLDSLAWCIGGGEKTPESRIRDFTRVFTRARYIDAYGLTEtCSGDTLMEAGreieKIGST 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 358 GKVMRNVELRVLDKLKMPLGINEVGIIYARLRFKWAGYYRNPEATRRALSSDgmWFRTGDIGYLDSEGYLYIQTRDTDVF 437
Cdd:PRK06145 322 GRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGD--WFRSGDVGYLDEEGFLYLTDRKKDMI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 438 KFNNFQIYPEQIEEFILRLPGVSEACVFGIPDAV-STNLTACAVVRtkspEGERLTADHIRNIVEHHLsGAYHIRGGVYF 516
Cdd:PRK06145 400 ISGGENIASSEVERVIYELPEVAEAAVIGVHDDRwGERITAVVVLN----PGATLTLEALDRHCRQRL-ASFKVPRQLKV 474
|
490
....*....|....*
gi 19922652 517 IDSLPKTPNDKLQRR 531
Cdd:PRK06145 475 RDELPRNPSGKVLKR 489
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
52-541 |
1.76e-38 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 148.65 E-value: 1.76e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 52 GQELTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNSTYLTSVIIAALLRG---IPINPLhpeFTEETVKYMYDITEPK 128
Cdd:PRK06178 56 GHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGavhVPVSPL---FREHELSYELNDAGAE 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 129 VIFC-------------DVENYHIIKTVNGKLQnPAKIYL-----VNGKLEGVLDISEMLNDEDSITAAAYVPCPKLhgD 190
Cdd:PRK06178 133 VLLAldqlapvveqvraETSLRHVIVTSLADVL-PAEPTLplpdsLRAPRLAAAGAIDLLPALRACTAPVPLPPPAL--D 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 191 HTAFIVCSSGTTGMPKGVTRSHRSLL----CNCKNPNTYTRDSVLLSFSPLYWISG-TIILLASLLNGCRRIITNRpYSV 265
Cdd:PRK06178 210 ALAALNYTGGTTGMPKGCEHTQRDMVytaaAAYAVAVVGGEDSVFLSFLPEFWIAGeNFGLLFPLFSGATLVLLAR-WDA 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 266 EYLLQLVARHKVTFLFLASHQIALLSKH----DSDVMELKAqlqsirvlIGAGSKVCK---AVCRRMYELIGNQRFVVGY 338
Cdd:PRK06178 289 VAFMAAVERYRVTRTVMLVDNAVELMDHprfaEYDLSSLRQ--------VRVVSFVKKlnpDYRQRWRALTGSVLAEAAW 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 339 GLSE-------MGGLSKN----------VGGPV-GCEGKVMrNVELRVLdklkMPLGinEVGIIYARLRFKWAGYYRNPE 400
Cdd:PRK06178 361 GMTEthtcdtfTAGFQDDdfdllsqpvfVGLPVpGTEFKIC-DFETGEL----LPLG--AEGEIVVRTPSLLKGYWNKPE 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 401 ATRRALsSDGmWFRTGDIGYLDSEGYLYIQTRDTDVFKFNNFQIYPEQIEEFILRLPGVSEACVFGIPDAVSTNLtACAV 480
Cdd:PRK06178 434 ATAEAL-RDG-WLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQV-PVAF 510
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19922652 481 VRTKspEGERLTADHIRNIVEHHLSgAYHIRgGVYFIDSLPKTPNDKLQRRKVLGLVQQLE 541
Cdd:PRK06178 511 VQLK--PGADLTAAALQAWCRENMA-VYKVP-EIRIVDALPMTATGKVRKQDLQALAEELK 567
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
55-530 |
2.22e-38 |
|
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: 146.12 E-value: 2.22e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 55 LTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNSTYLTSVIIAALLRGIPINPLHPEFTEETVKYMYDITEPKVIFCDV 134
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 135 ENYHiiktvngklqnpakiylvngKLegvldisemlnDEDsitaaayvpcPKLHgdhtafiVCSSGTTGMPKGVTRSHRS 214
Cdd:cd05973 81 ANRH--------------------KL-----------DSD----------PFVM-------MFTSGTTGLPKGVPVPLRA 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 215 LLCNcknpNTYTRDSVLLSFSPLYWISGT--------IILLASLLNGCRRIITNRPYSVEYLLQLVARHKVTFLFLASHQ 286
Cdd:cd05973 113 LAAF----GAYLRDAVDLRPEDSFWNAADpgwayglyYAITGPLALGHPTILLEGGFSVESTWRVIERLGVTNLAGSPTA 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 287 IALLSkhdSDVMELKAQLQ-SIRVLIGAGSKVCKAVCR----RMYELIGNQrfvvgYGLSEMGGLSKNVGGP-----VGC 356
Cdd:cd05973 189 YRLLM---AAGAEVPARPKgRLRRVSSAGEPLTPEVIRwfdaALGVPIHDH-----YGQTELGMVLANHHALehpvhAGS 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 357 EGKVMRNVELRVLDKLKMPLGINEVGII---YARLRFKWAGYYRNPEATrralSSDGMWFRTGDIGYLDSEGYLYIQTRD 433
Cdd:cd05973 261 AGRAMPGWRVAVLDDDGDELGPGEPGRLaidIANSPLMWFRGYQLPDTP----AIDGGYYLTGDTVEFDPDGSFSFIGRA 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 434 TDVFKFNNFQIYPEQIEEFILRLPGVSEACVFGIPDAVSTNLTACAVVRTKSPEGERLTADHIRNIVEHHLSGAYHIRgG 513
Cdd:cd05973 337 DDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHEGTPALADELQLHVKKRLSAHAYPR-T 415
|
490
....*....|....*..
gi 19922652 514 VYFIDSLPKTPNDKLQR 530
Cdd:cd05973 416 IHFVDELPKTPSGKIQR 432
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
55-531 |
2.87e-37 |
|
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: 143.03 E-value: 2.87e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 55 LTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNSTYLTSVIIAALLRGIPINPLHPEFTEETVKYmyditepkvifcdv 134
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRD-------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 135 enyhiiktvngKLQNP-AKIYLVNGKLEGVLDISEMlndedsitaaayvpcpklhgdhtAFIVCSSGTTGMPKGVTRSHR 213
Cdd:cd05969 67 -----------RLENSeAKVLITTEELYERTDPEDP-----------------------TLLHYTSGTTGTPKGVLHVHD 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 214 SLLcncknpnTY---TRDSVLLSFSPLY-------WISGTII-LLASLLNGCRRIITNRPYSVEYLLQLVARHKVTFLFL 282
Cdd:cd05969 113 AMI-------FYyftGKYVLDLHPDDIYwctadpgWVTGTVYgIWAPWLNGVTNVVYEGRFDAESWYGIIERVKVTVWYT 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 283 ASHQIALLSKHDsDVMELKAQLQSIRVLIGAGSKVCKAVCRRMYELIgNQRFVVGYGLSEMGG--LSKNVGGPV--GCEG 358
Cdd:cd05969 186 APTAIRMLMKEG-DELARKYDLSSLRFIHSVGEPLNPEAIRWGMEVF-GVPIHDTWWQTETGSimIANYPCMPIkpGSMG 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 359 KVMRNVELRVLDKLKMPLGINEVGIIyaRLRFKWA----GYYRNPEatRRALSSDGMWFRTGDIGYLDSEGYLYIQTRDT 434
Cdd:cd05969 264 KPLPGVKAAVVDENGNELPPGTKGIL--ALKPGWPsmfrGIWNDEE--RYKNSFIDGWYLTGDLAYRDEDGYFWFVGRAD 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 435 DVFKFNNFQIYPEQIEEFILRLPGVSEACVFGIPDAVSTNLTACAVVRTKSPEGERLTADHIRNIVEHHLSGAYHIRgGV 514
Cdd:cd05969 340 DIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPSDELKEEIINFVRQKLGAHVAPR-EI 418
|
490
....*....|....*..
gi 19922652 515 YFIDSLPKTPNDKLQRR 531
Cdd:cd05969 419 EFVDNLPKTRSGKIMRR 435
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
28-531 |
3.03e-37 |
|
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: 143.62 E-value: 3.03e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 28 TLGEVIMRVLQINADQVMQICDttGQELTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNSTYLTSVIIAALLRG-IPI 106
Cdd:cd05920 16 PLGDLLARSAARHPDRIAVVDG--DRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGaVPV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 107 N--PLHPEfteetvkymYDITepkvifcdvenyHIIKtvngklQNPAKIYLVNGKLEGVLdisemlNDEDSITAAAYVPC 184
Cdd:cd05920 94 LalPSHRR---------SELS------------AFCA------HAEAVAYIVPDRHAGFD------HRALARELAESIPE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 185 PklhgdhtAFIVCSSGTTGMPKGVTRSHRSLLCN-------CKnpntYTRDSVLLSFSPL---YWISGTIILlASLLNGC 254
Cdd:cd05920 141 V-------ALFLLSGGTTGTPKLIPRTHNDYAYNvrasaevCG----LDQDTVYLAVLPAahnFPLACPGVL-GTLLAGG 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 255 RRIITNRPySVEYLLQLVARHKVTFLFLAShqiALLSKHDSDVMELKAQLQSIRVLIGAGSKVCKAVCRRMYELIGNQRF 334
Cdd:cd05920 209 RVVLAPDP-SPDAAFPLIEREGVTVTALVP---ALVSLWLDAAASRRADLSSLRLLQVGGARLSPALARRVPPVLGCTLQ 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 335 VVgYGLSEmgGL--SKNVGGP----VGCEGKVM-RNVELRVLDKLKMPLGINEVGIIYARLRFKWAGYYRNPEATRRALS 407
Cdd:cd05920 285 QV-FGMAE--GLlnYTRLDDPdeviIHTQGRPMsPDDEIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFT 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 408 SDGmWFRTGDIGYLDSEGYLYIQTRDTDVFKFNNFQIYPEQIEEFILRLPGVSEACVFGIPDAVSTNlTACAVVrtkSPE 487
Cdd:cd05920 362 PDG-FYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGE-RSCAFV---VLR 436
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 19922652 488 GERLTADHIRNIVEHHLSGAYHIRGGVYFIDSLPKTPNDKLQRR 531
Cdd:cd05920 437 DPPPSAAQLRRFLRERGLAAYKLPDRIEFVDSLPLTAVGKIDKK 480
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
42-531 |
5.09e-37 |
|
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: 143.25 E-value: 5.09e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 42 DQVMQICDttGQELTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNSTYLTSVIIAALLRGIPINPLHPEFTEETVKYM 121
Cdd:cd17651 10 DAPALVAE--GRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERLAFM 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 122 YDITEPKVIfcdvenyhiiktvngkLQNPAkiylVNGKLEGVLDISEMLNDEDSITAAAYVPCPKLHGDHTAFIVCSSGT 201
Cdd:cd17651 88 LADAGPVLV----------------LTHPA----LAGELAVELVAVTLLDQPGAAAGADAEPDPALDADDLAYVIYTSGS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 202 TGMPKGVTRSHRSLLCNCKNPNTY---TRDSVLLSFSPLYW-ISGTIILLASLLNGCRRIITN--RPySVEYLLQLVARH 275
Cdd:cd17651 148 TGRPKGVVMPHRSLANLVAWQARAsslGPGARTLQFAGLGFdVSVQEIFSTLCAGATLVLPPEevRT-DPPALAAWLDEQ 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 276 KVTFLFL---ASHQIALLSKHDSdvmelkAQLQSIRVLIGAGSK-VCKAVCRRMYELIGNQRFVVGYGLSEM-----GGL 346
Cdd:cd17651 227 RISRVFLptvALRALAEHGRPLG------VRLAALRYLLTGGEQlVLTEDLREFCAGLPGLRLHNHYGPTEThvvtaLSL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 347 SKNVGG-----PVgceGKVMRNVELRVLDKLKMPLGINEVGIIY------ARlrfkwaGYYRNPEATRRALSSD-----G 410
Cdd:cd17651 301 PGDPAAwpappPI---GRPIDNTRVYVLDAALRPVPPGVPGELYiggaglAR------GYLNRPELTAERFVPDpfvpgA 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 411 MWFRTGDIGYLDSEGYL-YIQTRDTDVfKFNNFQIYPEQIEEFILRLPGVSEACVFGIPDAVST-NLTACAVVRtkspEG 488
Cdd:cd17651 372 RMYRTGDLARWLPDGELeFLGRADDQV-KIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEkRLVAYVVGD----PE 446
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 19922652 489 ERLTADHIRNIVEHHLSgAYHIRGGVYFIDSLPKTPNDKLQRR 531
Cdd:cd17651 447 APVDAAELRAALATHLP-EYMVPSAFVLLDALPLTPNGKLDRR 488
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
38-532 |
7.01e-37 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 143.29 E-value: 7.01e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 38 QINADQVMQICDTTGQELTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNSTYLTSVIIAALLRGIPINPLHPEFTEET 117
Cdd:PRK13391 8 QTTPDKPAVIMASTGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 118 VKYMYDITEPKVIFCDVENYHIIKTVNGKLQN--PAKIYLVNGKLEGVLDISEML--------NDEDSITAAAYvpcpkl 187
Cdd:PRK13391 88 AAYIVDDSGARALITSAAKLDVARALLKQCPGvrHRLVLDGDGELEGFVGYAEAVaglpatpiADESLGTDMLY------ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 188 hgdhtafivcSSGTTGMPKGVTR--------SHRSLLCNCKNPNTYTRDSVLLSFSPLY-----WISGTIILLasllnGC 254
Cdd:PRK13391 162 ----------SSGTTGRPKGIKRplpeqppdTPLPLTAFLQRLWGFRSDMVYLSPAPLYhsapqRAVMLVIRL-----GG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 255 RRIITNRpYSVEYLLQLVARHKVTFLFLASHQIALLSKHDSDVmELKAQLQSIRVLIGAGSKVCKAVCRRMYELIGNqrf 334
Cdd:PRK13391 227 TVIVMEH-FDAEQYLALIEEYGVTHTQLVPTMFSRMLKLPEEV-RDKYDLSSLEVAIHAAAPCPPQVKEQMIDWWGP--- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 335 VVG--YGLSEMGGLS-----KNVGGPvGCEGKVMRNVeLRVLDKLKMPLGINEVGIIYarlrfkWAG-----YYRNPEAT 402
Cdd:PRK13391 302 IIHeyYAATEGLGFTacdseEWLAHP-GTVGRAMFGD-LHILDDDGAELPPGEPGTIW------FEGgrpfeYLNDPAKT 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 403 RRALSSDGMWFRTGDIGYLDSEGYLYIQTRDTDVFKFNNFQIYPEQIEEFILRLPGVSEACVFGIPD-----AVStnlta 477
Cdd:PRK13391 374 AEARHPDGTWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNedlgeEVK----- 448
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 19922652 478 cAVVRTKSP-EGERLTADHIRNIVEHHLSGaYHIRGGVYFIDSLPKTPNDKLQRRK 532
Cdd:PRK13391 449 -AVVQPVDGvDPGPALAAELIAFCRQRLSR-QKCPRSIDFEDELPRLPTGKLYKRL 502
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
53-532 |
9.95e-37 |
|
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: 141.45 E-value: 9.95e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 53 QELTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNSTYLTSVIIAALLRGIPINPLHPEFTEETVKYMYDITEPKVIFc 132
Cdd:cd05919 9 RSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVV- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 133 dvenyhiiktvngklqnpakiylvngklegvldisemlndedsitaaayvpcpkLHGDHTAFIVCSSGTTGMPKGVTRSH 212
Cdd:cd05919 88 ------------------------------------------------------TSADDIAYLLYSSGTTGPPKGVMHAH 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 213 RSLLCNC----KNPNTYTRDSVLLSFSPLYWISGT-IILLASLLNGCRRIITNRPYSVEYLLQLVARHKVTFLFLASHQI 287
Cdd:cd05919 114 RDPLLFAdamaREALGLTPGDRVFSSAKMFFGYGLgNSLWFPLAVGASAVLNPGWPTAERVLATLARFRPTVLYGVPTFY 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 288 A--LLSKHDSdvmelKAQLQSIRVLIGAGSKVCKAVCRRMYELIGNQrFVVGYGLSEMGG--LSKNVGG-PVGCEGKVMR 362
Cdd:cd05919 194 AnlLDSCAGS-----PDALRSLRLCVSAGEALPRGLGERWMEHFGGP-ILDGIGATEVGHifLSNRPGAwRLGSTGRPVP 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 363 NVELRVLDKLKMPLGINEVGIIYARLRFKWAGYYRNPEATRRALSsdGMWFRTGDIGYLDSEGYLYIQTRDTDVFKFNNF 442
Cdd:cd05919 268 GYEIRLVDEEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATFN--GGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQ 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 443 QIYPEQIEEFILRLPGVSEACVFGIPDAVS-TNLTACAVVRTKSPEGERLtADHIRNIVEHHLSgAYHIRGGVYFIDSLP 521
Cdd:cd05919 346 WVSPVEVESLIIQHPAVAEAAVVAVPESTGlSRLTAFVVLKSPAAPQESL-ARDIHRHLLERLS-AHKVPRRIAFVDELP 423
|
490
....*....|.
gi 19922652 522 KTPNDKLQRRK 532
Cdd:cd05919 424 RTATGKLQRFK 434
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
192-530 |
1.80e-36 |
|
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: 138.40 E-value: 1.80e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 192 TAFIVCSSGTTGMPKGVTRSHRSLL------CNCKNpntYTRDSVLLSFSPLYWISGTII-LLASLLNGCRrIITNRPYS 264
Cdd:cd17638 2 VSDIMFTSGTTGRSKGVMCAHRQTLraaaawADCAD---LTEDDRYLIINPFFHTFGYKAgIVACLLTGAT-VVPVAVFD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 265 VEYLLQLVARHKVTFL------FLAshqiaLLSKHDSDvmelKAQLQSIRVLIGAGSKVCKAVCRRMYELIGNQRFVVGY 338
Cdd:cd17638 78 VDAILEAIERERITVLpgpptlFQS-----LLDHPGRK----KFDLSSLRAAVTGAATVPVELVRRMRSELGFETVLTAY 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 339 GLSE--MGGLSKNVGGPVGCE---GKVMRNVELRVLDKlkmplginevGIIYARLRFKWAGYYRNPEATRRALSSDGmWF 413
Cdd:cd17638 149 GLTEagVATMCRPGDDAETVAttcGRACPGFEVRIADD----------GEVLVRGYNVMQGYLDDPEATAEAIDADG-WL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 414 RTGDIGYLDSEGYLYIQTRDTDVFKFNNFQIYPEQIEEFILRLPGVSEACVFGIPDAvSTNLTACAVVRTKSPEGerLTA 493
Cdd:cd17638 218 HTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDE-RMGEVGKAFVVARPGVT--LTE 294
|
330 340 350
....*....|....*....|....*....|....*..
gi 19922652 494 DHIRNIVEHHLSGaYHIRGGVYFIDSLPKTPNDKLQR 530
Cdd:cd17638 295 EDVIAWCRERLAN-YKVPRFVRFLDELPRNASGKVMK 330
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
52-545 |
2.30e-36 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 142.48 E-value: 2.30e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 52 GQELTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNSTYLTSVIIAALLRGIPINPLHPEFTEETVKYMYDITEPKVIF 131
Cdd:PRK06710 47 GKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVIL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 132 C---------DVENY----HIIKT-VNGKLQNPAKI---YLVNGKLEGVLDISE-----MLND-EDSITAAAYVPC-PKl 187
Cdd:PRK06710 127 CldlvfprvtNVQSAtkieHVIVTrIADFLPFPKNLlypFVQKKQSNLVVKVSEsetihLWNSvEKEVNTGVEVPCdPE- 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 188 hgDHTAFIVCSSGTTGMPKGVTRSHRSLLCNCKNP-----NTYTRDSVLLSFSPLYWISG-TIILLASLLNGCRRIITNR 261
Cdd:PRK06710 206 --NDLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGvqwlyNCKEGEEVVLGVLPFFHVYGmTAVMNLSIMQGYKMVLIPK 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 262 pYSVEYLLQLVARHKVTF------LFLASHQIALLSKHDsdvmelkaqLQSIRVLIgAGSKVCKAVCRRMYELIGNQRFV 335
Cdd:PRK06710 284 -FDMKMVFEAIKKHKVTLfpgaptIYIALLNSPLLKEYD---------ISSIRACI-SGSAPLPVEVQEKFETVTGGKLV 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 336 VGYGLSEMGGLS-------KNVGGPVGCEGKvmrNVELRVLD-KLKMPLGINEVGIIYARLRFKWAGYYRNPEATRrALS 407
Cdd:PRK06710 353 EGYGLTESSPVThsnflweKRVPGSIGVPWP---DTEAMIMSlETGEALPPGEIGEIVVKGPQIMKGYWNKPEETA-AVL 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 408 SDGmWFRTGDIGYLDSEGYLYIQTRDTDVFKFNNFQIYPEQIEEFILRLPGVSEACVFGIPDAVSTNLTACAVVRTkspE 487
Cdd:PRK06710 429 QDG-WLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVLK---E 504
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 19922652 488 GERLTADHIRNIVEHHLSgAYHIRGGVYFIDSLPKTPNDKLQRRkvlGLVQQLELKAE 545
Cdd:PRK06710 505 GTECSEEELNQFARKYLA-AYKVPKVYEFRDELPKTTVGKILRR---VLIEEEKRKNE 558
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
181-531 |
7.87e-36 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 140.96 E-value: 7.87e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 181 YVPcPKLHGDHTAFIVCSSGTTGMPKGVTRSHRSLLCN---CK---NPNTYTRDSVLLSFSPLYWISGTII--LLASLLN 252
Cdd:PRK08974 198 YVK-PELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANleqAKaayGPLLHPGKELVVTALPLYHIFALTVncLLFIELG 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 253 GCRRIITNrPYSVEYLLQLVARHKVT------FLFlashqIALLskHDSDVMELkaQLQSIRVLIGAGSKVCKAVCRRMY 326
Cdd:PRK08974 277 GQNLLITN-PRDIPGFVKELKKYPFTaitgvnTLF-----NALL--NNEEFQEL--DFSSLKLSVGGGMAVQQAVAERWV 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 327 ELIGnQRFVVGYGLSEMGGL----SKNVGGPVGCEGKVMRNVELRVLDKLKMPLGINEVGIIYARLRFKWAGYYRNPEAT 402
Cdd:PRK08974 347 KLTG-QYLLEGYGLTECSPLvsvnPYDLDYYSGSIGLPVPSTEIKLVDDDGNEVPPGEPGELWVKGPQVMLGYWQRPEAT 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 403 RRALSsDGmWFRTGDIGYLDSEGYLYIQTRDTDVFKFNNFQIYPEQIEEFILRLPGVSEACVFGIPDAVSTNLTACAVVR 482
Cdd:PRK08974 426 DEVIK-DG-WLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAVKIFVVK 503
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 19922652 483 tkspEGERLTADHIRNIVEHHLSGaYHIRGGVYFIDSLPKTPNDKLQRR 531
Cdd:PRK08974 504 ----KDPSLTEEELITHCRRHLTG-YKVPKLVEFRDELPKSNVGKILRR 547
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
28-531 |
8.04e-36 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 140.93 E-value: 8.04e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 28 TLGEVIMRVLQINADQVMQICdtTGQELTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNsTYLTSVIIAALLRG---- 103
Cdd:PRK07059 24 SLADLLEESFRQYADRPAFIC--MGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPN-VLQYPVAIAAVLRAgyvv 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 104 IPINPLhpeFTEETVKYMYDITEPKVIFCdVENY--------------HIIKTVNGKLQNPaKIYLVN------GKLEGV 163
Cdd:PRK07059 101 VNVNPL---YTPRELEHQLKDSGAEAIVV-LENFattvqqvlaktavkHVVVASMGDLLGF-KGHIVNfvvrrvKKMVPA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 164 LDISEMLNDEDSITAAA---YVPcPKLHGDHTAFIVCSSGTTGMPKGVTRSHRSLLCNCK------NP--NTYTRDSVLL 232
Cdd:PRK07059 176 WSLPGHVRFNDALAEGArqtFKP-VKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVLqmeawlQPafEKKPRPDQLN 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 233 SFS--PLYWISG-TIILLASLLNGCRRIITNRPYSVEYLLQLVARHKV-TFLFLASHQIALLSKHDSDvmelKAQLQSIR 308
Cdd:PRK07059 255 FVCalPLYHIFAlTVCGLLGMRTGGRNILIPNPRDIPGFIKELKKYQVhIFPAVNTLYNALLNNPDFD----KLDFSKLI 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 309 VLIGAGSKVCKAVCRRMYELIGNQrFVVGYGLSEMGglsknvggPV------------GCEGKVMRNVELRVLDKL--KM 374
Cdd:PRK07059 331 VANGGGMAVQRPVAERWLEMTGCP-ITEGYGLSETS--------PVatcnpvdatefsGTIGLPLPSTEVSIRDDDgnDL 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 375 PLGinEVGIIYARLRFKWAGYYRNPEATRRALSSDGmWFRTGDIGYLDSEGYLYIQTRDTDVFKFNNFQIYPEQIEEFIL 454
Cdd:PRK07059 402 PLG--EPGEICIRGPQVMAGYWNRPDETAKVMTADG-FFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVA 478
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19922652 455 RLPGVSEACVFGIPDAVSTNLTACAVVRtKSPEgerLTADHIRNIVEHHLSGaYHIRGGVYFIDSLPKTPNDKLQRR 531
Cdd:PRK07059 479 SHPGVLEVAAVGVPDEHSGEAVKLFVVK-KDPA---LTEEDVKAFCKERLTN-YKRPKFVEFRTELPKTNVGKILRR 550
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
52-465 |
9.20e-36 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341240 [Multi-domain] Cd Length: 463 Bit Score: 139.11 E-value: 9.20e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 52 GQELTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNSTYLTSVIIAALLRGIPINPLHPEFTEETVKYMYDITEPKVIF 131
Cdd:cd05914 5 GEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 132 CdvenyhiiktvngklqnpakiylvngklegvldisemlNDEDSitaaayvpcpklhgdhTAFIVCSSGTTGMPKGVTRS 211
Cdd:cd05914 85 V--------------------------------------SDEDD----------------VALINYTSGTTGNSKGVMLT 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 212 HRSLLCN---CKNPNTYTRDSVLLSFSPLYWISG-TIILLASLLNGCR----------------------RIITNRPYSV 265
Cdd:cd05914 111 YRNIVSNvdgVKEVVLLGKGDKILSILPLHHIYPlTFTLLLPLLNGAHvvfldkipsakiialafaqvtpTLGVPVPLVI 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 266 EYLLQLVARHKVT---FLFLASHQIALLSKHDsdvMELKAQLQS----IRVLIGAGSKVCKAVCRRMYELigNQRFVVGY 338
Cdd:cd05914 191 EKIFKMDIIPKLTlkkFKFKLAKKINNRKIRK---LAFKKVHEAfggnIKEFVIGGAKINPDVEEFLRTI--GFPYTIGY 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 339 GLSEMGGL-SKNVGGPV--GCEGKVMRNVELRVLDklkmPLGINEVGIIYARLRFKWAGYYRNPEATRRALSSDGmWFRT 415
Cdd:cd05914 266 GMTETAPIiSYSPPNRIrlGSAGKVIDGVEVRIDS----PDPATGEGEIIVRGPNVMKGYYKNPEATAEAFDKDG-WFHT 340
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 19922652 416 GDIGYLDSEGYLYIQTRDTDVFKFNNFQ-IYPEQIEEFILRLPGVSEACVF 465
Cdd:cd05914 341 GDLGKIDAEGYLYIRGRKKEMIVLSSGKnIYPEEIEAKINNMPFVLESLVV 391
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
191-530 |
3.31e-35 |
|
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: 134.70 E-value: 3.31e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 191 HTAFIvcssgtTGMPKGVTRSHRSLLC-NCKNPNTY--TRDSVLLSFSPLYWISGTIILLASLLNGCRRIITNRpYSVEY 267
Cdd:cd17637 7 HTAAV------AGRPRGAVLSHGNLIAaNLQLIHAMglTEADVYLNMLPLFHIAGLNLALATFHAGGANVVMEK-FDPAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 268 LLQLVARHKVTFLF-----LAShqiaLLSKHDSDvmelKAQLQSIRVLIGAGSKvckAVCRRmYELIGNQRFVVGYGLSE 342
Cdd:cd17637 80 ALELIEEEKVTLMGsfppiLSN----LLDAAEKS----GVDLSSLRHVLGLDAP---ETIQR-FEETTGATFWSLYGQTE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 343 MGGLSknVGGPV----GCEGKVMRNVELRVLDKLKMPLGINEVGIIYAR--LRFKwaGYYRNPEATRRALssDGMWFRTG 416
Cdd:cd17637 148 TSGLV--TLSPYrerpGSAGRPGPLVRVRIVDDNDRPVPAGETGEIVVRgpLVFQ--GYWNLPELTAYTF--RNGWHHTG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 417 DIGYLDSEGYLYIQTR--DTDVFKFNNFQIYPEQIEEFILRLPGVSEACVFGIPD-----AVStnltacAVVRTKspEGE 489
Cdd:cd17637 222 DLGRFDEDGYLWYAGRkpEKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDpkwgeGIK------AVCVLK--PGA 293
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 19922652 490 RLTADHIRNIVEHHLSGaYHIRGGVYFIDSLPKTPNDKLQR 530
Cdd:cd17637 294 TLTADELIEFVGSRIAR-YKKPRYVVFVEALPKTADGSIDR 333
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
55-533 |
5.84e-35 |
|
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ligase, 4-hydroxybenzoate-CoA ligase, 2-aminobenzoate-CoA ligase, etc. Members are related to fatty acid and acetate CoA ligases.
Pssm-ID: 274059 [Multi-domain] Cd Length: 505 Bit Score: 137.66 E-value: 5.84e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 55 LTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNSTYLTSVIIAALLRGIPINPLHPEFTEETVKYMYDITEPKVIFCDV 134
Cdd:TIGR02262 31 LSYGELEAQVRRLAAALRRLGVKREERVLLLMLDGVDFPIAFLGAIRAGIVPVALNTLLTADDYAYMLEDSRARVVFVSG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 135 ENYHIIKTVNGKLQNPAKIYLVNGKLEGVLDISEMLNDE-DSITAAAyvpcpkLHGDHTAFIVCSSGTTGMPKGVTRSHR 213
Cdd:TIGR02262 111 ALLPVIKAALGKSPHLEHRVVVGRPEAGEVQLAELLATEsEQFKPAA------TQADDPAFWLYSSGSTGMPKGVVHTHS 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 214 SLLCNCKNPNT----YTRDSVLLSFSPLYWISG--------TIILLASLLNGcrriitNRPySVEYLLQLVARHKVTFLF 281
Cdd:TIGR02262 185 NPYWTAELYARntlgIREDDVCFSAAKLFFAYGlgnaltfpMSVGATTVLMG------ERP-TPDAVFDRLRRHQPTIFY 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 282 LASHQIA-LLSKHDSDvmelKAQLQSIRVLIGAGSKVCKAVCRRMYELIGNQrFVVGYGLSEMGGLS-KNVGGPV--GCE 357
Cdd:TIGR02262 258 GVPTLYAaMLADPNLP----SEDQVRLRLCTSAGEALPAEVGQRWQARFGVD-IVDGIGSTEMLHIFlSNLPGDVryGTS 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 358 GKVMRNVELRVLDKLKMPLGINEVGIIYARLRFKWAGYYRNPEATRRALssDGMWFRTGDIGYLDSEGYLYIQTRDTDVF 437
Cdd:TIGR02262 333 GKPVPGYRLRLVGDGGQDVADGEPGELLISGPSSATMYWNNRAKSRDTF--QGEWTRSGDKYVRNDDGSYTYAGRTDDML 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 438 KFNNFQIYPEQIEEFILRLPGVSEACVFGIPDAVS-TNLTACAVVRTKSPEGERLTADHIRNIVehhlsGAYHIRGGVYF 516
Cdd:TIGR02262 411 KVSGIYVSPFEIESALIQHPAVLEAAVVGVADEDGlIKPKAFVVLRPGQTALETELKEHVKDRL-----APYKYPRWIVF 485
|
490
....*....|....*..
gi 19922652 517 IDSLPKTPNDKLQRRKV 533
Cdd:TIGR02262 486 VDDLPKTATGKIQRFKL 502
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
28-541 |
1.06e-34 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 137.41 E-value: 1.06e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 28 TLGEVIMRVLQINADQVMQICDTTGQE--LTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNSTYLTSVIIAALLRGIP 105
Cdd:cd05906 11 TLLELLLRAAERGPTKGITYIDADGSEefQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 106 INPLhpefteeTVKYMYDITEPKVifcdVENYHIIKTVNGK--LQNPAKI--YLVNGKLEGVLDISEMLNDEDSITAAAY 181
Cdd:cd05906 91 PAPL-------TVPPTYDEPNARL----RKLRHIWQLLGSPvvLTDAELVaeFAGLETLSGLPGIRVLSIEELLDTAADH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 182 vPCPKLHGDHTAFIVCSSGTTGMPKGVTRSHRSLLCNCKNPNT---YTRDSVLLSFSPLYWISGTIIL-LASLLNGCRRI 257
Cdd:cd05906 160 -DLPQSRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQhngLTPQDVFLNWVPLDHVGGLVELhLRAVYLGCQQV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 258 ------ITNRPYSveyLLQLVARHKVTFLFLASHQIALLSKHDSDVMELKAQLQSIRVLIGAGSKVCKAVCRRMYELI-- 329
Cdd:cd05906 239 hvpteeILADPLR---WLDLIDRYRVTITWAPNFAFALLNDLLEEIEDGTWDLSSLRYLVNAGEAVVAKTIRRLLRLLep 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 330 -GNQRFVV--GYGLSEMG-GLSKNVGGPVG---------CEGKVMRNVELRVLDKLKMPLGINEVGIIYARLRFKWAGYY 396
Cdd:cd05906 316 yGLPPDAIrpAFGMTETCsGVIYSRSFPTYdhsqalefvSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYY 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 397 RNPEATRRALSSDGmWFRTGDIGYLDsEGYLYIQTRDTDVFKFNNFQIYPEQIEEFILRLPGV--SEACVFGIPDA-VST 473
Cdd:cd05906 396 NNPEANAEAFTEDG-WFRTGDLGFLD-NGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVepSFTAAFAVRDPgAET 473
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19922652 474 NLTACAVVRTKSPEGERL-TADHIRNIVEHHLSGAYHirggvYFI----DSLPKTPNDKLQRRKvlgLVQQLE 541
Cdd:cd05906 474 EELAIFFVPEYDLQDALSeTLRAIRSVVSREVGVSPA-----YLIplpkEEIPKTSLGKIQRSK---LKAAFE 538
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
52-532 |
2.21e-34 |
|
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: 138.84 E-value: 2.21e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 52 GQELTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNSTYLTSVIIAALLRG---IPINPLHPEfteETVKYMYDITEPK 128
Cdd:COG1020 499 DQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGaayVPLDPAYPA---ERLAYMLEDAGAR 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 129 VIfcdvenyhiiktvngklqnpakiyLVNGKLEGVLDISEM----LNDEDSITAAAYVPCPKLHGDHTAFIVCSSGTTGM 204
Cdd:COG1020 576 LV------------------------LTQSALAARLPELGVpvlaLDALALAAEPATNPPVPVTPDDLAYVIYTSGSTGR 631
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 205 PKGVTRSHRSLLCNCKNPNTY---TRDSVLLSFSPLYW-ISGTIILLAsLLNGCRRIITNR--PYSVEYLLQLVARHKVT 278
Cdd:COG1020 632 PKGVMVEHRALVNLLAWMQRRyglGPGDRVLQFASLSFdASVWEIFGA-LLSGATLVLAPPeaRRDPAALAELLARHRVT 710
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 279 FLFL-ASHqIALLskhdsdVMELKAQLQSIRVLIGAGSKVCKAVCRRMYELIGNQRFVVGYGLSE----------MGGLS 347
Cdd:COG1020 711 VLNLtPSL-LRAL------LDAAPEALPSLRLVLVGGEALPPELVRRWRARLPGARLVNLYGPTEttvdstyyevTPPDA 783
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 348 KNVGGPVgceGKVMRNVELRVLDKLKMPLGINEVGIIY------ARlrfkwaGYYRNPEATRRA-----LSSDGM-WFRT 415
Cdd:COG1020 784 DGGSVPI---GRPIANTRVYVLDAHLQPVPVGVPGELYiggaglAR------GYLNRPELTAERfvadpFGFPGArLYRT 854
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 416 GDIGYLDSEGYL-YIQTRDTDVfKFNNFQIYPEQIEEFILRLPGVSEACVFGIPDAVSTNLTACAVVrtksPEGERLTAD 494
Cdd:COG1020 855 GDLARWLPDGNLeFLGRADDQV-KIRGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVV----PEAGAAAAA 929
|
490 500 510
....*....|....*....|....*....|....*...
