|
Name |
Accession |
Description |
Interval |
E-value |
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
66-578 |
0e+00 |
|
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: 679.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 66 DKLAIVDDSGSHSYRDLYGSSRGLAGRIKAALDcpsgDLQGKRISFLCANDASYTVAQWASWMCGGTAVPLYREHPPSEL 145
Cdd:cd05941 1 DRIAIVDDGDSITYADLVARAARLANRLLALGK----DLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 146 EYIISDSQSSLLVagqpyadtmeplahrlglpylqlpptsslsslleapenqpepgitdwaqRPAMIIYTSGTTGRPKGV 225
Cdd:cd05941 77 EYVITDSEPSLVL-------------------------------------------------DPALILYTSGTTGRPKGV 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 226 LHTHSNIQAMVQGLVSEWGWSRDDVILHTLPLHHVHGIVNKLLCPLWVGATTVMLPTFQPQkvwEVLLSSKAPMVTVFMA 305
Cdd:cd05941 108 VLTHANLAANVRALVDAWRWTEDDVLLHVLPLHHVHGLVNALLCPLFAGASVEFLPKFDPK---EVAISRLMPSITVFMG 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 306 VPTIYSKLIQHYEQHFTQPrvqDFVRAACKERIRLMVSGSSALPQPTLLRWEEITGHTLLERYGMTEIGMALSNPLKGPR 385
Cdd:cd05941 185 VPTIYTRLLQYYEAHFTDP---QFARAAAAERLRLMVSGSAALPVPTLEEWEAITGHTLLERYGMTEIGMALSNPLDGER 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 386 IPGAVGVPLPGVEVRIVMTNATsttiaegnsretqvRPGLEGKEGELMVRGDQVFTEYWNKPEATRESFTEDGWFKTGDT 465
Cdd:cd05941 262 RPGTVGMPLPGVQARIVDEETG--------------EPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGWFKTGDL 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 466 AVYK-NGVYWIMGRTSVDIIKSGGYKISALEVERHLLAHPDITDVAVIGARDATWGQKVTAVVQLKRGR-SMTLSELKTW 543
Cdd:cd05941 328 GVVDeDGYYWILGRSSVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGAaALSLEELKEW 407
|
490 500 510
....*....|....*....|....*....|....*
gi 1367478878 544 AREHMAPYTIPTGLVLVEEMPRNQMGKVNKKDLLK 578
Cdd:cd05941 408 AKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
60-580 |
6.38e-142 |
|
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: 418.44 E-value: 6.38e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 60 RAQVYRDKLAIVDDSGSHSYRDLYGSSRGLAGRIKAAldcpsGDLQGKRISFLCANDASYTVAQWASWMCGGTAVPLYRE 139
Cdd:COG0318 8 AAARHPDRPALVFGGRRLTYAELDARARRLAAALRAL-----GVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 140 HPPSELEYIISDSQSSLLVAgqpyadtmeplahrlglpylqlpptsslsslleapenqpepgitdwaqrpAMIIYTSGTT 219
Cdd:COG0318 83 LTAEELAYILEDSGARALVT--------------------------------------------------ALILYTSGTT 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 220 GRPKGVLHTHSNIQAMVQGLVSEWGWSRDDVILHTLPLHHVHGIVNKLLCPLWVGATTVMLPTFQPQKVWEVLLSSKapm 299
Cdd:COG0318 113 GRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLPRFDPERVLELIERER--- 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 300 VTVFMAVPTIYSKLIQHYEQHFTqprvqDFvraackERIRLMVSGSSALPQPTLLRWEEITGHTLLERYGMTEIGMALS- 378
Cdd:COG0318 190 VTVLFGVPTMLARLLRHPEFARY-----DL------SSLRLVVSGGAPLPPELLERFEERFGVRIVEGYGLTETSPVVTv 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 379 NPL-KGPRIPGAVGVPLPGVEVRIVmtnatsttiaegnSRETQVRPglEGKEGELMVRGDQVFTEYWNKPEATRESFtED 457
Cdd:COG0318 259 NPEdPGERRPGSVGRPLPGVEVRIV-------------DEDGRELP--PGEVGEIVVRGPNVMKGYWNDPEATAEAF-RD 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 458 GWFKTGDTAVY-KNGVYWIMGRTSvDIIKSGGYKISALEVERHLLAHPDITDVAVIGARDATWGQKVTAVVQLKRGRSMT 536
Cdd:COG0318 323 GWLRTGDLGRLdEDGYLYIVGRKK-DMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPGAELD 401
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1367478878 537 LSELKTWAREHMAPYTIPTGLVLVEEMPRNQMGKVNKKDLLKHF 580
Cdd:COG0318 402 AEELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRERY 445
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
61-576 |
9.52e-112 |
|
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: 341.85 E-value: 9.52e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 61 AQVYRDKLAIVDDSGSHSYRDLYGSSRGLAGRIKAaLDCPSGDlqgkRISFLCANDASYTVAQWASWMCGGTAV---PLY 137
Cdd:cd05936 9 ARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQN-LGVQPGD----RVALMLPNCPQFPIAYFGALKAGAVVVplnPLY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 138 REHppsELEYIISDSQSSLLVAGQPYADTMEPLAhrlglpylqlpptsslsSLLEAPENQPEpgitDwaqrPAMIIYTSG 217
Cdd:cd05936 84 TPR---ELEHILNDSGAKALIVAVSFTDLLAAGA-----------------PLGERVALTPE----D----VAVLQYTSG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 218 TTGRPKGVLHTHSNIQAMVQGlVSEW---GWSRDDVILHTLPLHHVHGIVNKLLCPLWVGATTVMLPTFQPQKVWEVLls 294
Cdd:cd05936 136 TTGVPKGAMLTHRNLVANALQ-IKAWledLLEGDDVVLAALPLFHVFGLTVALLLPLALGATIVLIPRFRPIGVLKEI-- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 295 sKAPMVTVFMAVPTIYSKLIQHYEqhftqprvqdfVRAACKERIRLMVSGSSALPQPTLLRWEEITGHTLLERYGMTEIG 374
Cdd:cd05936 213 -RKHRVTIFPGVPTMYIALLNAPE-----------FKKRDFSSLRLCISGGAPLPVEVAERFEELTGVPIVEGYGLTETS 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 375 -MALSNPLKGPRIPGAVGVPLPGVEVRIVmtnatsttiaegnSRETQVRPglEGKEGELMVRGDQVFTEYWNKPEATRES 453
Cdd:cd05936 281 pVVAVNPLDGPRKPGSIGIPLPGTEVKIV-------------DDDGEELP--PGEVGELWVRGPQVMKGYWNRPEETAEA 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 454 FTeDGWFKTGDTAVY-KNGVYWIMGRTSvDIIKSGGYKISALEVERHLLAHPDITDVAVIGARDATWGQKVTAVVQLKRG 532
Cdd:cd05936 346 FV-DGWLRTGDIGYMdEDGYFFIVDRKK-DMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEG 423
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1367478878 533 RSMTLSELKTWAREHMAPYTIPTGLVLVEEMPRNQMGKVNKKDL 576
Cdd:cd05936 424 ASLTEEEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRREL 467
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
69-577 |
2.88e-110 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 338.12 E-value: 2.88e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 69 AIVDDSGSHSYRDLYGSSRGLAGRIKAAldcpsgdlqgKRISFLCANDASYTVAQWASWMCGGTAVPLYREHPPSELEYI 148
Cdd:PRK07787 18 AVRIGGRVLSRSDLAGAATAVAERVAGA----------RRVAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAERRHI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 149 ISDSQSSLLVAGQPyadtmeplAHRLGLPYLQLPPTSslssllEAPENQPEPGitdwAQRPAMIIYTSGTTGRPKGVLHT 228
Cdd:PRK07787 88 LADSGAQAWLGPAP--------DDPAGLPHVPVRLHA------RSWHRYPEPD----PDAPALIVYTSGTTGPPKGVVLS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 229 HSNIQAMVQGLVSEWGWSRDDVILHTLPLHHVHGIVNKLLCPLWVGATTVMLPTFQPQKVWEVlLSSKApmvTVFMAVPT 308
Cdd:PRK07787 150 RRAIAADLDALAEAWQWTADDVLVHGLPLFHVHGLVLGVLGPLRIGNRFVHTGRPTPEAYAQA-LSEGG---TLYFGVPT 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 309 IYSKLiqhyeqhftqprVQDFVRAACKERIRLMVSGSSALPQPTLLRWEEITGHTLLERYGMTEIGMALSNPLKGPRIPG 388
Cdd:PRK07787 226 VWSRI------------AADPEAARALRGARLLVSGSAALPVPVFDRLAALTGHRPVERYGMTETLITLSTRADGERRPG 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 389 AVGVPLPGVEVRIVMTNATSTTiAEGNSRetqvrpglegkeGELMVRGDQVFTEYWNKPEATRESFTEDGWFKTGDTAVY 468
Cdd:PRK07787 294 WVGLPLAGVETRLVDEDGGPVP-HDGETV------------GELQVRGPTLFDGYLNRPDATAAAFTADGWFRTGDVAVV 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 469 K-NGVYWIMGRTSVDIIKSGGYKISALEVERHLLAHPDITDVAVIGARDATWGQKVTAVVQlkRGRSMTLSELKTWAREH 547
Cdd:PRK07787 361 DpDGMHRIVGRESTDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVV--GADDVAADELIDFVAQQ 438
|
490 500 510
....*....|....*....|....*....|
gi 1367478878 548 MAPYTIPTGLVLVEEMPRNQMGKVNKKDLL 577
Cdd:PRK07787 439 LSVHKRPREVRFVDALPRNAMGKVLKKQLL 468
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
65-576 |
1.38e-109 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 337.23 E-value: 1.38e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 65 RDKLAIVDDSGSH-SYRDLYGSSRGLAGRIkAALDCPSGDlqgkRISFLCANDASYTVAQWASWMCGGTAVPLYREHPPS 143
Cdd:PRK07514 16 RDAPFIETPDGLRyTYGDLDAASARLANLL-VALGVKPGD----RVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 144 ELEYIISDSQSSLLVAGQPYADTMEPLAHRLGLPYLQLPPTSSLSSLLEAPENQPEPGITdwAQR----PAMIIYTSGTT 219
Cdd:PRK07514 91 ELDYFIGDAEPALVVCDPANFAWLSKIAAAAGAPHVETLDADGTGSLLEAAAAAPDDFET--VPRgaddLAAILYTSGTT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 220 GRPKGVLHTHSNIQAMVQGLVSEWGWSRDDVILHTLPLHHVHGIVNKLLCPLWVGATTVMLPTFQPQKVWEVLlsskaPM 299
Cdd:PRK07514 169 GRSKGAMLSHGNLLSNALTLVDYWRFTPDDVLIHALPIFHTHGLFVATNVALLAGASMIFLPKFDPDAVLALM-----PR 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 300 VTVFMAVPTIYSKLIQHyeqhftqPRvqdFVRAACKeRIRLMVSGSSALPQPTLLRWEEITGHTLLERYGMTEIGMALSN 379
Cdd:PRK07514 244 ATVMMGVPTFYTRLLQE-------PR---LTREAAA-HMRLFISGSAPLLAETHREFQERTGHAILERYGMTETNMNTSN 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 380 PLKGPRIPGAVGVPLPGVEVRIVmTNATSTTIAEGnsrETqvrpglegkeGELMVRGDQVFTEYWNKPEATRESFTEDGW 459
Cdd:PRK07514 313 PYDGERRAGTVGFPLPGVSLRVT-DPETGAELPPG---EI----------GMIEVKGPNVFKGYWRMPEKTAEEFRADGF 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 460 FKTGDTA-VYKNGVYWIMGRtSVDIIKSGGYKISALEVERHLLAHPDITDVAVIGARDATWGQKVTAVVQLKRGRSMTLS 538
Cdd:PRK07514 379 FITGDLGkIDERGYVHIVGR-GKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKPGAALDEA 457
|
490 500 510
....*....|....*....|....*....|....*...
gi 1367478878 539 ELKTWAREHMAPYTIPTGLVLVEEMPRNQMGKVNKKDL 576
Cdd:PRK07514 458 AILAALKGRLARFKQPKRVFFVDELPRNTMGKVQKNLL 495
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
208-571 |
1.29e-103 |
|
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: 316.15 E-value: 1.29e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 208 RPAMIIYTSGTTGRPKGVLHTHSNIQAMVQGLVSEWGWSRDDVILHTLPLHHVHGIvNKLLCPLWVGATTVMLPTFQPQK 287
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGL-FGLLGALLAGGTVVLLPKFDPEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 288 VWEVLlssKAPMVTVFMAVPTIYSKLIQHYEQHftqPRVQDFVRAACkerirlmvSGSSALPQPTLLRWEEITGHTLLER 367
Cdd:cd04433 80 ALELI---EREKVTILLGVPTLLARLLKAPESA---GYDLSSLRALV--------SGGAPLPPELLERFEEAPGIKLVNG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 368 YGMTEIG--MALSNPLKGPRIPGAVGVPLPGVEVRIVmtnatsttIAEGnsretqvRPGLEGKEGELMVRGDQVFTEYWN 445
Cdd:cd04433 146 YGLTETGgtVATGPPDDDARKPGSVGRPVPGVEVRIV--------DPDG-------GELPPGEIGELVVRGPSVMKGYWN 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 446 KPEATREsFTEDGWFKTGDTAVY-KNGVYWIMGRTSvDIIKSGGYKISALEVERHLLAHPDITDVAVIGARDATWGQKVT 524
Cdd:cd04433 211 NPEATAA-VDEDGWYRTGDLGRLdEDGYLYIVGRLK-DMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVV 288
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1367478878 525 AVVQLKRGRSMTLSELKTWAREHMAPYTIPTGLVLVEEMPRNQMGKV 571
Cdd:cd04433 289 AVVVLRPGADLDAEELRAHVRERLAPYKVPRRVVFVDALPRTASGKI 335
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
60-573 |
5.34e-101 |
|
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: 313.01 E-value: 5.34e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 60 RAQVYRDKLAIVDDSGSHSYRDLygssRGLAGRIKAALdCPSGDLQGKRISFLCANDASYTVAQWASWMCGGTAVPL-YR 138
Cdd:cd17631 4 RARRHPDRTALVFGGRSLTYAEL----DERVNRLAHAL-RALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLnFR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 139 EHPPsELEYIISDSQSSLLVAgqpyadtmeplahrlglpylqlpptsslsslleapenqpepgitDwaqrPAMIIYTSGT 218
Cdd:cd17631 79 LTPP-EVAYILADSGAKVLFD--------------------------------------------D----LALLMYTSGT 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 219 TGRPKGVLHTHSNIQAMVQGLVSEWGWSRDDVILHTLPLHHVHGIVNKLLCPLWVGATTVMLPTFQPQKVWEVLLSSKap 298
Cdd:cd17631 110 TGRPKGAMLTHRNLLWNAVNALAALDLGPDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVILRKFDPETVLDLIERHR-- 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 299 mVTVFMAVPTIYSKLIQHyeQHFTQPRVQdfvraackeRIRLMVSGSSALPQPTLLRWEEItGHTLLERYGMTEIGMALS 378
Cdd:cd17631 188 -VTSFFLVPTMIQALLQH--PRFATTDLS---------SLRAVIYGGAPMPERLLRALQAR-GVKFVQGYGMTETSPGVT 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 379 npLKGP----RIPGAVGVPLPGVEVRIVMTNAtsttiaegnsretqvRPGLEGKEGELMVRGDQVFTEYWNKPEATRESF 454
Cdd:cd17631 255 --FLSPedhrRKLGSAGRPVFFVEVRIVDPDG---------------REVPPGEVGEIVVRGPHVMAGYWNRPEATAAAF 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 455 tEDGWFKTGDTAVY-KNGVYWIMGRTSvDIIKSGGYKISALEVERHLLAHPDITDVAVIGARDATWGQKVTAVVQLKRGR 533
Cdd:cd17631 318 -RDGWFHTGDLGRLdEDGYLYIVDRKK-DMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPGA 395
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1367478878 534 SMTLSELKTWAREHMAPYTIPTGLVLVEEMPRNQMGKVNK 573
Cdd:cd17631 396 ELDEDELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
61-576 |
1.13e-100 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 314.82 E-value: 1.13e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 61 AQVYRDKLAIVDDSGSHSYRDLYGSSRGLAGRIKAAldcpsGDLQGKRISFLCANDASYTVAQWASWMCGGTAVPLYREH 140
Cdd:PRK06187 16 ARKHPDKEAVYFDGRRTTYAELDERVNRLANALRAL-----GVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPINIRL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 141 PPSELEYIISDSQSSLLVAGQPYADTMEPLAHRL----------GLPYLQLPPTS-SLSSLLEA-PENQPEPGITdwAQR 208
Cdd:PRK06187 91 KPEEIAYILNDAEDRVVLVDSEFVPLLAAILPQLptvrtvivegDGPAAPLAPEVgEYEELLAAaSDTFDFPDID--END 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 209 PAMIIYTSGTTGRPKGVLHTHSNIQAMVQGLVSEWGWSRDDVILHTLPLHHVHGIVNKLLcPLWVGATTVMLPTFQPQKV 288
Cdd:PRK06187 169 AAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVPMFHVHAWGLPYL-ALMAGAKQVIPRRFDPENL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 289 WEVLLSSKapmVTVFMAVPTIYSKLIQHYEQHFtqprvQDFVRaackerIRLMVSGSSALPQPTLLRWEEITGHTLLERY 368
Cdd:PRK06187 248 LDLIETER---VTFFFAVPTIWQMLLKAPRAYF-----VDFSS------LRLVIYGGAALPPALLREFKEKFGIDLVQGY 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 369 GMTEIGMALS-NPLK-----GPRIPGAVGVPLPGVEVRIVmtnatsttiaegNSRETQVRPglEGKE-GELMVRGDQVFT 441
Cdd:PRK06187 314 GMTETSPVVSvLPPEdqlpgQWTKRRSAGRPLPGVEARIV------------DDDGDELPP--DGGEvGEIIVRGPWLMQ 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 442 EYWNKPEATRESFtEDGWFKTGDTAVY-KNGVYWIMGRTSvDIIKSGGYKISALEVERHLLAHPDITDVAVIGARDATWG 520
Cdd:PRK06187 380 GYWNRPEATAETI-DGGWLHTGDVGYIdEDGYLYITDRIK-DVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWG 457
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1367478878 521 QKVTAVVQLKRGRSMTLSELKTWAREHMAPYTIPTGLVLVEEMPRNQMGKVNKKDL 576
Cdd:PRK06187 458 ERPVAVVVLKPGATLDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVL 513
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
65-578 |
3.55e-94 |
|
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: 297.30 E-value: 3.55e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 65 RDKLAIVDDSGSHSYRDLYGSSRGLAGRIkAALDCPSGDlqgkRISFLCANDASYTVAQWASWMCGGTAVPLYREHPPSE 144
Cdd:cd05926 3 APALVVPGSTPALTYADLAELVDDLARQL-AALGIKKGD----RVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 145 LEYIISDSQSSLLVAGQPYADTMEPLAHRLGLPYLQL----------PPTSSLSSLLEAPENQPEPGITDwAQRPAMIIY 214
Cdd:cd05926 78 FEFYLADLGSKLVLTPKGELGPASRAASKLGLAILELaldvgvliraPSAESLSNLLADKKNAKSEGVPL-PDDLALILH 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 215 TSGTTGRPKGVLHTHSNIQAMVQGLVSEWGWSRDDVILHTLPLHHVHGIVNKLLCPLWVGATTVMLPTFQPQKVWEvllS 294
Cdd:cd05926 157 TSGTTGRPKGVPLTHRNLAASATNITNTYKLTPDDRTLVVMPLFHVHGLVASLLSTLAAGGSVVLPPRFSASTFWP---D 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 295 SKAPMVTVFMAVPTIYSKLIQHYEQHFTQPRVqdfvraackeRIRLMVSGSSALPQPTLLRWEEITGHTLLERYGMTEIG 374
Cdd:cd05926 234 VRDYNATWYTAVPTIHQILLNRPEPNPESPPP----------KLRFIRSCSASLPPAVLEALEATFGAPVLEAYGMTEAA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 375 --MAlSNPLK-GPRIPGAVGVPLpGVEVRIVMtnatsttiAEGNSREtqvrpglEGKEGELMVRGDQVFTEYWNKPEATR 451
Cdd:cd05926 304 hqMT-SNPLPpGPRKPGSVGKPV-GVEVRILD--------EDGEILP-------PGVVGEICLRGPNVTRGYLNNPEANA 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 452 ESFTEDGWFKTGDTAVYK-NGVYWIMGRTSvDIIKSGGYKISALEVERHLLAHPDITDVAVIGARDATWGQKVTAVVQLK 530
Cdd:cd05926 367 EAAFKDGWFRTGDLGYLDaDGYLFLTGRIK-ELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLR 445
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1367478878 531 RGRSMTLSELKTWAREHMAPYTIPTGLVLVEEMPRNQMGKVNKKDLLK 578
Cdd:cd05926 446 EGASVTEEELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKVAE 493
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
57-576 |
1.25e-88 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 283.33 E-value: 1.25e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 57 VFSRAQVYRDKLAIVDDSGSHSYRDLYGSSRGLAGRIKAaldcpSGDLQGKRISFLCANDASYTVAQWASWMCGGTAVPL 136
Cdd:PRK07656 11 LARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAA-----LGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 137 YREHPPSELEYIISDSQSSLLVAGQPYADTMEPLAHRLglPYLQL-------------PPTSSLSSLLEAPEN-QPEPGI 202
Cdd:PRK07656 86 NTRYTADEAAYILARGDAKALFVLGLFLGVDYSATTRL--PALEHvviceteeddphtEKMKTFTDFLAAGDPaERAPEV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 203 TDwaQRPAMIIYTSGTTGRPKGVLHTHSNIQAMVQGLVSEWGWSRDDVILHTLPLHHVHGIVNKLLCPLWVGATTVMLPT 282
Cdd:PRK07656 164 DP--DDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLAANPFFHVFGYKAGVNAPLMRGATILPLPV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 283 FQPQKVWEVLLSSKApmvTVFMAVPTIYSKLIQHYEQhftqpRVQDFvraackERIRLMVSGSSALPQPTLLRWEEITG- 361
Cdd:PRK07656 242 FDPDEVFRLIETERI---TVLPGPPTMYNSLLQHPDR-----SAEDL------SSLRLAVTGAASMPVALLERFESELGv 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 362 HTLLERYGMTE-IGMALSNPLKGPR--IPGAVGVPLPGVEVRIVmtnatsttiaegnsrETQVRPGLEGKEGELMVRGDQ 438
Cdd:PRK07656 308 DIVLTGYGLSEaSGVTTFNRLDDDRktVAGTIGTAIAGVENKIV---------------NELGEEVPVGEVGELLVRGPN 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 439 VFTEYWNKPEATRESFTEDGWFKTGDTAVY-KNGVYWIMGRTSvDIIKSGGYKISALEVERHLLAHPDITDVAVIGARDA 517
Cdd:PRK07656 373 VMKGYYDDPEATAAAIDADGWLHTGDLGRLdEEGYLYIVDRKK-DMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDE 451
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1367478878 518 TWGQKVTAVVQLKRGRSMTLSELKTWAREHMAPYTIPTGLVLVEEMPRNQMGKVNKKDL 576
Cdd:PRK07656 452 RLGEVGKAYVVLKPGAELTEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRAL 510
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
60-487 |
4.57e-87 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 276.12 E-value: 4.57e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 60 RAQVYRDKLAIVDDSG-SHSYRDLYGSSRGLAGRIKAAldcpsGDLQGKRISFLCANDASYTVAQWASWMCGGTAVPLYR 138
Cdd:pfam00501 4 QAARTPDKTALEVGEGrRLTYRELDERANRLAAGLRAL-----GVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 139 EHPPSELEYIISDSQSSLLVAGQ--------PYADTMEPLAHRLGLPYLQLPPTSSLSSLLEAPENQPEPGITDWAQRPA 210
Cdd:pfam00501 79 RLPAEELAYILEDSGAKVLITDDalkleellEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVPPPPPPPPDPDDLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 211 MIIYTSGTTGRPKGVLHTHSNIQAMVQGLVSE----WGWSRDDVILHTLPLHHVHGIVNKLLCPLWVGATTVMLPTFQPQ 286
Cdd:pfam00501 159 YIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVrprgFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVVLPPGFPAL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 287 KVWEVLLSSKAPMVTVFMAVPTIYSKLIQHyeqhftqprvqDFVRAACKERIRLMVSGSSALPQPTLLRWEEITGHTLLE 366
Cdd:pfam00501 239 DPAALLELIERYKVTVLYGVPTLLNMLLEA-----------GAPKRALLSSLRLVLSGGAPLPPELARRFRELFGGALVN 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 367 RYGMTEIGMALSNPLKGP---RIPGAVGVPLPGVEVRIVmtnatstTIAEGNSRETqvrpgleGKEGELMVRGDQVFTEY 443
Cdd:pfam00501 308 GYGLTETTGVVTTPLPLDedlRSLGSVGRPLPGTEVKIV-------DDETGEPVPP-------GEPGELCVRGPGVMKGY 373
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1367478878 444 WNKPEATRESFTEDGWFKTGDTAVY-KNGVYWIMGRTSvDIIKSG 487
Cdd:pfam00501 374 LNDPELTAEAFDEDGWYRTGDLGRRdEDGYLEIVGRKK-DQIKLG 417
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
78-575 |
9.67e-87 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 280.35 E-value: 9.67e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 78 SYRDLYGSSRGLAGRIKAAldcpsGDLQGKRISFLCANDASYTVAQWASWMCGGTAV---PLYREHppsELEYIISDSQS 154
Cdd:PRK05605 59 TYAELGKQVRRAAAGLRAL-----GVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVehnPLYTAH---ELEHPFEDHGA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 155 SLLVAGQPYADTMEPL------------------------AHRLGLPYL-----QL----PPTSSLSSLLEAPE------ 195
Cdd:PRK05605 131 RVAIVWDKVAPTVERLrrttpletivsvnmiaampllqrlALRLPIPALrkaraALtgpaPGTVPWETLVDAAIggdgsd 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 196 -NQPEPGITDwaqrPAMIIYTSGTTGRPKGVLHTHSNIQA-MVQGL--VSEWGwSRDDVILHTLPLHHVHGIVNKLLCPL 271
Cdd:PRK05605 211 vSHPRPTPDD----VALILYTSGTTGKPKGAQLTHRNLFAnAAQGKawVPGLG-DGPERVLAALPMFHAYGLTLCLTLAV 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 272 WVGATTVMLPTFQPQKVWEVLlssKAPMVTVFMAVPTIYSKLiqhyeqhftqprvqdfvRAACKER------IRLMVSGS 345
Cdd:PRK05605 286 SIGGELVLLPAPDIDLILDAM---KKHPPTWLPGVPPLYEKI-----------------AEAAEERgvdlsgVRNAFSGA 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 346 SALPQPTLLRWEEITGHTLLERYGMTEIG-MALSNPLKGPRIPGAVGVPLPGVEVRIVMTNATSTTIAEGnsretqvrpg 424
Cdd:PRK05605 346 MALPVSTVELWEKLTGGLLVEGYGLTETSpIIVGNPMSDDRRPGYVGVPFPDTEVRIVDPEDPDETMPDG---------- 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 425 legKEGELMVRGDQVFTEYWNKPEATRESFtEDGWFKTGDTAVYK-NGVYWIMGRTSvDIIKSGGYKISALEVERHLLAH 503
Cdd:PRK05605 416 ---EEGELLVRGPQVFKGYWNRPEETAKSF-LDGWFRTGDVVVMEeDGFIRIVDRIK-ELIITGGFNVYPAEVEEVLREH 490
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1367478878 504 PDITDVAVIGARDATWGQKVTAVVQLKRGRSMTLSELKTWAREHMAPYTIPTGLVLVEEMPRNQMGKVNKKD 575
Cdd:PRK05605 491 PGVEDAAVVGLPREDGSEEVVAAVVLEPGAALDPEGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRRE 562
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
58-571 |
3.78e-85 |
|
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: 274.25 E-value: 3.78e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 58 FSRAQVYRDKLAIVDDSGSHSYRDLYGSSRGLAGRIKAAldcpsGDLQGKRISFLCANDASYTVAQWASWMCGGTAVPLY 137
Cdd:cd05959 11 LNLNEGRGDKTAFIDDAGSLTYAELEAEARRVAGALRAL-----GVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 138 REHPPSELEYIISDSQSSLLVAGQPYADTMEPLAHRLGL---------PYLQLPPTSSLSSLLEAPENQPEPGITdWAQR 208
Cdd:cd05959 86 TLLTPDDYAYYLEDSRARVVVVSGELAPVLAAALTKSEHtlvvlivsgGAGPEAGALLLAELVAAEAEQLKPAAT-HADD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 209 PAMIIYTSGTTGRPKGVLHTHSNIQAMVQGLVSE-WGWSRDDVILHTLPLHHVHGIVNKLLCPLWVGATTVMLPTF-QPQ 286
Cdd:cd05959 165 PAFWLYSSGSTGRPKGVVHLHADIYWTAELYARNvLGIREDDVCFSAAKLFFAYGLGNSLTFPLSVGATTVLMPERpTPA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 287 KVWEVLLSSKApmvTVFMAVPTIYSKLIQHYEqhftqPRVQDFVraackeRIRLMVSGSSALPQPTLLRWEEITGHTLLE 366
Cdd:cd05959 245 AVFKRIRRYRP---TVFFGVPTLYAAMLAAPN-----LPSRDLS------SLRLCVSAGEALPAEVGERWKARFGLDILD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 367 RYGMTEIG-MALSNpLKGPRIPGAVGVPLPGVEVRIVmtnatsttiaegNSRETQVRpglEGKEGELMVRGDQVFTEYWN 445
Cdd:cd05959 311 GIGSTEMLhIFLSN-RPGRVRYGTTGKPVPGYEVELR------------DEDGGDVA---DGEPGELYVRGPSSATMYWN 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 446 KPEATRESFtEDGWFKTGDTAVYK-NGVYWIMGRTSvDIIKSGGYKISALEVERHLLAHPDITDVAVIGARDATWGQKVT 524
Cdd:cd05959 375 NRDKTRDTF-QGEWTRTGDKYVRDdDGFYTYAGRAD-DMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPK 452
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1367478878 525 AVVQLKRGRSMT---LSELKTWAREHMAPYTIPTGLVLVEEMPRNQMGKV 571
Cdd:cd05959 453 AFVVLRPGYEDSealEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKI 502
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
61-571 |
1.71e-83 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 271.21 E-value: 1.71e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 61 AQVYRDKLAI--VDDSGSH---SYRDLYGSSRGLAGRIKAAldcpsGDLQGKRISFLCANDASYTVAQWASWMCGGTAVP 135
Cdd:COG0365 19 AEGRGDKVALiwEGEDGEErtlTYAELRREVNRFANALRAL-----GVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 136 LYREHPPSELEYIISDSQSSLLVA---------GQPYADTMEP-------LAHRLGLPYLQLPPTS----SLSSLLEAPE 195
Cdd:COG0365 94 VFPGFGAEALADRIEDAEAKVLITadgglrggkVIDLKEKVDEaleelpsLEHVIVVGRTGADVPMegdlDWDELLAAAS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 196 NQPEPGITDwAQRPAMIIYTSGTTGRPKGVLHTHSNIQAMVQGLVSEW-GWSRDDVILHTLPLHHVHGIVNKLLCPLWVG 274
Cdd:COG0365 174 AEFEPEPTD-ADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYVlDLKPGDVFWCTADIGWATGHSYIVYGPLLNG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 275 ATTVML---PTFQ-PQKVWEVLlsSKAPmVTVFMAVPTIYSKLIQHYEqhftqprvqDFVRAACKERIRLMVSGSSALPQ 350
Cdd:COG0365 253 ATVVLYegrPDFPdPGRLWELI--EKYG-VTVFFTAPTAIRALMKAGD---------EPLKKYDLSSLRLLGSAGEPLNP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 351 PTLLRWEEITGHTLLERYGMTEIGMA-LSNPLKGPRIPGAVGVPLPGVEVRIVmtNAtsttiaEGNSretqVRPGlegKE 429
Cdd:COG0365 321 EVWEWWYEAVGVPIVDGWGQTETGGIfISNLPGLPVKPGSMGKPVPGYDVAVV--DE------DGNP----VPPG---EE 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 430 GELMVRGDQ--VFTEYWNKPEATRESF--TEDGWFKTGDTAVY-KNGVYWIMGRTSvDIIKSGGYKISALEVERHLLAHP 504
Cdd:COG0365 386 GELVIKGPWpgMFRGYWNDPERYRETYfgRFPGWYRTGDGARRdEDGYFWILGRSD-DVINVSGHRIGTAEIESALVSHP 464
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 505 DITDVAVIGARDATWGQKVTAVVQLKRGRSMT---LSELKTWAREHMAPYTIPTGLVLVEEMPRNQMGKV 571
Cdd:COG0365 465 AVAEAAVVGVPDEIRGQVVKAFVVLKPGVEPSdelAKELQAHVREELGPYAYPREIEFVDELPKTRSGKI 534
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
61-571 |
1.23e-79 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 260.66 E-value: 1.23e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 61 AQVYRDKLAIVDDSGSHSYRDLYGSSRGLAGRIKAALDCPSGDlqgkRISFLCANDASYTVAQWASWMCGGTAVPLYREH 140
Cdd:PRK08314 20 ARRYPDKTAIVFYGRAISYRELLEEAERLAGYLQQECGVRKGD----RVLLYMQNSPQFVIAYYAILRANAVVVPVNPMN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 141 PPSELEYIISDSQSSLLVAGQPYADTMEPLAHRLGLPYL-------QLPPTSSLS---SLLEAPENQP--EPGITDWAQ- 207
Cdd:PRK08314 96 REEELAHYVTDSGARVAIVGSELAPKVAPAVGNLRLRHVivaqysdYLPAEPEIAvpaWLRAEPPLQAlaPGGVVAWKEa 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 208 -----RP----------AMIIYTSGTTGRPKGVLHTHSNIQAMVQGLVSEWGWSRDDVILHTLPLHHVHGIVNKLLCPLW 272
Cdd:PRK08314 176 laaglAPpphtagpddlAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVLPLFHVTGMVHSMNAPIY 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 273 VGATTVMLPTfqpqkvWEVLLSSKA---PMVTVFMAVPTIYSKLiqhyeqhFTQPRVQDFvraaCKERIRLMVSGSSALP 349
Cdd:PRK08314 256 AGATVVLMPR------WDREAAARLierYRVTHWTNIPTMVVDF-------LASPGLAER----DLSSLRYIGGGGAAMP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 350 QPTLLRWEEITGHTLLERYGMTE-IGMALSNPLKGPRiPGAVGVPLPGVEVRIVmtnaTSTTIAEgnsretqVRPGlegK 428
Cdd:PRK08314 319 EAVAERLKELTGLDYVEGYGLTEtMAQTHSNPPDRPK-LQCLGIPTFGVDARVI----DPETLEE-------LPPG---E 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 429 EGELMVRGDQVFTEYWNKPEATRESFTE-DG--WFKTGDTAVYKNGVYWIMgrtsVDIIK----SGGYKISALEVERHLL 501
Cdd:PRK08314 384 VGEIVVHGPQVFKGYWNRPEATAEAFIEiDGkrFFRTGDLGRMDEEGYFFI----TDRLKrminASGFKVWPAEVENLLY 459
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1367478878 502 AHPDITDVAVIGARDATWGQKVTAVVQLKRGRSMTLS--ELKTWAREHMAPYTIPTGLVLVEEMPRNQMGKV 571
Cdd:PRK08314 460 KHPAIQEACVIATPDPRRGETVKAVVVLRPEARGKTTeeEIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKI 531
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
69-572 |
5.80e-78 |
|
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: 254.44 E-value: 5.80e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 69 AIVDDSGSH--SYRDLYGSSRGLAGRIKAAldcpsGDLQGKRISFLCANDASYTVAQWASWMCGGTAVPLYREHPPSELE 146
Cdd:cd05911 1 AQIDADTGKelTYAQLRTLSRRLAAGLRKL-----GLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 147 YIISDSQSSLLVAGQPYADTMEPLAHRLG-----------LPYLQLPPTSSLSSLLEAPENQPEPGITDwAQRPAMIIYT 215
Cdd:cd05911 76 HQLKISKPKVIFTDPDGLEKVKEAAKELGpkdkiivlddkPDGVLSIEDLLSPTLGEEDEDLPPPLKDG-KDDTAAILYS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 216 SGTTGRPKGVLHTHSNIQA---MVQGLVSEWGWSrDDVILHTLPLHHVHGIvNKLLCPLWVGATTVMLPTFQPqkvwEVL 292
Cdd:cd05911 155 SGTTGLPKGVCLSHRNLIAnlsQVQTFLYGNDGS-NDVILGFLPLYHIYGL-FTTLASLLNGATVIIMPKFDS----ELF 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 293 LSS----KapmVTVFMAVPTIYSKLIQHyeqhftqPRVQDFvRAACkerIRLMVSGSSALPQPT--LLRwEEITGHTLLE 366
Cdd:cd05911 229 LDLiekyK---ITFLYLVPPIAAALAKS-------PLLDKY-DLSS---LRVILSGGAPLSKELqeLLA-KRFPNATIKQ 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 367 RYGMTEIGMALSNPLKGPRIPGAVGVPLPGVEVRIVMtnatsttiAEGNSRETqvrpglEGKEGELMVRGDQVFTEYWNK 446
Cdd:cd05911 294 GYGMTETGGILTVNPDGDDKPGSVGRLLPNVEAKIVD--------DDGKDSLG------PNEPGEICVRGPQVMKGYYNN 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 447 PEATRESFTEDGWFKTGDTAVY-KNGVYWIMGRtSVDIIKSGGYKISALEVERHLLAHPDITDVAVIGARDATWGQKVTA 525
Cdd:cd05911 360 PEATKETFDEDGWLHTGDIGYFdEDGYLYIVDR-KKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRA 438
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1367478878 526 VVQLKRGRSMTLSELKTWAREHMAPYT-IPTGLVLVEEMPRNQMGKVN 572
Cdd:cd05911 439 YVVRKPGEKLTEKEVKDYVAKKVASYKqLRGGVVFVDEIPKSASGKIL 486
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
57-574 |
1.01e-76 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 254.64 E-value: 1.01e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 57 VFSRAQVYRDKLAIVD-DSG---SHSYRDLYGSSRGLAGRIkAALDCPSGDlqgkRISFLCANDASYTVAQWASWMCGGT 132
Cdd:COG1022 17 LRRRAARFPDRVALREkEDGiwqSLTWAEFAERVRALAAGL-LALGVKPGD----RVAILSDNRPEWVIADLAILAAGAV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 133 AVPLYREHPPSELEYIISDSQSSLLVAG-QPYADTMEPLAHRL----------GLPYLQLPPTSSLSSLLEAPENQPEPG 201
Cdd:COG1022 92 TVPIYPTSSAEEVAYILNDSGAKVLFVEdQEQLDKLLEVRDELpslrhivvldPRGLRDDPRLLSLDELLALGREVADPA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 202 itDWAQR--------PAMIIYTSGTTGRPKGVLHTHSNIQAMVQGLVSEWGWSRDDVILHTLPLHHVHGIVNKLLCpLWV 273
Cdd:COG1022 172 --ELEARraavkpddLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFLPLAHVFERTVSYYA-LAA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 274 GAT--------TVM--LPTFQPQ------KVWEVLLSS-----------KAPMVTVFMAVPTIYSKLIQHYEQHFTQPRV 326
Cdd:COG1022 249 GATvafaespdTLAedLREVKPTfmlavpRVWEKVYAGiqakaeeagglKRKLFRWALAVGRRYARARLAGKSPSLLLRL 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 327 QDF---------VRAACKERIRLMVSGSSALPqPTLLRWEEITGHTLLERYGMTEI-GMALSNPLKGPRIpGAVGVPLPG 396
Cdd:COG1022 329 KHAladklvfskLREALGGRLRFAVSGGAALG-PELARFFRALGIPVLEGYGLTETsPVITVNRPGDNRI-GTVGPPLPG 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 397 VEVRIvmtnatsttiaegnsretqvrpgleGKEGELMVRGDQVFTEYWNKPEATRESFTEDGWFKTGDtAVY--KNGVYW 474
Cdd:COG1022 407 VEVKI-------------------------AEDGEILVRGPNVMKGYYKNPEATAEAFDADGWLHTGD-IGEldEDGFLR 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 475 IMGRTSvDIIK-SGGYKISALEVERHLLAHPDITDVAVIGArdatwGQK-VTAVVQLKrgrsmtLSELKTWAREHMAPYT 552
Cdd:COG1022 461 ITGRKK-DLIVtSGGKNVAPQPIENALKASPLIEQAVVVGD-----GRPfLAALIVPD------FEALGEWAEENGLPYT 528
|
570 580
....*....|....*....|....*
gi 1367478878 553 IPTGLV---LVEEMPRNQMGKVNKK 574
Cdd:COG1022 529 SYAELAqdpEVRALIQEEVDRANAG 553
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
43-576 |
1.87e-74 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 246.38 E-value: 1.87e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 43 STRARQAAAGDsapVFSR-AQVYRDKLAIVDDSGSHSYRDLygssRGLAGRIKAALdCPSGDLQGKRISFLCANDASYTV 121
Cdd:PRK08316 5 STRARRQTIGD---ILRRsARRYPDKTALVFGDRSWTYAEL----DAAVNRVAAAL-LDLGLKKGDRVAALGHNSDAYAL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 122 AQWASWMCGGTAVPLYREHPPSELEYIISDSQSSLLVAGQPYADTMEPLAHRLGLPYLQLPPTSSLSS-----------L 190
Cdd:PRK08316 77 LWLACARAGAVHVPVNFMLTGEELAYILDHSGARAFLVDPALAPTAEAALALLPVDTLILSLVLGGREapggwldfadwA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 191 LEAPENQPEPGITDwaQRPAMIIYTSGTTGRPKGVLHTHSNIQAMVQGLVSEWGWSRDDVILHTLPLHHVHGIVNKLLCP 270
Cdd:PRK08316 157 EAGSVAEPDVELAD--DDLAQILYTSGTESLPKGAMLTHRALIAEYVSCIVAGDMSADDIPLHALPLYHCAQLDVFLGPY 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 271 LWVGATTVMLPTFQPQKVWEVLLSSKapmVTVFMAVPTIYSKLIQHYEqhFTQPRVQDFVRAackerirlmVSGSSALPQ 350
Cdd:PRK08316 235 LYVGATNVILDAPDPELILRTIEAER---ITSFFAPPTVWISLLRHPD--FDTRDLSSLRKG---------YYGASIMPV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 351 PTLLRweeitghtLLER---------YGMTEIGmalsnPLK---GP----RIPGAVGVPLPGVEVRIVmtNATSTTIAEG 414
Cdd:PRK08316 301 EVLKE--------LRERlpglrfyncYGQTEIA-----PLAtvlGPeehlRRPGSAGRPVLNVETRVV--DDDGNDVAPG 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 415 NSretqvrpglegkeGELMVRGDQVFTEYWNKPEATRESFtEDGWFKTGDTAVY-KNGVYWIMGRTSvDIIKSGGYKISA 493
Cdd:PRK08316 366 EV-------------GEIVHRSPQLMLGYWDDPEKTAEAF-RGGWFHSGDLGVMdEEGYITVVDRKK-DMIKTGGENVAS 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 494 LEVERHLLAHPDITDVAVIGARDATWGQKVTAVVQLKRGRSMTLSELKTWAREHMAPYTIPTGLVLVEEMPRNQMGKVNK 573
Cdd:PRK08316 431 REVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAGATVTEDELIAHCRARLAGFKVPKRVIFVDELPRNPSGKILK 510
|
...
gi 1367478878 574 KDL 576
Cdd:PRK08316 511 REL 513
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
78-573 |
4.30e-74 |
|
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: 243.06 E-value: 4.30e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 78 SYRDLYGSSRGLAgRIKAALDCPSGDlqgkRISFLCANDASYTVAQWASWMCGGTAVPL---YREHppsELEYIISDSQS 154
Cdd:cd05903 3 TYSELDTRADRLA-AGLAALGVGPGD----VVAFQLPNWWEFAVLYLACLRIGAVTNPIlpfFREH---ELAFILRRAKA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 155 SLLVAGQPYADTmeplahrlglpylqlpptsslsslleapENQPEPGitdwaqRPAMIIYTSGTTGRPKGVLHTHSNIQA 234
Cdd:cd05903 75 KVFVVPERFRQF----------------------------DPAAMPD------AVALLLFTSGTTGEPKGVMHSHNTLSA 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 235 MVQGLVSEWGWSRDDVILHTLPLHHVHGIVNKLLCPLWVGATTVMLPTFQPQKVWEVLLSSKapmVTVFMAVPTIYSKLI 314
Cdd:cd05903 121 SIRQYAERLGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQDIWDPDKALALMREHG---VTFMMGATPFLTDLL 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 315 QHYEQHFTQPRvqdfvraackeRIRLMVSGSSALPQPTLLRWEEITGHTLLERYGMTEIGMALSNPLKGP--RIPGAVGV 392
Cdd:cd05903 198 NAVEEAGEPLS-----------RLRTFVCGGATVPRSLARRAAELLGAKVCSAYGSTECPGAVTSITPAPedRRLYTDGR 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 393 PLPGVEVRIVmtNATSTTIAEGnsretqvrpglegKEGELMVRGDQVFTEYWNKPEATRESFtEDGWFKTGDTAVY-KNG 471
Cdd:cd05903 267 PLPGVEIKVV--DDTGATLAPG-------------VEGELLSRGPSVFLGYLDRPDLTADAA-PEGWFRTGDLARLdEDG 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 472 VYWIMGRTSvDIIKSGGYKISALEVERHLLAHPDITDVAVIGARDATWGQKVTAVVQLKRGRSMTLSELKTW-AREHMAP 550
Cdd:cd05903 331 YLRITGRSK-DIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGALLTFDELVAYlDRQGVAK 409
|
490 500
....*....|....*....|...
gi 1367478878 551 YTIPTGLVLVEEMPRNQMGKVNK 573
Cdd:cd05903 410 QYWPERLVHVDDLPRTPSGKVQK 432
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
77-576 |
9.09e-73 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 239.12 E-value: 9.09e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 77 HSYRDLYGssrgLAGRIKAALdCPSGDLQGKRISFLCANDASYTVAQWASWMCGGTAVPLYREHPPSELEYIISDSQSSL 156
Cdd:cd05934 4 WTYAELLR----ESARIAAAL-AALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 157 LVagqpyadtmeplahrlglpylqlpptsslsslleapenqpepgiTDwaqrPAMIIYTSGTTGRPKGVLHTHSNIQAMV 236
Cdd:cd05934 79 VV--------------------------------------------VD----PASILYTSGTTGPPKGVVITHANLTFAG 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 237 QGLVSEWGWSRDDVILHTLPLHHVHGIVNKLLCPLWVGATTVMLPTFQPQKVWEVLLSSKApmvTVFMAVPTIYSKLIQh 316
Cdd:cd05934 111 YYSARRFGLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLLPRFSASRFWSDVRRYGA---TVTNYLGAMLSYLLA- 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 317 yeqhfTQPRVQDfvraaCKERIRLmVSGSSALPQpTLLRWEEITGHTLLERYGMTEIGMALSNPLKGPRIPGAVGVPLPG 396
Cdd:cd05934 187 -----QPPSPDD-----RAHRLRA-AYGAPNPPE-LHEEFEERFGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAPG 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 397 VEVRIVmtnatsttiaEGNSRETQVrpgleGKEGELMVRGDQ---VFTEYWNKPEATRESFtEDGWFKTGDTAVY-KNGV 472
Cdd:cd05934 255 YEVRIV----------DDDGQELPA-----GEPGELVIRGLRgwgFFKGYYNMPEATAEAM-RNGWFHTGDLGYRdADGF 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 473 YWIMGRTSvDIIKSGGYKISALEVERHLLAHPDITDVAVIGARDATWGQKVTAVVQLKRGRSMTLSELKTWAREHMAPYT 552
Cdd:cd05934 319 FYFVDRKK-DMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLDPEELFAFCEGQLAYFK 397
|
490 500
....*....|....*....|....
gi 1367478878 553 IPTGLVLVEEMPRNQMGKVNKKDL 576
Cdd:cd05934 398 VPRYIRFVDDLPKTPTEKVAKAQL 421
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
60-576 |
9.65e-70 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 233.21 E-value: 9.65e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 60 RAQVYRDKLAIVDDSGSHSYRDLYGSSRGLAGRIKAALDCPSGDlqgkRISFLCANDASYTVAQWASWMCGGTAVPLYRE 139
Cdd:PRK06839 11 RAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIYELNVKKGE----RIAILSQNSLEYIVLLFAIAKVECIAVPLNIR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 140 HPPSELEYIISDSQSSLLVAGQPYADTMEPLAHRLGLPylqlPPTS--SLSSLLEAPENQPEPGITDwaqRPAMIIYTSG 217
Cdd:PRK06839 87 LTENELIFQLKDSGTTVLFVEKTFQNMALSMQKVSYVQ----RVISitSLKEIEDRKIDNFVEKNES---ASFIICYTSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 218 TTGRPKGVLHTHSNIQAMVQGLVSEWGWSRDDVILHTLPLHHVHGIvNKLLCPLWVGATTVMLP-TFQPQKVWEVLLSSK 296
Cdd:PRK06839 160 TTGKPKGAVLTQENMFWNALNNTFAIDLTMHDRSIVLLPLFHIGGI-GLFAFPTLFAGGVIIVPrKFEPTKALSMIEKHK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 297 apmVTVFMAVPTIYSKLIQHYEqhFTQPRVQDfvraackerIRLMVSGSSALPQPTLLRWEEiTGHTLLERYGMTE---- 372
Cdd:PRK06839 239 ---VTVVMGVPTIHQALINCSK--FETTNLQS---------VRWFYNGGAPCPEELMREFID-RGFLFGQGFGMTEtspt 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 373 IGMALSNPLKgpRIPGAVGVPLPGVEVRIVMTNATsttiaegnsretQVRPGlegKEGELMVRGDQVFTEYWNKPEATRE 452
Cdd:PRK06839 304 VFMLSEEDAR--RKVGSIGKPVLFCDYELIDENKN------------KVEVG---EVGELLIRGPNVMKEYWNRPDATEE 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 453 SFtEDGWFKTGDTA-VYKNGVYWIMGRTSvDIIKSGGYKISALEVERHLLAHPDITDVAVIGARDATWGQKVTAVVQLKR 531
Cdd:PRK06839 367 TI-QDGWLCTGDLArVDEDGFVYIVGRKK-EMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKS 444
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1367478878 532 GRSMTLSELKTWAREHMAPYTIPTGLVLVEEMPRNQMGKVNKKDL 576
Cdd:PRK06839 445 SSVLIEKDVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQL 489
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
78-574 |
5.29e-69 |
|
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: 230.17 E-value: 5.29e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 78 SYRDLYGSSRGLAGRIKAAldcpsGDLQGKRISFLCANDASYTVAQWASWMCGGTAVPLYREHPPSELEYIISDSQSSLL 157
Cdd:cd05907 7 TWAEFAEEVRALAKGLIAL-----GVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 158 VAGQPyADTmeplahrlglpylqlpptsslsslleapenqpepgitdwaqrpAMIIYTSGTTGRPKGVLHTHSNIQAMVQ 237
Cdd:cd05907 82 FVEDP-DDL-------------------------------------------ATIIYTSGTTGRPKGVMLSHRNILSNAL 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 238 GLVSEWGWSRDDVILHTLPLHHVHGIVNKLLCPLWVGATTV----------MLPTFQPqkvwevllsskapmvTVFMAVP 307
Cdd:cd05907 118 ALAERLPATEGDRHLSFLPLAHVFERRAGLYVPLLAGARIYfassaetlldDLSEVRP---------------TVFLAVP 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 308 TIYSKLIQHYEQHfTQPRVQDFVRAACK-ERIRLMVSGSSALPqPTLLRWEEITGHTLLERYGMTEIGMALS-NPLKGPR 385
Cdd:cd05907 183 RVWEKVYAAIKVK-AVPGLKRKLFDLAVgGRLRFAASGGAPLP-AELLHFFRALGIPVYEGYGLTETSAVVTlNPPGDNR 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 386 IpGAVGVPLPGVEVRIvmtnatsttiaegnsretqvrpgleGKEGELMVRGDQVFTEYWNKPEATRESFTEDGWFKTGDT 465
Cdd:cd05907 261 I-GTVGKPLPGVEVRI-------------------------ADDGEILVRGPNVMLGYYKNPEATAEALDADGWLHTGDL 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 466 AVYK-NGVYWIMGRtSVDIIK-SGGYKISALEVERHLLAHPDITDVAVIGARDAtwgqKVTAVVQLkrgrsmTLSELKTW 543
Cdd:cd05907 315 GEIDeDGFLHITGR-KKDLIItSGGKNISPEPIENALKASPLISQAVVIGDGRP----FLVALIVP------DPEALEAW 383
|
490 500 510
....*....|....*....|....*....|....
gi 1367478878 544 AREHMAPYTIPTGLV---LVEEMPRNQMGKVNKK 574
Cdd:cd05907 384 AEEHGIAYTDVAELAanpAVRAEIEAAVEAANAR 417
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
76-576 |
6.10e-69 |
|
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: 229.29 E-value: 6.10e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 76 SHSYRDLYGSSRGLAGRIKAAldcpsGDLQGKRISFLCANDASYTVAQWASWMCGGTAVPLYREHPPSELEYIISDSQSS 155
Cdd:cd05935 1 SLTYLELLEVVKKLASFLSNK-----GVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 156 LLVAGqpyadtmeplahrlglpylqlpptSSLSSLleapenqpepgitdwaqrpAMIIYTSGTTGRPKGVLHTHSNIQAM 235
Cdd:cd05935 76 VAVVG------------------------SELDDL-------------------ALIPYTSGTTGLPKGCMHTHFSAAAN 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 236 VQGLVSEWGWSRDDVILHTLPLHHVHGIVNKLLCPLWVGATTVMLPTFQPQKVWEVLLSSKapmVTVFMAVPTIYSKLIq 315
Cdd:cd05935 113 ALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMARWDRETALELIEKYK---VTFWTNIPTMLVDLL- 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 316 hyeqhfTQPRVQDFvraaCKERIRLMVSGSSALPQPTLLRWEEITGHTLLERYGMTE-IGMALSNPLKGPRIPgAVGVPL 394
Cdd:cd05935 189 ------ATPEFKTR----DLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTEtMSQTHTNPPLRPKLQ-CLGIP* 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 395 PGVEVRIVmtnatsttiaegnSRETqVRPGLEGKEGELMVRGDQVFTEYWNKPEATRESFTEDG---WFKTGDTA-VYKN 470
Cdd:cd05935 258 FGVDARVI-------------DIET-GRELPPNEVGEIVVRGPQIFKGYWNRPEETEESFIEIKgrrFFRTGDLGyMDEE 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 471 GVYWIMGRTSvDIIKSGGYKISALEVERHLLAHPDITDVAVIGARDATWGQKVTAVVQLKRGRSMTLSE--LKTWAREHM 548
Cdd:cd05935 324 GYFFFVDRVK-RMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEYRGKVTEedIIEWAREQM 402
|
490 500
....*....|....*....|....*...
