|
Name |
Accession |
Description |
Interval |
E-value |
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
71-583 |
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: 695.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 71 DKPAIIDSSGSHSYKQLYcsslGLAGRISTALNLDFGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLFRKHPQSEL 150
Cdd:cd05941 1 DRIAIVDDGDSITYADLV----ARAARLANRLLALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 151 EYIISDSQSSLLVaghpyagtleplalklglpcltlpptsnlgtldgtdtqekeaaitdwadRPAMIIYTSGTTGRPKGV 230
Cdd:cd05941 77 EYVITDSEPSLVL-------------------------------------------------DPALILYTSGTTGRPKGV 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 231 LHMHSNIQAMVQGLVSEWAWTRDDVILHTLPLHHVHGIVNKLLCPLWVGATCVMLPEFQPQkvwEMLLSSKAPMVNVFMA 310
Cdd:cd05941 108 VLTHANLAANVRALVDAWRWTEDDVLLHVLPLHHVHGLVNALLCPLFAGASVEFLPKFDPK---EVAISRLMPSITVFMG 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 311 VPTIYSKLIQYYDQHFTQPhvkDFVRAVCKERIRLMVSGSAALPLPTLQRWEEITGHTLLERYGMTEIGMALSNPLKGPR 390
Cdd:cd05941 185 VPTIYTRLLQYYEAHFTDP---QFARAAAAERLRLMVSGSAALPVPTLEEWEAITGHTLLERYGMTEIGMALSNPLDGER 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 391 IPGAVGSPLPRVEVRIVMNNTTNttivlgdhrntrvcPGLEGKEGELLVRGPSVFKEYWNKPQETRESFIDGGWFKTGDT 470
Cdd:cd05941 262 RPGTVGMPLPGVQARIVDEETGE--------------PLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGWFKTGDL 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 471 VVYK-DGVYWIMGRSSVDIIKSAGYKISALEVERHLLAHPDIIDVAVIGAPDAIWGQKVTAVVQLRKG-QSMTLPDLKTW 548
Cdd:cd05941 328 GVVDeDGYYWILGRSSVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGaAALSLEELKEW 407
|
490 500 510
....*....|....*....|....*....|....*
gi 1250165799 549 AREHMAPYTIPTGLLLVEEMPRNQMGKVNKKDLLR 583
Cdd:cd05941 408 AKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
65-585 |
6.05e-140 |
|
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: 413.82 E-value: 6.05e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 65 RAPAFGDKPAIIDSSGSHSYKQLYcsslGLAGRISTALnLDFGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLFRK 144
Cdd:COG0318 8 AAARHPDRPALVFGGRRLTYAELD----ARARRLAAAL-RALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 145 HPQSELEYIISDSQSSLLVAghpyagtleplalklglpcltlpptsnlgtldgtdtqekeaaitdwadrpAMIIYTSGTT 224
Cdd:COG0318 83 LTAEELAYILEDSGARALVT--------------------------------------------------ALILYTSGTT 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 225 GRPKGVLHMHSNIQAMVQGLVSEWAWTRDDVILHTLPLHHVHGIVNKLLCPLWVGATCVMLPEFQPQKVWEMLLSSKapm 304
Cdd:COG0318 113 GRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLPRFDPERVLELIERER--- 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 305 VNVFMAVPTIYSKLIQYYDQHFTQPHvkdfvravckeRIRLMVSGSAALPLPTLQRWEEITGHTLLERYGMTEIGMALS- 383
Cdd:COG0318 190 VTVLFGVPTMLARLLRHPEFARYDLS-----------SLRLVVSGGAPLPPELLERFEERFGVRIVEGYGLTETSPVVTv 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 384 NPL-KGPRIPGAVGSPLPRVEVRIVmnnttnttivlgdHRNTRVCPglEGKEGELLVRGPSVFKEYWNKPQETRESFIDG 462
Cdd:COG0318 259 NPEdPGERRPGSVGRPLPGVEVRIV-------------DEDGRELP--PGEVGEIVVRGPNVMKGYWNDPEATAEAFRDG 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 463 gWFKTGDTVVY-KDGVYWIMGRSSvDIIKSAGYKISALEVERHLLAHPDIIDVAVIGAPDAIWGQKVTAVVQLRKGQSMT 541
Cdd:COG0318 324 -WLRTGDLGRLdEDGYLYIVGRKK-DMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPGAELD 401
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1250165799 542 LPDLKTWAREHMAPYTIPTGLLLVEEMPRNQMGKVNKKDLLRHF 585
Cdd:COG0318 402 AEELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRERY 445
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
69-581 |
6.20e-113 |
|
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: 344.93 E-value: 6.20e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 69 FGDKPAIIDSSGSHSYKQLYcsslGLAGRISTAL-NLDFGglEGKRISFLCANDASYTVAQWAAWMSGGTAVPLfrkHPQ 147