gi 19922652 495 HIRNIVEHHLSGAYHIRGGVYFIDSLPKTPNDKLQRRK 532
Cdd:COG1020 930 ALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLA 967
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
55-532 |
2.28e-33 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 133.78 E-value: 2.28e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 55 LTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNST------YLTSVIIAALLRgipINPLHPefTEEtVKYMYDITEPK 128
Cdd:PRK08315 44 WTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPewvltqFATAKIGAILVT---INPAYR--LSE-LEYALNQSGCK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 129 VIFC-----DVeNYH-IIKTV--------NGKLQNPAK------IYLVNGKLEGVLDISEMLNDEDSITAAAYVPC-PKL 187
Cdd:PRK08315 118 ALIAadgfkDS-DYVaMLYELapelatcePGQLQSARLpelrrvIFLGDEKHPGMLNFDELLALGRAVDDAELAARqATL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 188 HGDHTAFIVCSSGTTGMPKGVTRSHRSLLCN------CKNpntYT-RDSVLLSFsPLYWISGTII-LLASLLNGCRRIIT 259
Cdd:PRK08315 197 DPDDPINIQYTSGTTGFPKGATLTHRNILNNgyfigeAMK---LTeEDRLCIPV-PLYHCFGMVLgNLACVTHGATMVYP 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 260 NRPYSVEYLLQLVARHKVTFL------FLASHQIALLSKHDsdvmelkaqLQSIRVLIGAGS----KVCKAVCRRMY--E 327
Cdd:PRK08315 273 GEGFDPLATLAAVEEERCTALygvptmFIAELDHPDFARFD---------LSSLRTGIMAGSpcpiEVMKRVIDKMHmsE 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 328 LignqrfVVGYGLSEmgglsknvGGPVGCE--------------GKVMRNVELRVLDKLK-MPLGINEVGIIYARLRFKW 392
Cdd:PRK08315 344 V------TIAYGMTE--------TSPVSTQtrtddplekrvttvGRALPHLEVKIVDPETgETVPRGEQGELCTRGYSVM 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 393 AGYYRNPEATRRALSSDGmWFRTGDIGYLDSEGYLYIQTRDTDVFKFNNFQIYPEQIEEFILRLPGVSEACVFGIPDA-- 470
Cdd:PRK08315 410 KGYWNDPEKTAEAIDADG-WMHTGDLAVMDEEGYVNIVGRIKDMIIRGGENIYPREIEEFLYTHPKIQDVQVVGVPDEky 488
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19922652 471 ---VstnltaCAVVRTKspEGERLTADHIRniveHHLSG--AY-----HIRggvyFIDSLPKTPNDKLQRRK 532
Cdd:PRK08315 489 geeV------CAWIILR--PGATLTEEDVR----DFCRGkiAHykiprYIR----FVDEFPMTVTGKIQKFK 544
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
50-531 |
4.75e-33 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 133.04 E-value: 4.75e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 50 TTGQELTGAQLAQQSARIAQAF-KRLGLRRGDVVGISANNSTYLTSVIIAALLRGIPINPLHPEFTEETVKYMYDITEPK 128
Cdd:PLN02574 62 STGFSISYSELQPLVKSMAAGLyHVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVG 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 129 VIFCDVENYhiiktvnGKLQN--------PAKIYLVNGKLEGVLDISEMLNDEDsitaaaYVPCPKLHGDHTAFIVCSSG 200
Cdd:PLN02574 142 LAFTSPENV-------EKLSPlgvpvigvPENYDFDSKRIEFPKFYELIKEDFD------FVPKPVIKQDDVAAIMYSSG 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 201 TTGMPKGVTRSHRSLLCNCK-----------NPNTytrDSVLLSFSPLYWISGTIILLASLLNGCRRIITNRPYSVEYLL 269
Cdd:PLN02574 209 TTGASKGVVLTHRNLIAMVElfvrfeasqyeYPGS---DNVYLAALPMFHIYGLSLFVVGLLSLGSTIVVMRRFDASDMV 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 270 QLVARHKVTFLFLASHQIALLSKHDSDV--MELKAQLQsirVLIGAGSKVCKAVcRRMYELIGNQRFVVGYGLSEMG--- 344
Cdd:PLN02574 286 KVIDRFKVTHFPVVPPILMALTKKAKGVcgEVLKSLKQ---VSCGAAPLSGKFI-QDFVQTLPHVDFIQGYGMTESTavg 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 345 --GLSKNVGGPVGCEGKVMRNVELRVLDKLK---MPLGinEVGIIYARLRFKWAGYYRNPEATRRALSSDGmWFRTGDIG 419
Cdd:PLN02574 362 trGFNTEKLSKYSSVGLLAPNMQAKVVDWSTgclLPPG--NCGELWIQGPGVMKGYLNNPKATQSTIDKDG-WLRTGDIA 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 420 YLDSEGYLYIQTRDTDVFKFNNFQIYPEQIEEFILRLPGVSEACVFGIPDAVSTNLTACAVVRTkspEGERLTADHIRNI 499
Cdd:PLN02574 439 YFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRR---QGSTLSQEAVINY 515
|
490 500 510
....*....|....*....|....*....|..
gi 19922652 500 VEHHLSGAYHIRgGVYFIDSLPKTPNDKLQRR 531
Cdd:PLN02574 516 VAKQVAPYKKVR-KVVFVQSIPKSPAGKILRR 546
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
42-531 |
5.11e-33 |
|
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341304 [Multi-domain] Cd Length: 450 Bit Score: 131.34 E-value: 5.11e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 42 DQVMQICDttGQELTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNSTYLTSVIIAALLRGIPINPLHPEFTEETVKYM 121
Cdd:cd17649 2 DAVALVFG--DQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 122 YditepkvifcdvenyhiiktvngklqnpakiylvngklegvldisemlndEDSitAAAYVPCPklHGDHTAFIVCSSGT 201
Cdd:cd17649 80 L--------------------------------------------------EDS--GAGLLLTH--HPRQLAYVIYTSGS 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 202 TGMPKGVTRSHRSLLCNCKNPNTYTR---DSVLLSFSPLYWISGTIILLASLLNGCRRIITNRP--YSVEYLLQLVARHK 276
Cdd:cd17649 106 TGTPKGVAVSHGPLAAHCQATAERYGltpGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDElwASADELAEMVRELG 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 277 VTFLFLAS---HQIALLSKHDSDVMELkaqlqSIRVLIGAGSKVCKAVCRRMyeLIGNQRFVVGYGLSEmGGLSKNV--- 350
Cdd:cd17649 186 VTVLDLPPaylQQLAEEADRTGDGRPP-----SLRLYIFGGEALSPELLRRW--LKAPVRLFNAYGPTE-ATVTPLVwkc 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 351 ------GGPVGCEGKVMRNVELRVLDKLKMPLGINEVGIIY------ARlrfkwaGYYRNPEATRRALSSD------GMW 412
Cdd:cd17649 258 eagaarAGASMPIGRPLGGRSAYILDADLNPVPVGVTGELYiggeglAR------GYLGRPELTAERFVPDpfgapgSRL 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 413 FRTGDIG-YLDSEGYLYIQTRDTDVfKFNNFQIYPEQIEEFILRLPGVSEACVFGIPDAVSTNLTACAVVRtkspEGERL 491
Cdd:cd17649 332 YRTGDLArWRDDGVIEYLGRVDHQV-KIRGFRIELGEIEAALLEHPGVREAAVVALDGAGGKQLVAYVVLR----AAAAQ 406
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 19922652 492 TAD--HIRNIVEHHLSgAYHIRGGVYFIDSLPKTPNDKLQRR 531
Cdd:cd17649 407 PELraQLRTALRASLP-DYMVPAHLVFLARLPLTPNGKLDRK 447
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
38-533 |
7.44e-33 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 131.67 E-value: 7.44e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 38 QINADQVMQICDTTGQELTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNSTYLTSVIIAALLRGIPINPLHPEFTEET 117
Cdd:PRK13390 8 QIAPDRPAVIVAETGEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 118 VKYMYDITEPKVIFCDVENYHIIKTVNGKLqnPAKIYLvNGKLEGVLDIsemlndEDSITAA----AYVPCpklhgdhTA 193
Cdd:PRK13390 88 ADYIVGDSGARVLVASAALDGLAAKVGADL--PLRLSF-GGEIDGFGSF------EAALAGAgprlTEQPC-------GA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 194 FIVCSSGTTGMPKGVTRS--HRSL-------------LCNCKNPNTYTRDSVLLSFSPLYWISgtiilLASLLNGCrrII 258
Cdd:PRK13390 152 VMLYSSGTTGFPKGIQPDlpGRDVdapgdpivaiaraFYDISESDIYYSSAPIYHAAPLRWCS-----MVHALGGT--VV 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 259 TNRPYSVEYLLQLVARHKVTFLFLASHQIALLSKHDSDVMElKAQLQSIRVLIGAGSKVCKAVCRRMYELIGNQRFVVgY 338
Cdd:PRK13390 225 LAKRFDAQATLGHVERYRITVTQMVPTMFVRLLKLDADVRT-RYDVSSLRAVIHAAAPCPVDVKHAMIDWLGPIVYEY-Y 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 339 GLSEMGGLSK-NVGGPVGCEGKVMRNV--ELRVLDKLKMPLGINEVGIIY---ARLRFKwagYYRNPEATRRAL-SSDGM 411
Cdd:PRK13390 303 SSTEAHGMTFiDSPDWLAHPGSVGRSVlgDLHICDDDGNELPAGRIGTVYferDRLPFR---YLNDPEKTAAAQhPAHPF 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 412 WFRTGDIGYLDSEGYLYIQTRDTDVFKFNNFQIYPEQIEEFILRLPGVSEACVFGIPD-----AVSTNLTACAVVRtKSP 486
Cdd:PRK13390 380 WTTVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDpemgeQVKAVIQLVEGIR-GSD 458
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 19922652 487 EGERLTADHIRNIVEHhlsgaYHIRGGVYFIDSLPKTPNDKLQRRKV 533
Cdd:PRK13390 459 ELARELIDYTRSRIAH-----YKAPRSVEFVDELPRTPTGKLVKGLL 500
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
193-533 |
7.58e-33 |
|
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: 128.22 E-value: 7.58e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 193 AFIVCSSGTTGMPKGVTRSHRSLLCN----CKNPNTYTRDSVLLSfSPLYWISGTIILLASLLNGCRRIITNRPYSveyL 268
Cdd:cd17630 3 ATVILTSGSTGTPKAVVHTAANLLASaaglHSRLGFGGGDSWLLS-LPLYHVGGLAILVRSLLAGAELVLLERNQA---L 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 269 LQLVARHKVTFLFLASHQiaLLSKHDSDvmELKAQLQSIR-VLIGaGSKVCKAVCRRMYELigNQRFVVGYGLSEMGGLS 347
Cdd:cd17630 79 AEDLAPPGVTHVSLVPTQ--LQRLLDSG--QGPAALKSLRaVLLG-GAPIPPELLERAADR--GIPLYTTYGMTETASQV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 348 --KNVGGPV-GCEGKVMRNVELRVLDKlkmplgiNEVGIIYARLRfkwAGYYRNPEatRRALSSDGmWFRTGDIGYLDSE 424
Cdd:cd17630 152 atKRPDGFGrGGVGVLLPGRELRIVED-------GEIWVGGASLA---MGYLRGQL--VPEFNEDG-WFTTKDLGELHAD 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 425 GYLYIQTRDTDVFKFNNFQIYPEQIEEFILRLPGVSEACVFGIPDA------VstnltacAVVRTKSPegerLTADHIRN 498
Cdd:cd17630 219 GRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEelgqrpV-------AVIVGRGP----ADPAELRA 287
|
330 340 350
....*....|....*....|....*....|....*
gi 19922652 499 IVEHHLSGaYHIRGGVYFIDSLPKTPNDKLQRRKV 533
Cdd:cd17630 288 WLKDKLAR-FKLPKRIYPVPELPRTGGGKVDRRAL 321
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
49-533 |
1.68e-32 |
|
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: 129.67 E-value: 1.68e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 49 DTTGQELTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNSTYLTSVIIAALLRGIPINPLHPEFTEETVKYMYDITEPK 128
Cdd:cd05945 11 VEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERIREILDAAKPA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 129 VIFCDvenyhiiktvngklqnpakiylvngklegvldisemlndedsitaaayvpcpklhGDHTAFIVCSSGTTGMPKGV 208
Cdd:cd05945 91 LLIAD-------------------------------------------------------GDDNAYIIFTSGSTGRPKGV 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 209 TRSHRSLLCncknpntYTR----------DSVLLSFSPLYWISGTIILLASLLNGCRRIITNRpysveyllQLVARHKVT 278
Cdd:cd05945 116 QISHDNLVS-------FTNwmlsdfplgpGDVFLNQAPFSFDLSVMDLYPALASGATLVPVPR--------DATADPKQL 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 279 FLFLASHQI----------ALLSKHDSDvmeLKAQLQSIRVLIGAGSKVCKAVCRRMYELIGNQRFVVGYGLSEMGG--- 345
Cdd:cd05945 181 FRFLAEHGItvwvstpsfaAMCLLSPTF---TPESLPSLRHFLFCGEVLPHKTARALQQRFPDARIYNTYGPTEATVavt 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 346 --------LSKNVGGPVGcegKVMRNVELRVLDKLKMPLGINEVGIIYAR--LRFKwaGYYRNPEATRRALSSDGM--WF 413
Cdd:cd05945 258 yievtpevLDGYDRLPIG---YAKPGAKLVILDEDGRPVPPGEKGELVISgpSVSK--GYLNNPEKTAAAFFPDEGqrAY 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 414 RTGDIGYLDSEGYLYIQTRDTDVFKFNNFQIYPEQIEEFILRLPGVSEACVfgIPDAVSTNLTACAVVRTKSPEGERLTA 493
Cdd:cd05945 333 RTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVV--VPKYKGEKVTELIAFVVPKPGAEAGLT 410
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 19922652 494 DHIRNIVEHHLSgAYHIRGGVYFIDSLPKTPNDKLQRRKV 533
Cdd:cd05945 411 KAIKAELAERLP-PYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
52-528 |
5.84e-32 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 129.51 E-value: 5.84e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 52 GQELTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNST-YLTSVIIAALLRGIPInPLHPEFTEETVKYMYDITEPKVI 130
Cdd:PRK07786 40 GNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTeFVESVLAANMLGAIAV-PVNFRLTPPEIAFLVSDCGAHVV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 131 FCDVENYHIIKTVNGKLQNPAKIYLVNGKLE-GVLDISEMLNDEDSITAAAYVPcpklhGDHTAFIVCSSGTTGMPKGVT 209
Cdd:PRK07786 119 VTEAALAPVATAVRDIVPLLSTVVVAGGSSDdSVLGYEDLLAEAGPAHAPVDIP-----NDSPALIMYTSGTTGRPKGAV 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 210 RSHRSLLCN---CKNPNTY-TRDSVLLSFSPLYWISGTIILLASLLNGCRRIItnRP---YSVEYLLQLVARHKVTFLFL 282
Cdd:PRK07786 194 LTHANLTGQamtCLRTNGAdINSDVGFVGVPLFHIAGIGSMLPGLLLGAPTVI--YPlgaFDPGQLLDVLEAEKVTGIFL 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 283 ASHQI-ALLSKHDSDVMELKaqlqsIRVLIGAGSKVCKAVCRRMYELIGNQRFVVGYGLSEMGG-----LSKNVGGPVGC 356
Cdd:PRK07786 272 VPAQWqAVCAEQQARPRDLA-----LRVLSWGAAPASDTLLRQMAATFPEAQILAAFGQTEMSPvtcmlLGEDAIRKLGS 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 357 EGKVMRNVELRVLDKLKMPLGINEVGIIYARLRFKWAGYYRNPEATRRALssDGMWFRTGDIGYLDSEGYLYIQTRDTDV 436
Cdd:PRK07786 347 VGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAF--AGGWFHSGDLVRQDEEGYVWVVDRKKDM 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 437 FKFNNFQIYPEQIEEFILRLPGVSEACVFGIPDAVSTNL-TACAVVRtksPEGERLTADHIRNIVEHHLSGAYHIRgGVY 515
Cdd:PRK07786 425 IISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVpVAVAAVR---NDDAALTLEDLAEFLTDRLARYKHPK-ALE 500
|
490
....*....|...
gi 19922652 516 FIDSLPKTPNDKL 528
Cdd:PRK07786 501 IVDALPRNPAGKV 513
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
17-528 |
7.24e-32 |
|
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: 129.62 E-value: 7.24e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 17 PRGKDFYGPEMTLG-EVIMRVLQINADQVMQICD----TTGQELTGAQLAQQSARIAQAFKRLGLRRGDVVGIsannstY 91
Cdd:cd17634 42 PSIKWFEDATLNLAaNALDRHLRENGDRTAIIYEgddtSQSRTISYRELHREVCRFAGTLLDLGVKKGDRVAI------Y 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 92 LTSV--IIAALLRGIPINPLHPE----FTEETVKYMYDITEPKVIFCDVENYHIIKTVNGK--------LQNPAKIYLVN 157
Cdd:cd17634 116 MPMIpeAAVAMLACARIGAVHSVifggFAPEAVAGRIIDSSSRLLITADGGVRAGRSVPLKknvddalnPNVTSVEHVIV 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 158 GKLEGV---------LDISEMLNDEdsitAAAYVPCPkLHGDHTAFIVCSSGTTGMPKGVTRSHRSLLCNCKNPNTYTRD 228
Cdd:cd17634 196 LKRTGSdidwqegrdLWWRDLIAKA----SPEHQPEA-MNAEDPLFILYTSGTTGKPKGVLHTTGGYLVYAATTMKYVFD 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 229 ----SVLLSFSPLYWISG-TIILLASLLNGCRRII----TNRPySVEYLLQLVARHKVTFLFLASHQIALLSKHDSDVME 299
Cdd:cd17634 271 ygpgDIYWCTADVGWVTGhSYLLYGPLACGATTLLyegvPNWP-TPARMWQVVDKHGVNILYTAPTAIRALMAAGDDAIE 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 300 lKAQLQSIRVLIGAGSKVCKAVCRRMYELIGNQRF-VVGY-GLSEMGG-----LSKNVGGPVGCEGKVMRNVELRVLDKL 372
Cdd:cd17634 350 -GTDRSSLRILGSVGEPINPEAYEWYWKKIGKEKCpVVDTwWQTETGGfmitpLPGAIELKAGSATRPVFGVQPAVVDNE 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 373 KMPLGINEVGIIYarLRFKW-----AGYYRNPEATRRALSS-DGMWFrTGDIGYLDSEGYLYIQTRDTDVFKFNNFQIYP 446
Cdd:cd17634 429 GHPQPGGTEGNLV--ITDPWpgqtrTLFGDHERFEQTYFSTfKGMYF-SGDGARRDEDGYYWITGRSDDVINVAGHRLGT 505
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 447 EQIEEFILRLPGVSEACVFGIPDAVSTNLTACAVVRTKSPEGERLTADHIRNIVEHHLsGAYHIRGGVYFIDSLPKTPND 526
Cdd:cd17634 506 AEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLNHGVEPSPELYAELRNWVRKEI-GPLATPDVVHWVDSLPKTRSG 584
|
..
gi 19922652 527 KL 528
Cdd:cd17634 585 KI 586
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
52-530 |
1.82e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 127.23 E-value: 1.82e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 52 GQELTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNSTYLTSVIIAALLRGIPINPLHPEFTEETVKYMYDITEPKVIF 131
Cdd:PRK09088 20 GRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 132 CDVEnyhiiktvngklqnpakiyLVNGKLEGVlDISEMLndeDSITAAAYVPCPKLHGDHTAFIVCSSGTTGMPKGVTRS 211
Cdd:PRK09088 100 GDDA-------------------VAAGRTDVE-DLAAFI---ASADALEPADTPSIPPERVSLILFTSGTSGQPKGVMLS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 212 HRSLLCNCKNPNTYTR---DSVLLSFSPLYWISGTIILLASLL---------NGCRRIITNRPYSVEYLlqlvarhKVTF 279
Cdd:PRK09088 157 ERNLQQTAHNFGVLGRvdaHSSFLCDAPMFHIIGLITSVRPVLavggsilvsNGFEPKRTLGRLGDPAL-------GITH 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 280 LFLASHQIALLSKH-DSDvmelKAQLQSIRVLIGAGSKvcKAVCRRMYELIGNQRFVVGYGLSEMG---GLSKNVG---G 352
Cdd:PRK09088 230 YFCVPQMAQAFRAQpGFD----AAALRHLTALFTGGAP--HAAEDILGWLDDGIPMVDGFGMSEAGtvfGMSVDCDvirA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 353 PVGCEGKVMRNVELRVLDKLKMPLGINEVGIIYARLRFKWAGYYRNPEATRRALSSDGmWFRTGDIGYLDSEGYLYIQTR 432
Cdd:PRK09088 304 KAGAAGIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFTGDG-WFRTGDIARRDADGFFWVVDR 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 433 DTDVFKFNNFQIYPEQIEEFILRLPGVSEACVFGIPDAVSTNLTACAVVrtkSPEGERLTADHIRNIVEHHLSGaYHIRG 512
Cdd:PRK09088 383 KKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIV---PADGAPLDLERIRSHLSTRLAK-YKVPK 458
|
490
....*....|....*...
gi 19922652 513 GVYFIDSLPKTPNDKLQR 530
Cdd:PRK09088 459 HLRLVDALPRTASGKLQK 476
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
191-530 |
3.08e-31 |
|
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: 123.28 E-value: 3.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 191 HTAFivcSSGTTGMPKGVTRSHRSLL----CNCKNPNTYTRDSVL----LSFS-PLY------WISGTIILLA--SLLNG 253
Cdd:cd17633 4 YIGF---TSGTTGLPKAYYRSERSWIesfvCNEDLFNISGEDAILapgpLSHSlFLYgaisalYLGGTFIGQRkfNPKSW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 254 CRRIitnrpysveyllqlvARHKVTFLFLASHQIALLSKHDSDVmelkaqlQSIRVLIGAGSKVCKAVCRRMYELIGNQR 333
Cdd:cd17633 81 IRKI---------------NQYNATVIYLVPTMLQALARTLEPE-------SKIKSIFSSGQKLFESTKKKLKNIFPKAN 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 334 FVVGYGLSEMGGLSKNVGG---PVGCEGKVMRNVELRVLDKlkmplGINEVGIIYARLRFKWAGYYRNpeatrRALSSDG 410
Cdd:cd17633 139 LIEFYGTSELSFITYNFNQesrPPNSVGRPFPNVEIEIRNA-----DGGEIGKIFVKSEMVFSGYVRG-----GFSNPDG 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 411 mWFRTGDIGYLDSEGYLYIQTRDTDVFKFNNFQIYPEQIEEFILRLPGVSEACVFGIPDAvSTNLTACAVVrtkspEGER 490
Cdd:cd17633 209 -WMSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDA-RFGEIAVALY-----SGDK 281
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 19922652 491 LTADHIRNIVEHHLSgAYHIRGGVYFIDSLPKTPNDKLQR 530
Cdd:cd17633 282 LTYKQLKRFLKQKLS-RYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
51-531 |
4.18e-31 |
|
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: 126.24 E-value: 4.18e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 51 TGQELTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNSTYLTSVIIAALLRGIPINPLHPEFTEETVKYMYDITEPKVI 130
Cdd:cd17646 20 EGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRLAYMLADAGPAVV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 131 FCDvenyhiiktvnGKLQNPAkiylvngkleGVLDISEMLNDEDSITAAAYVPCPKLHGDHTAFIVCSSGTTGMPKGVTR 210
Cdd:cd17646 100 LTT-----------ADLAARL----------PAGGDVALLGDEALAAPPATPPLVPPRPDNLAYVIYTSGSTGRPKGVMV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 211 SHRS----LLCNCKNPNTYTRDSVL----LSFSPLYWisgtiILLASLLNGCRRIITnRP---YSVEYLLQLVARHKVTF 279
Cdd:cd17646 159 THAGivnrLLWMQDEYPLGPGDRVLqktpLSFDVSVW-----ELFWPLVAGARLVVA-RPgghRDPAYLAALIREHGVTT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 280 L-FLASHQIALLSKHDSDvmelkaQLQSIRVLIGAGSKVCKAVCRRMYELIGnQRFVVGYGLSE--MGGLSKNVGGPVGC 356
Cdd:cd17646 233 ChFVPSMLRVFLAEPAAG------SCASLRRVFCSGEALPPELAARFLALPG-AELHNLYGPTEaaIDVTHWPVRGPAET 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 357 E----GKVMRNVELRVLDKLKMPLGINEVGIIY------ARlrfkwaGYYRNPEATRRALSSDgmWF-------RTGDIG 419
Cdd:cd17646 306 PsvpiGRPVPNTRLYVLDDALRPVPVGVPGELYlggvqlAR------GYLGRPALTAERFVPD--PFgpgsrmyRTGDLA 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 420 YLDSEGYLYIQTRDTDVFKFNNFQIYPEQIEEFILRLPGVSEACVfgipdavstnltacaVVRTKSPEGERLTA------ 493
Cdd:cd17646 378 RWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVV---------------VARAAPAGAARLVGyvvpaa 442
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 19922652 494 -------DHIRNIVEHHLSgAYHIRGGVYFIDSLPKTPNDKLQRR 531
Cdd:cd17646 443 gaagpdtAALRAHLAERLP-EYMVPAAFVVLDALPLTANGKLDRA 486
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
52-530 |
7.02e-31 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 125.76 E-value: 7.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 52 GQELTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNSTYLTSVIIAALLRGIPINPLHPEFTEETVKYMYDITEPKVIF 131
Cdd:PRK07514 26 GLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYFIGDAEPALVV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 132 CDVENYHIIKTVNGKLqNPAKIYLVNGKLEGVLdiSEMLNDEDsiTAAAYVPCpklHGDHTAFIVCSSGTTGMPKGVTRS 211
Cdd:PRK07514 106 CDPANFAWLSKIAAAA-GAPHVETLDADGTGSL--LEAAAAAP--DDFETVPR---GADDLAAILYTSGTTGRSKGAMLS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 212 HRSLLCNCKNPNTY---TRDSVLLSFSPLYWISGtiILLAS---LLNGCRRIITNRpYSVEYLLQLVARHKV-----TFL 280
Cdd:PRK07514 178 HGNLLSNALTLVDYwrfTPDDVLIHALPIFHTHG--LFVATnvaLLAGASMIFLPK-FDPDAVLALMPRATVmmgvpTFY 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 281 flashqIALLSKHDSDvmelKAQLQSIRVLIgAGSKVCKAVCRRMYELIGNQRFVVGYGLSEMGGLSKN------VGGPV 354
Cdd:PRK07514 255 ------TRLLQEPRLT----REAAAHMRLFI-SGSAPLLAETHREFQERTGHAILERYGMTETNMNTSNpydgerRAGTV 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 355 GcegKVMRNVELRVLD-KLKMPLGINEVGIIYARLR--FKwaGYYRNPEATRRALSSDGmWFRTGDIGYLDSEGYLYIQT 431
Cdd:PRK07514 324 G---FPLPGVSLRVTDpETGAELPPGEIGMIEVKGPnvFK--GYWRMPEKTAEEFRADG-FFITGDLGKIDERGYVHIVG 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 432 RDTDVFKFNNFQIYPEQIEEFILRLPGVSEACVFGIP-----DAVstnlTAcAVVRTKspeGERLTADHIRNIVEHHLSG 506
Cdd:PRK07514 398 RGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPhpdfgEGV----TA-VVVPKP---GAALDEAAILAALKGRLAR 469
|
490 500
....*....|....*....|....
gi 19922652 507 aYHIRGGVYFIDSLPKTPNDKLQR 530
Cdd:PRK07514 470 -FKQPKRVFFVDELPRNTMGKVQK 492
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
52-533 |
1.22e-30 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 125.65 E-value: 1.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 52 GQELTGAQLAQQSARIAQAFKRL-GLRRGDVVGISANNSTYLTSVIIAALLRGIPINPLHPEFTEETVKYMYDITEPKVI 130
Cdd:PRK05677 47 GKTLTYGELYKLSGAFAAWLQQHtDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVNTNPLYTAREMEHQFNDSGAKAL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 131 FC---------------DVEnyHIIKTVNGKLQNPAKIYLVNGKLEGV--------LDISEMLNDEDSITAAAYVPCPKL 187
Cdd:PRK05677 127 VClanmahlaekvlpktGVK--HVIVTEVADMLPPLKRLLINAVVKHVkkmvpayhLPQAVKFNDALAKGAGQPVTEANP 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 188 HGDHTAFIVCSSGTTGMPKGVTRSHRSLLCN---CK---NPNTYTRDSVLLSFSPLYWI-SGTIILLASLLNGCRRIITN 260
Cdd:PRK05677 205 QADDVAVLQYTGGTTGVAKGAMLTHRNLVANmlqCRalmGSNLNEGCEILIAPLPLYHIyAFTFHCMAMMLIGNHNILIS 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 261 RPYSVEYLLQLVARHKVT-FLFLASHQIALLSKHDSDVMELKAqlqsIRVLIGAGSKVCKAVCRRMYELIGNQrFVVGYG 339
Cdd:PRK05677 285 NPRDLPAMVKELGKWKFSgFVGLNTLFVALCNNEAFRKLDFSA----LKLTLSGGMALQLATAERWKEVTGCA-ICEGYG 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 340 LSEMGGLSknVGGP-----VGCEGKVMRNVELRVLDKLKMPLGINEVGIIYARLRFKWAGYYRNPEATRRALSSDGmWFR 414
Cdd:PRK05677 360 MTETSPVV--SVNPsqaiqVGTIGIPVPSTLCKVIDDDGNELPLGEVGELCVKGPQVMKGYWQRPEATDEILDSDG-WLK 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 415 TGDIGYLDSEGYLYIQTRDTDVFKFNNFQIYPEQIEEFILRLPGVSEACVFGIPDAVSTNLTACAVVrtkSPEGERLTAD 494
Cdd:PRK05677 437 TGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIKVFVV---VKPGETLTKE 513
|
490 500 510
....*....|....*....|....*....|....*....
gi 19922652 495 HIRNIVEHHLSGaYHIRGGVYFIDSLPKTPNDKLQRRKV 533
Cdd:PRK05677 514 QVMEHMRANLTG-YKVPKAVEFRDELPTTNVGKILRREL 551
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
192-530 |
1.33e-30 |
|
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: 121.98 E-value: 1.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 192 TAFIVCSSGTTGMPKGVTRSHRSLLCNCKN----PNTYTRDSVLLSFSPLYWISGTIILLASLLNGCRRIITNRPYSVEY 267
Cdd:cd17635 3 PLAVIFTSGTTGEPKAVLLANKTFFAVPDIlqkeGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGENTTYKS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 268 LLQLVARHKVTFLFLAShqiALLSKHDSDVMELKAQLQSIRvLIGAGSKVCKAVCRRMYELIGNQRFVVGYGLSEMGGLS 347
Cdd:cd17635 83 LFKILTTNAVTTTCLVP---TLLSKLVSELKSANATVPSLR-LIGYGGSRAIAADVRFIEATGLTNTAQVYGLSETGTAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 348 ----KNVGGPVGCEGKVMRNVELRVLDKLKMPLGINEVGIIYARLRFKWAGYYRNPEATRRALSsdGMWFRTGDIGYLDS 423
Cdd:cd17635 159 clptDDDSIEINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLI--DGWVNTGDLGERRE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 424 EGYLYIQTRDTDVFKFNNFQIYPEQIEEFILRLPGVSEACVFGIPDAVSTNLTACAVVRTkspegERLTADHIRNIVE-- 501
Cdd:cd17635 237 DGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVAS-----AELDENAIRALKHti 311
|
330 340
....*....|....*....|....*....
gi 19922652 502 HHLSGAYHIRGGVYFIDSLPKTPNDKLQR 530
Cdd:cd17635 312 RRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
59-533 |
1.99e-30 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 124.99 E-value: 1.99e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 59 QLAQQSAriAQAFKRLGLRRGDVVGISANNSTYLTSVIIAALLRGIPINPLHPEFTEETVKYMYDITEPKVI-----FC- 132
Cdd:PRK08751 58 QLVEQFA--AYLLGELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVLvvidnFGt 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 133 -------DVENYHIIKTVNGKLQNPAKIYLVN------GKLEGVLDISEMLNDEDSITAAAYVPCPKLH--GDHTAFIVC 197
Cdd:PRK08751 136 tvqqviaDTPVKQVITTGLGDMLGFPKAALVNfvvkyvKKLVPEYRINGAIRFREALALGRKHSMPTLQiePDDIAFLQY 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 198 SSGTTGMPKGVTRSHRSLLCNCKNPNTYTRDS--------VLLSFSPLYWISGTII--LLASLLNGCRRIITNrPYSVEY 267
Cdd:PRK08751 216 TGGTTGVAKGAMLTHRNLVANMQQAHQWLAGTgkleegceVVITALPLYHIFALTAngLVFMKIGGCNHLISN-PRDMPG 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 268 LLQLVARHKVT-FLFLASHQIALLSKHDSDvmelKAQLQSIRVLIGAGSKVCKAVCRRMYELIGnQRFVVGYGLSEMGGL 346
Cdd:PRK08751 295 FVKELKKTRFTaFTGVNTLFNGLLNTPGFD----QIDFSSLKMTLGGGMAVQRSVAERWKQVTG-LTLVEAYGLTETSPA 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 347 S-------KNVGGPVGCEgkvMRNVELRVLDKLKMPLGINEVGIIYARLRFKWAGYYRNPEATRRALSSDGmWFRTGDIG 419
Cdd:PRK08751 370 AcinpltlKEYNGSIGLP---IPSTDACIKDDAGTVLAIGEIGELCIKGPQVMKGYWKRPEETAKVMDADG-WLHTGDIA 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 420 YLDSEGYLYIQTRDTDVFKFNNFQIYPEQIEEFILRLPGVSEACVFGIPDAVSTNLTACAVVRtKSPEgerLTADHIRNI 499
Cdd:PRK08751 446 RMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEIVKVVIVK-KDPA---LTAEDVKAH 521
|
490 500 510
....*....|....*....|....*....|....
gi 19922652 500 VEHHLSGAYHIRgGVYFIDSLPKTPNDKLQRRKV 533
Cdd:PRK08751 522 ARANLTGYKQPR-IIEFRKELPKTNVGKILRREL 554
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
52-532 |
3.49e-30 |
|
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: 122.80 E-value: 3.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 52 GQELTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNSTYLTSVIIAALLRGIPINPLHPEFTEETVKYMYDITEPKVIF 131
Cdd:cd17653 20 GGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSARIQAILRTSGATLLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 132 CDvenyhiiktvngklqnpakiylvngklegvldisemlndeDSitaaayvpcpklhGDHTAFIVCSSGTTGMPKGVTRS 211
Cdd:cd17653 100 TT----------------------------------------DS-------------PDDLAYIIFTSGSTGIPKGVMVP 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 212 HRSLLCNCKNP--NTYTR--DSVLLSFSPLYWISgTIILLASLLNGCRRIITNRPYSVEYLLQlvarhKVTFLFLAShqi 287
Cdd:cd17653 127 HRGVLNYVSQPpaRLDVGpgSRVAQVLSIAFDAC-IGEIFSTLCNGGTLVLADPSDPFAHVAR-----TVDALMSTP--- 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 288 ALLSKHDSDVmelkaqLQSIRVLIGAGSKVCKAVCRRMYEligNQRFVVGYGLSE------MGGLSknVGGPVGCeGKVM 361
Cdd:cd17653 198 SILSTLSPQD------FPNLKTIFLGGEAVPPSLLDRWSP---GRRLYNAYGPTEctisstMTELL--PGQPVTI-GKPI 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 362 RNVELRVLDKLKMPLGINEVGIIY------ARlrfkwaGYYRNPEATRRALSSDGMW-----FRTGDIGYLDSEGYLYIQ 430
Cdd:cd17653 266 PNSTCYILDADLQPVPEGVVGEICisgvqvAR------GYLGNPALTASKFVPDPFWpgsrmYRTGDYGRWTEDGGLEFL 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 431 TRDTDVFKFNNFQIYPEQIEEFILRL-PGVSEACVFGIPDAVstnltaCAVVRTKSPEGERLtadhiRNIVEHHLSgAYH 509
Cdd:cd17653 340 GREDNQVKVRGFRINLEEIEEVVLQSqPEVTQAAAIVVNGRL------VAFVTPETVDVDGL-----RSELAKHLP-SYA 407
|
490 500
....*....|....*....|...