gi 1367478878 549 APYTIPTGLVLVEEMPRNQMGKVNKKDL 576
Cdd:cd05935 403 AAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
57-576 |
7.64e-69 |
|
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: 230.97 E-value: 7.64e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 57 VFSRAQVYRDKLAIVDDSG--SHSYRDLYGSSRGLAgrikAALDCpSGDLQGKRISFLCANDASYTVAQWASWMCGG--- 131
Cdd:cd05904 11 SFLFASAHPSRPALIDAATgrALTYAELERRVRRLA----AGLAK-RGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAvvt 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 132 TAVPLYRehpPSELEYIISDSQSSLLVAGQPYADTMEPLAHRLGL-PYLQLPPTSSLSSLLEAPENQ-PEPGITdwAQRP 209
Cdd:cd05904 86 TANPLST---PAEIAKQVKDSGAKLAFTTAELAEKLASLALPVVLlDSAEFDSLSFSDLLFEADEAEpPVVVIK--QDDV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 210 AMIIYTSGTTGRPKGVLHTHSNIQAMVQGLVSEWG--WSRDDVILHTLPLHHVHGIVNKLLCPLWVGATTVMLPTFQPQK 287
Cdd:cd05904 161 AALLYSSGTTGRSKGVMLTHRNLIAMVAQFVAGEGsnSDSEDVFLCVLPMFHIYGLSSFALGLLRLGATVVVMPRFDLEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 288 VWEVLLSSKapmVTVFMAVPTIYSKLIQHyeqhftqPRVQDFVRAAckerIRLMVSGSSALPQPTLLRWEEITGHT-LLE 366
Cdd:cd05904 241 LLAAIERYK---VTHLPVVPPIVLALVKS-------PIVDKYDLSS----LRQIMSGAAPLGKELIEAFRAKFPNVdLGQ 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 367 RYGMTE---IGMALSNPLKGPRIPGAVGVPLPGVEVRIVMTNatsTTIAEGnsretqvrpglEGKEGELMVRGDQVFTEY 443
Cdd:cd05904 307 GYGMTEstgVVAMCFAPEKDRAKYGSVGRLVPNVEAKIVDPE---TGESLP-----------PNQTGELWIRGPSIMKGY 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 444 WNKPEATRESFTEDGWFKTGDTAVYKN-GVYWIMGRTSvDIIKSGGYKISALEVERHLLAHPDITDVAVIGARDATWGQK 522
Cdd:cd05904 373 LNNPEATAATIDKEGWLHTGDLCYIDEdGYLFIVDRLK-ELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEV 451
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1367478878 523 VTAVVQLKRGRSMTLSELKTWAREHMAPYTIPTGLVLVEEMPRNQMGKVNKKDL 576
Cdd:cd05904 452 PMAFVVRKPGSSLTEDEIMDFVAKQVAPYKKVRKVAFVDAIPKSPSGKILRKEL 505
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
64-576 |
6.34e-68 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 229.10 E-value: 6.34e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 64 YRDKLAIVDDSGSHSYRdlygssrGLAGRIK------AALDCPSGDlqgkRISFLCANDASYTVAQWASWMCGGTAVPLy 137
Cdd:PRK06188 25 YPDRPALVLGDTRLTYG-------QLADRISryiqafEALGLGTGD----AVALLSLNRPEVLMAIGAAQLAGLRRTAL- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 138 reHPPSELE---YIISDSQ-SSLLVAGQPYADTMEPLAHRL-GLPY-LQLPPTSSLSSLLEAPENQPEPGITDWAQRP-- 209
Cdd:PRK06188 93 --HPLGSLDdhaYVLEDAGiSTLIVDPAPFVERALALLARVpSLKHvLTLGPVPDGVDLLAAAAKFGPAPLVAAALPPdi 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 210 AMIIYTSGTTGRPKGVLHTHSNIQAMVQGLVSEWGWSRDDVILHTLPLHHVHGIvnKLLCPLWVGATTVMLPTFQPQKVW 289
Cdd:PRK06188 171 AGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLSHAGGA--FFLPTLLRGGTVIVLAKFDPAEVL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 290 EVLLSSKapmVTVFMAVPTIYSKLIQHyeqhftqPRVqdfvRAACKERIRLMVSGSSALpQPTLLRwE--EITGHTLLER 367
Cdd:PRK06188 249 RAIEEQR---ITATFLVPTMIYALLDH-------PDL----RTRDLSSLETVYYGASPM-SPVRLA-EaiERFGPIFAQY 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 368 YGMTEIGMALS------NPLKGPRIPGAVGVPLPGVEVRIVmtnatsttiaEGNSRETQVrpgleGKEGELMVRGDQVFT 441
Cdd:PRK06188 313 YGQTEAPMVITylrkrdHDPDDPKRLTSCGRPTPGLRVALL----------DEDGREVAQ-----GEVGEICVRGPLVMD 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 442 EYWNKPEATRESFtEDGWFKTGDTAVY-KNGVYWIMGRTSvDIIKSGGYKISALEVERHLLAHPDITDVAVIGARDATWG 520
Cdd:PRK06188 378 GYWNRPEETAEAF-RDGWLHTGDVAREdEDGFYYIVDRKK-DMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWG 455
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1367478878 521 QKVTAVVQLKRGRSMTLSELKTWAREHMAPYTIPTGLVLVEEMPRNQMGKVNKKDL 576
Cdd:PRK06188 456 EAVTAVVVLRPGAAVDAAELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKAL 511
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
60-578 |
6.01e-67 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 227.32 E-value: 6.01e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 60 RAQVYRDKLAIVDDSGShSYRdlYGSSRGLAGRIKA-ALDCpsGDLQGKRISFLCANDASYTVAQWASWMCGGTAVPLYR 138
Cdd:PRK06087 32 TARAMPDKIAVVDNHGA-SYT--YSALDHAASRLANwLLAK--GIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 139 EHPPSELEYIISDSQSSLLVAGQPYADT-MEPLAHRLG--LPYLQ-------LPPTSS---LSSLLEA--PENQPEPGIT 203
Cdd:PRK06087 107 SWREAELVWVLNKCQAKMFFAPTLFKQTrPVDLILPLQnqLPQLQqivgvdkLAPATSslsLSQIIADyePLTTAITTHG 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 204 DwaqRPAMIIYTSGTTGRPKGVLHTHSNIQAMVQGLVSEWGWSRDDVILHTLPLHHVHGIVNKLLCPLWVGATTVMLPTF 283
Cdd:PRK06087 187 D---ELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVLLDIF 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 284 QPQKVWEVLLSSKapmVTVFM-AVPTIYSkLIQHYEQHftQPRVqdfvraackERIRLMVSGSSALPQpTLLRWEEITGH 362
Cdd:PRK06087 264 TPDACLALLEQQR---CTCMLgATPFIYD-LLNLLEKQ--PADL---------SALRFFLCGGTTIPK-KVARECQQRGI 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 363 TLLERYGMTE----IGMALSNPLkgPRIPGAVGVPLPGVEVRIVmtnatsttiaEGNSREtqVRPGLEGKEGElmvRGDQ 438
Cdd:PRK06087 328 KLLSVYGSTEssphAVVNLDDPL--SRFMHTDGYAAAGVEIKVV----------DEARKT--LPPGCEGEEAS---RGPN 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 439 VFTEYWNKPEATRESFTEDGWFKTGDTAVY-KNGVYWIMGRTSvDIIKSGGYKISALEVERHLLAHPDITDVAVIGARDA 517
Cdd:PRK06087 391 VFMGYLDEPELTARALDEEGWYYSGDLCRMdEAGYIKITGRKK-DIIVRGGENISSREVEDILLQHPKIHDACVVAMPDE 469
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1367478878 518 TWGQKVTAVVQLKRG-RSMTLSELKTW-AREHMAPYTIPTGLVLVEEMPRNQMGKVNK----KDLLK 578
Cdd:PRK06087 470 RLGERSCAYVVLKAPhHSLTLEEVVAFfSRKRVAKYKYPEHIVVIDKLPRTASGKIQKfllrKDIMR 536
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
60-576 |
2.94e-66 |
|
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: 225.02 E-value: 2.94e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 60 RAQVYRDKLAIVDDSGSHSYRDLYGSSRGLAGRIkAALDCPSGDlqgkRISFLCANDASYTVAQWASWMCGgtAVPLY-- 137
Cdd:COG1021 34 RAERHPDRIAVVDGERRLSYAELDRRADRLAAGL-LALGLRPGD----RVVVQLPNVAEFVIVFFALFRAG--AIPVFal 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 138 ---REHppsELEYIISDSQSSLLVAGQPYADT-MEPLAHRL--GLPYLQL-------PPTSSLSSLLEAPENQPEPGITd 204
Cdd:COG1021 107 pahRRA---EISHFAEQSEAVAYIIPDRHRGFdYRALARELqaEVPSLRHvlvvgdaGEFTSLDALLAAPADLSEPRPD- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 205 wAQRPAMIIYTSGTTGRPKGVLHTHS----NIQAMVQglvsEWGWSRDDVILHTLPLHHvhgivN-KLLCP-----LWVG 274
Cdd:COG1021 183 -PDDVAFFQLSGGTTGLPKLIPRTHDdylySVRASAE----ICGLDADTVYLAALPAAH-----NfPLSSPgvlgvLYAG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 275 ATTVMLPTFQPQKVWEVLLSSKapmVTVFMAVPTIYSKLIQHYEQHFTQPrvqdfvraackERIRLMVSGSSALPQPTLL 354
Cdd:COG1021 253 GTVVLAPDPSPDTAFPLIERER---VTVTALVPPLALLWLDAAERSRYDL-----------SSLRVLQVGGAKLSPELAR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 355 RWEEITGHTLLERYGMTEiGMALSNPLKGPR--IPGAVGVPL-PGVEVRIVMtnatsttiAEGNsretQVRPGlegKEGE 431
Cdd:COG1021 319 RVRPALGCTLQQVFGMAE-GLVNYTRLDDPEevILTTQGRPIsPDDEVRIVD--------EDGN----PVPPG---EVGE 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 432 LMVRGDQVFTEYWNKPEATRESFTEDGWFKTGDTAVY-KNGVYWIMGRtSVDIIKSGGYKISALEVERHLLAHPDITDVA 510
Cdd:COG1021 383 LLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRtPDGYLVVEGR-AKDQINRGGEKIAAEEVENLLLAHPAVHDAA 461
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1367478878 511 VIGARDATWGQKVTAVVQLkRGRSMTLSELKTWARE-HMAPYTIPTGLVLVEEMPRNQMGKVNKKDL 576
Cdd:COG1021 462 VVAMPDEYLGERSCAFVVP-RGEPLTLAELRRFLRErGLAAFKLPDRLEFVDALPLTAVGKIDKKAL 527
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
66-573 |
5.40e-66 |
|
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: 223.56 E-value: 5.40e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 66 DKLAIVDDSGSHSYRDLYGSSRGLAGRIKAAldcpsGDLQGKRISFLCANDASYTVAQWASWMCGGTAVPLYREHPPSEL 145
Cdd:TIGR02262 20 GKTAFIDDISSLSYGELEAQVRRLAAALRRL-----GVKREERVLLLMLDGVDFPIAFLGAIRAGIVPVALNTLLTADDY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 146 EYIISDSQSSLLVAGQPYADTMEPLAHRLglPYLQ--------LPPTSSLSSLLEAPENQPEPGITDwAQRPAMIIYTSG 217
Cdd:TIGR02262 95 AYMLEDSRARVVFVSGALLPVIKAALGKS--PHLEhrvvvgrpEAGEVQLAELLATESEQFKPAATQ-ADDPAFWLYSSG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 218 TTGRPKGVLHTHSNIQAMVQGLVSE-WGWSRDDVILHTLPLHHVHGIVNKLLCPLWVGATTVML---PTfqPQKVWEVLL 293
Cdd:TIGR02262 172 STGMPKGVVHTHSNPYWTAELYARNtLGIREDDVCFSAAKLFFAYGLGNALTFPMSVGATTVLMgerPT--PDAVFDRLR 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 294 SSKApmvTVFMAVPTIYSKLIqhyeqhfTQPRvqdfVRAACKERIRLMVSGSSALPQPTLLRWEEITGHTLLERYGMTEI 373
Cdd:TIGR02262 250 RHQP---TIFYGVPTLYAAML-------ADPN----LPSEDQVRLRLCTSAGEALPAEVGQRWQARFGVDIVDGIGSTEM 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 374 G-MALSNpLKGPRIPGAVGVPLPGVEVRIVMTNATSTTiaegnsretqvrpglEGKEGELMVRGDQVFTEYWNKPEATRE 452
Cdd:TIGR02262 316 LhIFLSN-LPGDVRYGTSGKPVPGYRLRLVGDGGQDVA---------------DGEPGELLISGPSSATMYWNNRAKSRD 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 453 SFtEDGWFKTGDTAVYK-NGVYWIMGRTSvDIIKSGGYKISALEVERHLLAHPDITDVAVIGARDATWGQKVTAVVQLKR 531
Cdd:TIGR02262 380 TF-QGEWTRSGDKYVRNdDGSYTYAGRTD-DMLKVSGIYVSPFEIESALIQHPAVLEAAVVGVADEDGLIKPKAFVVLRP 457
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1367478878 532 GRSMTLSELKTWAREHMAPYTIPTGLVLVEEMPRNQMGKVNK 573
Cdd:TIGR02262 458 GQTALETELKEHVKDRLAPYKYPRWIVFVDDLPKTATGKIQR 499
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
61-573 |
1.23e-64 |
|
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: 219.48 E-value: 1.23e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 61 AQVYRDKLAIVDDSGSHSYRDLYGSSRGLAGRIKAAldcpsGDLQGKRISFLCANDASYTVAQWASWMCGGTAVPLYREH 140
Cdd:cd12118 14 AAVYPDRTSIVYGDRRYTWRQTYDRCRRLASALAAL-----GISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 141 PPSELEYIISDSQSSLLVAGQPYAdtmeplahrlglpYLQLPPTSSLSSLLEAPENQPEPgITdwaqrpamIIYTSGTTG 220
Cdd:cd12118 89 DAEEIAFILRHSEAKVLFVDREFE-------------YEDLLAEGDPDFEWIPPADEWDP-IA--------LNYTSGTTG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 221 RPKGVLHTHSNIQAMVQGLVSEWGWSRDDVILHTLPLHHVHGivnklLCPLW----VGATTVMLPTFQPQKVWEVLLSSK 296
Cdd:cd12118 147 RPKGVVYHHRGAYLNALANILEWEMKQHPVYLWTLPMFHCNG-----WCFPWtvaaVGGTNVCLRKVDAKAIYDLIEKHK 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 297 apmVTVFMAVPTIYSKLIQHYEQhftqprvqdfVRAACKERIRLMVSGSSalPQPTLLRWEEITGHTLLERYGMTEI-GM 375
Cdd:cd12118 222 ---VTHFCGAPTVLNMLANAPPS----------DARPLPHRVHVMTAGAP--PPAAVLAKMEELGFDVTHVYGLTETyGP 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 376 ALSNPLKGP----------RIPGAVGVPLPGVE-VRIVMTNATSTTIAEGnsrETQvrpglegkeGELMVRGDQVFTEYW 444
Cdd:cd12118 287 ATVCAWKPEwdelpteeraRLKARQGVRYVGLEeVDVLDPETMKPVPRDG---KTI---------GEIVFRGNIVMKGYL 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 445 NKPEATRESFtEDGWFKTGDTAV-YKNGVYWIMGRtSVDIIKSGGYKISALEVERHLLAHPDITDVAVIGARDATWGQKV 523
Cdd:cd12118 355 KNPEATAEAF-RGGWFHSGDLAViHPDGYIEIKDR-SKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVP 432
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1367478878 524 TAVVQLKRGRSMTLSELKTWAREHMAPYTIPTGLVlVEEMPRNQMGKVNK 573
Cdd:cd12118 433 CAFVELKEGAKVTEEEIIAFCREHLAGFMVPKTVV-FGELPKTSTGKIQK 481
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
60-578 |
2.33e-62 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 213.29 E-value: 2.33e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 60 RAQVYRDKLAIVDDSGSHSYRDLYGSSRGLAGRIKAAldcpsGDLQGKRISFLCANDASYTVAQWASWMCGGTAVPLYRE 139
Cdd:PRK03640 11 RAFLTPDRTAIEFEEKKVTFMELHEAVVSVAGKLAAL-----GVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 140 HPPSELEYIISDSQSSLLVAGQPYADTMEPLAhrlglpylqlppTSSLSSLLEAPENQPEPgITDWA-QRPAMIIYTSGT 218
Cdd:PRK03640 86 LSREELLWQLDDAEVKCLITDDDFEAKLIPGI------------SVKFAELMNGPKEEAEI-QEEFDlDEVATIMYTSGT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 219 TGRPKGVLHTHSNIQAMVQGLVSEWGWSRDDVILHTLPLHHVHGIvNKLLCPLWVGATTVMLPTFQPQKVWEVLLSSKap 298
Cdd:PRK03640 153 TGKPKGVIQTYGNHWWSAVGSALNLGLTEDDCWLAAVPIFHISGL-SILMRSVIYGMRVVLVEKFDAEKINKLLQTGG-- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 299 mVTVFMAVPTIYSKLIQHYEQHftqprvqdfvraACKERIRLMVSGSSALPQPTLLRWEEiTGHTLLERYGMTEIG---M 375
Cdd:PRK03640 230 -VTIISVVSTMLQRLLERLGEG------------TYPSSFRCMLLGGGPAPKPLLEQCKE-KGIPVYQSYGMTETAsqiV 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 376 ALSNPLKGPRIpGAVGVPLPGVEVRIvmtnatsttiaegnsrETQVRPGLEGKEGELMVRGDQVFTEYWNKPEATRESFt 455
Cdd:PRK03640 296 TLSPEDALTKL-GSAGKPLFPCELKI----------------EKDGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETF- 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 456 EDGWFKTGDTA-VYKNGVYWIMGRTSvDIIKSGGYKISALEVERHLLAHPDITDVAVIGARDATWGQKVTAVVqlKRGRS 534
Cdd:PRK03640 358 QDGWFKTGDIGyLDEEGFLYVLDRRS-DLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFV--VKSGE 434
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1367478878 535 MTLSELKTWAREHMAPYTIPTGLVLVEEMPRNQMGKVNKKDLLK 578
Cdd:PRK03640 435 VTEEELRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHELKQ 478
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
78-576 |
3.73e-62 |
|
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 162605 [Multi-domain] Cd Length: 436 Bit Score: 211.54 E-value: 3.73e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 78 SYRDLYGSSRGLAGRIKAaldcpSGDLQGKRISFLCANDASYTVAQWASWMCGGTAVPLYREHPPSELEYIISDSQSSLL 157
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKA-----QGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 158 VAGQPYA--DTMEPLAHRLGLPYLQlpPTSslsslLEAPENQpepgitdwaQRPAMIIYTSGTTGRPKGVLHTHSNIQAM 235
Cdd:TIGR01923 76 LTDSLLEekDFQADSLDRIEAAGRY--ETS-----LSASFNM---------DQIATLMFTSGTTGKPKAVPHTFRNHYAS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 236 VQGLVSEWGWSRDDVILHTLPLHHVHGiVNKLLCPLWVGATTVMlptfqPQKVWEVLLSSKAPMVTVFMAVPTIYSKLIQ 315
Cdd:TIGR01923 140 AVGSKENLGFTEDDNWLLSLPLYHISG-LSILFRWLIEGATLRI-----VDKFNQLLEMIANERVTHISLVPTQLNRLLD 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 316 HyeqhftqprvqdfvRAACkERIRLMVSGSSALPQPtLLRWEEITGHTLLERYGMTEIG---MALSNPLKGPRipGAVGV 392
Cdd:TIGR01923 214 E--------------GGHN-ENLRKILLGGSAIPAP-LIEEAQQYGLPIYLSYGMTETCsqvTTATPEMLHAR--PDVGR 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 393 PLPGVEVRIVmtnatsttiaegnsretqvRPGLEGkEGELMVRGDQVFTEYWNKPEAtRESFTEDGWFKTGDTAVYKN-G 471
Cdd:TIGR01923 276 PLAGREIKIK-------------------VDNKEG-HGEIMVKGANLMKGYLYQGEL-TPAFEQQGWFNTGDIGELDGeG 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 472 VYWIMGRTSvDIIKSGGYKISALEVERHLLAHPDITDVAVIGARDATWGQKVTAVVQLKRGRSMTlsELKTWAREHMAPY 551
Cdd:TIGR01923 335 FLYVLGRRD-DLIISGGENIYPEEIETVLYQHPGIQEAVVVPKPDAEWGQVPVAYIVSESDISQA--KLIAYLTEKLAKY 411
|
490 500
....*....|....*....|....*
gi 1367478878 552 TIPTGLVLVEEMPRNQMGKVNKKDL 576
Cdd:TIGR01923 412 KVPIAFEKLDELPYNASGKILRNQL 436
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
66-576 |
4.55e-61 |
|
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: 208.54 E-value: 4.55e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 66 DKLAIVDDSGSHSYRDLYGSSRGLAGRIKAAldcpsGDLQGKRISFLCANDASYTVAQWASWMCGGTAVPLYREHPPSEL 145
Cdd:cd05930 2 DAVAVVDGDQSLTYAELDARANRLARYLRER-----GVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 146 EYIISDSQSSLLvagqpyadtmeplahrlglpylqlpptsslsslLEAPENqpepgitdwaqrPAMIIYTSGTTGRPKGV 225
Cdd:cd05930 77 AYILEDSGAKLV---------------------------------LTDPDD------------LAYVIYTSGSTGKPKGV 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 226 LHTHSNIQAMVQGLVSEWGWSRDDVILHTLPLHHVHGIVNkLLCPLWVGATTVMLP---TFQPQKVWEVLLSSKapmVTV 302
Cdd:cd05930 112 MVEHRGLVNLLLWMQEAYPLTPGDRVLQFTSFSFDVSVWE-IFGALLAGATLVVLPeevRKDPEALADLLAEEG---ITV 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 303 FMAVPTIYSKLIQHYEqhftqprvqdfvRAACKeRIRLMVSGSSALPQPTLLRWEEI-TGHTLLERYGMTEI-GMALSNP 380
Cdd:cd05930 188 LHLTPSLLRLLLQELE------------LAALP-SLRLVLVGGEALPPDLVRRWRELlPGARLVNLYGPTEAtVDATYYR 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 381 LKGPRIPGA---VGVPLPGVEVRIVmtNAtsttiaegnsretQVRPGLEGKEGELMVRGDQVFTEYWNKPEATRESFTED 457
Cdd:cd05930 255 VPPDDEEDGrvpIGRPIPNTRVYVL--DE-------------NLRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPN 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 458 GWF------KTGDTAVYK-NG--VYwiMGRTSvDIIKSGGYKISALEVERHLLAHPDITDVAVIGARDATWGQKVTAVVQ 528
Cdd:cd05930 320 PFGpgermyRTGDLVRWLpDGnlEF--LGRID-DQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVV 396
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1367478878 529 LKRGRSMTLSELKTWAREHMAPYTIPTGLVLVEEMPRNQMGKVNKKDL 576
Cdd:cd05930 397 PDEGGELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
66-573 |
1.23e-60 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 210.29 E-value: 1.23e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 66 DKLAIVD---DSGSH---SYRDLygssRGLAGRIKAALdCPSGDLQGKRISFLCANDASYTVAQWASWMCGGTAVPL--- 136
Cdd:PRK13295 39 DKTAVTAvrlGTGAPrrfTYREL----AALVDRVAVGL-ARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLmpi 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 137 YREHppsELEYIISDSQSSLLVAGQPYAD-TMEPLAHRL--GLPYLQL------PPTSSLSSLLEAPENQPEPGITDWAQ 207
Cdd:PRK13295 114 FRER---ELSFMLKHAESKVLVVPKTFRGfDHAAMARRLrpELPALRHvvvvggDGADSFEALLITPAWEQEPDAPAILA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 208 RP-------AMIIYTSGTTGRPKGVLHTH----SNIQAMVQGLvsewGWSRDDVILHTLPLHHVHGIVNKLLCPLWVGAT 276
Cdd:PRK13295 191 RLrpgpddvTQLIYTSGTTGEPKGVMHTAntlmANIVPYAERL----GLGADDVILMASPMAHQTGFMYGLMMPVMLGAT 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 277 TVMlptfqpQKVWEvllsskapmvtvfmavPTIYSKLIQHYEQHFTQ---PRVQDFVRAAcKER------IRLMVSGSSA 347
Cdd:PRK13295 267 AVL------QDIWD----------------PARAAELIRTEGVTFTMastPFLTDLTRAV-KESgrpvssLRTFLCAGAP 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 348 LPQPTLLRWEEITGHTLLERYGMTEIGMA----LSNPLKgpRIPGAVGVPLPGVEVRIVMTNATsttiaegnsretqvrP 423
Cdd:PRK13295 324 IPGALVERARAALGAKIVSAWGMTENGAVtltkLDDPDE--RASTTDGCPLPGVEVRVVDADGA---------------P 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 424 GLEGKEGELMVRGDQVFTEYWNKPEATRESFteDGWFKTGDTA-VYKNGVYWIMGRTSvDIIKSGGYKISALEVERHLLA 502
Cdd:PRK13295 387 LPAGQIGRLQVRGCSNFGGYLKRPQLNGTDA--DGWFDTGDLArIDADGYIRISGRSK-DVIIRGGENIPVVEIEALLYR 463
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1367478878 503 HPDITDVAVIGARDATWGQKVTAVVQLKRGRSMTLSELKTWAREH-MAPYTIPTGLVLVEEMPRNQMGKVNK 573
Cdd:PRK13295 464 HPAIAQVAIVAYPDERLGERACAFVVPRPGQSLDFEEMVEFLKAQkVAKQYIPERLVVRDALPRTPSGKIQK 535
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
66-576 |
1.73e-60 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 208.51 E-value: 1.73e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 66 DKLAIVDDSGSHSYRdlYGSSRGLAGRIKAALDcPSGDLQGKRISFLCANDASYTVAQWASWMCGGTAVPLYREHPPSEL 145
Cdd:PRK09088 10 QRLAAVDLALGRRWT--YAELDALVGRLAAVLR-RRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASEL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 146 EYIISDSQSSLLVA-GQPYADTMEPLAhrlglpylqlppTSSLSSLLEAPENQPEPGITdwAQRPAMIIYTSGTTGRPKG 224
Cdd:PRK09088 87 DALLQDAEPRLLLGdDAVAAGRTDVED------------LAAFIASADALEPADTPSIP--PERVSLILFTSGTSGQPKG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 225 VLHTHSNIQAM-----VQGLVSEwgwsrDDVILHTLPLHHVHGIVNKLLCPLWVGATTVMLPTFQPQKV--WevlLSSKA 297
Cdd:PRK09088 153 VMLSERNLQQTahnfgVLGRVDA-----HSSFLCDAPMFHIIGLITSVRPVLAVGGSILVSNGFEPKRTlgR---LGDPA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 298 PMVTVFMAVPTIYSKLiqhyeqhftqpRVQDFVRAACKERIRLMVSGSSALPQPTLLRWEEiTGHTLLERYGMTEIGMAL 377
Cdd:PRK09088 225 LGITHYFCVPQMAQAF-----------RAQPGFDAAALRHLTALFTGGAPHAAEDILGWLD-DGIPMVDGFGMSEAGTVF 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 378 SNPLKGPRIP---GAVGVPLPGVEVRIVmtnatsttiaegNSRETQVRPGLEGkegELMVRGDQVFTEYWNKPEATRESF 454
Cdd:PRK09088 293 GMSVDCDVIRakaGAAGIPTPTVQTRVV------------DDQGNDCPAGVPG---ELLLRGPNLSPGYWRRPQATARAF 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 455 TEDGWFKTGDTAVYK-NGVYWIMGRTSvDIIKSGGYKISALEVERHLLAHPDITDVAVIGARDATWGQKVTAVVQLKRGR 533
Cdd:PRK09088 358 TGDGWFRTGDIARRDaDGFFWVVDRKK-DMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADGA 436
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1367478878 534 SMTLSELKTWAREHMAPYTIPTGLVLVEEMPRNQMGKVNKKDL 576
Cdd:PRK09088 437 PLDLERIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARL 479
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
202-578 |
3.12e-60 |
|
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: 206.03 E-value: 3.12e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 202 ITDwAQRPAMIIYTSGTTGRPKGVLHTHSNIQAMVQGLVSEWGWSRDDVILHTLPLHHVHGIVNKLLCPLWVGATTVM-- 279
Cdd:cd05972 77 VTD-AEDPALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGLRPDDIHWNIADPGWAKGAWSSFFGPWLLGATVFVye 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 280 LPTFQPQKVWEVLLSSKapmVTVFMAVPTIYSKLIQHYEQHFTqprvqdfvraacKERIRLMVSGSSALPQPTLLRWEEI 359
Cdd:cd05972 156 GPRFDAERILELLERYG---VTSFCGPPTAYRMLIKQDLSSYK------------FSHLRLVVSAGEPLNPEVIEWWRAA 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 360 TGHTLLERYGMTEIGMALSNPLKGPRIPGAVGVPLPGVEVRIVMtnatsttiAEGnsretqvRPGLEGKEGELMVRGD-- 437
Cdd:cd05972 221 TGLPIRDGYGQTETGLTVGNFPDMPVKPGSMGRPTPGYDVAIID--------DDG-------RELPPGEEGDIAIKLPpp 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 438 QVFTEYWNKPEATRESFTEDgWFKTGDTAVY-KNGVYWIMGRTSvDIIKSGGYKISALEVERHLLAHPDITDVAVIGARD 516
Cdd:cd05972 286 GLFLGYVGDPEKTEASIRGD-YYLTGDRAYRdEDGYFWFVGRAD-DIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPD 363
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1367478878 517 ATWGQKVTAVVQLKRG----RSMTLsELKTWAREHMAPYTIPTGLVLVEEMPRNQMGKVNKKDLLK 578
Cdd:cd05972 364 PVRGEVVKAFVVLTSGyepsEELAE-ELQGHVKKVLAPYKYPREIEFVEELPKTISGKIRRVELRD 428
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
76-580 |
4.01e-60 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 208.86 E-value: 4.01e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 76 SHSYRDLYGSSRGLAGRIKAaldcpSGDLQGKRISFLCANDASYTVAQWASWMCGGTAVPLYREHPPSELEYIISDSQSS 155
Cdd:PRK07786 42 TTTWRELDDRVAALAGALSR-----RGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAH 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 156 LLVAgqpyADTMEPLAH--RLGLPYLQL-------PPTSSLSSLLEAPENQPEPGITDWAQ-RPAMIIYTSGTTGRPKGV 225
Cdd:PRK07786 117 VVVT----EAALAPVATavRDIVPLLSTvvvaggsSDDSVLGYEDLLAEAGPAHAPVDIPNdSPALIMYTSGTTGRPKGA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 226 LHTHSNIQAMVQGLVSEWGWSR-DDVILHTLPLHHVHGIVNkLLCPLWVGATTVMLPT--FQPQKVWEVLLSSKApmVTV 302
Cdd:PRK07786 193 VLTHANLTGQAMTCLRTNGADInSDVGFVGVPLFHIAGIGS-MLPGLLLGAPTVIYPLgaFDPGQLLDVLEAEKV--TGI 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 303 FMaVPTIYSKLIQHYEqhfTQPRvqdfvraackeRIRLMVSGSSALPQP-TLLR--WEEITGHTLLERYGMTEIGmALSN 379
Cdd:PRK07786 270 FL-VPAQWQAVCAEQQ---ARPR-----------DLALRVLSWGAAPASdTLLRqmAATFPEAQILAAFGQTEMS-PVTC 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 380 PLKGP---RIPGAVGVPLPGVEVRIVMTNATSTTIaegnsretqvrpgleGKEGELMVRGDQVFTEYWNKPEATRESFtE 456
Cdd:PRK07786 334 MLLGEdaiRKLGSVGKVIPTVAARVVDENMNDVPV---------------GEVGEIVYRAPTLMSGYWNNPEATAEAF-A 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 457 DGWFKTGDTA-VYKNGVYWIMGRTSvDIIKSGGYKISALEVERHLLAHPDITDVAVIGARDATWGQKVTAVVQLKRG-RS 534
Cdd:PRK07786 398 GGWFHSGDLVrQDEEGYVWVVDRKK-DMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRNDdAA 476
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1367478878 535 MTLSELKTWAREHMAPYTIPTGLVLVEEMPRNQMGKVNKKDLLKHF 580
Cdd:PRK07786 477 LTLEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKVLKTELRERY 522
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
59-576 |
8.58e-60 |
|
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: 206.59 E-value: 8.58e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 59 SRAqvyRDKLAIVDDSGSH--SYRDLYGSSRGLAGRIKAaldcpSGDLQGKRISFLCANDASYTVAQWASWMCGGTAVPL 136
Cdd:cd05923 12 SRA---PDACAIADPARGLrlTYSELRARIEAVAARLHA-----RGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 137 YREHPPSELEYIISDSQSSLLVAgQPYADTMEPLAHRLG--LPYLQLPPTSSLSS---LLEAPENQPEpgitdwaqRPAM 211
Cdd:cd05923 84 NPRLKAAELAELIERGEMTAAVI-AVDAQVMDAIFQSGVrvLALSDLVGLGEPESagpLIEDPPREPE--------QPAF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 212 IIYTSGTTGRPKGVLHTHSNIQAMVQGLVSEWG--WSRDDVILHTLPLHHVHGIVNKLLCPLWVGATTVMLPTFQPQKVW 289
Cdd:cd05923 155 VFYTSGTTGLPKGAVIPQRAAESRVLFMSTQAGlrHGRHNVVLGLMPLYHVIGFFAVLVAALALDGTYVVVEEFDPADAL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 290 EVLlssKAPMVTVFMAVPTIYSKLIQHYEqhFTQPRVqdfvraackERIRLMVSGSSALPQPTLLRWEEITGHTLLERYG 369
Cdd:cd05923 235 KLI---EQERVTSLFATPTHLDALAAAAE--FAGLKL---------SSLRHVTFAGATMPDAVLERVNQHLPGEKVNIYG 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 370 MTEIGMALSNPlkGPRiPGAVGVPLPGVEVRIVMTNATSTTIAEgnsretqvrpglEGKEGELMVR--GDQVFTEYWNKP 447
Cdd:cd05923 301 TTEAMNSLYMR--DAR-TGTEMRPGFFSEVRIVRIGGSPDEALA------------NGEEGELIVAaaADAAFTGYLNQP 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 448 EATRESFtEDGWFKTGDTA-VYKNGVYWIMGRTSvDIIKSGGYKISALEVERHLLAHPDITDVAVIGARDATWGQKVTAV 526
Cdd:cd05923 366 EATAKKL-QDGWYRTGDVGyVDPSGDVRILGRVD-DMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTAC 443
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1367478878 527 VQLKRGRsMTLSELKTWARE-HMAPYTIPTGLVLVEEMPRNQMGKVNKKDL 576
Cdd:cd05923 444 VVPREGT-LSADELDQFCRAsELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
76-576 |
8.96e-60 |
|
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: 204.50 E-value: 8.96e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 76 SHSYRDLYGSSRGLAGRIKAAldcpsGDLQGKRISFLCANDASYTVAQWASWMCGGTAVPLYREHPPSELEYIISDSQSS 155
Cdd:cd05912 1 SYTFAELFEEVSRLAEHLAAL-----GVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 156 LlvagqpyadtmeplahrlglpylqlpptsslsslleapenqpepgitdwaQRPAMIIYTSGTTGRPKGVLHTHSNIQAM 235
Cdd:cd05912 76 L--------------------------------------------------DDIATIMYTSGTTGKPKGVQQTFGNHWWS 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 236 VQGLVSEWGWSRDDVILHTLPLHHVHGIvNKLLCPLWVGATTVMLPTFQPQKVWEVLLSSKAPMVTVfmaVPTIYSKLIQ 315
Cdd:cd05912 106 AIGSALNLGLTEDDNWLCALPLFHISGL-SILMRSVIYGMTVYLVDKFDAEQVLHLINSGKVTIISV---VPTMLQRLLE 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 316 HYEQHftqprvqdfvraaCKERIRLMVSGSSALPQPTLLRWEEiTGHTLLERYGMTEIG--MALSNPLKGPRIPGAVGVP 393
Cdd:cd05912 182 ILGEG-------------YPNNLRCILLGGGPAPKPLLEQCKE-KGIPVYQSYGMTETCsqIVTLSPEDALNKIGSAGKP 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 394 LPGVEVRIVMTNatsttiaegnsretqvrpGLEGKEGELMVRGDQVFTEYWNKPEATRESFtEDGWFKTGDTAVYKN-GV 472
Cdd:cd05912 248 LFPVELKIEDDG------------------QPPYEVGEILLKGPNVTKGYLNRPDATEESF-ENGWFKTGDIGYLDEeGF 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 473 YWIMGRTSvDIIKSGGYKISALEVERHLLAHPDITDVAVIGARDATWGQKVTAVVQLKrgRSMTLSELKTWAREHMAPYT 552
Cdd:cd05912 309 LYVLDRRS-DLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSE--RPISEEELIAYCSEKLAKYK 385
|
490 500
....*....|....*....|....
gi 1367478878 553 IPTGLVLVEEMPRNQMGKVNKKDL 576
Cdd:cd05912 386 VPKKIYFVDELPRTASGKLLRHEL 409
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
77-576 |
1.79e-59 |
|
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: 206.33 E-value: 1.79e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 77 HSYRDLYGSSRGLAGRIKAAldcpsGDLQGKRISFLCANDASYTVAQWASWMCGGTAVPLYREHPPSELEYIISDSQSSL 156
Cdd:cd12119 26 YTYAEVAERARRLANALRRL-----GVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAEDRV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 157 LVAGQPYADTMEPLAHRL-------------GLPYLQLPPTSSLSSLLEApenqpEPGITDWAQ----RPAMIIYTSGTT 219
Cdd:cd12119 101 VFVDRDFLPLLEAIAPRLptvehvvvmtddaAMPEPAGVGVLAYEELLAA-----ESPEYDWPDfdenTAAAICYTSGTT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 220 GRPKGVLHTHSNI--QAMVQGLVSEWGWSRDDVILHTLPLHHVHGIVNKLLCPlWVGATTVML-PTFQPQKVWEVLlssK 296
Cdd:cd12119 176 GNPKGVVYSHRSLvlHAMAALLTDGLGLSESDVVLPVVPMFHVNAWGLPYAAA-MVGAKLVLPgPYLDPASLAELI---E 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 297 APMVTVFMAVPTIYSKLIQHYEQHftqPRVQDFVRAackerirlMVSGSSALPqPTLLRWEEITGHTLLERYGMTE---I 373
Cdd:cd12119 252 REGVTFAAGVPTVWQGLLDHLEAN---GRDLSSLRR--------VVIGGSAVP-RSLIEAFEERGVRVIHAWGMTEtspL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 374 GMALSNPLKGPRIPGAV--------GVPLPGVEVRIVmtnatsttiaegnSRETQVRPGlEGKE-GELMVRGDQVFTEYW 444
Cdd:cd12119 320 GTVARPPSEHSNLSEDEqlalrakqGRPVPGVELRIV-------------DDDGRELPW-DGKAvGELQVRGPWVTKSYY 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 445 NKPEATrESFTEDGWFKTGDTA-VYKNGVYWIMGRTSvDIIKSGGYKISALEVERHLLAHPDITDVAVIGARDATWGQKV 523
Cdd:cd12119 386 KNDEES-EALTEDGWLRTGDVAtIDEDGYLTITDRSK-DVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERP 463
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1367478878 524 TAVVQLKRGRSMTLSELKTWAREHMAPYTIPTGLVLVEEMPRNQMGKVNKKDL 576
Cdd:cd12119 464 LAVVVLKEGATVTAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
156-579 |
1.08e-58 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 206.73 E-value: 1.08e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 156 LLVAGQPYADTMEPLAHRLGLPYLQLPPTSSLSSLLEAPENQPEPGITDWAQRPAMIIYTSGTTGRPKGVLHTHSNIQAM 235
Cdd:PRK07529 162 VEVDLARYLPGPKRLAVPLIRRKAHARILDFDAELARQPGDRLFSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVAN 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 236 VQGLVSEWGWSRDDVILHTLPLHHVHGIVNKLLCPLWVGATtVMLPTfqPQ---------KVWEVLLSSKapmVTVFMAV 306
Cdd:PRK07529 242 AWLGALLLGLGPGDTVFCGLPLFHVNALLVTGLAPLARGAH-VVLAT--PQgyrgpgviaNFWKIVERYR---INFLSGV 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 307 PTIYSKLIQhyeqhftQPrvqdfVRAACKERIRLMVSGSSALPQPTLLRWEEITGHTLLERYGMTEiGMALS--NPLKGP 384
Cdd:PRK07529 316 PTVYAALLQ-------VP-----VDGHDISSLRYALCGAAPLPVEVFRRFEAATGVRIVEGYGLTE-ATCVSsvNPPDGE 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 385 RIPGAVGVPLPGVEVRIVMTNAtsttiAEGNSRETQVrpgleGKEGELMVRGDQVFTEYWNkPEATRESFTEDGWFKTGD 464
Cdd:PRK07529 383 RRIGSVGLRLPYQRVRVVILDD-----AGRYLRDCAV-----DEVGVLCIAGPNVFSGYLE-AAHNKGLWLEDGWLNTGD 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 465 TA-VYKNGVYWIMGRTSvDIIKSGGYKISALEVERHLLAHPDITDVAVIGARDATWGQKVTAVVQLKRGRSMTLSELKTW 543
Cdd:PRK07529 452 LGrIDADGYFWLTGRAK-DLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGELPVAYVQLKPGASATEAELLAF 530
|
410 420 430
....*....|....*....|....*....|....*..
gi 1367478878 544 AREHMA-PYTIPTGLVLVEEMPRNQMGKVNKKDLLKH 579
Cdd:PRK07529 531 ARDHIAeRAAVPKHVRILDALPKTAVGKIFKPALRRD 567
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
95-578 |
3.11e-58 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 204.12 E-value: 3.11e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 95 AALDCPSGDLQGKRISFLCANDASYTVAQWASWMCGGTAVP---LYREHppsELEYIISDSQSSLLVAGQPYADTMEPLA 171
Cdd:PRK06178 72 AALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPvspLFREH---ELSYELNDAGAEVLLALDQLAPVVEQVR 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 172 HRLGLPYL-------QLP--PTSSLSSLLEAPENQPePGITDW--AQR---------------PAMIIYTSGTTGRPKGV 225
Cdd:PRK06178 149 AETSLRHVivtsladVLPaePTLPLPDSLRAPRLAA-AGAIDLlpALRactapvplpppaldaLAALNYTGGTTGMPKGC 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 226 LHTHSNI--QAMVQGLVSEWGwSRDDVILHTLPLHHVHGIVNKLLCPLWVGATTVMLPTFQPQKVWEVLLSSKapmVTV- 302
Cdd:PRK06178 228 EHTQRDMvyTAAAAYAVAVVG-GEDSVFLSFLPEFWIAGENFGLLFPLFSGATLVLLARWDAVAFMAAVERYR---VTRt 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 303 FMAVPTiYSKLIQHYEQH------FTQPRVQDFVRAACKERIRlmvsgssalpqptllRWEEITGHTLLE-RYGMTE--- 372
Cdd:PRK06178 304 VMLVDN-AVELMDHPRFAeydlssLRQVRVVSFVKKLNPDYRQ---------------RWRALTGSVLAEaAWGMTEtht 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 373 -----IGMALSN-PLKGPriPGAVGVPLPGVEVRIVmtnatsttiaegnSRET-QVRPglEGKEGELMVRGDQVFTEYWN 445
Cdd:PRK06178 368 cdtftAGFQDDDfDLLSQ--PVFVGLPVPGTEFKIC-------------DFETgELLP--LGAEGEIVVRTPSLLKGYWN 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 446 KPEATRESFtEDGWFKTGDTAVY-KNGVYWIMGRTSvDIIKSGGYKISALEVERHLLAHPDITDVAVIGARDATWGQKVT 524
Cdd:PRK06178 431 KPEATAEAL-RDGWLHTGDIGKIdEQGFLHYLGRRK-EMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPV 508
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1367478878 525 AVVQLKRGRSMTLSELKTWAREHMAPYTIPTgLVLVEEMPRNQMGKVNKKDLLK 578
Cdd:PRK06178 509 AFVQLKPGADLTAAALQAWCRENMAVYKVPE-IRIVDALPMTATGKVRKQDLQA 561
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
209-573 |
4.52e-58 |
|
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: 197.49 E-value: 4.52e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 209 PAMIIYTSGTTGRPKGVLHTHSNIQAMVQGLVSEWGWSRDDVILHTLPLHHVHGIvNKLLCPLWVGATTVMLPTFQPQKV 288
Cdd:cd17637 2 PFVIIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPLFHIAGL-NLALATFHAGGANVVMEKFDPAEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 289 WEVLLSSKapmVTVFMAVPTIYSKLIQHYEQHFTQPRvqdfvraackeRIRLmVSGSSAlPQpTLLRWEEITGHTLLERY 368
Cdd:cd17637 81 LELIEEEK---VTLMGSFPPILSNLLDAAEKSGVDLS-----------SLRH-VLGLDA-PE-TIQRFEETTGATFWSLY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 369 GMTEIGMALSNPLKGPRiPGAVGVPLPGVEVRIVmtnatsttiaegNSRETQVRPGlegKEGELMVRGDQVFTEYWNKPE 448
Cdd:cd17637 144 GQTETSGLVTLSPYRER-PGSAGRPGPLVRVRIV------------DDNDRPVPAG---ETGEIVVRGPLVFQGYWNLPE 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 449 ATRESFtEDGWFKTGDTAVY-KNGVYWIMGRTSV-DIIKSGGYKISALEVERHLLAHPDITDVAVIGARDATWGQKVTAV 526
Cdd:cd17637 208 LTAYTF-RNGWHHTGDLGRFdEDGYLWYAGRKPEkELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAV 286
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1367478878 527 VQLKRGRSMTLSELKTWAREHMAPYTIPTGLVLVEEMPRNQMGKVNK 573
Cdd:cd17637 287 CVLKPGATLTADELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
105-578 |
1.03e-57 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 202.96 E-value: 1.03e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 105 QGKRISFLCANDASYTVAQWASWMCGGTAV---PLYREHppsELEYIISDSQSSLL---------VAGQPYADTME---- 168
Cdd:PRK06710 73 KGDRVAIMLPNCPQAVIGYYGTLLAGGIVVqtnPLYTER---ELEYQLHDSGAKVIlcldlvfprVTNVQSATKIEhviv 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 169 -------PLAHRLGLPYLQLPPT--------SSLSSLLEAPENQPEPGI---TDWAQRPAMIIYTSGTTGRPKGVLHTHS 230
Cdd:PRK06710 150 triadflPFPKNLLYPFVQKKQSnlvvkvseSETIHLWNSVEKEVNTGVevpCDPENDLALLQYTGGTTGFPKGVMLTHK 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 231 N-IQAMVQGLvsEWGWS---RDDVILHTLPLHHVHGIVNKLLCPLWVGATTVMLPTFQPQKVWEVLLSSKapmVTVFMAV 306
Cdd:PRK06710 230 NlVSNTLMGV--QWLYNckeGEEVVLGVLPFFHVYGMTAVMNLSIMQGYKMVLIPKFDMKMVFEAIKKHK---VTLFPGA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 307 PTIYSKLIQhyeqhftQPRVQDFVRAAckerIRLMVSGSSALPQPTLLRWEEITGHTLLERYGMTEIG-MALSNPLKGPR 385
Cdd:PRK06710 305 PTIYIALLN-------SPLLKEYDISS----IRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTESSpVTHSNFLWEKR 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 386 IPGAVGVPLPGVEVRIVmtnatsttiaegnSRET--QVRPGlegKEGELMVRGDQVFTEYWNKPEATrESFTEDGWFKTG 463
Cdd:PRK06710 374 VPGSIGVPWPDTEAMIM-------------SLETgeALPPG---EIGEIVVKGPQIMKGYWNKPEET-AAVLQDGWLHTG 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 464 DTAVY-KNGVYWIMGRTSvDIIKSGGYKISALEVERHLLAHPDITDVAVIGARDATWGQKVTAVVQLKRGRSMTLSELKT 542
Cdd:PRK06710 437 DVGYMdEDGFFYVKDRKK-DMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVLKEGTECSEEELNQ 515
|
490 500 510
....*....|....*....|....*....|....*.
gi 1367478878 543 WAREHMAPYTIPTGLVLVEEMPRNQMGKVNKKDLLK 578
Cdd:PRK06710 516 FARKYLAAYKVPKVYEFRDELPKTTVGKILRRVLIE 551
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
78-576 |
3.17e-57 |
|
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: 198.47 E-value: 3.17e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 78 SYRDLygssRGLAGRIKAALDCPSGDLQGKRISFLCANDASYTVAQWASWMCGGTAVPLYREHPPSELEYIISDSQSSLL 157
Cdd:cd05958 12 TYRDL----LALANRIANVLVGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDKARITVA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 158 VagqpyadtmepLAHRLglpylqlppTSSlsslleapenqpePGITDWAqrpamiiYTSGTTGRPKGVLHTHSNIQAMVQ 237
Cdd:cd05958 88 L-----------CAHAL---------TAS-------------DDICILA-------FTSGTTGAPKATMHFHRDPLASAD 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 238 GL-VSEWGWSRDDVILHTLPLHHVHGIVNKLLCPLWVGATTVMLPTFQPQKVWEVLLSSKapmVTVFMAVPTIYSKLIQH 316
Cdd:cd05958 128 RYaVNVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEEATPDLLLSAIARYK---PTVLFTAPTAYRAMLAH 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 317 YEqhFTQPRVQDfvraackerIRLMVSGSSALPQPTLLRWEEITGHTLLERYGMTE-IGMALSNPLKGPRiPGAVGVPLP 395
Cdd:cd05958 205 PD--AAGPDLSS---------LRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEmFHIFISARPGDAR-PGATGKPVP 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 396 GVEVRIVMtnatsttiAEGNsretqvrPGLEGKEGELMVRGDqvfTEYWNKPEATRESFTEDGWFKTGDTAVYK-NGVYW 474
Cdd:cd05958 273 GYEAKVVD--------DEGN-------PVPDGTIGRLAVRGP---TGCRYLADKRQRTYVQGGWNITGDTYSRDpDGYFR 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 475 IMGRtSVDIIKSGGYKISALEVERHLLAHPDITDVAVIGARDATWGQKVTAVVQLKRGRS---MTLSELKTWAREHMAPY 551
Cdd:cd05958 335 HQGR-SDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIpgpVLARELQDHAKAHIAPY 413
|
490 500
....*....|....*....|....*
gi 1367478878 552 TIPTGLVLVEEMPRNQMGKVNKKDL 576
Cdd:cd05958 414 KYPRAIEFVTELPRTATGKLQRFAL 438
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
212-576 |
1.20e-55 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 191.34 E-value: 1.20e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 212 IIYTSGTTGRPKGVLHTHSNI--------QAMvqglvsewGWSRDDVILHTLPLHHVHGIVNKLLCPLWVGATTVML-PT 282
Cdd:cd05917 7 IQFTSGTTGSPKGATLTHHNIvnngyfigERL--------GLTEQDRLCIPVPLFHCFGSVLGVLACLTHGATMVFPsPS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 283 FQPQKVWEVLLSSKApmvTVFMAVPTIYSKLIQHYEqhFTQprvQDFvraackERIRLMVSGSSALPQPTLLRWEEITGH 362
Cdd:cd05917 79 FDPLAVLEAIEKEKC---TALHGVPTMFIAELEHPD--FDK---FDL------SSLRTGIMAGAPCPPELMKRVIEVMNM 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 363 T-LLERYGMTE----IGMALSNPLKGPRIpGAVGVPLPGVEVRIVmtnatsttiaegnSRETQVRPGLeGKEGELMVRGD 437
Cdd:cd05917 145 KdVTIAYGMTEtspvSTQTRTDDSIEKRV-NTVGRIMPHTEAKIV-------------DPEGGIVPPV-GVPGELCIRGY 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 438 QVFTEYWNKPEATRESFTEDGWFKTGDTAVY-KNGVYWIMGRTSvDIIKSGGYKISALEVERHLLAHPDITDVAVIGARD 516
Cdd:cd05917 210 SVMKGYWNDPEKTAEAIDGDGWLHTGDLAVMdEDGYCRIVGRIK-DMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPD 288
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 517 ATWGQKVTAVVQLKRGRSMTLSELKTWAREHMAPYTIPTGLVLVEEMPRNQMGKVNKKDL 576
Cdd:cd05917 289 ERYGEEVCAWIRLKEGAELTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKL 348
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
130-576 |
1.82e-55 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 195.67 E-value: 1.82e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 130 GGTAVPLYREHPPSELEYIISDSQSSLLVAGQPY--------ADTMEPLAHRLgLPYLQLPPTSSLSSLLEAPENQP--- 198
Cdd:PRK08008 86 GAIMVPINARLLREESAWILQNSQASLLVTSAQFypmyrqiqQEDATPLRHIC-LTRVALPADDGVSSFTQLKAQQPatl 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 199 --EPGITdwAQRPAMIIYTSGTTGRPKGVLHTHSNIQamVQGLVSEW--GWSRDDVILHTLPLHHVHGIVNKLLCPLWVG 274
Cdd:PRK08008 165 cyAPPLS--TDDTAEILFTSGTTSRPKGVVITHYNLR--FAGYYSAWqcALRDDDVYLTVMPAFHIDCQCTAAMAAFSAG 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 275 ATTVMLPTFQPQKVWEVLLSSKApmvTVFMAVPTIYSKLIqhyeqhfTQPrVQDFVRAACKERIRLMVSGSSALPQPtll 354
Cdd:PRK08008 241 ATFVLLEKYSARAFWGQVCKYRA---TITECIPMMIRTLM-------VQP-PSANDRQHCLREVMFYLNLSDQEKDA--- 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 355 rWEEITGHTLLERYGMTE-IGMALSNPLKGPRIPGAVGVPLPGVEVRIvmtnatsttiaegnsRETQVRPGLEGKEGELM 433
Cdd:PRK08008 307 -FEERFGVRLLTSYGMTEtIVGIIGDRPGDKRRWPSIGRPGFCYEAEI---------------RDDHNRPLPAGEIGEIC 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 434 VR---GDQVFTEYWNKPEATRESFTEDGWFKTGDTA-VYKNGVYWIMGRtSVDIIKSGGYKISALEVERHLLAHPDITDV 509
Cdd:PRK08008 371 IKgvpGKTIFKEYYLDPKATAKVLEADGWLHTGDTGyVDEEGFFYFVDR-RCNMIKRGGENVSCVELENIIATHPKIQDI 449
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1367478878 510 AVIGARDATWGQKVTAVVQLKRGRSMTLSELKTWAREHMAPYTIPTGLVLVEEMPRNQMGKVNKKDL 576
Cdd:PRK08008 450 VVVGIKDSIRDEAIKAFVVLNEGETLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNL 516
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
208-576 |
3.18e-55 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 190.77 E-value: 3.18e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 208 RPAMIIYTSGTTGRPKGVLHTHSNIQAMVQGLVSEWGWSRDDVILHTLPLHHVHGIVNKLLCPLWVGATtVMLPTFQP-- 285
Cdd:cd05944 3 DVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAH-VVLAGPAGyr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 286 -----QKVWEVLLSSKapmVTVFMAVPTIYSKLIQhyeqhftQPRVQDFvraackERIRLMVSGSSALPQPTLLRWEEIT 360
Cdd:cd05944 82 npglfDNFWKLVERYR---ITSLSTVPTVYAALLQ-------VPVNADI------SSLRFAMSGAAPLPVELRARFEDAT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 361 GHTLLERYGMTEIGMALS-NPLKGPRIPGAVGVPLPGVEVRIVMTNATSTTIaegnsretqvRPGLEGKEGELMVRGDQV 439
Cdd:cd05944 146 GLPVVEGYGLTEATCLVAvNPPDGPKRPGSVGLRLPYARVRIKVLDGVGRLL----------RDCAPDEVGEICVAGPGV 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 440 FTEYWNKpEATRESFTEDGWFKTGDTA-VYKNGVYWIMGRtSVDIIKSGGYKISALEVERHLLAHPDITDVAVIGARDAT 518
Cdd:cd05944 216 FGGYLYT-EGNKNAFVADGWLNTGDLGrLDADGYLFITGR-AKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAH 293
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1367478878 519 WGQKVTAVVQLKRGRSMTLSELKTWAREHMAPY-TIPTGLVLVEEMPRNQMGKVNKKDL 576
Cdd:cd05944 294 AGELPVAYVQLKPGAVVEEEELLAWARDHVPERaAVPKHIEVLEELPVTAVGKVFKPAL 352
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
60-576 |
1.04e-54 |
|
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.