Cdd:cd05936 12 FPDKTALIFMGRKLTYRELD----ALAEAFAAGLqNLGVQ--PGDRVALMLPNCPQFPIAYFGALKAGAVVVPL---NPL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 148 ---SELEYIISDSQSSLLVAGHPYAGTLEPLALKLGLPcltlpptsnlgTLDGTDTqekeaaitdwadrpAMIIYTSGTT 224
Cdd:cd05936 83 ytpRELEHILNDSGAKALIVAVSFTDLLAAGAPLGERV-----------ALTPEDV--------------AVLQYTSGTT 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 225 GRPKGVLHMHSNIQAMVQGLvseWAW-----TRDDVILHTLPLHHVHGIVNKLLCPLWVGATCVMLPEFQPQKVWEMLls 299
Cdd:cd05936 138 GVPKGAMLTHRNLVANALQI---KAWledllEGDDVVLAALPLFHVFGLTVALLLPLALGATIVLIPRFRPIGVLKEI-- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 300 sKAPMVNVFMAVPTIYSKLIQyydqhftQPHVKDFVRAvckeRIRLMVSGSAALPLPTLQRWEEITGHTLLERYGMTEIG 379
Cdd:cd05936 213 -RKHRVTIFPGVPTMYIALLN-------APEFKKRDFS----SLRLCISGGAPLPVEVAERFEELTGVPIVEGYGLTETS 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 380 -MALSNPLKGPRIPGAVGSPLPRVEVRIVMNNTTnttiVLGDhrntrvcpgleGKEGELLVRGPSVFKEYWNKPQETRES 458
Cdd:cd05936 281 pVVAVNPLDGPRKPGSIGIPLPGTEVKIVDDDGE----ELPP-----------GEVGELWVRGPQVMKGYWNRPEETAEA 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 459 FIDGgWFKTGDtVVY--KDGVYWIMGRSSvDIIKSAGYKISALEVERHLLAHPDIIDVAVIGAPDAIWGQKVTAVVQLRK 536
Cdd:cd05936 346 FVDG-WLRTGD-IGYmdEDGYFFIVDRKK-DMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKE 422
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1250165799 537 GQSMTLPDLKTWAREHMAPYTIPTGLLLVEEMPRNQMGKVNKKDL 581
Cdd:cd05936 423 GASLTEEEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRREL 467
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
71-583 |
1.57e-107 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 332.23 E-value: 1.57e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 71 DKPAIIDSSGSH-SYKQLycssLGLAGRISTALnLDFGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLFRKHPQSE 149
Cdd:PRK07514 17 DAPFIETPDGLRyTYGDL----DAASARLANLL-VALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 150 LEYIISDSQSSLLVAGHPYAGTLEPLALKLGlpcltlppTSNLGTLD----GTDTQEKEAAITDWADRP------AMIIY 219
Cdd:PRK07514 92 LDYFIGDAEPALVVCDPANFAWLSKIAAAAG--------APHVETLDadgtGSLLEAAAAAPDDFETVPrgaddlAAILY 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 220 TSGTTGRPKGVLHMHSNIQAMVQGLVSEWAWTRDDVILHTLPLHHVHGIVNKLLCPLWVGATCVMLPEFQPQKVWEMLls 299
Cdd:PRK07514 164 TSGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPDDVLIHALPIFHTHGLFVATNVALLAGASMIFLPKFDPDAVLALM-- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 300 skaPMVNVFMAVPTIYSKLIQyyDQHFTqphvkdfvRAVCKeRIRLMVSGSAALPLPTLQRWEEITGHTLLERYGMTEIG 379
Cdd:PRK07514 242 ---PRATVMMGVPTFYTRLLQ--EPRLT--------REAAA-HMRLFISGSAPLLAETHREFQERTGHAILERYGMTETN 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 380 MALSNPLKGPRIPGAVGSPLPRVEVRIVmnnttnttivlgDHRNTRVCPglEGKEGELLVRGPSVFKEYWNKPQETRESF 459
Cdd:PRK07514 308 MNTSNPYDGERRAGTVGFPLPGVSLRVT------------DPETGAELP--PGEIGMIEVKGPNVFKGYWRMPEKTAEEF 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 460 IDGGWFKTGDT-VVYKDGVYWIMGRSSvDIIKSAGYKISALEVERHLLAHPDIIDVAVIGAPDAIWGQKVTAVVQLRKGQ 538
Cdd:PRK07514 374 RADGFFITGDLgKIDERGYVHIVGRGK-DLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKPGA 452
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1250165799 539 SMTLPDLKTWAREHMAPYTIPTGLLLVEEMPRNQMGKVnKKDLLR 583
Cdd:PRK07514 453 ALDEAAILAALKGRLARFKQPKRVFFVDELPRNTMGKV-QKNLLR 496
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
66-583 |
1.22e-102 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 318.47 E-value: 1.22e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 66 APAFGDKPAIIDSSGSHSYKQLYCSSLGLAGRISTAlnldfgglegKRISFLCANDASYTVAQWAAWMSGGTAVPLFRKH 145
Cdd:PRK07787 10 AAAADIADAVRIGGRVLSRSDLAGAATAVAERVAGA----------RRVAVLATPTLATVLAVVGALIAGVPVVPVPPDS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 146 PQSELEYIISDSQSSLLVAGHPYAGtleplalkLGLPCLTLPPTSnlgtldGTDTQEKEAAitdwADRPAMIIYTSGTTG 225