gi 19922652 510 IRGGVYFIDSLPKTPNDKLQRRK 532
Cdd:cd17653 408 VPDRIIALDSFPLTANGKVDRKA 430
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
52-532 |
3.55e-30 |
|
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: 123.17 E-value: 3.55e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 52 GQELTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNSTYLTSVIIAALLRGIPINPLHPEFTEETVKYMYDITEPKVIF 131
Cdd:cd12116 10 DRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPALVL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 132 CDvenyhiiktvngklqnPAKIYLVNGKLEGVLDisemlnDEDSITAAAYVPCPKLHGDHTAFIVCSSGTTGMPKGVTRS 211
Cdd:cd12116 90 TD----------------DALPDRLPAGLPVLLL------ALAAAAAAPAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 212 HRSLLCNC----KNPNTYTRDSVLLSFSPLYWISGTIILLaSLLNGCRRIITNRP--YSVEYLLQLVARHKVTF------ 279
Cdd:cd12116 148 HRNLVNFLhsmrERLGLGPGDRLLAVTTYAFDISLLELLL-PLLAGARVVIAPREtqRDPEALARLIEAHSITVmqatpa 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 280 ---LFLASHQIALLSKH--------DSDvmeLKAQLQSiRVligagskvckavcRRMYELIGNQRFVVGYGLSEMGGLSK 348
Cdd:cd12116 227 twrMLLDAGWQGRAGLTalcggealPPD---LAARLLS-RV-------------GSLWNLYGPTETTIWSTAARVTAAAG 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 349 NV--GGPVGcegkvmrNVELRVLDKLKMPLGINEVGIIY------ARlrfkwaGYYRNPEATRRALSSD------GMWFR 414
Cdd:cd12116 290 PIpiGRPLA-------NTQVYVLDAALRPVPPGVPGELYiggdgvAQ------GYLGRPALTAERFVPDpfagpgSRLYR 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 415 TGDIGYLDSEGYL-YIQTRDTDVfKFNNFQIYPEQIEEFILRLPGVSEACVFGIPDAVSTNLTACAVvrtkSPEGERLTA 493
Cdd:cd12116 357 TGDLVRRRADGRLeYLGRADGQV-KIRGHRIELGEIEAALAAHPGVAQAAVVVREDGGDRRLVAYVV----LKAGAAPDA 431
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 19922652 494 DHIRniveHHLSG---AYHIRGGVYFIDSLPKTPNDKLQRRK 532
Cdd:cd12116 432 AALR----AHLRAtlpAYMVPSAFVRLDALPLTANGKLDRKA 469
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
47-533 |
3.97e-30 |
|
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: 124.27 E-value: 3.97e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 47 ICDTTGQE--LTGAQLAQQSARIAQAFKRLGlRRGDVVGISANNSTYLTSVIIAALLRGIPINPLHPEFTEETVKYMYDI 124
Cdd:cd05931 15 LDDEGGREetLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPPTPGRHAERLAAI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 125 ---TEPKVIFCDvenyhiiktvnGKLQNPAKIYLVNGKLEGVLDISEMlnDEDSITAAAYVPCPKLHGDHTAFIVCSSGT 201
Cdd:cd05931 94 ladAGPRVVLTT-----------AAALAAVRAFAASRPAAGTPRLLVV--DLLPDTSAADWPPPSPDPDDIAYLQYTSGS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 202 TGMPKGVTRSHRSLLCNCKNPNT---YTRDSVLLSFSPLY----WISGtiiLLASLLNGCRRIIT------NRPYSveyL 268
Cdd:cd05931 161 TGTPKGVVVTHRNLLANVRQIRRaygLDPGDVVVSWLPLYhdmgLIGG---LLTPLYSGGPSVLMspaaflRRPLR---W 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 269 LQLVARHKVT------FLF-LASHQIallskHDSDVMELkaQLQSIRVLIGAGSKVCKAVCRRMYELIG-----NQRFVV 336
Cdd:cd05931 235 LRLISRYRATisaapnFAYdLCVRRV-----RDEDLEGL--DLSSWRVALNGAEPVRPATLRRFAEAFApfgfrPEAFRP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 337 GYGLSE------MGG--------------LSKNVGGP----------VGCeGKVMRNVELRVLD-KLKMPLGINEVGIIy 385
Cdd:cd05931 308 SYGLAEatlfvsGGPpgtgpvvlrvdrdaLAGRAVAVaaddpaarelVSC-GRPLPDQEVRIVDpETGRELPDGEVGEI- 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 386 arlrfkW-------AGYYRNPEATRRALSS-----DGMWFRTGDIGYLdSEGYLYIQTRDTDVFKFNNFQIYPEQIEEFI 453
Cdd:cd05931 386 ------WvrgpsvaSGYWGRPEATAETFGAlaatdEGGWLRTGDLGFL-HDGELYITGRLKDLIIVRGRNHYPQDIEATA 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 454 LRLPGV---SEACVFGIPDAVSTNLTA-CAVVRTKSPEGERLTADHIRNIV--EHHLSGAyhirgGVYFI--DSLPKTPN 525
Cdd:cd05931 459 EEAHPAlrpGCVAAFSVPDDGEERLVVvAEVERGADPADLAAIAAAIRAAVarEHGVAPA-----DVVLVrpGSIPRTSS 533
|
....*...
gi 19922652 526 DKLQRRKV 533
Cdd:cd05931 534 GKIQRRAC 541
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
60-534 |
2.87e-29 |
|
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: 120.56 E-value: 2.87e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 60 LAQQSARIAQAFKRLGLRRGDVVGISANNST---YLTSVIIAALLRGIPINPLHPEFTEETVKYMYDITEPKVIFCDVEN 136
Cdd:cd05929 1 LEARDLDRAQVFHQRRLLLLDVYSIALNRNAraaAAEGVWIADGVYIYLINSILTVFAAAAAWKCGACPAYKSSRAPRAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 137 YHIIKTVNgKLQNPAKIYLVNGKLEGVLDISEMLNDEDSITAAAYVPcpklhgdhTAFIVCSSGTTGMPKGVTRSHrsll 216
Cdd:cd05929 81 ACAIIEIK-AAALVCGLFTGGGALDGLEDYEAAEGGSPETPIEDEAA--------GWKMLYSGGTTGRPKGIKRGL---- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 217 cNCKNPNTYTR-----------DSVLLSFSPLYWISGTIILLASLLNGCRRIITNRpYSVEYLLQLVARHKVTFL-FLAS 284
Cdd:cd05929 148 -PGGPPDNDTLmaaalgfgpgaDSVYLSPAPLYHAAPFRWSMTALFMGGTLVLMEK-FDPEEFLRLIERYRVTFAqFVPT 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 285 HQIALLSKhdSDVMELKAQLQSIRVLIGAGSKVCKAVCRRMYELiGNQRFVVGYGLSEMGGLS-----------KNVGGP 353
Cdd:cd05929 226 MFVRLLKL--PEAVRNAYDLSSLKRVIHAAAPCPPWVKEQWIDW-GGPIIWEYYGGTEGQGLTiingeewlthpGSVGRA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 354 VGCEgkvmrnveLRVLDKLKMPLGINEVGIIYarlrFKWAG---YYRNPEATRRALSSDGmWFRTGDIGYLDSEGYLYIQ 430
Cdd:cd05929 303 VLGK--------VHILDEDGNEVPPGEIGEVY----FANGPgfeYTNDPEKTAAARNEGG-WSTLGDVGYLDEDGYLYLT 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 431 TRDTDVFKFNNFQIYPEQIEEFILRLPGVSEACVFGIPDavsTNL--TACAVVRT-KSPEGERLTADHIRNIVEHHLSgA 507
Cdd:cd05929 370 DRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPD---EELgqRVHAVVQPaPGADAGTALAEELIAFLRDRLS-R 445
|
490 500
....*....|....*....|....*..
gi 19922652 508 YHIRGGVYFIDSLPKTPNDKLQRRKVL 534
Cdd:cd05929 446 YKCPRSIEFVAELPRDDTGKLYRRLLR 472
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
36-544 |
1.17e-28 |
|
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: 120.11 E-value: 1.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 36 VLQINADQVMQICDT--TGQE--LTGAQLAQQSARIAQAFKRLGLRRGDVVGIsannstYLTSV--IIAALLRGIPINPL 109
Cdd:cd05967 60 VEAGRGDQIALIYDSpvTGTErtYTYAELLDEVSRLAGVLRKLGVVKGDRVII------YMPMIpeAAIAMLACARIGAI 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 110 HP----EFTEETVKYMYDITEPKVIF---CDVENYHII-------KTVNGKLQNPAKIYLVN-GKLEGVLDISEMLNDED 174
Cdd:cd05967 134 HSvvfgGFAAKELASRIDDAKPKLIVtasCGIEPGKVVpykplldKALELSGHKPHHVLVLNrPQVPADLTKPGRDLDWS 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 175 SITA-AAYVPCPKLHGDHTAFIVCSSGTTGMPKGVTRSHR----SLLCNCKNPNTYTRDSVLLSFSPLYWISG-TIILLA 248
Cdd:cd05967 214 ELLAkAEPVDCVPVAATDPLYILYTSGTTGKPKGVVRDNGghavALNWSMRNIYGIKPGDVWWAASDVGWVVGhSYIVYG 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 249 SLLNGCRRII-----TNRPYSVEYLlQLVARHKVTFLFLASHQIALLSKHDSDVMEL-KAQLQSIRVLIGAGSKvCKAvc 322
Cdd:cd05967 294 PLLHGATTVLyegkpVGTPDPGAFW-RVIEKYQVNALFTAPTAIRAIRKEDPDGKYIkKYDLSSLRTLFLAGER-LDP-- 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 323 rRMYELIGNQ--RFVVG-YGLSEMG----GLSKNVGG---PVGCEGKVMRNVELRVLDKLKMPLGINEVGIIYARLRFK- 391
Cdd:cd05967 370 -PTLEWAENTlgVPVIDhWWQTETGwpitANPVGLEPlpiKAGSPGKPVPGYQVQVLDEDGEPVGPNELGNIVIKLPLPp 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 392 --WAGYYRNPEATRRA-LSSDGMWFRTGDIGYLDSEGYLYIQTRDTDVFKFNNFQIYPEQIEEFILRLPGVSEACVFGIP 468
Cdd:cd05967 449 gcLLTLWKNDERFKKLyLSKFPGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVR 528
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19922652 469 DAVSTNLTACAVVRTkspEGERLTADHIRN-IVEHHLS--GAYHIRGGVYFIDSLPKTPNDKLQRRKVLGLVQQLELKA 544
Cdd:cd05967 529 DELKGQVPLGLVVLK---EGVKITAEELEKeLVALVREqiGPVAAFRLVIFVKRLPKTRSGKILRRTLRKIADGEDYTI 604
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
175-535 |
1.28e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 118.94 E-value: 1.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 175 SITAAAYVPCPKLHGDHTAFIVCSSGTTGMPKGVTRSHRSLLCN---CKNPNTYTRDSVLLSFSPLYWISGTII-LLASL 250
Cdd:PRK07787 113 RLHARSWHRYPEPDPDAPALIVYTSGTTGPPKGVVLSRRAIAADldaLAEAWQWTADDVLVHGLPLFHVHGLVLgVLGPL 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 251 LNGCRRIITNRPYSVEYLLQLVARhkVTFLF---LASHQIAllskhdsDVMELKAQLQSIRVLIGAGSKVCKAVCRRMYE 327
Cdd:PRK07787 193 RIGNRFVHTGRPTPEAYAQALSEG--GTLYFgvpTVWSRIA-------ADPEAARALRGARLLVSGSAALPVPVFDRLAA 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 328 LIGnQRFVVGYGLSE-MGGLSKNVGGP--VGCEGKVMRNVELRVLDKLKMPLGIN--EVGIIYARLRFKWAGYYRNPEAT 402
Cdd:PRK07787 264 LTG-HRPVERYGMTEtLITLSTRADGErrPGWVGLPLAGVETRLVDEDGGPVPHDgeTVGELQVRGPTLFDGYLNRPDAT 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 403 RRALSSDGmWFRTGDIGYLDSEGYLYIQTRD-TDVFKFNNFQIYPEQIEEFILRLPGVSEACVFGIPDA-VSTNLTACAV 480
Cdd:PRK07787 343 AAAFTADG-WFRTGDVAVVDPDGMHRIVGREsTDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDdLGQRIVAYVV 421
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 19922652 481 VRTKSPEGErlTADHirniVEHHLSgaYHIRG-GVYFIDSLPKTPNDKLQRRKVLG 535
Cdd:PRK07787 422 GADDVAADE--LIDF----VAQQLS--VHKRPrEVRFVDALPRNAMGKVLKKQLLS 469
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
48-530 |
1.39e-28 |
|
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: 119.52 E-value: 1.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 48 CDTTGQE--LTGAQLAQQSARIAQAFKRLGLRRGDVVGISANnSTYLTSVIIAALLR-GIPINPLHPEFTEETVKYMYDI 124
Cdd:cd05970 39 CDDAGEEriFTFAELADYSDKTANFFKAMGIGKGDTVMLTLK-RRYEFWYSLLALHKlGAIAIPATHQLTAKDIVYRIES 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 125 TEPKVIFCDVENY--HIIKTVNGKLQNPAKIYLVNGKL-EGVLDISEMLNDEDSI----TAAAYvPCpklhGDHTAFIVC 197
Cdd:cd05970 118 ADIKMIVAIAEDNipEEIEKAAPECPSKPKLVWVGDPVpEGWIDFRKLIKNASPDferpTANSY-PC----GEDILLVYF 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 198 SSGTTGMPKGVTRSHRSLL---CNCKNPNTYTRDSVLLS----------FSPLY--WISGTIILLASLlngcrriitnRP 262
Cdd:cd05970 193 SSGTTGMPKMVEHDFTYPLghiVTAKYWQNVREGGLHLTvadtgwgkavWGKIYgqWIAGAAVFVYDY----------DK 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 263 YSVEYLLQLVARHKVT--------FLFLASHQialLSKHDsdvmelkaqLQSIRVLIGAGSKVCKAVCRRMYELIGNQrF 334
Cdd:cd05970 263 FDPKALLEKLSKYGVTtfcapptiYRFLIRED---LSRYD---------LSSLRYCTTAGEALNPEVFNTFKEKTGIK-L 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 335 VVGYGLSE----MGGLSKNVGGPvGCEGKVMRNVELRVLDKLKMPLGINEVGIIYARLRFK-----WAGYYRNPEATRRA 405
Cdd:cd05970 330 MEGFGQTEttltIATFPWMEPKP-GSMGKPAPGYEIDLIDREGRSCEAGEEGEIVIRTSKGkpvglFGGYYKDAEKTAEV 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 406 LSsDGmWFRTGDIGYLDSEGYLYIQTRDTDVFKFNNFQIYPEQIEEFILRLPGVSEACVFGIPDAVSTNLTACAVVRTKS 485
Cdd:cd05970 409 WH-DG-YYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIVLAKG 486
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 19922652 486 PE-GERLT---ADHIRNIvehhlSGAYHIRGGVYFIDSLPKTPNDKLQR 530
Cdd:cd05970 487 YEpSEELKkelQDHVKKV-----TAPYKYPRIVEFVDELPKTISGKIRR 530
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
53-466 |
1.89e-28 |
|
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341295 [Multi-domain] Cd Length: 468 Bit Score: 118.23 E-value: 1.89e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 53 QELTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNStYLTSVIIAALLRGIPIN-PLHPEFTEETVKYMYDITEPKVIF 131
Cdd:cd17640 4 KRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNS-PRWLIADQGIMALGAVDvVRGSDSSVEELLYILNHSESVALV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 132 cdVENyhiiktvngklqnpakiylvngklegvldisemlndedsitaaayvpcpklHGDHTAFIVCSSGTTGMPKGVTRS 211
Cdd:cd17640 83 --VEN---------------------------------------------------DSDDLATIIYTSGTTGNPKGVMLT 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 212 HRSLLCNCKNPNTYTRDSV---LLSFSPLYWISGTIILLASLLNGCRRIITnrpySVEYLLQLVARHKVTFL-------- 280
Cdd:cd17640 110 HANLLHQIRSLSDIVPPQPgdrFLSILPIWHSYERSAEYFIFACGCSQAYT----SIRTLKDDLKRVKPHYIvsvprlwe 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 281 -FLASHQIALLSKHDSDVMELKAQL--QSIRVLI-GAGSKVCKAVcrRMYELIGnQRFVVGYGLSEMGG------LSKNV 350
Cdd:cd17640 186 sLYSGIQKQVSKSSPIKQFLFLFFLsgGIFKFGIsGGGALPPHVD--TFFEAIG-IEVLNGYGLTETSPvvsarrLKCNV 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 351 GGPVGcegKVMRNVELRVLDKL-KMPLGINEVGIIYARLRFKWAGYYRNPEATRRALSSDGmWFRTGDIGYLDSEGYLYI 429
Cdd:cd17640 263 RGSVG---RPLPGTEIKIVDPEgNVVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDG-WFNTGDLGWLTCGGELVL 338
|
410 420 430
....*....|....*....|....*....|....*...
gi 19922652 430 QTRDTDVFKFNNFQ-IYPEQIEEFILRLPGVSEACVFG 466
Cdd:cd17640 339 TGRAKDTIVLSNGEnVEPQPIEEALMRSPFIEQIMVVG 376
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
54-524 |
2.07e-28 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 119.67 E-value: 2.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 54 ELTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNSTYLTSVIIAALLRGI--PINP-LHPEFTEETVKYmydiTEPKVI 130
Cdd:PRK07529 58 TWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGEAAGIanPINPlLEPEQIAELLRA----AGAKVL 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 131 FC-------DV------------ENYHIIKTVNGKLQNPAK---IYLVNGKL-EGVLDISEMLNDEDSITAaayVPCPKL 187
Cdd:PRK07529 134 VTlgpfpgtDIwqkvaevlaalpELRTVVEVDLARYLPGPKrlaVPLIRRKAhARILDFDAELARQPGDRL---FSGRPI 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 188 HGDHTAFIVCSSGTTGMPKGVTRSHRSLLCNCKNPNT---YTRDSVLLSFSPLYWISGTI-ILLASLLNGCRRII-TNRP 262
Cdd:PRK07529 211 GPDDVAAYFHTGGTTGMPKLAQHTHGNEVANAWLGALllgLGPGDTVFCGLPLFHVNALLvTGLAPLARGAHVVLaTPQG 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 263 YSVEYLLQ----LVARHKVTFLFLASHQIALLSKHDSDvmelKAQLQSIRVLIGAGSKVCKAVCRRMYELIGnQRFVVGY 338
Cdd:PRK07529 291 YRGPGVIAnfwkIVERYRINFLSGVPTVYAALLQVPVD----GHDISSLRYALCGAAPLPVEVFRRFEAATG-VRIVEGY 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 339 GLSE---------MGGLSK--NVGGPV-GCEgkvMRNVELRVLDKLKMPLGINEVGIIYARLRFKWAGYYRnpEATRRAL 406
Cdd:PRK07529 366 GLTEatcvssvnpPDGERRigSVGLRLpYQR---VRVVILDDAGRYLRDCAVDEVGVLCIAGPNVFSGYLE--AAHNKGL 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 407 SSDGMWFRTGDIGYLDSEGYLYIQTRDTDVFKFNNFQIYPEQIEEFILRLPGVSEACVFGIPDAVSTNLtACAVVR---- 482
Cdd:PRK07529 441 WLEDGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGEL-PVAYVQlkpg 519
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 19922652 483 TKSPEGERLT--ADHI--RNIVEHHlsgayhirggVYFIDSLPKTP 524
Cdd:PRK07529 520 ASATEAELLAfaRDHIaeRAAVPKH----------VRILDALPKTA 555
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
50-484 |
2.11e-28 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 119.13 E-value: 2.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 50 TTGQELTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNSTYLTSVIIAALLRGIPINPLHPEFTEETVKYMYDITEPKV 129
Cdd:PLN02860 28 SGNRRRTGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWSFEEAKSAMLLVRPVM 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 130 IFCDVENYH-IIKTVNGKLQnPAKIYLVNGKL--EGVLDISEMLNDEDSITAAA------YVPCPklhgDHTAFIVCSSG 200
Cdd:PLN02860 108 LVTDETCSSwYEELQNDRLP-SLMWQVFLESPssSVFIFLNSFLTTEMLKQRALgtteldYAWAP----DDAVLICFTSG 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 201 TTGMPKGVTRSHRSLLCNCKNPNT---YTRDSVLLSFSPLYWISGTIILLASLLNG-CRRIITNrpYSVEYLLQLVARHK 276
Cdd:PLN02860 183 TTGRPKGVTISHSALIVQSLAKIAivgYGEDDVYLHTAPLCHIGGLSSALAMLMVGaCHVLLPK--FDAKAALQAIKQHN 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 277 VTFLFLASHQIA-LLSKHDSDvmELKAQLQSIRVLIGAGSKVCKAVCRRMYELIGNQRFVVGYGLSE------------- 342
Cdd:PLN02860 261 VTSMITVPAMMAdLISLTRKS--MTWKVFPSVRKILNGGGSLSSRLLPDAKKLFPNAKLFSAYGMTEacssltfmtlhdp 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 343 ------------MGGLSKNVGGPVG-CEGKVMRNVELRVldklKMPlGINEVGIIYARLRFKWAGYYRNPEATRRALSSD 409
Cdd:PLN02860 339 tlespkqtlqtvNQTKSSSVHQPQGvCVGKPAPHVELKI----GLD-ESSRVGRILTRGPHVMLGYWGQNSETASVLSND 413
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19922652 410 GmWFRTGDIGYLDSEGYLYIQTRDTDVFKFNNFQIYPEQIEEFILRLPGVSEACVFGIPDAVSTNLTAcAVVRTK 484
Cdd:PLN02860 414 G-WLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEMVV-ACVRLR 486
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
54-530 |
2.73e-28 |
|
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: 118.17 E-value: 2.73e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 54 ELTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNSTYLTSVIIAALLRGIPINPLHPEFTEETVKYMYDITEPKVIFCD 133
Cdd:cd12118 29 RYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVLFVD 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 134 VE-NYH-IIKTVNG--KLQNPAkiylvngklegvldisemlnDEDSITAAAYvpcpklhgdhtafivcSSGTTGMPKGVT 209
Cdd:cd12118 109 REfEYEdLLAEGDPdfEWIPPA--------------------DEWDPIALNY----------------TSGTTGRPKGVV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 210 RSHRSLLCNCKNPNTYTR---DSVLLSFSPLY--------W----ISGTIIllasllngCRRIITnrpYSVEYllQLVAR 274
Cdd:cd12118 153 YHHRGAYLNALANILEWEmkqHPVYLWTLPMFhcngwcfpWtvaaVGGTNV--------CLRKVD---AKAIY--DLIEK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 275 HKVTFLFLASHQIALLSkhDSDVMELKAQLQSIRVLIgAGSKVCKAVCRRMyELIGnqrFVV--GYGLSEmgglsknVGG 352
Cdd:cd12118 220 HKVTHFCGAPTVLNMLA--NAPPSDARPLPHRVHVMT-AGAPPPAAVLAKM-EELG---FDVthVYGLTE-------TYG 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 353 PVG-CEGKV------------------MRNV---ELRVLDKLKM---PLGINEVGIIYARLRFKWAGYYRNPEATRRALS 407
Cdd:cd12118 286 PATvCAWKPewdelpteerarlkarqgVRYVgleEVDVLDPETMkpvPRDGKTIGEIVFRGNIVMKGYLKNPEATAEAFR 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 408 sdGMWFRTGDIGYLDSEGYLYIQTRDTDVFKFNNFQIYPEQIEEFILRLPGVSEACVFGIPDAvSTNLTACAVVRTKspE 487
Cdd:cd12118 366 --GGWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDE-KWGEVPCAFVELK--E 440
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 19922652 488 GERLTADHIRNIVEHHLSGaYHIRGGVYFIDsLPKTPNDKLQR 530
Cdd:cd12118 441 GAKVTEEEIIAFCREHLAG-FMVPKTVVFGE-LPKTSTGKIQK 481
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
42-527 |
8.51e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 116.91 E-value: 8.51e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 42 DQVMQICDttGQELTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNST-YLTSVIIAALLRGIPINpLHPEFTEETVKY 120
Cdd:PRK07798 18 DRVALVCG--DRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIeYVEAMLGAFKARAVPVN-VNYRYVEDELRY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 121 MYDITEPKVIFCDVENYHIIKTVNGKLQNPAKIYLV-----NGKLEGVLDISEMLNDEDsitaAAYVPCPKLHGDHtaFI 195
Cdd:PRK07798 95 LLDDSDAVALVYEREFAPRVAEVLPRLPKLRTLVVVedgsgNDLLPGAVDYEDALAAGS----PERDFGERSPDDL--YL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 196 VCSSGTTGMPKGVTRSH----RSLLcncKNPNTYTRD-----------------SVLLSFSPLYWISGTIILLASLLNGC 254
Cdd:PRK07798 169 LYTGGTTGMPKGVMWRQedifRVLL---GGRDFATGEpiedeeelakraaagpgMRRFPAPPLMHGAGQWAAFAALFSGQ 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 255 RRII-TNRPYSVEYLLQLVARHKVTFLFLASHQIA------LLSKHDSDvmelkaqLQSIRVLIGAGSKVCKAVCRRMYE 327
Cdd:PRK07798 246 TVVLlPDVRFDADEVWRTIEREKVNVITIVGDAMArplldaLEARGPYD-------LSSLFAIASGGALFSPSVKEALLE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 328 LIGNQRFVVGYGLSEMG--GLSKNVGGPVGCEG-KVMRNVELRVLDKLKMPL--GINEVGIIyARLRFKWAGYYRNPEAT 402
Cdd:PRK07798 319 LLPNVVLTDSIGSSETGfgGSGTVAKGAVHTGGpRFTIGPRTVVLDEDGNPVepGSGEIGWI-ARRGHIPLGYYKDPEKT 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 403 RRAlssdgmwFRT---------GDIGYLDSEGYLYIQTRDTDVFKFNNFQIYPEQIEEFILRLPGVSEACVFGIPD---- 469
Cdd:PRK07798 398 AET-------FPTidgvryaipGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVPDerwg 470
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 19922652 470 -AVStnltacAVVRTKspEGERLTADHIRNIVEHHLSGaYHIRGGVYFIDSLPKTPNDK 527
Cdd:PRK07798 471 qEVV------AVVQLR--EGARPDLAELRAHCRSSLAG-YKVPRAIWFVDEVQRSPAGK 520
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
53-531 |
1.29e-27 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 116.32 E-value: 1.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 53 QELTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNS-----TYLTSVIIAALLrgIPINPlhpEFTEETVKYMYDITEP 127
Cdd:PRK08008 36 RRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCpefifCWFGLAKIGAIM--VPINA---RLLREESAWILQNSQA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 128 KVIFCDVENYHIIKTVNGKLQNPAKIYLV----NGKLEGVLDISEMLNDEdsitAAAYVPCPKLHGDHTAFIVCSSGTTG 203
Cdd:PRK08008 111 SLLVTSAQFYPMYRQIQQEDATPLRHICLtrvaLPADDGVSSFTQLKAQQ----PATLCYAPPLSTDDTAEILFTSGTTS 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 204 MPKGVTRSHrsllCNCKNPNTYT-------RDSVLLSFSPLYWISGTI-ILLASLLNGCRRIITNRpYSVEYLLQLVARH 275
Cdd:PRK08008 187 RPKGVVITH----YNLRFAGYYSawqcalrDDDVYLTVMPAFHIDCQCtAAMAAFSAGATFVLLEK-YSARAFWGQVCKY 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 276 KVTFlflaSHQIALLskhdsdVMELKAQLQSirvligAGSKvckAVCRR--MYEL-IGNQ-------RFVV----GYGLS 341
Cdd:PRK08008 262 RATI----TECIPMM------IRTLMVQPPS------ANDR---QHCLRevMFYLnLSDQekdafeeRFGVrlltSYGMT 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 342 E-MGGLsknVGGPVGCE------GKVMRNVELRVLDKLKMPLGINEVGIIY-----ARLRFKwaGYYRNPEATRRALSSD 409
Cdd:PRK08008 323 EtIVGI---IGDRPGDKrrwpsiGRPGFCYEAEIRDDHNRPLPAGEIGEICikgvpGKTIFK--EYYLDPKATAKVLEAD 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 410 GmWFRTGDIGYLDSEGYLYIQTRDTDVFKFNNFQIYPEQIEEFILRLPGVSEACVFGIPDAVSTNLTACAVVRTkspEGE 489
Cdd:PRK08008 398 G-WLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLN---EGE 473
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 19922652 490 RLTADHIRNIVEHHLSGaYHIRGGVYFIDSLPKTPNDKLQRR 531
Cdd:PRK08008 474 TLSEEEFFAFCEQNMAK-FKVPSYLEIRKDLPRNCSGKIIKK 514
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
50-533 |
1.50e-27 |
|
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: 115.27 E-value: 1.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 50 TTGQELTGAQLAQQSARIAQAFK-RLGLRRGDVVGISANNSTYLTSVIIAALLRG---IPINPL--HPEFTeetvkYMYD 123
Cdd:cd05958 6 SPEREWTYRDLLALANRIANVLVgELGIVPGNRVLLRGSNSPELVACWFGIQKAGaiaVATMPLlrPKELA-----YILD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 124 ITEPKVIFCDvenyhiiktvngklqnpakiylvngklegvldisemlndeDSITAAayvpcpklhgDHTAFIVCSSGTTG 203
Cdd:cd05958 81 KARITVALCA----------------------------------------HALTAS----------DDICILAFTSGTTG 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 204 MPKGVTRSHRSLL--CNCKNPNTY--TRDSVLLSFSPLYWISGT-IILLASLLNGCRRIITNRPySVEYLLQLVARHKVT 278
Cdd:cd05958 111 APKATMHFHRDPLasADRYAVNVLrlREDDRFVGSPPLAFTFGLgGVLLFPFGVGASGVLLEEA-TPDLLLSAIARYKPT 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 279 FLFLA-SHQIALLSKHDsdvmELKAQLQSIRVLIGAGSKVCKAVCRRMYELIGNQrFVVGYGLSEMGGLS-KNVGGP--V 354
Cdd:cd05958 190 VLFTApTAYRAMLAHPD----AAGPDLSSLRKCVSAGEALPAALHRAWKEATGIP-IIDGIGSTEMFHIFiSARPGDarP 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 355 GCEGKVMRNVELRVLDKLKMPLGINEVGiiyaRLRFKWAGYYRNPEATRRALSSDGMWFRTGDIGYLDSEGYLYIQTRDT 434
Cdd:cd05958 265 GATGKPVPGYEAKVVDDEGNPVPDGTIG----RLAVRGPTGCRYLADKRQRTYVQGGWNITGDTYSRDPDGYFRHQGRSD 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 435 DVFKFNNFQIYPEQIEEFILRLPGVSEACVFGIPD-AVSTNLTACAVVRTKSPEGERLtADHIRNIVEHHLSgAYHIRGG 513
Cdd:cd05958 341 DMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDeSRGVVVKAFVVLRPGVIPGPVL-ARELQDHAKAHIA-PYKYPRA 418
|
490 500
....*....|....*....|
gi 19922652 514 VYFIDSLPKTPNDKLQRRKV 533
Cdd:cd05958 419 IEFVTELPRTATGKLQRFAL 438
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
52-531 |
2.27e-27 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 117.75 E-value: 2.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 52 GQELTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNSTYLTSVIIAALLRGIPINPLHPEFTEETVKYMYDITEPKVIF 131
Cdd:PRK12316 2026 DQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLL 2105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 132 CDvenyhiiKTVNGKLQNPAKIylvngkleGVLDISEMLNDEDSITAAayvPCPKLHGDHTAFIVCSSGTTGMPKGVTRS 211
Cdd:PRK12316 2106 TQ-------RHLLERLPLPAGV--------ARLPLDRDAEWADYPDTA---PAVQLAGENLAYVIYTSGSTGLPKGVAVS 2167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 212 HRSLLCNCKNPNTYTR----DSVlLSFSPLYWISGTIILLASLLNGCRRIItnRP---YSVEYLLQLVARHKVTFLFLAS 284
Cdd:PRK12316 2168 HGALVAHCQAAGERYElspaDCE-LQFMSFSFDGAHEQWFHPLLNGARVLI--RDdelWDPEQLYDEMERHGVTILDFPP 2244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 285 HQIALLSKHdsdvMELKAQLQSIRVLIGAGSKVCKAVCRRMYELIGNQRFVVGYGLSE--MGGLSKNVGGPVGCE----- 357
Cdd:PRK12316 2245 VYLQQLAEH----AERDGRPPAVRVYCFGGEAVPAASLRLAWEALRPVYLFNGYGPTEavVTPLLWKCRPQDPCGaayvp 2320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 358 -GKVMRNVELRVLDKLKMPLGINEVGIIY------ARlrfkwaGYYRNPEATRRALSSD------GMWFRTGDIGYLDSE 424
Cdd:PRK12316 2321 iGRALGNRRAYILDADLNLLAPGMAGELYlggeglAR------GYLNRPGLTAERFVPDpfsasgERLYRTGDLARYRAD 2394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 425 GYLYIQTRDTDVFKFNNFQIYPEQIEEFILRLPGVSEACVFGIPDAVSTNLTACAVVRTkspeGERLTADHIRNIVEHHL 504
Cdd:PRK12316 2395 GVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQDGASGKQLVAYVVPDD----AAEDLLAELRAWLAARL 2470
|
490 500
....*....|....*....|....*..
gi 19922652 505 SgAYHIRGGVYFIDSLPKTPNDKLQRR 531
Cdd:PRK12316 2471 P-AYMVPAHWVVLERLPLNPNGKLDRK 2496
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
52-531 |
2.32e-27 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 117.57 E-value: 2.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 52 GQELTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNSTYLTSVIIAALLRGIPINPLHPEFTEETVKYMYDITEPKVIF 131
Cdd:PRK12467 535 EQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLL 614
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 132 CDVEnyhiiktVNGKLQNPAKIylvngkleGVLDISEMLnDEDSITAAAYvPCPKLHGDHTAFIVCSSGTTGMPKGVTRS 211
Cdd:PRK12467 615 TQSH-------LLAQLPVPAGL--------RSLCLDEPA-DLLCGYSGHN-PEVALDPDNLAYVIYTSGSTGQPKGVAIS 677
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 212 HRSL---LCNCKNPNTYTRDSVLLSFSPLYWISGTIILLASLLNGCRRIItnRPYSV----EYLLQLVARHKVTFL-FLA 283
Cdd:PRK12467 678 HGALanyVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATLHL--LPPDCardaEAFAALMADQGVTVLkIVP 755
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 284 SHQIALLSKhdsdvmELKAQLQSIRVLIGAGSKVCKAVCRRMYELIGNQRFVVGYGLSE---------MGGLSKNVGG-P 353
Cdd:PRK12467 756 SHLQALLQA------SRVALPRPQRALVCGGEALQVDLLARVRALGPGARLINHYGPTEttvgvstyeLSDEERDFGNvP 829
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 354 VgceGKVMRNVELRVLDKLKMPLGINEVGIIY------ARlrfkwaGYYRNPEATRRALSSD------GMWFRTGDIGYL 421
Cdd:PRK12467 830 I---GQPLANLGLYILDHYLNPVPVGVVGELYiggaglAR------GYHRRPALTAERFVPDpfgadgGRLYRTGDLARY 900
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 422 DSEGYLYIQTRDTDVFKFNNFQIYPEQIEEFILRLPGVSEACVFGIPDAVSTNLTAcAVVRTKSPEGERLTA--DHIRNI 499
Cdd:PRK12467 901 RADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAGLQLVA-YLVPAAVADGAEHQAtrDELKAQ 979
|
490 500 510
....*....|....*....|....*....|..