Pssm-ID: 341244 [Multi-domain] Cd Length: 482 Bit Score: 192.54 E-value: 1.04e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 60 RAQVYRDKLAIVDDSGSHSYRDLYGSSRGLAGRIKAAldcpsGDLQGKRISFLCANDASYTVAQWASWMCGGT---AVPL 136
Cdd:cd05920 24 SAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGL-----GIRPGDRVVVQLPNVAEFVVLFFALLRLGAVpvlALPS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 137 YREHppsELEYIISDSQSSLLVAgqpyADTMEPLAHRlglpylqlpptsslSSLLEAPENQPEPgitdwaqrpAMIIYTS 216
Cdd:cd05920 99 HRRS---ELSAFCAHAEAVAYIV----PDRHAGFDHR--------------ALARELAESIPEV---------ALFLLSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 217 GTTGRPKGVLHTHSNIQAMVQGLVSEWGWSRDDVILHTLPLHHvhgivN-KLLCP-----LWVGATTVMLPTFQPQKVWE 290
Cdd:cd05920 149 GTTGTPKLIPRTHNDYAYNVRASAEVCGLDQDTVYLAVLPAAH-----NfPLACPgvlgtLLAGGRVVLAPDPSPDAAFP 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 291 VLLSSKapmVTVFMAVPTiyskLIQHYEQHFTQPRVQDfvraackERIRLMVSGSSALPQPTLLRWEEITGHTLLERYGM 370
Cdd:cd05920 224 LIEREG---VTVTALVPA----LVSLWLDAAASRRADL-------SSLRLLQVGGARLSPALARRVPPVLGCTLQQVFGM 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 371 TEiGM----ALSNPlkGPRIPGAVGVPL-PGVEVRIVmtnatsttiaegnsrETQVRPGLEGKEGELMVRGDQVFTEYWN 445
Cdd:cd05920 290 AE-GLlnytRLDDP--DEVIIHTQGRPMsPDDEIRVV---------------DEEGNPVPPGEEGELLTRGPYTIRGYYR 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 446 KPEATRESFTEDGWFKTGDTA-VYKNGVYWIMGRTSvDIIKSGGYKISALEVERHLLAHPDITDVAVIGARDATWGQKVT 524
Cdd:cd05920 352 APEHNARAFTPDGFYRTGDLVrRTPDGYLVVEGRIK-DQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSC 430
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1367478878 525 AVVQLkRGRSMTLSELKTWAREH-MAPYTIPTGLVLVEEMPRNQMGKVNKKDL 576
Cdd:cd05920 431 AFVVL-RDPPPSAAQLRRFLRERgLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
67-576 |
2.00e-54 |
|
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: 190.75 E-value: 2.00e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 67 KLAIVDDSGSHSYRDLYGSSRGLAGRIKAaLDCPSGDlqgkRISFLCANDASYTVAQWASWMCGGTAVPLYREHPPSELE 146
Cdd:cd05919 1 KTAFYAADRSVTYGQLHDGANRLGSALRN-LGVSSGD----RVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 147 YIISDSQSSLLVAgqpyadtmeplaHRLGLPYLQlpptsslsslleapenqpepgitdwaqrpamiiYTSGTTGRPKGVL 226
Cdd:cd05919 76 YIARDCEARLVVT------------SADDIAYLL---------------------------------YSSGTTGPPKGVM 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 227 HTHSNIQAMVQGLVSEW-GWSRDDVILHTLPLHHVHGIVNKLLCPLWVGATTVMLPTF-QPQKVWEvLLSSKAPmvTVFM 304
Cdd:cd05919 111 HAHRDPLLFADAMAREAlGLTPGDRVFSSAKMFFGYGLGNSLWFPLAVGASAVLNPGWpTAERVLA-TLARFRP--TVLY 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 305 AVPTIYSKLIqhyeqhftqpRVQDFVRAACKErIRLMVSGSSALPQPTLLRWEEITGHTLLERYGMTEIG-MALSNPLKG 383
Cdd:cd05919 188 GVPTFYANLL----------DSCAGSPDALRS-LRLCVSAGEALPRGLGERWMEHFGGPILDGIGATEVGhIFLSNRPGA 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 384 PRiPGAVGVPLPGVEVRIVMTnatsttiaEGNSREtqvrpglEGKEGELMVRGDQVFTEYWNKPEATRESFtEDGWFKTG 463
Cdd:cd05919 257 WR-LGSTGRPVPGYEIRLVDE--------EGHTIP-------PGEEGDLLVRGPSAAVGYWNNPEKSRATF-NGGWYRTG 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 464 DT-AVYKNGVYWIMGRtSVDIIKSGGYKISALEVERHLLAHPDITDVAVIGARDATWGQKVTAVVQLKRGR--SMTLSE- 539
Cdd:cd05919 320 DKfCRDADGWYTHAGR-ADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAapQESLARd 398
|
490 500 510
....*....|....*....|....*....|....*..
gi 1367478878 540 LKTWAREHMAPYTIPTGLVLVEEMPRNQMGKVNKKDL 576
Cdd:cd05919 399 IHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKL 435
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
78-511 |
8.90e-54 |
|
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: 188.24 E-value: 8.90e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 78 SYRDLYGSSRGLAGRIKAALDCPSGDlqgkRISFLCANDASYTVAQWASWMCGGTAVPLYREHPPSELEYIISDSQSSLL 157
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAGGVGPGD----RVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 158 VAGQPYADTMeplahrLGLPYLQLPPTSSLSSLLEAPENQPEPGITDWAQRPAMIIYTSGTTGRPKGVLHTHSNIQAMVQ 237
Cdd:TIGR01733 77 LTDSALASRL------AGLVLPVILLDPLELAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 238 GLVSEWGWSRDDVILHTLPLHHvHGIVNKLLCPLWVGATTVMLP---TFQPQKVWEVLLSSKapMVTVFMAVPTIYSKLI 314
Cdd:TIGR01733 151 WLARRYGLDPDDRVLQFASLSF-DASVEEIFGALLAGATLVVPPedeERDDAALLAALIAEH--PVTVLNLTPSLLALLA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 315 QHyeqhftqprvqdfvRAACKERIRLMVSGSSALPQPTLLRWEEITGHT-LLERYGMTEI-GMALSNPLKGPRIPGAV-- 390
Cdd:TIGR01733 228 AA--------------LPPALASLRLVILGGEALTPALVDRWRARGPGArLINLYGPTETtVWSTATLVDPDDAPRESpv 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 391 --GVPLPGVEVRIVmtnatsttiaegNSRETQVRPGLegkEGELMVRGDQVFTEYWNKPEATRESFTEDG--------WF 460
Cdd:TIGR01733 294 piGRPLANTRLYVL------------DDDLRPVPVGV---VGELYIGGPGVARGYLNRPELTAERFVPDPfaggdgarLY 358
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1367478878 461 KTGDTAVY-KNGVYWIMGRTSvDIIKSGGYKISALEVERHLLAHPDITDVAV 511
Cdd:TIGR01733 359 RTGDLVRYlPDGNLEFLGRID-DQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
77-578 |
1.29e-52 |
|
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.
Pssm-ID: 341273 [Multi-domain] Cd Length: 442 Bit Score: 186.17 E-value: 1.29e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 77 HSYRDLYGSSRGLAGRIKAaldcpSGDLQGKRISFLCANDASYTVAQWASWMCGGTAVPLYREHPPSELEYIISDSQSSL 156
Cdd:cd05969 1 YTFAQLKVLSARFANVLKS-----LGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 157 LVAGQPYADTMEPlahrlglpylqlpptsslsslleapenqpepgitdwaQRPAMIIYTSGTTGRPKGVLHTHSniqAMV 236
Cdd:cd05969 76 LITTEELYERTDP-------------------------------------EDPTLLHYTSGTTGTPKGVLHVHD---AMI 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 237 QGLVS-EW--GWSRDDVILHTLPLHHVHGIVNKLLCPLWVGATTVMLP-TFQPQKVWEVLLSSKapmVTVFMAVPTIYSK 312
Cdd:cd05969 116 FYYFTgKYvlDLHPDDIYWCTADPGWVTGTVYGIWAPWLNGVTNVVYEgRFDAESWYGIIERVK---VTVWYTAPTAIRM 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 313 LIQHYEQhftqprvqdFVRAACKERIRLMVSGSSALpQPTLLRW-EEITGHTLLERYGMTEIG-MALSNPLKGPRIPGAV 390
Cdd:cd05969 193 LMKEGDE---------LARKYDLSSLRFIHSVGEPL-NPEAIRWgMEVFGVPIHDTWWQTETGsIMIANYPCMPIKPGSM 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 391 GVPLPGVEVRIVMTNatsttiaeGNSretqVRPGlegKEGELMVRGD--QVFTEYWNKPEATRESFTeDGWFKTGDTAvY 468
Cdd:cd05969 263 GKPLPGVKAAVVDEN--------GNE----LPPG---TKGILALKPGwpSMFRGIWNDEERYKNSFI-DGWYLTGDLA-Y 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 469 KN--GVYWIMGRTSvDIIKSGGYKISALEVERHLLAHPDITDVAVIGARDATWGQKVTAVVQLKRGRSMT---LSELKTW 543
Cdd:cd05969 326 RDedGYFWFVGRAD-DIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPSdelKEEIINF 404
|
490 500 510
....*....|....*....|....*....|....*
gi 1367478878 544 AREHMAPYTIPTGLVLVEEMPRNQMGKVNKKdLLK 578
Cdd:cd05969 405 VRQKLGAHVAPREIEFVDNLPKTRSGKIMRR-VLK 438
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
61-576 |
1.84e-51 |
|
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: 182.83 E-value: 1.84e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 61 AQVYRDKLAIVDDSGSHSYRDLYGSSRGLAGRIKAAldcpsGDLQGKRISFLCANDASYTVAQWASWMCGGTAVPLYREH 140
Cdd:cd05945 1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASL-----GLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 141 PPSELEYIISDSQSSLLVAGQpyadtmeplahrlglpylqlpptsslsslleapenqpepgiTDwaqrPAMIIYTSGTTG 220
Cdd:cd05945 76 PAERIREILDAAKPALLIADG-----------------------------------------DD----NAYIIFTSGSTG 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 221 RPKGVLHTHSNIQAMVQGLVSEWGWSRDDVILHTLPLH---HVHGIvnklLCPLWVGATTVMLPTfqpqkvwEVLLSSKA 297
Cdd:cd05945 111 RPKGVQISHDNLVSFTNWMLSDFPLGPGDVFLNQAPFSfdlSVMDL----YPALASGATLVPVPR-------DATADPKQ 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 298 PM-------VTVFMAVPTIYSKLIQHyeQHFTQPRVqdfvraackERIRLMVSGSSALPQPTLLRWEEIT-GHTLLERYG 369
Cdd:cd05945 180 LFrflaehgITVWVSTPSFAAMCLLS--PTFTPESL---------PSLRHFLFCGEVLPHKTARALQQRFpDARIYNTYG 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 370 MTEIGMALS------NPLKG-PRIPgaVGVPLPGVEVRIVmtnatsttiaegnsrETQVRPGLEGKEGELMVRGDQVFTE 442
Cdd:cd05945 249 PTEATVAVTyievtpEVLDGyDRLP--IGYAKPGAKLVIL---------------DEDGRPVPPGEKGELVISGPSVSKG 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 443 YWNKPEATRESFTED---GWFKTGDTAVYKN-GVYWIMGRTSvDIIKSGGYKISALEVERHLLAHPDITDVAVIGARDAT 518
Cdd:cd05945 312 YLNNPEKTAAAFFPDegqRAYRTGDLVRLEAdGLLFYRGRLD-FQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGE 390
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1367478878 519 WGQKVTAVVQLKRGRSMTL-SELKTWAREHMAPYTIPTGLVLVEEMPRNQMGKVNKKDL 576
Cdd:cd05945 391 KVTELIAFVVPKPGAEAGLtKAIKAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
64-576 |
2.12e-51 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 185.26 E-value: 2.12e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 64 YRDKLAIVDDSGSHSYRDLYGSSRGLAGRIKAALDCPSGDlqgkRISFLCANDASYTVAQWASWMCGGTAV---PLYreh 140
Cdd:PRK08974 36 YADQPAFINMGEVMTFRKLEERSRAFAAYLQNGLGLKKGD----RVALMMPNLLQYPIALFGILRAGMIVVnvnPLY--- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 141 PPSELEYIISDSQSSLLVAGQPYADTME------PLAH----RLG---------------------LPYLQLPPTSSLSS 189
Cdd:PRK08974 109 TPRELEHQLNDSGAKAIVIVSNFAHTLEkvvfktPVKHviltRMGdqlstakgtlvnfvvkyikrlVPKYHLPDAISFRS 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 190 LLEAPENQ----PEPGITDWAqrpaMIIYTSGTTGRPKGVLHTHSNIQAMVqgLVSEWGWS-----RDDVILHTLPLHHV 260
Cdd:PRK08974 189 ALHKGRRMqyvkPELVPEDLA----FLQYTGGTTGVAKGAMLTHRNMLANL--EQAKAAYGpllhpGKELVVTALPLYHI 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 261 HGI-VNKLLCpLWVGATTVML--PTFQPQKVWEVllsSKAPmVTVFMAVPTIYSKLIQHYEqhFTQprvQDFvraackER 337
Cdd:PRK08974 263 FALtVNCLLF-IELGGQNLLItnPRDIPGFVKEL---KKYP-FTAITGVNTLFNALLNNEE--FQE---LDF------SS 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 338 IRLMVSGSSALPQPTLLRWEEITGHTLLERYGMTEIGMALS-NPLKGPRIPGAVGVPLPGVEVRIVMTnatsttiaEGNS 416
Cdd:PRK08974 327 LKLSVGGGMAVQQAVAERWVKLTGQYLLEGYGLTECSPLVSvNPYDLDYYSGSIGLPVPSTEIKLVDD--------DGNE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 417 REtqvrpglEGKEGELMVRGDQVFTEYWNKPEATRESFtEDGWFKTGDTAVY-KNGVYWIMGRTSvDIIKSGGYKISALE 495
Cdd:PRK08974 399 VP-------PGEPGELWVKGPQVMLGYWQRPEATDEVI-KDGWLATGDIAVMdEEGFLRIVDRKK-DMILVSGFNVYPNE 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 496 VERHLLAHPDITDVAVIGARDATWGQKVTAVVqLKRGRSMTLSELKTWAREHMAPYTIPTGLVLVEEMPRNQMGKVNKKD 575
Cdd:PRK08974 470 IEDVVMLHPKVLEVAAVGVPSEVSGEAVKIFV-VKKDPSLTEEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRRE 548
|
.
gi 1367478878 576 L 576
Cdd:PRK08974 549 L 549
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
212-573 |
5.27e-51 |
|
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: 178.46 E-value: 5.27e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 212 IIYTSGTTGRPKGVLHTHSniQAMvqGLVSEWG----WSRDDVILHTLPLHHVHGIVNKLLCPLWVGATTVMLPTFQPQK 287
Cdd:cd17638 5 IMFTSGTTGRSKGVMCAHR--QTL--RAAAAWAdcadLTEDDRYLIINPFFHTFGYKAGIVACLLTGATVVPVAVFDVDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 288 VWEVLLSSKapmVTVFMAVPTIYSKLIQHyeqhftqPRVQDFVRAAckerIRLMVSGSSALPqPTLLR--WEEITGHTLL 365
Cdd:cd17638 81 ILEAIERER---ITVLPGPPTLFQSLLDH-------PGRKKFDLSS----LRAAVTGAATVP-VELVRrmRSELGFETVL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 366 ERYGMTEIGMA-LSNPLKGPR-IPGAVGVPLPGVEVRIvmtnatsttiaegnsretqvrpgleGKEGELMVRGDQVFTEY 443
Cdd:cd17638 146 TAYGLTEAGVAtMCRPGDDAEtVATTCGRACPGFEVRI-------------------------ADDGEVLVRGYNVMQGY 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 444 WNKPEATRESFTEDGWFKTGDTAVY-KNGVYWIMGRTSvDIIKSGGYKISALEVERHLLAHPDITDVAVIGARDATWGQK 522
Cdd:cd17638 201 LDDPEATAEAIDADGWLHTGDVGELdERGYLRITDRLK-DMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEV 279
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1367478878 523 VTAVVQLKRGRSMTLSELKTWAREHMAPYTIPTGLVLVEEMPRNQMGKVNK 573
Cdd:cd17638 280 GKAFVVARPGVTLTEEDVIAWCRERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
54-576 |
6.13e-50 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 180.08 E-value: 6.13e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 54 SAPVFSRAQVYRDKLAIVDDSGSHSYRDLYGSSRGLAGRIKAaldcpSGDLQGKRISFLCANDASYTVAQWASWMCGGTA 133
Cdd:PRK06145 5 SASIAFHARRTPDRAALVYRDQEISYAEFHQRILQAAGMLHA-----RGIGQGDVVALLMKNSAAFLELAFAASYLGAVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 134 VPL-YREHPPsELEYIISDSQSSLLVAGQPYAdtmEPLAhrLGLPYLQL-PPTSSLSSLLEAPEnqpEPGITDWAQRPA- 210
Cdd:PRK06145 80 LPInYRLAAD-EVAYILGDAGAKLLLVDEEFD---AIVA--LETPKIVIdAAAQADSRRLAQGG---LEIPPQAAVAPTd 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 211 --MIIYTSGTTGRPKGVLHTHSNIQAMVQGLVSEWGWSRDDVILHTLPLHHVHGIVNKLLCPLWVGATTVMLPTFQPQKV 288
Cdd:PRK06145 151 lvRLMYTSGTTDRPKGVMHSYGNLHWKSIDHVIALGLTASERLLVVGPLYHVGAFDLPGIAVLWVGGTLRIHREFDPEAV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 289 WEVLLSSK------AP-MVTVFMAVPTIYSKLIqhyeqhftqprvqdfvraackERIRLMVSGSSALPQPTLLRWEEI-T 360
Cdd:PRK06145 231 LAAIERHRltcawmAPvMLSRVLTVPDRDRFDL---------------------DSLAWCIGGGEKTPESRIRDFTRVfT 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 361 GHTLLERYGMTEIGMALSNPLKGPRIP--GAVGVPLPGVEVRIvmtnatsttiAEGNSRetQVRPGLEGkegELMVRGDQ 438
Cdd:PRK06145 290 RARYIDAYGLTETCSGDTLMEAGREIEkiGSTGRALAHVEIRI----------ADGAGR--WLPPNMKG---EICMRGPK 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 439 VFTEYWNKPEATRESFTeDGWFKTGDTAVY-KNGVYWIMGRTSvDIIKSGGYKISALEVERHLLAHPDITDVAVIGARDA 517
Cdd:PRK06145 355 VTKGYWKDPEKTAEAFY-GDWFRSGDVGYLdEEGFLYLTDRKK-DMIISGGENIASSEVERVIYELPEVAEAAVIGVHDD 432
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1367478878 518 TWGQKVTAVVQLKRGRSMTLSELKTWAREHMAPYTIPTGLVLVEEMPRNQMGKVNKKDL 576
Cdd:PRK06145 433 RWGERITAVVVLNPGATLTLEALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVL 491
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
78-506 |
1.04e-49 |
|
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: 178.79 E-value: 1.04e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 78 SYRDLYGSsrglAGRIKAALDCpSGDLQGKRISFLCANDASYTVAQWASWMCGGTAVPLYREHPPSELEYIISDSQSSLL 157
Cdd:cd05914 9 TYKDLADN----IAKFALLLKI-NGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 158 VAGQPyadtmeplahrlglpylqlpptsslsslleapenqpepgitdwaQRPAMIIYTSGTTGRPKGVLHTHSNIQAMVQ 237
Cdd:cd05914 84 FVSDE--------------------------------------------DDVALINYTSGTTGNSKGVMLTYRNIVSNVD 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 238 GLVSEWGWSRDDVILHTLPLHHVHGIVNKLLCPLWVGATTVMLPTFQPQKVwevLLSSKApMVTVFMAVPTIYskLIQHY 317
Cdd:cd05914 120 GVKEVVLLGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFLDKIPSAKI---IALAFA-QVTPTLGVPVPL--VIEKI 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 318 EQHFTQPRV---------------QDFVRAACKE-------RIRLMVSGSSALPQPTLLRWEEItGHTLLERYGMTEIGM 375
Cdd:cd05914 194 FKMDIIPKLtlkkfkfklakkinnRKIRKLAFKKvheafggNIKEFVIGGAKINPDVEEFLRTI-GFPYTIGYGMTETAP 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 376 ALSNPLKGPRIPGAVGVPLPGVEVRIVmtnatsttiaegnsretqvRPGLEGKEGELMVRGDQVFTEYWNKPEATRESFT 455
Cdd:cd05914 273 IISYSPPNRIRLGSAGKVIDGVEVRID-------------------SPDPATGEGEIIVRGPNVMKGYYKNPEATAEAFD 333
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1367478878 456 EDGWFKTGDTAVYKNGVY-WIMGRTSVDIIKSGGYKISALEVERHLLAHPDI 506
Cdd:cd05914 334 KDGWFHTGDLGKIDAEGYlYIRGRKKEMIVLSSGKNIYPEEIEAKINNMPFV 385
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
69-576 |
1.11e-49 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 179.33 E-value: 1.11e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 69 AIVDDSG-SHSYRDLYGSSRGLAGRIKAAldcpsGDLQGKRISFLCANDASYTVAQWASWMCGGTAVPLYREHPPSELEY 147
Cdd:PRK08276 3 VIMAPSGeVVTYGELEARSNRLAHGLRAL-----GLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 148 IISDSQSSLLVAGQPYADTMEPLAHRL--GLPYL-----QLPPTSSLSSLLEApenQPEPGITDWAQRPAMIiYTSGTTG 220
Cdd:PRK08276 78 IVDDSGAKVLIVSAALADTAAELAAELpaGVPLLlvvagPVPGFRSYEEALAA---QPDTPIADETAGADML-YSSGTTG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 221 RPKGVLH--THSNI---QAMVQGLVSEWGWSRDD-VILHTLPLHHV-----HGIVNKLlcplwvGATTVMLPTFQPQKVW 289
Cdd:PRK08276 154 RPKGIKRplPGLDPdeaPGMMLALLGFGMYGGPDsVYLSPAPLYHTaplrfGMSALAL------GGTVVVMEKFDAEEAL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 290 EVLLSSKapmVTVFMAVPTIYSKLIQHYEQhftqprvqdfVRAackeR-----IRLMVSGSSALPQPT---LLRWeeiTG 361
Cdd:PRK08276 228 ALIERYR---VTHSQLVPTMFVRMLKLPEE----------VRA----RydvssLRVAIHAAAPCPVEVkraMIDW---WG 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 362 HTLLERYGMTE-IGMALSNPLKGPRIPGAVGVPLPGvEVRIVmtnatsttiaEGNSRETQVrpgleGKEGELMVRGDQVF 440
Cdd:PRK08276 288 PIIHEYYASSEgGGVTVITSEDWLAHPGSVGKAVLG-EVRIL----------DEDGNELPP-----GEIGTVYFEMDGYP 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 441 TEYWNKPEATRESFTEDGWFKTGDTA-VYKNGVYWIMGRTSvDIIKSGGYKISALEVERHLLAHPDITDVAVIGARDATW 519
Cdd:PRK08276 352 FEYHNDPEKTAAARNPHGWVTVGDVGyLDEDGYLYLTDRKS-DMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEM 430
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 520 GQKVTAVVQLKRG---RSMTLSELKTWAREHMAPYTIPTGLVLVEEMPRNQMGKVNKKDL 576
Cdd:PRK08276 431 GERVKAVVQPADGadaGDALAAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRL 490
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
78-576 |
2.28e-49 |
|
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: 177.24 E-value: 2.28e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 78 SYRDLYGSSRGLAGRIKAAldcpsGDLQGKRISFLCANDASYTVAQWASWMCGGTAVPLYREHPPSELEYIISDSQSSLL 157
Cdd:cd05971 8 TFKELKTASNRFANVLKEI-----GLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 158 VagqpyadtmeplahrlglpylqlpptsslsslleapenqpepgiTDWAQRPAMIIYTSGTTGRPKGVLHTHS------- 230
Cdd:cd05971 83 V--------------------------------------------TDGSDDPALIIYTSGTTGPPKGALHAHRvllghlp 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 231 NIQaMVQGLV----------SEWGWsrddvilhtlplhhVHGIVNKLLCPLWVGATTVM--LPTFQPQKVWEVLlsSKAP 298
Cdd:cd05971 119 GVQ-FPFNLFprdgdlywtpADWAW--------------IGGLLDVLLPSLYFGVPVLAhrMTKFDPKAALDLM--SRYG 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 299 MVTVFMAvPTIYSKLIQHYEQHFTQPRvqdfvraackeRIRLMVSGSSALPQpTLLRW-EEITGHTLLERYGMTEIGMAL 377
Cdd:cd05971 182 VTTAFLP-PTALKMMRQQGEQLKHAQV-----------KLRAIATGGESLGE-ELLGWaREQFGVEVNEFYGQTECNLVI 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 378 SN-PLKGPRIPGAVGVPLPGVEVRIVmtnatsttiaegNSRETQVRPGlegKEGELMVR-GDQV-FTEYWNKPEATRESF 454
Cdd:cd05971 249 GNcSALFPIKPGSMGKPIPGHRVAIV------------DDNGTPLPPG---EVGEIAVElPDPVaFLGYWNNPSATEKKM 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 455 TEDgWFKTGDTAVYKNGVY-WIMGRTSvDIIKSGGYKISALEVERHLLAHPDITDVAVIGARDATWGQKVTAVVQLKRG- 532
Cdd:cd05971 314 AGD-WLLTGDLGRKDSDGYfWYVGRDD-DVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGe 391
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1367478878 533 -RSMTLS-ELKTWAREHMAPYTIPTGLVLVEEMPRNQMGKVNKKDL 576
Cdd:cd05971 392 tPSDALArEIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRREL 437
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
14-576 |
2.62e-49 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 179.35 E-value: 2.62e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 14 RSALASGCLQCEaGPGRwLLRQVLRRAYTSTRARQAAAGdsapvfsrAQVYRDKLAIVDDSGSHSYRDLYGSSRGLAGRI 93
Cdd:PRK07788 22 RVMIRSGAVDLE-RPDN-GLRLAADIRRYGPFAGLVAHA--------ARRAPDRAALIDERGTLTYAELDEQSNALARGL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 94 KAAldcpsGDLQGKRISFLCANDASYTVAQWASWMCGGTAVPLYREHPPSELEYIISDSQSSLLVAGQPYADTMEPLAhr 173
Cdd:PRK07788 92 LAL-----GVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQLAEVAAREGVKALVYDDEFTDLLSALP-- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 174 lglpylqlPPTSSLSSLLEAPENQPEPGITD-----------------WAQRPAMIIYTSGTTGRPKGVLHTHSNIQAMV 236
Cdd:PRK07788 165 --------PDLGRLRAWGGNPDDDEPSGSTDetlddliagsstaplpkPPKPGGIVILTSGTTGTPKGAPRPEPSPLAPL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 237 QGLVSEWGWSRDDVILHTLPLHHVHGIVNKLLCpLWVGATTVMLPTFQPQKVWEVLLSSKApmvTVFMAVPTIYSKLIQH 316
Cdd:PRK07788 237 AGLLSRVPFRAGETTLLPAPMFHATGWAHLTLA-MALGSTVVLRRRFDPEATLEDIAKHKA---TALVVVPVMLSRILDL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 317 YEQHFTQPRVQdfvraackeRIRLMVSGSSALPQPTLLRWEEITGHTLLERYGMTEIGMA-LSNPLKGPRIPGAVGVPLP 395
Cdd:PRK07788 313 GPEVLAKYDTS---------SLKIIFVSGSALSPELATRALEAFGPVLYNLYGSTEVAFAtIATPEDLAEAPGTVGRPPK 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 396 GVEVRIVMTNAtsttiaegnsretqvRPGLEGKEGELMVRGDQVFTEYWNkpeaTRESFTEDGWFKTGDTAVY-KNGVYW 474
Cdd:PRK07788 384 GVTVKILDENG---------------NEVPRGVVGRIFVGNGFPFEGYTD----GRDKQIIDGLLSSGDVGYFdEDGLLF 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 475 IMGRTSvDIIKSGGYKISALEVERHLLAHPDITDVAVIGARDATWGQKVTAVVQLKRGRSMTLSELKTWAREHMAPYTIP 554
Cdd:PRK07788 445 VDGRDD-DMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKAPGAALDEDAIKDYVRDNLARYKVP 523
|
570 580
....*....|....*....|..
gi 1367478878 555 TGLVLVEEMPRNQMGKVNKKDL 576
Cdd:PRK07788 524 RDVVFLDELPRNPTGKVLKREL 545
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
208-580 |
2.78e-49 |
|
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: 173.67 E-value: 2.78e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 208 RPAMIIYTSGTTGRPKGVLHTHSNIQAMVQGLVSEWGWSRDDVILHTLPLHHVHGIVNKLLCpLWVGATTVMLPtfqpqK 287
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLYHVGGLAILVRS-LLAGAELVLLE-----R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 288 VWEVLLSSKAPMVTVFMAVPTIYSKLIqhyEQHFTQPRVqdfvraackERIRLMVSGSSALPQP-----TLLRWEEITGh 362
Cdd:cd17630 75 NQALAEDLAPPGVTHVSLVPTQLQRLL---DSGQGPAAL---------KSLRAVLLGGAPIPPElleraADRGIPLYTT- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 363 tllerYGMTEIGMALSNPLKGPRIPGAVGVPLPGVEVRIVmtnatsttiaegnsretqvrpglegKEGELMVRGDQVFTE 442
Cdd:cd17630 142 -----YGMTETASQVATKRPDGFGRGGVGVLLPGRELRIV-------------------------EDGEIWVGGASLAMG 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 443 YWNKPEatRESFTEDGWFKTGDTAVY-KNGVYWIMGRTSvDIIKSGGYKISALEVERHLLAHPDITDVAVIGARDATWGQ 521
Cdd:cd17630 192 YLRGQL--VPEFNEDGWFTTKDLGELhADGRLTVLGRAD-NMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQ 268
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1367478878 522 KVTAVVQLKRGRsmTLSELKTWAREHMAPYTIPTGLVLVEEMPRNQMGKVNKKDLLKHF 580
Cdd:cd17630 269 RPVAVIVGRGPA--DPAELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRAWL 325
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
57-576 |
2.93e-49 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 179.57 E-value: 2.93e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 57 VFSRA-QVYRDKLAIVDDSGSHSYRDLYGSSRGLAGRIKAALDCPSGDlqgkRISFLCANDASYTVAQWASWMCGGTAV- 134
Cdd:PRK05677 29 VLKQScQRFADKPAFSNLGKTLTYGELYKLSGAFAAWLQQHTDLKPGD----RIAVQLPNVLQYPVAVFGAMRAGLIVVn 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 135 --PLYrehPPSELEYIISDSQSSLLVAGQPYADTMEPLAHRLGL-------------------------------PYLQL 181
Cdd:PRK05677 105 tnPLY---TAREMEHQFNDSGAKALVCLANMAHLAEKVLPKTGVkhvivtevadmlpplkrllinavvkhvkkmvPAYHL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 182 PPTSSLSSLLEAPENQPEPGITDWAQRPAMIIYTSGTTGRPKGVLHTHSNI-------QAMVQGLVSEwgwsRDDVILHT 254
Cdd:PRK05677 182 PQAVKFNDALAKGAGQPVTEANPQADDVAVLQYTGGTTGVAKGAMLTHRNLvanmlqcRALMGSNLNE----GCEILIAP 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 255 LPLHHVHGIVNKLLCPLWVGATTVMLPtfQPQKVWEVLLSSKAPMVTVFMAVPTIYSKLIQHyeQHFtqpRVQDFvraac 334
Cdd:PRK05677 258 LPLYHIYAFTFHCMAMMLIGNHNILIS--NPRDLPAMVKELGKWKFSGFVGLNTLFVALCNN--EAF---RKLDF----- 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 335 kERIRLMVSGSSALPQPTLLRWEEITGHTLLERYGMTEIG-MALSNPLKGPRIpGAVGVPLPGVEVRIVMTNATSTTIae 413
Cdd:PRK05677 326 -SALKLTLSGGMALQLATAERWKEVTGCAICEGYGMTETSpVVSVNPSQAIQV-GTIGIPVPSTLCKVIDDDGNELPL-- 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 414 gnsretqvrpgleGKEGELMVRGDQVFTEYWNKPEATRESFTEDGWFKTGDTAVYKNGVYW-IMGRTSvDIIKSGGYKIS 492
Cdd:PRK05677 402 -------------GEVGELCVKGPQVMKGYWQRPEATDEILDSDGWLKTGDIALIQEDGYMrIVDRKK-DMILVSGFNVY 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 493 ALEVERHLLAHPDITDVAVIGARDATWGQKVTAVVQLKRGRSMTLSELKTWAREHMAPYTIPTGLVLVEEMPRNQMGKVN 572
Cdd:PRK05677 468 PNELEDVLAALPGVLQCAAIGVPDEKSGEAIKVFVVVKPGETLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKIL 547
|
....
gi 1367478878 573 KKDL 576
Cdd:PRK05677 548 RREL 551
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
66-576 |
2.99e-49 |
|
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: 177.48 E-value: 2.99e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 66 DKLAIVDDSGSHSYRDLYGSSRGLAGRIKAALDCPsgdlqGKRISFLCANDASYTVAQWASWMCGGTAVPLYREHPPSEL 145
Cdd:cd12116 2 DATAVRDDDRSLSYAELDERANRLAARLRARGVGP-----GDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 146 EYIISDSQSSLLVAGQpyaDTMEPLAHRLGLPYLQLPptsSLSSLLEAPENQPEPGitdwaqRPAMIIYTSGTTGRPKGV 225
Cdd:cd12116 77 RYILEDAEPALVLTDD---ALPDRLPAGLPVLLLALA---AAAAAPAAPRTPVSPD------DLAYVIYTSGSTGRPKGV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 226 LHTHSNIQAMVQGLVSEWGWSRDDVILH-TLPLHHVHGIvnKLLCPLWVGATTVMLP---TFQPQKVWEVLlssKAPMVT 301
Cdd:cd12116 145 VVSHRNLVNFLHSMRERLGLGPGDRLLAvTTYAFDISLL--ELLLPLLAGARVVIAPretQRDPEALARLI---EAHSIT 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 302 VFMAVPTIYSKLIQhyeqhfTQPRVQDFVRAACkerirlmvsGSSALPqPTLLRWEEITGHTLLERYGMTEI----GMAL 377
Cdd:cd12116 220 VMQATPATWRMLLD------AGWQGRAGLTALC---------GGEALP-PDLAARLLSRVGSLWNLYGPTETtiwsTAAR 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 378 SNPLKGPrIPgaVGVPLPGVEVRIVmtnatsttiaegnsrETQVRPGLEGKEGELMVRGDQVFTEYWNKPEATRESFTED 457
Cdd:cd12116 284 VTAAAGP-IP--IGRPLANTQVYVL---------------DAALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPD 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 458 G-------WFKTGDTAVYK-NGVYWIMGRTSvDIIKSGGYKISALEVERHLLAHPDITDVAVIgARDATWGQKVTAVVQL 529
Cdd:cd12116 346 PfagpgsrLYRTGDLVRRRaDGRLEYLGRAD-GQVKIRGHRIELGEIEAALAAHPGVAQAAVV-VREDGGDRRLVAYVVL 423
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1367478878 530 KRGRSMTLSELKTWAREHMAPYTIPTGLVLVEEMPRNQMGKVNKKDL 576
Cdd:cd12116 424 KAGAAPDAAALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
61-573 |
3.65e-49 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 178.99 E-value: 3.65e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 61 AQVYRDKLAIVDDSGSHSYRDLYGSSRGLAGRIKAAldcpsGDLQGKRISFLCANDASYTVAQWASWMCGGTAVPLYREH 140
Cdd:PRK08162 28 AEVYPDRPAVIHGDRRRTWAETYARCRRLASALARR-----GIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 141 PPSELEYIISDSQSSLLVAGQPYADTMEPLAHRLGLPYL--------QLPPTSSLSSL-LEAPENQPEPGItDWaQRPA- 210
Cdd:PRK08162 103 DAASIAFMLRHGEAKVLIVDTEFAEVAREALALLPGPKPlvidvddpEYPGGRFIGALdYEAFLASGDPDF-AW-TLPAd 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 211 -----MIIYTSGTTGRPKGVLHTHSNIQAMVQGLVSEWGWSRDDVILHTLPLHHVHGivnklLCPLW----VGATTVMLP 281
Cdd:PRK08162 181 ewdaiALNYTSGTTGNPKGVVYHHRGAYLNALSNILAWGMPKHPVYLWTLPMFHCNG-----WCFPWtvaaRAGTNVCLR 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 282 TFQPQKVWEVLLSSKapmVTVFMAVPTIYSKLIQHYEQHftqprvqdfvRAACKERIRLMVSGssALPQPTLLRWEEITG 361
Cdd:PRK08162 256 KVDPKLIFDLIREHG---VTHYCGAPIVLSALINAPAEW----------RAGIDHPVHAMVAG--AAPPAAVIAKMEEIG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 362 HTLLERYGMTEI-GMALSNPLKGP----------RIPGAVGVPLPGVEVRIVMTNATSTTI-AEGnsrETQvrpglegke 429
Cdd:PRK08162 321 FDLTHVYGLTETyGPATVCAWQPEwdalplderaQLKARQGVRYPLQEGVTVLDPDTMQPVpADG---ETI--------- 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 430 GELMVRGDQVFTEYWNKPEATRESFtEDGWFKTGDTAV-YKNGVYWIMGRtSVDIIKSGGYKISALEVERHLLAHPDITD 508
Cdd:PRK08162 389 GEIMFRGNIVMKGYLKNPKATEEAF-AGGWFHTGDLAVlHPDGYIKIKDR-SKDIIISGGENISSIEVEDVLYRHPAVLV 466
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1367478878 509 VAVIGARDATWGQKVTAVVQLKRGRSMTLSELKTWAREHMAPYTIPTGLVLvEEMPRNQMGKVNK 573
Cdd:PRK08162 467 AAVVAKPDPKWGEVPCAFVELKDGASATEEEIIAHCREHLAGFKVPKAVVF-GELPKTSTGKIQK 530
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
90-576 |
6.58e-49 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 177.58 E-value: 6.58e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 90 AGRIKAALDcPSGDLQGKRISFLCANDASYTVAQWASWMCGGTAVPLYREHPPSELEYIISDSQSSLLVAgqpYADTMEP 169
Cdd:PRK12406 21 AARAAGGLA-ALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIA---HADLLHG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 170 LAHRL--GLPYLQLPPTSSLSSL--LEAPENQPEPGITDWAQ--------------RPAMIIYTSGTTGRPKGVLHTHSN 231
Cdd:PRK12406 97 LASALpaGVTVLSVPTPPEIAAAyrISPALLTPPAGAIDWEGwlaqqepydgppvpQPQSMIYTSGTTGHPKGVRRAAPT 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 232 I-QAMVQGLVSE--WGWSRDDVILHTLPLHH----VHGIVNKLLcplwvGATTVMLPTFQPQKVWEVLLSSKapMVTVFM 304
Cdd:PRK12406 177 PeQAAAAEQMRAliYGLKPGIRALLTGPLYHsapnAYGLRAGRL-----GGVLVLQPRFDPEELLQLIERHR--ITHMHM 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 305 aVPTIYSKLIqhyeqhftqpRVQDFVRAACK-ERIRLMVSGssALPQPTLLRWEEIT--GHTLLERYGMTEIG-MALSNP 380
Cdd:PRK12406 250 -VPTMFIRLL----------KLPEEVRAKYDvSSLRHVIHA--AAPCPADVKRAMIEwwGPVIYEYYGSTESGaVTFATS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 381 LKGPRIPGAVGVPLPGVEVRIVMTNAtsttiaegnsretqvRPGLEGKEGELMVR--GDQVFTeYWNKPEATRESfTEDG 458
Cdd:PRK12406 317 EDALSHPGTVGKAAPGAELRFVDEDG---------------RPLPQGEIGEIYSRiaGNPDFT-YHNKPEKRAEI-DRGG 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 459 WFKTGDTA-VYKNGVYWIMGRTSvDIIKSGGYKISALEVERHLLAHPDITDVAVIGARDATWGQKVTAVVQLKRGRSMTL 537
Cdd:PRK12406 380 FITSGDVGyLDADGYLFLCDRKR-DMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPGATLDE 458
|
490 500 510
....*....|....*....|....*....|....*....
gi 1367478878 538 SELKTWAREHMAPYTIPTGLVLVEEMPRNQMGKVNKKDL 576
Cdd:PRK12406 459 ADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRL 497
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
68-580 |
1.01e-48 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 177.39 E-value: 1.01e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 68 LAIVDDSGSHSYRDLYGSSRGLAGRIKAAldcpsGDLQGKRISFLCANDASYTVAQWASWMCGGTAVPLYREHPPSELey 147
Cdd:PRK05852 35 LVVTADRIAISYRDLARLVDDLAGQLTRS-----GLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQ-- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 148 iISDSQSS----LLVAGQPYADTMEPlAHRLglpylqLPPTSSLSSLLEAPENQPEPGITDWAQ-----------RP--A 210
Cdd:PRK05852 108 -RVRSQAAgarvVLIDADGPHDRAEP-TTRW------WPLTVNVGGDSGPSGGTLSVHLDAATEptpatstpeglRPddA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 211 MIIYTSGTTGRPKGVLHTHSNIQAMVQGLVSEWGWSRDDVILHTLPLHHVHGIVNKLLCPLwVGATTVMLPT---FQPQK 287
Cdd:PRK05852 180 MIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHGHGLIAALLATL-ASGGAVLLPArgrFSAHT 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 288 VWEVLlssKAPMVTVFMAVPTIYSKLIQhyeqhftQPRVQDFVRAACKerIRLMVSGSSALPQPTLLRWEEITGHTLLER 367
Cdd:PRK05852 259 FWDDI---KAVGATWYTAVPTIHQILLE-------RAATEPSGRKPAA--LRFIRSCSAPLTAETAQALQTEFAAPVVCA 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 368 YGMTEIG-MALSNPLKG------PRI-PGAVGVPlPGVEVRIVMTNATSTTIAEgnsretqvrpglegkEGELMVRGDQV 439
Cdd:PRK05852 327 FGMTEAThQVTTTQIEGigqtenPVVsTGLVGRS-TGAQIRIVGSDGLPLPAGA---------------VGEVWLRGTTV 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 440 FTEYWNKPEATRESFTeDGWFKTGDT-AVYKNGVYWIMGRTSvDIIKSGGYKISALEVERHLLAHPDITDVAVIGARDAT 518
Cdd:PRK05852 391 VRGYLGDPTITAANFT-DGWLRTGDLgSLSAAGDLSIRGRIK-ELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQL 468
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1367478878 519 WGQKVTAVVQLKRGRSMTLSELKTWAREHMAPYTIPTGLVLVEEMPRNQMGKVNKKDLLKHF 580
Cdd:PRK05852 469 YGEAVAAVIVPRESAPPTAEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRRAVAEQF 530
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
71-580 |
2.08e-48 |
|
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: 176.70 E-value: 2.08e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 71 VDDSGSH---SYRDLYGSSRGLAGRIKAaldcpSGDLQGKRISFLCANDASYTVAQWASWMCGGTAVPL-----YREHPP 142
Cdd:cd05906 31 IDADGSEefqSYQDLLEDARRLAAGLRQ-----LGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLtvpptYDEPNA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 143 SE--LEYIISDSQSSLLVAGQPYADTMEPLAHRLGLPYLQLpptSSLSSLLEAPENQPEPGITdwAQRPAMIIYTSGTTG 220
Cdd:cd05906 106 RLrkLRHIWQLLGSPVVLTDAELVAEFAGLETLSGLPGIRV---LSIEELLDTAADHDLPQSR--PDDLALLMLTSGSTG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 221 RPKGVLHTHSNIQAMVQGLVSEWGWSRDDVILHTLPLHHVHGIVNKLLCPLWVGATTVMLPTfqpqkvwEVLLSSkapmv 300
Cdd:cd05906 181 FPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVPLDHVGGLVELHLRAVYLGCQQVHVPT-------EEILAD----- 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 301 tvfmavPTIYSKLIQHYEQHFT-QPrvqDF-----VRAACKE--------RIRLMVSGSSALPQPTLLRWEEitghtLLE 366
Cdd:cd05906 249 ------PLRWLDLIDRYRVTITwAP---NFafallNDLLEEIedgtwdlsSLRYLVNAGEAVVAKTIRRLLR-----LLE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 367 RY-----------GMTEI--GMALSNPLKGPRIPGA-----VGVPLPGVEVRIVmtnatsttiaegnSRETQVRPglEGK 428
Cdd:cd05906 315 PYglppdairpafGMTETcsGVIYSRSFPTYDHSQAlefvsLGRPIPGVSMRIV-------------DDEGQLLP--EGE 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 429 EGELMVRGDQVFTEYWNKPEATRESFTEDGWFKTGDTAVYKNGVYWIMGRTSvDIIKSGGYKISALEVERHLLAHPDITD 508
Cdd:cd05906 380 VGRLQVRGPVVTKGYYNNPEANAEAFTEDGWFRTGDLGFLDNGNLTITGRTK-DTIIVNGVNYYSHEIEAAVEEVPGVEP 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 509 --VAVIGARDATWGQKVTAVVQLKR-----GRSMTLSELKTWAREHM---APYTIPTGLvlvEEMPRNQMGKVNKKDLLK 578
Cdd:cd05906 459 sfTAAFAVRDPGAETEELAIFFVPEydlqdALSETLRAIRSVVSREVgvsPAYLIPLPK---EEIPKTSLGKIQRSKLKA 535
|
..
gi 1367478878 579 HF 580
Cdd:cd05906 536 AF 537
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
25-573 |
3.13e-48 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 176.50 E-value: 3.13e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 25 EAGPGRWLLRQVLRRAYTSTRARQAaagDSAPVFSRAQVYRdklaivddsgsHSYRDLYGSS----RGLAGRikaaldcp 100
Cdd:PRK12583 8 QGGGDKPLLTQTIGDAFDATVARFP---DREALVVRHQALR-----------YTWRQLADAVdrlaRGLLAL-------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 101 sGDLQGKRISFLCANDASYTVAQWASWMCGGTAV---PLYREhppSELEYIISDSQSSL--------------------- 156
Cdd:PRK12583 66 -GVQPGDRVGIWAPNCAEWLLTQFATARIGAILVninPAYRA---SELEYALGQSGVRWvicadafktsdyhamlqellp 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 157 -LVAGQPYADTMEPLAHRLGLPYLQLPPTSSLSS---LLEAPEnqpepGIT--DWAQR--------PAMIIYTSGTTGRP 222
Cdd:PRK12583 142 gLAEGQPGALACERLPELRGVVSLAPAPPPGFLAwheLQARGE-----TVSreALAERqasldrddPINIQYTSGTTGFP 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 223 KGVLHTHSNIQAMVQGLVSEWGWSRDDVILHTLPLHHVHGIVNKLLCPLWVGATtVMLPT--FQPQKVWEVLLSSKApmv 300
Cdd:PRK12583 217 KGATLSHHNILNNGYFVAESLGLTEHDRLCVPVPLYHCFGMVLANLGCMTVGAC-LVYPNeaFDPLATLQAVEEERC--- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 301 TVFMAVPTIYSKLIQHyeqhftqPRVQDFVRAACKERIrlmVSGSSALPQPTLLRWEEITGHTLLERYGMTEIG-----M 375
Cdd:PRK12583 293 TALYGVPTMFIAELDH-------PQRGNFDLSSLRTGI---MAGAPCPIEVMRRVMDEMHMAEVQIAYGMTETSpvslqT 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 376 ALSNPLkgPRIPGAVGVPLPGVEVRIVMtnatsttiAEGNSRETqvrpgleGKEGELMVRGDQVFTEYWNKPEATRESFT 455
Cdd:PRK12583 363 TAADDL--ERRVETVGRTQPHLEVKVVD--------PDGATVPR-------GEIGELCTRGYSVMKGYWNNPEATAESID 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 456 EDGWFKTGDTAVY-KNGVYWIMGRtSVDIIKSGGYKISALEVERHLLAHPDITDVAVIGARDATWGQKVTAVVQLKRGRS 534
Cdd:PRK12583 426 EDGWMHTGDLATMdEQGYVRIVGR-SKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRLHPGHA 504
|
570 580 590
....*....|....*....|....*....|....*....
gi 1367478878 535 MTLSELKTWAREHMAPYTIPTGLVLVEEMPRNQMGKVNK 573
Cdd:PRK12583 505 ASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQK 543
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
57-576 |
3.42e-48 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 176.55 E-value: 3.42e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 57 VFSRA-QVYRDKLAIVDDSGSHSYRDLYGSSRGLAGRIKAALDCPSGDlqgkRISFLCANDASYTVAQWASWMCGGTAV- 134
Cdd:PRK12492 29 VFERScKKFADRPAFSNLGVTLSYAELERHSAAFAAYLQQHTDLVPGD----RIAVQMPNVLQYPIAVFGALRAGLIVVn 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 135 --PLY--RE--H------------------------PPSELEYIISDSQSSLLVAGQPY-ADTMEPLAHRLgLPYLQLPP 183
Cdd:PRK12492 105 tnPLYtaREmrHqfkdsgaralvylnmfgklvqevlPDTGIEYLIEAKMGDLLPAAKGWlVNTVVDKVKKM-VPAYHLPQ 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 184 TSSLSSLLEAPENQPEPGITDWAQRPAMIIYTSGTTGRPKGVLHTHSNIQAMVQGLVSEWGWSRDD----------VILH 253
Cdd:PRK12492 184 AVPFKQALRQGRGLSLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVRACLSQLGPDgqplmkegqeVMIA 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 254 TLPLHHVHGIVNKLLCPLWVGATTVMLPtfQPQKVWEVLLSSKAPMVTVFMAVPTIYSKLIQHyeqhfTQPRVQDFvraa 333
Cdd:PRK12492 264 PLPLYHIYAFTANCMCMMVSGNHNVLIT--NPRDIPGFIKELGKWRFSALLGLNTLFVALMDH-----PGFKDLDF---- 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 334 ckERIRLMVSGSSALPQPTLLRWEEITGHTLLERYGMTEIG-MALSNPLKGPRIPGAVGVPLPGVEVRIVMTNATSTTIa 412
Cdd:PRK12492 333 --SALKLTNSGGTALVKATAERWEQLTGCTIVEGYGLTETSpVASTNPYGELARLGTVGIPVPGTALKVIDDDGNELPL- 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 413 egnsretqvrpgleGKEGELMVRGDQVFTEYWNKPEATRESFTEDGWFKTGDTAVY-KNGVYWIMGRTSvDIIKSGGYKI 491
Cdd:PRK12492 410 --------------GERGELCIKGPQVMKGYWQQPEATAEALDAEGWFKTGDIAVIdPDGFVRIVDRKK-DLIIVSGFNV 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 492 SALEVERHLLAHPDITDVAVIGARDATWGQKVTAVVqLKRGRSMTLSELKTWAREHMAPYTIPTGLVLVEEMPRNQMGKV 571
Cdd:PRK12492 475 YPNEIEDVVMAHPKVANCAAIGVPDERSGEAVKLFV-VARDPGLSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKI 553
|
....*
gi 1367478878 572 NKKDL 576
Cdd:PRK12492 554 LRREL 558
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
87-514 |
1.52e-47 |
|
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: 173.81 E-value: 1.52e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 87 RGLAGRIKAaLDCPSGDlqgkRISFLCANDASYTVAQWASWMCGGTAVPLYREHPPSELEYIISDSQSSLLVAGQpyADT 166
Cdd:cd05932 17 RRLAAALRA-LGLEPGS----KIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFVGK--LDD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 167 MEPLAHRL--GLPYLQLPPTSSLS-----SLLEAPENQPEPGITDWAQRPAMIIYTSGTTGRPKGVLHTHSNIQAMVQGL 239
Cdd:cd05932 90 WKAMAPGVpeGLISISLPPPSAANcqyqwDDLIAQHPPLEERPTRFPEQLATLIYTSGTTGQPKGVMLTFGSFAWAAQAG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 240 VSEWGWSRDDVILHTLPLHHVHGIVNKLLCPLWVGATTVM---LPTFqPQKVwevllssKAPMVTVFMAVPTIYSKLIQH 316
Cdd:cd05932 170 IEHIGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVAFaesLDTF-VEDV-------QRARPTLFFSVPRLWTKFQQG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 317 YEQHFTQPRVQ-----DFVRAACKERI---------RLMVSGSSALPqPTLLRWEEITGHTLLERYGMTEiGMALSNPLK 382
Cdd:cd05932 242 VQDKIPQQKLNlllkiPVVNSLVKRKVlkglgldqcRLAGCGSAPVP-PALLEWYRSLGLNILEAYGMTE-NFAYSHLNY 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 383 -GPRIPGAVGVPLPGVEVRIvmtnatsttiaegnsretqvrpgleGKEGELMVRGDQVFTEYWNKPEATRESFTEDGWFK 461
Cdd:cd05932 320 pGRDKIGTVGNAGPGVEVRI-------------------------SEDGEILVRSPALMMGYYKDPEATAEAFTADGFLR 374
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1367478878 462 TGDT-AVYKNGVYWIMGRTSvDIIK-SGGYKISALEVERHLLAHPDITDVAVIGA 514
Cdd:cd05932 375 TGDKgELDADGNLTITGRVK-DIFKtSKGKYVAPAPIENKLAEHDRVEMVCVIGS 428
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
61-576 |
8.30e-47 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 172.15 E-value: 8.30e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 61 AQVYRDKLAIVDDSGSHSYRDLYGSSRGLAGRIKAAldcpsGDLQGKRISFLCANDASYTVAQWASWMCGGTAVPL-YRE 139
Cdd:PRK07470 17 ARRFPDRIALVWGDRSWTWREIDARVDALAAALAAR-----GVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTnFRQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 140 HPPsELEYIISDSQSSLLVAGQPYADTMEplAHRLGLPYLQL-------PPTSSLSSLL-EAPENQPEPGITDWAQrPAM 211
Cdd:PRK07470 92 TPD-EVAYLAEASGARAMICHADFPEHAA--AVRAASPDLTHvvaiggaRAGLDYEALVaRHLGARVANAAVDHDD-PCW 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 212 IIYTSGTTGRPKGVLHTHSNIQAMVQGLVSEW--GWSRDDVILHTLPLHHVHGIvnKLLCPLWVGATTVMLPT--FQPQK 287
Cdd:PRK07470 168 FFFTSGTTGRPKAAVLTHGQMAFVITNHLADLmpGTTEQDASLVVAPLSHGAGI--HQLCQVARGAATVLLPSerFDPAE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 288 VWEVLLSSKapmVTVFMAVPTIYSKLIQHyeqhftqPRVQDFVRAAckerIRLMVSGSSALPQPTLLRWEEITGHTLLER 367
Cdd:PRK07470 246 VWALVERHR---VTNLFTVPTILKMLVEH-------PAVDRYDHSS----LRYVIYAGAPMYRADQKRALAKLGKVLVQY 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 368 YGMTEIG-------MALSNPLKGP--RIpGAVGVPLPGVEVRIvmtnatsttiaegnsRETQVRPGLEGKEGELMVRGDQ 438
Cdd:PRK07470 312 FGLGEVTgnitvlpPALHDAEDGPdaRI-GTCGFERTGMEVQI---------------QDDEGRELPPGETGEICVIGPA 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 439 VFTEYWNKPEATRESFtEDGWFKTGDTA-VYKNGVYWIMGRTSvDIIKSGGYKISALEVERHLLAHPDITDVAVIGARDA 517
Cdd:PRK07470 376 VFAGYYNNPEANAKAF-RDGWFRTGDLGhLDARGFLYITGRAS-DMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDP 453
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1367478878 518 TWGQKVTAVVQLKRGRSMTLSELKTWAREHMAPYTIPTGLVLVEEMPRNQMGKVNKKDL 576
Cdd:PRK07470 454 VWGEVGVAVCVARDGAPVDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMV 512
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
120-583 |
3.20e-46 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 171.14 E-value: 3.20e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 120 TVAQWASwmcggtavPLYREHPPSELEYIISDSQSSLLVAGQPYADTMEPLahrlglpyLQLPPTSSLSSLLEAPENQpe 199
Cdd:PLN02860 113 TCSSWYE--------ELQNDRLPSLMWQVFLESPSSSVFIFLNSFLTTEML--------KQRALGTTELDYAWAPDDA-- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 200 pgitdwaqrpAMIIYTSGTTGRPKGVLHTHSNIqaMVQGL--VSEWGWSRDDVILHTLPLHHVHGIvNKLLCPLWVGATT 277
Cdd:PLN02860 175 ----------VLICFTSGTTGRPKGVTISHSAL--IVQSLakIAIVGYGEDDVYLHTAPLCHIGGL-SSALAMLMVGACH 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 278 VMLPTFQPQKVWEVLlssKAPMVTVFMAVPTIYSKLIQHYEQHFTQprvqdfvraACKERIRLMVSGSSALPQPTLLRWE 357
Cdd:PLN02860 242 VLLPKFDAKAALQAI---KQHNVTSMITVPAMMADLISLTRKSMTW---------KVFPSVRKILNGGGSLSSRLLPDAK 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 358 EITGHT-LLERYGMTEIG-----MALSNP-LKGPRIPGA-----------------VGVPLPGVEVRIVMTNATsttiae 413
Cdd:PLN02860 310 KLFPNAkLFSAYGMTEACssltfMTLHDPtLESPKQTLQtvnqtksssvhqpqgvcVGKPAPHVELKIGLDESS------ 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 414 gnsretqvrpglegKEGELMVRGDQVFTEYWNKPEATRESFTEDGWFKTGDT-AVYKNGVYWIMGRTSvDIIKSGGYKIS 492
Cdd:PLN02860 384 --------------RVGRILTRGPHVMLGYWGQNSETASVLSNDGWLDTGDIgWIDKAGNLWLIGRSN-DRIKTGGENVY 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 493 ALEVERHLLAHPDITDVAVIGARDATWGQKVTAVVQLK------------RGRSMTLSE--LKTWARE-HMAPYTIPTGL 557
Cdd:PLN02860 449 PEEVEAVLSQHPGVASVVVVGVPDSRLTEMVVACVRLRdgwiwsdnekenAKKNLTLSSetLRHHCREkNLSRFKIPKLF 528
|
490 500 510
....*....|....*....|....*....|....
gi 1367478878 558 VLVEE-MPRNQMGKVnKKDLLK-------HFFPS 583
Cdd:PLN02860 529 VQWRKpFPLTTTGKI-RRDEVRrevlshlQSLPS 561
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
57-576 |
5.98e-46 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 169.78 E-value: 5.98e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 57 VFSRAQVYRDKLAIVDDSGSHSYRdlYGSSRGLAGRIKAALDcPSGDLQGKRISFLCANDASYTVAQWASWMCGG---TA 133
Cdd:PLN02246 29 CFERLSEFSDRPCLIDGATGRVYT--YADVELLSRRVAAGLH-KLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAvttTA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 134 VPLYrehPPSELEYIISDSQSSLLVAGQPYADTMEPLAHRLGLPYLQL--PPTSSL--SSLLEAPENQ-PEPGITDwaQR 208
Cdd:PLN02246 106 NPFY---TPAEIAKQAKASGAKLIITQSCYVDKLKGLAEDDGVTVVTIddPPEGCLhfSELTQADENElPEVEISP--DD 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 209 PAMIIYTSGTTGRPKGVLHTH----SNIQAMVQGLVSEWGWSRDDVILHTLPLHHVHGIVNKLLCPLWVGATTVMLPTFQ 284
Cdd:PLN02246 181 VVALPYSSGTTGLPKGVMLTHkglvTSVAQQVDGENPNLYFHSDDVILCVLPMFHIYSLNSVLLCGLRVGAAILIMPKFE 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 285 PQKVWEVLLSSKapmVTVFMAVPTIYSKLIQhyeqhftQPRVQDFVRAAckerIRLMVSGSSALP---QPTLLRweEITG 361
Cdd:PLN02246 261 IGALLELIQRHK---VTIAPFVPPIVLAIAK-------SPVVEKYDLSS----IRMVLSGAAPLGkelEDAFRA--KLPN 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 362 HTLLERYGMTEIGMALS-------NPLkgPRIPGAVGVPLPGVEVRIVMTNaTSTTIAEGnsretqvrpglegKEGELMV 434
Cdd:PLN02246 325 AVLGQGYGMTEAGPVLAmclafakEPF--PVKSGSCGTVVRNAELKIVDPE-TGASLPRN-------------QPGEICI 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 435 RGDQVFTEYWNKPEATRESFTEDGWFKTGDTA-VYKNGVYWIMGRTSvDIIKSGGYKISALEVERHLLAHPDITDVAVIG 513
Cdd:PLN02246 389 RGPQIMKGYLNDPEATANTIDKDGWLHTGDIGyIDDDDELFIVDRLK-ELIKYKGFQVAPAELEALLISHPSIADAAVVP 467
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1367478878 514 ARDATWGQKVTAVVQLKRGRSMTLSELKTWAREHMAPYTIPTGLVLVEEMPRNQMGKVNKKDL 576
Cdd:PLN02246 468 MKDEVAGEVPVAFVVRSNGSEITEDEIKQFVAKQVVFYKRIHKVFFVDSIPKAPSGKILRKDL 530
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
66-576 |
7.71e-46 |
|
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341304 [Multi-domain] Cd Length: 450 Bit Score: 167.55 E-value: 7.71e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 66 DKLAIVDDSGSHSYRDLYGSSRGLAGRIKAAldcpsGDLQGKRISFLCANDASYTVAQWASWMCGGTAVPLYREHPPSEL 145
Cdd:cd17649 2 DAVALVFGDQSLSYAELDARANRLAHRLRAL-----GVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 146 EYIISDSQSSLLvagqpyadtmepLAHRlglpylqlpptsslsslleaPENqpepgitdwaqrPAMIIYTSGTTGRPKGV 225
Cdd:cd17649 77 RYMLEDSGAGLL------------LTHH--------------------PRQ------------LAYVIYTSGSTGTPKGV 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 226 LHTHSNIQAMVQGLVSEWGWSRDDVILHTLPLhHVHGIVNKLLCPLWVGATTVMLPTFQPQKVWEVLLSSKAPMVTVfMA 305
Cdd:cd17649 113 AVSHGPLAAHCQATAERYGLTPGDRELQFASF-NFDGAHEQLLPPLICGACVVLRPDELWASADELAEMVRELGVTV-LD 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 306 VPTIY-SKLIQHYEQHftQPRVQdfvraackERIRLMVSGSSALPQPTLLRWEEItGHTLLERYGMTEigmALSNPL--- 381
Cdd:cd17649 191 LPPAYlQQLAEEADRT--GDGRP--------PSLRLYIFGGEALSPELLRRWLKA-PVRLFNAYGPTE---ATVTPLvwk 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 382 -------KGPRIPgaVGVPLPGVEVRIVmtnatsttiaegnsrETQVRPGLEGKEGELMVRGDQVFTEYWNKPEATRESF 454
Cdd:cd17649 257 ceagaarAGASMP--IGRPLGGRSAYIL---------------DADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERF 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 455 TEDG-------WFKTGDTAVYK-NGVYWIMGRTSvDIIKSGGYKISALEVERHLLAHPDITDVAVIgARDATWGQKVTAV 526
Cdd:cd17649 320 VPDPfgapgsrLYRTGDLARWRdDGVIEYLGRVD-HQVKIRGFRIELGEIEAALLEHPGVREAAVV-ALDGAGGKQLVAY 397
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1367478878 527 VQLKRGRSM--TLSELKTWAREHMAPYTIPTGLVLVEEMPRNQMGKVNKKDL 576
Cdd:cd17649 398 VVLRAAAAQpeLRAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKAL 449
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
46-576 |
8.23e-46 |
|
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: 168.68 E-value: 8.23e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 46 ARQAAAgdsAPvfsraqvyrDKLAIVDDSGSHSYRDLYGSSRGLAGRIkAALDCPSGDLQGkrisfLCAN-DASYTVAQW 124
Cdd:cd17651 2 ERQAAR---TP---------DAPALVAEGRRLTYAELDRRANRLAHRL-RARGVGPGDLVA-----LCARrSAELVVALL 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 125 ASWMCGGTAVPLYREHPPSELEYIISDSQSSLLVAGQPYADTMEPLAHrLGLPYLQLPPTSslsslleAPENQPEPGITd 204
Cdd:cd17651 64 AILKAGAAYVPLDPAYPAERLAFMLADAGPVLVLTHPALAGELAVELV-AVTLLDQPGAAA-------GADAEPDPALD- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 205 wAQRPAMIIYTSGTTGRPKGVLHTHSNIQAMVQGLVSEWGWSRDDVILHTLPLH---HVHGIVNKLLCplwvGATTVMLP 281
Cdd:cd17651 135 -ADDLAYVIYTSGSTGRPKGVVMPHRSLANLVAWQARASSLGPGARTLQFAGLGfdvSVQEIFSTLCA----GATLVLPP 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 282 T---FQPQKVWEVLlsSKAPMVTVFMavPTIYSK-LIQHYEQHFTQPrvqdfvraackERIRLMVSGSSALPQPTLLRwE 357
Cdd:cd17651 210 EevrTDPPALAAWL--DEQRISRVFL--PTVALRaLAEHGRPLGVRL-----------AALRYLLTGGEQLVLTEDLR-E 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 358 EITGH---TLLERYGMTE----IGMALSNPLKGPRIPGAVGVPLPGVEVRIVmtnatsttiaegnsrETQVRPGLEGKEG 430
Cdd:cd17651 274 FCAGLpglRLHNHYGPTEthvvTALSLPGDPAAWPAPPPIGRPIDNTRVYVL---------------DAALRPVPPGVPG 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 431 ELMVRGDQVFTEYWNKPEATRESFTEDGW------FKTGDTAVY-KNGVYWIMGRTSvDIIKSGGYKISALEVERHLLAH 503
Cdd:cd17651 339 ELYIGGAGLARGYLNRPELTAERFVPDPFvpgarmYRTGDLARWlPDGELEFLGRAD-DQVKIRGFRIELGEIEAALARH 417
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1367478878 504 PDITDVAVIGARDATWGQKVTAVVQLKRGRSMTLSELKTWAREHMAPYTIPTGLVLVEEMPRNQMGKVNKKDL 576
Cdd:cd17651 418 PGVREAVVLAREDRPGEKRLVAYVVGDPEAPVDAAELRAALATHLPEYMVPSAFVLLDALPLTPNGKLDRRAL 490
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
66-576 |
2.16e-45 |
|
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: 166.33 E-value: 2.16e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 66 DKLAIVDDSGSHSYRDLYGSSRGLAGRIKAAldcpsGDLQGKRISFLCANDASYTVAQWASWMCGGTAVPLYREHPPSEL 145
Cdd:cd17643 2 EAVAVVDEDRRLTYGELDARANRLARTLRAE-----GVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 146 EYIISDSQSSLLVagqpyadtmeplahrlglpylqlpptsslsslleapeNQPEpgitdwaqRPAMIIYTSGTTGRPKGV 225
Cdd:cd17643 77 AFILADSGPSLLL-------------------------------------TDPD--------DLAYVIYTSGSTGRPKGV 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 226 LHTHSNIQAMVQGLVSEWGWSRDDVilhTLPLHH---------VHGivnkllcPLWVGATTVMLP---TFQPQKVWEVLL 293
Cdd:cd17643 112 VVSHANVLALFAATQRWFGFNEDDV---WTLFHSyafdfsvweIWG-------ALLHGGRLVVVPyevARSPEDFARLLR 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 294 SSKapmVTVFMAVPTIYSKLIQHYEQHFTQPrvqdfvraackERIRLMVSGSSALPQPTLLRWEEITGH---TLLERYGM 370
Cdd:cd17643 182 DEG---VTVLNQTPSAFYQLVEAADRDGRDP-----------LALRYVIFGGEALEAAMLRPWAGRFGLdrpQLVNMYGI 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 371 TEIGMALS-NPLKGPRIPGA----VGVPLPGVEVRIVMTNatsttiaegnsretqVRPGLEGKEGELMVRGDQVFTEYWN 445
Cdd:cd17643 248 TETTVHVTfRPLDAADLPAAaaspIGRPLPGLRVYVLDAD---------------GRPVPPGVVGELYVSGAGVARGYLG 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 446 KPEATRESFTEDGW-------FKTGDTAVYK-NGVYWIMGRTSvDIIKSGGYKISALEVERHLLAHPDITDVAVIGARDA 517
Cdd:cd17643 313 RPELTAERFVANPFggpgsrmYRTGDLARRLpDGELEYLGRAD-EQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDE 391
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1367478878 518 TWGQKVTAVVQLKRGRSMTLSELKTWAREHMAPYTIPTGLVLVEEMPRNQMGKVNKKDL 576
Cdd:cd17643 392 PGDTRLVAYVVADDGAAADIAELRALLKELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
60-573 |
3.19e-45 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 168.01 E-value: 3.19e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 60 RAQVYRDKLAIVDDSGSHSYRDLYGSSRGLAGRIKAAldcpsGDLQGKRISFLCANDASY-TVAQWASWMcGGTAVPLYR 138
Cdd:PRK06155 30 QAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAA-----GVKRGDRVALMCGNRIEFlDVFLGCAWL-GAIAVPINT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 139 EHPPSELEYIISDSQSSLLVAGQPYADTMEPLAHRL-------------------GLPYLQLPPTSSLsslleAPENQPE 199
Cdd:PRK06155 104 ALRGPQLEHILRNSGARLLVVEAALLAALEAADPGDlplpavwlldapasvsvpaGWSTAPLPPLDAP-----APAAAVQ 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 200 PGitdwaqRPAMIIYTSGTTGRPKGVLHTHSNIQAMVQGLVSEWGWSRDDVILHTLPLHHVHGIvNKLLCPLWVGATTVM 279
Cdd:PRK06155 179 PG------DTAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADDVLYTTLPLFHTNAL-NAFFQALLAGATYVL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 280 LPTFQPQKVWEVLLSSKApmvTVFMAVPTIYSKLIQhyeqhfTQPRVQDfvrAACKERIRLMVSGSSALPQPTLLRweei 359
Cdd:PRK06155 252 EPRFSASGFWPAVRRHGA---TVTYLLGAMVSILLS------QPARESD---RAHRVRVALGPGVPAALHAAFRER---- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 360 TGHTLLERYGMTEIGMALSNPLKGPRiPGAVGVPLPGVEVRIVmtnatsttiaegNSRETQVRPGlegKEGELMVRGDQV 439
Cdd:PRK06155 316 FGVDLLDGYGSTETNFVIAVTHGSQR-PGSMGRLAPGFEARVV------------DEHDQELPDG---EPGELLLRADEP 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 440 F---TEYWNKPEATRESFtEDGWFKTGDTAVYK-NGVYWIMGRTSvDIIKSGGYKISALEVERHLLAHPDITDVAVIGAR 515
Cdd:PRK06155 380 FafaTGYFGMPEKTVEAW-RNLWFHTGDRVVRDaDGWFRFVDRIK-DAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVP 457
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1367478878 516 DATWGQKVTAVVQLKRGRSMTLSELKTWAREHMAPYTIPTGLVLVEEMPRNQMGKVNK 573
Cdd:PRK06155 458 SELGEDEVMAAVVLRDGTALEPVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQK 515
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
57-576 |
8.99e-45 |
|
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an AMP-binding domain (pfam00501) associated with acyl CoA-ligases. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present next to a decarboxylase enzyme. A number of sequences from Burkholderia species also hit this model, but the genomic context is obviously different. The hypothesis of a constant substrate for this family is only strong where the exosortase context is present.
Pssm-ID: 211788 [Multi-domain] Cd Length: 517 Bit Score: 166.11 E-value: 8.99e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 57 VFSRAQVYRDKLAIVDDSGSHSYRDLYGSSRGLAGRIKAAldcpsGDLQGKRISFLCANDASYTVAQWASWMCGGTAVPL 136
Cdd:TIGR03098 6 LEDAAARLPDATALVHHDRTLTYAALSERVLALASGLRGL-----GLARGERVAIYLDKRLETVTAMFGAALAGGVFVPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 137 YREHPPSELEYIISDSQSSLLVAGqpyadtmeplAHRLGLPYLQLPPTSSLSSLL------EAPENQPEPGITDWAQ--- 207
Cdd:TIGR03098 81 NPLLKAEQVAHILADCNVRLLVTS----------SERLDLLHPALPGCHDLRTLIivgdpaHASEGHPGEEPASWPKlla 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 208 -------------RPAMIIYTSGTTGRPKGVLHTHSNIQAMVQGLVSEWGWSRDDVILHTLPLHHVHGIvNKLLCPLWVG 274
Cdd:TIGR03098 151 lgdadpphpvidsDMAAILYTSGSTGRPKGVVLSHRNLVAGAQSVATYLENRPDDRLLAVLPLSFDYGF-NQLTTAFYVG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 275 ATTVMLPTFQPQkvwEVLLSSKAPMVTVFMAVPTIYSKLiqhyeqhftqprVQDFVRAACKERIRLMVSGSSALPQPTLL 354
Cdd:TIGR03098 230 ATVVLHDYLLPR---DVLKALEKHGITGLAAVPPLWAQL------------AQLDWPESAAPSLRYLTNSGGAMPRATLS 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 355 RWEEITGHT-LLERYGMTEIGMALS-NPLKGPRIPGAVGVPLPGVEVRIVMtnatsttiAEGNSRETqvrpgleGKEGEL 432
Cdd:TIGR03098 295 RLRSFLPNArLFLMYGLTEAFRSTYlPPEEVDRRPDSIGKAIPNAEVLVLR--------EDGSECAP-------GEEGEL 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 433 MVRGDQVFTEYWNKPEATRESFT----EDGWFKTGDTAVY--------KNGVYWIMGRTSvDIIKSGGYKISALEVERHL 500
Cdd:TIGR03098 360 VHRGALVAMGYWNDPEKTAERFRplppFPGELHLPELAVWsgdtvrrdEEGFLYFVGRRD-EMIKTSGYRVSPTEVEEVA 438
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1367478878 501 LAHPDITDVAVIGARDATWGQKVTAVVQLKRGRSMTLSELKTWAREHMAPYTIPTGLVLVEEMPRNQMGKVNKKDL 576
Cdd:TIGR03098 439 YATGLVAEAVAFGVPDPTLGQAIVLVVTPPGGEELDRAALLAECRARLPNYMVPALIHVRQALPRNANGKIDRKAL 514
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
34-577 |
1.16e-43 |
|
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: 167.73 E-value: 1.16e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 34 RQVLRRAYTSTRARQAAAGD-SAPVFSRAQVYRDKLAIVDDSGSHSYRDLYGSSRGLAGRIkAALDCPSGDLQGkrisfL 112
Cdd:COG1020 458 RQQLLAEWNATAAPYPADATlHELFEAQAARTPDAVAVVFGDQSLTYAELNARANRLAHHL-RALGVGPGDLVG-----V 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 113 CAN-DASYTVAQWASWMCGGTAVPLYREHPPSELEYIISDSQSSLLVAGQPYADTMEPLahrlGLPYLQLPPtsslSSLL 191
Cdd:COG1020 532 CLErSLEMVVALLAVLKAGAAYVPLDPAYPAERLAYMLEDAGARLVLTQSALAARLPEL----GVPVLALDA----LALA 603
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 192 EAPENQPEPGITdwAQRPAMIIYTSGTTGRPKGVLHTHSNIQAMVQGLVSEWGWSRDDVILHTLPLHH---VHGIvnklL 268
Cdd:COG1020 604 AEPATNPPVPVT--PDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFASLSFdasVWEI----F 677
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 269 CPLWVGATTVMLP---TFQPQKVWEVLLSSKapmVTVFMAVPTIYSKLIQHYEQHFTQPRvqdfvraackeriRLMVSGs 345
Cdd:COG1020 678 GALLSGATLVLAPpeaRRDPAALAELLARHR---VTVLNLTPSLLRALLDAAPEALPSLR-------------LVLVGG- 740
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 346 SALPQPTLLRWEEITGHT-LLERYGMTE------IGMALSNPLKGPRIPgaVGVPLPGVEVRIVmtnatsttiaegNSRE 418
Cdd:COG1020 741 EALPPELVRRWRARLPGArLVNLYGPTEttvdstYYEVTPPDADGGSVP--IGRPIANTRVYVL------------DAHL 806
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 419 TQVRPGLegkEGELMVRGDQVFTEYWNKPEATRESFTEDG-------WFKTGDTAVY-KNGVYWIMGRTSvDIIKSGGYK 490
Cdd:COG1020 807 QPVPVGV---PGELYIGGAGLARGYLNRPELTAERFVADPfgfpgarLYRTGDLARWlPDGNLEFLGRAD-DQVKIRGFR 882
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 491 ISALEVERHLLAHPDITDVAVIGARDATWGQKVTAVVQLKRGRSMTLSELKTWAREHMAPYTIPTGLVLVEEMPRNQMGK 570
Cdd:COG1020 883 IELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGK 962
|
....*..
gi 1367478878 571 VNKKDLL 577
Cdd:COG1020 963 LDRLALP 969
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
61-573 |
1.72e-43 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 163.44 E-value: 1.72e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 61 AQVYRDKLAIVD-DSGSH-SYRDLYGSSRGLA-GRIKAALDcpsgdlQGKRISFLCANDASYTVAQWASWMCGGTAV--- 134
Cdd:PRK08315 26 AARYPDREALVYrDQGLRwTYREFNEEVDALAkGLLALGIE------KGDRVGIWAPNVPEWVLTQFATAKIGAILVtin 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 135 PLYREHppsELEYIISDSQSSLLVA-----GQPYADTMEPLAHRLG-----------LPYLQ---------LPPTSSLSS 189
Cdd:PRK08315 100 PAYRLS---ELEYALNQSGCKALIAadgfkDSDYVAMLYELAPELAtcepgqlqsarLPELRrviflgdekHPGMLNFDE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 190 LLEAPENQPEPGITDWAQR-----PAMIIYTSGTTGRPKGVLHTHSNI--------QAMvqglvsewGWSRDDVILHTLP 256
Cdd:PRK08315 177 LLALGRAVDDAELAARQATldpddPINIQYTSGTTGFPKGATLTHRNIlnngyfigEAM--------KLTEEDRLCIPVP 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 257 LHHVHGIVNKLLCPLWVGATTV-MLPTFQPQKVWEVLLSSKApmvTVFMAVPTIYSKLIQHyeqhftqPRVQDF----VR 331
Cdd:PRK08315 249 LYHCFGMVLGNLACVTHGATMVyPGEGFDPLATLAAVEEERC---TALYGVPTMFIAELDH-------PDFARFdlssLR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 332 ------AAC-----KERIRLMvsgssalpqptllRWEEITghtllERYGMTEI--GMALSN---PLKgpRIPGAVGVPLP 395
Cdd:PRK08315 319 tgimagSPCpievmKRVIDKM-------------HMSEVT-----IAYGMTETspVSTQTRtddPLE--KRVTTVGRALP 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 396 GVEVRIVmtnatsttiaEGNSRETQVRpgleGKEGELMVRGDQVFTEYWNKPEATRESFTEDGWFKTGDTAVY-KNGVYW 474
Cdd:PRK08315 379 HLEVKIV----------DPETGETVPR----GEQGELCTRGYSVMKGYWNDPEKTAEAIDADGWMHTGDLAVMdEEGYVN 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 475 IMGRTSvDIIKSGGYKISALEVERHLLAHPDITDVAVIGARDATWGQKVTAVVQLKRGRSMTLSELKTWAREHMAPYTIP 554
Cdd:PRK08315 445 IVGRIK-DMIIRGGENIYPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRPGATLTEEDVRDFCRGKIAHYKIP 523
|
570
....*....|....*....
gi 1367478878 555 TGLVLVEEMPRNQMGKVNK 573
Cdd:PRK08315 524 RYIRFVDEFPMTVTGKIQK 542
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
46-576 |
1.78e-43 |
|
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: 162.06 E-value: 1.78e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 46 ARQAAAGDSAPvfsraqvyrdklAIVDDSGSHSYRDLYGSSRGLAGRIKAAldcpsGDLQGKRISFLCANDASYTVAQWA 125
Cdd:cd17646 5 AEQAARTPDAP------------AVVDEGRTLTYRELDERANRLAHLLRAR-----GVGPEDRVAVLLPRSADLVVALLA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 126 SWMCGGTAVPLYREHPPSELEYIISDSQSSLLVAGqpyADTMEPLAHRLGLPYLQLPPTSSLSSLLEAPENQPEpgitdw 205
Cdd:cd17646 68 VLKAGAAYLPLDPGYPADRLAYMLADAGPAVVLTT---ADLAARLPAGGDVALLGDEALAAPPATPPLVPPRPD------ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 206 aqRPAMIIYTSGTTGRPKGVLHTHSNIQAMVQGLVSEWGWSRDDVILHTLPLhhvhGI---VNKLLCPLWVGATTVMLPt 282
Cdd:cd17646 139 --NLAYVIYTSGSTGRPKGVMVTHAGIVNRLLWMQDEYPLGPGDRVLQKTPL----SFdvsVWELFWPLVAGARLVVAR- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 283 fqPQKvwevllsskapmvtvfMAVPTIYSKLIQHYE---QHFTQPRVQDFVRAACKER---IRLMVSGSSALPQPTLLRW 356
Cdd:cd17646 212 --PGG----------------HRDPAYLAALIREHGvttCHFVPSMLRVFLAEPAAGScasLRRVFCSGEALPPELAARF 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 357 EEITGHTLLERYGMTE--IGM---ALSNPLKGPRIPgaVGVPLPGVEVRIVmtnatsttiaegnsrETQVRPGLEGKEGE 431
Cdd:cd17646 274 LALPGAELHNLYGPTEaaIDVthwPVRGPAETPSVP--IGRPVPNTRLYVL---------------DDALRPVPVGVPGE 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 432 LMVRGDQVFTEYWNKPEATRESFTEDgWF-------KTGDTAVYK-NGVYWIMGRTSvDIIKSGGYKISALEVERHLLAH 503
Cdd:cd17646 337 LYLGGVQLARGYLGRPALTAERFVPD-PFgpgsrmyRTGDLARWRpDGALEFLGRSD-DQVKIRGFRVEPGEIEAALAAH 414
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1367478878 504 PDITDVAVIGARDATWGQKVTAVVQLKRGRS-MTLSELKTWAREHMAPYTIPTGLVLVEEMPRNQMGKVNKKDL 576
Cdd:cd17646 415 PAVTHAVVVARAAPAGAARLVGYVVPAAGAAgPDTAALRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
125-577 |
2.24e-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.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 161.07 E-value: 2.24e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 125 ASWMCGGTAVPLYREHPPSELEYIISDSQSSLLVAGQPYADTMeplahRLGLPYLQLPPTSSLSSLLEAPEnQPEPGITD 204
Cdd:cd05922 41 AGGRLGLVFVPLNPTLKESVLRYLVADAGGRIVLADAGAADRL-----RDALPASPDPGTVLDADGIRAAR-ASAPAHEV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 205 WAQRPAMIIYTSGTTGRPKGVLHTHSNIQAMVQGLVSEWGWSRDDVILHTLPLHHVHGIvNKLLCPLWVGATTVMLPTFQ 284
Cdd:cd05922 115 SHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADDRALTVLPLSYDYGL-SVLNTHLLRGATLVLTNDGV 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 285 -PQKVWEVLlssKAPMVTVFMAVPTIYSKLiqhyeqhftqpRVQDFVRAACKErIRLMVSGSSALPQPTLLRWEE-ITGH 362
Cdd:cd05922 194 lDDAFWEDL---REHGATGLAGVPSTYAML-----------TRLGFDPAKLPS-LRYLTQAGGRLPQETIARLRElLPGA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 363 TLLERYGMTEI--GMALSNPLKGPRIPGAVGVPLPGVEVRIVmtnatsttiaegNSRETQVRPgleGKEGELMVRGDQVF 440
Cdd:cd05922 259 QVYVMYGQTEAtrRMTYLPPERILEKPGSIGLAIPGGEFEIL------------DDDGTPTPP---GEPGEIVHRGPNVM 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 441 TEYWNKPEATRESFTEDGWFKTGDTAVY-KNGVYWIMGRTSvDIIKSGGYKISALEVERHLLAHPDITDVAVIGArDATW 519
Cdd:cd05922 324 KGYWNDPPYRRKEGRGGGVLHTGDLARRdEDGFLFIVGRRD-RMIKLFGNRISPTEIEAAARSIGLIIEAAAVGL-PDPL 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1367478878 520 GQKVTAVVQLKRGrsMTLSELKTWAREHMAPYTIPTGLVLVEEMPRNQMGKVNKKDLL 577
Cdd:cd05922 402 GEKLALFVTAPDK--IDPKDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
66-570 |
3.00e-43 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 162.36 E-value: 3.00e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 66 DKLAIVDDSGSHSYRDLYGSSRGLAGRIKAAldcpsGDLQGKRISFLCANDASYTVAQWASWMCGGTAVPL-YReHPPSE 144
Cdd:PRK07798 18 DRVALVCGDRRLTYAELEERANRLAHYLIAQ-----GLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVnYR-YVEDE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 145 LEYIISDSQSSLLVAGQPYADTMEPLAHRL-GLPYL----------QLPPTSSLSSLLEAPEnqPEPgitDWAQRPA--- 210
Cdd:PRK07798 92 LRYLLDDSDAVALVYEREFAPRVAEVLPRLpKLRTLvvvedgsgndLLPGAVDYEDALAAGS--PER---DFGERSPddl 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 211 MIIYTSGTTGRPKGVLHTHSNIQaMVQG----------LVSEWGWSRDD------VILHTLPLHHVHGIVNKLLCpLWVG 274
Cdd:PRK07798 167 YLLYTGGTTGMPKGVMWRQEDIF-RVLLggrdfatgepIEDEEELAKRAaagpgmRRFPAPPLMHGAGQWAAFAA-LFSG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 275 ATTVMLP--TFQPQKVWEVLLSSKAPMVTVF---MAVPtiyskLIQHYEQhftqPRVQDFvraackERIRLMVSGSSALP 349
Cdd:PRK07798 245 QTVVLLPdvRFDADEVWRTIEREKVNVITIVgdaMARP-----LLDALEA----RGPYDL------SSLFAIASGGALFS 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 350 QPTLLRWEEITGH-TLLERYGMTEIG-MALSNPLKGPRIPGAvgvplPGVEVRivmtnaTSTTIAEGNSREtqVRPGlEG 427
Cdd:PRK07798 310 PSVKEALLELLPNvVLTDSIGSSETGfGGSGTVAKGAVHTGG-----PRFTIG------PRTVVLDEDGNP--VEPG-SG 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 428 KEGELmVRGDQVFTEYWNKPEATRESFTE-DG--WFKTGDTA-VYKNGVYWIMGRTSVdIIKSGGYKISALEVERHLLAH 503
Cdd:PRK07798 376 EIGWI-ARRGHIPLGYYKDPEKTAETFPTiDGvrYAIPGDRArVEADGTITLLGRGSV-CINTGGEKVFPEEVEEALKAH 453
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1367478878 504 PDITDVAVIGARDATWGQKVTAVVQLKRGRSMTLSELKTWAREHMAPYTIPTGLVLVEEMPRNQMGK 570
Cdd:PRK07798 454 PDVADALVVGVPDERWGQEVVAVVQLREGARPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
57-581 |
4.18e-43 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 162.32 E-value: 4.18e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 57 VFSRAQvYRDKLAIVDDSG--SHSYRDLygssRGLAGRIKAALDCPSGDLQGKRISFLCANDASYTVAQWASWMCGGTAV 134
Cdd:PLN02574 46 IFSHHN-HNGDTALIDSSTgfSISYSEL----QPLVKSMAAGLYHVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 135 PLYREHPPSELEYIISDSQSSLLVAGQPYADTMEPLahrlGLPYLQLPPTSSLSS-----------LLEAPENQPEPGIT 203
Cdd:PLN02574 121 TMNPSSSLGEIKKRVVDCSVGLAFTSPENVEKLSPL----GVPVIGVPENYDFDSkriefpkfyelIKEDFDFVPKPVIK 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 204 DwaQRPAMIIYTSGTTGRPKGVLHTHSNIQAMVQGLV----SEWGWS-RDDVILHTLPLHHVHGIVNKLLCPLWVGATTV 278
Cdd:PLN02574 197 Q--DDVAAIMYSSGTTGASKGVVLTHRNLIAMVELFVrfeaSQYEYPgSDNVYLAALPMFHIYGLSLFVVGLLSLGSTIV 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 279 MLPTFQPQKVWEVLLSSKapmVTVFMAVPTIYSKLIqhyeqHFTQPrvqdfVRAACKERIRLMVSGSSALPQPTLLRWEE 358
Cdd:PLN02574 275 VMRRFDASDMVKVIDRFK---VTHFPVVPPILMALT-----KKAKG-----VCGEVLKSLKQVSCGAAPLSGKFIQDFVQ 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 359 ITGHT-LLERYGMTE---IGMALSNPLKGPRIpGAVGVPLPGVEVRIVMTnATSTTIAEGNSretqvrpglegkeGELMV 434
Cdd:PLN02574 342 TLPHVdFIQGYGMTEstaVGTRGFNTEKLSKY-SSVGLLAPNMQAKVVDW-STGCLLPPGNC-------------GELWI 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 435 RGDQVFTEYWNKPEATRESFTEDGWFKTGDTAVY-KNGVYWIMGRTSvDIIKSGGYKISALEVERHLLAHPDITDVAVIG 513
Cdd:PLN02574 407 QGPGVMKGYLNNPKATQSTIDKDGWLRTGDIAYFdEDGYLYIVDRLK-EIIKYKGFQIAPADLEAVLISHPEIIDAAVTA 485
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1367478878 514 ARDATWGQKVTAVVQLKRGRSMTLSELKTWAREHMAPYTIPTGLVLVEEMPRNQMGKVNKKdLLKHFF 581
Cdd:PLN02574 486 VPDKECGEIPVAFVVRRQGSTLSQEAVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRR-ELKRSL 552
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
60-576 |
1.08e-42 |
|
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: 159.67 E-value: 1.08e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 60 RAQVYR--DKLAIVDDSGSHSYRDLYGSSRGLAGRIKAAldcpsGDLQGKRISFLCANDASYTVAQWASWMCGGTAVPLY 137
Cdd:cd12117 4 EEQAARtpDAVAVVYGDRSLTYAELNERANRLARRLRAA-----GVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 138 REHPPSELEYIISDSQSSLLVAGQPYADTmeplahrlglpyLQLPPTSSLSSLLEAPENQPEPGITDWAQRPAMIIYTSG 217
Cdd:cd12117 79 PELPAERLAFMLADAGAKVLLTDRSLAGR------------AGGLEVAVVIDEALDAGPAGNPAVPVSPDDLAYVMYTSG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 218 TTGRPKGVLHTHSNiqamVQGLVSEWGWSR---DDVILHTLPL------HHVHGivnkllcPLWVGATTVMLPT---FQP 285
Cdd:cd12117 147 STGRPKGVAVTHRG----VVRLVKNTNYVTlgpDDRVLQTSPLafdastFEIWG-------ALLNGARLVLAPKgtlLDP 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 286 QKVWEVLLSSKapmVTVFMAVPTIYSKLIQHyeqhftqprvqdfvRAACKERIRLMVSGSSALPQPTLLRWEEITGH-TL 364
Cdd:cd12117 216 DALGALIAEEG---VTVLWLTAALFNQLADE--------------DPECFAGLRELLTGGEVVSPPHVRRVLAACPGlRL 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 365 LERYGMTE-IGMALSNPLK-----GPRIPgaVGVPLPGVEVRIVmtnatsttiaegnsrETQVRPGLEGKEGELMVRGDQ 438
Cdd:cd12117 279 VNGYGPTEnTTFTTSHVVTeldevAGSIP--IGRPIANTRVYVL---------------DEDGRPVPPGVPGELYVGGDG 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 439 VFTEYWNKPEATRESFTEDGW------FKTGDTAVYK-NGVYWIMGRTSvDIIKSGGYKISALEVERHLLAHPDITDVAV 511
Cdd:cd12117 342 LALGYLNRPALTAERFVADPFgpgerlYRTGDLARWLpDGRLEFLGRID-DQVKIRGFRIELGEIEAALRAHPGVREAVV 420
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1367478878 512 IgARDATWGQK--VTAVVqlkRGRSMTLSELKTWAREHMAPYTIPTGLVLVEEMPRNQMGKVNKKDL 576
Cdd:cd12117 421 V-VREDAGGDKrlVAYVV---AEGALDAAELRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
208-571 |
2.52e-42 |
|
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: 154.49 E-value: 2.52e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 208 RPAMIIYTSGTTGRPKGVLHTH-SNIQAMVQGlVSEWGWSRDDVILHTLPLHHVHGIvNKLLCPLWVGATTVMLPTFQPQ 286
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRSErSWIESFVCN-EDLFNISGEDAILAPGPLSHSLFL-YGAISALYLGGTFIGQRKFNPK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 287 KVWEVLLSSKApmvTVFMAVPTIYSKLIQHYEQHFTqprvqdfvraackerIRLMVSGSSALPQPTLLRWEEITGHT-LL 365
Cdd:cd17633 79 SWIRKINQYNA---TVIYLVPTMLQALARTLEPESK---------------IKSIFSSGQKLFESTKKKLKNIFPKAnLI 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 366 ERYGMTEIGMALSNPLKGPRIPGAVGVPLPGVEVRIvmTNATSttiaegnsretqvrpgleGKEGELMVRGDQVFTEYwn 445
Cdd:cd17633 141 EFYGTSELSFITYNFNQESRPPNSVGRPFPNVEIEI--RNADG------------------GEIGKIFVKSEMVFSGY-- 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 446 kpeATRESFTEDGWFKTGDTAVYK-NGVYWIMGRTSvDIIKSGGYKISALEVERHLLAHPDITDVAVIGARDATWGQKVT 524
Cdd:cd17633 199 ---VRGGFSNPDGWMSVGDIGYVDeEGYLYLVGRES-DMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAV 274
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1367478878 525 AVVQlkrGRSMTLSELKTWAREHMAPYTIPTGLVLVEEMPRNQMGKV 571
Cdd:cd17633 275 ALYS---GDKLTYKQLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKI 318
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
64-576 |
1.43e-41 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 157.87 E-value: 1.43e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 64 YRDKLAIVDDSGSHSYRDLYGSSRGLAGRIKAaldcpSGDLQGKRISFLCANDASYTVAQWASWMCGGTAV---PLYreh 140
Cdd:PRK07059 36 YADRPAFICMGKAITYGELDELSRALAAWLQS-----RGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVnvnPLY--- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 141 PPSELEYIISDSQSSLLVAGQPYADTME------PLAH--------RLGL----------------PYLQLPPTSSLSSL 190
Cdd:PRK07059 108 TPRELEHQLKDSGAEAIVVLENFATTVQqvlaktAVKHvvvasmgdLLGFkghivnfvvrrvkkmvPAWSLPGHVRFNDA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 191 LEAPENQ----PEPGITDwaqrPAMIIYTSGTTGRPKGVLHTHSNIQAMVqgLVSEwGW--------SRDD--VILHTLP 256
Cdd:PRK07059 188 LAEGARQtfkpVKLGPDD----VAFLQYTGGTTGVSKGATLLHRNIVANV--LQME-AWlqpafekkPRPDqlNFVCALP 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 257 LHHVHGI-VNKLLcPLWVGATTVMLPtfQPQKVWEVLLSSKAPMVTVFMAVPTIYSKLIQHYEqhFTQprvQDFvraack 335
Cdd:PRK07059 261 LYHIFALtVCGLL-GMRTGGRNILIP--NPRDIPGFIKELKKYQVHIFPAVNTLYNALLNNPD--FDK---LDF------ 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 336 ERIRLMVSGSSALPQPTLLRWEEITGHTLLERYGMTEIG-MALSNPLKGPRIPGAVGVPLPGVEVRIvmtnatstTIAEG 414
Cdd:PRK07059 327 SKLIVANGGGMAVQRPVAERWLEMTGCPITEGYGLSETSpVATCNPVDATEFSGTIGLPLPSTEVSI--------RDDDG 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 415 NSRETqvrpgleGKEGELMVRGDQVFTEYWNKPEATRESFTEDGWFKTGDTAVY-KNGVYWIMGRTSvDIIKSGGYKISA 493
Cdd:PRK07059 399 NDLPL-------GEPGEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMdERGYTKIVDRKK-DMILVSGFNVYP 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 494 LEVERHLLAHPDITDVAVIGARDATWGQKVTAVVqLKRGRSMTLSELKTWAREHMAPYTIPTGLVLVEEMPRNQMGKVNK 573
Cdd:PRK07059 471 NEIEEVVASHPGVLEVAAVGVPDEHSGEAVKLFV-VKKDPALTEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILR 549
|
...
gi 1367478878 574 KDL 576
Cdd:PRK07059 550 REL 552
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
55-576 |
1.78e-41 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 157.73 E-value: 1.78e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 55 APVFSRAQV-YRDKLAIVDDSGSHSYRDLYGSSRGLAGRIKAALDCPSGDlqgkRISFLCANDASYTVAQWASWMCGGTA 133
Cdd:PRK08751 28 AEVFATSVAkFADRPAYHSFGKTITYREADQLVEQFAAYLLGELQLKKGD----RVALMMPNCLQYPIATFGVLRAGLTV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 134 V---PLYrehPPSELEYIISDSQSSLLVAGQPYADTMEP--------------LAHRLGLP----------YLQ-LPPTS 185
Cdd:PRK08751 104 VnvnPLY---TPRELKHQLIDSGASVLVVIDNFGTTVQQviadtpvkqvittgLGDMLGFPkaalvnfvvkYVKkLVPEY 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 186 SLSSLLEAPE------NQPEPGITDWAQRPAMIIYTSGTTGRPKGVLHTHSNIQAMVQGlVSEWGWSRD------DVILH 253
Cdd:PRK08751 181 RINGAIRFREalalgrKHSMPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQ-AHQWLAGTGkleegcEVVIT 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 254 TLPLHHVHGIVNKLLCPLWVGATTVML--PTFQPQKVWEVllssKAPMVTVFMAVPTIYSKLIQhyEQHFTQprvQDFvr 331
Cdd:PRK08751 260 ALPLYHIFALTANGLVFMKIGGCNHLIsnPRDMPGFVKEL----KKTRFTAFTGVNTLFNGLLN--TPGFDQ---IDF-- 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 332 aackERIRLMVSGSSALPQPTLLRWEEITGHTLLERYGMTEIG-MALSNPLKGPRIPGAVGVPLPGVEVRIVMTNATSTT 410
Cdd:PRK08751 329 ----SSLKMTLGGGMAVQRSVAERWKQVTGLTLVEAYGLTETSpAACINPLTLKEYNGSIGLPIPSTDACIKDDAGTVLA 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 411 IaegnsretqvrpgleGKEGELMVRGDQVFTEYWNKPEATRESFTEDGWFKTGDTA-VYKNGVYWIMGRTSvDIIKSGGY 489
Cdd:PRK08751 405 I---------------GEIGELCIKGPQVMKGYWKRPEETAKVMDADGWLHTGDIArMDEQGFVYIVDRKK-DMILVSGF 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 490 KISALEVERHLLAHPDITDVAVIGARDATWGQKVTAVVqLKRGRSMTLSELKTWAREHMAPYTIPTGLVLVEEMPRNQMG 569
Cdd:PRK08751 469 NVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEIVKVVI-VKKDPALTAEDVKAHARANLTGYKQPRIIEFRKELPKTNVG 547
|
....*..