gi 19922652 500 VEHHLSgAYHIRGGVYFIDSLPKTPNDKLQRR 531
Cdd:PRK12467 980 LRQVLP-DYMVPAHLLLLDSLPLTPNGKLDRK 1010
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
53-533 |
2.98e-27 |
|
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: 115.26 E-value: 2.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 53 QELTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNSTYLTSVIIAALLRGIPINPLHPEFTEETVKYMYDITEPKVIFC 132
Cdd:cd05932 5 VEFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 133 dvenyhiiktvnGKL-QNPAkiyLVNGKLEGVLDISEMLNDE-------DSITAAAyvpcPKLHG------DHTAFIVCS 198
Cdd:cd05932 85 ------------GKLdDWKA---MAPGVPEGLISISLPPPSAancqyqwDDLIAQH----PPLEErptrfpEQLATLIYT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 199 SGTTGMPKGVTRSHRSLLCNCKNPNTYTR---DSVLLSFSPLYWISG-TIILLASLLNGCRriiTNRPYSVEYLLQLVAR 274
Cdd:cd05932 146 SGTTGQPKGVMLTFGSFAWAAQAGIEHIGteeNDRMLSYLPLAHVTErVFVEGGSLYGGVL---VAFAESLDTFVEDVQR 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 275 HKVTFLF-----LASHQIALLSKHDSDVMELKAQLQSIRVLIGagSKVCKAV----CRRM--------------YELIGn 331
Cdd:cd05932 223 ARPTLFFsvprlWTKFQQGVQDKIPQQKLNLLLKIPVVNSLVK--RKVLKGLgldqCRLAgcgsapvppallewYRSLG- 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 332 QRFVVGYGLSEMGGLSK-NVGG--PVGCEGKVMRNVELRvldklkmplgINEVGIIYARLRFKWAGYYRNPEATRRALSS 408
Cdd:cd05932 300 LNILEAYGMTENFAYSHlNYPGrdKIGTVGNAGPGVEVR----------ISEDGEILVRSPALMMGYYKDPEATAEAFTA 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 409 DGmWFRTGDIGYLDSEGYLYIQTRDTDVFKFNNFQ-IYPEQIEEFILRLPGVSEACVFGipdavsTNLTA-------CAV 480
Cdd:cd05932 370 DG-FLRTGDKGELDADGNLTITGRVKDIFKTSKGKyVAPAPIENKLAEHDRVEMVCVIG------SGLPAplalvvlSEE 442
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19922652 481 VRTKSPEG-----ERLTADHIRNiVEHHLSGAYHIRGGV-----YFIDSLPKTPNDKLQRRKV 533
Cdd:cd05932 443 ARLRADAFaraelEASLRAHLAR-VNSTLDSHEQLAGIVvvkdpWSIDNGILTPTLKIKRNVL 504
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
26-532 |
4.80e-27 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 114.86 E-value: 4.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 26 EMTLGEVIMRVLQINADQVMQICDttGQELTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNSTYLTSVIIAALLRGIP 105
Cdd:PRK06155 20 ERTLPAMLARQAERYPDRPLLVFG--GTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 106 INPLHPEFTEETVKYMYDITEPKVIFCDVENYHIIKTVNGKLQNPAKIYLVNGKLEGVLDISemLNDEDSITAAAYVPCP 185
Cdd:PRK06155 98 AVPINTALRGPQLEHILRNSGARLLVVEAALLAALEAADPGDLPLPAVWLLDAPASVSVPAG--WSTAPLPPLDAPAPAA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 186 KLHGDHTAFIVCSSGTTGMPKGVTRSHRSLL---CNCKNPNTYTRDSVLLSFSPLYWISGTIILLASLLNGCRRIITNRp 262
Cdd:PRK06155 176 AVQPGDTAAILYTSGTTGPSKGVCCPHAQFYwwgRNSAEDLEIGADDVLYTTLPLFHTNALNAFFQALLAGATYVLEPR- 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 263 YSVEYLLQLVARHKVTFLFLASHQIALL-----SKHDSDvmelkaqlQSIRVLIGAGskVCKAVCRRMYELIGnQRFVVG 337
Cdd:PRK06155 255 FSASGFWPAVRRHGATVTYLLGAMVSILlsqpaRESDRA--------HRVRVALGPG--VPAALHAAFRERFG-VDLLDG 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 338 YGLSEMGGLsknVGGPV-----GCEGKVMRNVELRVLDKLKMPLGINEVG--IIYARLRFKWA-GYYRNPEATRRALSSd 409
Cdd:PRK06155 324 YGSTETNFV---IAVTHgsqrpGSMGRLAPGFEARVVDEHDQELPDGEPGelLLRADEPFAFAtGYFGMPEKTVEAWRN- 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 410 gMWFRTGDIGYLDSEGYLYIQTRDTDVFKFNNFQIYPEQIEEFILRLPGVSEACVFGIPDAVSTNLTACAVVRTkspEGE 489
Cdd:PRK06155 400 -LWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLR---DGT 475
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 19922652 490 RLTADhirNIVEHHLSG-AYH-IRGGVYFIDSLPKTPNDKLQRRK 532
Cdd:PRK06155 476 ALEPV---ALVRHCEPRlAYFaVPRYVEFVAALPKTENGKVQKFV 517
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
52-532 |
7.38e-27 |
|
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: 113.96 E-value: 7.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 52 GQELTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNSTYLTSVIIAALLRGIPINPLHPEFTEETVKYMYDitepkvif 131
Cdd:cd17655 20 DQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEERIQYILE-------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 132 cdvenyhiiktvngklQNPAKIYLVNGKLEGVLDISE---MLNDEDSITAAAYVPCPKLHGDHTAFIVCSSGTTGMPKGV 208
Cdd:cd17655 92 ----------------DSGADILLTQSHLQPPIAFIGlidLLDEDTIYHEESENLEPVSKSDDLAYVIYTSGSTGKPKGV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 209 TRSHRSLLcNCKN--PNTYTRDSVL--LSFSPLYWISGTIILLASLLNGCRRIITNRP--YSVEYLLQLVARHKVTFLFL 282
Cdd:cd17655 156 MIEHRGVV-NLVEwaNKVIYQGEHLrvALFASISFDASVTEIFASLLSGNTLYIVRKEtvLDGQALTQYIRQNRITIIDL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 283 ASHQIALLSKHDsdvmelKAQLQSIRVLIGAGSKVCKAVCRRMYELIG-NQRFVVGYGLSEM----------GGLSKNVG 351
Cdd:cd17655 235 TPAHLKLLDAAD------DSEGLSLKHLIVGGEALSTELAKKIIELFGtNPTITNAYGPTETtvdasiyqyePETDQQVS 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 352 GPVgceGKVMRNVELRVLDKLKMPLGINEVGIIY------ARlrfkwaGYYRNPEATRRALSSD-----GMWFRTGDIGY 420
Cdd:cd17655 309 VPI---GKPLGNTRIYILDQYGRPQPVGVAGELYiggegvAR------GYLNRPELTAEKFVDDpfvpgERMYRTGDLAR 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 421 LDSEGYL-YIQTRDTDVfKFNNFQIYPEQIEEFILRLPGVSEACVFGIPDAvSTNLTACAVVRTKSPegerLTADHIRNI 499
Cdd:cd17655 380 WLPDGNIeFLGRIDHQV-KIRGYRIELGEIEARLLQHPDIKEAVVIARKDE-QGQNYLCAYIVSEKE----LPVAQLREF 453
|
490 500 510
....*....|....*....|....*....|....*
gi 19922652 500 VEHHLSGaYHIRGgvYFI--DSLPKTPNDKLQRRK 532
Cdd:cd17655 454 LARELPD-YMIPS--YFIklDEIPLTPNGKVDRKA 485
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
36-531 |
4.67e-26 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 113.72 E-value: 4.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 36 VLQINADQVMQICDTT-----GQELTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNSTYLTSVIIAALLRGIPINPLH 110
Cdd:PRK12467 1576 VHQLIEDQAAATPEAValvfgEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLD 1655
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 111 PEFTEETVKYMYditEPKVIFCDVENYHIIktvngklqnpAKIYLVNGKLEGVLDISEMLNDEDSITAAAYVPCPklhgD 190
Cdd:PRK12467 1656 PEYPRERLAYMI---EDSGIELLLTQSHLQ----------ARLPLPDGLRSLVLDQEDDWLEGYSDSNPAVNLAP----Q 1718
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 191 HTAFIVCSSGTTGMPKGVTRSHRSL---LCNCKNPNTYTRDSVLLSFSPLYWISGTIILLASLLNGCRRIItnRPYSV-- 265
Cdd:PRK12467 1719 NLAYVIYTSGSTGRPKGAGNRHGALvnrLCATQEAYQLSAADVVLQFTSFAFDVSVWELFWPLINGARLVI--APPGAhr 1796
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 266 --EYLLQLVARHKVTFL-FLASHQIALLSkhdsdVMELKAQLQSIRVLIGAGSKVCKAVCRRMYELIGNQRFVVGYGLSE 342
Cdd:PRK12467 1797 dpEQLIQLIERQQVTTLhFVPSMLQQLLQ-----MDEQVEHPLSLRRVVCGGEALEVEALRPWLERLPDTGLFNLYGPTE 1871
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 343 -----------MGGLSKNVGGPVgceGKVMRNVELRVLDKLKMPLGINEVGIIY------ARlrfkwaGYYRNPEAT-RR 404
Cdd:PRK12467 1872 tavdvthwtcrRKDLEGRDSVPI---GQPIANLSTYILDASLNPVPIGVAGELYlggvglAR------GYLNRPALTaER 1942
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 405 ALSS-----DGMWFRTGDIGYLDSEGYL-YIQTRDTDVfKFNNFQIYPEQIEEFILRLPGVSEACVFGIPDAVSTNLTAC 478
Cdd:PRK12467 1943 FVADpfgtvGSRLYRTGDLARYRADGVIeYLGRIDHQV-KIRGFRIELGEIEARLREQGGVREAVVIAQDGANGKQLVAY 2021
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19922652 479 AVvrtksPEGERLTADHI-----RNIVEHHLSGA---YHIRGGVYFIDSLPKTPNDKLQRR 531
Cdd:PRK12467 2022 VV-----PTDPGLVDDDEaqvalRAILKNHLKASlpeYMVPAHLVFLARMPLTPNGKLDRK 2077
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
49-533 |
4.75e-26 |
|
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: 112.20 E-value: 4.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 49 DTTGQELTGAQLAQQSARIAQAFKRLGLRRGDVVGIsannstYL--TSVIIAALLR----GIPINPLHPEFTEETVKYMY 122
Cdd:cd05968 86 DGTSRTLTYGELLYEVKRLANGLRALGVGKGDRVGI------YLpmIPEIVPAFLAvariGGIVVPIFSGFGKEAAATRL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 123 DITEPKVIFCDVENYHIIKTVNGK-------LQNPA--KIYLVNGKleGVLDISEMLND--EDSITAAAYVPCPKLHGDH 191
Cdd:cd05968 160 QDAEAKALITADGFTRRGREVNLKeeadkacAQCPTveKVVVVRHL--GNDFTPAKGRDlsYDEEKETAGDGAERTESED 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 192 TAFIVCSSGTTGMPKGVTRSH----------RSLLCNCKNPNTytrdsvLLSFSPLYWISGTIILLASLLNGCRRII--- 258
Cdd:cd05968 238 PLMIIYTSGTTGKPKGTVHVHagfplkaaqdMYFQFDLKPGDL------LTWFTDLGWMMGPWLIFGGLILGATMVLydg 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 259 -TNRPySVEYLLQLVARHKVTFLFLASHQIALLSKHDSDVMElKAQLQSIRVLIGAGSKVCKAVCRRMYELIGNQRF-VV 336
Cdd:cd05968 312 aPDHP-KADRLWRMVEDHEITHLGLSPTLIRALKPRGDAPVN-AHDLSSLRVLGSTGEPWNPEPWNWLFETVGKGRNpII 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 337 GY-GLSEM-GGLSKNVG----GPVGCEGKV--MRNVelrVLDKLKMPLgINEVGIIYarLRFKWAG----YYRNPEatrR 404
Cdd:cd05968 390 NYsGGTEIsGGILGNVLikpiKPSSFNGPVpgMKAD---VLDESGKPA-RPEVGELV--LLAPWPGmtrgFWRDED---R 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 405 ALSS-----DGMWFRtGDIGYLDSEGYLYIQTRDTDVFKFNNFQIYPEQIEEFILRLPGVSEACVFGIPDAVSTNLTAC- 478
Cdd:cd05968 461 YLETywsrfDNVWVH-GDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCf 539
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 19922652 479 AVVRTKSPEGERLtADHIRNIVEHHLSGAYHIRgGVYFIDSLPKTPNDKLQRRKV 533
Cdd:cd05968 540 VVLKPGVTPTEAL-AEELMERVADELGKPLSPE-RILFVKDLPKTRNAKVMRRVI 592
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
52-533 |
6.48e-26 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 111.45 E-value: 6.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 52 GQELTGAQLAQQSARIAQAF-KRLGLRRGDVVGISANNSTYLTSVIIAALLRGIPINPLHPEFTEETVKYMYDITEPKV- 129
Cdd:PRK12492 47 GVTLSYAELERHSAAFAAYLqQHTDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVNTNPLYTAREMRHQFKDSGARAl 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 130 ------------IFCDVENYHIIKTVNGKLQNPAKIYLVNGKLEGVldiSEMLNDEDSITAAAY------------VPCP 185
Cdd:PRK12492 127 vylnmfgklvqeVLPDTGIEYLIEAKMGDLLPAAKGWLVNTVVDKV---KKMVPAYHLPQAVPFkqalrqgrglslKPVP 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 186 KLHGDhTAFIVCSSGTTGMPKGVTRSHRSLLCNCKN-------------PNTYTRDSVLLSFSPLYWISG-TIILLASLL 251
Cdd:PRK12492 204 VGLDD-IAVLQYTGGTTGLAKGAMLTHGNLVANMLQvraclsqlgpdgqPLMKEGQEVMIAPLPLYHIYAfTANCMCMMV 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 252 NGCRRIITNRPYSVEYLLQLVARHKVT-FLFLASHQIALLSKHDSDVMELKAqlqsIRVLIGAGSKVCKAVCRRMYELIG 330
Cdd:PRK12492 283 SGNHNVLITNPRDIPGFIKELGKWRFSaLLGLNTLFVALMDHPGFKDLDFSA----LKLTNSGGTALVKATAERWEQLTG 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 331 NqRFVVGYGLSEM---------GGLSK--NVGGPVGcegkvmrNVELRVLDK--LKMPLGinEVGIIYARLRFKWAGYYR 397
Cdd:PRK12492 359 C-TIVEGYGLTETspvastnpyGELARlgTVGIPVP-------GTALKVIDDdgNELPLG--ERGELCIKGPQVMKGYWQ 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 398 NPEATRRALSSDGmWFRTGDIGYLDSEGYLYIQTRDTDVFKFNNFQIYPEQIEEFILRLPGVSEACVFGIPDAVSTNLTA 477
Cdd:PRK12492 429 QPEATAEALDAEG-WFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVK 507
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 19922652 478 CAVVrtksPEGERLTADHIRNIVEHHLSGaYHIRGGVYFIDSLPKTPNDKLQRRKV 533
Cdd:PRK12492 508 LFVV----ARDPGLSVEELKAYCKENFTG-YKVPKHIVLRDSLPMTPVGKILRREL 558
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
53-466 |
2.85e-25 |
|
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: 109.82 E-value: 2.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 53 QELTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNS-TYLTSVIIAALLRGIPInPLHPEFTEETVKYMYDITEPKVIF 131
Cdd:cd17641 10 QEFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRpEWVWAELAAQAIGALSL-GIYQDSMAEEVAYLLNYTGARVVI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 132 CDVEnyhiiktvngklQNPAKIYLVNGKLEGVLDI------------SEMLNDEDSITA---AAYVPCPKL--------H 188
Cdd:cd17641 89 AEDE------------EQVDKLLEIADRIPSVRYViycdprgmrkydDPRLISFEDVVAlgrALDRRDPGLyerevaagK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 189 GDHTAFIVCSSGTTGMPKGVTRSHRSLLCNCKN---PNTYTRDSVLLSFSPLYWISGTIILLASLLNGcrRIITNRPYSV 265
Cdd:cd17641 157 GEDVAVLCTTSGTTGKPKLAMLSHGNFLGHCAAylaADPLGPGDEYVSVLPLPWIGEQMYSVGQALVC--GFIVNFPEEP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 266 EYLLQLVARHKVTFLFLA----SHQIALLSKHDSDVMELKAQLqsIRVLIGAGSKVCKAV-------------------- 321
Cdd:cd17641 235 ETMMEDLREIGPTFVLLPprvwEGIAADVRARMMDATPFKRFM--FELGMKLGLRALDRGkrgrpvslwlrlaswladal 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 322 -------------CRRMY---ELIGNQRF----VVG------YGLSEMGGL----------SKNVGGPvgcegkvMRNVE 365
Cdd:cd17641 313 lfrplrdrlgfsrLRSAAtggAALGPDTFrffhAIGvplkqlYGQTELAGAytvhrdgdvdPDTVGVP-------FPGTE 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 366 LRvldklkmplgINEVGIIYARLRFKWAGYYRNPEATRRALSSDGmWFRTGDIGYLDSEGYLYIQTRDTDVFKFNNFQIY 445
Cdd:cd17641 386 VR----------IDEVGEILVRSPGVFVGYYKNPEATAEDFDEDG-WLHTGDAGYFKENGHLVVIDRAKDVGTTSDGTRF 454
|
490 500
....*....|....*....|..
gi 19922652 446 PEQIEEFILRL-PGVSEACVFG 466
Cdd:cd17641 455 SPQFIENKLKFsPYIAEAVVLG 476
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
49-470 |
3.23e-25 |
|
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: 108.96 E-value: 3.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 49 DTTGQELTGAQLAQQSARIAQAFKRlGLRRGDVVGISANNSTYLTSVIIAALLRG-IPINpLHPEFTEETVKYMYDITEP 127
Cdd:cd05909 2 DTLGTSLTYRKLLTGAIALARKLAK-MTKEGENVGVMLPPSAGGALANFALALSGkVPVM-LNYTAGLRELRACIKLAGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 128 KVIFCdvenyhiiktvngklqnpAKIYLVNGKLEGVLDISEM-----LND-------EDSITAAAYVPCPKLHG------ 189
Cdd:cd05909 80 KTVLT------------------SKQFIEKLKLHHLFDVEYDarivyLEDlrakiskADKCKAFLAGKFPPKWLlrifgv 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 190 -----DHTAFIVCSSGTTGMPKGVTRSHRSLLCN---CKNPNTYTRDSVLLSFSPLYWISG-TIILLASLLNGCRRIITN 260
Cdd:cd05909 142 apvqpDDPAVILFTSGSEGLPKGVVLSHKNLLANveqITAIFDPNPEDVVFGALPFFHSFGlTGCLWLPLLSGIKVVFHP 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 261 RPYSVEYLLQLVARHKVTFLFLAS--HQIALLSKHDSDvmelkaqLQSIRVLIgAGSKVCKAVCRRMYELIGNQRFVVGY 338
Cdd:cd05909 222 NPLDYKKIPELIYDKKATILLGTPtfLRGYARAAHPED-------FSSLRLVV-AGAEKLKDTLRQEFQEKFGIRILEGY 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 339 GLSEMGG-LSKNVGGP---VGCEGKVMRNVELRVLDK-LKMPLGINEVGIIYARLRFKWAGYYRNPEATrRALSSDGmWF 413
Cdd:cd05909 294 GTTECSPvISVNTPQSpnkEGTVGRPLPGMEVKIVSVeTHEEVPIGEGGLLLVRGPNVMLGYLNEPELT-SFAFGDG-WY 371
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 19922652 414 RTGDIGYLDSEGYLYIQTRDTDVFKFNNFQIYPEQIEEFIL-RLPGVSEACVFGIPDA 470
Cdd:cd05909 372 DTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSeILPEDNEVAVVSVPDG 429
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
189-532 |
5.23e-25 |
|
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: 106.41 E-value: 5.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 189 GDHTAFIVCSSGTTGMPKGVTRSHRSLLCN--CKNPNT-YTRDSVLLSFSPLYWISGTI-ILLASLLNGCRRIITN---- 260
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYNawMLALNSlFDPDDVLLCGLPLFHVNGSVvTLLTPLASGAHVVLAGpagy 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 261 -RPYSVEYLLQLVARHKVTFLFLASHQIALLSKHDSDvmelkAQLQSIRVLIGAGSKVCKAVCRRMYELIGNQrFVVGYG 339
Cdd:cd05944 81 rNPGLFDNFWKLVERYRITSLSTVPTVYAALLQVPVN-----ADISSLRFAMSGAAPLPVELRARFEDATGLP-VVEGYG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 340 LSEMG-GLSKNV-GGP--VGCEGKVM--RNVELRVLD---KLKMPLGINEVGIIYARLRFKWAGYYrNPEATRRALSSDG 410
Cdd:cd05944 155 LTEATcLVAVNPpDGPkrPGSVGLRLpyARVRIKVLDgvgRLLRDCAPDEVGEICVAGPGVFGGYL-YTEGNKNAFVADG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 411 mWFRTGDIGYLDSEGYLYIQTRDTDVFKFNNFQIYPEQIEEFILRLPGVSEACVFGIPDAVSTNLtACAVVRTK---SPE 487
Cdd:cd05944 234 -WLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGEL-PVAYVQLKpgaVVE 311
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 19922652 488 GERLTA---DHI--RNIVEHHlsgayhirggVYFIDSLPKT---PNDKLQRRK 532
Cdd:cd05944 312 EEELLAwarDHVpeRAAVPKH----------IEVLEELPVTavgKVFKPALRA 354
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
53-531 |
5.85e-25 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 110.43 E-value: 5.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 53 QELTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNSTYLTSVIIAALLRGIPINPLHPEFTEETVKYMYDITEPKVIFC 132
Cdd:PRK12316 535 ETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLS 614
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 133 DvenYHIIKT--VNGKLQNpakiylvngklegvldiseMLNDEDSITAAAY---VPCPKLHGDHTAFIVCSSGTTGMPKG 207
Cdd:PRK12316 615 Q---SHLGRKlpLAAGVQV-------------------LDLDRPAAWLEGYseeNPGTELNPENLAYVIYTSGSTGKPKG 672
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 208 VTRSHRSLLCN-CKNPNTYTR---DSVLLSfSPLYWISGTIILLASLLNGCRRIIT--NRPYSVEYLLQLVARHKVTFL- 280
Cdd:PRK12316 673 AGNRHRALSNRlCWMQQAYGLgvgDTVLQK-TPFSFDVSVWEFFWPLMSGARLVVAapGDHRDPAKLVELINREGVDTLh 751
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 281 FLASHQIALLskHDSDVmelkAQLQSIRVLIGAGSKVCKAVCRRMYELIGNQRFVVGYGLSEM------------GGLSK 348
Cdd:PRK12316 752 FVPSMLQAFL--QDEDV----ASCTSLRRIVCSGEALPADAQEQVFAKLPQAGLYNLYGPTEAaidvthwtcveeGGDSV 825
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 349 NVGGPVGcegkvmrNVELRVLDKLKMPLGINEVGIIYARLRFKWAGYYRNPEAT-RRALSS---DG-MWFRTGDIGYLDS 423
Cdd:PRK12316 826 PIGRPIA-------NLACYILDANLEPVPVGVLGELYLAGRGLARGYHGRPGLTaERFVPSpfvAGeRMYRTGDLARYRA 898
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 424 EGYLYIQTRDTDVFKFNNFQIYPEQIEEFILRLPGVSEACVFgipdAVSTNLTACAVVrtksPEGErltADHIRNIVEHH 503
Cdd:PRK12316 899 DGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVL----AVDGKQLVGYVV----LESE---GGDWREALKAH 967
|
490 500 510
....*....|....*....|....*....|.
gi 19922652 504 LSGA---YHIRGGVYFIDSLPKTPNDKLQRR 531
Cdd:PRK12316 968 LAASlpeYMVPAQWLALERLPLTPNGKLDRK 998
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
53-531 |
6.48e-25 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 108.72 E-value: 6.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 53 QELTGAQLAQQSARIAQAFK-RLGLRRGDVVGISANNSTYLTSVIIAALLRGIPINPLHPEFTEETVKYMYDITEPKVIF 131
Cdd:PRK05620 37 EQTTFAAIGARAAALAHALHdELGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 132 CD-------VENYHIIKTVNGKL---QNPAKIYLVNgKLEGVLDIS-EMLNDEDSitaaAYVPCPKLHGDHTAFIVCSSG 200
Cdd:PRK05620 117 ADprlaeqlGEILKECPCVRAVVfigPSDADSAAAH-MPEGIKVYSyEALLDGRS----TVYDWPELDETTAAAICYSTG 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 201 TTGMPKGVTRSHRSLLCNCKNPNT-----YTRDSVLLSFSPLYWISGTIILLASLLNGCRRIITNRPYSVEYLLQLVAR- 274
Cdd:PRK05620 192 TTGAPKGVVYSHRSLYLQSLSLRTtdslaVTHGESFLCCVPIYHVLSWGVPLAAFMSGTPLVFPGPDLSAPTLAKIIATa 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 275 -----HKVTFLFlashqIALLS---KHDSDVMelkaqlqSIRVLIGAGSKVCKAVCRrMYElignQRFVVG----YGLSE 342
Cdd:PRK05620 272 mprvaHGVPTLW-----IQLMVhylKNPPERM-------SLQEIYVGGSAVPPILIK-AWE----ERYGVDvvhvWGMTE 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 343 MGGLSKNVGGPVGCEGKVMRN-----------VELRVLDKLKMPLGI--NEvGIIYARLRFKWAGYYRNPEATRRALSS- 408
Cdd:PRK05620 335 TSPVGTVARPPSGVSGEARWAyrvsqgrfpasLEYRIVNDGQVMESTdrNE-GEIQVRGNWVTASYYHSPTEEGGGAASt 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 409 ---------------DGmWFRTGDIGYLDSEGYLYIQTRDTDVFKFNNFQIYPEQIEEFILRLPGVSEACVFGIPDAVST 473
Cdd:PRK05620 414 frgedvedandrftaDG-WLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWG 492
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 19922652 474 NLTACAVVRTKSPEGERLTADHIRNIVEHHLSGaYHIRGGVYFIDSLPKTPNDKLQRR 531
Cdd:PRK05620 493 ERPLAVTVLAPGIEPTRETAERLRDQLRDRLPN-WMLPEYWTFVDEIDKTSVGKFDKK 549
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
52-531 |
6.62e-25 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 110.05 E-value: 6.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 52 GQELTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNSTYLTSVIIAALLRGIPINPLHPEFTEETVKYMYDitepkvif 131
Cdd:PRK12316 4574 EEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMME-------- 4645
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 132 cdvenyhiiktvngklQNPAKIYLVNGKLEGVLDISEMLN------DEDSITAAAYVPCPKLHGDHTAFIVCSSGTTGMP 205
Cdd:PRK12316 4646 ----------------DSGAALLLTQSHLLQRLPIPDGLAslaldrDEDWEGFPAHDPAVRLHPDNLAYVIYTSGSTGRP 4709
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 206 KGVTRSHRSL---LCNCKNPNTYTRDSVLLSFSPLYWISGTIILLASLLNGCRRIITNRPYSV-EYLLQLVARHKVTFLF 281
Cdd:PRK12316 4710 KGVAVSHGSLvnhLHATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLINGASVVIRDDSLWDpERLYAEIHEHRVTVLV 4789
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 282 LASHQIALLSKHDsdvmELKAQLQSIRVLIGAGSKVCKAVCRRMYELIGNQRFVVGYGLSE--MGGLSKNVGGPVGCE-- 357
Cdd:PRK12316 4790 FPPVYLQQLAEHA----ERDGEPPSLRVYCFGGEAVAQASYDLAWRALKPVYLFNGYGPTEttVTVLLWKARDGDACGaa 4865
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 358 ----GKVMRNVELRVLDKLKMPLGINEVGIIY------ARlrfkwaGYYRNPEATRRALSSD------GMWFRTGDIGYL 421
Cdd:PRK12316 4866 ympiGTPLGNRSGYVLDGQLNPLPVGVAGELYlggegvAR------GYLERPALTAERFVPDpfgapgGRLYRTGDLARY 4939
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 422 DSEGYL-YIQTRDTDVfKFNNFQIYPEQIEEFILRLPGVSEACVFGIPDAVSTNLTACAVvrtksPEGERLTADH----- 495
Cdd:PRK12316 4940 RADGVIdYLGRVDHQV-KIRGFRIELGEIEARLREHPAVREAVVIAQEGAVGKQLVGYVV-----PQDPALADADeaqae 5013
|
490 500 510
....*....|....*....|....*....|....*....
gi 19922652 496 IRNIVEHHLSGA---YHIRGGVYFIDSLPKTPNDKLQRR 531
Cdd:PRK12316 5014 LRDELKAALRERlpeYMVPAHLVFLARMPLTPNGKLDRK 5052
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
82-533 |
2.18e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 106.40 E-value: 2.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 82 VGISANNSTYLTSVIIAALLRGIPINPLHPEFTEETVKYMYDITEPKVIFCDVENYHIIKTVNGKlqnpakiylvngkle 161
Cdd:PRK07638 53 IAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKERLAISNADMIVTERYKLNDLPDEEGR--------------- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 162 gVLDISEMLNDedsITAAAYVPCPKLHGDHTAFIV-CSSGTTGMPKGVTRSHRSLL----CNCKNPNTYTRDSVLL---- 232
Cdd:PRK07638 118 -VIEIDEWKRM---IEKYLPTYAPIENVQNAPFYMgFTSGSTGKPKAFLRAQQSWLhsfdCNVHDFHMKREDSVLIagtl 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 233 --------SFSPLYwISGTIILLasllngcrriitnRPYSVEYLLQLVARHKVTFLFLASHQIALLSKhdsdvmeLKAQL 304
Cdd:PRK07638 194 vhslflygAISTLY-VGQTVHLM-------------RKFIPNQVLDKLETENISVMYTVPTMLESLYK-------ENRVI 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 305 QSIRVLIGAGSKVCKAVCRRMYELIGNQRFVVGYGLSEMGGLSKNVGG----PVGCEGKVMRNVELRVLDKLKMPLGINE 380
Cdd:PRK07638 253 ENKMKIISSGAKWEAEAKEKIKNIFPYAKLYEFYGASELSFVTALVDEeserRPNSVGRPFHNVQVRICNEAGEEVQKGE 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 381 VGIIYARLRFKWAGYyRNPEATRRALSSDGmWFRTGDIGYLDSEGYLYIQTRDTDVFKFNNFQIYPEQIEEFILRLPGVS 460
Cdd:PRK07638 333 IGTVYVKSPQFFMGY-IIGGVLARELNADG-WMTVRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVD 410
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19922652 461 EACVFGIPDAVSTNLtACAVVRtkspegERLTADHIRNIVEHHLSgAYHIRGGVYFIDSLPKTPNDKLQRRKV 533
Cdd:PRK07638 411 EIVVIGVPDSYWGEK-PVAIIK------GSATKQQLKSFCLQRLS-SFKIPKEWHFVDEIPYTNSGKIARMEA 475
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
55-535 |
1.58e-23 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 104.73 E-value: 1.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 55 LTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNSTYLTSVIIAALLRGIPINPLHPEFTEETVKYMYDITEPKVIFcdv 134
Cdd:PRK06060 31 VTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPALVV--- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 135 enyhiiktVNGKLQNpakiylvNGKLEGVLDISEMLNDEDSITAAAYVPcpkLHGDHTAFIVCSSGTTGMPKGVTRSHRS 214
Cdd:PRK06060 108 --------TSDALRD-------RFQPSRVAEAAELMSEAARVAPGGYEP---MGGDALAYATYTSGTTGPPKAAIHRHAD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 215 LL----CNCKNPNTYTRDSVLLSFSPLYWISGT-IILLASLLNGCRRIITNRPYSVEYLLQLVARHKVTFLFLASHQIA- 288
Cdd:PRK06060 170 PLtfvdAMCRKALRLTPEDTGLCSARMYFAYGLgNSVWFPLATGGSAVINSAPVTPEAAAILSARFGPSVLYGVPNFFAr 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 289 LLSKHDSDvmelkaQLQSIRVLIGAGSKVCKAVCRRMYELIGNQRFVVGYGLSEMGG--LSKNVGG-PVGCEGKVMRNVE 365
Cdd:PRK06060 250 VIDSCSPD------SFRSLRCVVSAGEALELGLAERLMEFFGGIPILDGIGSTEVGQtfVSNRVDEwRLGTLGRVLPPYE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 366 LRVLDKLKMPLGINEVGIIYARLRFKWAGYYRNPEatrrALSSDGMWFRTGDIGYLDSEGYLYIQTRDTDVFKFNNFQIY 445
Cdd:PRK06060 324 IRVVAPDGTTAGPGVEGDLWVRGPAIAKGYWNRPD----SPVANEGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVD 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 446 PEQIEEFILRLPGVSEACVFGIPDAV-STNLTACAVvrtkSPEGERLTADHIRNIVEHHLS--GAYHIRGGVYFIDSLPK 522
Cdd:PRK06060 400 PREVERLIIEDEAVAEAAVVAVRESTgASTLQAFLV----ATSGATIDGSVMRDLHRGLLNrlSAFKVPHRFAVVDRLPR 475
|
490
....*....|...
gi 19922652 523 TPNDKLQRRKVLG 535
Cdd:PRK06060 476 TPNGKLVRGALRK 488
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
29-534 |
1.95e-23 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 103.92 E-value: 1.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 29 LGEVIMRvlQINADQVMQICDttGQELTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNST--YLTsviIAALLR-GI- 104
Cdd:PRK10946 27 LTDILTR--HAASDAIAVICG--ERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAefYIT---FFALLKlGVa 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 105 PINPLHPEFTEETVKYMYDItEPKVIFCDVEnyHIIKTVNGKL-----QNPAKIYLVNGKLEGVLDISEMLNDEdsitAA 179
Cdd:PRK10946 100 PVNALFSHQRSELNAYASQI-EPALLIADRQ--HALFSDDDFLntlvaEHSSLRVVLLLNDDGEHSLDDAINHP----AE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 180 AYVPCPKlHGDHTAFIVCSSGTTGMPKGVTRSH--------RS-----------LLCNCKNPNTYTrdsvlLSfSP---- 236
Cdd:PRK10946 173 DFTATPS-PADEVAFFQLSGGSTGTPKLIPRTHndyyysvrRSveicgftpqtrYLCALPAAHNYP-----MS-SPgalg 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 237 LYWISGTIILLA--SLLNgCrriitnrpysveylLQLVARHKVTFLFLASHQIALLSKHDSDVmELKAQLQSIRVLIGAG 314
Cdd:PRK10946 246 VFLAGGTVVLAPdpSATL-C--------------FPLIEKHQVNVTALVPPAVSLWLQAIAEG-GSRAQLASLKLLQVGG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 315 SKVCKAVCRRMYELIG---NQRFVVGYGLSEMGGLSKNVGGPVGCEGKVMR-NVELRVLDKLKMPLGINEVGIIYARLRF 390
Cdd:PRK10946 310 ARLSETLARRIPAELGcqlQQVFGMAEGLVNYTRLDDSDERIFTTQGRPMSpDDEVWVADADGNPLPQGEVGRLMTRGPY 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 391 KWAGYYRNPEATRRALSSDGMWFrTGDIGYLDSEGYLYIQTRDTDVFKFNNFQIYPEQIEEFILRLPGVSEACVFGIPDA 470
Cdd:PRK10946 390 TFRGYYKSPQHNASAFDANGFYC-SGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDE 468
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19922652 471 VSTNlTACAVVRTKSPegerLTADHIRNIVEHHLSGAYHIRGGVYFIDSLPKTPN---DKLQRRKVL 534
Cdd:PRK10946 469 LMGE-KSCAFLVVKEP----LKAVQLRRFLREQGIAEFKLPDRVECVDSLPLTAVgkvDKKQLRQWL 530
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
55-531 |
2.17e-23 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 103.68 E-value: 2.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 55 LTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNSTYLTSVIIAALLRGIPINPLHPEFTEETVKYMYDITEPKVIFCDV 134
Cdd:PRK13382 69 LTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPALAEVVTREGVDTVIYDE 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 135 EnyhIIKTVNGKLQN-PAKIYLVNGKLEGVLDISEMLNDedsiTAAAYVPCPKlhGDHTAFIVCSSGTTGMPKGVTRShr 213
Cdd:PRK13382 149 E---FSATVDRALADcPQATRIVAWTDEDHDLTVEVLIA----AHAGQRPEPT--GRKGRVILLTSGTTGTPKGARRS-- 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 214 sllcnckNPNTYTRDSVLLSFSPLY--------------WISGTIILLASLLNgcrRIITNRPYSVEYLLQLVARHKVTf 279
Cdd:PRK13382 218 -------GPGGIGTLKAILDRTPWRaeeptvivapmfhaWGFSQLVLAASLAC---TIVTRRRFDPEATLDLIDRHRAT- 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 280 lflashQIALLSKHDSDVMELKAQL------QSIRVLIGAGSKVCKAVCRRMYELIGNqrfVV--GYGLSEMGGLS---- 347
Cdd:PRK13382 287 ------GLAVVPVMFDRIMDLPAEVrnrysgRSLRFAAASGSRMRPDVVIAFMDQFGD---VIynNYNATEAGMIAtatp 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 348 KNVGGPVGCEGKVMRNVELRVLDKLKMPLGINEVGIIYARLRFKWAGYyrNPEATRRalSSDGMwFRTGDIGYLDSEGYL 427
Cdd:PRK13382 358 ADLRAAPDTAGRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGY--TSGSTKD--FHDGF-MASGDVGYLDENGRL 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 428 YIQTRDTDVFKFNNFQIYPEQIEEFILRLPGVSEACVFGIPDAVSTNLTACAVVRTkspEGERLTADHIRNIVEHHLSGa 507
Cdd:PRK13382 433 FVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLK---PGASATPETLKQHVRDNLAN- 508
|
490 500
....*....|....*....|....
gi 19922652 508 YHIRGGVYFIDSLPKTPNDKLQRR 531
Cdd:PRK13382 509 YKVPRDIVVLDELPRGATGKILRR 532
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
47-535 |
2.81e-23 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 103.15 E-value: 2.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 47 ICDTTGQeLTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNSTYLTSVIIAALLRGIPINPLHPEFTEETVKYMYDITE 126
Cdd:PRK13383 54 IIDDDGA-LSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAALRAHH 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 127 PKVIFCDVEnyhIIKTVNGklqnpakiylvNGKLEGVLDISeMLNDEDSITAAAYVPCPKLhgdhtafIVCSSGTTGMPK 206
Cdd:PRK13383 133 ISTVVADNE---FAERIAG-----------ADDAVAVIDPA-TAGAEESGGRPAVAAPGRI-------VLLTSGTTGKPK 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 207 GVTRSHR---------SLLcncknPNTYTRDSVLLSFS-PLYWISGTIILLASL-LNGCrrIITNRPYSVEYLLQLVARH 275
Cdd:PRK13383 191 GVPRAPQlrsavgvwvTIL-----DRTRLRTGSRISVAmPMFHGLGLGMLMLTIaLGGT--VLTHRHFDAEAALAQASLH 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 276 KVTFLFLASHQIAllskhdsDVMELKAQLQS------IRVLIGAGSKVCKAVCRRMYELIGNQRFVvGYGLSEMG----- 344
Cdd:PRK13383 264 RADAFTAVPVVLA-------RILELPPRVRArnplpqLRVVMSSGDRLDPTLGQRFMDTYGDILYN-GYGSTEVGigala 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 345 ------GLSKNVGGPV-GCEgkvmrnveLRVLDKLKMPLGINEVGIIYARLRFKWAGYyrnPEATRRALSsDGMwFRTGD 417
Cdd:PRK13383 336 tpadlrDAPETVGKPVaGCP--------VRILDRNNRPVGPRVTGRIFVGGELAGTRY---TDGGGKAVV-DGM-TSTGD 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 418 IGYLDSEGYLYIQTRDTDVFKFNNFQIYPEQIEEFILRLPGVSEACVFGIPDA-VSTNLTACAVVRTkspeGERLTADHI 496
Cdd:PRK13383 403 MGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDErFGHRLAAFVVLHP----GSGVDAAQL 478
|
490 500 510
....*....|....*....|....*....|....*....
gi 19922652 497 RNIVEHHLSGAYHIRgGVYFIDSLPKTPNDKLQRRKVLG 535
Cdd:PRK13383 479 RDYLKDRVSRFEQPR-DINIVSSIPRNPTGKVLRKELPG 516
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
50-532 |
3.70e-23 |
|
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: 102.40 E-value: 3.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 50 TTGQE-LTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNSTYLTSVIIAALLRG---IPINPLHPEfteETVKYMYDIT 125
Cdd:cd12115 19 VCGDEsLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGaayVPLDPAYPP---ERLRFILEDA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 126 EPKVIFCDvenyhiiktvngklqnpakiylvngklegvldisemlndedsitaaayvpcpklhGDHTAFIVCSSGTTGMP 205
Cdd:cd12115 96 QARLVLTD-------------------------------------------------------PDDLAYVIYTSGSTGRP 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 206 KGVTRSHRS---LLCNCKNpnTYTRD---SVLLSFSPLYWISgTIILLASLLNGCRRIITNrpySVEYLLQLVARHKVTF 279
Cdd:cd12115 121 KGVAIEHRNaaaFLQWAAA--AFSAEelaGVLASTSICFDLS-VFELFGPLATGGKVVLAD---NVLALPDLPAAAEVTL 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 280 LFLASHQIALLSKHDsdvmelkAQLQSIRVLIGAGSKVCKAVCRRMYELIGNQRFVVGYGLSEMGGLSKNVGGPVGCEGK 359
Cdd:cd12115 195 INTVPSAAAELLRHD-------ALPASVRVVNLAGEPLPRDLVQRLYARLQVERVVNLYGPSEDTTYSTVAPVPPGASGE 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 360 V-----MRNVELRVLDKLKMPLGINEVGIIY------ARlrfkwaGYYRNPEATRR-----ALSSDGMWFRTGDIGYLDS 423
Cdd:cd12115 268 VsigrpLANTQAYVLDRALQPVPLGVPGELYiggagvAR------GYLGRPGLTAErflpdPFGPGARLYRTGDLVRWRP 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 424 EGYLYIQTRDTDVFKFNNFQIYPEQIEEFILRLPGVSEACVFGIPDAVSTNLTACAVVrtkspeGERLTADHIRNIVEH- 502
Cdd:cd12115 342 DGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIV------AEPGAAGLVEDLRRHl 415
|
490 500 510
....*....|....*....|....*....|.
gi 19922652 503 -HLSGAYHIRGGVYFIDSLPKTPNDKLQRRK 532
Cdd:cd12115 416 gTRLPAYMVPSRFVRLDALPLTPNGKIDRSA 446
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
52-532 |
1.19e-22 |
|
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: 100.40 E-value: 1.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 52 GQELTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNSTYLTSVIIAALLRGIPINPLHPEFTEETVKYMYDITEPKVIf 131
Cdd:cd17652 10 DETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYMLADARPALL- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 132 cdvenyhiiktvngklqnpakiylvngklegvldisemlndedsITaaayvpcpklHGDHTAFIVCSSGTTGMPKGVTRS 211
Cdd:cd17652 89 --------------------------------------------LT----------TPDNLAYVIYTSGSTGRPKGVVVT 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 212 HRSLlcnCKNPNTYTR------DSVLLSFSPLYWISGTIILLASLLNGCRRIITNRPYSV--EYLLQLVARHKVTFLFLA 283
Cdd:cd17652 115 HRGL---ANLAAAQIAafdvgpGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLpgEPLADLLREHRITHVTLP 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 284 SHQIALLSKhdsdvmelkAQLQSIRVLIGAGsKVCKAvcrrmyELI----GNQRFVVGYGLSE-------MGGLSKNVGG 352
Cdd:cd17652 192 PAALAALPP---------DDLPDLRTLVVAG-EACPA------ELVdrwaPGRRMINAYGPTEttvcatmAGPLPGGGVP 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 353 PVGCEgkvMRNVELRVLDKLKMPLGINEVGIIY------ARlrfkwaGYYRNPEATRRALSSD------GMWFRTGDIGY 420
Cdd:cd17652 256 PIGRP---VPGTRVYVLDARLRPVPPGVPGELYiagaglAR------GYLNRPGLTAERFVADpfgapgSRMYRTGDLAR 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 421 LDSEGYLYIQTRDTDVFKFNNFQIYPEQIEEFILRLPGVSEACVFGIPDAVSTN-LTACAVVRtkspEGERLTADHIRNI 499
Cdd:cd17652 327 WRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKrLVAYVVPA----PGAAPTAAELRAH 402
|
490 500 510
....*....|....*....|....*....|...
gi 19922652 500 VEHHLSGaYHIRGGVYFIDSLPKTPNDKLQRRK 532
Cdd:cd17652 403 LAERLPG-YMVPAAFVVLDALPLTPNGKLDRRA 434
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
49-531 |
1.91e-22 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 101.13 E-value: 1.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 49 DTTGQELTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNSTYLTSVIIAALLRGIPINPLHPEFTEETVKYMYDITEPK 128
Cdd:PRK04319 68 ASRKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAK 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 129 VIFCDVENYHiiKTVNGKLQNPAKIYLVN---GKLEGVLDISEMLNDedsitAAAYVPCPKLHGDHTAFIVCSSGTTGMP 205
Cdd:PRK04319 148 VLITTPALLE--RKPADDLPSLKHVLLVGedvEEGPGTLDFNALMEQ-----ASDEFDIEWTDREDGAILHYTSGSTGKP 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 206 KGVTRSHRSLLCNcknpntYTRDSVLLSFSP--LYW-------ISGT---IIllASLLNGCRRIITNRPYSVEYLLQLVA 273
Cdd:PRK04319 221 KGVLHVHNAMLQH------YQTGKYVLDLHEddVYWctadpgwVTGTsygIF--APWLNGATNVIDGGRFSPERWYRILE 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 274 RHKVTFLFLASHQIALLSKHDSDVMElKAQLQSIRVLIGAGSKVCKAVCRRMYELIGnQRFVVGYGLSEMGG--LSKNVG 351
Cdd:PRK04319 293 DYKVTVWYTAPTAIRMLMGAGDDLVK-KYDLSSLRHILSVGEPLNPEVVRWGMKVFG-LPIHDNWWMTETGGimIANYPA 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 352 GPV--GCEGKVMRNVELRVLDKLKMPLGINEVGIIyaRLRFKWA----GYYRNPEATRRALSSDgmWFRTGDIGYLDSEG 425
Cdd:PRK04319 371 MDIkpGSMGKPLPGIEAAIVDDQGNELPPNRMGNL--AIKKGWPsmmrGIWNNPEKYESYFAGD--WYVSGDSAYMDEDG 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 426 YLYIQTRDTDVFKFNNFQIYPEQIEEFILRLPGVSEACVFGIPDAVSTNLT-ACAVVRTKSPEGERLTADhIRNIVEHHL 504
Cdd:PRK04319 447 YFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVRGEIIkAFVALRPGYEPSEELKEE-IRGFVKKGL 525
|
490 500
....*....|....*....|....*..
gi 19922652 505 SGAYHIRgGVYFIDSLPKTPNDKLQRR 531
Cdd:PRK04319 526 GAHAAPR-EIEFKDKLPKTRSGKIMRR 551
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
50-531 |
2.72e-22 |
|
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: 100.04 E-value: 2.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 50 TTGQELTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNSTYLTSVIIAALLRGIPINPLHPEFTEETVKYMYditepkv 129
Cdd:cd12114 8 CGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 130 ifcdvENYHIiktvngklqnpaKIYLVNGK--LEGVLDISEMLNDEDSITAAAYVPCPKLHGDHTAFIVCSSGTTGMPKG 207
Cdd:cd12114 81 -----ADAGA------------RLVLTDGPdaQLDVAVFDVLILDLDALAAPAPPPPVDVAPDDLAYVIFTSGSTGTPKG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 208 VTRSHRSLLCNCKNPN---TYTRDSVLLSFSPL------YWISGTIILLASLL--NGCRRIITNRpysveyLLQLVARHK 276
Cdd:cd12114 144 VMISHRAALNTILDINrrfAVGPDDRVLALSSLsfdlsvYDIFGALSAGATLVlpDEARRRDPAH------WAELIERHG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 277 VTFLFLASHQIALLSKHDSDVMELkaqLQSIRVLIGAGSKVCKAVCRRMYELIGNQRFVVgyglseMGGLSK----NVGG 352
Cdd:cd12114 218 VTLWNSVPALLEMLLDVLEAAQAL---LPSLRLVLLSGDWIPLDLPARLRALAPDARLIS------LGGATEasiwSIYH 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 353 PVGCE---------GKVMRNVELRVLDKLKMPLGINEVGIIY------ARlrfkwaGYYRNPEATRRALSSD---GMWFR 414
Cdd:cd12114 289 PIDEVppdwrsipyGRPLANQRYRVLDPRGRDCPDWVPGELWiggrgvAL------GYLGDPELTAARFVTHpdgERLYR 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 415 TGDIGYLDSEGYLYIQTRDTDVFKFNNFQIYPEQIEEFILRLPGVSEACVFGIPDAVSTNLTACAVVRtksPEGERLTAD 494
Cdd:cd12114 363 TGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDPGGKRLAAFVVPD---NDGTPIAPD 439
|
490 500 510
....*....|....*....|....*....|....*..
gi 19922652 495 HIRNIVEHHLsGAYHIRGGVYFIDSLPKTPNDKLQRR 531
Cdd:cd12114 440 ALRAFLAQTL-PAYMIPSRVIALEALPLTANGKVDRA 475
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
181-530 |
3.58e-22 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 100.59 E-value: 3.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 181 YVPcpkLHGDHTAFIVCSSGTTGMPKGVTRSHRSLLCnCKNPNTYTR-----DSVLLSFSPLYWISGTIILLASLLNGCR 255
Cdd:PTZ00237 248 YVP---VESSHPLYILYTSGTTGNSKAVVRSNGPHLV-GLKYYWRSIiekdiPTVVFSHSSIGWVSFHGFLYGSLSLGNT 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 256 RI-----ITNRPYSVEYLLQLVARHKVTFLFLASHQIALLSKHDSDVMELKAQ--LQSIRVLIGAGSKVCKAVCrrmyEL 328
Cdd:PTZ00237 324 FVmfeggIIKNKHIEDDLWNTIEKHKVTHTLTLPKTIRYLIKTDPEATIIRSKydLSNLKEIWCGGEVIEESIP----EY 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 329 IGNQ---RFVVGYGLSEMGGLS----KNVGGPVGCEGKVMRNVELRVLDKLKMPLGINEVGIIYARL----RFKwAGYYR 397
Cdd:PTZ00237 400 IENKlkiKSSRGYGQTEIGITYlycyGHINIPYNATGVPSIFIKPSILSEDGKELNVNEIGEVAFKLpmppSFA-TTFYK 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 398 NPEATRRALSSDGMWFRTGDIGYLDSEGYLYIQTRDTDVFKFNNFQIYPEQIEEFILRLPGVSEACVFGIPDAVSTNLTA 477
Cdd:PTZ00237 479 NDEKFKQLFSKFPGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPI 558
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 19922652 478 CAVVRTKSPEGERLTADHIRNIVEHHLS---GAYHIRGGVYFIDSLPKTPNDKLQR 530
Cdd:PTZ00237 559 GLLVLKQDQSNQSIDLNKLKNEINNIITqdiESLAVLRKIIIVNQLPKTKTGKIPR 614
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
190-533 |
4.15e-22 |
|
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: 99.48 E-value: 4.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 190 DHTAFIVCSSGTTGMPKGVTRSHRSL---LCNCKNPNTYTRDSVLLSFSPLYWISGTIIL-LASLLNGCRR-IITNRPYS 264
Cdd:cd05908 106 DELAFIQFSSGSTGDPKGVMLTHENLvhnMFAILNSTEWKTKDRILSWMPLTHDMGLIAFhLAPLIAGMNQyLMPTRLFI 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 265 VEYLLQL--VARHKVTFLFLASHQIALLSKHDSDVMELKAQLQSIRVLI-GA---GSKVCKAVCRRM--YELIGNQRFVV 336
Cdd:cd05908 186 RRPILWLkkASEHKATIVSSPNFGYKYFLKTLKPEKANDWDLSSIRMILnGAepiDYELCHEFLDHMskYGLKRNAILPV 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 337 gYGLSE--MGGLSKNVGGP--------------VGCE---------------GKVMRNVELRVLDKLKMPLGINEVGIIY 385
Cdd:cd05908 266 -YGLAEasVGASLPKAQSPfktitlgrrhvthgEPEPevdkkdsecltfvevGKPIDETDIRICDEDNKILPDGYIGHIQ 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 386 ARLRFKWAGYYRNPEATRRALSSDGmWFRTGDIGYLdSEGYLYIQTRDTDVFKFNNFQIYPEQIEEFILRLPGVSeacvf 465
Cdd:cd05908 345 IRGKNVTPGYYNNPEATAKVFTDDG-WLKTGDLGFI-RNGRLVITGREKDIIFVNGQNVYPHDIERIAEELEGVE----- 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 466 gipdavSTNLTACAVVRTKSPEGE-------RLTADHIRNI---VEHHLS--GAYHIRgGVYFIDSLPKTPNDKLQRRKV 533
Cdd:cd05908 418 ------LGRVVACGVNNSNTRNEEifcfiehRKSEDDFYPLgkkIKKHLNkrGGWQIN-EVLPIRRIPKTTSGKVKRYEL 490
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
54-534 |
5.16e-22 |
|
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: 99.43 E-value: 5.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 54 ELTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNSTYLTSVIIAALLRGIPINPLHPEFTEETVKYMYDITEPKVIFCD 133
Cdd:cd05915 24 RTTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVLLFD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 134 VENYHIIKTVNGKLQNPAKIYLVNGKLEGVLDISEMLNDEdsitaaaYVPCPKLHGDHTAFIVCSSGTTGMPKGVTRSHR 213
Cdd:cd05915 104 PNLLPLVEAIRGELKTVQHFVVMDEKAPEGYLAYEEALGE-------EADPVRVPERAACGMAYTTGTTGLPKGVVYSHR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 214 SLLCNCK-----NPNTYTRDSVLLSFSPLYWISG-TIILLASLLNG---CRRIITNRpysvEYLLQLVARHKVTFlFLAS 284
Cdd:cd05915 177 ALVLHSLaaslvDGTALSEKDVVLPVVPMFHVNAwCLPYAATLVGAkqvLPGPRLDP----ASLVELFDGEGVTF-TAGV 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 285 HQIALLSKHDSDVMElKAQLQSIRVLIGAGSKvcKAVCRRMYELiGNQRFVVGYGLSEMGGLSknvggpVGC----EGKV 360
Cdd:cd05915 252 PTVWLALADYLESTG-HRLKTLRRLVVGGSAA--PRSLIARFER-MGVEVRQGYGLTETSPVV------VQNfvksHLES 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 361 MRNVE-LR---------------VLDKLKM--PLGINEVGIIYARLRFKWAGYYRNPEATRrALSSDGMWFRTGDIGYLD 422
Cdd:cd05915 322 LSEEEkLTlkaktglpiplvrlrVADEEGRpvPKDGKALGEVQLKGPWITGGYYGNEEATR-SALTPDGFFRTGDIAVWD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 423 SEGYLYIQTRDTDVFKFNNFQIYPEQIEEFILRLPGVSEACVFGIPDAvSTNLTACAVVRTKSPEGERltaDHIRNIVEH 502
Cdd:cd05915 401 EEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHP-KWQERPLAVVVPRGEKPTP---EELNEHLLK 476
|
490 500 510
....*....|....*....|....*....|..
gi 19922652 503 HLSGAYHIRGGVYFIDSLPKTPNDKLqRRKVL 534
Cdd:cd05915 477 AGFAKWQLPDAYVFAEEIPRTSAGKF-LKRAL 507
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
52-531 |
1.28e-21 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 99.86 E-value: 1.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 52 GQELTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNSTYLTSVIIAALLRGIPINPLHPEFTEETVKYMyditepkvif 131
Cdd:PRK05691 1154 GGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYM---------- 1223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 132 cdvenyhiiktvngkLQNP-AKIYLVNGKLEGVLDISEMLN--DEDSITAAAY---VPCPKLHGDHTAFIVCSSGTTGMP 205
Cdd:PRK05691 1224 ---------------LADSgVELLLTQSHLLERLPQAEGVSaiALDSLHLDSWpsqAPGLHLHGDNLAYVIYTSGSTGQP 1288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 206 KGVTRSHRSLLCNCK-NPNTYTRDS--VLLSFSPLYWISGTIILLASLLNGCRRIIT-----NRPYSveyLLQLVARHKV 277
Cdd:PRK05691 1289 KGVGNTHAALAERLQwMQATYALDDsdVLMQKAPISFDVSVWECFWPLITGCRLVLAgpgehRDPQR---IAELVQQYGV 1365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 278 TFLFLASHQIALLskhdsdVME-LKAQLQSIRVLIGAGSKVCKAVCRRMYELIGNQRFVVGYGLSEMG------------ 344
Cdd:PRK05691 1366 TTLHFVPPLLQLF------IDEpLAAACTSLRRLFSGGEALPAELRNRVLQRLPQVQLHNRYGPTETAinvthwqcqaed 1439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 345 GLSKNVGGPVGcegkvmrNVELRVLD-KLK-MPLGI-NEV---GIIYARlrfkwaGYYRNPEATRR-----ALSSDGM-W 412
Cdd:PRK05691 1440 GERSPIGRPLG-------NVLCRVLDaELNlLPPGVaGELcigGAGLAR------GYLGRPALTAErfvpdPLGEDGArL 1506
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 413 FRTGDIGYLDSEGYL-YIQTRDTDVfKFNNFQIYPEQIEEFILRLPGVSEACVFGIPDAVSTNLtacaVVRTKSPEGERL 491
Cdd:PRK05691 1507 YRTGDRARWNADGALeYLGRLDQQV-KLRGFRVEPEEIQARLLAQPGVAQAAVLVREGAAGAQL----VGYYTGEAGQEA 1581
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 19922652 492 TADHIRNIVEHHLSgAYHIRGGVYFIDSLPKTPNDKLQRR 531
Cdd:PRK05691 1582 EAERLKAALAAELP-EYMVPAQLIRLDQMPLGPSGKLDRR 1620
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
198-540 |
1.83e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 97.89 E-value: 1.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 198 SSGTTGMPKGVTRSHRSLLCN---CKNPNTYTRDSVLLSFSPLYWISGTIILLASLLNGCRrIITNRPYSVEYLLQLVAR 274
Cdd:PRK06164 189 TSGTTSGPKLVLHRQATLLRHaraIARAYGYDPGAVLLAALPFCGVFGFSTLLGALAGGAP-LVCEPVFDAARTARALRR 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 275 HKVTFLFLASHQIALLSkhdsDVMELKAQLQSIRVL-----IGAGSKVCKAVCRRMYELIGNqrfvvgYGLSEMGGL--- 346
Cdd:PRK06164 268 HRVTHTFGNDEMLRRIL----DTAGERADFPSARLFgfasfAPALGELAALARARGVPLTGL------YGSSEVQALval 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 347 ---------SKNVGG-PVGCEGKVmrnvelRVLDKLK---MPLGinEVGIIYARLRFKWAGYYRNPEATRRALSSDGmWF 413
Cdd:PRK06164 338 qpatdpvsvRIEGGGrPASPEARV------RARDPQDgalLPDG--ESGEIEIRAPSLMRGYLDNPDATARALTDDG-YF 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 414 RTGDIGYLDSEGYLYIQTRDTDVFKFNNFQIYPEQIEEFILRLPGVSEACVFGIpdAVSTNLTACAVVRTKspEGERLTA 493
Cdd:PRK06164 409 RTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGA--TRDGKTVPVAFVIPT--DGASPDE 484
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 19922652 494 DHIRNIVEHHLSGaYHIRGGVYFIDSLPKTPND---KLQRRKVLGLVQQL 540
Cdd:PRK06164 485 AGLMAACREALAG-FKVPARVQVVEAFPVTESAngaKIQKHRLREMAQAR 533
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
202-525 |
2.16e-21 |
|
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: 95.45 E-value: 2.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 202 TGMPKGVTRSHRSLLC---NCKNPNTYTRDSVLLSFSPLYWISGTIILLASLLNGCRRIITNRpYSVEYLLQLVARHKVT 278
Cdd:cd17636 12 SGRPNGALLSHQALLAqalVLAVLQAIDEGTVFLNSGPLFHIGTLMFTLATFHAGGTNVFVRR-VDAEEVLELIEAERCT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 279 FLFLAS---HQIALL---SKHDSDVMELKAQLQSIRVLIGAGSKvckAVCRRMYelignqrfvvGYGLSEMGGLS--KNV 350
Cdd:cd17636 91 HAFLLPptiDQIVELnadGLYDLSSLRSSPAAPEWNDMATVDTS---PWGRKPG----------GYGQTEVMGLAtfAAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 351 GGP-VGCEGKVMRNVELRVLDKLKMPLGINEVGIIYARLRFKWAGYYRNPEAT-RRalSSDGmWFRTGDIGYLDSEGYL- 427
Cdd:cd17636 158 GGGaIGGAGRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNaRR--TRGG-WHHTNDLGRREPDGSLs 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 428 YIQTRdTDVFKFNNFQIYPEQIEEFILRLPGVSEACVFGIPDAVSTNlTACAVVRTKspEGERLTADhirNIVEH--HLS 505
Cdd:cd17636 235 FVGPK-TRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQ-SVKAIVVLK--PGASVTEA---ELIEHcrARI 307
|
330 340
....*....|....*....|
gi 19922652 506 GAYHIRGGVYFIDSLPKTPN 525
Cdd:cd17636 308 ASYKKPKSVEFADALPRTAG 327
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
55-532 |
2.48e-21 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 97.77 E-value: 2.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 55 LTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNSTYLTSVIIAALLRG-------IPINPLHPEFTEETVKYMYDITEP 127
Cdd:PRK09192 50 LPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGlvpvplpLPMGFGGRESYIAQLRGMLASAQP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 128 KVIFCDVEnyhIIKTVNGklqnpakiylVNGKLEGVLDIS-EMLNDEDsitaAAYVPCPKLHGDHTAFIVCSSGTTGMPK 206
Cdd:PRK09192 130 AAIITPDE---LLPWVNE----------ATHGNPLLHVLShAWFKALP----EADVALPRPTPDDIAYLQYSSGSTRFPR 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 207 GVTRSHRSLLCNCknpNTYTRDSVLL-------SFSPLYWISGTI-ILLASLLNGcrriitnrpYSVEYL---------- 268
Cdd:PRK09192 193 GVIITHRALMANL---RAISHDGLKVrpgdrcvSWLPFYHDMGLVgFLLTPVATQ---------LSVDYLptrdfarrpl 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 269 --LQLVARHKVTFLFLAS--HQIALLSKHDSDVMELkaQLQSIRVL-IGAG---SKVCKAVCRRMYELIGNQR-FVVGYG 339
Cdd:PRK09192 261 qwLDLISRNRGTISYSPPfgYELCARRVNSKDLAEL--DLSCWRVAgIGADmirPDVLHQFAEAFAPAGFDDKaFMPSYG 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 340 LSEM-------------------------GGLSKNVGGP-------VGCeGKVMRNVELRVLDKLKMPLGINEVGIIYAR 387
Cdd:PRK09192 339 LAEAtlavsfsplgsgivveevdrdrleyQGKAVAPGAEtrrvrtfVNC-GKALPGHEIEIRNEAGMPLPERVVGHICVR 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 388 LRFKWAGYYRNPEATRrALSSDGmWFRTGDIGYLdSEGYLYIQTRDTDVFKFNNFQIYPEQIEEFILRLPGV--SEACVF 465
Cdd:PRK09192 418 GPSLMSGYFRDEESQD-VLAADG-WLDTGDLGYL-LDGYLYITGRAKDLIIINGRNIWPQDIEWIAEQEPELrsGDAAAF 494
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19922652 466 GIPDAVSTNLTACAVVRTKSPEGERLTADHIRNIV--EHHLSGAYHIRGGvyfiDSLPKTPNDKLQRRK 532
Cdd:PRK09192 495 SIAQENGEKIVLLVQCRISDEERRGQLIHALAALVrsEFGVEAAVELVPP----HSLPRTSSGKLSRAK 559
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
52-531 |
7.09e-21 |
|
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: 95.45 E-value: 7.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 52 GQELTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNSTYLTSVIIAALLRG---IPINPLHPEfteETVKYMYDITEPK 128
Cdd:cd17643 10 DRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGgayVPIDPAYPV---ERIAFILADSGPS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 129 VIFCDvenyhiiktvngklqnpakiylvngklegvldisemlndedsitaaayvpcpklhGDHTAFIVCSSGTTGMPKGV 208
Cdd:cd17643 87 LLLTD-------------------------------------------------------PDDLAYVIYTSGSTGRPKGV 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 209 TRSHRS---LLCNCKNPNTYTRDSVLLSFSPL-----YW-ISGtiillaSLLNGCRRIITnrPYSV----EYLLQLVARH 275
Cdd:cd17643 112 VVSHANvlaLFAATQRWFGFNEDDVWTLFHSYafdfsVWeIWG------ALLHGGRLVVV--PYEVarspEDFARLLRDE 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 276 KVTFLflasHQI--ALLSKHDSDVMELKAQLqSIRVLIGAGSKVCKAVCRRMYELIGNQR--FVVGYGLSE--------- 342
Cdd:cd17643 184 GVTVL----NQTpsAFYQLVEAADRDGRDPL-ALRYVIFGGEALEAAMLRPWAGRFGLDRpqLVNMYGITEttvhvtfrp 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 343 ------MGGLSKNVGGPVGcegkvmrNVELRVLDKLKMPLGINEVGIIY------ARlrfkwaGYYRNPE--ATRRALSS 408
Cdd:cd17643 259 ldaadlPAAAASPIGRPLP-------GLRVYVLDADGRPVPPGVVGELYvsgagvAR------GYLGRPEltAERFVANP 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 409 DGM----WFRTGDIGYLDSEGYL-YIQTRDTDVfKFNNFQIYPEQIEEFILRLPGVSEACVFGIPDAVSTNLTACAVVrt 483
Cdd:cd17643 326 FGGpgsrMYRTGDLARRLPDGELeYLGRADEQV-KIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVV-- 402
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 19922652 484 kSPEGERLTADHIRNIVEHHLSGayHIRGGVY-FIDSLPKTPNDKLQRR 531
Cdd:cd17643 403 -ADDGAAADIAELRALLKELLPD--YMVPARYvPLDALPLTVNGKLDRA 448
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
194-527 |
6.72e-20 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 91.29 E-value: 6.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 194 FIVCSSGTTGMPKGVTRSHRSLLCNCKNPNTYTR-----------------DSVLLSFSPLywISGTIILLA-SLLNGCR 255
Cdd:cd05924 7 YILYTGGTTGMPKGVMWRQEDIFRMLMGGADFGTgeftpsedahkaaaaaaGTVMFPAPPL--MHGTGSWTAfGGLLGGQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 256 RIITNRP-YSVEYLLQLVARHKVTFLFLASHQIA------LLSKHDSDvmelkaqLQSIRVLIGAGSKVCKAVCRRMYEL 328
Cdd:cd05924 85 TVVLPDDrFDPEEVWRTIEKHKVTSMTIVGDAMArplidaLRDAGPYD-------LSSLFAISSGGALLSPEVKQGLLEL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 329 IGNQRFVVGYGLSE--MGGLSKNVGGPVGCEGKVMRNVELRVLDK--LKMPLGINEVGIIyARLRFKWAGYYRNPEATRR 404
Cdd:cd05924 158 VPNITLVDAFGSSEtgFTGSGHSAGSGPETGPFTRANPDTVVLDDdgRVVPPGSGGVGWI-ARRGHIPLGYYGDEAKTAE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 405 ALSS-DGM-WFRTGDIGYLDSEGYLYIQTRDTDVFKFNNFQIYPEQIEEFILRLPGVSEACVFGIPDAVSTNLTAcAVVR 482
Cdd:cd05924 237 TFPEvDGVrYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQEVV-AVVQ 315
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 19922652 483 TKspEGERLTADHIRNIVEHHLSGaYHIRGGVYFIDSLPKTPNDK 527
Cdd:cd05924 316 LR--EGAGVDLEELREHCRTRIAR-YKLPKQVVFVDEIERSPAGK 357
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
66-466 |
1.02e-19 |
|
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: 92.28 E-value: 1.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 66 RIAQAFKRLGLRR--GDVVGISANNSTYLTSVIIAALLRGIPINPLHPEFTEETVKYMYDITEPKVIFCDvenyhiiKTV 143
Cdd:cd05927 17 NIGSALRSLGGKPapASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVFCD-------AGV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 144 NgklqnpakiylvngklegVLDISEMLNDEDSITAAAYVPCPklhgDHTAFIVCSSGTTGMPKGVTRSHRSLLCNC---- 219
Cdd:cd05927 90 K------------------VYSLEEFEKLGKKNKVPPPPPKP----EDLATICYTSGTTGNPKGVMLTHGNIVSNVagvf 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 220 ---KNPNTYTRDSVLLSFSPLYWISGTIILLASLLNGCR--------RIITN-----RPY---SVEYLLQLV-------- 272
Cdd:cd05927 148 kilEILNKINPTDVYISYLPLAHIFERVVEALFLYHGAKigfysgdiRLLLDdikalKPTvfpGVPRVLNRIydkifnkv 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 273 ----ARHKVTFLFLASHQIALLSKHDS--DVM-------ELKAQLQS-IRVLIGAGSKVCKAVCRRMYELIGNQrFVVGY 338
Cdd:cd05927 228 qakgPLKRKLFNFALNYKLAELRSGVVraSPFwdklvfnKIKQALGGnVRLMLTGSAPLSPEVLEFLRVALGCP-VLEGY 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 339 GLSEMGGLSK----------NVGGPVGCegkvmrnVELRVLDKLKM---PLGINEVGIIYARLRFKWAGYYRNPEATRRA 405
Cdd:cd05927 307 GQTECTAGATltlpgdtsvgHVGGPLPC-------AEVKLVDVPEMnydAKDPNPRGEVCIRGPNVFSGYYKDPEKTAEA 379
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19922652 406 LSSDGmWFRTGDIGYLDSEGYLYIQTRDTDVFKFNnfQ---IYPEQIEEFILRLPGVSEACVFG 466
Cdd:cd05927 380 LDEDG-WLHTGDIGEWLPNGTLKIIDRKKNIFKLS--QgeyVAPEKIENIYARSPFVAQIFVYG 440
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
36-531 |
1.27e-19 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 93.48 E-value: 1.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 36 VLQINADQVMQICDTT-----GQELTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNSTYLTSVIIAALLRGIPINPLH 110
Cdd:PRK12316 3059 VHRLFEEQVERTPDAValafgEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLD 3138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 111 PEFTEETVKYMYDITEPKVIFCdvenyhiiktvngklQNPAKIYLVNGklegvldISEMLNDEDSITAAAYVPCPKLHGD 190
Cdd:PRK12316 3139 PEYPEERLAYMLEDSGAQLLLS---------------QSHLRLPLAQG-------VQVLDLDRGDENYAEANPAIRTMPE 3196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 191 HTAFIVCSSGTTGMPKGVTRSHRSL---LCNCKNPNTYTRDSVLLSFSPLYWISGTIILLASLLNGCRRII--TNRPYSV 265
Cdd:PRK12316 3197 NLAYVIYTSGSTGKPKGVGIRHSALsnhLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLagPEDWRDP 3276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 266 EYLLQLVARHKVTFLFLASHQIA--LLSKHDSDVMELKAQLQSIRVLI--GAGSKVCKAVCRRMYELIGNQRFVVGYGLS 341
Cdd:PRK12316 3277 ALLVELINSEGVDVLHAYPSMLQafLEEEDAHRCTSLKRIVCGGEALPadLQQQVFAGLPLYNLYGPTEATITVTHWQCV 3356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 342 EMGGLSKNVGGPVGcegkvmrNVELRVLDKLKMPLGINEVGIIYARLRFKWAGYYRNPEATRRALSSD-----GMWFRTG 416
Cdd:PRK12316 3357 EEGKDAVPIGRPIA-------NRACYILDGSLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDpfvpgERLYRTG 3429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 417 DIGYLDSEGYLYIQTRDTDVFKFNNFQIYPEQIEEFILRLPGVSEACVFgipDAVSTNLTACAVVRTKSPEGERLTADHI 496
Cdd:PRK12316 3430 DLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVL---AVDGRQLVAYVVPEDEAGDLREALKAHL 3506
|
490 500 510
....*....|....*....|....*....|....*
gi 19922652 497 RNIVEHHLSGAYHIrggvyFIDSLPKTPNDKLQRR 531
Cdd:PRK12316 3507 KASLPEYMVPAHLL-----FLERMPLTPNGKLDRK 3536
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
47-540 |
1.50e-19 |
|
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: 91.45 E-value: 1.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 47 ICDTTGQeLTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNSTYLTSVIIAALLRG---IPINPLHPEfteETVKYMYD 123
Cdd:cd05918 18 VCAWDGS-LTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGgafVPLDPSHPL---QRLQEILQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 124 ITEPKVIFCDvenyhiiktvngklqnpakiylvngklegvldisemlndedsitaaayvpcpklHGDHTAFIVCSSGTTG 203
Cdd:cd05918 94 DTGAKVVLTS------------------------------------------------------SPSDAAYVIFTSGSTG 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 204 MPKGVTRSHRSLLCNCK--NPNT-YTRDSVLLSFSPlYWISGTI--ILLASLLNGC-----RRIITNRpysveyLLQLVA 273
Cdd:cd05918 120 KPKGVVIEHRALSTSALahGRALgLTSESRVLQFAS-YTFDVSIleIFTTLAAGGClcipsEEDRLND------LAGFIN 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 274 RHKVTFLFLASHQIALLSkhdsdvmelKAQLQSIRVLIGAGSKVCKAVCRRmyeLIGNQRFVVGYGLSE----------- 342
Cdd:cd05918 193 RLRVTWAFLTPSVARLLD---------PEDVPSLRTLVLGGEALTQSDVDT---WADRVRLINAYGPAEctiaatvspvv 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 343 MGGLSKNVGGPVGCegkVMRNVELRVLDKLkMPLG-INEV---GIIYARlrfkwaGYYRNPEATRRALSSDGMW------ 412
Cdd:cd05918 261 PSTDPRNIGRPLGA---TCWVVDPDNHDRL-VPIGaVGELlieGPILAR------GYLNDPEKTAAAFIEDPAWlkqegs 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 413 ------FRTGDIGYLDSEGYL-YIQTRDTDVfKFNNFQIYPEQIEEFILR-LPGVSEACVFGIP---DAVSTNLTACAVV 481
Cdd:cd05918 331 grgrrlYRTGDLVRYNPDGSLeYVGRKDTQV-KIRGQRVELGEIEHHLRQsLPGAKEVVVEVVKpkdGSSSPQLVAFVVL 409
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19922652 482 RTKSPEGE-------------RLTADHIRNIVEHHLSgAYHIRgGVYF-IDSLPKTPNDKLQRRKVLGLVQQL 540
Cdd:cd05918 410 DGSSSGSGdgdslflepsdefRALVAELRSKLRQRLP-SYMVP-SVFLpLSHLPLTASGKIDRRALRELAESL 480
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
51-531 |
1.62e-19 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 91.93 E-value: 1.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 51 TGQE--LTGAQLAQQSARIAQAFKRLGLRRGDVVGIsannstYLTSVIIA--ALLRGIPINPLHP----EFTEETVKYMY 122
Cdd:PRK10524 79 TDEErtYTFRQLHDEVNRMAAMLRSLGVQRGDRVLI------YMPMIAEAafAMLACARIGAIHSvvfgGFASHSLAARI 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 123 DITEPKVIF--------CDVENY-----HIIKTVNGKlqnPAKIYLVNGKLEGVLDISEMLNDEDSITAA---AYVPCPK 186
Cdd:PRK10524 153 DDAKPVLIVsadagsrgGKVVPYkplldEAIALAQHK---PRHVLLVDRGLAPMARVAGRDVDYATLRAQhlgARVPVEW 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 187 LHGDHTAFIVCSSGTTGMPKGVTR-----------SHRSLLCnCKNPNTYtrdsvlLSFSPLYWISG-TIILLASLLNGC 254
Cdd:PRK10524 230 LESNEPSYILYTSGTTGKPKGVQRdtggyavalatSMDTIFG-GKAGETF------FCASDIGWVVGhSYIVYAPLLAGM 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 255 RRIITN----RPySVEYLLQLVARHKVTFLFLASHQIALLSKHDSDVMElKAQLQSIRVLIGAGSKVCKAVCRRMYELIG 330
Cdd:PRK10524 303 ATIMYEglptRP-DAGIWWRIVEKYKVNRMFSAPTAIRVLKKQDPALLR-KHDLSSLRALFLAGEPLDEPTASWISEALG 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 331 nqRFVV-GYGLSEMG----GLSKNVGG-PV--GCEGKVMRNVELRVLDKLK-MPLGINEVGI--IYARL----------- 388
Cdd:PRK10524 381 --VPVIdNYWQTETGwpilAIARGVEDrPTrlGSPGVPMYGYNVKLLNEVTgEPCGPNEKGVlvIEGPLppgcmqtvwgd 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 389 --RFKwAGYYRnpeatrralSSDGMWFRTGDIGYLDSEGYLYIQTRDTDVFKFNNFQIYPEQIEEFILRLPGVSEACVFG 466
Cdd:PRK10524 459 ddRFV-KTYWS---------LFGRQVYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVG 528
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 467 IPDAVSTNLTACAVV-----RTKSPEGERLTADHIRNIVEHHLsGAYHIRGGVYFIDSLPKTPNDKLQRR 531
Cdd:PRK10524 529 VKDALKGQVAVAFVVpkdsdSLADREARLALEKEIMALVDSQL-GAVARPARVWFVSALPKTRSGKLLRR 597
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
59-533 |
2.33e-19 |
|
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: 91.37 E-value: 2.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 59 QLAQQSARIAQAF-KRLGLRRGDVVGISANNSTYLTSVIIAALLRGIPINPLHPEFTEETVKYMYDITEPKVIFCDVENY 137
Cdd:cd05928 46 ELGSLSRKAANVLsGACGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSDELA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 138 HIIKTVNGKLQNPAKIYLVNGK-LEGVLDISEMLNDedsitAAAYVPCPKLHGDHTAFIVCSSGTTGMPKGVTRSHRSLL 216
Cdd:cd05928 126 PEVDSVASECPSLKTKLLVSEKsRDGWLNFKELLNE-----ASTEHHCVETGSQEPMAIYFTSGTTGSPKMAEHSHSSLG 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 217 CNCKNPNTYTRD----SVLLSFSPLYWISGTI-ILLASLLNGCRRIITNRP-YSVEYLLQLVARHKVTFLFLASHQIALL 290
Cdd:cd05928 201 LGLKVNGRYWLDltasDIMWNTSDTGWIKSAWsSLFEPWIQGACVFVHHLPrFDPLVILKTLSSYPITTFCGAPTVYRML 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 291 SKHDSDvmelKAQLQSIRVLIGAGSKVCKAVCRRMYELIGNQRFVvGYGLSEMGGLSKNVGG----PvGCEGKVMRNVEL 366
Cdd:cd05928 281 VQQDLS----SYKFPSLQHCVTGGEPLNPEVLEKWKAQTGLDIYE-GYGQTETGLICANFKGmkikP-GSMGKASPPYDV 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 367 RVLDKLKMPLGINEVGIIYARLR-----FKWAGYYRNPEATrrALSSDGMWFRTGDIGYLDSEGYLYIQTRDTDVFKFNN 441
Cdd:cd05928 355 QIIDDNGNVLPPGTEGDIGIRVKpirpfGLFSGYVDNPEKT--AATIRGDFYLTGDRGIMDEDGYFWFMGRADDVINSSG 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 442 FQIYPEQIEEFILRLPGVSEACVFGIPDAVSTNLTACAVVRT---KSPEGERLTA---DHIRNIvehhlSGAYHIRGGVY 515
Cdd:cd05928 433 YRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLApqfLSHDPEQLTKelqQHVKSV-----TAPYKYPRKVE 507
|
490
....*....|....*...