gi 1367478878 570 KVNKKDL 576
Cdd:PRK08751 548 KILRREL 554
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
61-576 |
4.29e-41 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 156.07 E-value: 4.29e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 61 AQVYRDKLAIVDDSGSHSYRDLYGSSRGLAgriKAALDCPSGdlQGKRISFLCANDASYTVAQWASWMCGGTAVPLYREH 140
Cdd:PRK13382 53 AQRCPDRPGLIDELGTLTWRELDERSDALA---AALQALPIG--EPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSF 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 141 PPSELEYIISDSQSSLLVAGQPYADTME------PLAHRLgLPYLQLPPTSSLSSLLEAPENQ-PEPGitdwAQRPAMII 213
Cdd:PRK13382 128 AGPALAEVVTREGVDTVIYDEEFSATVDraladcPQATRI-VAWTDEDHDLTVEVLIAAHAGQrPEPT----GRKGRVIL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 214 YTSGTTGRPKGVLHTHSNIQAMVQGLVSEWGWSRDDVILHTLPLHHVHGIVNkLLCPLWVGATTVMLPTFQPQKVWEVLL 293
Cdd:PRK13382 203 LTSGTTGTPKGARRSGPGGIGTLKAILDRTPWRAEEPTVIVAPMFHAWGFSQ-LVLAASLACTIVTRRRFDPEATLDLID 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 294 SSKApmvTVFMAVPTIYSKLIQhyeqhftqprVQDFVRAACKER-IRLMVSGSSALPQPTLLRWEEITGHTLLERYGMTE 372
Cdd:PRK13382 282 RHRA---TGLAVVPVMFDRIMD----------LPAEVRNRYSGRsLRFAAASGSRMRPDVVIAFMDQFGDVIYNNYNATE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 373 IGM-ALSNPLKGPRIPGAVGVPLPGVEVRIVmtnatsttiaEGNSRETQvrpglEGKEGELMVRGDQVFTEYwnKPEATR 451
Cdd:PRK13382 349 AGMiATATPADLRAAPDTAGRPAEGTEIRIL----------DQDFREVP-----TGEVGTIFVRNDTQFDGY--TSGSTK 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 452 EsfTEDGWFKTGDTAVY-KNGVYWIMGRtSVDIIKSGGYKISALEVERHLLAHPDITDVAVIGARDATWGQKVTAVVQLK 530
Cdd:PRK13382 412 D--FHDGFMASGDVGYLdENGRLFVVGR-DDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLK 488
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1367478878 531 RGRSMTLSELKTWAREHMAPYTIPTGLVLVEEMPRNQMGKVNKKDL 576
Cdd:PRK13382 489 PGASATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRREL 534
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
207-578 |
9.95e-41 |
|
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: 154.93 E-value: 9.95e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 207 QRPAMIIYTSGTTGRPKGVLHTHSniqAMVQGLVSEWGWSRD----DVILHTLPLHHVHGIVNKLLCPLWVGATTVM--L 280
Cdd:cd05928 174 QEPMAIYFTSGTTGSPKMAEHSHS---SLGLGLKVNGRYWLDltasDIMWNTSDTGWIKSAWSSLFEPWIQGACVFVhhL 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 281 PTFQPQKVWEVLlsSKAPmVTVFMAVPTIYSKLIQhyeqhftqprvQDFVRAACKeRIRLMVSGSSALPQPTLLRWEEIT 360
Cdd:cd05928 251 PRFDPLVILKTL--SSYP-ITTFCGAPTVYRMLVQ-----------QDLSSYKFP-SLQHCVTGGEPLNPEVLEKWKAQT 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 361 GHTLLERYGMTEIGMALSNPlKGPRI-PGAVGVPLPGVEVRIVMTNatsttiaeGNsretqVRPglEGKEGELMVRGDQV 439
Cdd:cd05928 316 GLDIYEGYGQTETGLICANF-KGMKIkPGSMGKASPPYDVQIIDDN--------GN-----VLP--PGTEGDIGIRVKPI 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 440 -----FTEYWNKPEATRESFTEDGWFkTGDTAVY-KNGVYWIMGRtSVDIIKSGGYKISALEVERHLLAHPDITDVAVIG 513
Cdd:cd05928 380 rpfglFSGYVDNPEKTAATIRGDFYL-TGDRGIMdEDGYFWFMGR-ADDVINSSGYRIGPFEVESALIEHPAVVESAVVS 457
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 514 ARDATWGQKVTAVVQL-----KRGRSMTLSELKTWAREHMAPYTIPTGLVLVEEMPRNQMGKVNKKDLLK 578
Cdd:cd05928 458 SPDPIRGEVVKAFVVLapqflSHDPEQLTKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNELRD 527
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
78-513 |
9.95e-41 |
|
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: 154.05 E-value: 9.95e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 78 SYRDLYGSSRGLAGRIKAAldcpsGDLQGKRISFLCANDASYTVAQWASWMCGGTAVPLYREHPPSELEYIISDSQSSLL 157
Cdd:cd17640 7 TYKDLYQEILDFAAGLRSL-----GVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 158 VAgqpyadtmeplahrlglpylqlpptsslsslleapENQPEpgitdwaqRPAMIIYTSGTTGRPKGVLHTHSN------ 231
Cdd:cd17640 82 VV-----------------------------------ENDSD--------DLATIIYTSGTTGNPKGVMLTHANllhqir 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 232 -IQAMVQGLVSewgwsrdDVILHTLPLHHVHGIVNKLLCPLWVGA---TTVM-----LPTFQPQkvwevllsskapmvtV 302
Cdd:cd17640 119 sLSDIVPPQPG-------DRFLSILPIWHSYERSAEYFIFACGCSqayTSIRtlkddLKRVKPH---------------Y 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 303 FMAVPTIYSKLIQH-YEQHFTQPRVQDFVRAACK--ERIRLMVSGSSALPqPTLLRWEEITGHTLLERYGMTEIGMALS- 378
Cdd:cd17640 177 IVSVPRLWESLYSGiQKQVSKSSPIKQFLFLFFLsgGIFKFGISGGGALP-PHVDTFFEAIGIEVLNGYGLTETSPVVSa 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 379 NPLKGPrIPGAVGVPLPGVEVRIVmtnatsttiaEGNSRETqVRPgleGKEGELMVRGDQVFTEYWNKPEATRESFTEDG 458
Cdd:cd17640 256 RRLKCN-VRGSVGRPLPGTEIKIV----------DPEGNVV-LPP---GEKGIVWVRGPQVMKGYYKNPEATSKVLDSDG 320
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1367478878 459 WFKTGDTA-VYKNGVYWIMGRTSVDIIKSGGYKISALEVERHLLAHPDITDVAVIG 513
Cdd:cd17640 321 WFNTGDLGwLTCGGELVLTGRAKDTIVLSNGENVEPQPIEEALMRSPFIEQIMVVG 376
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
187-579 |
1.87e-40 |
|
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: 154.58 E-value: 1.87e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 187 LSSLLEAPENQPEPGITDwaqrPAMIIYTSGTTGRPKGVLHTHSN-----IQAMV------QGL---VSEWGWSRddvil 252
Cdd:cd05970 169 ASPDFERPTANSYPCGED----ILLVYFSSGTTGMPKMVEHDFTYplghiVTAKYwqnvreGGLhltVADTGWGK----- 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 253 htlplhhvhGIVNKLLCPlWVGATTVML---PTFQPQKVWEVLLSSKapmVTVFMAVPTIYSKLIQHYEQHFtqprvqDF 329
Cdd:cd05970 240 ---------AVWGKIYGQ-WIAGAAVFVydyDKFDPKALLEKLSKYG---VTTFCAPPTIYRFLIREDLSRY------DL 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 330 vraackERIRLMVSGSSALPQPTLLRWEEITGHTLLERYGMTEIGMALSN-PLKGPRiPGAVGVPLPGVEVRIVMTnats 408
Cdd:cd05970 301 ------SSLRYCTTAGEALNPEVFNTFKEKTGIKLMEGFGQTETTLTIATfPWMEPK-PGSMGKPAPGYEIDLIDR---- 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 409 ttiaEGNSRETqvrpgleGKEGELMVRGDQ-----VFTEYWNKPEATRESFtEDGWFKTGDTA-VYKNGVYWIMGRTSvD 482
Cdd:cd05970 370 ----EGRSCEA-------GEEGEIVIRTSKgkpvgLFGGYYKDAEKTAEVW-HDGYYHTGDAAwMDEDGYLWFVGRTD-D 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 483 IIKSGGYKISALEVERHLLAHPDITDVAVIGARDATWGQKVTAVVQLKRGRSMTLS---ELKTWAREHMAPYTIPTGLVL 559
Cdd:cd05970 437 LIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIVLAKGYEPSEElkkELQDHVKKVTAPYKYPRIVEF 516
|
410 420
....*....|....*....|
gi 1367478878 560 VEEMPRNQMGKVNKKDLLKH 579
Cdd:cd05970 517 VDELPKTISGKIRRVEIRER 536
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
209-576 |
2.29e-40 |
|
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: 153.26 E-value: 2.29e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 209 PAMIIYTSGTTGRPKGVLHTHSNIQAMVQGLVSEWGWSRDDVILHTLPLHHVHGIVNKLLCPLWVGATTVMLPT-FQPQK 287
Cdd:cd05909 149 PAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPFFHSFGLTGCLWLPLLSGIKVVFHPNpLDYKK 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 288 VWEVLLSSKApmvTVFMAVPTIYSKliqhyeqhftqprvqdFVRAACKE---RIRLMVSGSSALPQPTLLRWEEITGHTL 364
Cdd:cd05909 229 IPELIYDKKA---TILLGTPTFLRG----------------YARAAHPEdfsSLRLVVAGAEKLKDTLRQEFQEKFGIRI 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 365 LERYGMTEIGMALS-NPLKGPRIPGAVGVPLPGVEVRIVmtnatsttiaegnSRETQVrPGLEGKEGELMVRGDQVFTEY 443
Cdd:cd05909 290 LEGYGTTECSPVISvNTPQSPNKEGTVGRPLPGMEVKIV-------------SVETHE-EVPIGEGGLLLVRGPNVMLGY 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 444 WNKPEATRESFtEDGWFKTGDTA-VYKNGVYWIMGRTSvDIIKSGGYKISALEVERHLLAH-PDITDVAVIGARDATWGQ 521
Cdd:cd05909 356 LNEPELTSFAF-GDGWYDTGDIGkIDGEGFLTITGRLS-RFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVPDGRKGE 433
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1367478878 522 KVTAVVQLKrgrSMTLSELKTWAREHMAP-YTIPTGLVLVEEMPRNQMGKVNKKDL 576
Cdd:cd05909 434 KIVLLTTTT---DTDPSSLNDILKNAGISnLAKPSYIHQVEEIPLLGTGKPDYVTL 486
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
209-565 |
7.23e-40 |
|
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: 148.22 E-value: 7.23e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 209 PAMIIYTSGTTGRPKGVLHTHSNIqaMVQGLVSEWG--WSRDDVILHTLPLHHVhGIVNKLLCPLWVGATTVMLPTFQPQ 286
Cdd:cd17636 2 PVLAIYTAAFSGRPNGALLSHQAL--LAQALVLAVLqaIDEGTVFLNSGPLFHI-GTLMFTLATFHAGGTNVFVRRVDAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 287 KVWEVLLSSKApmVTVFMAVPTIyskliqhyeqhftqprvqDFVRAACKERIRLMvsgSSALPQPTLLRWEEI--TGHTL 364
Cdd:cd17636 79 EVLELIEAERC--THAFLLPPTI------------------DQIVELNADGLYDL---SSLRSSPAAPEWNDMatVDTSP 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 365 LER----YGMTEI-GMALSNPLKGPRIPGAvGVPLPGVEVRIVMTnatsttiaEGNsretQVRPGlegKEGELMVRGDQV 439
Cdd:cd17636 136 WGRkpggYGQTEVmGLATFAALGGGAIGGA-GRPSPLVQVRILDE--------DGR----EVPDG---EVGEIVARGPTV 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 440 FTEYWNKPEATRESFTeDGWFKTGDtavykngvywiMGRTSVD-----------IIKSGGYKISALEVERHLLAHPDITD 508
Cdd:cd17636 200 MAGYWNRPEVNARRTR-GGWHHTND-----------LGRREPDgslsfvgpktrMIKSGAENIYPAEVERCLRQHPAVAD 267
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1367478878 509 VAVIGARDATWGQKVTAVVQLKRGRSMTLSELKTWAREHMAPYTIPTGLVLVEEMPR 565
Cdd:cd17636 268 AAVIGVPDPRWAQSVKAIVVLKPGASVTEAELIEHCRARIASYKKPKSVEFADALPR 324
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
209-573 |
1.10e-39 |
|
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: 148.18 E-value: 1.10e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 209 PAMIIYTSGTTGRPKGVLHTHSNIQAMVQGLVSE-WGWSRDDVILHTLPLHHVHGIVNKLLCPLWVGATTVMLPTFQPQK 287
Cdd:cd17635 3 PLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEgLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGENTTYKS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 288 VWEVLLSSKapmVTVFMAVPTIYSKLIQHYEQhftqprvqdfVRAACkERIRLMVSGSSaLPQPTLLRWEEITGHT-LLE 366
Cdd:cd17635 83 LFKILTTNA---VTTTCLVPTLLSKLVSELKS----------ANATV-PSLRLIGYGGS-RAIAADVRFIEATGLTnTAQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 367 RYGMTEIGMALSNPL-KGPRIPGAVGVPLPGVEVRIVMTNATSttiaegnsretqvrpGLEGKEGELMVRGDQVFTEYWN 445
Cdd:cd17635 148 VYGLSETGTALCLPTdDDSIEINAVGRPYPGVDVYLAATDGIA---------------GPSASFGTIWIKSPANMLGYWN 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 446 KPEATRESFTeDGWFKTGDTA-VYKNGVYWIMGRTSVDIIKsGGYKISALEVERHLLAHPDITDVAVIGARDATWGqkvt 524
Cdd:cd17635 213 NPERTAEVLI-DGWVNTGDLGeRREDGFLFITGRSSESINC-GGVKIAPDEVERIAEGVSGVQECACYEISDEEFG---- 286
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1367478878 525 AVVQLKRGRSMTLSE-----LKTWAREHMAPYTIPTGLVLVEEMPRNQMGKVNK 573
Cdd:cd17635 287 ELVGLAVVASAELDEnairaLKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
210-551 |
1.10e-38 |
|
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: 148.90 E-value: 1.10e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 210 AMIIYTSGTTGRPKGVLHTHSNIQAMVQGL---VSEWgWSRDDVILHTLPLHHVHGIVNKLLCPLW---VGATTVM---- 279
Cdd:cd17639 91 ACIMYTSGSTGNPKGVMLTHGNLVAGIAGLgdrVPEL-LGPDDRYLAYLPLAHIFELAAENVCLYRggtIGYGSPRtltd 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 280 ---------LPTFQPQ------KVWE-----VL--LSSKAPMV-TVFMavpTIYS---KLIQH-YEQHFTQPRVQDFVRA 332
Cdd:cd17639 170 kskrgckgdLTEFKPTlmvgvpAIWDtirkgVLakLNPMGGLKrTLFW---TAYQsklKALKEgPGTPLLDELVFKKVRA 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 333 ACKERIRLMVSGSSALPQPTLlRWEEITGHTLLERYGMTEI--GMALSNPlkGPRIPGAVGVPLPGVEVRIVmtnatstT 410
Cdd:cd17639 247 ALGGRLRYMLSGGAPLSADTQ-EFLNIVLCPVIQGYGLTETcaGGTVQDP--GDLETGRVGPPLPCCEIKLV-------D 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 411 IAEGNSRETQVRPglegkEGELMVRGDQVFTEYWNKPEATRESFTEDGWFKTGDTA-VYKNGVYWIMGRTSvDIIKS--G 487
Cdd:cd17639 317 WEEGGYSTDKPPP-----RGEILIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGeFHPDGTLKIIDRKK-DLVKLqnG 390
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1367478878 488 GYkiSALE-VERHLLAHPDITDVAVIGARDATwgqKVTAVVQLKRGRsmtlseLKTWAREHMAPY 551
Cdd:cd17639 391 EY--IALEkLESIYRSNPLVNNICVYADPDKS---YPVAIVVPNEKH------LTKLAEKHGVIN 444
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
210-576 |
1.49e-37 |
|
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: 146.13 E-value: 1.49e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 210 AMIIYTSGTTGRPKGVLHTHSNI--------QAMVQGLVSEwgwsrDDVILHTLPLHHVHGIVNkLLCPLWVGATTVMLP 281
Cdd:cd17642 187 ALIMNSSGSTGLPKGVQLTHKNIvarfsharDPIFGNQIIP-----DTAILTVIPFHHGFGMFT-TLGYLICGFRVVLMY 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 282 TFQPqkvwEVLLSS--KAPMVTVFMaVPTIYSKLIQHyeqhftqPRVQDFVRAACKErirlMVSGSSALPQPTllrweei 359
Cdd:cd17642 261 KFEE----ELFLRSlqDYKVQSALL-VPTLFAFFAKS-------TLVDKYDLSNLHE----IASGGAPLSKEV------- 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 360 tGHTLLER---------YGMTEIGMALSNPLKGPRIPGAVGVPLPGVEVRIVmtNATSTTIAEGNSRetqvrpglegkeG 430
Cdd:cd17642 318 -GEAVAKRfklpgirqgYGLTETTSAILITPEGDDKPGAVGKVVPFFYAKVV--DLDTGKTLGPNER------------G 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 431 ELMVRGDQVFTEYWNKPEATRESFTEDGWFKTGDTAVY-KNGVYWIMGRTSvDIIKSGGYKISALEVERHLLAHPDITDV 509
Cdd:cd17642 383 ELCVKGPMIMKGYVNNPEATKALIDKDGWLHSGDIAYYdEDGHFFIVDRLK-SLIKYKGYQVPPAELESILLQHPKIFDA 461
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1367478878 510 AVIGARDATWGQKVTAVVQLKRGRSMTLSELKTWAREHMAPYT-IPTGLVLVEEMPRNQMGKVNKKDL 576
Cdd:cd17642 462 GVAGIPDEDAGELPAAVVVLEAGKTMTEKEVMDYVASQVSTAKrLRGGVKFVDEVPKGLTGKIDRRKI 529
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
210-580 |
1.52e-37 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 146.05 E-value: 1.52e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 210 AMIIYTSGTTGRPKGVLHTH-SNI-QAMVQGLVSEWGWSRDDVILHTLPLHHVHGIVNKLLCPLwVGATTVML-PTFQPQ 286
Cdd:PRK06018 180 AGMCYTSGTTGDPKGVLYSHrSNVlHALMANNGDALGTSAADTMLPVVPLFHANSWGIAFSAPS-MGTKLVMPgAKLDGA 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 287 KVWEVLLSSKapmVTVFMAVPTIYSKLIQHYEQH-FTQPRvqdfvraackerIRLMVSGSSALPQPTLLRWEEItGHTLL 365
Cdd:PRK06018 259 SVYELLDTEK---VTFTAGVPTVWLMLLQYMEKEgLKLPH------------LKMVVCGGSAMPRSMIKAFEDM-GVEVR 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 366 ERYGMTEIG-MALSNPLKGP--RIPGAV--------GVPLPGVEVRIvmtnatstTIAEGNSRETqvrpglEGKE-GELM 433
Cdd:PRK06018 323 HAWGMTEMSpLGTLAALKPPfsKLPGDArldvlqkqGYPPFGVEMKI--------TDDAGKELPW------DGKTfGRLK 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 434 VRGDQVFTEYWnkpEATRESFTEDGWFKTGDTAVYKNGVYWIMGRTSVDIIKSGGYKISALEVERHLLAHPDITDVAVIG 513
Cdd:PRK06018 389 VRGPAVAAAYY---RVDGEILDDDGFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIG 465
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1367478878 514 ARDATWGQKVTAVVQLKRGRSMTLSELKTWAREHMAPYTIPTGLVLVEEMPRNQMGKVNKKDLLKHF 580
Cdd:PRK06018 466 VYHPKWDERPLLIVQLKPGETATREEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALREQF 532
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
130-576 |
2.10e-37 |
|
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: 144.78 E-value: 2.10e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 130 GGTAVPLYREHPPSELEYIISDSQSSLLVAGQPYAdtmEPLAHRLGLPYLQLPPTSSLSSLLEAPENQPepgitdwaQRP 209
Cdd:cd17655 71 GGAYLPIDPDYPEERIQYILEDSGADILLTQSHLQ---PPIAFIGLIDLLDEDTIYHEESENLEPVSKS--------DDL 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 210 AMIIYTSGTTGRPKGVLHTHSNIQAMVQGLVSEWGWSRDDVILHTLPLH---HVHGIVNKLLCplwvGATTVMLPTFQPQ 286
Cdd:cd17655 140 AYVIYTSGSTGKPKGVMIEHRGVVNLVEWANKVIYQGEHLRVALFASISfdaSVTEIFASLLS----GNTLYIVRKETVL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 287 KVWEVLLSSKAPMVTVFMAVPTiYSKLIQhYEQHFTQPrvqdfvraackeRIRLMVSGSSALPQPTLLRWEEITGH--TL 364
Cdd:cd17655 216 DGQALTQYIRQNRITIIDLTPA-HLKLLD-AADDSEGL------------SLKHLIVGGEALSTELAKKIIELFGTnpTI 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 365 LERYGMTE------IGMALSNPLKGPRIPgaVGVPLPGVEVRIVmtnatsttiaegnsrETQVRPGLEGKEGELMVRGDQ 438
Cdd:cd17655 282 TNAYGPTEttvdasIYQYEPETDQQVSVP--IGKPLGNTRIYIL---------------DQYGRPQPVGVAGELYIGGEG 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 439 VFTEYWNKPEATRESFTEDGW------FKTGDTAVY-KNGVYWIMGRTSvDIIKSGGYKISALEVERHLLAHPDITDVAV 511
Cdd:cd17655 345 VARGYLNRPELTAEKFVDDPFvpgermYRTGDLARWlPDGNIEFLGRID-HQVKIRGYRIELGEIEARLLQHPDIKEAVV 423
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1367478878 512 IGARDATWGQKVTAVVQLKrgRSMTLSELKTWAREHMAPYTIPTGLVLVEEMPRNQMGKVNKKDL 576
Cdd:cd17655 424 IARKDEQGQNYLCAYIVSE--KELPVAQLREFLARELPDYMIPSYFIKLDEIPLTPNGKVDRKAL 486
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
77-577 |
1.10e-36 |
|
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: 142.52 E-value: 1.10e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 77 HSYRDLYGSSRGLAGRIKAALDCPSGdlQGKRISFLCANDASYTVAQWASWMCGGTAVPLYREHPPSELEYIIsdsqssl 156
Cdd:cd05929 15 RRLLLLDVYSIALNRNARAAAAEGVW--IADGVYIYLINSILTVFAAAAAWKCGACPAYKSSRAPRAEACAII------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 157 lvagQPYADTMEPLAHRLGlpylqlPPTSSLSSLLEAPENQPEPGITDWAqRPAMIIYTSGTTGRPKGVLHTHSNIQAMV 236
Cdd:cd05929 86 ----EIKAAALVCGLFTGG------GALDGLEDYEAAEGGSPETPIEDEA-AGWKMLYSGGTTGRPKGIKRGLPGGPPDN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 237 QGLVS---EWGWSRDDVILHTLPLHHVHGIVNKLLCpLWVGATTVMLPTFQPQkvwEVLLSSKAPMVTVFMAVPTIYSKL 313
Cdd:cd05929 155 DTLMAaalGFGPGADSVYLSPAPLYHAAPFRWSMTA-LFMGGTLVLMEKFDPE---EFLRLIERYRVTFAQFVPTMFVRL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 314 IQHYEQhftQPRVQDF--VRAACKerirlmvsgsSALPQPTLL--RWEEITGHTLLERYGMTE-IGMALSNPLKGPRIPG 388
Cdd:cd05929 231 LKLPEA---VRNAYDLssLKRVIH----------AAAPCPPWVkeQWIDWGGPIIWEYYGGTEgQGLTIINGEEWLTHPG 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 389 AVGVPLPGvEVRIVmtnatsttiaEGNSREtqVRPGlegKEGELMVRGDQVFtEYWNKPEATRESFTEDGWFKTGDTA-V 467
Cdd:cd05929 298 SVGRAVLG-KVHIL----------DEDGNE--VPPG---EIGEVYFANGPGF-EYTNDPEKTAAARNEGGWSTLGDVGyL 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 468 YKNGVYWIMGRTSvDIIKSGGYKISALEVERHLLAHPDITDVAVIGARDATWGQKVTAVVQ---LKRGRSMTLSELKTWA 544
Cdd:cd05929 361 DEDGYLYLTDRRS-DMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVQpapGADAGTALAEELIAFL 439
|
490 500 510
....*....|....*....|....*....|...
gi 1367478878 545 REHMAPYTIPTGLVLVEEMPRNQMGKVNKKDLL 577
Cdd:cd05929 440 RDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLR 472
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
66-573 |
4.18e-36 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 142.19 E-value: 4.18e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 66 DKLAIVDDSGSHSYRDLygssRGLAGRIKAALDcPSGDLQGKRISFLCANDASYTVAQWASWMCGGTAVPL---YREHpp 142
Cdd:PRK06164 25 DAVALIDEDRPLSRAEL----RALVDRLAAWLA-AQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVntrYRSH-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 143 sELEYIISDSQSSLLVagqpYADTME--PLAHRL-GLPYLQLPPTSSLSSLLEAPENQPEPGITDWAQ------------ 207
Cdd:PRK06164 98 -EVAHILGRGRARWLV----VWPGFKgiDFAAILaAVPPDALPPLRAIAVVDDAADATPAPAPGARVQlfalpdpappaa 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 208 ---------RPAMIIYTSGTTGRPKGVLHTHSNIQAMVQGLVSEWGWSRDDVILHTLPLHHVHGIvNKLLCPLWVGATTV 278
Cdd:PRK06164 173 ageraadpdAGALLFTTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFGF-STLLGALAGGAPLV 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 279 MLPTFQPQKVWEVLLSSKapmVTVFMAVPTIYSKLIQhyeqhfTQPRVQDFVRAackeriRLMVSGSSALPQPTLLRWEE 358
Cdd:PRK06164 252 CEPVFDAARTARALRRHR---VTHTFGNDEMLRRILD------TAGERADFPSA------RLFGFASFAPALGELAALAR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 359 ITGHTLLERYGMTE-IGMALSNPLKGP---RIPGAvGVPL-PGVEVRIVMTnATSTTIAEGNSretqvrpglegkeGELM 433
Cdd:PRK06164 317 ARGVPLTGLYGSSEvQALVALQPATDPvsvRIEGG-GRPAsPEARVRARDP-QDGALLPDGES-------------GEIE 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 434 VRGDQVFTEYWNKPEATRESFTEDGWFKTGDTAVYK-NGVYWIMGRTSvDIIKSGGYKISALEVERHLLAHPDITDVAVI 512
Cdd:PRK06164 382 IRAPSLMRGYLDNPDATARALTDDGYFRTGDLGYTRgDGQFVYQTRMG-DSLRLGGFLVNPAEIEHALEALPGVAAAQVV 460
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1367478878 513 GA-RDatwGQKV-TAVVQLKRGRSMTLSELKTWAREHMAPYTIPTGLVLVEEMPRNQMGKVNK 573
Cdd:PRK06164 461 GAtRD---GKTVpVAFVIPTDGASPDEAGLMAACREALAGFKVPARVQVVEAFPVTESANGAK 520
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
60-576 |
1.04e-35 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 140.60 E-value: 1.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 60 RAQVYRDKLA-IVDDSG-SHSYRDLYGSSRGLAGRIKAAldcpsGDLQGKRISFLCANDASYTVAQWASWMCGGTAVPLY 137
Cdd:PRK13391 6 HAQTTPDKPAvIMASTGeVVTYRELDERSNRLAHLFRSL-----GLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 138 REHPPSELEYIISDSQSSLLVAGQPYADTMEPLAHRL--GLPYLQLPPTSSLS---SLLEAPENQPEPGITDWAQRPAMI 212
Cdd:PRK13391 81 SHLTPAEAAYIVDDSGARALITSAAKLDVARALLKQCpgVRHRLVLDGDGELEgfvGYAEAVAGLPATPIADESLGTDML 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 213 iYTSGTTGRPKGVLH--------THSNIQAMVQGLvseWGWSRDDVILHTLPLHHVH-----GIVNKLlcplwvGATTVM 279
Cdd:PRK13391 161 -YSSGTTGRPKGIKRplpeqppdTPLPLTAFLQRL---WGFRSDMVYLSPAPLYHSApqravMLVIRL------GGTVIV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 280 LPTFQPQKVWEVLLSSKapmVTVFMAVPTIYS---KLIQHYEQHFTQPRVQDFVRAA--CKERIRlmvsgssalpqPTLL 354
Cdd:PRK13391 231 MEHFDAEQYLALIEEYG---VTHTQLVPTMFSrmlKLPEEVRDKYDLSSLEVAIHAAapCPPQVK-----------EQMI 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 355 RWeeiTGHTLLERYGMTE-IGMALSNPLKGPRIPGAVGVPLPGVeVRIvmtnatsttiaegnsRETQVRPGLEGKEGELM 433
Cdd:PRK13391 297 DW---WGPIIHEYYAATEgLGFTACDSEEWLAHPGTVGRAMFGD-LHI---------------LDDDGAELPPGEPGTIW 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 434 VRGDQVFtEYWNKPEATRESFTEDG-WFKTGDTA-VYKNGVYWIMGRTSVDIIkSGGYKISALEVERHLLAHPDITDVAV 511
Cdd:PRK13391 358 FEGGRPF-EYLNDPAKTAEARHPDGtWSTVGDIGyVDEDGYLYLTDRAAFMII-SGGVNIYPQEAENLLITHPKVADAAV 435
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1367478878 512 IGARDATWGQKVTAVVQLKRGRSMT---LSELKTWAREHMAPYTIPTGLVLVEEMPRNQMGKVNKKDL 576
Cdd:PRK13391 436 FGVPNEDLGEEVKAVVQPVDGVDPGpalAAELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLL 503
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
66-571 |
1.41e-35 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 139.53 E-value: 1.41e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 66 DKLAIVDDSGSHSYRDLYGSSRGLAGRIKAALDCPsgdlqgKRISFLCANDASYTVAQWASWMCGGTAVPLYREHPPSEL 145
Cdd:PRK07638 16 NKIAIKENDRVLTYKDWFESVCKVANWLNEKESKN------KTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 146 EYIISDSQSSLLVAGQpyadtmeplahrlglpYLQLPPTSSLSSLLEAPENQPEpgITDWAQRPAMII----------YT 215
Cdd:PRK07638 90 KERLAISNADMIVTER----------------YKLNDLPDEEGRVIEIDEWKRM--IEKYLPTYAPIEnvqnapfymgFT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 216 SGTTGRPKGVLHTHSNIQAMVQGLVSEWGWSRDDVILHTLPLHHVH---GIVNKLlcplWVGATTVMLPTFQPQKVWEVL 292
Cdd:PRK07638 152 SGSTGKPKAFLRAQQSWLHSFDCNVHDFHMKREDSVLIAGTLVHSLflyGAISTL----YVGQTVHLMRKFIPNQVLDKL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 293 lssKAPMVTVFMAVPTIYSKLIqhyeqhftqpRVQDFVraackERIRLMVSGSSALPQPTLLRWEEITGH-TLLERYGMT 371
Cdd:PRK07638 228 ---ETENISVMYTVPTMLESLY----------KENRVI-----ENKMKIISSGAKWEAEAKEKIKNIFPYaKLYEFYGAS 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 372 EIG-MALSNPLKGPRIPGAVGVPLPGVEVRIVmtnatsttiaegNSRETQVRPGLEGKegeLMVRGDQVFTEYWNKPEAT 450
Cdd:PRK07638 290 ELSfVTALVDEESERRPNSVGRPFHNVQVRIC------------NEAGEEVQKGEIGT---VYVKSPQFFMGYIIGGVLA 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 451 REsFTEDGWFKTGDTA-VYKNGVYWIMGRTSvDIIKSGGYKISALEVERHLLAHPDITDVAVIGARDATWGQKVTAVVQl 529
Cdd:PRK07638 355 RE-LNADGWMTVRDVGyEDEEGFIYIVGREK-NMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAIIK- 431
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1367478878 530 krgRSMTLSELKTWAREHMAPYTIPTGLVLVEEMPRNQMGKV 571
Cdd:PRK07638 432 ---GSATKQQLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKI 470
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
66-576 |
3.94e-35 |
|
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: 137.38 E-value: 3.94e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 66 DKLAIVDDSGSHSYRDLYGSSRGLAGRIKAAldcpsGDLQGKRISFLCANDASYTVAQWASWMCGGTAVPLYREHPPSEL 145
Cdd:cd17652 2 DAPAVVFGDETLTYAELNARANRLARLLAAR-----GVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 146 EYIISDSQSSLLVAgqpyadtmeplahrlglpylqlpptsslsslleapenQPEpgitdwaqRPAMIIYTSGTTGRPKGV 225
Cdd:cd17652 77 AYMLADARPALLLT-------------------------------------TPD--------NLAYVIYTSGSTGRPKGV 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 226 LHTHSNIQAMVQGLVSEWGWSRDDVILHTLPLHhVHGIVNKLLCPLWVGATTVMLPTfqpqkvwEVLLSSkAPMVTVfma 305
Cdd:cd17652 112 VVTHRGLANLAAAQIAAFDVGPGSRVLQFASPS-FDASVWELLMALLAGATLVLAPA-------EELLPG-EPLADL--- 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 306 vptiyskLIQHYEQHFTQ-PRVQDFVRAACKERIRLMVSGSSALPQPTLLRWEeiTGHTLLERYGMTE--IGMALSNPLK 382
Cdd:cd17652 180 -------LREHRITHVTLpPAALAALPPDDLPDLRTLVVAGEACPAELVDRWA--PGRRMINAYGPTEttVCATMAGPLP 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 383 GPRIPgAVGVPLPGVEVRIVmtnatsttiaegnsrETQVRPGLEGKEGELMVRGDQVFTEYWNKPEATRESFTEDGW--- 459
Cdd:cd17652 251 GGGVP-PIGRPVPGTRVYVL---------------DARLRPVPPGVPGELYIAGAGLARGYLNRPGLTAERFVADPFgap 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 460 ----FKTGDTAVYKN-GVYWIMGRTSvDIIKSGGYKISALEVERHLLAHPDITDVAVIGARDATWGQKVTAVVQLKRGRS 534
Cdd:cd17652 315 gsrmYRTGDLARWRAdGQLEFLGRAD-DQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAPGAA 393
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1367478878 535 MTLSELKTWAREHMAPYTIPTGLVLVEEMPRNQMGKVNKKDL 576
Cdd:cd17652 394 PTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
78-573 |
4.39e-35 |
|
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: 139.48 E-value: 4.39e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 78 SYRDLYGSSRGLAGRIKAAldcpsGDLQGKRISFLCANDASYTVAQWASWMCGGTAVPLYREHPPSELEYIISDSQSSLL 157
Cdd:cd17641 13 TWADYADRVRAFALGLLAL-----GVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 158 VAG-QPYADTMEPLAHRL------------GLPYLQLPPTSSLSSLLEAPE--NQPEPGITD---WAQRP---AMIIYTS 216
Cdd:cd17641 88 IAEdEEQVDKLLEIADRIpsvryviycdprGMRKYDDPRLISFEDVVALGRalDRRDPGLYErevAAGKGedvAVLCTTS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 217 GTTGRPKGVLHTHSNIQAMVQGLVSEWGWSRDDVILHTLPLHHVHGIVNKLLCPLWVG--------ATTVML------PT 282
Cdd:cd17641 168 GTTGKPKLAMLSHGNFLGHCAAYLAADPLGPGDEYVSVLPLPWIGEQMYSVGQALVCGfivnfpeePETMMEdlreigPT 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 283 F--QPQKVWEVLLSSkapmVTVFMA-VPTIYSKLIQHY--------EQHFTQPRVQDFVRAACK---------------- 335
Cdd:cd17641 248 FvlLPPRVWEGIAAD----VRARMMdATPFKRFMFELGmklglralDRGKRGRPVSLWLRLASWladallfrplrdrlgf 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 336 ERIRLMVSGSSALpQPTLLRWEEITGHTLLERYGMTEIGMALSNPLKGPRIPGAVGVPLPGVEVRIVmtnatsttiaegn 415
Cdd:cd17641 324 SRLRSAATGGAAL-GPDTFRFFHAIGVPLKQLYGQTELAGAYTVHRDGDVDPDTVGVPFPGTEVRID------------- 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 416 sretqvrpglegKEGELMVRGDQVFTEYWNKPEATRESFTEDGWFKTGDTAVYK-NGVYWIMGRTSvDIIK-SGGYKISA 493
Cdd:cd17641 390 ------------EVGEILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKeNGHLVVIDRAK-DVGTtSDGTRFSP 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 494 LEVERHLLAHPDITDVAVIGARDatwgQKVTAVVQLKrgrsmtLSELKTWAREHMAPYTIPTGLVL---VEEMPRNQMGK 570
Cdd:cd17641 457 QFIENKLKFSPYIAEAVVLGAGR----PYLTAFICID------YAIVGKWAEQRGIAFTTYTDLASrpeVYELIRKEVEK 526
|
...
gi 1367478878 571 VNK 573
Cdd:cd17641 527 VNA 529
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
66-576 |
7.17e-35 |
|
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: 137.40 E-value: 7.17e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 66 DKLAIVDDSGSHSYRDLYGSSRGLAGRIKAAldcpsGDLQGKRISFLCANDASYTVAQWASWMCGGTAVPLYREHPPSEL 145
Cdd:cd12114 2 DATAVICGDGTLTYGELAERARRVAGALKAA-----GVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 146 EYIISDSQSSLLVAGQPYADTMEPLahrlglpylqlPPTSSLSSLLEAPENQPEPGITDwAQRPAMIIYTSGTTGRPKGV 225
Cdd:cd12114 77 EAILADAGARLVLTDGPDAQLDVAV-----------FDVLILDLDALAAPAPPPPVDVA-PDDLAYVIFTSGSTGTPKGV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 226 LHTHSNIQAMVQGLVSEWGWSRDDVILHTLPLHH---VHGIVNkllcPLWVGATTVMLPTFQPQKV--WEVLLSSKApmV 300
Cdd:cd12114 145 MISHRAALNTILDINRRFAVGPDDRVLALSSLSFdlsVYDIFG----ALSAGATLVLPDEARRRDPahWAELIERHG--V 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 301 TVFMAVPTIYSKLIQHYEQHFTQPRVQdfvRAAckerirlMVSGS-SALPQPTLLR--WEEITGHTLlerYGMTEiGMAL 377
Cdd:cd12114 219 TLWNSVPALLEMLLDVLEAAQALLPSL---RLV-------LLSGDwIPLDLPARLRalAPDARLISL---GGATE-ASIW 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 378 SN--PL-KGPRIPGAV--GVPLPGVEVRIVmtnatsttiaegnsrETQVRPGLEGKEGELMVRGDQVFTEYWNKPEATRE 452
Cdd:cd12114 285 SIyhPIdEVPPDWRSIpyGRPLANQRYRVL---------------DPRGRDCPDWVPGELWIGGRGVALGYLGDPELTAA 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 453 SFTEDG----WFKTGDTAVYK-NGVYWIMGRtsVDI-IKSGGYKISALEVERHLLAHPDITDVAVIGARDATWGQKVTAV 526
Cdd:cd12114 350 RFVTHPdgerLYRTGDLGRYRpDGTLEFLGR--RDGqVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDPGGKRLAAFV 427
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1367478878 527 VQLKRGRSMTLSELKTWAREHMAPYTIPTGLVLVEEMPRNQMGKVNKKDL 576
Cdd:cd12114 428 VPDNDGTPIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
47-576 |
7.65e-35 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 138.21 E-value: 7.65e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 47 RQAAAGDS---APVFSRAQVYRDKLAIVDDSGSHSYRDLYGSSRGLAGRIKAALDCPsgdlqGKRISFLCANDASYTVAQ 123
Cdd:PRK13383 28 REASRGGTnpyTLLAVTAARWPGRTAIIDDDGALSYRELQRATESLARRLTRDGVAP-----GRAVGVMCRNGRGFVTAV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 124 WASWMCGGTAVPLYREHPPSELEYIISDSQSSLLVAGQPYADTMEPLahrlGLPYLQLPPTSSlssllEAPENQPEPGIt 203
Cdd:PRK13383 103 FAVGLLGADVVPISTEFRSDALAAALRAHHISTVVADNEFAERIAGA----DDAVAVIDPATA-----GAEESGGRPAV- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 204 dwAQRPAMIIYTSGTTGRPKGVLHthsniQAMVQGLVSEWGWSRDDVILHT-------LPLHHVHGIvNKLLCPLWVGAT 276
Cdd:PRK13383 173 --AAPGRIVLLTSGTTGKPKGVPR-----APQLRSAVGVWVTILDRTRLRTgsrisvaMPMFHGLGL-GMLMLTIALGGT 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 277 TVMLPTFQPQKVwevLLSSKAPMVTVFMAVPTIYSKLIQhyeqhfTQPRVQDFVRAACkerIRLMVSGSSALpQPTL-LR 355
Cdd:PRK13383 245 VLTHRHFDAEAA---LAQASLHRADAFTAVPVVLARILE------LPPRVRARNPLPQ---LRVVMSSGDRL-DPTLgQR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 356 WEEITGHTLLERYGMTEIGM-ALSNPLKGPRIPGAVGVPLPGVEVRIVMTNAtsttiaegnsretqvRPGLEGKEGELMV 434
Cdd:PRK13383 312 FMDTYGDILYNGYGSTEVGIgALATPADLRDAPETVGKPVAGCPVRILDRNN---------------RPVGPRVTGRIFV 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 435 RGDQVFTEYWNKPEATresfTEDGWFKTGDTAVYKN-GVYWIMGRTSvDIIKSGGYKISALEVERHLLAHPDITDVAVIG 513
Cdd:PRK13383 377 GGELAGTRYTDGGGKA----VVDGMTSTGDMGYLDNaGRLFIVGRED-DMIISGGENVYPRAVENALAAHPAVADNAVIG 451
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1367478878 514 ARDATWGQKVTAVVQLKRGRSMTLSELKTWAREHMAPYTIPTGLVLVEEMPRNQMGKVNKKDL 576
Cdd:PRK13383 452 VPDERFGHRLAAFVVLHPGSGVDAAQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
106-580 |
8.28e-35 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 138.76 E-value: 8.28e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 106 GKRISFLCANDASYTVAQWASWMCGGTAVPLYREHPPSELEYIISDSQSSLLVAGQPYADTMEPLAHR------------ 173
Cdd:PRK05620 64 DQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIVADPRLAEQLGEILKEcpcvravvfigp 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 174 --LGLPYLQLPP---TSSLSSLLEApenqpEPGITDWAQ----RPAMIIYTSGTTGRPKGVLHTHSN--IQAMVQGLVSE 242
Cdd:PRK05620 144 sdADSAAAHMPEgikVYSYEALLDG-----RSTVYDWPEldetTAAAICYSTGTTGAPKGVVYSHRSlyLQSLSLRTTDS 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 243 WGWSRDDVILHTLPLHHV--HGIvnkllcPL--WVGATTVMLP--TFQPQKVWEVLLSSkapMVTVFMAVPTIYSKLIQH 316
Cdd:PRK05620 219 LAVTHGESFLCCVPIYHVlsWGV------PLaaFMSGTPLVFPgpDLSAPTLAKIIATA---MPRVAHGVPTLWIQLMVH 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 317 YEQHftQPRvqdfvraacKERIRLMVSGSSALPQPTLLRWEEITGHTLLERYGMTEIGMAlsnplkgpripGAVGVPLPG 396
Cdd:PRK05620 290 YLKN--PPE---------RMSLQEIYVGGSAVPPILIKAWEERYGVDVVHVWGMTETSPV-----------GTVARPPSG 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 397 V--EVRIVMTNATSTTIAEGNSR---ETQVRPGLEGKEGELMVRGDQVFTEYWNKP----------------EATRESFT 455
Cdd:PRK05620 348 VsgEARWAYRVSQGRFPASLEYRivnDGQVMESTDRNEGEIQVRGNWVTASYYHSPteegggaastfrgedvEDANDRFT 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 456 EDGWFKTGDTA-VYKNGVYWIMGRTSvDIIKSGGYKISALEVERHLLAHPDITDVAVIGARDATWGQKVTAVVQLKRGRS 534
Cdd:PRK05620 428 ADGWLRTGDVGsVTRDGFLTIHDRAR-DVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLAVTVLAPGIE 506
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1367478878 535 ---MTLSELKTWAREHMAPYTIPTGLVLVEEMPRNQMGKVNKKDLLKHF 580
Cdd:PRK05620 507 ptrETAERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDLRQHL 555
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
83-573 |
9.07e-35 |
|
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: 136.49 E-value: 9.07e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 83 YGSSRGLAGRIKAALDcPSGDLQGKRISFLCANDASYTVAQWASWMCGGTAVPLYREHPPSELEyiisdsqssllvagqp 162
Cdd:cd05973 3 FGELRALSARFANALQ-ELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIE---------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 163 yadtmeplaHRLGlpylqlpptSSLSSLLeapenqpepgITDWAQR------PAMIIYTSGTTGRPKGVLHTHSNIQAMV 236
Cdd:cd05973 66 ---------HRLR---------TSGARLV----------VTDAANRhkldsdPFVMMFTSGTTGLPKGVPVPLRALAAFG 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 237 QGLVSEWGWSRDDVILHTLPLHHVHGIVNKLLCPLWVGATTVMLPT-FQPQKVWEVLLSSKapmVTVFMAVPTIYSKLIQ 315
Cdd:cd05973 118 AYLRDAVDLRPEDSFWNAADPGWAYGLYYAITGPLALGHPTILLEGgFSVESTWRVIERLG---VTNLAGSPTAYRLLMA 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 316 hyeqhftqprvqDFVRAACKERIRLMVSGSSALP-QPTLLRWEEIT-GHTLLERYGMTEIGMALSN--PLKGPRIPGAVG 391
Cdd:cd05973 195 ------------AGAEVPARPKGRLRRVSSAGEPlTPEVIRWFDAAlGVPIHDHYGQTELGMVLANhhALEHPVHAGSAG 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 392 VPLPGVevRIVMTNATSTTIAEGnsretqvRPG---LEGKEGELMVrgdqvFTEYWNKPEATresfTEDGWFKTGDTA-V 467
Cdd:cd05973 263 RAMPGW--RVAVLDDDGDELGPG-------EPGrlaIDIANSPLMW-----FRGYQLPDTPA----IDGGYYLTGDTVeF 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 468 YKNGVYWIMGRTSvDIIKSGGYKISALEVERHLLAHPDITDVAVIGARDATWGQKVTAVVQLKRGRSMT---LSELKTWA 544
Cdd:cd05973 325 DPDGSFSFIGRAD-DVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHEGTpalADELQLHV 403
|
490 500
....*....|....*....|....*....
gi 1367478878 545 REHMAPYTIPTGLVLVEEMPRNQMGKVNK 573
Cdd:cd05973 404 KKRLSAHAYPRTIHFVDELPKTPSGKIQR 432
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
182-578 |
1.53e-34 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 137.72 E-value: 1.53e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 182 PPTSSLSSLLEAPENQPEPGITDwAQRPAMIIYTSGTTGRPKGVLHTHsniQAMVQGLVS-EWG--WSRDDVILHTLPLH 258
Cdd:PRK04319 181 PGTLDFNALMEQASDEFDIEWTD-REDGAILHYTSGSTGKPKGVLHVH---NAMLQHYQTgKYVldLHEDDVYWCTADPG 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 259 HVHGIVNKLLCPLWVGATTVMLPT-FQPQKVWEVLLSSKapmVTVFMAVPTIYSKLIQHYEQHFTQprvQDFvraackER 337
Cdd:PRK04319 257 WVTGTSYGIFAPWLNGATNVIDGGrFSPERWYRILEDYK---VTVWYTAPTAIRMLMGAGDDLVKK---YDL------SS 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 338 IRLMVSGSSALpQPTLLRW-EEITGHTLLERYGMTEIGMAL-----SNPLKgpriPGAVGVPLPGVEVRIVmtnatstti 411
Cdd:PRK04319 325 LRHILSVGEPL-NPEVVRWgMKVFGLPIHDNWWMTETGGIMianypAMDIK----PGSMGKPLPGIEAAIV--------- 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 412 aegnSRETQVRPglEGKEGEL--------MVRGdqvfteYWNKPEATRESFtEDGWFKTGDTAvYKN--GVYWIMGRTSv 481
Cdd:PRK04319 391 ----DDQGNELP--PNRMGNLaikkgwpsMMRG------IWNNPEKYESYF-AGDWYVSGDSA-YMDedGYFWFQGRVD- 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 482 DIIKSGGYKISALEVERHLLAHPDITDVAVIGARDATWGQKVTAVVQLKRGRSMT---LSELKTWAREHMAPYTIPTGLV 558
Cdd:PRK04319 456 DVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVALRPGYEPSeelKEEIRGFVKKGLGAHAAPREIE 535
|
410 420
....*....|....*....|
gi 1367478878 559 LVEEMPRNQMGKVNKKdLLK 578
Cdd:PRK04319 536 FKDKLPKTRSGKIMRR-VLK 554
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
61-576 |
1.90e-34 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 140.30 E-value: 1.90e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 61 AQVYRDKLAIVDDSGSHSYRDLYGSSRGLAGRIKAAldcpsGDLQGKRISFLCANDASYTVAQWASWMCGGTAVPLYREH 140
Cdd:PRK12467 522 ARQHPERPALVFGEQVLSYAELNRQANRLAHVLIAA-----GVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEY 596
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 141 PPSELEYIISDSQSSLLVaGQPYADTMEPLAhrLGLPYLQLPPTSSLssLLEAPENQPEPGITdwAQRPAMIIYTSGTTG 220
Cdd:PRK12467 597 PQDRLAYMLDDSGVRLLL-TQSHLLAQLPVP--AGLRSLCLDEPADL--LCGYSGHNPEVALD--PDNLAYVIYTSGSTG 669
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 221 RPKGVLHTHSNIQAMVQGLVSEWGWSRDDVILHTLPLhHVHGIVNKLLCPLWVGATTVMLP---TFQPQKVWEVLLSSKa 297
Cdd:PRK12467 670 QPKGVAISHGALANYVCVIAERLQLAADDSMLMVSTF-AFDLGVTELFGALASGATLHLLPpdcARDAEAFAALMADQG- 747
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 298 pmVTVFMAVPTIYSKLIQhyeqhftQPRVqdfvrAACKERIRLMVSGsSALPQPTLLRWEEIT-GHTLLERYGMTE--IG 374
Cdd:PRK12467 748 --VTVLKIVPSHLQALLQ-------ASRV-----ALPRPQRALVCGG-EALQVDLLARVRALGpGARLINHYGPTEttVG 812
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 375 MALSNPLKGPRIPGAV--GVPLPGVEVRIVmtnatsttiaegnsrETQVRPGLEGKEGELMVRGDQVFTEYWNKPEATRE 452
Cdd:PRK12467 813 VSTYELSDEERDFGNVpiGQPLANLGLYIL---------------DHYLNPVPVGVVGELYIGGAGLARGYHRRPALTAE 877
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 453 SFTEDGW-------FKTGDTAVY-KNGVYWIMGRTSvDIIKSGGYKISALEVERHLLAHPDITDVAVIGARDATWGQKVT 524
Cdd:PRK12467 878 RFVPDPFgadggrlYRTGDLARYrADGVIEYLGRMD-HQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAGLQLVA 956
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1367478878 525 AVVQLKRG----RSMTLSELKTWAREHMAPYTIPTGLVLVEEMPRNQMGKVNKKDL 576
Cdd:PRK12467 957 YLVPAAVAdgaeHQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKAL 1012
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
130-464 |
4.16e-34 |
|
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: 136.19 E-value: 4.16e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 130 GGTAVPLYREHPPSELEYIISDSQSSLLVAgqpyADTMEplahrlglpylqlppTSSLSSLLEAPENQPEPGITDWAQRP 209
Cdd:cd05927 56 SLVTVPLYDTLGPEAIEYILNHAEISIVFC----DAGVK---------------VYSLEEFEKLGKKNKVPPPPPKPEDL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 210 AMIIYTSGTTGRPKGVLHTHSNIQAMVQGLVSEWG----WSRDDVILHTLPLHHV--HGIVNKLLC-----PLWVGATTV 278
Cdd:cd05927 117 ATICYTSGTTGNPKGVMLTHGNIVSNVAGVFKILEilnkINPTDVYISYLPLAHIfeRVVEALFLYhgakiGFYSGDIRL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 279 MLPTFQPQKvwevllsskaPmvTVFMAVPTIYSKL---IQHYEQ-----------------------------HFTQPRV 326
Cdd:cd05927 197 LLDDIKALK----------P--TVFPGVPRVLNRIydkIFNKVQakgplkrklfnfalnyklaelrsgvvrasPFWDKLV 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 327 QDFVRAACKERIRLMVSGSSALPQPTLLRWEEITGHTLLERYGMTEI--GMALSNPlkGPRIPGAVGVPLPGVEVRIVmt 404
Cdd:cd05927 265 FNKIKQALGGNVRLMLTGSAPLSPEVLEFLRVALGCPVLEGYGQTECtaGATLTLP--GDTSVGHVGGPLPCAEVKLV-- 340
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 405 natstTIAEGNSRETQVRPglegkEGELMVRGDQVFTEYWNKPEATRESFTEDGWFKTGD 464
Cdd:cd05927 341 -----DVPEMNYDAKDPNP-----RGEVCIRGPNVFSGYYKDPEKTAEALDEDGWLHTGD 390
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
77-580 |
6.76e-34 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 135.60 E-value: 6.76e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 77 HSYRDLYGSSRGLAGRIkAALDCPSGDlqgkRISFLCANDASYTVAQWAswmCGGTAVPLYREHP---PSELEYIISDSQ 153
Cdd:PRK07008 40 YTYRDCERRAKQLAQAL-AALGVEPGD----RVGTLAWNGYRHLEAYYG---VSGSGAVCHTINPrlfPEQIAYIVNHAE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 154 SSLL------------VAGQ-PYADTMEPLAHRLGLPYLQLPpTSSLSSLLEApenqpEPGITDWAQ----RPAMIIYTS 216
Cdd:PRK07008 112 DRYVlfdltflplvdaLAPQcPNVKGWVAMTDAAHLPAGSTP-LLCYETLVGA-----QDGDYDWPRfdenQASSLCYTS 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 217 GTTGRPKGVLHTH--SNIQAMVQGLVSEWGWSRDDVILHTLPLHHVHGIVNKLLCPLwVGATTVML-PTFQPQKVWEVLL 293
Cdd:PRK07008 186 GTTGNPKGALYSHrsTVLHAYGAALPDAMGLSARDAVLPVVPMFHVNAWGLPYSAPL-TGAKLVLPgPDLDGKSLYELIE 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 294 SSKapmVTVFMAVPTIYSKLIQHYEQhfTQPRVQDFVRAackerirlmVSGSSALPqPTLLR-WEEITGHTLLERYGMTE 372
Cdd:PRK07008 265 AER---VTFSAGVPTVWLGLLNHMRE--AGLRFSTLRRT---------VIGGSACP-PAMIRtFEDEYGVEVIHAWGMTE 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 373 I---GMALSNPLKGPRIPGAV--------GVPLPGVEVRIVmtnatsttiaEGNSRETQvrpgLEGKE-GELMVRGDQVF 440
Cdd:PRK07008 330 MsplGTLCKLKWKHSQLPLDEqrkllekqGRVIYGVDMKIV----------GDDGRELP----WDGKAfGDLQVRGPWVI 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 441 TEYWNKpeatRESFTEDGWFKTGDTA-VYKNGVYWIMGRtSVDIIKSGGYKISALEVERHLLAHPDITDVAVIGARDATW 519
Cdd:PRK07008 396 DRYFRG----DASPLVDGWFPTGDVAtIDADGFMQITDR-SKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKW 470
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1367478878 520 GQKVTAVVQLKRGRSMTLSELKTWAREHMAPYTIPTGLVLVEEMPRNQMGKVNKKDLLKHF 580
Cdd:PRK07008 471 DERPLLVVVKRPGAEVTREELLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKLREQF 531
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
43-578 |
2.94e-33 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 136.63 E-value: 2.94e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 43 STRARQAAAGDSAP--------VFSR--AQVYR--DKLAIVDDSGSHSYRDLYGSSRGLAGRIKAAldcpsGDLQGKRIS 110
Cdd:PRK12316 1983 GERQRILADWDRTPeayprgpgVHQRiaEQAARapEAIAVVFGDQHLSYAELDSRANRLAHRLRAR-----GVGPEVRVA 2057
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 111 FLCANDASYTVAQWASWMCGGTAVPLYREHPPSELEYIISDSQSSLLVagqpyadTMEPLAHRL----GLPYLQLPPTSS 186
Cdd:PRK12316 2058 IAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLL-------TQRHLLERLplpaGVARLPLDRDAE 2130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 187 LSsllEAPENQPEPGITdwAQRPAMIIYTSGTTGRPKGVLHTHSNIQAMVQGLVSEWGWSRDDVILHTLPLHhVHGIVNK 266
Cdd:PRK12316 2131 WA---DYPDTAPAVQLA--GENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPADCELQFMSFS-FDGAHEQ 2204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 267 LLCPLWVGATTVMLPTFQ--PQKVWEVLLSSKapmVTVFMAVPTIYSKLIQHYEqhftqprvqdfvRAACKERIRLMVSG 344
Cdd:PRK12316 2205 WFHPLLNGARVLIRDDELwdPEQLYDEMERHG---VTILDFPPVYLQQLAEHAE------------RDGRPPAVRVYCFG 2269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 345 SSALPQPTL-LRWEEITGHTLLERYGMTEIGMALSNPLKGPRIP-GAVGVPLpgvevrivmtnatSTTIaeGNSR----E 418
Cdd:PRK12316 2270 GEAVPAASLrLAWEALRPVYLFNGYGPTEAVVTPLLWKCRPQDPcGAAYVPI-------------GRAL--GNRRayilD 2334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 419 TQVRPGLEGKEGELMVRGDQVFTEYWNKPEATRESFTEDGW-------FKTGDTAVYK-NGVYWIMGRtsVD-IIKSGGY 489
Cdd:PRK12316 2335 ADLNLLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFsasgerlYRTGDLARYRaDGVVEYLGR--IDhQVKIRGF 2412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 490 KISALEVERHLLAHPDITDVAVIgARDATWGQKVTAVVQLKRGRSMTLSELKTWAREHMAPYTIPTGLVLVEEMPRNQMG 569
Cdd:PRK12316 2413 RIELGEIEARLQAHPAVREAVVV-AQDGASGKQLVAYVVPDDAAEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNG 2491
|
....*....
gi 1367478878 570 KVNKKDLLK 578
Cdd:PRK12316 2492 KLDRKALPK 2500
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
66-571 |
3.38e-33 |
|
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: 134.24 E-value: 3.38e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 66 DKLAIVDD------SGSHSYRDLYGSSRGLAGRIKAAldcpsGDLQGKRISFLCANDASYTVAQWASWMCGGTAVPLYRE 139
Cdd:cd17634 68 DRTAIIYEgddtsqSRTISYRELHREVCRFAGTLLDL-----GVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGG 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 140 HPPSELEYIISDSQSSLLVAGQ---------PY----ADTMEPLA---------HRLGLPYlQLPPTSSL--SSLLEA-- 193
Cdd:cd17634 143 FAPEAVAGRIIDSSSRLLITADggvragrsvPLkknvDDALNPNVtsvehvivlKRTGSDI-DWQEGRDLwwRDLIAKas 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 194 PENQPEPGItdwAQRPAMIIYTSGTTGRPKGVLHTHSN-IQAMVQGLVSEWGWSRDDVILHTLPLHHVHGIVNKLLCPLW 272
Cdd:cd17634 222 PEHQPEAMN---AEDPLFILYTSGTTGKPKGVLHTTGGyLVYAATTMKYVFDYGPGDIYWCTADVGWVTGHSYLLYGPLA 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 273 VGATTVML------PTfqPQKVWEVLLSSKapmVTVFMAVPTIYSKLiqhyeqhftQPRVQDFVRAACKERIRLMVS-GS 345
Cdd:cd17634 299 CGATTLLYegvpnwPT--PARMWQVVDKHG---VNILYTAPTAIRAL---------MAAGDDAIEGTDRSSLRILGSvGE 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 346 SALPQPTLLRWEEITGH--TLLERYGMTEIGMALSNPLKG--PRIPGAVGVPLPGVEVRIVMtnatsttiAEGNSRETqv 421
Cdd:cd17634 365 PINPEAYEWYWKKIGKEkcPVVDTWWQTETGGFMITPLPGaiELKAGSATRPVFGVQPAVVD--------NEGHPQPG-- 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 422 rpgleGKEGELMVRGD---QVFTEYWNKPEATRESF-TEDGWFKTGDTA-VYKNGVYWIMGRtSVDIIKSGGYKISALEV 496
Cdd:cd17634 435 -----GTEGNLVITDPwpgQTRTLFGDHERFEQTYFsTFKGMYFSGDGArRDEDGYYWITGR-SDDVINVAGHRLGTAEI 508
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1367478878 497 ERHLLAHPDITDVAVIGARDATWGQKVTAVVQLKRGR--SMTL-SELKTWAREHMAPYTIPTGLVLVEEMPRNQMGKV 571
Cdd:cd17634 509 ESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLNHGVepSPELyAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
60-571 |
9.80e-33 |
|
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.