gi 19922652 516 FIDSLPKTPNDKLQRRKV 533
Cdd:cd05928 508 FVQELPKTVTGKIQRNEL 525
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
56-530 |
2.48e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 91.16 E-value: 2.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 56 TGAQLAQQSARIAQAFKRLGLRRGDVVGISANNstyltsviIAALLR---GIP-----INPLHPEFTEETVKYMYDITEP 127
Cdd:PRK08162 45 TWAETYARCRRLASALARRGIGRGDTVAVLLPN--------IPAMVEahfGVPmagavLNTLNTRLDAASIAFMLRHGEA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 128 KVIFCDVENYHIIKTVNGKLQNPaKIYLVN--------GKLEGVLDISEMLNDEDSITAAAYvpcPKLHGDHTAfIVCSS 199
Cdd:PRK08162 117 KVLIVDTEFAEVAREALALLPGP-KPLVIDvddpeypgGRFIGALDYEAFLASGDPDFAWTL---PADEWDAIA-LNYTS 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 200 GTTGMPKGVTRSHRSLLCNCKNpNTYTRD----SVLLSFSPLYWISG-----TIILLASLlNGCRRIITNRPysveyLLQ 270
Cdd:PRK08162 192 GTTGNPKGVVYHHRGAYLNALS-NILAWGmpkhPVYLWTLPMFHCNGwcfpwTVAARAGT-NVCLRKVDPKL-----IFD 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 271 LVARHKVTFLFLAS--HQiALLSKHDsdvmELKAQL-QSIRVLIgAGSKVCKAVCRRMyELIGnqrFVVG--YGLSEmgg 345
Cdd:PRK08162 265 LIREHGVTHYCGAPivLS-ALINAPA----EWRAGIdHPVHAMV-AGAAPPAAVIAKM-EEIG---FDLThvYGLTE--- 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 346 lsknVGGPVG-CEG---------------KVMRNV------ELRVLDKLKM---PLGINEVGIIYARLRFKWAGYYRNPE 400
Cdd:PRK08162 332 ----TYGPATvCAWqpewdalplderaqlKARQGVryplqeGVTVLDPDTMqpvPADGETIGEIMFRGNIVMKGYLKNPK 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 401 ATRRALSsdGMWFRTGDIGYLDSEGYLYIQTRDTDVFKFNNFQIYPEQIEEFILRLPGVSEACVFGIPDAvSTNLTACAV 480
Cdd:PRK08162 408 ATEEAFA--GGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDP-KWGEVPCAF 484
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 19922652 481 VRTKspEGERLTADHIRNIVEHHLSGaYHIRGGVYFiDSLPKTPNDKLQR 530
Cdd:PRK08162 485 VELK--DGASATEEEIIAHCREHLAG-FKVPKAVVF-GELPKTSTGKIQK 530
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
177-533 |
2.98e-19 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 89.33 E-value: 2.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 177 TAAAYVPCPKLHGDHT-----------------AFIVCSSGTTGMPKGVTRSHRSLLCNCKNpnTYTR----DSVLLSFs 235
Cdd:PRK07824 5 RAPALLPVPAQDERRAallrdalrvgepidddvALVVATSGTTGTPKGAMLTAAALTASADA--THDRlggpGQWLLAL- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 236 PLYWISGTIILLASLLNGCRRIITNRP--YSVEYLLQLVARHKV--TFLFLASHQialLSK--HDSDVMELKAQLQSirV 309
Cdd:PRK07824 82 PAHHIAGLQVLVRSVIAGSEPVELDVSagFDPTALPRAVAELGGgrRYTSLVPMQ---LAKalDDPAATAALAELDA--V 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 310 LIGaGSKVCKAVCRRMYELigNQRFVVGYGLSEMGGlsknvggpvGC--EGKVMRNVELRVLDKlKMPLGinevGIIYAR 387
Cdd:PRK07824 157 LVG-GGPAPAPVLDAAAAA--GINVVRTYGMSETSG---------GCvyDGVPLDGVRVRVEDG-RIALG----GPTLAK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 388 lrfkwaGYyRNPEaTRRALSSDGmWFRTGDIGYLDSeGYLYIQTRDTDVFKFNNFQIYPEQIEEFILRLPGVSEACVFGI 467
Cdd:PRK07824 220 ------GY-RNPV-DPDPFAEPG-WFRTDDLGALDD-GVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGL 289
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19922652 468 PDAVSTNLTACAVVRTKSPegeRLTADHIRNIVEHHLSgAYHIRGGVYFIDSLPKTPNDKLQRRKV 533
Cdd:PRK07824 290 PDDRLGQRVVAAVVGDGGP---APTLEALRAHVARTLD-RTAAPRELHVVDELPRRGIGKVDRRAL 351
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
25-470 |
3.09e-19 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 91.09 E-value: 3.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 25 PEMTLGEVIMRVLQINADQVMQICDttGQELTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNS-TYLTSV-------I 96
Cdd:PRK08279 35 SKRSLGDVFEEAAARHPDRPALLFE--DQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRpEYLAAWlglaklgA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 97 IAALL----RGipinplhpefteETVKYMYDITEPKVIFCDVENYHIIKTVNGKLQNPAKIYLVNGK----LEGVLDISE 168
Cdd:PRK08279 113 VVALLntqqRG------------AVLAHSLNLVDAKHLIVGEELVEAFEEARADLARPPRLWVAGGDtlddPEGYEDLAA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 169 MLNDEDSITAAAyvpCPKLHGDHTAFIVCSSGTTGMPKGVTRSHR---------SLLCNCknpntyTRDSVLLSFSPLYW 239
Cdd:PRK08279 181 AAAGAPTTNPAS---RSGVTAKDTAFYIYTSGTTGLPKAAVMSHMrwlkamggfGGLLRL------TPDDVLYCCLPLYH 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 240 ISGTIILLASLLNGCRRIITNRPYSVEYLLQLVARHKVTFL--------FLASHQIallSKHDSDvmelkaqlQSIRVLI 311
Cdd:PRK08279 252 NTGGTVAWSSVLAAGATLALRRKFSASRFWDDVRRYRATAFqyigelcrYLLNQPP---KPTDRD--------HRLRLMI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 312 GAGskvckavcrrmyeLIGN------QRFVV-----GYGLSEmGGLS----KNVGGPVG-CEGKVMRNVEL--------- 366
Cdd:PRK08279 321 GNG-------------LRPDiwdefqQRFGIprileFYAASE-GNVGfinvFNFDGTVGrVPLWLAHPYAIvkydvdtge 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 367 --RVLDKLKMPLGINEVGI----IYARLRFKwaGyYRNPEATRRALSSDGM-----WFRTGDIGYLDSEGYLYIQTRDTD 435
Cdd:PRK08279 387 pvRDADGRCIKVKPGEVGLligrITDRGPFD--G-YTDPEASEKKILRDVFkkgdaWFNTGDLMRDDGFGHAQFVDRLGD 463
|
490 500 510
....*....|....*....|....*....|....*..
gi 19922652 436 VFKFNNFQIYPEQIEEFILRLPGVSEACVFG--IPDA 470
Cdd:PRK08279 464 TFRWKGENVATTEVENALSGFPGVEEAVVYGveVPGT 500
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
53-459 |
3.85e-19 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 90.73 E-value: 3.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 53 QELTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNSTYLTSVIIAALLRGIP---INP-------------LHPE-Fte 115
Cdd:PRK09274 40 DELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGAVpvlVDPgmgiknlkqclaeAQPDaF-- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 116 etvkymydITEPKVifcdvenyHIIKTVNGKlQNPAKIYLVN---GKLEGVLDISEMLNDedsiTAAAYVPCPKLHGDHT 192
Cdd:PRK09274 118 --------IGIPKA--------HLARRLFGW-GKPSVRRLVTvggRLLWGGTTLATLLRD----GAAAPFPMADLAPDDM 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 193 AFIVCSSGTTGMPKGVTRSHRSLLCNCKN-PNTY-----TRDsvLLSFsPLYwisgtiillaSLLN---GCRRIITN--- 260
Cdd:PRK09274 177 AAILFTSGSTGTPKGVVYTHGMFEAQIEAlREDYgiepgEID--LPTF-PLF----------ALFGpalGMTSVIPDmdp 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 261 -RPYSV--EYLLQLVARHKVTFLFLAShqiALLSKHDSDVMELKAQLQSIRVLIGAGSKVCKAVCRRMYELIGNQ-RFVV 336
Cdd:PRK09274 244 tRPATVdpAKLFAAIERYGVTNLFGSP---ALLERLGRYGEANGIKLPSLRRVISAGAPVPIAVIERFRAMLPPDaEILT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 337 GYG---------------LSEMGGLSKNVGGPvgCEGKVMRNVELRVL-----------DKLKMPLGinEVGIIYAR--- 387
Cdd:PRK09274 321 PYGatealpissiesreiLFATRAATDNGAGI--CVGRPVDGVEVRIIaisdapipewdDALRLATG--EIGEIVVAgpm 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19922652 388 -LRfkwaGYYRNPEATRRALSSDG---MWFRTGDIGYLDSEGYLYIQTRDTDVFKFNNFQIYPEQIEEFILRLPGV 459
Cdd:PRK09274 397 vTR----SYYNRPEATRLAKIPDGqgdVWHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGV 468
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
55-545 |
5.26e-19 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 90.46 E-value: 5.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 55 LTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNSTYLTSVIIAALLRGIPINPLHPEFTEETVKYMYDITEPKVIFCDV 134
Cdd:PLN03102 40 FTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFVDR 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 135 -------ENYHIIKTVNGKLQNPakIYLVNGKLEGVLDISEMLNDEDSI-----TAAAYVPCPKLHGDHTAF-IVCSSGT 201
Cdd:PLN03102 120 sfeplarEVLHLLSSEDSNLNLP--VIFIHEIDFPKRPSSEELDYECLIqrgepTPSLVARMFRIQDEHDPIsLNYTSGT 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 202 TGMPKGVTRSHR-SLLCNCKNPNTYTRDS--VLLSFSPLYWISGTIILLASLLNG----CRRIITnrpysVEYLLQLVAR 274
Cdd:PLN03102 198 TADPKGVVISHRgAYLSTLSAIIGWEMGTcpVYLWTLPMFHCNGWTFTWGTAARGgtsvCMRHVT-----APEIYKNIEM 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 275 HKVTFLFLASHQIALLSKHDSdvMELKAQLQSIRVLIGAGSKvcKAVCRRMYELIGNQrFVVGYGLSEmgglsknVGGPV 354
Cdd:PLN03102 273 HNVTHMCCVPTVFNILLKGNS--LDLSPRSGPVHVLTGGSPP--PAALVKKVQRLGFQ-VMHAYGLTE-------ATGPV 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 355 -GCEGKVMRN-------VELRVLDKLKMpLGINEV------------------GIIYARLRFKWAGYYRNPEATRRALSS 408
Cdd:PLN03102 341 lFCEWQDEWNrlpenqqMELKARQGVSI-LGLADVdvknketqesvprdgktmGEIVIKGSSIMKGYLKNPKATSEAFKH 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 409 DgmWFRTGDIGYLDSEGYLYIQTRDTDVFKFNNFQIYPEQIEEFILRLPGVSEACVFGIPDAVSTNlTACA-VVRTKSPE 487
Cdd:PLN03102 420 G--WLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGE-TPCAfVVLEKGET 496
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19922652 488 GERLTADHI----RNIVEHHLSGAYHIR--GGVYFIDSLPKTPNDKLQRRKVLGLVQQLELKAE 545
Cdd:PLN03102 497 TKEDRVDKLvtreRDLIEYCRENLPHFMcpRKVVFLQELPKNGNGKILKPKLRDIAKGLVVEDE 560
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
55-533 |
6.42e-19 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 89.95 E-value: 6.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 55 LTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNSTYLTSVIIAALLRGIPINPLHPEF--TEETVK--------YMYDI 124
Cdd:PRK05852 44 ISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALpiAEQRVRsqaagarvVLIDA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 125 TEPkvifCD-----VENYHIIKTVNGklqnpakiylVNGKLEGVLDISemLNDEDSITAAAYVPCPKLHGDhtAFIVCSS 199
Cdd:PRK05852 124 DGP----HDraeptTRWWPLTVNVGG----------DSGPSGGTLSVH--LDAATEPTPATSTPEGLRPDD--AMIMFTG 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 200 GTTGMPKGVTRSHRSLLCN----CKNPNTYTRDSVLlSFSPLYWISGTI-ILLASLLNGCRRIITNR-PYSVEYLLQLVA 273
Cdd:PRK05852 186 GTTGLPKMVPWTHANIASSvraiITGYRLSPRDATV-AVMPLYHGHGLIaALLATLASGGAVLLPARgRFSAHTFWDDIK 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 274 RHKVTFlFLAS---HQIaLLSKHDSDVMELK-AQLQSIRVligagskvCKAVCRRMYELIGNQRF----VVGYGLSEMG- 344
Cdd:PRK05852 265 AVGATW-YTAVptiHQI-LLERAATEPSGRKpAALRFIRS--------CSAPLTAETAQALQTEFaapvVCAFGMTEATh 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 345 -GLSKNVGG------PVGCEGKVMRN--VELRVLDKLKMPLGINEVGIIYARLRFKWAGYYRNPEATRRALSsDGmWFRT 415
Cdd:PRK05852 335 qVTTTQIEGigqtenPVVSTGLVGRStgAQIRIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDPTITAANFT-DG-WLRT 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 416 GDIGYLDSEGYLYIQTRDTDVFKFNNFQIYPEQIEEFILRLPGVSEACVFGIPDAVSTNLTACAVVrtkSPEGERLTADH 495
Cdd:PRK05852 413 GDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIV---PRESAPPTAEE 489
|
490 500 510
....*....|....*....|....*....|....*...
gi 19922652 496 IRNIVEHHLSgAYHIRGGVYFIDSLPKTPNDKLQRRKV 533
Cdd:PRK05852 490 LVQFCRERLA-AFEIPASFQEASGLPHTAKGSLDRRAV 526
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
50-537 |
7.70e-19 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 89.67 E-value: 7.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 50 TTGQ-----ELTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNSTYLTSVIIAALLRGIPINPLH--------PEFTEE 116
Cdd:PRK07768 20 VTGEpdapvRHTWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASLTMLHqptprtdlAVWAED 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 117 TVKYMYDITEPKVIFCDvenyhiiktvngklqnP--AKIYLVNGKLEGVLDISEMLndedsitAAAYVPCPKLHGDHTAF 194
Cdd:PRK07768 100 TLRVIGMIGAKAVVVGE----------------PflAAAPVLEEKGIRVLTVADLL-------AADPIDPVETGEDDLAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 195 IVCSSGTTGMPKGVTRSHRSLLCNCKNPNTYTR----DSVLLSFSPLYWISGTIILLAS-LLNGCRRI-ITNRPYSVEYL 268
Cdd:PRK07768 157 MQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEfdveTDVMVSWLPLFHDMGMVGFLTVpMYFGAELVkVTPMDFLRDPL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 269 L--QLVARHKVTFLFLASHQIALLSKhdsdVMELKAQ-----LQSIRVLIGAGSKVCKAVCRRMYEL-----IGNQRFVV 336
Cdd:PRK07768 237 LwaELISKYRGTMTAAPNFAYALLAR----RLRRQAKpgafdLSSLRFALNGAEPIDPADVEDLLDAgarfgLRPEAILP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 337 GYGLSEM----------GGL-------------------SKNVGGPVGCEGKVMRNVELRVLDKLKMPLGINEVGIIYAR 387
Cdd:PRK07768 313 AYGMAEAtlavsfspcgAGLvvdevdadllaalrravpaTKGNTRRLATLGPPLPGLEVRVVDEDGQVLPPRGVGVIELR 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 388 LRFKWAGYyRNPEATRRALSSDGmWFRTGDIGYLDSEGYLYIQTRDTDVFKFNNFQIYPEQIEEFILRLPGVSEACVFGI 467
Cdd:PRK07768 393 GESVTPGY-LTMDGFIPAQDADG-WLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVRPGNAVAV 470
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19922652 468 P-DAVSTNLTACAVVRTK---SPEGERltadHIRNIVEHHLSGAYHIRGGVYFI---DSLPKTPNDKLQRRKVLGLV 537
Cdd:PRK07768 471 RlDAGHSREGFAVAVESNafeDPAEVR----RIRHQVAHEVVAEVGVRPRNVVVlgpGSIPKTPSGKLRRANAAELV 543
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
53-531 |
8.98e-19 |
|
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: 89.06 E-value: 8.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 53 QELTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNSTYLTSVIIAALLRGIPINPLHPEFTEETVKYMYDITEPKVIFC 132
Cdd:cd17650 11 RQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYMLEDSGAKLLLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 133 DVENyhiiktvngklqnpakiylvngklegvldisemlndedsitaaayvpcpklhgdhTAFIVCSSGTTGMPKGVTRSH 212
Cdd:cd17650 91 QPED-------------------------------------------------------LAYVIYTSGTTGKPKGVMVEH 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 213 RSLLcncKNPNTYTRDSVLLSFSP----LYWISGTII---LLASLLNGCRRIITNRPYSVE--YLLQLVARHKVTFL-FL 282
Cdd:cd17650 116 RNVA---HAAHAWRREYELDSFPVrllqMASFSFDVFagdFARSLLNGGTLVICPDEVKLDpaALYDLILKSRITLMeST 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 283 ASHQIALLSKhdsdVMELKAQLQSIRVLIgAGSKVCKAVCRR-MYELIGNQ-RFVVGYGLSE-----------MGGLSKN 349
Cdd:cd17650 193 PALIRPVMAY----VYRNGLDLSAMRLLI-VGSDGCKAQDFKtLAARFGQGmRIINSYGVTEatidstyyeegRDPLGDS 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 350 VGGPVGcegKVMRNVELRVLDKLKMPLGINEVGIIYARLRFKWAGYYRNPEATRR-----ALSSDGMWFRTGDIGYLDSE 424
Cdd:cd17650 268 ANVPIG---RPLPNTAMYVLDERLQPQPVGVAGELYIGGAGVARGYLNRPELTAErfvenPFAPGERMYRTGDLARWRAD 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 425 GYLYIQTRDTDVFKFNNFQIYPEQIEEFILRLPGVSEACVFGIPDAVSTNLTACAVVRTKSPEGERLtadhiRNIVEHHL 504
Cdd:cd17650 345 GNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVREDKGGEARLCAYVVAAATLNTAEL-----RAFLAKEL 419
|
490 500
....*....|....*....|....*..
gi 19922652 505 SgAYHIRGGVYFIDSLPKTPNDKLQRR 531
Cdd:cd17650 420 P-SYMIPSYYVQLDALPLTPNGKVDRR 445
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
28-432 |
1.15e-18 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 89.98 E-value: 1.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 28 TLGEVIMRVLQINADQvMQICDTTGQELTGAQLAQQSARIAQAFKRLgLRRGDVVGISANNSTYLTSVIIAALLRG-IPI 106
Cdd:PRK08633 616 PLAEAWIDTAKRNWSR-LAVADSTGGELSYGKALTGALALARLLKRE-LKDEENVGILLPPSVAGALANLALLLAGkVPV 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 107 NpLHPEFTEETVKYMYDITEPKVI-----FCD-VENYHIIKTVngkLQNPAKIYLvngklEgvlDISEMLNDEDSITAAA 180
Cdd:PRK08633 694 N-LNYTASEAALKSAIEQAQIKTVitsrkFLEkLKNKGFDLEL---PENVKVIYL-----E---DLKAKISKVDKLTALL 761
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 181 -------------YVPCPKLhgDHTAFIVCSSGTTGMPKGVTRSHRSLLCNCKNPNT---YTRDSVLLSFSPLYWISG-T 243
Cdd:PRK08633 762 aarllparllkrlYGPTFKP--DDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDvfnLRNDDVILSSLPFFHSFGlT 839
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 244 IILLASLLNGCRRIITNRPYSVEYLLQLVARHKVTFLFLASHQIALLSKHDSdvmELKAQLQSIRVLIgAGSKVCKAVCR 323
Cdd:PRK08633 840 VTLWLPLLEGIKVVYHPDPTDALGIAKLVAKHRATILLGTPTFLRLYLRNKK---LHPLMFASLRLVV-AGAEKLKPEVA 915
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 324 RMYELIGNQRFVVGYGLSEMGG---------LSKNVGGPVGC-EGKVMR---NVELRVLDKLKM-PLGINEVGIIYARLR 389
Cdd:PRK08633 916 DAFEEKFGIRILEGYGATETSPvasvnlpdvLAADFKRQTGSkEGSVGMplpGVAVRIVDPETFeELPPGEDGLILIGGP 995
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 19922652 390 FKWAGYYRNPEATRRAL-SSDGM-WFRTGDIGYLDSEGYLYIQTR 432
Cdd:PRK08633 996 QVMKGYLGDPEKTAEVIkDIDGIgWYVTGDKGHLDEDGFLTITDR 1040
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
53-533 |
2.31e-18 |
|
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: 87.91 E-value: 2.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 53 QELTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNSTYLTSVIIAALLRGIPINPLHPEFTEETVKYMYDITEPKVIFC 132
Cdd:cd17656 12 QKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGVRVVLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 133 DVEnyhiiktVNGKLQNPAKIYLVNGKLEGVLDISEMlndeDSITAAayvpcpklhgDHTAFIVCSSGTTGMPKGVTRSH 212
Cdd:cd17656 92 QRH-------LKSKLSFNKSTILLEDPSISQEDTSNI----DYINNS----------DDLLYIIYTSGTTGKPKGVQLEH 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 213 RSLLCNCKNPNTYTR----DSVLLSFSPLYWISGTIILLASLLNGCRRIITNRP-YSVEYLLQLVARHKVTFLFLAshqI 287
Cdd:cd17656 151 KNMVNLLHFEREKTNinfsDKVLQFATCSFDVCYQEIFSTLLSGGTLYIIREETkRDVEQLFDLVKRHNIEVVFLP---V 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 288 ALLsKHDSDVMELKAQL-QSIRVLIGAGSKVCKAVCRRMYELIGNQRFVVGYGLSEMGGLSKNVGGPvGCE-------GK 359
Cdd:cd17656 228 AFL-KFIFSEREFINRFpTCVKHIITAGEQLVITNEFKEMLHEHNVHLHNHYGPSETHVVTTYTINP-EAEipelppiGK 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 360 VMRNVELRVLDKLKMPLGINEVGIIY------ARlrfkwaGYYRNPEATRRALSSD-----GMWFRTGDIGYLDSEGYLY 428
Cdd:cd17656 306 PISNTWIYILDQEQQLQPQGIVGELYisgasvAR------GYLNRQELTAEKFFPDpfdpnERMYRTGDLARYLPDGNIE 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 429 IQTRDTDVFKFNNFQIYPEQIEEFILRLPGVSEACVFGIPD-AVSTNLTACAVVRTKspegerLTADHIRNIVEHHLSGa 507
Cdd:cd17656 380 FLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADdKGEKYLCAYFVMEQE------LNISQLREYLAKQLPE- 452
|
490 500
....*....|....*....|....*.
gi 19922652 508 YHIRGGVYFIDSLPKTPNDKLQRRKV 533
Cdd:cd17656 453 YMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
38-531 |
3.00e-18 |
|
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: 87.22 E-value: 3.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 38 QINADQVMQICDTT-----GQELTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNSTYLTSVIIAALLRGIPINPLHPE 112
Cdd:cd17645 2 QLFEEQVERTPDHVavvdrGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 113 FTEETVKYMYDITEPKVIFCDVENYhiiktvngklqnpakiylvngklegvldisemlndedsitaaayvpcpklhgdht 192
Cdd:cd17645 82 YPGERIAYMLADSSAKILLTNPDDL------------------------------------------------------- 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 193 AFIVCSSGTTGMPKGVTRSHRSLLCNCKNPNTY------TRDSVLLSFSplywISGTII-LLASLLNGCRRIITN--RPY 263
Cdd:cd17645 107 AYVIYTSGSTGLPKGVMIEHHNLVNLCEWHRPYfgvtpaDKSLVYASFS----FDASAWeIFPHLTAGAALHVVPseRRL 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 264 SVEYLLQLVARHKVTFLFLAShQIAllskhdSDVMELKAqlQSIRVLIGAGSKVCKAVcRRMYELIGNqrfvvgYGLSE- 342
Cdd:cd17645 183 DLDALNDYFNQEGITISFLPT-GAA------EQFMQLDN--QSLRVLLTGGDKLKKIE-RKGYKLVNN------YGPTEn 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 343 -----MGGLSKNVGG-PVgceGKVMRNVELRVLDK-LKM-PLGINE----VGIIYARlrfkwaGYYRNPEATRRALSSDG 410
Cdd:cd17645 247 tvvatSFEIDKPYANiPI---GKPIDNTRVYILDEaLQLqPIGVAGelciAGEGLAR------GYLNRPELTAEKFIVHP 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 411 MW-----FRTGDIGYLDSEGYLYIQTRDTDVFKFNNFQIYPEQIEEFILRLPGVSEACVFGIPDA-VSTNLTACAVVRTK 484
Cdd:cd17645 318 FVpgermYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDAdGRKYLVAYVTAPEE 397
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 19922652 485 SPEGErltadhIRNIVEHHLSGaYHIRGGVYFIDSLPKTPNDKLQRR 531
Cdd:cd17645 398 IPHEE------LREWLKNDLPD-YMIPTYFVHLKALPLTANGKVDRK 437
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
50-531 |
1.03e-17 |
|
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: 86.46 E-value: 1.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 50 TTGQELTGAQLAQQSARIAQAFKRLGLRRGDVVGIsannstYLTSV--IIAALLRGIPINPLHP----EFTEETVKYMYD 123
Cdd:cd05966 80 DQSRTITYRELLREVCRFANVLKSLGVKKGDRVAI------YMPMIpeLVIAMLACARIGAVHSvvfaGFSAESLADRIN 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 124 ITEPKVIFCDVENYHIIKTVNGK------LQNPAKI--YLVNGKLEGVLDISE---MLNDEDSITAAAYVPCPKLHGDHT 192
Cdd:cd05966 154 DAQCKLVITADGGYRGGKVIPLKeivdeaLEKCPSVekVLVVKRTGGEVPMTEgrdLWWHDLMAKQSPECEPEWMDSEDP 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 193 AFIVCSSGTTGMPKGVTRSHRSLLcncknpnTYTRDSVLLSF----SPLY-------WISG-TIILLASLLNGCRRII-- 258
Cdd:cd05966 234 LFILYTSGSTGKPKGVVHTTGGYL-------LYAATTFKYVFdyhpDDIYwctadigWITGhSYIVYGPLANGATTVMfe 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 259 --TNRPYSVEYLlQLVARHKVTFLFLASHQIALLSKHDSDVMElKAQLQSIRVLIGAGSKVCKAVCRRMYELIGNQR--F 334
Cdd:cd05966 307 gtPTYPDPGRYW-DIVEKHKVTIFYTAPTAIRALMKFGDEWVK-KHDLSSLRVLGSVGEPINPEAWMWYYEVIGKERcpI 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 335 VVGYGLSEMGG-LSKNVGG-----PvGCEGKVMRNVELRVLDKLKMPLGINEVGiiYARLRFKWAGY----YRNPEATRR 404
Cdd:cd05966 385 VDTWWQTETGGiMITPLPGatplkP-GSATRPFFGIEPAILDEEGNEVEGEVEG--YLVIKRPWPGMartiYGDHERYED 461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 405 ALSSD--GMWFrTGDIGYLDSEGYLYIQTRDTDVFKFNNFQIYPEQIEEFILRLPGVSEACVFGIPDAVSTNLTACAVVR 482
Cdd:cd05966 462 TYFSKfpGYYF-TGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTL 540
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 19922652 483 TKSPEGERLTADHIRNIVEHHLsGAYHIRGGVYFIDSLPKTPNDKLQRR 531
Cdd:cd05966 541 KDGEEPSDELRKELRKHVRKEI-GPIATPDKIQFVPGLPKTRSGKIMRR 588
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
52-531 |
1.16e-17 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 87.15 E-value: 1.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 52 GQELTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNSTYLTSVIIAALLRGIPINPLHPEFTEETVKYMyditepkvif 131
Cdd:PRK05691 2211 GQTLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHYM---------- 2280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 132 cdVENYHIiktvnGKLQNPAKIYLVNGKLEGvlDISEMLNDEDSITAAAY--VPCPKLHG-DHTAFIVCSSGTTGMPKGV 208
Cdd:PRK05691 2281 --IEDSGI-----GLLLSDRALFEALGELPA--GVARWCLEDDAAALAAYsdAPLPFLSLpQHQAYLIYTSGSTGKPKGV 2351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 209 TRSHRSLLCNCK---NPNTYTRDSVLLSFSPLYWISGTIILLASLLNGCRRIITNR-PYSVEYLLQLVARHKVTFLFLAS 284
Cdd:PRK05691 2352 VVSHGEIAMHCQaviERFGMRADDCELHFYSINFDAASERLLVPLLCGARVVLRAQgQWGAEEICQLIREQQVSILGFTP 2431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 285 HQIALLSKHdsdvMELKAQLQSIRVLIGAGSKVCKAVCRRMYELIGNQRFVVGYGLSEmgglskNVGGPVGC-------E 357
Cdd:PRK05691 2432 SYGSQLAQW----LAGQGEQLPVRMCITGGEALTGEHLQRIRQAFAPQLFFNAYGPTE------TVVMPLAClapeqleE 2501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 358 GK----VMRNVELRV---LDKLKMPLGINEVGIIY------ARlrfkwaGYYRNPEATRRALSSD------GMWFRTGDI 418
Cdd:PRK05691 2502 GAasvpIGRVVGARVayiLDADLALVPQGATGELYvggaglAQ------GYHDRPGLTAERFVADpfaadgGRLYRTGDL 2575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 419 GYLDSEGYL-YIQTRDTDVfKFNNFQIYPEQIEEFILRLPGVSEACVFGIpDAVSTNLTACAVVrTKSPEGERLTADHIR 497
Cdd:PRK05691 2576 VRLRADGLVeYVGRIDHQV-KIRGFRIELGEIESRLLEHPAVREAVVLAL-DTPSGKQLAGYLV-SAVAGQDDEAQAALR 2652
|
490 500 510
....*....|....*....|....*....|....*..
gi 19922652 498 NIVEHHLSGA---YHIRGGVYFIDSLPKTPNDKLQRR 531
Cdd:PRK05691 2653 EALKAHLKQQlpdYMVPAHLILLDSLPLTANGKLDRR 2689
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
56-532 |
1.18e-17 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 85.91 E-value: 1.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 56 TGAQLAQQSARIAQAFKRLGLRRGDVVGISANN-----STYLTSVIIAALLRgiPINP-LHPEfteeTVKYMYDITEPKV 129
Cdd:PRK07008 41 TYRDCERRAKQLAQALAALGVEPGDRVGTLAWNgyrhlEAYYGVSGSGAVCH--TINPrLFPE----QIAYIVNHAEDRY 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 130 IFCDVENYHIIKTVNGKLQNPAKIYLVNGKLEGVLDISEMLNDEDSITA--AAYVpCPKLHgDHTAFIVC-SSGTTGMPK 206
Cdd:PRK07008 115 VLFDLTFLPLVDALAPQCPNVKGWVAMTDAAHLPAGSTPLLCYETLVGAqdGDYD-WPRFD-ENQASSLCyTSGTTGNPK 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 207 GVTRSHRSLLCNCKN---PNTY---TRDSVLlSFSPLYWISGTIILLASLLNGCRRIITNRPYSVEYLLQLVARHKVTF- 279
Cdd:PRK07008 193 GALYSHRSTVLHAYGaalPDAMglsARDAVL-PVVPMFHVNAWGLPYSAPLTGAKLVLPGPDLDGKSLYELIEAERVTFs 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 280 -------LFLASHqiallskhdsdVMELKAQLQSI-RVLIGaGSKVCKAVCRRMYELIGnQRFVVGYGLSEMGGL----- 346
Cdd:PRK07008 272 agvptvwLGLLNH-----------MREAGLRFSTLrRTVIG-GSACPPAMIRTFEDEYG-VEVIHAWGMTEMSPLgtlck 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 347 --SKNVGGPVGC-------EGKVMRNVELRVLDKLKMPLGINevGIIYARL--RFKW--AGYYRNPEATRralsSDGmWF 413
Cdd:PRK07008 339 lkWKHSQLPLDEqrkllekQGRVIYGVDMKIVGDDGRELPWD--GKAFGDLqvRGPWviDRYFRGDASPL----VDG-WF 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 414 RTGDIGYLDSEGYLYIQTRDTDVFKFNNFQIYPEQIEEFILRLPGVSEACVFGIPDAVSTNLTACAVVRTkspEGERLTA 493
Cdd:PRK07008 412 PTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLVVVKR---PGAEVTR 488
|
490 500 510
....*....|....*....|....*....|....*....
gi 19922652 494 DHIRNIVEHHLSgAYHIRGGVYFIDSLPKTPNDKLQRRK 532
Cdd:PRK07008 489 EELLAFYEGKVA-KWWIPDDVVFVDAIPHTATGKLQKLK 526
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
25-531 |
1.47e-17 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 86.64 E-value: 1.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 25 PEMTLGEVIMRVLQINADQVMQICDttGQELTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNSTYLTSVIIAALLRGI 104
Cdd:PRK10252 456 PETTLSALVAQQAAKTPDAPALADA--RYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGA 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 105 PINPLHPEFTEETVKYMYDITEPKVIFCDVEnyhiiktvngklqnpakiylVNGKLEGVlDISEMLNDEDSITAAAYVPC 184
Cdd:PRK10252 534 AWLPLDTGYPDDRLKMMLEDARPSLLITTAD--------------------QLPRFADV-PDLTSLCYNAPLAPQGAAPL 592
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 185 PKLHGDHTAFIVCSSGTTGMPKGVTRSHRSL---LCNCKNPNTYTRDSVLLSFSP---------LYW--ISGTIILLASl 250
Cdd:PRK10252 593 QLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIvnrLLWMQNHYPLTADDVVLQKTPcsfdvsvweFFWpfIAGAKLVMAE- 671
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 251 lngcrriitnrPYS---VEYLLQLVARHKVTFL-FLASHQIALLSKHDSDvmELKAQLQSIRVLIGAGSKVCKAVCRRMY 326
Cdd:PRK10252 672 -----------PEAhrdPLAMQQFFAEYGVTTThFVPSMLAAFVASLTPE--GARQSCASLRQVFCSGEALPADLCREWQ 738
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 327 ELIG----NQrfvvgYG-----------------LSEMGGLSKNVGGPVGcegkvmrNVELRVLDKLKMPLGINEVGIIY 385
Cdd:PRK10252 739 QLTGaplhNL-----YGpteaavdvswypafgeeLAAVRGSSVPIGYPVW-------NTGLRILDARMRPVPPGVAGDLY 806
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 386 ------ARlrfkwaGYYRNPEATRRALSSD-----GMWFRTGDIGYLDSEGYLYIQTRDTDVFKFNNFQIYPEQIEEFIL 454
Cdd:PRK10252 807 ltgiqlAQ------GYLGRPDLTASRFIADpfapgERMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQ 880
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 455 RLPGVSE----ACVFGIPDAV---STNLTACAVvrtkSPEGERLTADHIRNIVEHHLSgAYHIRGGVYFIDSLPKTPNDK 527
Cdd:PRK10252 881 ALPDVEQavthACVINQAAATggdARQLVGYLV----SQSGLPLDTSALQAQLRERLP-PHMVPVVLLQLDQLPLSANGK 955
|
....
gi 19922652 528 LQRR 531
Cdd:PRK10252 956 LDRK 959
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
58-530 |
9.96e-17 |
|
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: 82.62 E-value: 9.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 58 AQLAQQSARIAQAFKRLGLRRGDVVGISANNSTYLTSVIIAALLRGIPINPLHPEFTEETVKYMYDITepKVIFCDVENy 137
Cdd:cd05974 4 AEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRDRVDRG--GAVYAAVDE- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 138 hiiktvNGKLQNPAKIYLvngklegvldisemlndedsitaaayvpcpklhgdhtafivcSSGTTGMPKGVTRSHRSLlc 217
Cdd:cd05974 81 ------NTHADDPMLLYF------------------------------------------TSGTTSKPKLVEHTHRSY-- 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 218 ncknPNTYtrdsvllsFSPLYWIS---GTI---------------ILLASLLNGCRRIITNRP-YSVEYLLQLVARHKVT 278
Cdd:cd05974 111 ----PVGH--------LSTMYWIGlkpGDVhwnisspgwakhawsCFFAPWNAGATVFLFNYArFDAKRVLAALVRYGVT 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 279 FLFLASHQIALLSKHDsdvmeLKAQLQSIRVLIGAGSKVCKAVCRRMYELIGnQRFVVGYGLSEMGGLSKNVGGP---VG 355
Cdd:cd05974 179 TLCAPPTVWRMLIQQD-----LASFDVKLREVVGAGEPLNPEVIEQVRRAWG-LTIRDGYGQTETTALVGNSPGQpvkAG 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 356 CEGKVMRNVELRVLDKLKMPLGINEVGIIYARLRFK--WAGYYRNPEATRRALSsdGMWFRTGDIGYLDSEGYLYIQTRD 433
Cdd:cd05974 253 SMGRPLPGYRVALLDPDGAPATEGEVALDLGDTRPVglMKGYAGDPDKTAHAMR--GGYYRTGDIAMRDEDGYLTYVGRA 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 434 TDVFKFNNFQIYPEQIEEFILRLPGVSEACVFGIPDAVSTNLTACAVVRTKSPEGERLTADHIRNIVEHHLSGAYHIRgG 513
Cdd:cd05974 331 DDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGYEPSPETALEIFRFSRERLAPYKRIR-R 409
|
490
....*....|....*..
gi 19922652 514 VYFIDsLPKTPNDKLQR 530
Cdd:cd05974 410 LEFAE-LPKTISGKIRR 425
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
56-531 |
1.14e-16 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 82.88 E-value: 1.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 56 TGAQLAQQSARIAQAFKRLGLRRGDVVGISANNS-----TYLTSVIIAALLRgiPINP-LHPEfteeTVKYMYDITEPKV 129
Cdd:PRK06018 41 TYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTwrhleAWYGIMGIGAICH--TVNPrLFPE----QIAWIINHAEDRV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 130 IFCDVENYHIIKTVNGKLQNpAKIYLVNG--------KLEGVLDISEMLNDEDSITAAAYVPcpklhgDHTAFIVC-SSG 200
Cdd:PRK06018 115 VITDLTFVPILEKIADKLPS-VERYVVLTdaahmpqtTLKNAVAYEEWIAEADGDFAWKTFD------ENTAAGMCyTSG 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 201 TTGMPKGVTRSHRS-----LLCNCKNPNTYTRDSVLLSFSPLYWISGTIILLASLLNGCRRIITNRPYSVEYLLQLVARH 275
Cdd:PRK06018 188 TTGDPKGVLYSHRSnvlhaLMANNGDALGTSAADTMLPVVPLFHANSWGIAFSAPSMGTKLVMPGAKLDGASVYELLDTE 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 276 KVTF--------LFLASHqialLSKHDSDVMELKaqlqsiRVLIGaGSKVCKAVCRRMYELIGNQRFvvGYGLSEMggls 347
Cdd:PRK06018 268 KVTFtagvptvwLMLLQY----MEKEGLKLPHLK------MVVCG-GSAMPRSMIKAFEDMGVEVRH--AWGMTEM---- 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 348 knvgGPVGCEGKV---MRNVELRV-LDKLKM----PLGI---------NEV---GIIYARLRFKW----AGYYRnpeATR 403
Cdd:PRK06018 331 ----SPLGTLAALkppFSKLPGDArLDVLQKqgypPFGVemkitddagKELpwdGKTFGRLKVRGpavaAAYYR---VDG 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 404 RALSSDGmWFRTGDIGYLDSEGYLYIQTRDTDVFKFNNFQIYPEQIEEFILRLPGVSEACVFGIPDAvSTNLTACAVVRT 483
Cdd:PRK06018 404 EILDDDG-FFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHP-KWDERPLLIVQL 481
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 19922652 484 KspEGERLTADHIRNIVEHHLSgAYHIRGGVYFIDSLPKTPNDKLQRR 531
Cdd:PRK06018 482 K--PGETATREEILKYMDGKIA-KWWMPDDVAFVDAIPHTATGKILKT 526
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
195-480 |
2.62e-16 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 82.17 E-value: 2.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 195 IVCSSGTTGMPKGVTRSHRSL--------LCNCKNPNTYTRDSVLLSFSPLYWISGTII--------------------- 245
Cdd:PLN02430 225 IMYTSGTSGDPKGVVLTHEAVatfvrgvdLFMEQFEDKMTHDDVYLSFLPLAHILDRMIeeyffrkgasvgyyhgdlnal 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 246 ------LLASLLNGCRRIITNRPYSVEYLLQ-LVARHKVTFLFLASHQIALLS---KHD-----SDVM---ELKAQLQS- 306
Cdd:PLN02430 305 rddlmeLKPTLLAGVPRVFERIHEGIQKALQeLNPRRRLIFNALYKYKLAWMNrgySHKkaspmADFLafrKVKAKLGGr 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 307 IRVLIGAGSKVCKAVcRRMYELIGNQRFVVGYGLSEMGGLSkNVGGP-----VGCEGKVMRNVELRVLDKLKM---PLGI 378
Cdd:PLN02430 385 LRLLISGGAPLSTEI-EEFLRVTSCAFVVQGYGLTETLGPT-TLGFPdemcmLGTVGAPAVYNELRLEEVPEMgydPLGE 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 379 NEVGIIYARLRFKWAGYYRNPEATRRALsSDGmWFRTGDIGYLDSEGYLYIQTRDTDVFKFNNFQ-IYPEQIEEFILRLP 457
Cdd:PLN02430 463 PPRGEICVRGKCLFSGYYKNPELTEEVM-KDG-WFHTGDIGEILPNGVLKIIDRKKNLIKLSQGEyVALEYLENVYGQNP 540
|
330 340
....*....|....*....|...
gi 19922652 458 GVSEACVFGipDAVSTNLTACAV 480
Cdd:PLN02430 541 IVEDIWVYG--DSFKSMLVAVVV 561
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
52-470 |
1.58e-15 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 79.15 E-value: 1.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 52 GQELTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNST-----YLTSVIIAAllRGIPINPLHPEftEETVKYMYDITe 126
Cdd:PRK09029 26 DEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPetllaYLALLQCGA--RVLPLNPQLPQ--PLLEELLPSLT- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 127 pkVIFCDVENYHiiktvngklQNPAKIYLVngklegvldiseMLNDEDSITAAAYvpcpklHGDHTAFIVCSSGTTGMPK 206
Cdd:PRK09029 101 --LDFALVLEGE---------NTFSALTSL------------HLQLVEGAHAVAW------QPQRLATMTLTSGSTGLPK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 207 GVTRSHRSLLCNCK---NPNTYTR-DSVLLSFsPLYWISGTIILLASLLNGCRriitnrpysveyllqLVARHKVTF--- 279
Cdd:PRK09029 152 AAVHTAQAHLASAEgvlSLMPFTAqDSWLLSL-PLFHVSGQGIVWRWLYAGAT---------------LVVRDKQPLeqa 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 280 LFLASH------QIALLSKHDSDVMELKAqlqsirVLIGaGSKVCKAVCRRMyELIGNQRFvVGYGLSEMG--------- 344
Cdd:PRK09029 216 LAGCTHaslvptQLWRLLDNRSEPLSLKA------VLLG-GAAIPVELTEQA-EQQGIRCW-CGYGLTEMAstvcakrad 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 345 GLSkNVGGPvgcegkvMRNVELRVLDklkmplgiNEVGIIYARLRfkwAGYYRNPEATrrALSSDGMWFRTGDIGYLDsE 424
Cdd:PRK09029 287 GLA-GVGSP-------LPGREVKLVD--------GEIWLRGASLA---LGYWRQGQLV--PLVNDEGWFATRDRGEWQ-N 344
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 19922652 425 GYLYIQTR-DtdvfkfNNF-----QIYPEQIEEFILRLPGVSEACVFGIPDA 470
Cdd:PRK09029 345 GELTILGRlD------NLFfsggeGIQPEEIERVINQHPLVQQVFVVPVADA 390
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
193-532 |
3.06e-15 |
|
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: 78.21 E-value: 3.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 193 AFIVCSSGTTGMPKGVTRSHRSLLCNCKN-PNTY----TRDSVLLSFSPLYWISGTIILLASLLNGCRRIITNRPYSV-- 265
Cdd:cd17648 97 AYAIYTSGTTGKPKGVLVEHGSVVNLRTSlSERYfgrdNGDEAVLFFSNYVFDFFVEQMTLALLNGQKLVVPPDEMRFdp 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 266 EYLLQLVARHKVTFLflaSHQIALLSKHDSdvmelkAQLQSIRVLIGAGSKVCKAVCRRMYELIGNqRFVVGYGLSEMG- 344
Cdd:cd17648 177 DRFYAYINREKVTYL---SGTPSVLQQYDL------ARLPHLKRVDAAGEEFTAPVFEKLRSRFAG-LIINAYGPTETTv 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 345 -----------GLSKNVGGPVgcegkvmRNVELRVLDKLKMPLGINEVGIIY------ARlrfkwaGYYRNPEATR---- 403
Cdd:cd17648 247 tnhkrffpgdqRFDKSLGRPV-------RNTKCYVLNDAMKRVPVGAVGELYlggdgvAR------GYLNRPELTAerfl 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 404 ---------RALSSDGMWFRTGDIGYLDSEGYL-YIQTRDTDVfKFNNFQIYPEQIEEFILRLPGVSEACVFGIPDAVST 473
Cdd:cd17648 314 pnpfqteqeRARGRNARLYKTGDLVRWLPSGELeYLGRNDFQV-KIRGQRIEPGEVEAALASYPGVRECAVVAKEDASQA 392
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 474 NLT-ACAVVRTKSPEGERLTADHIRNIVEHHLSgAYHIRGGVYFIDSLPKTPNDKLQRRK 532
Cdd:cd17648 393 QSRiQKYLVGYYLPEPGHVPESDLLSFLRAKLP-RYMVPARLVRLEGIPVTINGKLDVRA 451
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
49-539 |
4.03e-15 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 78.01 E-value: 4.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 49 DTTGQELTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNSTYLTSVIIAALLRG---IPINPLHPEfteETVKYMYDIT 125
Cdd:PRK04813 22 DYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGhayIPVDVSSPA---ERIEMIIEVA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 126 EPKVIFC------DVENYHIIKTVngklqnpakiylvngklegvlDISEMLNDEDSITAAAYVpcpklHGDHTAFIVCSS 199
Cdd:PRK04813 99 KPSLIIAteelplEILGIPVITLD---------------------ELKDIFATGNPYDFDHAV-----KGDDNYYIIFTS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 200 GTTGMPKGVTRSHRSLL--CN--CKNPNTYTRDSVL----LSF--SPLYW-----ISGTIILLAsllngcrRIITNRPYS 264
Cdd:PRK04813 153 GTTGKPKGVQISHDNLVsfTNwmLEDFALPEGPQFLnqapYSFdlSVMDLyptlaSGGTLVALP-------KDMTANFKQ 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 265 V-EYLLQLVARHKV-TFLFLashQIALLSKH-DSDvmelkaQLQSIRVLIGAGSKVCKAVCRRMYELIGNQRFVVGYGLS 341
Cdd:PRK04813 226 LfETLPQLPINVWVsTPSFA---DMCLLDPSfNEE------HLPNLTHFLFCGEELPHKTAKKLLERFPSATIYNTYGPT 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 342 EMGG-----------LSKNVGGPVGcegKVMRNVELRVLDKLKMPLGINEVG--IIYARLRFKwaGYYRNPEATRRAL-S 407
Cdd:PRK04813 297 EATVavtsieitdemLDQYKRLPIG---YAKPDSPLLIIDEEGTKLPDGEQGeiVISGPSVSK--GYLNNPEKTAEAFfT 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 408 SDGMW-FRTGDIGYLDsEGYLYIQTR-DTDVfKFNNFQIYPEQIEEFILRLPGVSEACVFGI-PDAVSTNLTACAVVRTK 484
Cdd:PRK04813 372 FDGQPaYHTGDAGYLE-DGLLFYQGRiDFQI-KLNGYRIELEEIEQNLRQSSYVESAVVVPYnKDHKVQYLIAYVVPKEE 449
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 19922652 485 SPEGER-LTADhIRNIVEHHLSgAYHI-RGGVYfIDSLPKTPNDKLQRRKVLGLVQQ 539
Cdd:PRK04813 450 DFEREFeLTKA-IKKELKERLM-EYMIpRKFIY-RDSLPLTPNGKIDRKALIEEVNK 503
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
185-530 |
6.47e-15 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 78.29 E-value: 6.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 185 PKLHGDHTAFIVCSSGTTGMPKGVTRSHRSLLCN----------CKNPntytrDSVLLSFSPLYWISGTI-ILLASLLNG 253
Cdd:PRK05691 161 PALQPDDIAFLQYTSGSTALPKGVQVSHGNLVANeqlirhgfgiDLNP-----DDVIVSWLPLYHDMGLIgGLLQPIFSG 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 254 CRRIITNRPYSVEY---LLQLVARHKVTFLFLASHQIALLSKHDSDVMELKAQLQSIRVLIGAGSKVCKAVCRRMYELIG 330
Cdd:PRK05691 236 VPCVLMSPAYFLERplrWLEAISEYGGTISGGPDFAYRLCSERVSESALERLDLSRWRVAYSGSEPIRQDSLERFAEKFA 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 331 N-----QRFVVGYGLSEM-----GG---------------LSKNV-----GGPVGCEGKVMRNVELRVLDKLKMP-LGIN 379
Cdd:PRK05691 316 AcgfdpDSFFASYGLAEAtlfvsGGrrgqgipaleldaeaLARNRaepgtGSVLMSCGRSQPGHAVLIVDPQSLEvLGDN 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 380 EVGIIYARLRFKWAGYYRNPEATRRA-LSSDG-MWFRTGDIGYLdSEGYLYIQTRDTDVFKFNNFQIYPEQIEEFIlrlp 457
Cdd:PRK05691 396 RVGEIWASGPSIAHGYWRNPEASAKTfVEHDGrTWLRTGDLGFL-RDGELFVTGRLKDMLIVRGHNLYPQDIEKTV---- 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 458 gvsEACVfgipDAVSTNLTACAVVRTKSPEG------------ERLTADHIRNIVEHHLSGAYHIRGGVYFI---DSLPK 522
Cdd:PRK05691 471 ---EREV----EVVRKGRVAAFAVNHQGEEGigiaaeisrsvqKILPPQALIKSIRQAVAEACQEAPSVVLLlnpGALPK 543
|
....*...
gi 19922652 523 TPNDKLQR 530
Cdd:PRK05691 544 TSSGKLQR 551
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
449-527 |
8.73e-15 |
|
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: 69.50 E-value: 8.73e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19922652 449 IEEFILRLPGVSEACVFGIPDAVSTNLTACAVVRtksPEGERLTADHIRNIVEHHLsGAYHIRGGVYFIDSLPKTPNDK 527
Cdd:pfam13193 2 VESALVSHPAVAEAAVVGVPDELKGEAPVAFVVL---KPGVELLEEELVAHVREEL-GPYAVPKEVVFVDELPKTRSGK 76
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
177-481 |
1.02e-14 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 76.99 E-value: 1.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 177 TAAAYVPCPKLHGDHTAFIVCSSGTTGMPKGVTRSH-RSLLCNCKNPNTY--TRDSVLLSFSPLYWISGTIILLASLLNG 253
Cdd:PRK13388 137 AAGALTPHREVDAMDPFMLIFTSGTTGAPKAVRCSHgRLAFAGRALTERFglTRDDVCYVSMPLFHSNAVMAGWAPAVAS 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 254 CRRIITNRPYSVEYLLQLVARHKVTFLFLASHQIALL---SKHDSDvmelkAQlQSIRVLIG--AGSKVCKAVCRRMyel 328
Cdd:PRK13388 217 GAAVALPAKFSASGFLDDVRRYGATYFNYVGKPLAYIlatPERPDD-----AD-NPLRVAFGneASPRDIAEFSRRF--- 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 329 igNQRFVVGYGLSEMGG-LSKNVGGPVGCEGKVMRNVELRVLDKLKM--PLGINEVG-----------IIYARLRFKWAG 394
Cdd:PRK13388 288 --GCQVEDGYGSSEGAViVVREPGTPPGSIGRGAPGVAIYNPETLTEcaVARFDAHGallnadeaigeLVNTAGAGFFEG 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 395 YYRNPEATRRALSsDGmWFRTGDIGYLDSEGYLYIQTRDTDVFKFN--NFQIYPeqIEEFILRLPGVSEACVFGIPDAVS 472
Cdd:PRK13388 366 YYNNPEATAERMR-HG-MYWSGDLAYRDADGWIYFAGRTADWMRVDgeNLSAAP--IERILLRHPAINRVAVYAVPDERV 441
|
....*....
gi 19922652 473 TNLTACAVV 481
Cdd:PRK13388 442 GDQVMAALV 450
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
193-471 |
4.96e-14 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.
Pssm-ID: 341294 [Multi-domain] Cd Length: 507 Bit Score: 74.56 E-value: 4.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 193 AFIVCSSGTTGMPKGVTRSHRSLLCNCKN-----PNTYTRDSVLLSFSPLYWISGTIILLASLLNGCR------RIITNR 261
Cdd:cd17639 91 ACIMYTSGSTGNPKGVMLTHGNLVAGIAGlgdrvPELLGPDDRYLAYLPLAHIFELAAENVCLYRGGTigygspRTLTDK 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 262 PYS------VEYllqlvarhKVTfLFLASHQI------ALLSKHDS------DVMELKAQLQSIRVLIGAGSKVC-KAVC 322
Cdd:cd17639 171 SKRgckgdlTEF--------KPT-LMVGVPAIwdtirkGVLAKLNPmgglkrTLFWTAYQSKLKALKEGPGTPLLdELVF 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 323 RRMYELIGN----------------QRF--------VVGYGLSE---MGGLS-------KNVGGPVGCegkvmrnVELRV 368
Cdd:cd17639 242 KKVRAALGGrlrymlsggaplsadtQEFlnivlcpvIQGYGLTEtcaGGTVQdpgdletGRVGPPLPC-------CEIKL 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 369 LD--------KLKMPLGinEVGIiyaRLRFKWAGYYRNPEATRRALSSDGmWFRTGDIGYLDSEGYLYIQTRDTDVFKFN 440
Cdd:cd17639 315 VDweeggystDKPPPRG--EILI---RGPNVFKGYYKNPEKTKEAFDGDG-WFHTGDIGEFHPDGTLKIIDRKKDLVKLQ 388
|
330 340 350
....*....|....*....|....*....|..
gi 19922652 441 NFQ-IYPEQIEEFILRLPGVSEACVFGIPDAV 471
Cdd:cd17639 389 NGEyIALEKLESIYRSNPLVNNICVYADPDKS 420
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
333-481 |
3.06e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 72.02 E-value: 3.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 333 RFVVGYGLSEMG-GLSKNVGGPVGCEGKVMRNVELR-----------VLDKLKMPLGINEVG-IIYARLRFKWAGYYRNP 399
Cdd:PRK07867 292 VVVDGFGSTEGGvAITRTPDTPPGALGPLPPGVAIVdpdtgtecppaEDADGRLLNADEAIGeLVNTAGPGGFEGYYNDP 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 400 EATRRALSsDGmWFRTGDIGYLDSEGYLYIQTRDTDVFKFNNFQIYPEQIEEFILRLPGVSEACVFGIPDAVSTNLTACA 479
Cdd:PRK07867 372 EADAERMR-GG-VYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVMAA 449
|
..
gi 19922652 480 VV 481
Cdd:PRK07867 450 LV 451
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
48-530 |
6.71e-13 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 71.19 E-value: 6.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 48 CDTTgQELTGAQLAQQSARIAQAFKRLGLRRGD-VVGISANN-STYLtSVIIAALLRGIPI---NPLHPEfteeTVKYMY 122
Cdd:PRK05857 36 CDGT-SALRYRELVAEVGGLAADLRAQSVSRGSrVLVISDNGpETYL-SVLACAKLGAIAVmadGNLPIA----AIERFC 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 123 DITEPKVIF----CDV------ENYHIIKTVNGKLQNPAKIYLVNGklegvldisemlnDEDSITAAayvpcPKLHGDHT 192
Cdd:PRK05857 110 QITDPAAALvapgSKMassavpEALHSIPVIAVDIAAVTRESEHSL-------------DAASLAGN-----ADQGSEDP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 193 AFIVCSSGTTGMPKGVTRSHRSL-----LCNCKNPNTYTRDSVLLSFSPL--YWISGTIILLASLLNG--CrriITNRPY 263
Cdd:PRK05857 172 LAMIFTSGTTGEPKAVLLANRTFfavpdILQKEGLNWVTWVVGETTYSPLpaTHIGGLWWILTCLMHGglC---VTGGEN 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 264 SVEyLLQLVARHKVTFLFLAShqiALLSKHDSDVMELKAQLQSIRVLIGAGSKVCKAVCRrMYELIGNQRFVVgYGLSEM 343
Cdd:PRK05857 249 TTS-LLEILTTNAVATTCLVP---TLLSKLVSELKSANATVPSLRLVGYGGSRAIAADVR-FIEATGVRTAQV-YGLSET 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 344 G-----------GLSKNVGGPVGcegKVMRNVELRVLDK----LKMPLGINEV--GIIYARLRFKWAGYYRNPEATRRAL 406
Cdd:PRK05857 323 GctalclptddgSIVKIEAGAVG---RPYPGVDVYLAATdgigPTAPGAGPSAsfGTLWIKSPANMLGYWNNPERTAEVL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 407 SsDGmWFRTGDIGYLDSEGYLYIQTRDTDVFKFNNFQIYPEQIEEFILRLPGVSEACVFGIPDAVSTNLTACAVVRTKSP 486
Cdd:PRK05857 400 I-DG-WVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGALVGLAVVASAEL 477
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 19922652 487 EGERlTADHIRNIVEHHL--SGAYHIRGGVYFIDSLPKTPNDKLQR 530
Cdd:PRK05857 478 DESA-ARALKHTIAARFRreSEPMARPSTIVIVTDIPRTQSGKVMR 522
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
115-432 |
1.05e-12 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 70.78 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 115 EETVKYMYDITEPKVIFCDVENyhiIKTV-----NGKLQNPAKIYLvnGKLEGVLDISEM-------LNDEDSITAAAYV 182
Cdd:PTZ00216 182 EDALAYALRETECKAIVCNGKN---VPNLlrlmkSGGMPNTTIIYL--DSLPASVDTEGCrlvawtdVVAKGHSAGSHHP 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 183 PCPKLHGDHTAFIVCSSGTTGMPKGVTRSHRSL-------------LCNCKNPN-TYtrdsvlLSFSPLYWI---SGTII 245
Cdd:PTZ00216 257 LNIPENNDDLALIMYTSGTTGDPKGVMHTHGSLtagilaledrlndLIGPPEEDeTY------CSYLPLAHImefGVTNI 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 246 LLA--SLLN-GCRRIITN---RPYS--VEYllqlvarhkVTFLFLASHQI------ALLSKHDSdVMELKAQL-----QS 306
Cdd:PTZ00216 331 FLArgALIGfGSPRTLTDtfaRPHGdlTEF---------RPVFLIGVPRIfdtikkAVEAKLPP-VGSLKRRVfdhayQS 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 307 IRVLIGAG-----------SKVCKAVCRRMYELIG--------NQRF--VV------GYGLSE---MGGLSKNVGGPVGC 356
Cdd:PTZ00216 401 RLRALKEGkdtpywnekvfSAPRAVLGGRVRAMLSgggplsaaTQEFvnVVfgmviqGWGLTEtvcCGGIQRTGDLEPNA 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 357 EGKVMRNVELRVLDklkmplgINEV---------GIIYARLRFKWAGYYRNPEATRRALSSDGmWFRTGDIGYLDSEGYL 427
Cdd:PTZ00216 481 VGQLLKGVEMKLLD-------TEEYkhtdtpeprGEILLRGPFLFKGYYKQEELTREVLDEDG-WFHTGDVGSIAANGTL 552
|
....*
gi 19922652 428 YIQTR 432
Cdd:PTZ00216 553 RIIGR 557
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
53-467 |
1.29e-12 |
|
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: 69.80 E-value: 1.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 53 QELTGAQLAQQSARIAQAFKRLGLRRGdvvgisannstyltsviiaalLRGIPINPLHPEFTEETVKYMyditepKVIFC 132
Cdd:cd05910 1 SRLSFRELDERSDRIAQGLTAYGIRRG---------------------MRAVLMVPPGPDFFALTFALF------KAGAV 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 133 DVenyhiiktvngkLQNPAkiylvngklegvLDISEMLNDEDSITAAAYVPCPKlhGDHTAFIVCSSGTTGMPKGVTRSH 212
Cdd:cd05910 54 PV------------LIDPG------------MGRKNLKQCLQEAEPDAFIGIPK--ADEPAAILFTSGSTGTPKGVVYRH 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 213 RSL---LCNCKNPNTYTRDSVLLSFSPLYWISGTIILLASLLNgcrRIITNRPYSV--EYLLQLVARHKVTFLFLASHQI 287
Cdd:cd05910 108 GTFaaqIDALRQLYGIRPGEVDLATFPLFALFGPALGLTSVIP---DMDPTRPARAdpQKLVGAIRQYGVSIVFGSPALL 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 288 ALLSKHdsdVMELKAQLQSIRVLIGAGSKVCKAVCRRMYELIGNQ-RFVVGYG---------------LSEMGGLSKNVG 351
Cdd:cd05910 185 ERVARY---CAQHGITLPSLRRVLSAGAPVPIALAARLRKMLSDEaEILTPYGatealpvssigsrelLATTTAATSGGA 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 352 GPvgCEGKVMRNVELRVL-----------DKLKMPLGinEVGIIYARLRFKWAGYYRNPEATRRALSSD---GMWFRTGD 417
Cdd:cd05910 262 GT--CVGRPIPGVRVRIIeiddepiaewdDTLELPRG--EIGEITVTGPTVTPTYVNRPVATALAKIDDnseGFWHRMGD 337
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 19922652 418 IGYLDSEGYLYIQTRDTDVFKFNNFQIYPEQIEEFILRLPGVSEACVFGI 467
Cdd:cd05910 338 LGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVGV 387
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
56-530 |
3.78e-12 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 68.72 E-value: 3.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 56 TGAQLAQQSARIAQAFKRLGLRRGDVVGISANNSTYLTSVIIAALLRGIPINPLHPEFTEETVKYMYDITEPKVIFCDVE 135
Cdd:PLN02479 47 TWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRLNAPTIAFLLEHSKSEVVMVDQE 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 136 NYHII----KTVNGKLQNPAKIYLV---------NGKLE-----GVLDISEMLNDEDSitAAAYVPcPKLHGDHTAfIVC 197
Cdd:PLN02479 127 FFTLAeealKILAEKKKSSFKPPLLivigdptcdPKSLQyalgkGAIEYEKFLETGDP--EFAWKP-PADEWQSIA-LGY 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 198 SSGTTGMPKGVTRSHR-SLLCNCKNPNTYTRD--SVLLSFSPLYWISGTIIL--LASLlngCRRIITNRPYSVEYLLQLV 272
Cdd:PLN02479 203 TSGTTASPKGVVLHHRgAYLMALSNALIWGMNegAVYLWTLPMFHCNGWCFTwtLAAL---CGTNICLRQVTAKAIYSAI 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 273 ARHKVTFLFLAShqIALLSKHDSDVMELKAQLQSIRVLIGAGSKVCKAVCRRMYELigNQRFVVGYGLSEMGGLSKNVG- 351
Cdd:PLN02479 280 ANYGVTHFCAAP--VVLNTIVNAPKSETILPLPRVVHVMTAGAAPPPSVLFAMSEK--GFRVTHTYGLSETYGPSTVCAw 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 352 GP---------------------VGCEGkvmrnveLRVLDKLKM---PLGINEVGIIYARLRFKWAGYYRNPEATRRALS 407
Cdd:PLN02479 356 KPewdslppeeqarlnarqgvryIGLEG-------LDVVDTKTMkpvPADGKTMGEIVMRGNMVMKGYLKNPKANEEAFA 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 408 sdGMWFRTGDIGYLDSEGYLYIQTRDTDVFKFNNFQIYPEQIEEFILRLPGVSEACVFGIPDAvSTNLTACAVVRTKS-- 485
Cdd:PLN02479 429 --NGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDE-RWGESPCAFVTLKPgv 505
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 19922652 486 -PEGERLTADHIRNIVEHHLSGaYHIRGGVYFiDSLPKTPNDKLQR 530
Cdd:PLN02479 506 dKSDEAALAEDIMKFCRERLPA-YWVPKSVVF-GPLPKTATGKIQK 549
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
52-493 |
4.51e-12 |
|
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: 68.15 E-value: 4.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 52 GQELTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNS-TYLtsVIIAALLR-GIPINPLHPEFTEETVKYMYDITEPKV 129
Cdd:cd05940 1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRpEYV--LLWLGLVKiGAVAALINYNLRGESLAHCLNVSSAKH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 130 IFCDvenyhiiktvngklqnpakiylvngklegvldisemlndedsitaaayvpcpklhgdhTAFIVCSSGTTGMPKGVT 209
Cdd:cd05940 79 LVVD----------------------------------------------------------AALYIYTSGTTGLPKAAI 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 210 RSHRSLLcncknpNTYT---------RDSVLLSFSPLYWISGTIILLASLLNGCRRIITNRPYSVEYLLQLVARHKVTFL 280
Cdd:cd05940 101 ISHRRAW------RGGAffagsggalPSDVLYTCLPLYHSTALIVGWSACLASGATLVIRKKFSASNFWDDIRKYQATIF 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 281 ---------FLASHQIALLSKHdsdvmelkaqlqSIRVLIGAGSKvcKAVCRRMYELIGNQRFVVGYGLSEMGGLSKNVG 351
Cdd:cd05940 175 qyigelcryLLNQPPKPTERKH------------KVRMIFGNGLR--PDIWEEFKERFGVPRIAEFYAATEGNSGFINFF 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 352 GPVGCEG-------KVMR------NVE----LRVLDKLKMPLGINEVGIIYARLRFKWA--GYYRNPEATRRALSS---D 409
Cdd:cd05940 241 GKPGAIGrnpsllrKVAPlalvkyDLEsgepIRDAEGRCIKVPRGEPGLLISRINPLEPfdGYTDPAATEKKILRDvfkK 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 410 G-MWFRTGDIGYLDSEGYLYIQTRDTDVFKFNNFQIYPEQIEEFILRLPGVSEACVFGIPDAVSTNLTACAVVRTKSPEG 488
Cdd:cd05940 321 GdAWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQVPGTDGRAGMAAIVLQPNEE 400
|
....*
gi 19922652 489 ERLTA 493
Cdd:cd05940 401 FDLSA 405
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
53-466 |
4.74e-12 |
|
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: 68.54 E-value: 4.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 53 QELTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNSTYLTSVIIAALLRGIPINPLHPEFTEETVKYMYDITEPKVIFc 132
Cdd:cd05933 7 HTLTYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSEANILV- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 133 dVENYH---IIKTVNGKL---------QNP-----AKIYLVNGKLEGVLDIS--EMLNDEDSITAaayvpcpklhgDHTA 193
Cdd:cd05933 86 -VENQKqlqKILQIQDKLphlkaiiqyKEPlkekePNLYSWDEFMELGRSIPdeQLDAIISSQKP-----------NQCC 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 194 FIVCSSGTTGMPKGVTRSHRSLLCNCKNPNTYTRD-------SVLLSFSPLYWISGTII-------------------LL 247
Cdd:cd05933 154 TLIYTSGTTGMPKGVMLSHDNITWTAKAASQHMDLrpatvgqESVVSYLPLSHIAAQILdiwlpikvggqvyfaqpdaLK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 248 ASLLNGCRRIitnRPYS----------VEYLLQLVARHKVTFlflaSHQIALLSKHDSDVMELKAQLQSIRVLIGAG--- 314
Cdd:cd05933 234 GTLVKTLREV---RPTAfmgvprvwekIQEKMKAVGAKSGTL----KRKIASWAKGVGLETNLKLMGGESPSPLFYRlak 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 315 ----SKVCKAV----CRRMYE-------------LIGNQRFVVGYGLSEMGGLsKNVGGP----VGCEGKVMRNVELRVL 369
Cdd:cd05933 307 klvfKKVRKALgldrCQKFFTgaapisretleffLSLNIPIMELYGMSETSGP-HTISNPqayrLLSCGKALPGCKTKIH 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 370 DKLKMplGINEVgIIYARLRFKwaGYYRNPEATRRALSSDGmWFRTGDIGYLDSEGYLYIQTRDTDVFKFNNFQ-IYPEQ 448
Cdd:cd05933 386 NPDAD--GIGEI-CFWGRHVFM--GYLNMEDKTEEAIDEDG-WLHSGDLGKLDEDGFLYITGRIKELIITAGGEnVPPVP 459
|
490
....*....|....*....
gi 19922652 449 IEEFI-LRLPGVSEACVFG 466
Cdd:cd05933 460 IEDAVkKELPIISNAMLIG 478
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
54-419 |
6.35e-12 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 68.15 E-value: 6.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 54 ELTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNSTYLTSVIIAALLRGIPINPLHPEFT-----EETVKYMYDITEPK 128
Cdd:PRK12582 80 KVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAGVPAAPVSPAYSlmshdHAKLKHLFDLVKPR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 129 VIFCD--VENYHIIKTVNgkLQNPaKIYLVNGKLEG--VLDISEMLNdeDSITAAAYVPCPKLHGDHTAFIVCSSGTTGM 204
Cdd:PRK12582 160 VVFAQsgAPFARALAALD--LLDV-TVVHVTGPGEGiaSIAFADLAA--TPPTAAVAAAIAAITPDTVAKYLFTSGSTGM 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 205 PKGVTRSHRSLLCNCKNPNTYTRD------SVLLSFSPLYWISGTIILLASLLN--GCRRIITNRPYSVEYLLQLVARHK 276
Cdd:PRK12582 235 PKAVINTQRMMCANIAMQEQLRPRepdpppPVSLDWMPWNHTMGGNANFNGLLWggGTLYIDDGKPLPGMFEETIRNLRE 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 277 VTFLFLASHQIA---LLSKHDSDVMELKAQLQSIRVLIGAGSKVCKAVCRRMYEL---IGNQRFVV--GYGLSEMGGLSK 348
Cdd:PRK12582 315 ISPTVYGNVPAGyamLAEAMEKDDALRRSFFKNLRLMAYGGATLSDDLYERMQALavrTTGHRIPFytGYGATETAPTTT 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 349 NVGGP---VGCEGKVMRNVELRVL---DKLKmplginevgiiyarLRFK----WAGYYRNPEATRRALSSDGmWFRTGDI 418
Cdd:PRK12582 395 GTHWDterVGLIGLPLPGVELKLApvgDKYE--------------VRVKgpnvTPGYHKDPELTAAAFDEEG-FYRLGDA 459
|
.
gi 19922652 419 G 419
Cdd:PRK12582 460 A 460
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
165-468 |
6.84e-12 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 67.92 E-value: 6.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 165 DISEMLNDEDSITAAAYVPCP-----KLHG------DHTAFIVCSSGTTGMPKGVTRSHRSLLCN------CKNPNTytr 227
Cdd:PRK06334 147 EVRKELSFWEKCRIGIYMSIPfewlmRWFGvsdkdpEDVAVILFTSGTEKLPKGVPLTHANLLANqraclkFFSPKE--- 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 228 DSVLLSFSPLYWISG-TIILLASLLNGCRRIITNRPYSVEYLLQLVARHKVTFL-----FLaSHQIALLSKHDSdvmelk 301
Cdd:PRK06334 224 DDVMMSFLPPFHAYGfNSCTLFPLLSGVPVVFAYNPLYPKKIVEMIDEAKVTFLgstpvFF-DYILKTAKKQES------ 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 302 aQLQSIRVLIGAGSKVCKAVCRRMYELIGNQRFVVGYGLSEMGGL----SKNVGGPVGCEGKVMRNVELRVLDK-LKMPL 376
Cdd:PRK06334 297 -CLPSLRFVVIGGDAFKDSLYQEALKTFPHIQLRQGYGTTECSPVitinTVNSPKHESCVGMPIRGMDVLIVSEeTKVPV 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 377 GINEVGIIYARLRFKWAGYYRNPEaTRRALSSDG-MWFRTGDIGYLDSEGYLYIQTRDTDVFKFNNFQIYPEQIEEFILR 455
Cdd:PRK06334 376 SSGETGLVLTRGTSLFSGYLGEDF-GQGFVELGGeTWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILME 454
|
330
....*....|....*....
gi 19922652 456 LPGVSEA------CVFGIP 468
Cdd:PRK06334 455 GFGQNAAdhagplVVCGLP 473
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
176-467 |
8.46e-12 |
|
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: 67.46 E-value: 8.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 176 ITAAAYVPCPKLHG--------DHTAFIVCSSGTTGMPKGVTRSHRSLLCNCKN-PNTYTRDSVLLSFS--PLYWISGTI 244
Cdd:cd05937 65 LSGDPLIHCLKLSGsrfvivdpDDPAILIYTSGTTGLPKAAAISWRRTLVTSNLlSHDLNLKNGDRTYTcmPLYHGTAAF 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 245 ILLASLLNGCRRIITNRPYSV-EYLLQLVARHKVTFLFLASHQIALLSKHDSDvmelKAQLQSIRVLIGAGskvckavcr 323
Cdd:cd05937 145 LGACNCLMSGGTLALSRKFSAsQFWKDVRDSGATIIQYVGELCRYLLSTPPSP----YDRDHKVRVAWGNG--------- 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 324 rmyeLIGN--QRFVVGYGLSEMG-------GLSK----NVG----GPVGCEGKVMR----NVELRVL------DKLKMP- 375
Cdd:cd05937 212 ----LRPDiwERFRERFNVPEIGefyaateGVFAltnhNVGdfgaGAIGHHGLIRRwkfeNQVVLVKmdpetdDPIRDPk 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 376 ------LGINEVGIIYARLRFK----WAGYYRNPEATRRALSSD-----GMWFRTGDIGYLDSEGYLYIQTRDTDVFKFN 440
Cdd:cd05937 288 tgfcvrAPVGEPGEMLGRVPFKnreaFQGYLHNEDATESKLVRDvfrkgDIYFRTGDLLRQDADGRWYFLDRLGDTFRWK 367
|
330 340
....*....|....*....|....*..
gi 19922652 441 NFQIYPEQIEEFILRLPGVSEACVFGI 467
Cdd:cd05937 368 SENVSTTEVADVLGAHPDIAEANVYGV 394
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
414-533 |
1.91e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 65.83 E-value: 1.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 414 RTGDIGYLDSEGYLYIQTRDTDVFKFNNFQIYPEQIEEFILRLPGVSEACVFGIPDAVSTNLTACAVVRTkspegERLTA 493
Cdd:PRK08308 294 FTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVISH-----EEIDP 368
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 19922652 494 DHIRNIVEHHLSgAYHIRGGVYFIDSLPKTPNDKLQRRKV 533
Cdd:PRK08308 369 VQLREWCIQHLA-PYQVPHEIESVTEIPKNANGKVSRKLL 407
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
394-543 |
2.33e-11 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 65.79 E-value: 2.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 394 GYYRNPEATRRalssdgmWFRTGDIGYLDSEGYLYIQTRDTDVFKFNNFQIYPEQIEEFILRLPGVSEACVFGIPDAV-S 472
Cdd:PRK07445 314 GYYPQILDSQG-------IFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHwG 386
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19922652 473 TNLTACAVvrtksPEGERLTADHIRNIVEHHLSGAYHIRggvYFI--DSLPKTPNDKLQRRKVL-GLVQQLELK 543
Cdd:PRK07445 387 EVVTAIYV-----PKDPSISLEELKTAIKDQLSPFKQPK---HWIpvPQLPRNPQGKINRQQLQqIAVQRLGLP 452
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
49-530 |
8.06e-11 |
|
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.