Pssm-ID: 341254 [Multi-domain] Cd Length: 547 Bit Score: 132.36 E-value: 9.80e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 60 RAQVYRDKLA--IVDDSG----SHSYRDLYGSSRGLAGRIKAAldcpsgDLQGKRISFLCANDASYTVAQWASWMCGGTA 133
Cdd:cd05931 2 RAAARPDRPAytFLDDEGgreeTLTYAELDRRARAIAARLQAV------GKPGDRVLLLAPPGLDFVAAFLGCLYAGAIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 134 VPLYREHPPSE---LEYIISDSQSSLLVAGQPYADTMEPLAHRL-GLPYLQLPPTSSLSSLLEAPENQPEPGITDwaqrP 209
Cdd:cd05931 76 VPLPPPTPGRHaerLAAILADAGPRVVLTTAAALAAVRAFAASRpAAGTPRLLVVDLLPDTSAADWPPPSPDPDD----I 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 210 AMIIYTSGTTGRPKGVLHTHSNIQAMVQGLVSEWGWSRDDVILHTLPLHHVHGIVNKLLCPLWVGATTVMLPTFQpqkvw 289
Cdd:cd05931 152 AYLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGPSVLMSPAA----- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 290 evllsskapmvtvFMAVPTIYSKLIQHYEQHFTQprVQDFVRAACKERIRlmvsgSSALPQPTLLRW-------EEITGH 362
Cdd:cd05931 227 -------------FLRRPLRWLRLISRYRATISA--APNFAYDLCVRRVR-----DEDLEGLDLSSWrvalngaEPVRPA 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 363 TL---LER--------------YGMTEIGMALSNP---------------------LKGPRIPGAV-----GVPLPGVEV 399
Cdd:cd05931 287 TLrrfAEAfapfgfrpeafrpsYGLAEATLFVSGGppgtgpvvlrvdrdalagravAVAADDPAARelvscGRPLPDQEV 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 400 RIVmtnatsttiaEGNSRetQVRPglEGKEGELMVRGDQVFTEYWNKPEATRESF------TEDGWFKTGDTAVYKNGVY 473
Cdd:cd05931 367 RIV----------DPETG--RELP--DGEVGEIWVRGPSVASGYWGRPEATAETFgalaatDEGGWLRTGDLGFLHDGEL 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 474 WIMGRTSvDIIKSGGYKISALEVERHLLAHPD---ITDVAVIGARDATwGQKVTAVVQLKRGRSMT-LSELK-----TWA 544
Cdd:cd05931 433 YITGRLK-DLIIVRGRNHYPQDIEATAEEAHPalrPGCVAAFSVPDDG-EERLVVVAEVERGADPAdLAAIAaairaAVA 510
|
570 580 590
....*....|....*....|....*....|
gi 1367478878 545 REH-MAPYTIptglVLVE--EMPRNQMGKV 571
Cdd:cd05931 511 REHgVAPADV----VLVRpgSIPRTSSGKI 536
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
61-576 |
1.06e-32 |
|
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: 130.52 E-value: 1.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 61 AQVYR--DKLAIVDDSGSHSYRDLYGSSRGLAGRIKAAldcpsGDLQGKRISFLCANDASYTVAQWASWMCGGTAVPLYR 138
Cdd:cd12115 7 AQAARtpDAIALVCGDESLTYAELNRRANRLAARLRAA-----GVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 139 EHPPSELEYIISDSQSSLLvagqpyadtmeplahrlglpylqlpptsslsslleapenqpepgITDwAQRPAMIIYTSGT 218
Cdd:cd12115 82 AYPPERLRFILEDAQARLV--------------------------------------------LTD-PDDLAYVIYTSGS 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 219 TGRPKGVLHTHSNIQAMVQglvsewgWSRddvilHTLPLHHVHGI-----------VNKLLCPLWVGATTVMLptfqpQK 287
Cdd:cd12115 117 TGRPKGVAIEHRNAAAFLQ-------WAA-----AAFSAEELAGVlastsicfdlsVFELFGPLATGGKVVLA-----DN 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 288 VWEVLLSSKAPMVTVFMAVPTIYSKLIQHyeqhftqprvqdfvrAACKERIRLMVSGSSALPQPTLLR-WEEITGHTLLE 366
Cdd:cd12115 180 VLALPDLPAAAEVTLINTVPSAAAELLRH---------------DALPASVRVVNLAGEPLPRDLVQRlYARLQVERVVN 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 367 RYGMTE-----IGMALSnplKGPRIPGAVGVPLPGVEVRIVmtnatsttiaegnSRETQVRPglEGKEGELMVRGDQVFT 441
Cdd:cd12115 245 LYGPSEdttysTVAPVP---PGASGEVSIGRPLANTQAYVL-------------DRALQPVP--LGVPGELYIGGAGVAR 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 442 EYWNKPEATRESFTEDGW------FKTGDTAVYK-NGVYWIMGRTSvDIIKSGGYKISALEVERHLLAHPDITDVAVIGA 514
Cdd:cd12115 307 GYLGRPGLTAERFLPDPFgpgarlYRTGDLVRWRpDGLLEFLGRAD-NQVKVRGFRIELGEIEAALRSIPGVREAVVVAI 385
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1367478878 515 RDATWGQKVTAVVQLKRGRSMTLSELKTWAREHMAPYTIPTGLVLVEEMPRNQMGKVNKKDL 576
Cdd:cd12115 386 GDAAGERRLVAYIVAEPGAAGLVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
130-576 |
1.32e-32 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 134.52 E-value: 1.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 130 GGTAVPLYREHPPSELEYIISDSQSSLLvagqpyadtmepLAHRLGLPylQLPPTSSLSSL-LEAP----ENQPE--PGI 202
Cdd:PRK12467 1648 GGAYVPLDPEYPRERLAYMIEDSGIELL------------LTQSHLQA--RLPLPDGLRSLvLDQEddwlEGYSDsnPAV 1713
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 203 TDWAQRPAMIIYTSGTTGRPKGVLHTHSNIQAMVQGLVSEWGWSRDDVILHTLPlHHVHGIVNKLLCPLWVGATTVMLP- 281
Cdd:PRK12467 1714 NLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTS-FAFDVSVWELFWPLINGARLVIAPp 1792
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 282 --TFQPQKVWEVLLSSKapmVTVFMAVPTIYSKLIQHYEqHFTQPRvqdfvraackeRIRLMVSGSSALPQPTLLRWEEI 359
Cdd:PRK12467 1793 gaHRDPEQLIQLIERQQ---VTTLHFVPSMLQQLLQMDE-QVEHPL-----------SLRRVVCGGEALEVEALRPWLER 1857
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 360 TGHT-LLERYGMTEIGM-------ALSNPLKGPRIPgaVGVPLPGVEVRIVmtnatsttiaegnsrETQVRPGLEGKEGE 431
Cdd:PRK12467 1858 LPDTgLFNLYGPTETAVdvthwtcRRKDLEGRDSVP--IGQPIANLSTYIL---------------DASLNPVPIGVAGE 1920
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 432 LMVRGDQVFTEYWNKPEATRESFTEDGW-------FKTGDTAVYK-NGVYWIMGRtsVD-IIKSGGYKISALEVERHLLA 502
Cdd:PRK12467 1921 LYLGGVGLARGYLNRPALTAERFVADPFgtvgsrlYRTGDLARYRaDGVIEYLGR--IDhQVKIRGFRIELGEIEARLRE 1998
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 503 HPDITDVAVIgARDATWGQKVTA--------VVQLKRGRSMTLSELKTWAREHMAPYTIPTGLVLVEEMPRNQMGKVNKK 574
Cdd:PRK12467 1999 QGGVREAVVI-AQDGANGKQLVAyvvptdpgLVDDDEAQVALRAILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRK 2077
|
..
gi 1367478878 575 DL 576
Cdd:PRK12467 2078 AL 2079
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
192-571 |
1.82e-32 |
|
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called acetyl-CoA synthetase and acetyl-activating enzyme. It catalyzes the reaction ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA and belongs to the family of AMP-binding enzymes described by pfam00501.
Pssm-ID: 274022 [Multi-domain] Cd Length: 626 Bit Score: 132.37 E-value: 1.82e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 192 EAPENQPEPgiTDwAQRPAMIIYTSGTTGRPKGVLHTHSNIqaMVQGLVS-EW----------------GWsrddVILHT 254
Cdd:TIGR02188 225 ASAYCEPEP--MD-SEDPLFILYTSGSTGKPKGVLHTTGGY--LLYAAMTmKYvfdikdgdifwctadvGW----ITGHS 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 255 lplHHVHGivnkllcPLWVGATTVML---PTF-QPQKVWEVLLSSKapmVTVFMAVPTIYSKLIQHYEQHftqPRVQDfv 330
Cdd:TIGR02188 296 ---YIVYG-------PLANGATTVMFegvPTYpDPGRFWEIIEKHK---VTIFYTAPTAIRALMRLGDEW---VKKHD-- 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 331 raackeRIRLMVSGSSALP-QPTLLRW-EEITGHT---LLERYGMTEIGMALSNPLKG--PRIPGAVGVPLPGVEVRIVM 403
Cdd:TIGR02188 358 ------LSSLRLLGSVGEPiNPEAWMWyYKVVGKErcpIVDTWWQTETGGIMITPLPGatPTKPGSATLPFFGIEPAVVD 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 404 TnatsttiaEGNSRETqvrpglEGKEGEL--------MVRGdqvfteYWNKPEATRESFTED--GWFKTGDTAVY-KNGV 472
Cdd:TIGR02188 432 E--------EGNPVEG------PGEGGYLvikqpwpgMLRT------IYGDHERFVDTYFSPfpGYYFTGDGARRdKDGY 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 473 YWIMGRTSvDIIKSGGYKISALEVERHLLAHPDITDVAVIGARDATWGQKVTAVVQLKRGRSMTL---SELKTWAREHMA 549
Cdd:TIGR02188 492 IWITGRVD-DVINVSGHRLGTAEIESALVSHPAVAEAAVVGIPDDIKGQAIYAFVTLKDGYEPDDelrKELRKHVRKEIG 570
|
410 420
....*....|....*....|..
gi 1367478878 550 PYTIPTGLVLVEEMPRNQMGKV 571
Cdd:TIGR02188 571 PIAKPDKIRFVPGLPKTRSGKI 592
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
212-572 |
1.86e-32 |
|
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: 128.27 E-value: 1.86e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 212 IIYTSGTTGRPKGVLHTHSNIQAMVQG---------LVSEWGWSR-----DDVILHTLPLHHVHGIVNKLLCPLwvGATT 277
Cdd:cd05924 8 ILYTGGTTGMPKGVMWRQEDIFRMLMGgadfgtgefTPSEDAHKAaaaaaGTVMFPAPPLMHGTGSWTAFGGLL--GGQT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 278 VMLPT--FQPQKVWEVLLSSKAPMVTVF---MAVPTIyskliqhyeQHFTQPRVQDFvraackERIRLMVSGSSALPQPT 352
Cdd:cd05924 86 VVLPDdrFDPEEVWRTIEKHKVTSMTIVgdaMARPLI---------DALRDAGPYDL------SSLFAISSGGALLSPEV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 353 LLRWEEITGH-TLLERYGMTEIGMalsnplkgpripGAVGVPLPGVEVRIVMTNATSTTI-AEGNSRETQVRPGLEGKEG 430
Cdd:cd05924 151 KQGLLELVPNiTLVDAFGSSETGF------------TGSGHSAGSGPETGPFTRANPDTVvLDDDGRVVPPGSGGVGWIA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 431 elmvRGDQVFTEYWNKPEATRESFTE-DG--WFKTGDTA-VYKNGVYWIMGRTSVdIIKSGGYKISALEVERHLLAHPDI 506
Cdd:cd05924 219 ----RRGHIPLGYYGDEAKTAETFPEvDGvrYAVPGDRAtVEADGTVTLLGRGSV-CINTGGEKVFPEEVEEALKSHPAV 293
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1367478878 507 TDVAVIGARDATWGQKVTAVVQLKRGRSMTLSELKTWAREHMAPYTIPTGLVLVEEMPRNQMGKVN 572
Cdd:cd05924 294 YDVLVVGRPDERWGQEVVAVVQLREGAGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGKAD 359
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
130-576 |
3.56e-32 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 133.16 E-value: 3.56e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 130 GGTAVPLYREHPPSELEYIISDSQSSLLvagqpyadtmepLAHRLGLPylQLPPTSSLSSLLEAPENqpepgitDWAQRP 209
Cdd:PRK12316 4625 GGAYVPLDPEYPRERLAYMMEDSGAALL------------LTQSHLLQ--RLPIPDGLASLALDRDE-------DWEGFP 4683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 210 -------------AMIIYTSGTTGRPKGVLHTHSNIQAMVQGLVSEWGWSRDDVILHTLPLhHVHGIVNKLLCPLWVGAT 276
Cdd:PRK12316 4684 ahdpavrlhpdnlAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSF-SFDGSHEGLYHPLINGAS 4762
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 277 TVMLPTFQ--PQKVWEVLLSSKapmVTVFMAVPTIYSKLIQHYEQHFTQPRVqdfvraackeriRLMVSGSSALPQPTLL 354
Cdd:PRK12316 4763 VVIRDDSLwdPERLYAEIHEHR---VTVLVFPPVYLQQLAEHAERDGEPPSL------------RVYCFGGEAVAQASYD 4827
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 355 RWEEITGHT-LLERYGMTEIGM-ALSNPLKGPRIPGA----VGVPLPGVEVRIVmtnatsttiaegnsrETQVRPGLEGK 428
Cdd:PRK12316 4828 LAWRALKPVyLFNGYGPTETTVtVLLWKARDGDACGAaympIGTPLGNRSGYVL---------------DGQLNPLPVGV 4892
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 429 EGELMVRGDQVFTEYWNKPEATRESFTEDGW-------FKTGDTAVYK-NGVYWIMGRtsVD-IIKSGGYKISALEVERH 499
Cdd:PRK12316 4893 AGELYLGGEGVARGYLERPALTAERFVPDPFgapggrlYRTGDLARYRaDGVIDYLGR--VDhQVKIRGFRIELGEIEAR 4970
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 500 LLAHPDITDVAVIGARDATWGQKV-------TAVVQLKRGRSMTLSELKTWAREHMAPYTIPTGLVLVEEMPRNQMGKVN 572
Cdd:PRK12316 4971 LREHPAVREAVVIAQEGAVGKQLVgyvvpqdPALADADEAQAELRDELKAALRERLPEYMVPAHLVFLARMPLTPNGKLD 5050
|
....
gi 1367478878 573 KKDL 576
Cdd:PRK12316 5051 RKAL 5054
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
68-576 |
3.59e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 130.57 E-value: 3.59e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 68 LAIVDDSGSH------SYRDLYGSSRGLAGRIKAALD----CPSGDLQGkrisflcaNDASYTVAQWASWMCGGTAVPLY 137
Cdd:PRK07867 14 LAEDDDRGLYfedsftSWREHIRGSAARAAALRARLDptrpPHVGVLLD--------NTPEFSLLLGAAALSGIVPVGLN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 138 REHPPSELEYIISDSQSSLLVAGQPYADTMEPLAHrlGLPYLQLPpTSSLSSLLEAPENQPEPGITDWAQRPAMIIYTSG 217
Cdd:PRK07867 86 PTRRGAALARDIAHADCQLVLTESAHAELLDGLDP--GVRVINVD-SPAWADELAAHRDAEPPFRVADPDDLFMLIFTSG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 218 TTGRPKGVLHTHSNIQAMVQGLVSEWGWSRDDVILHTLPLHHVHGIVNKLLCPLWVGATTVMLPTFQpqkVWEVLLSSKA 297
Cdd:PRK07867 163 TSGDPKAVRCTHRKVASAGVMLAQRFGLGPDDVCYVSMPLFHSNAVMAGWAVALAAGASIALRRKFS---ASGFLPDVRR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 298 PMVTVFMAVPTIYSKLIQhyeqhfTQPRVQDfvraacKERIRLMVSGSSALPqPTLLRWEEITGHTLLERYGMTEIGMAL 377
Cdd:PRK07867 240 YGATYANYVGKPLSYVLA------TPERPDD------ADNPLRIVYGNEGAP-GDIARFARRFGCVVVDGFGSTEGGVAI 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 378 SNPLKGPriPGAVGVPLPGVEVRIVmtnATSTTIAEGNSRETQVRPGLEGKeGELM-VRGDQVFTEYWNKPEATRESFtE 456
Cdd:PRK07867 307 TRTPDTP--PGALGPLPPGVAIVDP---DTGTECPPAEDADGRLLNADEAI-GELVnTAGPGGFEGYYNDPEADAERM-R 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 457 DGWFKTGDTAvYK--NGVYWIMGRTSvDIIKSGGYKISALEVERHLLAHPDITDVAVIGARDATWGQKVTAVVQLKRGRS 534
Cdd:PRK07867 380 GGVYWSGDLA-YRdaDGYAYFAGRLG-DWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVMAALVLAPGAK 457
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1367478878 535 MTLSELKTW--AREHMAPYTIPTGLVLVEEMPRNQMGKVNKKDL 576
Cdd:PRK07867 458 FDPDAFAEFlaAQPDLGPKQWPSYVRVCAELPRTATFKVLKRQL 501
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
60-576 |
4.67e-32 |
|
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341308 [Multi-domain] Cd Length: 433 Bit Score: 128.58 E-value: 4.67e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 60 RAQVYRDKLAIVDDSGSHSYRDLYGSSRGLAGRIKAALDCPsgdlqGKRISFLCANDASYTVAQWASWMCGGTAVPLYRE 139
Cdd:cd17653 6 IAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVP-----GDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 140 HPPSELEYIISDSQSSLLVAgqpyadtmeplahrlglpylqlpptsslsslleapenqpepgiTDWAQRPAMIIYTSGTT 219
Cdd:cd17653 81 LPSARIQAILRTSGATLLLT-------------------------------------------TDSPDDLAYIIFTSGST 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 220 GRPKGVLHTHSNIQAMVQglvsewgWSRDDviLHTLP---LHHVHGI-----VNKLLCPLWVGATTVMLPTFQPqkvwev 291
Cdd:cd17653 118 GIPKGVMVPHRGVLNYVS-------QPPAR--LDVGPgsrVAQVLSIafdacIGEIFSTLCNGGTLVLADPSDP------ 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 292 lLSSKAPMVTVFMAVPTIYSKLiqhyeqhftqpRVQDFvraackERIRLMVSGSSALPQPTLLRWEEitGHTLLERYGMT 371
Cdd:cd17653 183 -FAHVARTVDALMSTPSILSTL-----------SPQDF------PNLKTIFLGGEAVPPSLLDRWSP--GRRLYNAYGPT 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 372 EIGMALSNPLKGPRIPGAVGVPLPGVEVRIVmtnatsttiaegnsrETQVRPGLEGKEGELMVRGDQVFTEYWNKPEATR 451
Cdd:cd17653 243 ECTISSTMTELLPGQPVTIGKPIPNSTCYIL---------------DADLQPVPEGVVGEICISGVQVARGYLGNPALTA 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 452 ESFTEDGW------FKTGDTAVY--KNGVYWImGRTSVDIiKSGGYKISALEVERHLLA-HPDITDVAVIGARDAtwgqk 522
Cdd:cd17653 308 SKFVPDPFwpgsrmYRTGDYGRWteDGGLEFL-GREDNQV-KVRGFRINLEEIEEVVLQsQPEVTQAAAIVVNGR----- 380
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1367478878 523 vtaVVQLKRGRSMTLSELKTWAREHMAPYTIPTGLVLVEEMPRNQMGKVNKKDL 576
Cdd:cd17653 381 ---LVAFVTPETVDVDGLRSELAKHLPSYAVPDRIIALDSFPLTANGKVDRKAL 431
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
66-576 |
5.73e-32 |
|
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341305 [Multi-domain] Cd Length: 447 Bit Score: 128.74 E-value: 5.73e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 66 DKLAIVDDSGSHSYRDLYGSSRGLAgRIKAALDCPSGDLQGkrisfLCANDASYT-VAQWASWMCGGTAVPLYREHPPSE 144
Cdd:cd17650 2 DAIAVSDATRQLTYRELNERANQLA-RTLRGLGVAPGSVVG-----VCADRSLDAiVGLLAVLKAGGAYVPIDPDYPAER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 145 LEYIISDSQSSLLVAgqpyadtmeplahrlglpylqlpptsslsslleapenQPEpgitdwaqRPAMIIYTSGTTGRPKG 224
Cdd:cd17650 76 LQYMLEDSGAKLLLT-------------------------------------QPE--------DLAYVIYTSGTTGKPKG 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 225 VLHTHSNIQAMVQGLVSEWGWSRDDVILHTLPLHHVHGIVNKLLCPLWVGATTVMLP---TFQPQKVWEVLLSSKApmvT 301
Cdd:cd17650 111 VMVEHRNVAHAAHAWRREYELDSFPVRLLQMASFSFDVFAGDFARSLLNGGTLVICPdevKLDPAALYDLILKSRI---T 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 302 VFMAVPTIYSKLIQHYEQHFTQPrvqdfvraackERIRLMVSGSSALPQP---TLLRweEITGHT-LLERYGMTE--IGM 375
Cdd:cd17650 188 LMESTPALIRPVMAYVYRNGLDL-----------SAMRLLIVGSDGCKAQdfkTLAA--RFGQGMrIINSYGVTEatIDS 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 376 ALSNPLKGPRIPGA---VGVPLPGVEVRIVmtnatsttiaegnsrETQVRPGLEGKEGELMVRGDQVFTEYWNKPEATRE 452
Cdd:cd17650 255 TYYEEGRDPLGDSAnvpIGRPLPNTAMYVL---------------DERLQPQPVGVAGELYIGGAGVARGYLNRPELTAE 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 453 SFTEDGW------FKTGDTAVYK-NGVYWIMGRTSvDIIKSGGYKISALEVERHLLAHPDITDVAVIGARDAtwGQKVTA 525
Cdd:cd17650 320 RFVENPFapgermYRTGDLARWRaDGNVELLGRVD-HQVKIRGFRIELGEIESQLARHPAIDEAVVAVREDK--GGEARL 396
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1367478878 526 VVQLKRGRSMTLSELKTWAREHMAPYTIPTGLVLVEEMPRNQMGKVNKKDL 576
Cdd:cd17650 397 CAYVVAAATLNTAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
206-578 |
4.30e-31 |
|
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: 128.20 E-value: 4.30e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 206 AQRPAMIIYTSGTTGRPKGVL-----------HTHSNIQAMVQGLV----SEWGWsrddVILHTLPlhhVHGivnkllcP 270
Cdd:cd05967 229 ATDPLYILYTSGTTGKPKGVVrdngghavalnWSMRNIYGIKPGDVwwaaSDVGW----VVGHSYI---VYG-------P 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 271 LWVGATTVM---LPTFQPQ--KVWEVLlsSKAPMVTVFMAvPTIYSKLIQhyeqhftQPRVQDFVRAACKERIRLMVSGS 345
Cdd:cd05967 295 LLHGATTVLyegKPVGTPDpgAFWRVI--EKYQVNALFTA-PTAIRAIRK-------EDPDGKYIKKYDLSSLRTLFLAG 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 346 SALPQPTLLRWEEITGHTLLERYGMTEIGMALSNPLKG----PRIPGAVGVPLPGVEVRIVMtnatsttiAEGNsretQV 421
Cdd:cd05967 365 ERLDPPTLEWAENTLGVPVIDHWWQTETGWPITANPVGleplPIKAGSPGKPVPGYQVQVLD--------EDGE----PV 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 422 RPGlegKEGELMVRGD---QVFTEYWNKPEATRESFTED--GWFKTGDTAVY-KNGVYWIMGRTSvDIIKSGGYKISALE 495
Cdd:cd05967 433 GPN---ELGNIVIKLPlppGCLLTLWKNDERFKKLYLSKfpGYYDTGDAGYKdEDGYLFIMGRTD-DVINVAGHRLSTGE 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 496 VERHLLAHPDITDVAVIGARDATWGQKVTAVVQLKRGRSMTLSELKT----WAREHMAPYTIPTGLVLVEEMPRNQMGKV 571
Cdd:cd05967 509 MEESVLSHPAVAECAVVGVRDELKGQVPLGLVVLKEGVKITAEELEKelvaLVREQIGPVAAFRLVIFVKRLPKTRSGKI 588
|
....*..
gi 1367478878 572 NKKDLLK 578
Cdd:cd05967 589 LRRTLRK 595
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
210-580 |
1.18e-30 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 122.85 E-value: 1.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 210 AMIIYTSGTTGRPKGVLHTHSNI----QAMVQGLVSEWGWsrddviLHTLPLHHVHGIvNKLLCPLWVGATTVMLPT--- 282
Cdd:PRK07824 38 ALVVATSGTTGTPKGAMLTAAALtasaDATHDRLGGPGQW------LLALPAHHIAGL-QVLVRSVIAGSEPVELDVsag 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 283 FQPqkvwevllsSKAPMVTVFMAVPTIYSKLIQhyeqhfTQ--PRVQDFVRAACKERIRLMVSGSSALPQPTLLRWEEIt 360
Cdd:PRK07824 111 FDP---------TALPRAVAELGGGRRYTSLVP------MQlaKALDDPAATAALAELDAVLVGGGPAPAPVLDAAAAA- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 361 GHTLLERYGMTEIGmalsnplkgpriPGAV--GVPLPGVEVRIVmtnatsttiaegnsretqvrpglegkEGELMVRGDQ 438
Cdd:PRK07824 175 GINVVRTYGMSETS------------GGCVydGVPLDGVRVRVE--------------------------DGRIALGGPT 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 439 VFTEYWNKPEatRESFTEDGWFKTGDTAVYKNGVYWIMGRTSvDIIKSGGYKISALEVERHLLAHPDITDVAVIGARDAT 518
Cdd:PRK07824 217 LAKGYRNPVD--PDPFAEPGWFRTDDLGALDDGVLTVLGRAD-DAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDR 293
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1367478878 519 WGQKVTAVVQLKRGRSMTLSELKTWAREHMAPYTIPTGLVLVEEMPRNQMGKVNKKDLLKHF 580
Cdd:PRK07824 294 LGQRVVAAVVGDGGPAPTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALVRRF 355
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
206-574 |
1.52e-30 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 127.73 E-value: 1.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 206 AQRPAMIIYTSGTTGRPKGVLHTHSNIQAMVQGLVSEWGWSRDDVILHTLPLHHVHGIVNKLLCPLWVGATTVMLPtfQP 285
Cdd:PRK08633 781 PDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSSLPFFHSFGLTVTLWLPLLEGIKVVYHP--DP 858
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 286 QKVWEVLLSSKAPMVTVFMAVPT---IYSKliqhyeqhftQPRVQ--DFvraackERIRLMVSGSSALPQPTLLRWEEIT 360
Cdd:PRK08633 859 TDALGIAKLVAKHRATILLGTPTflrLYLR----------NKKLHplMF------ASLRLVVAGAEKLKPEVADAFEEKF 922
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 361 GHTLLERYGMTE-----------IGMALSNPLKGPRiPGAVGVPLPGVEVRIVMTNatstTIAEGNsretqvrpglEGKE 429
Cdd:PRK08633 923 GIRILEGYGATEtspvasvnlpdVLAADFKRQTGSK-EGSVGMPLPGVAVRIVDPE----TFEELP----------PGED 987
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 430 GELMVRGDQVFTEYWNKPEATRESFTE---DGWFKTGDTAVY-KNGVYWIMGRTSvDIIKSGGYKIS--ALEVERHLLAH 503
Cdd:PRK08633 988 GLILIGGPQVMKGYLGDPEKTAEVIKDidgIGWYVTGDKGHLdEDGFLTITDRYS-RFAKIGGEMVPlgAVEEELAKALG 1066
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1367478878 504 PDITDVAVIGARDATWGQKVTAVVQLKRGRSMTLSELKTWARehMAPYTIPTGLVLVEEMPRNQMGKVNKK 574
Cdd:PRK08633 1067 GEEVVFAVTAVPDEKKGEKLVVLHTCGAEDVEELKRAIKESG--LPNLWKPSRYFKVEALPLLGSGKLDLK 1135
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
214-576 |
2.41e-30 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 125.34 E-value: 2.41e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 214 YTSGTTGRPKGVLHTHSNIQAMVQGLVSEWGWSRDDVILHTLPLHHVHGivnklLCPLWVGA----TTVMLPTFQPQKVW 289
Cdd:PLN02479 202 YTSGTTASPKGVVLHHRGAYLMALSNALIWGMNEGAVYLWTLPMFHCNG-----WCFTWTLAalcgTNICLRQVTAKAIY 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 290 EVLLSSKapmVTVFMAVPTIYSKLIQ--HYEQHFTQPRVqdfvraackerIRLMVSGssALPQPTLLRWEEITGHTLLER 367
Cdd:PLN02479 277 SAIANYG---VTHFCAAPVVLNTIVNapKSETILPLPRV-----------VHVMTAG--AAPPPSVLFAMSEKGFRVTHT 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 368 YGMTEIGMALS-----------NPLKGPRIPGAVGVPLPGVE-VRIVMTNATSTTIAEGNSRetqvrpglegkeGELMVR 435
Cdd:PLN02479 341 YGLSETYGPSTvcawkpewdslPPEEQARLNARQGVRYIGLEgLDVVDTKTMKPVPADGKTM------------GEIVMR 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 436 GDQVFTEYWNKPEATRESFtEDGWFKTGDTAVYKNGVYWIMGRTSVDIIKSGGYKISALEVERHLLAHPDITDVAVIGAR 515
Cdd:PLN02479 409 GNMVMKGYLKNPKANEEAF-ANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARP 487
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1367478878 516 DATWGQKVTAVVQLKRG-----RSMTLSELKTWAREHMAPYTIPTGLVLvEEMPRNQMGKVNKKDL 576
Cdd:PLN02479 488 DERWGESPCAFVTLKPGvdksdEAALAEDIMKFCRERLPAYWVPKSVVF-GPLPKTATGKIQKHVL 552
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
48-576 |
3.80e-30 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 124.74 E-value: 3.80e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 48 QAAAGDSAPVFSR--AQVYRDKLAIV----DDSGSHSYRDLYGSSRGLAGRIKAaldcpSGDLQGKRISFLCANDASYTV 121
Cdd:PRK05857 7 QAMPQLPSTVLDRvfEQARQQPEAIAlrrcDGTSALRYRELVAEVGGLAADLRA-----QSVSRGSRVLVISDNGPETYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 122 AQWASWMCGGTAVPLYREHPPSELEYI--ISDSqSSLLVAGQPYADTMEPLAHRLGLPYLQLPPTSSLSSLLEAPE---- 195
Cdd:PRK05857 82 SVLACAKLGAIAVMADGNLPIAAIERFcqITDP-AAALVAPGSKMASSAVPEALHSIPVIAVDIAAVTRESEHSLDaasl 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 196 -NQPEPGITDwaqrPAMIIYTSGTTGRPKGVLHTHSNIQAMVQGLVSE---W-GWSRDDVILHTLPLHHVHGIVNKLLCp 270
Cdd:PRK05857 161 aGNADQGSED----PLAMIFTSGTTGEPKAVLLANRTFFAVPDILQKEglnWvTWVVGETTYSPLPATHIGGLWWILTC- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 271 LWVGATTVMLPTfQPQKVWEVLLSSKapmVTVFMAVPTIYSKLIqhYEQHFTQPRVQDfvraackerIRLMVSGSSALPQ 350
Cdd:PRK05857 236 LMHGGLCVTGGE-NTTSLLEILTTNA---VATTCLVPTLLSKLV--SELKSANATVPS---------LRLVGYGGSRAIA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 351 PTlLRWEEITGHTLLERYGMTEIG-MALSNPLKGPRIP----GAVGVPLPGVEVRIVMTNATSTTIAEGNSRETQvrpgl 425
Cdd:PRK05857 301 AD-VRFIEATGVRTAQVYGLSETGcTALCLPTDDGSIVkieaGAVGRPYPGVDVYLAATDGIGPTAPGAGPSASF----- 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 426 egkeGELMVRGDQVFTEYWNKPEATRESFTeDGWFKTGD-TAVYKNGVYWIMGRTSvDIIKSGGYKISALEVERHLLAHP 504
Cdd:PRK05857 375 ----GTLWIKSPANMLGYWNNPERTAEVLI-DGWVNTGDlLERREDGFFYIKGRSS-EMIICGGVNIAPDEVDRIAEGVS 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 505 DITDVAVIGARDATWGQKV-TAVVQLKRGRSMTLSELK--TWAR-----EHMAPytiPTGLVLVEEMPRNQMGKVNKKDL 576
Cdd:PRK05857 449 GVREAACYEIPDEEFGALVgLAVVASAELDESAARALKhtIAARfrresEPMAR---PSTIVIVTDIPRTQSGKVMRASL 525
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
59-576 |
6.60e-30 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 123.58 E-value: 6.60e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 59 SRAQVYRDKLA-IVDDSGSH-SYRDLYGSSRGLAgRIKAALDCPSGDLqgkrISFLCANDASYTVAQWASWMCGGTAVPL 136
Cdd:PRK13390 5 THAQIAPDRPAvIVAETGEQvSYRQLDDDSAALA-RVLYDAGLRTGDV----VALLSDNSPEALVVLWAALRSGLYITAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 137 YREHPPSELEYIISDSQSSLLVAgqpyADTMEPLAHRLGLPY-LQLPPTSSLSSL--LEAPENQPEPGITdwaQRP--AM 211
Cdd:PRK13390 80 NHHLTAPEADYIVGDSGARVLVA----SAALDGLAAKVGADLpLRLSFGGEIDGFgsFEAALAGAGPRLT---EQPcgAV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 212 IIYTSGTTGRPKG---------VLHTHSNIQAMVQGLvseWGWSRDDVILHTLPLHHVH-----GIVNKLlcplwvGATT 277
Cdd:PRK13390 153 MLYSSGTTGFPKGiqpdlpgrdVDAPGDPIVAIARAF---YDISESDIYYSSAPIYHAAplrwcSMVHAL------GGTV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 278 VMLPTFQPQkvwEVLLSSKAPMVTVFMAVPTIYSKLIqhyeqhftqpRVQDFVRAACK-ERIRLMVSGSSALP---QPTL 353
Cdd:PRK13390 224 VLAKRFDAQ---ATLGHVERYRITVTQMVPTMFVRLL----------KLDADVRTRYDvSSLRAVIHAAAPCPvdvKHAM 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 354 LRWeeiTGHTLLERYGMTEI-GMALSNPLKGPRIPGAVGVPLPGvevrivmtnatSTTIAEGNSRETQVrpgleGKEGEL 432
Cdd:PRK13390 291 IDW---LGPIVYEYYSSTEAhGMTFIDSPDWLAHPGSVGRSVLG-----------DLHICDDDGNELPA-----GRIGTV 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 433 MVRGDQVFTEYWNKPEATRESF--TEDGWFKTGDTA-VYKNGVYWIMGRTSVDIIkSGGYKISALEVERHLLAHPDITDV 509
Cdd:PRK13390 352 YFERDRLPFRYLNDPEKTAAAQhpAHPFWTTVGDLGsVDEDGYLYLADRKSFMII-SGGVNIYPQETENALTMHPAVHDV 430
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 510 AVIGARDATWGQKVTAVVQLK---RGRSMTLSELKTWAREHMAPYTIPTGLVLVEEMPRNQMGKVNKKDL 576
Cdd:PRK13390 431 AVIGVPDPEMGEQVKAVIQLVegiRGSDELARELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLL 500
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
209-576 |
1.91e-29 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 122.82 E-value: 1.91e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 209 PAMIIYTSGTTGRPKGVLHTHSNiqAMVQGLVSEWGWSRD--DVILHTLPLHHVHGIVNKLLCPLWVGATTVMLPTFQPq 286
Cdd:PLN03102 188 PISLNYTSGTTADPKGVVISHRG--AYLSTLSAIIGWEMGtcPVYLWTLPMFHCNGWTFTWGTAARGGTSVCMRHVTAP- 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 287 kvwEVLLSSKAPMVTVFMAVPTIYSKLIQ--HYEQHFTQPRVQdfvraackerirLMVSGSSalPQPTLLRWEEITGHTL 364
Cdd:PLN03102 265 ---EIYKNIEMHNVTHMCCVPTVFNILLKgnSLDLSPRSGPVH------------VLTGGSP--PPAALVKKVQRLGFQV 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 365 LERYGMTEIgmalsnplKGP-----------RIPGAVGVPLpgvEVRIVMTNATSTTIAEGNsRETQVRPGLEGKE-GEL 432
Cdd:PLN03102 328 MHAYGLTEA--------TGPvlfcewqdewnRLPENQQMEL---KARQGVSILGLADVDVKN-KETQESVPRDGKTmGEI 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 433 MVRGDQVFTEYWNKPEATRESFtEDGWFKTGDTAV-YKNGVYWIMGRtSVDIIKSGGYKISALEVERHLLAHPDITDVAV 511
Cdd:PLN03102 396 VIKGSSIMKGYLKNPKATSEAF-KHGWLNTGDVGViHPDGHVEIKDR-SKDIIISGGENISSVEVENVLYKYPKVLETAV 473
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1367478878 512 IGARDATWGQKVTAVVQLKRGRSMTLS----------ELKTWAREHMAPYTIPTGLVLVEEMPRNQMGKVNKKDL 576
Cdd:PLN03102 474 VAMPHPTWGETPCAFVVLEKGETTKEDrvdklvtrerDLIEYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKL 548
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
34-576 |
2.18e-29 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 124.68 E-value: 2.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 34 RQVLRRAYTSTRARQAAAGDSAPVFSrAQVYR--DKLAIVDDSGSHSYRDLYGSSRGLAGRIKAALDCPSgdlqgKRISF 111
Cdd:PRK12316 3039 RGQLLEAWNATAAEYPLERGVHRLFE-EQVERtpDAVALAFGEQRLSYAELNRRANRLAHRLIERGVGPD-----VLVGV 3112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 112 LCANDASYTVAQWASWMCGGTAVPLYREHPPSELEYIISDSQSSLLvagqpyadtmeplahrLGLPYLQLPPTSSLSSLL 191
Cdd:PRK12316 3113 AVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLL----------------LSQSHLRLPLAQGVQVLD 3176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 192 --EAPENQPE--PGITDWAQRPAMIIYTSGTTGRPKGVLHTHSNIQAMVQGLVSEWGWSRDDVILHTLPLhHVHGIVNKL 267
Cdd:PRK12316 3177 ldRGDENYAEanPAIRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTF-SFDVFVEEL 3255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 268 LCPLWVGATTVMLPTFQPQKVWEVLLSSKAPMVTVFMAVPTIYSKLIQHyeqhftqprvqdfVRAACKERIRLMVSGSSA 347
Cdd:PRK12316 3256 FWPLMSGARVVLAGPEDWRDPALLVELINSEGVDVLHAYPSMLQAFLEE-------------EDAHRCTSLKRIVCGGEA 3322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 348 LPQPTLLRWeeITGHTLLERYGMTEIGMALSNPLKGPRIPGA--VGVPLPGVEVRIVMTNATsttiaegnsretqvrPGL 425
Cdd:PRK12316 3323 LPADLQQQV--FAGLPLYNLYGPTEATITVTHWQCVEEGKDAvpIGRPIANRACYILDGSLE---------------PVP 3385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 426 EGKEGELMVRGDQVFTEYWNKPEATRESFTEDGW------FKTGDTAVYK-NGVYWIMGRTSVDiIKSGGYKISALEVER 498
Cdd:PRK12316 3386 VGALGELYLGGEGLARGYHNRPGLTAERFVPDPFvpgerlYRTGDLARYRaDGVIEYIGRVDHQ-VKIRGFRIELGEIEA 3464
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1367478878 499 HLLAHPDITDVAVIgardATWGQKVTAVVQLKRGRSMTLSELKTWAREHMAPYTIPTGLVLVEEMPRNQMGKVNKKDL 576
Cdd:PRK12316 3465 RLLEHPWVREAVVL----AVDGRQLVAYVVPEDEAGDLREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKAL 3538
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
34-576 |
2.22e-29 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 124.68 E-value: 2.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 34 RQVLRRAYTSTRARQAAAGDSAPVFsRAQVYR--DKLAIVDDSGSHSYRDLYGSSRGLAGRIKAaldcpSGDLQGKRISF 111
Cdd:PRK12316 493 RGQLVEGWNATAAEYPLQRGVHRLF-EEQVERtpEAPALAFGEETLDYAELNRRANRLAHALIE-----RGVGPDVLVGV 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 112 LCANDASYTVAQWASWMCGGTAVPLYREHPPSELEYIISDSQSSLLVAGQPYADTMePLAHRLGLPYLQLPptsslSSLL 191
Cdd:PRK12316 567 AMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQSHLGRKL-PLAAGVQVLDLDRP-----AAWL 640
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 192 EA-PENQPEPGITdwAQRPAMIIYTSGTTGRPKGVLHTHSNIQAMVQGLVSEWGWSRDDVILHTLPLHHVHGiVNKLLCP 270
Cdd:PRK12316 641 EGySEENPGTELN--PENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVS-VWEFFWP 717
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 271 LWVGATTVMLPT---FQPQKVWEVllsSKAPMVTVFMAVPTIYSKLIQhyeqhftQPRVQDFVraackeRIRLMVSGSSA 347
Cdd:PRK12316 718 LMSGARLVVAAPgdhRDPAKLVEL---INREGVDTLHFVPSMLQAFLQ-------DEDVASCT------SLRRIVCSGEA 781
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 348 LPQPTLLRWEEITGHT-LLERYGMTE--IGMALSNPLK--GPRIPgaVGVPLPGVEVRIVmtnatsttiaegnsrETQVR 422
Cdd:PRK12316 782 LPADAQEQVFAKLPQAgLYNLYGPTEaaIDVTHWTCVEegGDSVP--IGRPIANLACYIL---------------DANLE 844
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 423 PGLEGKEGELMVRGDQVFTEYWNKPEATRESFTEDGW------FKTGDTAVYK-NGVYWIMGRTSvDIIKSGGYKISALE 495
Cdd:PRK12316 845 PVPVGVLGELYLAGRGLARGYHGRPGLTAERFVPSPFvagermYRTGDLARYRaDGVIEYAGRID-HQVKLRGLRIELGE 923
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 496 VERHLLAHPDITDVAVIgardATWGQKVTAVVQLKRGRSMTLSELKTWAREHMAPYTIPTGLVLVEEMPRNQMGKVNKKD 575
Cdd:PRK12316 924 IEARLLEHPWVREAAVL----AVDGKQLVGYVVLESEGGDWREALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKA 999
|
.
gi 1367478878 576 L 576
Cdd:PRK12316 1000 L 1000
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
194-571 |
6.32e-29 |
|
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: 121.51 E-value: 6.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 194 PENQPEPgiTDwAQRPAMIIYTSGTTGRPKGVLHTHSNIqaMVQ-GLVSEW----------------GWsrddVILHTlp 256
Cdd:cd05966 221 PECEPEW--MD-SEDPLFILYTSGSTGKPKGVVHTTGGY--LLYaATTFKYvfdyhpddiywctadiGW----ITGHS-- 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 257 lHHVHGivnkllcPLWVGATTVML---PTF-QPQKVWEVLLSSKapmVTVFMAVPTIYSKLIQHYEqhftqprvqDFVRA 332
Cdd:cd05966 290 -YIVYG-------PLANGATTVMFegtPTYpDPGRYWDIVEKHK---VTIFYTAPTAIRALMKFGD---------EWVKK 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 333 ACKERIRLMvsGSSALP-QPTLLRW-EEITGH---TLLERYGMTEIGMALSNPLKG--PRIPGAVGVPLPGVEVRIVMtn 405
Cdd:cd05966 350 HDLSSLRVL--GSVGEPiNPEAWMWyYEVIGKercPIVDTWWQTETGGIMITPLPGatPLKPGSATRPFFGIEPAILD-- 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 406 atsttiAEGNSRETQVrpglegkEGEL--------MVRGdqvfteYWNKPEATRESFTED--GWFKTGDTAVY-KNGVYW 474
Cdd:cd05966 426 ------EEGNEVEGEV-------EGYLvikrpwpgMART------IYGDHERYEDTYFSKfpGYYFTGDGARRdEDGYYW 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 475 IMGRTSvDIIKSGGYKISALEVERHLLAHPDITDVAVIGARDATWGQKVTAVVQLKRGRSMT---LSELKTWAREHMAPY 551
Cdd:cd05966 487 ITGRVD-DVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGEEPSdelRKELRKHVRKEIGPI 565
|
410 420
....*....|....*....|
gi 1367478878 552 TIPTGLVLVEEMPRNQMGKV 571
Cdd:cd05966 566 ATPDKIQFVPGLPKTRSGKI 585
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
57-578 |
1.66e-28 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 119.70 E-value: 1.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 57 VFSRAQVYRDKLAIVD--DSGSHSYRDLYGSSRGLAGRIKAAldcpsGDLQGKRISFLCANDASYTVAQWASWMCGGT-- 132
Cdd:PLN02330 34 VLQDAELYADKVAFVEavTGKAVTYGEVVRDTRRFAKALRSL-----GLRKGQVVVVVLPNVAEYGIVALGIMAAGGVfs 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 133 -AVPLYREhppSELEYIISDSQSSLLVAGqpyaDTMEPLAHRLGLPYLQLPPTS-----SLSSLLEAPENQPEPGI---- 202
Cdd:PLN02330 109 gANPTALE---SEIKKQAEAAGAKLIVTN----DTNYGKVKGLGLPVIVLGEEKiegavNWKELLEAADRAGDTSDneei 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 203 --TDWAQRPamiiYTSGTTGRPKGVLHTHSNiqaMVQGLVSEWGWSRDDVI-----LHTLPLHHVHGIVNKLLCPLWVGA 275
Cdd:PLN02330 182 lqTDLCALP----FSSGTTGISKGVMLTHRN---LVANLCSSLFSVGPEMIgqvvtLGLIPFFHIYGITGICCATLRNKG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 276 TTVMLPTFQPQKVWEVLLSSKapmVTVFMAVPTIYSKLIQHyeqhftqPRVQDFvrAACKERIRLMVSGSSALPQPTLLR 355
Cdd:PLN02330 255 KVVVMSRFELRTFLNALITQE---VSFAPIVPPIILNLVKN-------PIVEEF--DLSKLKLQAIMTAAAPLAPELLTA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 356 WE-EITGHTLLERYGMTE---IGMALSNPLKGPRIP--GAVGVPLPGVEVRIVmtnatsttiaegNSRETQVRPglEGKE 429
Cdd:PLN02330 323 FEaKFPGVQVQEAYGLTEhscITLTHGDPEKGHGIAkkNSVGFILPNLEVKFI------------DPDTGRSLP--KNTP 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 430 GELMVRGDQVFTEYWNKPEATRESFTEDGWFKTGDTAVYKN-GVYWIMGRTSvDIIKSGGYKISALEVERHLLAHPDITD 508
Cdd:PLN02330 389 GELCVRSQCVMQGYYNNKEETDRTIDEDGWLHTGDIGYIDDdGDIFIVDRIK-ELIKYKGFQVAPAELEAILLTHPSVED 467
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 509 VAVIGARDATWGQKVTAVVQLKRGRSMTLSELKTWAREHMAPYTIPTGLVLVEEMPRNQMGKVNKKdLLK 578
Cdd:PLN02330 468 AAVVPLPDEEAGEIPAACVVINPKAKESEEDILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRR-LLK 536
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
151-571 |
2.37e-28 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 120.14 E-value: 2.37e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 151 DSQSSLLVAGQPYADTMEPLAhrlglpylQLPPTSSLSSLLEAPENQPEPGITDWAqrpAMIIYTSGTTGRPKGVLHTHS 230
Cdd:PRK06060 100 NTEPALVVTSDALRDRFQPSR--------VAEAAELMSEAARVAPGGYEPMGGDAL---AYATYTSGTTGPPKAAIHRHA 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 231 NIQAMVQGLVSE-WGWSRDDVILHTLPLHHVHGIVNKLLCPLWVGATTVMLPTFQPQKVWEVLLSSKAPmvTVFMAVPTI 309
Cdd:PRK06060 169 DPLTFVDAMCRKaLRLTPEDTGLCSARMYFAYGLGNSVWFPLATGGSAVINSAPVTPEAAAILSARFGP--SVLYGVPNF 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 310 YSkliqhyeqhftqpRVQDFVRAACKERIRLMVSGSSALPQPTLLRWEEITGHT-LLERYGMTEIGMA-LSNPLKGPRiP 387
Cdd:PRK06060 247 FA-------------RVIDSCSPDSFRSLRCVVSAGEALELGLAERLMEFFGGIpILDGIGSTEVGQTfVSNRVDEWR-L 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 388 GAVGVPLPGVEVRIVMTNATSTTiaegnsretqvrpglEGKEGELMVRGDQVFTEYWNKPEATresFTEDGWFKTGDTaV 467
Cdd:PRK06060 313 GTLGRVLPPYEIRVVAPDGTTAG---------------PGVEGDLWVRGPAIAKGYWNRPDSP---VANEGWLDTRDR-V 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 468 YKNGVYWIM-GRTSVDIIKSGGYKISALEVERHLLAHPDITDVAVIGARDATWGQKVTAVVQLKRGRSMTLSELKTWARE 546
Cdd:PRK06060 374 CIDSDGWVTyRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSGATIDGSVMRDLHRG 453
|
410 420
....*....|....*....|....*...
gi 1367478878 547 ---HMAPYTIPTGLVLVEEMPRNQMGKV 571
Cdd:PRK06060 454 llnRLSAFKVPHRFAVVDRLPRTPNGKL 481
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
182-466 |
3.04e-28 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 119.21 E-value: 3.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 182 PPTSSLSSLLEAPenqPEPGITDWAQR-----PAMIIYTSGTTGRPKGVLHTHSNIQAMVQGLVSEWGWSRDD--VILHT 254
Cdd:PRK08180 182 RAATPFAALLATP---PTAAVDAAHAAvgpdtIAKFLFTSGSTGLPKAVINTHRMLCANQQMLAQTFPFLAEEppVLVDW 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 255 LPLHHVHGIVNKLLCPLWVGATtvmL------PTfqPQKVWEVL--LSSKAPmvTVFMAVPTIYSKLIQHYEQhftqprv 326
Cdd:PRK08180 259 LPWNHTFGGNHNLGIVLYNGGT---LyiddgkPT--PGGFDETLrnLREISP--TVYFNVPKGWEMLVPALER------- 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 327 QDFVRAACKERIRLMVSGSSALPQPTLLRWEEITGHTLLER------YGMTEIG-MALS--NPLKGpriPGAVGVPLPGV 397
Cdd:PRK08180 325 DAALRRRFFSRLKLLFYAGAALSQDVWDRLDRVAEATCGERirmmtgLGMTETApSATFttGPLSR---AGNIGLPAPGC 401
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1367478878 398 EVRIVmtnatsttiaegnsretqvrPgLEGKEgELMVRGDQVFTEYWNKPEATRESFTEDGWFKTGDTA 466
Cdd:PRK08180 402 EVKLV--------------------P-VGGKL-EVRVKGPNVTPGYWRAPELTAEAFDEEGYYRSGDAV 448
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
62-576 |
4.54e-28 |
|
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: 117.54 E-value: 4.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 62 QVYR--DKLAIVDDSGSHSYRDLYGSSRGLAGRIKAaLDCPSGDLQGkrisfLCANDA-SYTVAQWASWMCGGTAVPLYR 138
Cdd:cd17644 9 QVERtpDAVAVVFEDQQLTYEELNTKANQLAHYLQS-LGVKSESLVG-----ICVERSlEMIIGLLAILKAGGAYVPLDP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 139 EHPPSELEYIISDSQSSLLVAgqpyadtmeplahrlglpylqlpptsslsslleAPENQpepgitdwaqrpAMIIYTSGT 218
Cdd:cd17644 83 NYPQERLTYILEDAQISVLLT---------------------------------QPENL------------AYVIYTSGS 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 219 TGRPKGVLHTHSNIQAMVQGLVSEWGWSRDDVILHTLPLHhVHGIVNKLLCPLWVGATTVMLPT---FQPQKVWEVLLSS 295
Cdd:cd17644 118 TGKPKGVMIEHQSLVNLSHGLIKEYGITSSDRVLQFASIA-FDVAAEEIYVTLLSGATLVLRPEemrSSLEDFVQYIQQW 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 296 KapmVTVFMAVPTIYSKLIQHYEQHftqprvqdfvRAACKERIRLMVSGSSALpQPTLLR-WEEITGH--TLLERYGMTE 372
Cdd:cd17644 197 Q---LTVLSLPPAYWHLLVLELLLS----------TIDLPSSLRLVIVGGEAV-QPELVRqWQKNVGNfiQLINVYGPTE 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 373 IGMA-----LSNPLKGPRIPGAVGVPLPGVEVRIVmtnatsttiaegNSRETQVRPGLEGkegELMVRGDQVFTEYWNKP 447
Cdd:cd17644 263 ATIAatvcrLTQLTERNITSVPIGRPIANTQVYIL------------DENLQPVPVGVPG---ELHIGGVGLARGYLNRP 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 448 EATRESFTEDGW--------FKTGDTAVY-KNGVYWIMGRTSvDIIKSGGYKISALEVERHLLAHPDITDVAVIGARDAT 518
Cdd:cd17644 328 ELTAEKFISHPFnsseserlYKTGDLARYlPDGNIEYLGRID-NQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQP 406
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1367478878 519 WGQKVTAVVQLKRGRSMTLSELKTWAREHMAPYTIPTGLVLVEEMPRNQMGKVNKKDL 576
Cdd:cd17644 407 GNKRLVAYIVPHYEESPSTVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
121-576 |
6.11e-28 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 119.88 E-value: 6.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 121 VAQWASWMCGGTAVPLYREHPPSELEYIISDSQSSLLVagqpyadTMEPLAHRLGLPYLQLPPTSSLSSLLEAPENQPEP 200
Cdd:PRK12467 3160 VALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLL-------TQAHLLEQLPAPAGDTALTLDRLDLNGYSENNPST 3232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 201 GITdwAQRPAMIIYTSGTTGRPKGVLHTHSNIQAMVQGLVSEWGWSRDDVILHTLPLhHVHGIVNKLLCPLWVGATTVML 280
Cdd:PRK12467 3233 RVM--GENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDRVLLFMSF-SFDGAQERFLWTLICGGCLVVR 3309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 281 P--TFQPQKVWEVLLsskAPMVTVFMAVPTiyskliqhYEQHFtqprVQDFVRAACKeRIRLMVSGSSALPQPTLLRWE- 357
Cdd:PRK12467 3310 DndLWDPEELWQAIH---AHRISIACFPPA--------YLQQF----AEDAGGADCA-SLDIYVFGGEAVPPAAFEQVKr 3373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 358 EITGHTLLERYGMTEIG---MALSNPLKGPRIPGAV--GVPLPGVEVRIVmtnatsttiaegnsrETQVRPGLEGKEGEL 432
Cdd:PRK12467 3374 KLKPRGLTNGYGPTEAVvtvTLWKCGGDAVCEAPYApiGRPVAGRSIYVL---------------DGQLNPVPVGVAGEL 3438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 433 MVRGDQVFTEYWNKPEATRESFTEDGW-------FKTGDTAVYK-NGVYWIMGRtsVD-IIKSGGYKISALEVERHLLAH 503
Cdd:PRK12467 3439 YIGGVGLARGYHQRPSLTAERFVADPFsgsggrlYRTGDLARYRaDGVIEYLGR--IDhQVKIRGFRIELGEIEARLLQH 3516
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1367478878 504 PDITDVAVIgARDATWGQKVTAVVQLKRGRSMTLSELKTWAREHMAPYTIPTGLVLVEEMPRNQMGKVNKKDL 576
Cdd:PRK12467 3517 PSVREAVVL-ARDGAGGKQLVAYVVPADPQGDWRETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKAL 3588
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
194-570 |
3.20e-27 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 116.39 E-value: 3.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 194 PENQPEPgiTDwAQRPAMIIYTSGTTGRPKGVLHThsniQA--MVQGLVS-EW----------------GWsrddVILHT 254
Cdd:PRK00174 235 DECEPEP--MD-AEDPLFILYTSGSTGKPKGVLHT----TGgyLVYAAMTmKYvfdykdgdvywctadvGW----VTGHS 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 255 lplHHVHGivnkllcPLWVGATTVML---PTF-QPQKVWEVLLSSKapmVTVFMAVPTIYSKLIQHYEQHftqprvqdfV 330
Cdd:PRK00174 304 ---YIVYG-------PLANGATTLMFegvPNYpDPGRFWEVIDKHK---VTIFYTAPTAIRALMKEGDEH---------P 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 331 RAACKERIRLMvsGSSALP-QPTLLRW-EEITGHtllER------YGMTEIGMALSNPLKG--PRIPGAVGVPLPGVEVR 400
Cdd:PRK00174 362 KKYDLSSLRLL--GSVGEPiNPEAWEWyYKVVGG---ERcpivdtWWQTETGGIMITPLPGatPLKPGSATRPLPGIQPA 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 401 IVMtnatsttiAEGNSREtqvrpglEGKEGEL--------MVRGdqvfteYWNKPEATRESF--TEDGWFKTGDTAVY-K 469
Cdd:PRK00174 437 VVD--------EEGNPLE-------GGEGGNLvikdpwpgMMRT------IYGDHERFVKTYfsTFKGMYFTGDGARRdE 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 470 NGVYWIMGRTSvDIIKSGGYKISALEVERHLLAHPDITDVAVIGARDATWGQKVTAVVQLKRGR--SMTL-SELKTWARE 546
Cdd:PRK00174 496 DGYYWITGRVD-DVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLKGGEepSDELrKELRNWVRK 574
|
410 420
....*....|....*....|....