Pssm-ID: 341231 [Multi-domain] Cd Length: 571 Bit Score: 64.68 E-value: 8.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 49 DTTGQE---LTGAQLAQQSARIAQAF-KRLGLRRGDVVGISANNSTYLTSVIIAALLRG---IPINPLHPE----FTEET 117
Cdd:cd05905 6 DSKGKEattLTWGKLLSRAEKIAAVLqKKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGvvpIPIEPPDISqqlgFLLGT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 118 VKYMYDITepkVIFCDVENyhiIKTVNGKLQNPAKIYLVngKLEGVLDISEmLNDEDSITAAAYVPCPKLHGDHTAFIVC 197
Cdd:cd05905 86 CKVRVALT---VEACLKGL---PKKLLKSKTAAEIAKKK--GWPKILDFVK-IPKSKRSKLKKWGPHPPTRDGDTAYIEY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 198 SSGTTGMPKGVTRSHRSLLCNCKNPNT---YTRDSVLLSFSPLYWISGTII-LLASLLNGCRRI------ITNRPYSvey 267
Cdd:cd05905 157 SFSSDGSLSGVAVSHSSLLAHCRALKEaceLYESRPLVTVLDFKSGLGLWHgCLLSVYSGHHTIlippelMKTNPLL--- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 268 LLQLVARHKVTFLFLASHQIALLSKHDSDVMELKAQ----LQSIRVL-IGAGSKVCKAVCRRMYELIGNQ---------- 332
Cdd:cd05905 234 WLQTLSQYKVRDAYVKLRTLHWCLKDLSSTLASLKNrdvnLSSLRMCmVPCENRPRISSCDSFLKLFQTLglspravste 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 333 ------RFV---------VGYGLSEMGGLSKNVGGPVG---------CE-GKVMRNVELRVLD-KLKMPLGINEVGIIYA 386
Cdd:cd05905 314 fgtrvnPFIcwqgtsgpePSRVYLDMRALRHGVVRLDErdkpnslplQDsGKVLPGAQVAIVNpETKGLCKDGEIGEIWV 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 387 RLRFKWAGYYRNP-------EATRRALSSDGM----WFRTGDIGYL------DSEGY----LYIQTRDTDVFKFNNFQIY 445
Cdd:cd05905 394 NSPANASGYFLLDgetndtfKVFPSTRLSTGItnnsYARTGLLGFLrptkctDLNVEehdlLFVVGSIDETLEVRGLRHH 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 446 PEQIEEFILRlpgvSEACVFGIPDAVSTNLTACaVVRTKsPEGERLTADHIRNIV-----EHHLsgayhIRGGVYFID-- 518
Cdd:cd05905 474 PSDIEATVMR----VHPYRGRCAVFSITGLVVV-VAEQP-PGSEEEALDLVPLVLnaileEHQV-----IVDCVALVPpg 542
|
570
....*....|..
gi 19922652 519 SLPKTPNDKLQR 530
Cdd:cd05905 543 SLPKNPLGEKQR 554
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
52-531 |
8.26e-11 |
|
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: 64.38 E-value: 8.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 52 GQELTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNSTYLTSVIIAALLRGIPINPLHPEFTEETVKYMYDITEPKVIF 131
Cdd:cd17644 23 DQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLDPNYPQERLTYILEDAQISVLL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 132 CDVENYhiiktvngklqnpakiylvngklegvldisemlndedsitaaayvpcpklhgdhtAFIVCSSGTTGMPKGVTRS 211
Cdd:cd17644 103 TQPENL-------------------------------------------------------AYVIYTSGSTGKPKGVMIE 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 212 HRSLLCNC----KNPNTYTRDSVLLSFSPLYWISGTIILLaSLLNGCRRIItnRP----YSVEYLLQLVARHKVTFLFLA 283
Cdd:cd17644 128 HQSLVNLShgliKEYGITSSDRVLQFASIAFDVAAEEIYV-TLLSGATLVL--RPeemrSSLEDFVQYIQQWQLTVLSLP 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 284 SHQIALLSkhDSDVMELKAQLQSIRVLIGAGSKVCKAVCRRMYELIGNQ-RFVVGYGLSE-------------MGGLSKN 349
Cdd:cd17644 205 PAYWHLLV--LELLLSTIDLPSSLRLVIVGGEAVQPELVRQWQKNVGNFiQLINVYGPTEatiaatvcrltqlTERNITS 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 350 VggPVgceGKVMRNVELRVLDKLKMPLGINEVGIIY------ARlrfkwaGYYRNPEATRRALSSDGM-------WFRTG 416
Cdd:cd17644 283 V--PI---GRPIANTQVYILDENLQPVPVGVPGELHiggvglAR------GYLNRPELTAEKFISHPFnsseserLYKTG 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 417 DIG-YLDSEGYLYIQTRDTDVfKFNNFQIYPEQIEEFILRLPGVSEACVfgipdavstnltacaVVRTKSPEGERLTA-- 493
Cdd:cd17644 352 DLArYLPDGNIEYLGRIDNQV-KIRGFRIELGEIEAVLSQHNDVKTAVV---------------IVREDQPGNKRLVAyi 415
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 19922652 494 ----DHIRNIVE--HHLSG---AYHIRGGVYFIDSLPKTPNDKLQRR 531
Cdd:cd17644 416 vphyEESPSTVElrQFLKAklpDYMIPSAFVVLEELPLTPNGKIDRR 462
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
52-468 |
1.96e-10 |
|
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: 63.08 E-value: 1.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 52 GQELTGAQLAQQSARIAQAFKR-LGLRRGDVVGISANNSTYLTSVIIAALLRGIPINPLHPEFTEETVKYMYDITEPKVI 130
Cdd:cd05938 3 GETYTYRDVDRRSNQAARALLAhAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAKVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 131 FCDVENYHIIKTVNGKL-QNPAKIYLVNGKL--EGVLDISEMLNDEDSITAAAYVPCPkLHGDHTAFIVCSSGTTGMPKG 207
Cdd:cd05938 83 VVAPELQEAVEEVLPALrADGVSVWYLSHTSntEGVISLLDKVDAASDEPVPASLRAH-VTIKSPALYIYTSGTTGLPKA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 208 VTRSHRSLL--------CNCknpntyTRDSVLLSFSPLYWISGTIILLAsllnGCrriitnrpysVEYLLQLVARHKvtf 279
Cdd:cd05938 162 ARISHLRVLqcsgflslCGV------TADDVIYITLPLYHSSGFLLGIG----GC----------IELGATCVLKPK--- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 280 lFLASHQIALLSKHDSDVM----EL---------KAQLQSIRVLIGAGSKVCKAVCRRMYELIGNQRFVVGYGLSE--MG 344
Cdd:cd05938 219 -FSASQFWDDCRKHNVTVIqyigELlrylcnqpqSPNDRDHKVRLAIGNGLRADVWREFLRRFGPIRIREFYGSTEgnIG 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 345 GLskNVGGPVGCEGKV-----------------MRNVELRVLDKLKMPLGINEVGIIYARLRFK--WAGYYRNPEATRRA 405
Cdd:cd05938 298 FF--NYTGKIGAVGRVsylykllfpfelikfdvEKEEPVRDAQGFCIPVAKGEPGLLVAKITQQspFLGYAGDKEQTEKK 375
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19922652 406 LSSD-----GMWFRTGDIGYLDSEGYLYIQTRDTDVFKFNNFQIYPEQIEEFILRLPGVSEACVFGIP 468
Cdd:cd05938 376 LLRDvfkkgDVYFNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVYGVT 443
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
190-432 |
2.00e-10 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 63.58 E-value: 2.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 190 DHTAFIVCSSGTTGMPKGVTRSHRSLLCNCKNPNT---YTRDSVLLSFSPLYWISG-TIILLASLLNGCRRIITNRPYSV 265
Cdd:PRK08043 365 EDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTiadFTPNDRFMSALPLFHSFGlTVGLFTPLLTGAEVFLYPSPLHY 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 266 EYLLQLVARHKVTFLFLASHQIALLSK--HDSDVMELKaqlqsirvLIGAGSKVCKAVCRRMYELIGNQRFVVGYGLSEM 343
Cdd:PRK08043 445 RIVPELVYDRNCTVLFGTSTFLGNYARfaNPYDFARLR--------YVVAGAEKLQESTKQLWQDKFGLRILEGYGVTEC 516
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 344 GG-LSKNV--GGPVGCEGKVMRNVELRVldkLKMPlGINEVG--------IIYARLRFKWAGYYRNPEATRRALSSDGMW 412
Cdd:PRK08043 517 APvVSINVpmAAKPGTVGRILPGMDARL---LSVP-GIEQGGrlqlkgpnIMNGYLRVEKPGVLEVPTAENARGEMERGW 592
|
250 260
....*....|....*....|
gi 19922652 413 FRTGDIGYLDSEGYLYIQTR 432
Cdd:PRK08043 593 YDTGDIVRFDEQGFVQIQGR 612
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
55-534 |
3.97e-10 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 62.55 E-value: 3.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 55 LTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNSTYLTSVIIAALLRGIPINPLHPEFTEETVKYMYDITEPKVIFCDV 134
Cdd:PLN02861 78 LTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVSIAFVQE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 135 ENYHIIKTVNGKLQNPAKIYLVNGKLEGV-------LDISEMLNDEDSITAAAYVPCPKLHGDHTAFIVCSSGTTGMPKG 207
Cdd:PLN02861 158 SKISSILSCLPKCSSNLKTIVSFGDVSSEqkeeaeeLGVSCFSWEEFSLMGSLDCELPPKQKTDICTIMYTSGTTGEPKG 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 208 VTRSHRSLLCNCKNPN--------TYTRDSVLLSFSPL----------YWIS-GTII----------------LLASLLN 252
Cdd:PLN02861 238 VILTNRAIIAEVLSTDhllkvtdrVATEEDSYFSYLPLahvydqvietYCISkGASIgfwqgdirylmedvqaLKPTIFC 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 253 GCRRIItNRPYS------------VEYLLQLVARHKVTFLFLASHQIALLSKHDSDVME-LKAQLQS-IRVLIGAGSKVC 318
Cdd:PLN02861 318 GVPRVY-DRIYTgimqkissggmlRKKLFDFAYNYKLGNLRKGLKQEEASPRLDRLVFDkIKEGLGGrVRLLLSGAAPLP 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 319 KAVcRRMYELIGNQRFVVGYGLSEMGGLS----KNVGGPVGCEGKVMRNVELRVLDKLKM---PLGINEVGIIYARLRFK 391
Cdd:PLN02861 397 RHV-EEFLRVTSCSVLSQGYGLTESCGGCftsiANVFSMVGTVGVPMTTIEARLESVPEMgydALSDVPRGEICLRGNTL 475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 392 WAGYYRNPEATRRALSsDGmWFRTGDIGYLDSEGYLYIQTRDTDVFKFNNFQ-IYPEQIEEFILRLPGVSEACVFG---- 466
Cdd:PLN02861 476 FSGYHKRQDLTEEVLI-DG-WFHTGDIGEWQPNGAMKIIDRKKNIFKLSQGEyVAVENLENTYSRCPLIASIWVYGnsfe 553
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 467 -------IPD-------AVSTNLTACAVVRTKSPEGERLTADHIRNI-VEHHLSG-----AYHIRGGVYFIDSLPKTPND 526
Cdd:PLN02861 554 sflvavvVPDrqaledwAANNNKTGDFKSLCKNLKARKYILDELNSTgKKLQLRGfemlkAIHLEPNPFDIERDLITPTF 633
|
....*...
gi 19922652 527 KLQRRKVL 534
Cdd:PLN02861 634 KLKRPQLL 641
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
178-470 |
4.69e-10 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 62.68 E-value: 4.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 178 AAAYVPCPKLHGDHTAFIVCSSGTTGMPKGVTRSHRSLLCNCKNPNT---YTRDSVLLSFSPLY----WISGTIIllaSL 250
Cdd:PRK06814 781 RFPLVYFCNRDPDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAAridFSPEDKVFNALPVFhsfgLTGGLVL---PL 857
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 251 LNGCRRIITNRPYSVEYLLQLVARHKVTFL-----FLASHQialLSKHDSDvmelkaqLQSIRvLIGAGSKVCKAVCRRM 325
Cdd:PRK06814 858 LSGVKVFLYPSPLHYRIIPELIYDTNATILfgtdtFLNGYA---RYAHPYD-------FRSLR-YVFAGAEKVKEETRQT 926
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 326 YELIGNQRFVVGYGLSEMG-GLSKNVggP----VGCEGKVMRNVELRvLDKLKmplGINEVGiiyaRLRFK----WAGYY 396
Cdd:PRK06814 927 WMEKFGIRILEGYGVTETApVIALNT--PmhnkAGTVGRLLPGIEYR-LEPVP---GIDEGG----RLFVRgpnvMLGYL 996
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19922652 397 R--NPEATRRAlsSDGmWFRTGDIGYLDSEGYLYIQTRDTDVFKFNNFQIYPEQIEEFILRL-PGVSEACVfGIPDA 470
Cdd:PRK06814 997 RaeNPGVLEPP--ADG-WYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELwPDALHAAV-SIPDA 1069
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
55-481 |
7.30e-10 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 61.65 E-value: 7.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 55 LTGAQLAQQSARIAQAFKRLGLRRGDVVGI-SANNSTYLtsVIIAALLRGIPIN-PLHPEFTEETVKYMYDITEPKVIFC 132
Cdd:PLN02736 79 MTYGEAGTARTAIGSGLVQHGIPKGACVGLyFINRPEWL--IVDHACSAYSYVSvPLYDTLGPDAVKFIVNHAEVAAIFC 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 133 DVENYHIIKTVNGKLQNPAKIYLVNGKLEG-----------VLDISEMLNdEDSITAAAYVPcPKLHGdhTAFIVCSSGT 201
Cdd:PLN02736 157 VPQTLNTLLSCLSEIPSVRLIVVVGGADEPlpslpsgtgveIVTYSKLLA-QGRSSPQPFRP-PKPED--VATICYTSGT 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 202 TGMPKGVTRSHRSLLCN----CKNPNTYTRDsVLLSFSPLYWISGTIILLASLLNGCR-------------RIITNRPY- 263
Cdd:PLN02736 233 TGTPKGVVLTHGNLIANvagsSLSTKFYPSD-VHISYLPLAHIYERVNQIVMLHYGVAvgfyqgdnlklmdDLAALRPTi 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 264 --SVEYLLQLV-------------ARHKVTFLFLASHQIALLSKHDSDVM-------ELKAQLQSiRV-LIGAGSKVCKA 320
Cdd:PLN02736 312 fcSVPRLYNRIydgitnavkesggLKERLFNAAYNAKKQALENGKNPSPMwdrlvfnKIKAKLGG-RVrFMSSGASPLSP 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 321 VCRRMYELIGNQRFVVGYGLSEMG----------GLSKNVGGPVGCegkvmrnVELRVLDKLKMPLGINEV----GIIYA 386
Cdd:PLN02736 391 DVMEFLRICFGGRVLEGYGMTETScvisgmdegdNLSGHVGSPNPA-------CEVKLVDVPEMNYTSEDQpyprGEICV 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 387 RLRFKWAGYYRNPEATRRALSSDGmWFRTGDIGYLDSEGYLYIQTRDTDVFKFNNFQ-IYPEQIEEFILRLPGVSEACVF 465
Cdd:PLN02736 464 RGPIIFKGYYKDEVQTREVIDEDG-WLHTGDIGLWLPGGRLKIIDRKKNIFKLAQGEyIAPEKIENVYAKCKFVAQCFVY 542
|
490
....*....|....*.
gi 19922652 466 GipDAVSTNLTACAVV 481
Cdd:PLN02736 543 G--DSLNSSLVAVVVV 556
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
53-417 |
1.26e-09 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 60.66 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 53 QELTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNSTYLTSVIIAALLRGIPINPLHP-------EFTEetVKYMYDIT 125
Cdd:PRK08180 68 RRLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALAAMYAGVPYAPVSPayslvsqDFGK--LRHVLELL 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 126 EPKVIFCDvenyhiiktvNGKLQNPA---------KIYLVNGKLEG--VLDISEMLNDEDSITA-AAYvpcPKLHGDHTA 193
Cdd:PRK08180 146 TPGLVFAD----------DGAAFARAlaavvpadvEVVAVRGAVPGraATPFAALLATPPTAAVdAAH---AAVGPDTIA 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 194 FIVCSSGTTGMPKGVTRSHRSLlcnCKN--------PNTYTRDSVLLSFSP--------------LYWiSGTI-I----- 245
Cdd:PRK08180 213 KFLFTSGSTGLPKAVINTHRML---CANqqmlaqtfPFLAEEPPVLVDWLPwnhtfggnhnlgivLYN-GGTLyIddgkp 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 246 ---LLASLLNGCRRII----TNRPYSVEYLLQL------VARH---KVTFLFLAShqiALLSKHDSDVMElkaqlqsirv 309
Cdd:PRK08180 289 tpgGFDETLRNLREISptvyFNVPKGWEMLVPAlerdaaLRRRffsRLKLLFYAG---AALSQDVWDRLD---------- 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 310 ligagsKVCKAVC-RRMyelignqRFVVGYGLSEMGGL----------SKNVGGPV-GCEGKVmrnveLRVLDKLKMplg 377
Cdd:PRK08180 356 ------RVAEATCgERI-------RMMTGLGMTETAPSatfttgplsrAGNIGLPApGCEVKL-----VPVGGKLEV--- 414
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 19922652 378 inevgiiyarlRFK----WAGYYRNPEATRRALSSDGmWFRTGD 417
Cdd:PRK08180 415 -----------RVKgpnvTPGYWRAPELTAEAFDEEG-YYRSGD 446
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
53-212 |
1.60e-09 |
|
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: 60.36 E-value: 1.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 53 QELTGAQLAQQSARIAQAFKRLGLRRGD-VVGISANNSTYLTSVIIAALLRGIpINPLHPEFTEETVKYMYDITEPKVIF 131
Cdd:cd05943 97 TEVTWAELRRRVARLAAALRALGVKPGDrVAGYLPNIPEAVVAMLATASIGAI-WSSCSPDFGVPGVLDRFGQIEPKVLF 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 132 -CDVENYhiiktvNGKLQN------------PAKIYLV---NGKLEGVLDISEMLND---EDSITAAAYVPCP--KLHGD 190
Cdd:cd05943 176 aVDAYTY------NGKRHDvrekvaelvkglPSLLAVVvvpYTVAAGQPDLSKIAKAltlEDFLATGAAGELEfePLPFD 249
|
170 180
....*....|....*....|..
gi 19922652 191 HTAFIVCSSGTTGMPKGVTRSH 212
Cdd:cd05943 250 HPLYILYSSGTTGLPKCIVHGA 271
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
56-440 |
3.40e-09 |
|
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: 59.37 E-value: 3.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 56 TGAQLAQQSARIAQAFKRLGLRRGDVVGISANNSTYLTSVIIAALLRGIPINPLHPEFTEET-----VKYMYDITEPKVI 130
Cdd:cd05921 27 TYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSPAYSLMSqdlakLKHLFELLKPGLV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 131 FC-DVENYH-IIKTVngKLQNPAKIYLVN-GKLEGVLDISEMLndEDSITAAAYVPCPKLHGDHTAFIVCSSGTTGMPKG 207
Cdd:cd05921 107 FAqDAAPFArALAAI--FPLGTPLVVSRNaVAGRGAISFAELA--ATPPTAAVDAAFAAVGPDTVAKFLFTSGSTGLPKA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 208 VTRSHRSLlcnCKNP----NTYTR----DSVLLSFSPlyW---ISGTIILLASLLNGCRRIITN---RPYSVEYLLQLVA 273
Cdd:cd05921 183 VINTQRML---CANQamleQTYPFfgeePPVLVDWLP--WnhtFGGNHNFNLVLYNGGTLYIDDgkpMPGGFEETLRNLR 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 274 RHKVTFLFLASHQIALLSKHDSDVMELKAQ-LQSIRVLIGAGSKVCKAVCRRMYEL----IGNQ-RFVVGYGLSEMGGL- 346
Cdd:cd05921 258 EISPTVYFNVPAGWEMLVAALEKDEALRRRfFKRLKLMFYAGAGLSQDVWDRLQALavatVGERiPMMAGLGATETAPTa 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 347 ---------SKNVGGPV-GCEGKVMRN---VELRVLDKLKMPlginevgiiyarlrfkwaGYYRNPEATRRALSSDGmWF 413
Cdd:cd05921 338 tfthwpterSGLIGLPApGTELKLVPSggkYEVRVKGPNVTP------------------GYWRQPELTAQAFDEEG-FY 398
|
410 420 430
....*....|....*....|....*....|.
gi 19922652 414 RTGDIGYL----DSEGYLYIQTRDTDVFKFN 440
Cdd:cd05921 399 CLGDAAKLadpdDPAKGLVFDGRVAEDFKLA 429
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
53-212 |
7.56e-09 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 58.27 E-value: 7.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 53 QELTGAQLAQQSARIAQAFKRLGLRRGDVVgisannSTYLTSVI--IAALLRGIPINPL----HPEFTEETVKYMYDITE 126
Cdd:PRK03584 113 RELSWAELRRQVAALAAALRALGVGPGDRV------AAYLPNIPetVVAMLATASLGAIwsscSPDFGVQGVLDRFGQIE 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 127 PKVIFCdVENYH----------IIKTVNGKLQNPAKIYLVN--------GKLEGVLDISEMLNDEDSiTAAAYVPCPklh 188
Cdd:PRK03584 187 PKVLIA-VDGYRyggkafdrraKVAELRAALPSLEHVVVVPylgpaaaaAALPGALLWEDFLAPAEA-AELEFEPVP--- 261
|
170 180
....*....|....*....|....
gi 19922652 189 GDHTAFIVCSSGTTGMPKGVTRSH 212
Cdd:PRK03584 262 FDHPLWILYSSGTTGLPKCIVHGH 285
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
192-450 |
1.27e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 57.64 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 192 TAFIVCSSGTTGMPKGVTRSHRSLLCNCKN---------PNTYTRDSVLLSFSPLYWISGTII-LLASLLNGCRRIITNr 261
Cdd:PRK05850 162 TAYLQYTSGSTRTPAGVMVSHRNVIANFEQlmsdyfgdtGGVPPPDTTVVSWLPFYHDMGLVLgVCAPILGGCPAVLTS- 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 262 PysVEYL------LQLVARHKVT------FLF-LASHQIAllskhDSDVMELkaQLQSIRVLIGAGSKVCKAVCRRMyel 328
Cdd:PRK05850 241 P--VAFLqrparwMQLLASNPHAfsaapnFAFeLAVRKTS-----DDDMAGL--DLGGVLGIISGSERVHPATLKRF--- 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 329 igNQRF--------VV--GYGLSEM---------GGLSKNV---------GGPVGCEG---------KVMRNVELRVLD- 370
Cdd:PRK05850 309 --ADRFapfnlretAIrpSYGLAEAtvyvatrepGQPPESVrfdyeklsaGHAKRCETgggtplvsyGSPRSPTVRIVDp 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 371 --KLKMPLGIneVGIIYARLRFKWAGYYRNPEATRR----------ALSSDGMWFRTGDIGYLdSEGYLYIQTRDTDVFK 438
Cdd:PRK05850 387 dtCIECPAGT--VGEIWVHGDNVAAGYWQKPEETERtfgatlvdpsPGTPEGPWLRTGDLGFI-SEGELFIVGRIKDLLI 463
|
330
....*....|..
gi 19922652 439 FNNFQIYPEQIE 450
Cdd:PRK05850 464 VDGRNHYPDDIE 475
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
55-418 |
1.98e-08 |
|
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: 57.08 E-value: 1.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 55 LTGAQLAQQSARIAQAFK-RLGLRRGDVVGISANNSTYLTSVIIAALLRGIPINPLHPEFTEETVKYMYDITEPKVIFCD 133
Cdd:cd17632 68 ITYAELWERVGAVAAAHDpEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLAVS 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 134 VENYHIIKTVNGKLQNPAKIYLVNGKLEG-----VLDIS--------------EMLNDEDSITAAAYVPCPKLHGDHTAF 194
Cdd:cd17632 148 AEHLDLAVEAVLEGGTPPRLVVFDHRPEVdahraALESArerlaavgipvttlTLIAVRGRDLPPAPLFRPEPDDDPLAL 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 195 IVCSSGTTGMPKGVTRSHRSL----LCNCKNPNTYTRDSVLLSFSPLYWISGTIILLASLLNGCRRIITNRPySVEYLLQ 270
Cdd:cd17632 228 LIYTSGSTGTPKGAMYTERLVatfwLKVSSIQDIRPPASITLNFMPMSHIAGRISLYGTLARGGTAYFAAAS-DMSTLFD 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 271 LVARHKVTFLFLASHQIALLSKH---------------DSDVMELKAQLQSiRVLigaGSKVCKAVC---------RRMY 326
Cdd:cd17632 307 DLALVRPTELFLVPRVCDMLFQRyqaeldrrsvagadaETLAERVKAELRE-RVL---GGRLLAAVCgsaplsaemKAFM 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 327 ELIGNQRFVVGYGLSEMGGLSKNvggpvgceGKVMRNvelRVLD-KLkmpLGINEVGII-----YAR--LRFK----WAG 394
Cdd:cd17632 383 ESLLDLDLHDGYGSTEAGAVILD--------GVIVRP---PVLDyKL---VDVPELGYFrtdrpHPRgeLLVKtdtlFPG 448
|
410 420
....*....|....*....|....
gi 19922652 395 YYRNPEATRRALSSDGmWFRTGDI 418
Cdd:cd17632 449 YYKRPEVTAEVFDEDG-FYRTGDV 471
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
186-528 |
1.87e-07 |
|
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: 53.63 E-value: 1.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 186 KLHGDHTAFIVCSSGTTGMPKGVTRSHRSL---------LCNCknpntyTRDSVLLSFSPLYWISGTIILLASLLNGCRR 256
Cdd:cd17654 114 IRTDECLAYVIHTSGTTGTPKIVAVPHKCIlpniqhfrsLFNI------TSEDILFLTSPLTFDPSVVEIFLSLSSGATL 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 257 IITnrPYSVEYLLQLVA-----RHKVTFLFL----------ASHQIALLSKHdsdvmelkaqlQSIRVLIGAGSKVCKAV 321
Cdd:cd17654 188 LIV--PTSVKVLPSKLAdilfkRHRITVLQAtptlfrrfgsQSIKSTVLSAT-----------SSLRVLALGGEPFPSLV 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 322 CRRMYELIGNQRFVVG-YGLSEM-----------GGLSKNVGGPVG---CEGKVMRNVELRVLDKLKmplGINEVGIIya 386
Cdd:cd17654 255 ILSSWRGKGNRTRIFNiYGITEVscwalaykvpeEDSPVQLGSPLLgtvIEVRDQNGSEGTGQVFLG---GLNRVCIL-- 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 387 rlrfkwAGYYRNPEATRRAlssdgmwfrTGDIgyLDSE-GYLYIQTRDTDVFKFNNFQIYPEQIEEFILRLPGVsEACVF 465
Cdd:cd17654 330 ------DDEVTVPKGTMRA---------TGDF--VTVKdGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGV-ESCAV 391
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19922652 466 GIPDavSTNLTACAVVRTKSpegerltaDHIRNIVEHHLSGAYHIRGGVYFIDSLPKTPNDKL 528
Cdd:cd17654 392 TLSD--QQRLIAFIVGESSS--------SRIHKELQLTLLSSHAIPDTFVQIDKLPLTSHGKV 444
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
52-467 |
2.92e-05 |
|
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: 46.65 E-value: 2.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 52 GQELTGAQLAQQSARIAQAFKRLGLRRGDVVGISANNSTYLTSV--------IIAAL----LRGipinplhpefteetvk 119
Cdd:cd05939 1 DRHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALwlglakigVETALinsnLRL---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 120 ymyditEPKVifcdvenyHIIKTVNGKlqnpAKIYLVNGKLEgvLDISEMLNDEDsitaaayvpcPKLHGDHTAFIVcSS 199
Cdd:cd05939 65 ------ESLL--------HCITVSKAK----ALIFNLLDPLL--TQSSTEPPSQD----------DVNFRDKLFYIY-TS 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 200 GTTGMPKGVTRSH-RSLLCNCKNPNTY--TRDSVLLSFSPLYWISGTIILLAS-LLNGcrriitnrpysveylLQLVARH 275
Cdd:cd05939 114 GTTGLPKAAVIVHsRYYRIAAGAYYAFgmRPEDVVYDCLPLYHSAGGIMGVGQaLLHG---------------STVVIRK 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 276 KvtflFLASHQIALLSKHDSDVMELKAQLqsIRVLIGAgsKVCKAVCR-RMYELIGN-----------QRFVVG-----Y 338
Cdd:cd05939 179 K----FSASNFWDDCVKYNCTIVQYIGEI--CRYLLAQ--PPSEEEQKhNVRLAVGNglrpqiweqfvRRFGIPqigefY 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 339 GLSEMGGLSKNVGGPVGCEGKVMR----------------NVEL-RVLDKLKMPLGINEVGIIYARLR-----FKWAGYY 396
Cdd:cd05939 251 GATEGNSSLVNIDNHVGACGFNSRilpsvypirlikvdedTGELiRDSDGLCIPCQPGEPGLLVGKIIqndplRRFDGYV 330
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19922652 397 rNPEATRRALSSD-----GMWFRTGDIGYLDSEGYLYIQTRDTDVFKFNNFQIYPEQIEEFILRLPGVSEACVFGI 467
Cdd:cd05939 331 -NEGATNKKIARDvfkkgDSAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVYGV 405
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
173-541 |
1.11e-04 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 44.76 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 173 EDSITAAAYVPCPKLHGDHTAFIVC--SSGTTGMPKGVTRSHRSLLCNCKNPNTYTR----DSVLLSFSPLYWISGTIIL 246
Cdd:PRK05851 133 DLATAAHTNRSASLTPPDSGGPAVLqgTAGSTGTPRTAILSPGAVLSNLRGLNARVGldaaTDVGCSWLPLYHDMGLAFL 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 247 LASLLNGCR------RIITNRPYSveyLLQLVARHKVTFLFLASHQIALLSKHDSDVMELkaQLQSIRVLIGAGSKV-CK 319
Cdd:PRK05851 213 LTAALAGAPlwlaptTAFSASPFR---WLSWLSDSRATLTAAPNFAYNLIGKYARRVSDV--DLGALRVALNGGEPVdCD 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 320 AVCRRMYELignQRF-------VVGYGLSE-----------MGGLSKNVGGPVGCE-------GKVMRNVELRVLDKlKM 374
Cdd:PRK05851 288 GFERFATAM---APFgfdagaaAPSYGLAEstcavtvpvpgIGLRVDEVTTDDGSGarrhavlGNPIPGMEVRISPG-DG 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 375 PLGIN--EVGIIYARLRFKWAGYYrnPEATRRAlssdGMWFRTGDIGYLdSEGYLYIQTRDTDVFKFNNFQIYPEQIEEF 452
Cdd:PRK05851 364 AAGVAgrEIGEIEIRGASMMSGYL--GQAPIDP----DDWFPTGDLGYL-VDGGLVVCGRAKELITVAGRNIFPTEIERV 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 453 ILRLPGVSEACVFgipdAVSTN-------LTACAVVRTKSPEGERltadhiRNIVEHHLSGAYHIRGGVYFID--SLPKT 523
Cdd:PRK05851 437 AAQVRGVREGAVV----AVGTGegsarpgLVIAAEFRGPDEAGAR------SEVVQRVASECGVVPSDVVFVApgSLPRT 506
|
410
....*....|....*...
gi 19922652 524 PNDKLQRrkvLGLVQQLE 541
Cdd:PRK05851 507 SSGKLRR---LAVKRSLE 521
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
394-450 |
1.84e-04 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 44.35 E-value: 1.84e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19922652 394 GYYRNPEATRR----ALSS-------------DGMWFRTGDIG-YLDSEgyLYIQTRDTDVFKFNNFQIYPEQIE 450
Cdd:PRK12476 442 GYWGRPEETERtfgaKLQSrlaegshadgaadDGTWLRTGDLGvYLDGE--LYITGRIADLIVIDGRNHYPQDIE 514
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
337-466 |
5.26e-04 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 42.70 E-value: 5.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 337 GYGLSE--MGGLSK--NVGGPVGCEGKVMRNVELRVLDKLKM---PLGINEVGIIYARLRFKWAGYYRNPEATRRALSsD 409
Cdd:PLN02614 417 GYGLTEscAGTFVSlpDELDMLGTVGPPVPNVDIRLESVPEMeydALASTPRGEICIRGKTLFSGYYKREDLTKEVLI-D 495
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 19922652 410 GmWFRTGDIGYLDSEGYLYIQTRDTDVFKFNNFQ-IYPEQIEEFILRLPGVSEACVFG 466
Cdd:PLN02614 496 G-WLHTGDVGEWQPNGSMKIIDRKKNIFKLSQGEyVAVENIENIYGEVQAVDSVWVYG 552
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
190-427 |
9.53e-04 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 42.01 E-value: 9.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 190 DHTAFIVCSSGTTGMPKGVTRSHRSL------LCNCknpntytrdSVLLSFSPLYWIS---------GTIILLASLLNGC 254
Cdd:PTZ00342 304 DFITSIVYTSGTSGKPKGVMLSNKNLyntvvpLCKH---------SIFKKYNPKTHLSylpishiyeRVIAYLSFMLGGT 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 255 RRI-------------------------ITNRPYSVeyLLQLVARHKVTFLFLASHQIAL-LSKHD---SDVME------ 299
Cdd:PTZ00342 375 INIwskdinyfskdiynskgnilagvpkVFNRIYTN--IMTEINNLPPLKRFLVKKILSLrKSNNNggfSKFLEgithis 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 300 --LKAQLQ-SIRVLIGAGSKVCKAVCRRMYELIgNQRFVVGYGLSEMGGL----------SKNVGGPVGCEGKvmrnVEL 366
Cdd:PTZ00342 453 skIKDKVNpNLEVILNGGGKLSPKIAEELSVLL-NVNYYQGYGLTETTGPifvqhaddnnTESIGGPISPNTK----YKV 527
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19922652 367 RVLDKLK----MPLGinEVgIIYARLRFKwaGYYRNPEATRRALSSDGmWFRTGDIGYLDSEGYL 427
Cdd:PTZ00342 528 RTWETYKatdtLPKG--EL-LIKSDSIFS--GYFLEKEQTKNAFTEDG-YFKTGDIVQINKNGSL 586
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
393-438 |
1.45e-03 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 41.26 E-value: 1.45e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 19922652 393 AGYYRNPEATRRALSSD--GM-WFRTGDIGYLDSEGYLYIQTRDTDVFK 438
Cdd:PLN02387 514 LGYFKNQEKTDEVYKVDerGMrWFYTGDIGQFHPDGCLEIIDRKKDIVK 562
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
410-531 |
6.54e-03 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 39.35 E-value: 6.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922652 410 GMWFrTGDIGYLDSEGYLYIQTRDTDVFKFNNFQIYPEQIEEFILRLPGVSEACVFGIPDAVSTN-LTACAVVRTKSPEG 488
Cdd:PRK00174 483 GMYF-TGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQgIYAFVTLKGGEEPS 561
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 19922652 489 ERLTADhIRNIVEHHLsGAYHIRGGVYFIDSLPKTPNDKLQRR 531
Cdd:PRK00174 562 DELRKE-LRNWVRKEI-GPIAKPDVIQFAPGLPKTRSGKIMRR 602
|
|
| |