gi 1367478878 547 HMAPYTIPTGLVLVEEMPRNQMGK 570
Cdd:PRK00174 575 EIGPIAKPDVIQFAPGLPKTRSGK 598
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
181-547 |
3.75e-27 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 115.77 E-value: 3.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 181 LPPTSSLSSLLEAPENQPEPGITDWAQRPAMIIYTSGTTGRPKGVLHTHSNIQAMVQGLVSEWGWSRDDVILHTLPLHHV 260
Cdd:PRK09274 148 LWGGTTLATLLRDGAAAPFPMADLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEIDLPTFPLFAL 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 261 HGIVnkllcplwVGATTV---MLPT----FQPQKVWEVLLSSKapmVTVFMAVPTIYSKLIQHYEQH-FTQPRVqdfvra 332
Cdd:PRK09274 228 FGPA--------LGMTSVipdMDPTrpatVDPAKLFAAIERYG---VTNLFGSPALLERLGRYGEANgIKLPSL------ 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 333 ackeriRLMVSGSSALPQPTLLRWEEITGHT--LLERYGMTE------IGMalSNPLKGPRI---PGA---VGVPLPGVE 398
Cdd:PRK09274 291 ------RRVISAGAPVPIAVIERFRAMLPPDaeILTPYGATEalpissIES--REILFATRAatdNGAgicVGRPVDGVE 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 399 VRIVmtNATSTTIAEGnsreTQVRPGLEGKEGELMVRGDQVFTEYWNKPEATRESFTEDG----WFKTGDTAvYK--NGV 472
Cdd:PRK09274 363 VRII--AISDAPIPEW----DDALRLATGEIGEIVVAGPMVTRSYYNRPEATRLAKIPDGqgdvWHRMGDLG-YLdaQGR 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 473 YWIMGRTSVDIIKSGG--YKIsalEVERHLLAHPDITDVAVIGARDATwGQKVTAVVQLKRGRSMTLS----ELKTWARE 546
Cdd:PRK09274 436 LWFCGRKAHRVETAGGtlYTI---PCERIFNTHPGVKRSALVGVGVPG-AQRPVLCVELEPGVACSKSalyqELRALAAA 511
|
.
gi 1367478878 547 H 547
Cdd:PRK09274 512 H 512
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
206-579 |
6.03e-27 |
|
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: 113.82 E-value: 6.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 206 AQRPAMIIYTSGTTGRPKGVLHTHSNIQAmvqGLVSEWGW---SRDDVILH-TLPLHHVHGIVNkLLCPLWVGATTVML- 280
Cdd:cd05974 84 ADDPMLLYFTSGTTSKPKLVEHTHRSYPV---GHLSTMYWiglKPGDVHWNiSSPGWAKHAWSC-FFAPWNAGATVFLFn 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 281 -PTFQPQKVWEVLLSSKapmVTVFMAVPTIYSKLIQhyeqhftqprvQDFVRAACKerIRLMVSGSSALPQPTLLRWEEI 359
Cdd:cd05974 160 yARFDAKRVLAALVRYG---VTTLCAPPTVWRMLIQ-----------QDLASFDVK--LREVVGAGEPLNPEVIEQVRRA 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 360 TGHTLLERYGMTEIGMALSNPLKGPRIPGAVGVPLPGVevRIVMTNATsttiaegnsretqvrpGLEGKEGEL-MVRGDQ 438
Cdd:cd05974 224 WGLTIRDGYGQTETTALVGNSPGQPVKAGSMGRPLPGY--RVALLDPD----------------GAPATEGEVaLDLGDT 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 439 ----VFTEYWNKPEATRESFtEDGWFKTGDTAVY-KNGVYWIMGRTSvDIIKSGGYKISALEVERHLLAHPDITDVAVIG 513
Cdd:cd05974 286 rpvgLMKGYAGDPDKTAHAM-RGGYYRTGDIAMRdEDGYLTYVGRAD-DVFKSSDYRISPFELESVLIEHPAVAEAAVVP 363
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 514 ARDATWGQKVTAVVQL----KRGRSMTLSELKtWAREHMAPYTIPTGLVLVeEMPRNQMGKVNKKDLLKH 579
Cdd:cd05974 364 SPDPVRLSVPKAFIVLragyEPSPETALEIFR-FSRERLAPYKRIRRLEFA-ELPKTISGKIRRVELRRR 431
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
46-576 |
1.33e-26 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 115.53 E-value: 1.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 46 ARQAAAGDSAPvfsraqvyrdklAIVDDSGSHSYRDLYGSSRGLAGRIKAAldcpsGDLQGKRISFLCANDASYTVAQWA 125
Cdd:PRK10252 465 AQQAAKTPDAP------------ALADARYQFSYREMREQVVALANLLRER-----GVKPGDSVAVALPRSVFLTLALHA 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 126 SWMCGGTAVPLYREHPPSELEYIISDSQSSLLVAGQPYADTmepLAHRLGLPYLQLPptsslsSLLEAPENQPEPgiTDW 205
Cdd:PRK10252 528 IVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITTADQLPR---FADVPDLTSLCYN------APLAPQGAAPLQ--LSQ 596
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 206 AQRPAMIIYTSGTTGRPKGVLHTHsniQAMVQGLV---SEWGWSRDDVILHTLPL-HHVHgiVNKLLCPLWVGATTVMLP 281
Cdd:PRK10252 597 PHHTAYIIFTSGSTGRPKGVMVGQ---TAIVNRLLwmqNHYPLTADDVVLQKTPCsFDVS--VWEFFWPFIAGAKLVMAE 671
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 282 tfqPQkvwevllSSKAPmvtVFMAvptiysKLIQHYE---QHFTQPRVQDFV--------RAACKERIRLMVSGsSALPQ 350
Cdd:PRK10252 672 ---PE-------AHRDP---LAMQ------QFFAEYGvttTHFVPSMLAAFVasltpegaRQSCASLRQVFCSG-EALPA 731
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 351 PTLLRWEEITGHTLLERYGMTEIGMALSN-PLKGPRIPGAVGVPLP-GVEV-----RIVmtnatsttiaegNSRETQVRP 423
Cdd:PRK10252 732 DLCREWQQLTGAPLHNLYGPTEAAVDVSWyPAFGEELAAVRGSSVPiGYPVwntglRIL------------DARMRPVPP 799
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 424 GLegkEGELMVRGDQVFTEYWNKPEATRESFTEDGW------FKTGDTAVYK-NGVYWIMGRtSVDIIKSGGYKISALEV 496
Cdd:PRK10252 800 GV---AGDLYLTGIQLAQGYLGRPDLTASRFIADPFapgermYRTGDVARWLdDGAVEYLGR-SDDQLKIRGQRIELGEI 875
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 497 ERHLLAHPDITDVA----VIGARDATWG---QKVTAVVQlKRGRSMTLSELKTWAREHMAPYTIPTGLVLVEEMPRNQMG 569
Cdd:PRK10252 876 DRAMQALPDVEQAVthacVINQAAATGGdarQLVGYLVS-QSGLPLDTSALQAQLRERLPPHMVPVVLLQLDQLPLSANG 954
|
....*..
gi 1367478878 570 KVNKKDL 576
Cdd:PRK10252 955 KLDRKAL 961
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
61-576 |
3.00e-26 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 114.88 E-value: 3.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 61 AQVYRDKLAIVDDSGSHSYRDLYGSSRGLAGRIKaalDCPSG-DLqgkRISFLCANDASYTVAQWASWMCGGTAVPLYRE 139
Cdd:PRK05691 1141 ARQTPERIALVWDGGSLDYAELHAQANRLAHYLR---DKGVGpDV---CVAIAAERSPQLLVGLLAILKAGGAYVPLDPD 1214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 140 HPPSELEYIISDSQSSLLVAGqpyadtmeplAHRLG-LPYLQLPPTSSLSSL-LEAPENQPePGITDWAQRPAMIIYTSG 217
Cdd:PRK05691 1215 YPAERLAYMLADSGVELLLTQ----------SHLLErLPQAEGVSAIALDSLhLDSWPSQA-PGLHLHGDNLAYVIYTSG 1283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 218 TTGRPKGVLHTHSNIQAMVQGLVSEWGWSRDDVILHTLPLhhvhgivnkllcplwvgattvmlpTFQpQKVWEVLLsska 297
Cdd:PRK05691 1284 STGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKAPI------------------------SFD-VSVWECFW---- 1334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 298 PMVT----VFMAV-----PTIYSKLIQHYEQ---HFTQPRVQDFVR----AACKeRIRLMVSGSSALPQPTLLR-WEEIT 360
Cdd:PRK05691 1335 PLITgcrlVLAGPgehrdPQRIAELVQQYGVttlHFVPPLLQLFIDeplaAACT-SLRRLFSGGEALPAELRNRvLQRLP 1413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 361 GHTLLERYGMTEIGMALSN----PLKGPRIPgaVGVPLPGVEVRIvmtnatsttiaegnsRETQVRPGLEGKEGELMVRG 436
Cdd:PRK05691 1414 QVQLHNRYGPTETAINVTHwqcqAEDGERSP--IGRPLGNVLCRV---------------LDAELNLLPPGVAGELCIGG 1476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 437 DQVFTEYWNKPEATRESFT-----EDG--WFKTGDTAVYK-NGVYWIMGRTSVDiIKSGGYKISALEVERHLLAHPDITD 508
Cdd:PRK05691 1477 AGLARGYLGRPALTAERFVpdplgEDGarLYRTGDRARWNaDGALEYLGRLDQQ-VKLRGFRVEPEEIQARLLAQPGVAQ 1555
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1367478878 509 VAVIgARDATWGQKVTAVVQLKRGRSMTLSELKTWAREHMAPYTIPTGLVLVEEMPRNQMGKVNKKDL 576
Cdd:PRK05691 1556 AAVL-VREGAAGAQLVGYYTGEAGQEAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRAL 1622
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
181-464 |
3.75e-26 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 113.27 E-value: 3.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 181 LPPTS-----SLSSLLEAPENQPEPGITDWAQRPAMIIYTSGTTGRPKGVLHTHSNIQAMVQGLVSEWGWSRDDVILHTL 255
Cdd:PLN02736 190 LPSGTgveivTYSKLLAQGRSSPQPFRPPKPEDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTKFYPSDVHISYL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 256 PLHHVHGIVNKLLCpLWVGATTvmlpTFQPQKVWEVLLSSKAPMVTVFMAVP----TIYSKLI----------------- 314
Cdd:PLN02736 270 PLAHIYERVNQIVM-LHYGVAV----GFYQGDNLKLMDDLAALRPTIFCSVPrlynRIYDGITnavkesgglkerlfnaa 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 315 -QHYEQHFTQPR---------VQDFVRAACKERIRLMVSGSSALpQPTLLRWEEIT-GHTLLERYGMTEIGMALSNPLKG 383
Cdd:PLN02736 345 yNAKKQALENGKnpspmwdrlVFNKIKAKLGGRVRFMSSGASPL-SPDVMEFLRICfGGRVLEGYGMTETSCVISGMDEG 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 384 PRIPGAVGVPLPGVEVRIV----MtNATSttiaegnsrETQVRPglegkEGELMVRGDQVFTEYWNKPEATRESFTEDGW 459
Cdd:PLN02736 424 DNLSGHVGSPNPACEVKLVdvpeM-NYTS---------EDQPYP-----RGEICVRGPIIFKGYYKDEVQTREVIDEDGW 488
|
....*
gi 1367478878 460 FKTGD 464
Cdd:PLN02736 489 LHTGD 493
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
206-576 |
6.23e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 110.51 E-value: 6.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 206 AQRPAMIIYTSGTTGRPKGVLHTHSNIQAMVQGLVSEWGWSRDDVILHTLPLHHVHGIVNKLLCPLWVGATTVMLPTFQP 285
Cdd:PRK08308 100 AEEPSLLQYSSGTTGEPKLIRRSWTEIDREIEAYNEALNCEQDETPIVACPVTHSYGLICGVLAALTRGSKPVIITNKNP 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 286 QKVWEVLLSSKAPMVtvfMAVPTIYSKLIQhyeqhFTQPRVQDFvraackeriRLMVSGSsALPQPTLLRWEEITGHtLL 365
Cdd:PRK08308 180 KFALNILRNTPQHIL---YAVPLMLHILGR-----LLPGTFQFH---------AVMTSGT-PLPEAWFYKLRERTTY-MM 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 366 ERYGMTEIG-MALSNPLkgpRIPGAVGVPLPGVEVrivmtnatSTTIAEGNSRETQVRPGlegkegelmvrgdqvfteyw 444
Cdd:PRK08308 241 QQYGCSEAGcVSICPDM---KSHLDLGNPLPHVSV--------SAGSDENAPEEIVVKMG-------------------- 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 445 nkpeaTRESFTEDGWFKTGDtavyknGVYWIMGRTSvDIIKSGGYKISALEVERHLLAHPDITDVAVIGARDATWGQKVT 524
Cdd:PRK08308 290 -----DKEIFTKDLGYKSER------GTLHFMGRMD-DVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVK 357
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1367478878 525 AVVQLKRGrsMTLSELKTWAREHMAPYTIPTGLVLVEEMPRNQMGKVNKKDL 576
Cdd:PRK08308 358 AKVISHEE--IDPVQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLL 407
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
66-576 |
2.16e-25 |
|
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: 109.49 E-value: 2.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 66 DKLAIVDDSGSHSYRDLYGSSRGLAGRIKAaldcpSGDLQGKRISFLCANDASYTVAQWASWMCGGTAVPLYREHPPSEL 145
Cdd:cd17656 3 DAVAVVFENQKLTYRELNERSNQLARFLRE-----KGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 146 EYIISDSQSSLLVAGQPYADtmePLAHRLGLPYLQLPptsslsslLEAPENQPEPGITDWAQRPAMIIYTSGTTGRPKGV 225
Cdd:cd17656 78 IYIMLDSGVRVVLTQRHLKS---KLSFNKSTILLEDP--------SISQEDTSNIDYINNSDDLLYIIYTSGTTGKPKGV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 226 LHTHSNIQAMVQGLVSEWGWSR-DDVILHTLPLHHV--HGIVNKLLcplwVGATTVMLPTFQPQKVWEVL-LSSKAPMVT 301
Cdd:cd17656 147 QLEHKNMVNLLHFEREKTNINFsDKVLQFATCSFDVcyQEIFSTLL----SGGTLYIIREETKRDVEQLFdLVKRHNIEV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 302 VFMavPTIYSKLIQHYEQHFtqPRVQDFVRAACKERIRLMVSGssalPQPTLLRWEEITGHTlleRYGMTE---IGMALS 378
Cdd:cd17656 223 VFL--PVAFLKFIFSEREFI--NRFPTCVKHIITAGEQLVITN----EFKEMLHEHNVHLHN---HYGPSEthvVTTYTI 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 379 NPlkGPRIP--GAVGVPLPGVEVRIVmtnatsttiaegnSRETQVRPglEGKEGELMVRGDQVFTEYWNKPEATRESFTE 456
Cdd:cd17656 292 NP--EAEIPelPPIGKPISNTWIYIL-------------DQEQQLQP--QGIVGELYISGASVARGYLNRQELTAEKFFP 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 457 DGW------FKTGDTAVY-KNGVYWIMGRTSvDIIKSGGYKISALEVERHLLAHPDITDvAVIGARDATWGQK-----VT 524
Cdd:cd17656 355 DPFdpnermYRTGDLARYlPDGNIEFLGRAD-HQVKIRGYRIELGEIEAQLLNHPGVSE-AVVLDKADDKGEKylcayFV 432
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1367478878 525 AVVQLkrgrsmTLSELKTWAREHMAPYTIPTGLVLVEEMPRNQMGKVNKKDL 576
Cdd:cd17656 433 MEQEL------NISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
130-576 |
1.52e-24 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 109.49 E-value: 1.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 130 GGTAVPLYREHPPSELEYIISDSQSSLLVAGQPYADTMEPLAHRLG-------LPYLQLPPTSSLSSLleapeNQPepgi 202
Cdd:PRK05691 2262 GGAYVPLDPEYPLERLHYMIEDSGIGLLLSDRALFEALGELPAGVArwcleddAAALAAYSDAPLPFL-----SLP---- 2332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 203 tdwaQRPAMIIYTSGTTGRPKGVLHTHSNIQAMVQGLVSEWGWSRDDVILHTLPLhHVHGIVNKLLCPLWVGATTVMlpt 282
Cdd:PRK05691 2333 ----QHQAYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIERFGMRADDCELHFYSI-NFDAASERLLVPLLCGARVVL--- 2404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 283 fQPQKVW---EVLLSSKAPMVTVFMAVPTIYSKLIQHYE-QHFTQPrvqdfvraackerIRLMVSGSSALPQPTLLRWEE 358
Cdd:PRK05691 2405 -RAQGQWgaeEICQLIREQQVSILGFTPSYGSQLAQWLAgQGEQLP-------------VRMCITGGEALTGEHLQRIRQ 2470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 359 ITGHTLL-ERYGMTE-IGMALSNPLKGPRIPGAVGVPLPgvevRIVmtNATSTTIAEGNsretqVRPGLEGKEGELMVRG 436
Cdd:PRK05691 2471 AFAPQLFfNAYGPTEtVVMPLACLAPEQLEEGAASVPIG----RVV--GARVAYILDAD-----LALVPQGATGELYVGG 2539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 437 DQVFTEYWNKPEATRESFTEDGW-------FKTGDTAVYK-NGVYWIMGRTSVDiIKSGGYKISALEVERHLLAHPDITD 508
Cdd:PRK05691 2540 AGLAQGYHDRPGLTAERFVADPFaadggrlYRTGDLVRLRaDGLVEYVGRIDHQ-VKIRGFRIELGEIESRLLEHPAVRE 2618
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1367478878 509 VAVIgARDATWGQK-----VTAVVQLKRGRSMTLSE-LKTWAREHMAPYTIPTGLVLVEEMPRNQMGKVNKKDL 576
Cdd:PRK05691 2619 AVVL-ALDTPSGKQlagylVSAVAGQDDEAQAALREaLKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRAL 2691
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
156-466 |
5.12e-24 |
|
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: 105.98 E-value: 5.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 156 LLVAGQPYADTMEPLAHRLGLPYLQLPP------------TSSLSSLLEAPENQPEPGITDWAQrPAMI---IYTSGTTG 220
Cdd:cd05921 100 LLKPGLVFAQDAAPFARALAAIFPLGTPlvvsrnavagrgAISFAELAATPPTAAVDAAFAAVG-PDTVakfLFTSGSTG 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 221 RPKGVLHTHSNIQAMVQGLVSEWGWSRDD--VILHTLPLHHVHGiVNKLLCPLWVGATTVML----PTfqPQKVWEVLLS 294
Cdd:cd05921 179 LPKAVINTQRMLCANQAMLEQTYPFFGEEppVLVDWLPWNHTFG-GNHNFNLVLYNGGTLYIddgkPM--PGGFEETLRN 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 295 SKAPMVTVFMAVPTIYSKLIQHYEQhftqprvQDFVRAACKERIRLMVSGSSALPQPTLLRWEEI----TGH--TLLERY 368
Cdd:cd05921 256 LREISPTVYFNVPAGWEMLVAALEK-------DEALRRRFFKRLKLMFYAGAGLSQDVWDRLQALavatVGEriPMMAGL 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 369 GMTEIGMALSNPLKGPRIPGAVGVPLPGVEVRIVMTNatsttiaegnsretqvrpgleGKEgELMVRGDQVFTEYWNKPE 448
Cdd:cd05921 329 GATETAPTATFTHWPTERSGLIGLPAPGTELKLVPSG---------------------GKY-EVRVKGPNVTPGYWRQPE 386
|
330
....*....|....*...
gi 1367478878 449 ATRESFTEDGWFKTGDTA 466
Cdd:cd05921 387 LTAQAFDEEGFYCLGDAA 404
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
60-583 |
1.08e-23 |
|
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341242 [Multi-domain] Cd Length: 481 Bit Score: 104.55 E-value: 1.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 60 RAQVYRDKLAIVDDSGSHSYRDLYGSSRGLAGRIkaaldCPSGDLQGKRISfLCANDASYT-VAQWASWMCGGTAVPLYR 138
Cdd:cd05918 8 RARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHL-----RSLGVGPGVFVP-LCFEKSKWAvVAMLAVLKAGGAFVPLDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 139 EHPPSELEYIISDSQSSLLVAGQPyadtmeplahrlglpylqlpptsslsslleapenqpepgitdwaQRPAMIIYTSGT 218
Cdd:cd05918 82 SHPLQRLQEILQDTGAKVVLTSSP--------------------------------------------SDAAYVIFTSGS 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 219 TGRPKGVLHTHSNIQAMVQGLVSEWGWSRDDVIL----HTLPLHhvhgiVNKLLCPLWVGATTVMLPTFQ-PQKVWEVLL 293
Cdd:cd05918 118 TGKPKGVVIEHRALSTSALAHGRALGLTSESRVLqfasYTFDVS-----ILEIFTTLAAGGCLCIPSEEDrLNDLAGFIN 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 294 SSKapmVTVFMAVPTIySKLIQHyeqhftqprvQDFVRaackerIRLMVSGSSALPQPTLLRWEEitGHTLLERYGMTE- 372
Cdd:cd05918 193 RLR---VTWAFLTPSV-ARLLDP----------EDVPS------LRTLVLGGEALTQSDVDTWAD--RVRLINAYGPAEc 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 373 -IGMALSNPLKGPRiPGAVGVPLPGVeVRIVmtnatsttiaegnSRETQVRPGLEGKEGELMVRGDQVFTEYWNKPEATR 451
Cdd:cd05918 251 tIAATVSPVVPSTD-PRNIGRPLGAT-CWVV-------------DPDNHDRLVPIGAVGELLIEGPILARGYLNDPEKTA 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 452 ESFTED-GW------------FKTGDTAVY-KNGVYWIMGRTSvDIIKSGGYKISALEVERHLLAH-PDITDVAV--IGA 514
Cdd:cd05918 316 AAFIEDpAWlkqegsgrgrrlYRTGDLVRYnPDGSLEYVGRKD-TQVKIRGQRVELGEIEHHLRQSlPGAKEVVVevVKP 394
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 515 RDATWGQKVTAVVQLKRGRSMT-----------------LSELKTWAREHMAPYTIPTGLVLVEEMPRNQMGKVNKKdLL 577
Cdd:cd05918 395 KDGSSSPQLVAFVVLDGSSSGSgdgdslflepsdefralVAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRR-AL 473
|
....*.
gi 1367478878 578 KHFFPS 583
Cdd:cd05918 474 RELAES 479
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
109-576 |
1.57e-23 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 104.34 E-value: 1.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 109 ISFLCANDASYTVAQWASWMCGGTAVPLYREHPPSELEYIISDSQSSLLVAGQPYAdtmePLAHRLGLPYLQLPPTSS-- 186
Cdd:PRK13388 55 VGVLLGNTPEMLFWLAAAALGGYVLVGLNTTRRGAALAADIRRADCQLLVTDAEHR----PLLDGLDLPGVRVLDVDTpa 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 187 -LSSLLEAPENQPEPGITdwAQRPAMIIYTSGTTGRPKGVLHTHSNIQAMVQGLVSEWGWSRDDVILHTLPLHHVHGIVN 265
Cdd:PRK13388 131 yAELVAAAGALTPHREVD--AMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLTRDDVCYVSMPLFHSNAVMA 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 266 KLLCPLWVGATTVMLPTFQPqkvwevllSSKAPMV-----TVF----------MAVPtiyskliQHYEQHFTQPRVQdFV 330
Cdd:PRK13388 209 GWAPAVASGAAVALPAKFSA--------SGFLDDVrrygaTYFnyvgkplayiLATP-------ERPDDADNPLRVA-FG 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 331 RAACKERIRlmvsgssalpqptllRWEEITGHTLLERYGMTEIGMALSNPLKGPriPGAVGVPLPGVEVRIVMTnATSTT 410
Cdd:PRK13388 273 NEASPRDIA---------------EFSRRFGCQVEDGYGSSEGAVIVVREPGTP--PGSIGRGAPGVAIYNPET-LTECA 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 411 IAEGNSRETQVRPglEGKEGELMVR-GDQVFTEYWNKPEATRESFtEDGWFKTGDTAvYKNGVYWI--MGRTSvDIIKSG 487
Cdd:PRK13388 335 VARFDAHGALLNA--DEAIGELVNTaGAGFFEGYYNNPEATAERM-RHGMYWSGDLA-YRDADGWIyfAGRTA-DWMRVD 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 488 GYKISALEVERHLLAHPDITDVAVIGARDATWGQKVTAVVQLKRGRSMTLSELKTW--AREHMAPYTIPTGLVLVEEMPR 565
Cdd:PRK13388 410 GENLSAAPIERILLRHPAINRVAVYAVPDERVGDQVMAALVLRDGATFDPDAFAAFlaAQPDLGTKAWPRYVRIAADLPS 489
|
490
....*....|.
gi 1367478878 566 NQMGKVNKKDL 576
Cdd:PRK13388 490 TATNKVLKREL 500
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
210-468 |
2.63e-23 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 104.36 E-value: 2.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 210 AMIIYTSGTTGRPKGVLHTH----SNIqAMVQGLVSEWGWSRDDVILHTLPLHHVHGiVNKLLCPLWVGATTVML----P 281
Cdd:PRK12582 223 AKYLFTSGSTGMPKAVINTQrmmcANI-AMQEQLRPREPDPPPPVSLDWMPWNHTMG-GNANFNGLLWGGGTLYIddgkP 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 282 TfqPQKVWEVL--LSSKAPmvTVFMAVPTIYSKLIQHYEQhftqprvQDFVRAACKERIRLMVSGSSALPQPTLLRWEE- 358
Cdd:PRK12582 301 L--PGMFEETIrnLREISP--TVYGNVPAGYAMLAEAMEK-------DDALRRSFFKNLRLMAYGGATLSDDLYERMQAl 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 359 ---ITGH--TLLERYGMTEIGMALSNPLKGPRIPGAVGVPLPGVEVRIVMTnatsttiaegnsretqvrpgleGKEGELM 433
Cdd:PRK12582 370 avrTTGHriPFYTGYGATETAPTTTGTHWDTERVGLIGLPLPGVELKLAPV----------------------GDKYEVR 427
|
250 260 270
....*....|....*....|....*....|....*
gi 1367478878 434 VRGDQVFTEYWNKPEATRESFTEDGWFKTGDTAVY 468
Cdd:PRK12582 428 VKGPNVTPGYHKDPELTAAAFDEEGFYRLGDAARF 462
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
60-478 |
1.19e-22 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 103.32 E-value: 1.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 60 RAQVYRDKLAI--VDDSGSH----SYRDLYGSSRGLAgrikAALDCPSGdlQGKRISFLCANDASYTVAQWASWMCGGTA 133
Cdd:PRK05691 18 RAAQTPDRLALrfLADDPGEgvvlSYRDLDLRARTIA----AALQARAS--FGDRAVLLFPSGPDYVAAFFGCLYAGVIA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 134 VPLY-----REHPPSELEYIISDSQSSLLVAGqpyADTMEPLAHRLGLPYLQLPPTSSLSSLLEAP-ENQPEPGITdwAQ 207
Cdd:PRK05691 92 VPAYppesaRRHHQERLLSIIADAEPRLLLTV---ADLRDSLLQMEELAAANAPELLCVDTLDPALaEAWQEPALQ--PD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 208 RPAMIIYTSGTTGRPKGVLHTHSNIQAMVQGLVSEWG--WSRDDVILHTLPLHHVHGIVNKLLCPLWVGATTV-MLPTFq 284
Cdd:PRK05691 167 DIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGidLNPDDVIVSWLPLYHDMGLIGGLLQPIFSGVPCVlMSPAY- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 285 pqkvwevllsskapmvtvFMAVPTIYSKLIQHYEQhfTQPRVQDFVRAACKERI-------------RLMVSGSSALPQP 351
Cdd:PRK05691 246 ------------------FLERPLRWLEAISEYGG--TISGGPDFAYRLCSERVsesalerldlsrwRVAYSGSEPIRQD 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 352 TLLRWEE------ITGHTLLERYGMTEIGMALSNPLKGPRIP------------------GAV----GVPLPGVEVRIVm 403
Cdd:PRK05691 306 SLERFAEkfaacgFDPDSFFASYGLAEATLFVSGGRRGQGIPaleldaealarnraepgtGSVlmscGRSQPGHAVLIV- 384
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1367478878 404 tnatsttiaegnsrETQVRPGL-EGKEGELMVRGDQVFTEYWNKPEATRESFTE-DG--WFKTGDTAVYKNGVYWIMGR 478
Cdd:PRK05691 385 --------------DPQSLEVLgDNRVGEIWASGPSIAHGYWRNPEASAKTFVEhDGrtWLRTGDLGFLRDGELFVTGR 449
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
61-576 |
1.43e-22 |
|
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: 100.71 E-value: 1.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 61 AQVYRDKLAIVDDSGSHSYRDLYGSSRGLAGRIKaalDCpsGDLQGKRISFLCANDASYTVAQWASWMCGGTAVPLYREH 140
Cdd:cd17645 8 VERTPDHVAVVDRGQSLTYKQLNEKANQLARHLR---GK--GVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 141 PPSELEYIISDSQSSLLvagqpyadtmeplahrlglpylqlpptsslsslLEAPENQpepgitdwaqrpAMIIYTSGTTG 220
Cdd:cd17645 83 PGERIAYMLADSSAKIL---------------------------------LTNPDDL------------AYVIYTSGSTG 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 221 RPKGVLHTHsniqamvQGLVSEWGWSRDDVILHTLPLHHVH------GIVNKLLCPLWVGATTVMLPTFQPQKVWEVLLS 294
Cdd:cd17645 118 LPKGVMIEH-------HNLVNLCEWHRPYFGVTPADKSLVYasfsfdASAWEIFPHLTAGAALHVVPSERRLDLDALNDY 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 295 SKAPMVTVFMaVPTiyskliQHYEQhFTQPRVQDFvraackeriRLMVSGSSALPqptllRWEEiTGHTLLERYGMTEIG 374
Cdd:cd17645 191 FNQEGITISF-LPT------GAAEQ-FMQLDNQSL---------RVLLTGGDKLK-----KIER-KGYKLVNNYGPTENT 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 375 -MALSNPLKGPRIPGAVGVPLPGVEVRIvmtnatsttIAEGNsretQVRPglEGKEGELMVRGDQVFTEYWNKPEATRES 453
Cdd:cd17645 248 vVATSFEIDKPYANIPIGKPIDNTRVYI---------LDEAL----QLQP--IGVAGELCIAGEGLARGYLNRPELTAEK 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 454 FTEDGW------FKTGDTAVYKN-GVYWIMGRTSvDIIKSGGYKISALEVERHLLAHPDITDVAVIGARDATWGQKVTAV 526
Cdd:cd17645 313 FIVHPFvpgermYRTGDLAKFLPdGNIEFLGRLD-QQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAY 391
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1367478878 527 VQLKRgrSMTLSELKTWAREHMAPYTIPTGLVLVEEMPRNQMGKVNKKDL 576
Cdd:cd17645 392 VTAPE--EIPHEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
210-478 |
2.69e-22 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 101.21 E-value: 2.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 210 AMIIYTSGTTGRPKGVLHTHSNIQAMVQGLvSEW------GWSRDDVILHTLPLHHV--HGIVNKLL---CPLWVGATTV 278
Cdd:PTZ00216 267 ALIMYTSGTTGDPKGVMHTHGSLTAGILAL-EDRlndligPPEEDETYCSYLPLAHImeFGVTNIFLargALIGFGSPRT 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 279 MLPTF-QPQKVwevlLSSKAPMVTVfmAVPTIY--------SKL----------IQH------------YEQHFTQPRVQ 327
Cdd:PTZ00216 346 LTDTFaRPHGD----LTEFRPVFLI--GVPRIFdtikkaveAKLppvgslkrrvFDHayqsrlralkegKDTPYWNEKVF 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 328 DFVRAACKERIRLMVSGSSALPQPTLlRWEEITGHTLLERYGMTEIGMALSNPLKGPRIPGAVGVPLPGVEVRIVMTnat 407
Cdd:PTZ00216 420 SAPRAVLGGRVRAMLSGGGPLSAATQ-EFVNVVFGMVIQGWGLTETVCCGGIQRTGDLEPNAVGQLLKGVEMKLLDT--- 495
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1367478878 408 sttiaEGNSRETQVRPglegkEGELMVRGDQVFTEYWNKPEATRESFTEDGWFKTGDTA-VYKNGVYWIMGR 478
Cdd:PTZ00216 496 -----EEYKHTDTPEP-----RGEILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGsIAANGTLRIIGR 557
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
61-578 |
4.35e-22 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 99.58 E-value: 4.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 61 AQVYRDKLAIVDDSGSHSYRDLYGSSRGLAGRIKAaLDCPSGD---LQGKR-----ISFLCANDAsytvaqwaswmcgGT 132
Cdd:PRK04813 12 AQTQPDFPAYDYLGEKLTYGQLKEDSDALAAFIDS-LKLPDKSpiiVFGHMspemlATFLGAVKA-------------GH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 133 A-VPLyREHPPSE-LEYIISDSQSSLLVAgqpyadtmeplAHRLGLPYLQLPpTSSLSSLLEAPENQPEPGITDWAQ--R 208
Cdd:PRK04813 78 AyIPV-DVSSPAErIEMIIEVAKPSLIIA-----------TEELPLEILGIP-VITLDELKDIFATGNPYDFDHAVKgdD 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 209 PAMIIYTSGTTGRPKGVLHTHSNIQAMVQGLVSEWGWSRDDVILHTLPLHHVHGIVNKLLCpLWVGATTVMLP---TFQP 285
Cdd:PRK04813 145 NYYIIFTSGTTGKPKGVQISHDNLVSFTNWMLEDFALPEGPQFLNQAPYSFDLSVMDLYPT-LASGGTLVALPkdmTANF 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 286 QKVWEVLLSSKapmVTVFMAVPTiyskliqhyeqhftqprvqdFVRAAckerirLMVSGSSALPQPTLLRW----EEITG 361
Cdd:PRK04813 224 KQLFETLPQLP---INVWVSTPS--------------------FADMC------LLDPSFNEEHLPNLTHFlfcgEELPH 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 362 HT---LLER---------YGMTEIGMALSNPL-------KGPRIPgaVGVPLPGVEVRIVMTNATsttiaegnsretqvr 422
Cdd:PRK04813 275 KTakkLLERfpsatiyntYGPTEATVAVTSIEitdemldQYKRLP--IGYAKPDSPLLIIDEEGT--------------- 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 423 PGLEGKEGELMVRGDQVFTEYWNKPEATRESF-TEDGW--FKTGDTAVYKNGVYWIMGRtsVDI-IKSGGYKISALEVER 498
Cdd:PRK04813 338 KLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFfTFDGQpaYHTGDAGYLEDGLLFYQGR--IDFqIKLNGYRIELEEIEQ 415
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 499 HLLAHPDI-TDVAVIGARDATWGQKVTAVV----QLKRGRSMTlSELKTWAREHMAPYTIPTGLVLVEEMPRNQMGKVNK 573
Cdd:PRK04813 416 NLRQSSYVeSAVVVPYNKDHKVQYLIAYVVpkeeDFEREFELT-KAIKKELKERLMEYMIPRKFIYRDSLPLTPNGKIDR 494
|
....*
gi 1367478878 574 KDLLK 578
Cdd:PRK04813 495 KALIE 499
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
115-513 |
5.12e-22 |
|
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: 100.12 E-value: 5.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 115 NDASYTVAQWASWMCGGTAVPLYREHPPSELEYIISDSQSSLLVAgqpyaDTMEPLAhRLGLPYLQLPPTSSLSSLLEAP 194
Cdd:cd05933 42 NSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSEANILVV-----ENQKQLQ-KILQIQDKLPHLKAIIQYKEPL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 195 ENQpEPGITDWA--------------------QRP---AMIIYTSGTTGRPKGVLHTHSNI----QAMVQGLVSEWGWSR 247
Cdd:cd05933 116 KEK-EPNLYSWDefmelgrsipdeqldaiissQKPnqcCTLIYTSGTTGMPKGVMLSHDNItwtaKAASQHMDLRPATVG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 248 DDVILHTLPLHHVHGIVNKLLCPLWVGATTvmlpTF-QPQKV-WEVLLSSKAPMVTVFMAVPTIYSKLIQHYEQHFTQPR 325
Cdd:cd05933 195 QESVVSYLPLSHIAAQILDIWLPIKVGGQV----YFaQPDALkGTLVKTLREVRPTAFMGVPRVWEKIQEKMKAVGAKSG 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 326 VQDFVRAACKERIRL---MVSGSSALPQPTLLRWEE-------------------------ITGHTL----------LER 367
Cdd:cd05933 271 TLKRKIASWAKGVGLetnLKLMGGESPSPLFYRLAKklvfkkvrkalgldrcqkfftgaapISRETLefflslnipiMEL 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 368 YGMTEIGMA--LSNPlKGPRIpGAVGVPLPGVEVRIVMTNatsttiAEGNsretqvrpglegkeGELMVRGDQVFTEYWN 445
Cdd:cd05933 351 YGMSETSGPhtISNP-QAYRL-LSCGKALPGCKTKIHNPD------ADGI--------------GEICFWGRHVFMGYLN 408
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 446 KPEATRESFTEDGWFKTGDTA-VYKNGVYWIMGRTSVDIIKSGGYKISALEVERHLLAH-PDITDVAVIG 513
Cdd:cd05933 409 MEDKTEEAIDEDGWLHSGDLGkLDEDGFLYITGRIKELIITAGGENVPPVPIEDAVKKElPIISNAMLIG 478
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
209-572 |
7.33e-22 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 100.43 E-value: 7.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 209 PAMIIYTSGTTGRPKGVLHTHSNIQAMVQGLVSEWGWSRDDVILHTLPLHHVHGIVNKLLCPLWVGATTVMLPTfqP--- 285
Cdd:PRK06814 795 PAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARIDFSPEDKVFNALPVFHSFGLTGGLVLPLLSGVKVFLYPS--Plhy 872
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 286 QKVWEVLLSSKApmvTVFMAVPTI---YSKLIQHYeqhftqprvqDFvraackERIRLMVSGSSALPQPTLLRWEEITGH 362
Cdd:PRK06814 873 RIIPELIYDTNA---TILFGTDTFlngYARYAHPY----------DF------RSLRYVFAGAEKVKEETRQTWMEKFGI 933
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 363 TLLERYGMTEIG--MALSNPLKGPriPGAVGVPLPGVEVRIVMTnatsttiaegnsretqvrPGL-EGkeGELMVRGDQV 439
Cdd:PRK06814 934 RILEGYGVTETApvIALNTPMHNK--AGTVGRLLPGIEYRLEPV------------------PGIdEG--GRLFVRGPNV 991
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 440 FTEYW--NKPEATREsfTEDGWFKTGD-TAVYKNGVYWIMGRTSvDIIKSGGYKISALEVERhlLAH---PDiTDVAVIG 513
Cdd:PRK06814 992 MLGYLraENPGVLEP--PADGWYDTGDiVTIDEEGFITIKGRAK-RFAKIAGEMISLAAVEE--LAAelwPD-ALHAAVS 1065
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 514 ARDATWGQKvtaVVQLKRGRSMTLSELKTWAREHMAP-YTIPTGLVLVEEMPRNQMGKVN 572
Cdd:PRK06814 1066 IPDARKGER---IILLTTASDATRAAFLAHAKAAGASeLMVPAEIITIDEIPLLGTGKID 1122
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
206-540 |
1.01e-21 |
|
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: 98.30 E-value: 1.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 206 AQRPAMIIYTSGTTGRPKGVLHTHSNIQAMVQGLVSEWGWSRDDVILHTLPLHhvhgivnKLLCPLwVGATTV---MLPT 282
Cdd:cd05910 84 ADEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGEVDLATFPLF-------ALFGPA-LGLTSVipdMDPT 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 283 ----FQPQKVWEVLLSSKapmVTVFMAVPTIYSKLIQHYEQH-FTQP---RVQDF---VRAACKERIRLMVSGSSALPQP 351
Cdd:cd05910 156 rparADPQKLVGAIRQYG---VSIVFGSPALLERVARYCAQHgITLPslrRVLSAgapVPIALAARLRKMLSDEAEILTP 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 352 tllrweeitghtllerYGMTE---IGMALSNPLKGPRIPGA-------VGVPLPGVEVRIVmtNATSTTIAE-GNSRETQ 420
Cdd:cd05910 233 ----------------YGATEalpVSSIGSRELLATTTAATsggagtcVGRPIPGVRVRII--EIDDEPIAEwDDTLELP 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 421 vrpglEGKEGELMVRGDQVFTEYWNKPEATRESFTEDG----WFKTGDTAVYKN-GVYWIMGRTSVDIIKSGGyKISALE 495
Cdd:cd05910 295 -----RGEIGEITVTGPTVTPTYVNRPVATALAKIDDNsegfWHRMGDLGYLDDeGRLWFCGRKAHRVITTGG-TLYTEP 368
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1367478878 496 VERHLLAHPDITDVAVIGARDATwGQKVTAVVQLKRGRSMTLSEL 540
Cdd:cd05910 369 VERVFNTHPGVRRSALVGVGKPG-CQLPVLCVEPLPGTITPRARL 412
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
194-578 |
2.12e-21 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 97.37 E-value: 2.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 194 PENQPEPGITDWAQRPAMIIYTSGTTGRPKGVLHTHSNIQAMVQGLVSEWgwsRDDVI--LHTLPLHHVHGIVnKLLCPL 271
Cdd:PRK07445 107 PPPLPSQGILPNLETGWIMIPTGGSSGQIRFAIHTWETLTASVQGFQRYF---QLQQVnsFCVLPLYHVSGLM-QFMRSF 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 272 WVGATTVMLPtfqpqkvWEVLLSSKAPMVTV---FMA-VPTiysKLiqhyeQHFTQPRVQdFVRaackeRIRLMVSGSSA 347
Cdd:PRK07445 183 LTGGKLVILP-------YKRLKSGQELPPNPsdfFLSlVPT---QL-----QRLLQLRPQ-WLA-----QFRTILLGGAP 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 348 lPQPTLLRWEEITGHTLLERYGMTEIG--MALSNP---LKGPRipgAVGVPLPGVEVRIVmtnatsttiaegnsretqvr 422
Cdd:PRK07445 242 -AWPSLLEQARQLQLRLAPTYGMTETAsqIATLKPddfLAGNN---SSGQVLPHAQITIP-------------------- 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 423 pglEGKEGELMVRGDQVFTEYWNKPEATRESFTED--GWFKtgdtavyKNGVYWIMGRTSVDIIkSGGYKISALEVERHL 500
Cdd:PRK07445 298 ---ANQTGNITIQAQSLALGYYPQILDSQGIFETDdlGYLD-------AQGYLHILGRNSQKII-TGGENVYPAEVEAAI 366
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1367478878 501 LAHPDITDVAVIGARDATWGQKVTAVVQLKRGrSMTLSELKTWAREHMAPYTIPTGLVLVEEMPRNQMGKVNKKDLLK 578
Cdd:PRK07445 367 LATGLVQDVCVLGLPDPHWGEVVTAIYVPKDP-SISLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQQ 443
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
72-564 |
2.96e-21 |
|
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: 97.53 E-value: 2.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 72 DDSGSHSYRDL-------YGSSRGLAGRIKAALDCPSGDLQGKRISFLCANDASYTVAQWASWMCGGTAVPLYREHPPSE 144
Cdd:cd17632 52 PATGRTTLRLLprfetitYAELWERVGAVAAAHDPEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQ 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 145 LEYIISDSQSSLL--------VAGQPYADTMEPL------------AHRLGL--PYLQLPPTSSLSSLLE---------- 192
Cdd:cd17632 132 LAPILAETEPRLLavsaehldLAVEAVLEGGTPPrlvvfdhrpevdAHRAALesARERLAAVGIPVTTLTliavrgrdlp 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 193 -APENQPEPGitdwAQRPAMIIYTSGTTGRPKGVLHTHSNIQAMVQGLVSEWGWSRDDVI-LHTLPLHHVHGiVNKLLCP 270
Cdd:cd17632 212 pAPLFRPEPD----DDPLALLIYTSGSTGTPKGAMYTERLVATFWLKVSSIQDIRPPASItLNFMPMSHIAG-RISLYGT 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 271 LWVGATTVMLPTFQPQKVWEVLLSSKApmvTVFMAVPTIYSKLIQHYEQHFTQPRVQDFVRAACKERIR----------- 339
Cdd:cd17632 287 LARGGTAYFAAASDMSTLFDDLALVRP---TELFLVPRVCDMLFQRYQAELDRRSVAGADAETLAERVKaelrervlggr 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 340 --LMVSGSSALPQPTLLRWEEITGHTLLERYGMTEIGmalsnplkgpripgavGVPLPGVEVRIVMTNATSTTIAE-GNS 416
Cdd:cd17632 364 llAAVCGSAPLSAEMKAFMESLLDLDLHDGYGSTEAG----------------AVILDGVIVRPPVLDYKLVDVPElGYF 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 417 RETQVRPglegkEGELMVRGDQVFTEYWNKPEATRESFTEDGWFKTGDtavykngvywIMGRTSVD----------IIK- 485
Cdd:cd17632 428 RTDRPHP-----RGELLVKTDTLFPGYYKRPEVTAEVFDEDGFYRTGD----------VMAELGPDrlvyvdrrnnVLKl 492
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 486 SGGYKISALEVERHLLAHPDITDVAVIGARDATW-------GQKVTAVVQLKRGRSMTLSELKTWAREH-MAPYTIPTGl 557
Cdd:cd17632 493 SQGEFVTVARLEAVFAASPLVRQIFVYGNSERAYllavvvpTQDALAGEDTARLRAALAESLQRIAREAgLQSYEIPRD- 571
|
....*..
gi 1367478878 558 VLVEEMP 564
Cdd:cd17632 572 FLIETEP 578
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
74-571 |
4.02e-21 |
|
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: 97.56 E-value: 4.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 74 SGSHSYRDLYGSSRGLAGRIKAAldcpsGDLQGKRISFLCANDASYTVAQWASWMCGGTAVPLYREHPPSELEYIISDSQ 153
Cdd:cd05968 89 SRTLTYGELLYEVKRLANGLRAL-----GVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAE 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 154 SSLLVAG----------QPYADTMEPLAH-----------RLGLPYLqlPPTSSLSSLLEAPENQPEPGITDWAQRPAMI 212
Cdd:cd05968 164 AKALITAdgftrrgrevNLKEEADKACAQcptvekvvvvrHLGNDFT--PAKGRDLSYDEEKETAGDGAERTESEDPLMI 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 213 IYTSGTTGRPKGVLHTHSN--IQA---------MVQGLVSEW----GWSRDDVILhtlplhhvhgivnklLCPLWVGATT 277
Cdd:cd05968 242 IYTSGTTGKPKGTVHVHAGfpLKAaqdmyfqfdLKPGDLLTWftdlGWMMGPWLI---------------FGGLILGATM 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 278 VM---LPTF-QPQKVWEVLLSSKapmVTVFMAVPTIYSKLIqhyeqhftqPRVQDFVRAACKERIRLMVS-GSSALPQPT 352
Cdd:cd05968 307 VLydgAPDHpKADRLWRMVEDHE---ITHLGLSPTLIRALK---------PRGDAPVNAHDLSSLRVLGStGEPWNPEPW 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 353 LLRWEEI-TGHTLLERY-GMTEI-GMALSNPLKGPRIPGAVGVPLPGVEVRIVmtnatsttiaegNSRETQVRPglegKE 429
Cdd:cd05968 375 NWLFETVgKGRNPIINYsGGTEIsGGILGNVLIKPIKPSSFNGPVPGMKADVL------------DESGKPARP----EV 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 430 GEL--------MVRGdqvfteYWNKPEATRESFTE--DGWFKTGDTAVYKNGVYW-IMGRtSVDIIKSGGYKISALEVER 498
Cdd:cd05968 439 GELvllapwpgMTRG------FWRDEDRYLETYWSrfDNVWVHGDFAYYDEEGYFyILGR-SDDTINVAGKRVGPAEIES 511
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1367478878 499 HLLAHPDITDVAVIGARDATWGQKVTAVVQLKRGRSMT---LSELKTWAREHMAPYTIPTGLVLVEEMPRNQMGKV 571
Cdd:cd05968 512 VLNAHPAVLESAAIGVPHPVKGEAIVCFVVLKPGVTPTealAEELMERVADELGKPLSPERILFVKDLPKTRNAKV 587
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
170-549 |
5.40e-21 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 96.09 E-value: 5.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 170 LAHRLGLPYLQLPPTSSLSSLLEAPENQPepgiTDW-AQRPAMIIYTSGTTGRPKGVLHTHSNIQAMVQGLVSEWGWSRD 248
Cdd:PRK09029 101 LDFALVLEGENTFSALTSLHLQLVEGAHA----VAWqPQRLATMTLTSGSTGLPKAAVHTAQAHLASAEGVLSLMPFTAQ 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 249 DVILHTLPLHHVHG--IVnkllcplW----VGATTVmLPTFQPqkvwevlLSSKAPMVTVFMAVPTIYSKLIQHYEQHFT 322
Cdd:PRK09029 177 DSWLLSLPLFHVSGqgIV-------WrwlyAGATLV-VRDKQP-------LEQALAGCTHASLVPTQLWRLLDNRSEPLS 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 323 QPRVqdfvraackerirLMvsGSSALPqptllrweeitgHTLLER-----------YGMTEigMA------LSNPLKGpr 385
Cdd:PRK09029 242 LKAV-------------LL--GGAAIP------------VELTEQaeqqgircwcgYGLTE--MAstvcakRADGLAG-- 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 386 ipgaVGVPLPGVEVRIVmtnatsttiaegnsretqvrpglegkEGELMVRGDQVFTEYWNKPEATreSFT-EDGWFKTGD 464
Cdd:PRK09029 291 ----VGSPLPGREVKLV--------------------------DGEIWLRGASLALGYWRQGQLV--PLVnDEGWFATRD 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 465 TAVYKNGVYWIMGRTSVDIIkSGGYKISALEVERHLLAHPDITDVAVIGARDATWGQKVTAVVQLKRGRsmTLSELKTWA 544
Cdd:PRK09029 339 RGEWQNGELTILGRLDNLFF-SGGEGIQPEEIERVINQHPLVQQVFVVPVADAEFGQRPVAVVESDSEA--AVVNLAEWL 415
|
....*
gi 1367478878 545 REHMA 549
Cdd:PRK09029 416 QDKLA 420
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
173-576 |
8.53e-21 |
|
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: 95.23 E-value: 8.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 173 RLGLPYLQLPPTS------------SLSSLLEAPENQPEPGITDWAQRP---------AMIIYTSGTTGRPKGVLHTHSN 231
Cdd:cd17654 63 FLGAAYAPIDPASpeqrsltvmkkcHVSYLLQNKELDNAPLSFTPEHRHfnirtdeclAYVIHTSGTTGTPKIVAVPHKC 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 232 IQAMVQGLVSEWGWSRDDVILHTLPLHHVHGIVNKLLCpLWVGATTVMLPT---FQPQKVWEVLLssKAPMVTVFMAVPT 308
Cdd:cd17654 143 ILPNIQHFRSLFNITSEDILFLTSPLTFDPSVVEIFLS-LSSGATLLIVPTsvkVLPSKLADILF--KRHRITVLQATPT 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 309 IYSKliqhyeqhFTQPRVQDFVRAACKErIRLMVSGSSALPQPTLLR-W-EEITGHTLLERYGMTEIGM-ALSNPLKGPR 385
Cdd:cd17654 220 LFRR--------FGSQSIKSTVLSATSS-LRVLALGGEPFPSLVILSsWrGKGNRTRIFNIYGITEVSCwALAYKVPEED 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 386 IPGAVGVPLPGVEVRIVMTNatsttiaeGNSRETQVRPGLEGKEGELmvrgdqvfTEYWNKPEATresftedgWFKTGDT 465
Cdd:cd17654 291 SPVQLGSPLLGTVIEVRDQN--------GSEGTGQVFLGGLNRVCIL--------DDEVTVPKGT--------MRATGDF 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 466 AVYKNGVYWIMGRTSvDIIKSGGYKISALEVERHLLAHPDITDVAVigardatWGQKVTAVVQLKRGRSMTLSELKTWAR 545
Cdd:cd17654 347 VTVKDGELFFLGRKD-SQIKRRGKRINLDLIQQVIESCLGVESCAV-------TLSDQQRLIAFIVGESSSSRIHKELQL 418
|
410 420 430
....*....|....*....|....*....|.
gi 1367478878 546 EHMAPYTIPTGLVLVEEMPRNQMGKVNKKDL 576
Cdd:cd17654 419 TLLSSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
206-578 |
3.02e-20 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 94.96 E-value: 3.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 206 AQRPAMIIYTSGTTGRPKGVLHTHSNIqaMVQGLVS---EWGWSRDDVILHTLPLHHVHGIVNKLLCPLWVGATTVML-- 280
Cdd:PLN02654 274 AEDPLFLLYTSGSTGKPKGVLHTTGGY--MVYTATTfkyAFDYKPTDVYWCTADCGWITGHSYVTYGPMLNGATVLVFeg 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 281 -PTF-QPQKVWEVLLSSKapmVTVFMAVPTIYSKLIQHYEQHFTQprvqdfvraacKERIRLMVSGSSALP-QPTLLRW- 356
Cdd:PLN02654 352 aPNYpDSGRCWDIVDKYK---VTIFYTAPTLVRSLMRDGDEYVTR-----------HSRKSLRVLGSVGEPiNPSAWRWf 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 357 EEITGHT---LLERYGMTEIGMALSNPLKG--PRIPGAVGVPLPGVEVRIVMTNATSTtiaEGN-SRETQVRPGLEGKEG 430
Cdd:PLN02654 418 FNVVGDSrcpISDTWWQTETGGFMITPLPGawPQKPGSATFPFFGVQPVIVDEKGKEI---EGEcSGYLCVKKSWPGAFR 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 431 ELMVRGDQVFTEYWnKPEAtresftedGWFKTGDTAVY-KNGVYWIMGRTSvDIIKSGGYKISALEVERHLLAHPDITDV 509
Cdd:PLN02654 495 TLYGDHERYETTYF-KPFA--------GYYFSGDGCSRdKDGYYWLTGRVD-DVINVSGHRIGTAEVESALVSHPQCAEA 564
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1367478878 510 AVIGARDATWGQKVTAVVQLKRGRSMTlSELKT----WAREHMAPYTIPTGLVLVEEMPRNQMGKVNKKDLLK 578
Cdd:PLN02654 565 AVVGIEHEVKGQGIYAFVTLVEGVPYS-EELRKslilTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRK 636
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
106-513 |
4.41e-20 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 94.14 E-value: 4.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 106 GKRISFLCANDASYTVAQWASWMCGGTAVPLYREHPPSELEYIISDSQSSL----------LVAGQP------------- 162
Cdd:PLN02861 102 GDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVSIafvqeskissILSCLPkcssnlktivsfg 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 163 -YADTMEPLAHRLGLPYLQLPPTSSLSSL-LEAPENQPEPGITdwaqrpamIIYTSGTTGRPKGVLHTHSNIQAMVQG-- 238
Cdd:PLN02861 182 dVSSEQKEEAEELGVSCFSWEEFSLMGSLdCELPPKQKTDICT--------IMYTSGTTGEPKGVILTNRAIIAEVLStd 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 239 ---LVSEWGWSRDDVILHTLPLHHVHGIVNKLLC-------PLWVGATTVMLPTFQPQKvwevllsskaPmvTVFMAVPT 308
Cdd:PLN02861 254 hllKVTDRVATEEDSYFSYLPLAHVYDQVIETYCiskgasiGFWQGDIRYLMEDVQALK----------P--TIFCGVPR 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 309 IY------------------SKLIQH------------YEQHFTQPRVQDFVRAACKE----RIRLMVSGSSALPQPTLL 354
Cdd:PLN02861 322 VYdriytgimqkissggmlrKKLFDFaynyklgnlrkgLKQEEASPRLDRLVFDKIKEglggRVRLLLSGAAPLPRHVEE 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 355 RWEEITGHTLLERYGMTE-IGMALSNPLKGPRIPGAVGVPLPGVEVRIVmtnatstTIAEGNSRETQVRPglegkEGELM 433
Cdd:PLN02861 402 FLRVTSCSVLSQGYGLTEsCGGCFTSIANVFSMVGTVGVPMTTIEARLE-------SVPEMGYDALSDVP-----RGEIC 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 434 VRGDQVFTEYWNKPEATRESFTeDGWFKTGDTAVYK-NGVYWIMGRTSvDIIK-SGGYKISALEVERHLLAHPDITDVAV 511
Cdd:PLN02861 470 LRGNTLFSGYHKRQDLTEEVLI-DGWFHTGDIGEWQpNGAMKIIDRKK-NIFKlSQGEYVAVENLENTYSRCPLIASIWV 547
|
..
gi 1367478878 512 IG 513
Cdd:PLN02861 548 YG 549
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
66-576 |
7.47e-20 |
|
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: 92.46 E-value: 7.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 66 DKLAIVDDSGSHSYRDLYGSSRGLAGRIKAALDCPSGDLQGkriSFLcanDAS--YTVAQWASWMCGGTAVPLYREHPPS 143
Cdd:cd17648 2 DRVAVVYGDKRLTYRELNERANRLAHYLLSVAEIRPDDLVG---LVL---DKSelMIIAILAVWKAGAAYVPIDPSYPDE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 144 ELEYIISDSQSSLLVAGqpyadtmeplahrlglpylqlpptsslsslleapenqpepgITDWAqrpaMIIYTSGTTGRPK 223
Cdd:cd17648 76 RIQFILEDTGARVVITN-----------------------------------------STDLA----YAIYTSGTTGKPK 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 224 GVLHTHSNIQAMVQGLVSEWGWSR--DDVILhTLPLHHVHGIVNKLLCPLWVGATTVMLP---TFQPQKVWEVLLSSKap 298
Cdd:cd17648 111 GVLVEHGSVVNLRTSLSERYFGRDngDEAVL-FFSNYVFDFFVEQMTLALLNGQKLVVPPdemRFDPDRFYAYINREK-- 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 299 mVTVFMAVPTiyskLIQHYeqhftqprvqDFVRAACKERIRLMvsgSSALPQPTLLRWEEITGHTLLERYGMTEIGM-AL 377
Cdd:cd17648 188 -VTYLSGTPS----VLQQY----------DLARLPHLKRVDAA---GEEFTAPVFEKLRSRFAGLIINAYGPTETTVtNH 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 378 SNPLKGP-RIPGAVGVPLPGVEVRIVmtnatsttiaegnSRETQVRPglEGKEGELMVRGDQVFTEYWNKPEATRESFTE 456
Cdd:cd17648 250 KRFFPGDqRFDKSLGRPVRNTKCYVL-------------NDAMKRVP--VGAVGELYLGGDGVARGYLNRPELTAERFLP 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 457 DGWFKTGDTA------VYKNG--VYWI-------MGRTSVDiIKSGGYKISALEVERHLLAHPDITDVAVIGARDATW-- 519
Cdd:cd17648 315 NPFQTEQERArgrnarLYKTGdlVRWLpsgeleyLGRNDFQ-VKIRGQRIEPGEVEAALASYPGVRECAVVAKEDASQaq 393
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1367478878 520 --GQKVTAVVQLKRGRSMTLSELKTWAREHMAPYTIPTGLVLVEEMPRNQMGKVNKKDL 576
Cdd:cd17648 394 srIQKYLVGYYLPEPGHVPESDLLSFLRAKLPRYMVPARLVRLEGIPVTINGKLDVRAL 452
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
206-564 |
7.97e-20 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 93.62 E-value: 7.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 206 AQRP---AMIIYTSGTTGRPKGVLHTHSNIQAMVQGLVSEWGWSRDDVILHTLPLHHVHGIVNKLLCPLWVGATTVMLPT 282
Cdd:PRK08043 361 KQQPedaALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPS 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 283 FQPQKVWEVLLSSKApmVTVFMAVPTiyskLIQHYEQhFTQPrvQDFVraackeRIRLMVSGSSALPQPTLLRWEEITGH 362
Cdd:PRK08043 441 PLHYRIVPELVYDRN--CTVLFGTST----FLGNYAR-FANP--YDFA------RLRYVVAGAEKLQESTKQLWQDKFGL 505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 363 TLLERYGMTEIG--MALSNPLKGPriPGAVGVPLPGVEVRIVMTnatsttiaegnsretqvrPGLEgKEGELMVRGDQVF 440
Cdd:PRK08043 506 RILEGYGVTECApvVSINVPMAAK--PGTVGRILPGMDARLLSV------------------PGIE-QGGRLQLKGPNIM 564
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 441 TEY--------WNKPEATR-ESFTEDGWFKTGD-TAVYKNGVYWIMGRTSvDIIKSGGYKISALEVER-HLLAHPDITDV 509
Cdd:PRK08043 565 NGYlrvekpgvLEVPTAENaRGEMERGWYDTGDiVRFDEQGFVQIQGRAK-RFAKIAGEMVSLEMVEQlALGVSPDKQHA 643
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1367478878 510 AVIGArDATWGQkvtAVVQLKRGRSMTLSELKTWAREHMAP-YTIPTGLVLVEEMP 564
Cdd:PRK08043 644 TAIKS-DASKGE---ALVLFTTDSELTREKLQQYAREHGVPeLAVPRDIRYLKQLP 695
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
209-578 |
1.11e-19 |
|
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: 92.49 E-value: 1.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 209 PAMIIYTSGTTGRPKGVLHTH--SNIQAMVQGLVSEWGWSRDDVILHTLPLHHVHGivnklLCPLWV-----GATTVMLP 281
Cdd:cd05915 155 ACGMAYTTGTTGLPKGVVYSHraLVLHSLAASLVDGTALSEKDVVLPVVPMFHVNA-----WCLPYAatlvgAKQVLPGP 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 282 TFQPQKVWEVLLSSKapmVTVFMAVPTIYSKLiqhyeqhftqPRVQDFVRAACKERIRLMVSGSSalPQPTLLRWEEITG 361
Cdd:cd05915 230 RLDPASLVELFDGEG---VTFTAGVPTVWLAL----------ADYLESTGHRLKTLRRLVVGGSA--APRSLIARFERMG 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 362 HTLLERYGMTEI-GMalsnplkgpripGAVGVPLPGVEvrivmtnatstTIAEGNSRETQVRPGL--------------- 425
Cdd:cd05915 295 VEVRQGYGLTETsPV------------VVQNFVKSHLE-----------SLSEEEKLTLKAKTGLpiplvrlrvadeegr 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 426 ----EGKEGELM-VRGDQVFTEYWNKPEATRESFTEDGWFKTGDTAVYKNGVYWIMGRTSVDIIKSGGYKISALEVERHL 500
Cdd:cd05915 352 pvpkDGKALGEVqLKGPWITGGYYGNEEATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENAL 431
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1367478878 501 LAHPDITDVAVIGARDATWGQKVTAVVQLKRGRSMTLSELKTWAREHMAPYTIPTGLVLVEEMPRNQMGKVNKKDLLK 578
Cdd:cd05915 432 MGHPKVKEAAVVAIPHPKWQERPLAVVVPRGEKPTPEELNEHLLKAGFAKWQLPDAYVFAEEIPRTSAGKFLKRALRE 509
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
206-516 |
1.13e-19 |
|
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: 92.17 E-value: 1.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 206 AQRPAMIIYTSGTTGRPKGVLHTHSNIQAMVQGLVSEWGWSRDDVILHTLPLHHVHGIVNKLLCPLWVGATTVMLPTfqp 285
Cdd:cd05908 105 ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGMNQYLMPT--- 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 286 qkvwevllsskapmvTVFMAVPTIYSKLIQHYE------QHFTQPRVQDFVRAACKE-----RIRLMVSGSSALpQPTLL 354
Cdd:cd05908 182 ---------------RLFIRRPILWLKKASEHKativssPNFGYKYFLKTLKPEKANdwdlsSIRMILNGAEPI-DYELC 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 355 rwEEITGH---------TLLERYGMTEIGMALSNP----------------LKGPRIPG------------AVGVPLPGV 397
Cdd:cd05908 246 --HEFLDHmskyglkrnAILPVYGLAEASVGASLPkaqspfktitlgrrhvTHGEPEPEvdkkdsecltfvEVGKPIDET 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 398 EVRIVmtnatsttiaegnSRETQVRPglEGKEGELMVRGDQVFTEYWNKPEATRESFTEDGWFKTGDTAVYKNGVYWIMG 477
Cdd:cd05908 324 DIRIC-------------DEDNKILP--DGYIGHIQIRGKNVTPGYYNNPEATAKVFTDDGWLKTGDLGFIRNGRLVITG 388
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1367478878 478 RTSvDIIKSGGYKISALEVERHL--LAHPDITDVAVIGARD 516
Cdd:cd05908 389 REK-DIIFVNGQNVYPHDIERIAeeLEGVELGRVVACGVNN 428
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
66-576 |
4.84e-19 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 90.43 E-value: 4.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 66 DKLAIVDDSGSHSYRDLYGSSRGLAGRIKAAldcpsGDLQGKRISFLCANDASYTVAQWASWMCGGTAVPLYREHPPSEL 145
Cdd:PRK10946 38 DAIAVICGERQFSYRELNQASDNLACSLRRQ-----GIKPGDTALVQLGNVAEFYITFFALLKLGVAPVNALFSHQRSEL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 146 -EYI--------ISDSQSSLLvAGQPYADTMepLAHRLGLPYLQL---PPTSSLSSLLEAPENQPEPGITDwAQRPAMII 213
Cdd:PRK10946 113 nAYAsqiepallIADRQHALF-SDDDFLNTL--VAEHSSLRVVLLlndDGEHSLDDAINHPAEDFTATPSP-ADEVAFFQ 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 214 YTSGTTGRPKGVLHTHSNIQAMVQGLVSEWGWSRDDVILHTLPLHHvhgivN-KLLCP-----LWVGATTVMLPTFQPQK 287
Cdd:PRK10946 189 LSGGSTGTPKLIPRTHNDYYYSVRRSVEICGFTPQTRYLCALPAAH-----NyPMSSPgalgvFLAGGTVVLAPDPSATL 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 288 VWEVLLSSKapmVTVFMAVPTIYSKLIQHyeqhftqprVQDFVRAACKERIRLMVSGSSALPQPTLLRWEEITGHTLLER 367
Cdd:PRK10946 264 CFPLIEKHQ---VNVTALVPPAVSLWLQA---------IAEGGSRAQLASLKLLQVGGARLSETLARRIPAELGCQLQQV 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 368 YGMTEiGMALSNPLKGP--RIPGAVGVPL-PGVEVRIVMtnatsttiAEGNsretqvrPGLEGKEGELMVRGDQVFTEYW 444
Cdd:PRK10946 332 FGMAE-GLVNYTRLDDSdeRIFTTQGRPMsPDDEVWVAD--------ADGN-------PLPQGEVGRLMTRGPYTFRGYY 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 445 NKPEATRESFTEDGWFKTGD-TAVYKNGVYWIMGRTSvDIIKSGGYKISALEVERHLLAHPDITDVAVIGARDATWGQKV 523
Cdd:PRK10946 396 KSPQHNASAFDANGFYCSGDlVSIDPDGYITVVGREK-DQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKS 474
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1367478878 524 TAVVQLKrgRSMTLSELKTWAREH-MAPYTIPTGLVLVEEMPRNQMGKVNKKDL 576
Cdd:PRK10946 475 CAFLVVK--EPLKAVQLRRFLREQgIAEFKLPDRVECVDSLPLTAVGKVDKKQL 526
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
78-580 |
3.49e-18 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 88.33 E-value: 3.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 78 SYRDLYGSSRGLAGRIKAaldcpSGDLQGKRISFLCANDASYTVAQWA----SWMCggtaVPLYREHPPSELEYIISDSQ 153
Cdd:PLN02430 78 TYKEVYEEVLQIGSALRA-----SGAEPGSRVGIYGSNCPQWIVAMEAcaahSLIC----VPLYDTLGPGAVDYIVDHAE 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 154 SSLL-VAGQPYADTMEP---LAHRLGL---------------PYLQLPPTSSLSSLLEAPENQPEPgitdWAQRP---AM 211
Cdd:PLN02430 149 IDFVfVQDKKIKELLEPdckSAKRLKAivsftsvteeesdkaSQIGVKTYSWIDFLHMGKENPSET----NPPKPldiCT 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 212 IIYTSGTTGRPKGVLHTHSNIQAMVQGL-----VSEWGWSRDDVILHTLPLHHV-------------------HGIVNKL 267
Cdd:PLN02430 225 IMYTSGTSGDPKGVVLTHEAVATFVRGVdlfmeQFEDKMTHDDVYLSFLPLAHIldrmieeyffrkgasvgyyHGDLNAL 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 268 ------LCP-LWVGATTVMlptfqpQKVWEVL---LSSKAPMVTVfmavptIYSKLIQH--------YEQHFTQPrVQDF 329
Cdd:PLN02430 305 rddlmeLKPtLLAGVPRVF------ERIHEGIqkaLQELNPRRRL------IFNALYKYklawmnrgYSHKKASP-MADF 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 330 -----VRAACKERIRLMVSGSSalpqPTLLRWEEITGHT----LLERYGMTEI--GMALSNPLKGPRIpGAVGVPlpgve 398
Cdd:PLN02430 372 lafrkVKAKLGGRLRLLISGGA----PLSTEIEEFLRVTscafVVQGYGLTETlgPTTLGFPDEMCML-GTVGAP----- 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 399 vrivmtnATSTTIAEGNSRETQVRPGLEGKEGELMVRGDQVFTEYWNKPEATRESFtEDGWFKTGDTA-VYKNGVYWIMG 477
Cdd:PLN02430 442 -------AVYNELRLEEVPEMGYDPLGEPPRGEICVRGKCLFSGYYKNPELTEEVM-KDGWFHTGDIGeILPNGVLKIID 513
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 478 RTSvDIIK-SGGYKISALEVERHLLAHPDITDVAVIGardATWGQKVTAVVQLKRgrsmtlSELKTWARE--HMAPYTIP 554
Cdd:PLN02430 514 RKK-NLIKlSQGEYVALEYLENVYGQNPIVEDIWVYG---DSFKSMLVAVVVPNE------ENTNKWAKDngFTGSFEEL 583
|
570 580
....*....|....*....|....*.
gi 1367478878 555 TGLVLVEEMPRNQMGKVNKKDLLKHF 580
Cdd:PLN02430 584 CSLPELKEHILSELKSTAEKNKLRGF 609
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
32-498 |
4.06e-18 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 87.74 E-value: 4.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 32 LLRQVLRRAYTSTRARQAAAGDsAPVFsraqvyrdklaivddsgsHSYRDLYGSSRGLAGRIKAAldcpsGDLQGKRISF 111
Cdd:PRK07768 4 FTEKMYANARTSPRGMVTGEPD-APVR------------------HTWGEVHERARRIAGGLAAA-----GVGPGDAVAV 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 112 LCANDASYTVAQWASWMCGGTAVPLYREHPPSELEYIISDS-------QSSLLVAGQPYADTMEPLAHRlGLPYLqlppt 184
Cdd:PRK07768 60 LAGAPVEIAPTAQGLWMRGASLTMLHQPTPRTDLAVWAEDTlrvigmiGAKAVVVGEPFLAAAPVLEEK-GIRVL----- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 185 sSLSSLLEAPENQPEPGITDwaqRPAMIIYTSGTTGRPKGVLHTHSNIQAMVQGLVSEWGWSRD-DVILHTLPLHHVHGI 263
Cdd:PRK07768 134 -TVADLLAADPIDPVETGED---DLALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEFDVEtDVMVSWLPLFHDMGM 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 264 VNKLLCPLWVGATTVmlptfqpqKVwevllsskAPMvtVFMAVPTIYSKLIQHYE------QHFTQPRVQDFVRAACKER 337
Cdd:PRK07768 210 VGFLTVPMYFGAELV--------KV--------TPM--DFLRDPLLWAELISKYRgtmtaaPNFAYALLARRLRRQAKPG 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 338 ------IRLMVSGSSALPQPTLLRWEEITG------HTLLERYGMTEIGMALSNPLKG--------------------PR 385
Cdd:PRK07768 272 afdlssLRFALNGAEPIDPADVEDLLDAGArfglrpEAILPAYGMAEATLAVSFSPCGaglvvdevdadllaalrravPA 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 386 IPGAV------GVPLPGVEVRIVmtnatsttiaegnSRETQVRPglEGKEGELMVRGDQVfTEYWNKPEATRESFTEDGW 459
Cdd:PRK07768 352 TKGNTrrlatlGPPLPGLEVRVV-------------DEDGQVLP--PRGVGVIELRGESV-TPGYLTMDGFIPAQDADGW 415
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1367478878 460 FKTGDTAvY--KNGVYWIMGRTSvDIIKSGGYKISALEVER 498
Cdd:PRK07768 416 LDTGDLG-YltEEGEVVVCGRVK-DVIIMAGRNIYPTDIER 454
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
210-495 |
4.27e-18 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 87.56 E-value: 4.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 210 AMIIYTSGTTGRPKGVLHTHSNIQAMVQGLVSEWGWSRDDVILHTLPLHHVHGIVNKLLCPLWVGATTVMLPT-FQPQKV 288
Cdd:PRK06334 186 AVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSFLPPFHAYGFNSCTLFPLLSGVPVVFAYNpLYPKKI 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 289 WEVLLSSKapmVTVFMAVPTIYSKLIQHYEQHFTqprvqdfvraaCKERIRLMVSGSSALPQPTLLRWEEITGH-TLLER 367
Cdd:PRK06334 266 VEMIDEAK---VTFLGSTPVFFDYILKTAKKQES-----------CLPSLRFVVIGGDAFKDSLYQEALKTFPHiQLRQG 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 368 YGMTEIGMALS-NPLKGPRIPGAVGVPLPGVEVRIVmtnatsttiaegnSRETQVrPGLEGKEGELMVRGDQVFTEYWNK 446
Cdd:PRK06334 332 YGTTECSPVITiNTVNSPKHESCVGMPIRGMDVLIV-------------SEETKV-PVSSGETGLVLTRGTSLFSGYLGE 397
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1367478878 447 PEAtrESFTE---DGWFKTGDTA-VYKNGVYWIMGRTSvDIIKSGGYKIS--ALE 495
Cdd:PRK06334 398 DFG--QGFVElggETWYVTGDLGyVDRHGELFLKGRLS-RFVKIGAEMVSleALE 449
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
495-570 |
2.14e-17 |
|
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: 76.81 E-value: 2.14e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1367478878 495 EVERHLLAHPDITDVAVIGARDATWGQKVTAVVQLKRGRSMTLSELKTWAREHMAPYTIPTGLVLVEEMPRNQMGK 570
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
209-581 |
4.76e-17 |
|
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: 83.94 E-value: 4.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 209 PAMIIYTSGTTGRPKGVLHTHSNIQAMVQGLVSEWGWSRDDVILHTLPLHHVHGIVNKLLCPLWVGATTVMLPTFQPQKV 288
Cdd:cd05940 83 AALYIYTSGTTGLPKAAIISHRRAWRGGAFFAGSGGALPSDVLYTCLPLYHSTALIVGWSACLASGATLVIRKKFSASNF 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 289 WEVLLSSKApmvTVFMAVPTIYSKLIQhyeqhftQPRVQDfvraACKERIRlMVSGSSalpqptlLR---WEEITGH--- 362
Cdd:cd05940 163 WDDIRKYQA---TIFQYIGELCRYLLN-------QPPKPT----ERKHKVR-MIFGNG-------LRpdiWEEFKERfgv 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 363 -TLLERYGMTEIGMALSNPlkgPRIPGAVGV----PLPGVEVRIVMTNATSTTI---AEGNSRETQVrpgleGKEGELMV 434
Cdd:cd05940 221 pRIAEFYAATEGNSGFINF---FGKPGAIGRnpslLRKVAPLALVKYDLESGEPirdAEGRCIKVPR-----GEPGLLIS 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 435 RGDQV--FTEYWNKPEAT----RESFTE-DGWFKTGD-TAVYKNGVYWIMGRTSvDIIKSGGYKISALEVERHLLAHPDI 506
Cdd:cd05940 293 RINPLepFDGYTDPAATEkkilRDVFKKgDAWFNTGDlMRLDGEGFWYFVDRLG-DTFRWKGENVSTTEVAAVLGAFPGV 371
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1367478878 507 TDVAVIGAR-DATWGQKVTAVVQLKRGRSMTLSELKTWAREHMAPYTIPTGLVLVEEMPRNQMGKVNKKDLLKHFF 581
Cdd:cd05940 372 EEANVYGVQvPGTDGRAGMAAIVLQPNEEFDLSALAAHLEKNLPGYARPLFLRLQPEMEITGTFKQQKVDLRNEGF 447
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
209-576 |
2.13e-16 |
|
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: 82.09 E-value: 2.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 209 PAMIIYTSGTTGRPKGVLHTHSNIQAMVQGLVSEWGWSRDDVILHTLPLHHVHGIVNKLLCPLWVGATTVMLPTFQPQKV 288
Cdd:cd05937 89 PAILIYTSGTTGLPKAAAISWRRTLVTSNLLSHDLNLKNGDRTYTCMPLYHGTAAFLGACNCLMSGGTLALSRKFSASQF 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 289 W-EVLLSSKAPMVTV------FMAVP-TIYSKliqhyeQHftqpRVQdfvraackerirlMVSGSSALPQPtllrWEEIT 360
Cdd:cd05937 169 WkDVRDSGATIIQYVgelcryLLSTPpSPYDR------DH----KVR-------------VAWGNGLRPDI----WERFR 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 361 ghtllERYGMTEIG---------MALSNPLKGPRIPGAVGvpLPGVEVRIVMTNATSTTIAEGNSRETQVRP--GL---- 425
Cdd:cd05937 222 -----ERFNVPEIGefyaategvFALTNHNVGDFGAGAIG--HHGLIRRWKFENQVVLVKMDPETDDPIRDPktGFcvra 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 426 -EGKEGELMVR----GDQVFTEYWNKPEATRESFTE------DGWFKTGDTAVY-KNGVYWIMGRTSvDIIKSGGYKISA 493
Cdd:cd05937 295 pVGEPGEMLGRvpfkNREAFQGYLHNEDATESKLVRdvfrkgDIYFRTGDLLRQdADGRWYFLDRLG-DTFRWKSENVST 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 494 LEVERHLLAHPDITDVAVIGARDATW-GQKVTAVVQLKRGRS----MTLSELKTWAREHMAPYTIPTGLVLVEEMPRNQM 568
Cdd:cd05937 374 TEVADVLGAHPDIAEANVYGVKVPGHdGRAGCAAITLEESSAvpteFTKSLLASLARKNLPSYAVPLFLRLTEEVATTDN 453
|
....*...
gi 1367478878 569 GKVNKKDL 576
Cdd:cd05937 454 HKQQKGVL 461
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
143-563 |
2.22e-15 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 79.15 E-value: 2.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 143 SELEYIISDSQSSLLVAGQPYADTMEPLAHRLGLpylqlpptSSLSSLL-EAPENQPE--PGITdwAQRPAMIIYTSGTT 219
Cdd:PRK08279 142 EELVEAFEEARADLARPPRLWVAGGDTLDDPEGY--------EDLAAAAaGAPTTNPAsrSGVT--AKDTAFYIYTSGTT 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 220 GRPKGVLHTHSNIQAMVQGLVSEWGWSRDDVILHTLPLHHVHGIVNKLLCPLWVGATTVMLPTFQPQKVWEVLLSSKApm 299
Cdd:PRK08279 212 GLPKAAVMSHMRWLKAMGGFGGLLRLTPDDVLYCCLPLYHNTGGTVAWSSVLAAGATLALRRKFSASRFWDDVRRYRA-- 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 300 vTVFMAVPTIYSKLIQHYEQHftqprvQDfvRAackERIRLMV-SGssalpqptlLR---WEEITG----HTLLERYGMT 371
Cdd:PRK08279 290 -TAFQYIGELCRYLLNQPPKP------TD--RD---HRLRLMIgNG---------LRpdiWDEFQQrfgiPRILEFYAAS 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 372 EIGMALSNPLKgprIPGAVG-VPLPGVE-VRIVMTNATSTTIAEG-NSRETQVRPGlegkE-GEL--MVRGDQVFTEYwN 445
Cdd:PRK08279 349 EGNVGFINVFN---FDGTVGrVPLWLAHpYAIVKYDVDTGEPVRDaDGRCIKVKPG----EvGLLigRITDRGPFDGY-T 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 446 KPEAT-----RESFTE-DGWFKTGDTAVY-KNGVYWImgrtsVDII------KsgGYKISALEVERHLLAHPDITDVAVI 512
Cdd:PRK08279 421 DPEASekkilRDVFKKgDAWFNTGDLMRDdGFGHAQF-----VDRLgdtfrwK--GENVATTEVENALSGFPGVEEAVVY 493
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1367478878 513 GAR-DATWGQKVTAVVQLKRGRSMTLSELKTWAREHMAPYTIPTGLVLVEEM 563
Cdd:PRK08279 494 GVEvPGTDGRAGMAAIVLADGAEFDLAALAAHLYERLPAYAVPLFVRLVPEL 545
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
126-576 |
1.16e-13 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 74.82 E-value: 1.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 126 SWMCGGTAVPLYREHPPSELEYIISDSQSSLLVAGQPYADtmeplahrLGLPYLQLPPTSSLSSLLEAPENQP------E 199
Cdd:PRK05691 3790 SFKAGAGYLPLDPGLPAQRLQRIIELSRTPVLVCSAACRE--------QARALLDELGCANRPRLLVWEEVQAgevashN 3861
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 200 PGITDWAQRPAMIIYTSGTTGRPKGVLHTHsniQAMVQGLVSE---WGWSRDDVILHTLPLHHVHGIVNKLLCPLWvGAT 276
Cdd:PRK05691 3862 PGIYSGPDNLAYVIYTSGSTGLPKGVMVEQ---RGMLNNQLSKvpyLALSEADVIAQTASQSFDISVWQFLAAPLF-GAR 3937
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 277 TVMLPTFQPQKVWEVLLSSKAPMVTVFMAVPTIYSKLIQHYEQHFtqprvqdfvraackERIRLMVSGSSALPQPTLLRW 356
Cdd:PRK05691 3938 VEIVPNAIAHDPQGLLAHVQAQGITVLESVPSLIQGMLAEDRQAL--------------DGLRWMLPTGEAMPPELARQW 4003
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 357 eeitghtlLERYgmteigmalsnplkgPRIpGAVGVPLPG------VEVRIVMTNATSTTIAEG----NSRETQVRPGLE 426
Cdd:PRK05691 4004 --------LQRY---------------PQI-GLVNAYGPAecsddvAFFRVDLASTRGSYLPIGsptdNNRLYLLDEALE 4059
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 427 ----GKEGELMVRGDQVFTEYWNKPEATRESFTEDGW-------FKTGDTAVY-KNGVYWIMGRtsVD-IIKSGGYKISA 493
Cdd:PRK05691 4060 lvplGAVGELCVAGTGVGRGYVGDPLRTALAFVPHPFgapgerlYRTGDLARRrSDGVLEYVGR--IDhQVKIRGYRIEL 4137
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 494 LEVERHLLAHPDITDVAViGARDATWGQKVTAVV---QLKRGRSMTLSELKTWAREHMAPYTIPTGLVLVEEMPRNQMGK 570
Cdd:PRK05691 4138 GEIEARLHEQAEVREAAV-AVQEGVNGKHLVGYLvphQTVLAQGALLERIKQRLRAELPDYMVPLHWLWLDRLPLNANGK 4216
|
....*.
gi 1367478878 571 VNKKDL 576
Cdd:PRK05691 4217 LDRKAL 4222
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
74-391 |
5.58e-13 |
|
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: 71.55 E-value: 5.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 74 SGSHSYRDLYGSSRGLAgrikAALDCPSGDLQGKRISFLCANDASYtVAQWASWMCGGTAVPLYREHPPSE-LEYIISDS 152
Cdd:cd05938 3 GETYTYRDVDRRSNQAA----RALLAHAGLRPGDTVALLLGNEPAF-LWIWLGLAKLGCPVAFLNTNIRSKsLLHCFRCC 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 153 QSSLLVAGQPYADTMEPLahrlgLPYLQ--------LPPTSS---LSSLLEAPENQP-EPGITDWAQR-----PAMIIYT 215
Cdd:cd05938 78 GAKVLVVAPELQEAVEEV-----LPALRadgvsvwyLSHTSNtegVISLLDKVDAASdEPVPASLRAHvtiksPALYIYT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 216 SGTTGRPKGVLHTHSNIQAMvQGLVSEWGWSRDDVILHTLPLHHVHGIVNKLLCPLWVGATTVMLPTFQPQKVWEvllSS 295
Cdd:cd05938 153 SGTTGLPKAARISHLRVLQC-SGFLSLCGVTADDVIYITLPLYHSSGFLLGIGGCIELGATCVLKPKFSASQFWD---DC 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 296 KAPMVTVFMAVPTIYSKLIQhyeqhfTQPRVQDfvraaCKERIRLMVsGSSalpqptlLR---WEEIT---GHT-LLERY 368
Cdd:cd05938 229 RKHNVTVIQYIGELLRYLCN------QPQSPND-----RDHKVRLAI-GNG-------LRadvWREFLrrfGPIrIREFY 289
|
330 340
....*....|....*....|...
gi 1367478878 369 GMTEIGMALSNPlkgPRIPGAVG 391
Cdd:cd05938 290 GSTEGNIGFFNY---TGKIGAVG 309
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
212-478 |
1.06e-12 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 70.82 E-value: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 212 IIYTSGTTGRPKGVLHTHSNIQAMVQGLVSEWG-----WSRDDVILHTLPLHHVHGIVNKLlCPLWVGATTvmlpTFQPQ 286
Cdd:PLN02614 228 IMYTSGTTGDPKGVMISNESIVTLIAGVIRLLKsanaaLTVKDVYLSYLPLAHIFDRVIEE-CFIQHGAAI----GFWRG 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 287 KVwEVLLSSKAPMV-TVFMAVPTIYSKLIQHYEQHFT------------------------------QPRVQDFVRAACK 335
Cdd:PLN02614 303 DV-KLLIEDLGELKpTIFCAVPRVLDRVYSGLQKKLSdggflkkfvfdsafsykfgnmkkgqshveaSPLCDKLVFNKVK 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 336 E----RIRLMVSGSSALPQPTLLRWEEITGHTLLERYGMTE--IGMALSNPLKGPRIpGAVGVPLPGVEVRIvmtnatsT 409
Cdd:PLN02614 382 QglggNVRIILSGAAPLASHVESFLRVVACCHVLQGYGLTEscAGTFVSLPDELDML-GTVGPPVPNVDIRL-------E 453
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 410 TIAEGNSRETQVRPglegkEGELMVRGDQVFTEYWNKPEATRESFTeDGWFKTGDTAVYK-NGVYWIMGR 478
Cdd:PLN02614 454 SVPEMEYDALASTP-----RGEICIRGKTLFSGYYKREDLTKEVLI-DGWLHTGDVGEWQpNGSMKIIDR 517
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
209-534 |
4.54e-12 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 68.82 E-value: 4.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 209 PAMIIYTSGTTGRPKGVL-----HTHSNIQAM----------VQGLVSEWGWsrddVILHTlplHHVHGivnkllcPLWV 273
Cdd:PRK10524 235 PSYILYTSGTTGKPKGVQrdtggYAVALATSMdtifggkageTFFCASDIGW----VVGHS---YIVYA-------PLLA 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 274 GATTVM---LPTfQPQkvwevllsskapmvtvfmavPTIYSKLIQHYE--QHFTQP---RV---QD--FVRAACKERIRL 340
Cdd:PRK10524 301 GMATIMyegLPT-RPD--------------------AGIWWRIVEKYKvnRMFSAPtaiRVlkkQDpaLLRKHDLSSLRA 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 341 MVSGSSALPQPTLlRW-EEITGHTLLERYGMTEIG---MALSNPL-KGPRIPGAVGVPLPGVEVRIvmtnatsttIAEGN 415
Cdd:PRK10524 360 LFLAGEPLDEPTA-SWiSEALGVPVIDNYWQTETGwpiLAIARGVeDRPTRLGSPGVPMYGYNVKL---------LNEVT 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 416 SRETQVrpgleGKEGELMVRG-------------DQVFTE-YWnkpeatrESFTEDgWFKTGDTAVY-KNGVYWIMGRTS 480
Cdd:PRK10524 430 GEPCGP-----NEKGVLVIEGplppgcmqtvwgdDDRFVKtYW-------SLFGRQ-VYSTFDWGIRdADGYYFILGRTD 496
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1367478878 481 vDIIKSGGYKISALEVERHLLAHPDITDVAVIGARDATWGQKVTAVVQLKRGRS 534
Cdd:PRK10524 497 -DVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPKDSDS 549
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
184-504 |
2.41e-11 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 66.68 E-value: 2.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 184 TSSLSSLLEAPENQPEPGITDWAQRPAMIIYTSGTTGRPKGVLHTHSNIQAMVQGLVSEW-GWSRDDVILHTLPLHHVhg 262
Cdd:PLN02387 227 VSSFSEVEKLGKENPVDPDLPSPNDIAVIMYTSGSTGLPKGVMMTHGNIVATVAGVMTVVpKLGKNDVYLAYLPLAHI-- 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 263 ivnkllcpLWVGATTVMLPT------FQPQKVWEVllSSK--------APMV--TVFMAVPTIYSKL------------- 313
Cdd:PLN02387 305 --------LELAAESVMAAVgaaigyGSPLTLTDT--SNKikkgtkgdASALkpTLMTAVPAILDRVrdgvrkkvdakgg 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 314 -------IQHY----------------EQHFTQPRVQDFVRAACKERIRLMVSGSSALPQPTlLRWEEIT-GHTLLERYG 369
Cdd:PLN02387 375 lakklfdIAYKrrlaaiegswfgawglEKLLWDALVFKKIRAVLGGRIRFMLSGGAPLSGDT-QRFINIClGAPIGQGYG 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 370 MTEI--GMALSNPlKGPRIpGAVGVPLPGVEVRIVmtnatstTIAEGNSRETQvRPgleGKEGELMVRGDQVFTEYWNKP 447
Cdd:PLN02387 454 LTETcaGATFSEW-DDTSV-GRVGPPLPCCYVKLV-------SWEEGGYLISD-KP---MPRGEIVIGGPSVTLGYFKNQ 520
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1367478878 448 EATRESFTEDG----WFKTGDTA-VYKNGVYWIMGRTSvDIIK--SGGYkISALEVERHLLAHP 504
Cdd:PLN02387 521 EKTDEVYKVDErgmrWFYTGDIGqFHPDGCLEIIDRKK-DIVKlqHGEY-VSLGKVEAALSVSP 582
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
209-571 |
5.53e-11 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 65.53 E-value: 5.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 209 PAMIIYTSGTTGRPKGVLHthSNIQAMVqGLVSEWGW---SRDDVILHTlplHH------VHGIVNKLLCplwVGATTVM 279
Cdd:PTZ00237 256 PLYILYTSGTTGNSKAVVR--SNGPHLV-GLKYYWRSiieKDIPTVVFS---HSsigwvsFHGFLYGSLS---LGNTFVM 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 280 L------PTFQPQKVWEVLLSSKapmVTVFMAVPTIYSKLIQhyeqhfTQPRVQDFVRAACKERIRLMVSGSSALPQPTL 353
Cdd:PTZ00237 327 FeggiikNKHIEDDLWNTIEKHK---VTHTLTLPKTIRYLIK------TDPEATIIRSKYDLSNLKEIWCGGEVIEESIP 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 354 LRWEEITGHTLLERYGMTEIGMALSNPLKGPRIP-GAVGVPLPGVEVRIVMTNatsttiaegnsretqvrpGLEGKEGEL 432
Cdd:PTZ00237 398 EYIENKLKIKSSRGYGQTEIGITYLYCYGHINIPyNATGVPSIFIKPSILSED------------------GKELNVNEI 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 433 mvrGDQVF---------TEYWNKPEATRESFTE-DGWFKTGDTAvYK--NGVYWIMGRtSVDIIKSGGYKISALEVERHL 500
Cdd:PTZ00237 460 ---GEVAFklpmppsfaTTFYKNDEKFKQLFSKfPGYYNSGDLG-FKdeNGYYTIVSR-SDDQIKISGNKVQLNTIETSI 534
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1367478878 501 LAHPDITDVAVIGARDATWGQKVTAVVQLKRG---RSMTLSELKTWARE----HMAPYTIPTGLVLVEEMPRNQMGKV 571
Cdd:PTZ00237 535 LKHPLVLECCSIGIYDPDCYNVPIGLLVLKQDqsnQSIDLNKLKNEINNiitqDIESLAVLRKIIIVNQLPKTKTGKI 612
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
119-478 |
1.57e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 63.81 E-value: 1.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 119 YTVAQWASWMCGGTAVPLYREHPPSELEYIIS---DSQSSLLVAGQPYADTMEPlahrlglpYLQLPPTSSLSSLLE--- 192
Cdd:PRK05850 72 YIVAFLGALQAGLIAVPLSVPQGGAHDERVSAvlrDTSPSVVLTTSAVVDDVTE--------YVAPQPGQSAPPVIEvdl 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 193 ---APENQPEPGITDwAQRPAMIIYTSGTTGRPKGVLHTHSNIQAMVQGLVSEW------GWSRDDVILHTLPLHHVHGI 263
Cdd:PRK05850 144 ldlDSPRGSDARPRD-LPSTAYLQYTSGSTRTPAGVMVSHRNVIANFEQLMSDYfgdtggVPPPDTTVVSWLPFYHDMGL 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 264 VNKLLCPLWVGATTVmlptfqpqkvwevLLSskaPMVtvFMAVPTIYSKLIQHYEQHFTQPRVQDFVRAACKER------ 337
Cdd:PRK05850 223 VLGVCAPILGGCPAV-------------LTS---PVA--FLQRPARWMQLLASNPHAFSAAPNFAFELAVRKTSdddmag 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 338 -----IRLMVSGSSALPQPTLLRWEE------ITGHTLLERYGMTE--IGMALSNPLKGPRI----------------PG 388
Cdd:PRK05850 285 ldlggVLGIISGSERVHPATLKRFADrfapfnLRETAIRPSYGLAEatVYVATREPGQPPESvrfdyeklsaghakrcET 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 389 AVGVPLpgveVRIVMTNATSTTIAEGNSR-ETQvrpglEGKEGELMVRGDQVFTEYWNKPEATRESF----------TED 457
Cdd:PRK05850 365 GGGTPL----VSYGSPRSPTVRIVDPDTCiECP-----AGTVGEIWVHGDNVAAGYWQKPEETERTFgatlvdpspgTPE 435
|
410 420
....*....|....*....|..
gi 1367478878 458 G-WFKTGDTAVYKNGVYWIMGR 478
Cdd:PRK05850 436 GpWLRTGDLGFISEGELFIVGR 457
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
79-528 |
1.78e-10 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 63.49 E-value: 1.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 79 YRDLYGSSRGLAGRIKAAldcpsGDLQGKRISFLCANDASYTVAQWASWMCGGTAVPLY-------REHPPSELEYIISD 151
Cdd:PRK09192 52 YQTLRARAEAGARRLLAL-----GLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPLPlpmgfggRESYIAQLRGMLAS 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 152 SQSSLLVAGQPYADTMEPLAHRLGLPY------LQLPPTSSLssllEAPENQPEpgitdwaqRPAMIIYTSGTTGRPKGV 225
Cdd:PRK09192 127 AQPAAIITPDELLPWVNEATHGNPLLHvlshawFKALPEADV----ALPRPTPD--------DIAYLQYSSGSTRFPRGV 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 226 LHTHSNIQAMVQGLvsewgwSRD-------DVILHTLPLHHVHGIVNKLLCPLWVGATTVMLPT--F--QPQkVWEVLLS 294
Cdd:PRK09192 195 IITHRALMANLRAI------SHDglkvrpgDRCVSWLPFYHDMGLVGFLLTPVATQLSVDYLPTrdFarRPL-QWLDLIS 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 295 SKAPMVTVfmaVPTIYSKLiqhyeqhftqprvqdfvraaCKERIRlmvsgSSALPQPTLLRW-------EEITGHTL--- 364
Cdd:PRK09192 268 RNRGTISY---SPPFGYEL--------------------CARRVN-----SKDLAELDLSCWrvagigaDMIRPDVLhqf 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 365 --------------LERYGMTEIGMALS-NPL-KGPRI--------------------PGAV------GVPLPGVEVRIV 402
Cdd:PRK09192 320 aeafapagfddkafMPSYGLAEATLAVSfSPLgSGIVVeevdrdrleyqgkavapgaeTRRVrtfvncGKALPGHEIEIR 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 403 mtNATSTTIAegnsrETQVrpglegkeGELMVRGDQVFTEYWNKPEATREsFTEDGWFKTGDTAVYKNGVYWIMGRTSvD 482
Cdd:PRK09192 400 --NEAGMPLP-----ERVV--------GHICVRGPSLMSGYFRDEESQDV-LAADGWLDTGDLGYLLDGYLYITGRAK-D 462
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1367478878 483 IIKSGGYKISALEVERHLLAHPDIT--DVAVIGARDATwGQKVTAVVQ 528
Cdd:PRK09192 463 LIIINGRNIWPQDIEWIAEQEPELRsgDAAAFSIAQEN-GEKIVLLVQ 509
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
213-581 |
2.00e-10 |
|
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: 63.21 E-value: 2.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 213 IYTSGTTGRPKGVLHTHSNIQAMVQGLVSEWGWSRDDVILHTLPLHH----VHGIVNKLLcplwVGATTVMLPTFQPQKV 288
Cdd:cd05939 110 IYTSGTTGLPKAAVIVHSRYYRIAAGAYYAFGMRPEDVVYDCLPLYHsaggIMGVGQALL----HGSTVVIRKKFSASNF 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 289 WEVLLSSKapmVTVFMAVPTIYSKLIqhyeqhfTQPRVQDfvraACKERIRLMVsGSSALPQPtllrWEEITGH----TL 364
Cdd:cd05939 186 WDDCVKYN---CTIVQYIGEICRYLL-------AQPPSEE----EQKHNVRLAV-GNGLRPQI----WEQFVRRfgipQI 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 365 LERYGMTEIGMALSNplkgprIPGAVG------VPLPGV-EVRIVMTN-ATSTTIAEGNSRETQVRPGLEGKEGELMVRG 436
Cdd:cd05939 247 GEFYGATEGNSSLVN------IDNHVGacgfnsRILPSVyPIRLIKVDeDTGELIRDSDGLCIPCQPGEPGLLVGKIIQN 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 437 DQV--FTEYWNKPEAT----RESFTE-DGWFKTGDTAVYKN-GVYWIMGRTSvDIIKSGGYKISALEVERHLLAHPDITD 508
Cdd:cd05939 321 DPLrrFDGYVNEGATNkkiaRDVFKKgDSAFLSGDVLVMDElGYLYFKDRTG-DTFRWKGENVSTTEVEGILSNVLGLED 399
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1367478878 509 VAV----IGARDATWGqkVTAVVQLKRGrsMTLSELKTWAREHMAPYTIPTGLVLVEEMPRNQMGKVNKKDLLKHFF 581
Cdd:cd05939 400 VVVygveVPGVEGRAG--MAAIVDPERK--VDLDRFSAVLAKSLPPYARPQFIRLLPEVDKTGTFKLQKTDLQKEGY 472
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
209-498 |
4.39e-09 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 59.01 E-value: 4.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 209 PAMIIYTSGTTGRPKGVLHTHSNIQAMVQGLVSEWGWSRD-DVILHTLPLHHVHGIVNkLLCPLWVGATTVMLPT--FQ- 284
Cdd:PRK05851 154 PAVLQGTAGSTGTPRTAILSPGAVLSNLRGLNARVGLDAAtDVGCSWLPLYHDMGLAF-LLTAALAGAPLWLAPTtaFSa 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 285 -PQKVWEVLLSSKAPMVtvfmAVPTIYSKLIQHYEQhftqpRVQDFVRAAckerIRLMVSGSSALPQPTLLRWEEITGH- 362
Cdd:PRK05851 233 sPFRWLSWLSDSRATLT----AAPNFAYNLIGKYAR-----RVSDVDLGA----LRVALNGGEPVDCDGFERFATAMAPf 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 363 -----TLLERYGMTEIGMALSNPLKG---------------PRIPGAVGVPLPGVEVRIVMTNATsttiAEGNSRETqvr 422
Cdd:PRK05851 300 gfdagAAAPSYGLAESTCAVTVPVPGiglrvdevttddgsgARRHAVLGNPIPGMEVRISPGDGA----AGVAGREI--- 372
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1367478878 423 pglegkeGELMVRGDQVFTEYWNKPeatreSFTEDGWFKTGDTAVYKNGVYWIMGRTSvDIIKSGGYKISALEVER 498
Cdd:PRK05851 373 -------GEIEIRGASMMSGYLGQA-----PIDPDDWFPTGDLGYLVDGGLVVCGRAK-ELITVAGRNIFPTEIER 435
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
106-478 |
1.75e-08 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 57.43 E-value: 1.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 106 GKRISFLCANDASYTVAQWASWMCGGTAVPLYrehPPSE------LEYIISDSQSSLLVAGQPYADTMEPLAHrlGLPYL 179
Cdd:PRK07769 79 GDRVAILAPQNLDYLIAFFGALYAGRIAVPLF---DPAEpghvgrLHAVLDDCTPSAILTTTDSAEGVRKFFR--ARPAK 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 180 QLP--------PTSSLSSLLeapenQPEPGITDWAqrpaMIIYTSGTTGRPKGVLHTHSNIQAMVQGLVSEWGWSRDDVI 251
Cdd:PRK07769 154 ERPrviavdavPDEVGATWV-----PPEANEDTIA----YLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALEGQEGDRG 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 252 LHTLPLHHVHGIVNKLLCPLWVGATTVMLP-TF--QPQKvWEVLLSSKAP-MVTVFMAVPTIyskLIQHYEQhftqprvq 327
Cdd:PRK07769 225 VSWLPFFHDMGLITVLLPALLGHYITFMSPaAFvrRPGR-WIRELARKPGgTGGTFSAAPNF---AFEHAAA-------- 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 328 dfvRAACKE--------RIRLMVSGSSALPQPTLLRWEEITGHTLLER------YGMTEIGMALSNP------------- 380
Cdd:PRK07769 293 ---RGLPKDgeppldlsNVKGLLNGSEPVSPASMRKFNEAFAPYGLPPtaikpsYGMAEATLFVSTTpmdeeptviyvdr 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 381 --LKGPRI-------PGAVGVPLPGVEVR----IVMTNATSTTIAEGnsretQVrpglegkeGELMVRGDQVFTEYWNKP 447
Cdd:PRK07769 370 deLNAGRFvevpadaPNAVAQVSAGKVGVsewaVIVDPETASELPDG-----QI--------GEIWLHGNNIGTGYWGKP 436
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1367478878 448 EATRESF----------------TEDG-WFKTGDTAVYKNGVYWIMGR 478
Cdd:PRK07769 437 EETAATFqnilksrlseshaegaPDDAlWVRTGDYGVYFDGELYITGR 484
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
430-471 |
4.30e-08 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 56.27 E-value: 4.30e-08
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1367478878 430 GELMVRGDQVFTEYWNKPEATRESFTEDGWFKTGDTA-VYKNG 471
Cdd:PTZ00342 542 GELLIKSDSIFSGYFLEKEQTKNAFTEDGYFKTGDIVqINKNG 584
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
68-487 |
4.76e-07 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 52.82 E-value: 4.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 68 LAIVDDSGSHSYRDLYGSSRGLA-----GRIKAALDCPSGDLQ-----GKRISFLCANDASYTVAQWASWMCGGTAVPLY 137
Cdd:PRK12476 44 IANVGDTVAYRYLDHSHSAAGCAveltwTQLGVRLRAVGARLQqvagpGDRVAILAPQGIDYVAGFFAAIKAGTIAVPLF 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 138 REHPP---SELEYIISDSQSSLLVAGQPYADTMEPLAHrlGLPYLQLP--------PTSSLSSLLEAPenqpePGITDWA 206
Cdd:PRK12476 124 APELPghaERLDTALRDAEPTVVLTTTAAAEAVEGFLR--NLPRLRRPrviaidaiPDSAGESFVPVE-----LDTDDVS 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 207 QrpamIIYTSGTTGRPKGVLHTHSNIQA-MVQGLVSEWGWSRDDVILHTLPLHHVHGIVNKLLCPLWVGATTVMLPT-F- 283
Cdd:PRK12476 197 H----LQYTSGSTRPPVGVEITHRAVGTnLVQMILSIDLLDRNTHGVSWLPLYHDMGLSMIGFPAVYGGHSTLMSPTaFv 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 284 -QPQKvWEVLLSSKAPMVTVFMAVPTIYSKLIQHyeqhftqprvqdfvRAACK--ERIRL----MVSGSSALPQPTLLRW 356
Cdd:PRK12476 273 rRPQR-WIKALSEGSRTGRVVTAAPNFAYEWAAQ--------------RGLPAegDDIDLsnvvLIIGSEPVSIDAVTTF 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 357 EEITGHTLLER------YGMTEIGMALSN--PLKGP------RIPGAVG--VPLPGVEVRIVmtnatsTTIAEGNSRETQ 420
Cdd:PRK12476 338 NKAFAPYGLPRtafkpsYGIAEATLFVATiaPDAEPsvvyldREQLGAGraVRVAADAPNAV------AHVSCGQVARSQ 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 421 ----VRPGLE-----GKEGELMVRGDQVFTEYWNKPEATRESF----------------TEDG--WFKTGDTAVYKNGVY 473
Cdd:PRK12476 412 waviVDPDTGaelpdGEVGEIWLHGDNIGRGYWGRPEETERTFgaklqsrlaegshadgAADDgtWLRTGDLGVYLDGEL 491
|
490
....*....|....
gi 1367478878 474 WIMGRTSVDIIKSG 487
Cdd:PRK12476 492 YITGRIADLIVIDG 505
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
214-576 |
4.61e-06 |
|
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Pssm-ID: 341302 [Multi-domain] Cd Length: 520 Bit Score: 49.44 E-value: 4.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 214 YTSGTTGRPKGVLHTHSNIQAMVQGLVSEWGWSRDDVILHTLPLHHvHGIVNKLLCPLWVGATtVMLPT----FQPQKVW 289
Cdd:cd17647 116 FTSGSEGIPKGVLGRHFSLAYYFPWMAKRFNLSENDKFTMLSGIAH-DPIQRDMFTPLFLGAQ-LLVPTqddiGTPGRLA 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 290 EVLLSSKApMVTvfmavptiyskliqhyeqHFTQPRVQdfvraackerirlMVSGSSALPQPTLLRwEEITGHTLLER-- 367
Cdd:cd17647 194 EWMAKYGA-TVT------------------HLTPAMGQ-------------LLTAQATTPFPKLHH-AFFVGDILTKRdc 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 368 ---------------YGMTEIGMALS---------NP--LKGPR--IPGAVGvpLPGVEVRIVMTNATSTTIAEGNSRET 419
Cdd:cd17647 241 lrlqtlaenvrivnmYGTTETQRAVSyfevpsrssDPtfLKNLKdvMPAGRG--MLNVQLLVVNRNDRTQICGIGEVGEI 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 420 QVRPG--LEGKEG------ELMVRGDQVFTEYWN-KPEATRESFTE------DGWFKTGDTAVY-KNGVYWIMGRTSvDI 483
Cdd:cd17647 319 YVRAGglAEGYRGlpelnkEKFVNNWFVEPDHWNyLDKDNNEPWRQfwlgprDRLYRTGDLGRYlPNGDCECCGRAD-DQ 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 484 IKSGGYKISALEVERHLLAHPDI---------------TDVAVIGARDATWGQKVTA------------VVQLKRGRSMT 536
Cdd:cd17647 398 VKIRGFRIELGEIDTHISQHPLVrenitlvrrdkdeepTLVSYIVPRFDKPDDESFAqedvpkevstdpIVKGLIGYRKL 477
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1367478878 537 LSELKTWAREHMAPYTIPTGLVLVEEMPRNQMGKVNKKDL 576
Cdd:cd17647 478 IKDIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKL 517
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
215-512 |
4.63e-05 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 45.91 E-value: 4.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 215 TSGTTGRPKGVLHTHSNIQA----MVQGLVSEwGWSRDDVILHTLPLHhvhgivnkllcpLWV------------GATTV 278
Cdd:COG1541 91 SSGTTGKPTVVGYTRKDLDRwaelFARSLRAA-GVRPGDRVQNAFGYG------------LFTgglglhygaerlGATVI 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 279 MLPTFQPQKVWEVLLSSKapmVTVFMAVPTiYSK-LIQHYEQHFTQPRvqdfvraacKERIRLMVSGSSALPQPTLLRWE 357
Cdd:COG1541 158 PAGGGNTERQLRLMQDFG---PTVLVGTPS-YLLyLAEVAEEEGIDPR---------DLSLKKGIFGGEPWSEEMRKEIE 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 358 EITGHTLLERYGMTEIGMALSN---PLKGPRIPGAV----------GVPLPgvevrivmtnatsttiaegnsretqvrpg 424
Cdd:COG1541 225 ERWGIKAYDIYGLTEVGPGVAYeceAQDGLHIWEDHflveiidpetGEPVP----------------------------- 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367478878 425 lEGKEGELmvrgdqVFTeywnkpeatreSFTEDGW----FKTGDTAVYKNG----------VYWIMGRTSvDIIKSGGYK 490
Cdd:COG1541 276 -EGEEGEL------VVT-----------TLTKEAMplirYRTGDLTRLLPEpcpcgrthprIGRILGRAD-DMLIIRGVN 336
|
330 340
....*....|....*....|..
gi 1367478878 491 ISALEVERHLLAHPDITDVAVI 512
Cdd:COG1541 337 VFPSQIEEVLLRIPEVGPEYQI 358
|
|
| |