Cdd:PRK07787 80 GVAERRHILADSGAQAWLGPAPDDP--------AGLPHVPVRLHA------RSWHRYPEPD----PDAPALIVYTSGTTG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 226 RPKGVLHMHSNIQAMVQGLVSEWAWTRDDVILHTLPLHHVHGIVNKLLCPLWVGATCVMLPEFQPQKVWEMlLSSKAPMv 305
Cdd:PRK07787 142 PPKGVVLSRRAIAADLDALAEAWQWTADDVLVHGLPLFHVHGLVLGVLGPLRIGNRFVHTGRPTPEAYAQA-LSEGGTL- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 306 nvFMAVPTIYSKLIQYYDqhftqpHVKDFVRAvckeriRLMVSGSAALPLPTLQRWEEITGHTLLERYGMTEIGMALSNP 385
Cdd:PRK07787 220 --YFGVPTVWSRIAADPE------AARALRGA------RLLVSGSAALPVPVFDRLAALTGHRPVERYGMTETLITLSTR 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 386 LKGPRIPGAVGSPLPRVEVRIVmnnttnttivlgDHRNTRVcpGLEGKE-GELLVRGPSVFKEYWNKPQETRESFIDGGW 464
Cdd:PRK07787 286 ADGERRPGWVGLPLAGVETRLV------------DEDGGPV--PHDGETvGELQVRGPTLFDGYLNRPDATAAAFTADGW 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 465 FKTGD-TVVYKDGVYWIMGRSSVDIIKSAGYKISALEVERHLLAHPDIIDVAVIGAPDAIWGQKVTA-VVQLRKGQSMTL 542
Cdd:PRK07787 352 FRTGDvAVVDPDGMHRIVGRESTDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAyVVGADDVAADEL 431
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1250165799 543 PDLktwAREHMAPYTIPTGLLLVEEMPRNQMGKVNKKDLLR 583
Cdd:PRK07787 432 IDF---VAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLLS 469
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
213-576 |
2.34e-100 |
|
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: 308.06 E-value: 2.34e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 213 RPAMIIYTSGTTGRPKGVLHMHSNIQAMVQGLVSEWAWTRDDVILHTLPLHHVHGIvNKLLCPLWVGATCVMLPEFQPQK 292
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGL-FGLLGALLAGGTVVLLPKFDPEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 293 VWEMLlssKAPMVNVFMAVPTIYSKLIQYYDQHftqPHVKDFVRAVCkerirlmvSGSAALPLPTLQRWEEITGHTLLER 372
Cdd:cd04433 80 ALELI---EREKVTILLGVPTLLARLLKAPESA---GYDLSSLRALV--------SGGAPLPPELLERFEEAPGIKLVNG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 373 YGMTEIG--MALSNPLKGPRIPGAVGSPLPRVEVRIVmnnttnttivlgdHRNTRVCPglEGKEGELLVRGPSVFKEYWN 450
Cdd:cd04433 146 YGLTETGgtVATGPPDDDARKPGSVGRPVPGVEVRIV-------------DPDGGELP--PGEIGELVVRGPSVMKGYWN 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 451 KPQETRESFIDGgWFKTGDtVVYKD--GVYWIMGRSSvDIIKSAGYKISALEVERHLLAHPDIIDVAVIGAPDAIWGQKV 528
Cdd:cd04433 211 NPEATAAVDEDG-WYRTGD-LGRLDedGYLYIVGRLK-DMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERV 287
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1250165799 529 TAVVQLRKGQSMTLPDLKTWAREHMAPYTIPTGLLLVEEMPRNQMGKV 576
Cdd:cd04433 288 VAVVVLRPGADLDAEELRAHVRERLAPYKVPRRVVFVDALPRTASGKI 335
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
65-578 |
7.95e-99 |
|
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: 307.23 E-value: 7.95e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 65 RAPAFGDKPAIIDSSGSHSYKQLYcsslGLAGRISTALnLDFGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPL-FR 143
Cdd:cd17631 4 RARRHPDRTALVFGGRSLTYAELD----ERVNRLAHAL-RALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLnFR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 144 KHPqSELEYIISDSQSSLLVaghpyagtleplalklglpcltlpptsnlgtldgtdtqekeaaitdwaDRPAMIIYTSGT 223
Cdd:cd17631 79 LTP-PEVAYILADSGAKVLF------------------------------------------------DDLALLMYTSGT 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 224 TGRPKGVLHMHSNIQAMVQGLVSEWAWTRDDVILHTLPLHHVHGIVNKLLCPLWVGATCVMLPEFQPQKVWEMLLSSKap 303
Cdd:cd17631 110 TGRPKGAMLTHRNLLWNAVNALAALDLGPDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVILRKFDPETVLDLIERHR-- 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 304 mVNVFMAVPTIYSKLIQYYDqhFTQPhvkDFvravckERIRLMVSGSAALPLPTLQRWEEItGHTLLERYGMTEIGMALS 383
Cdd:cd17631 188 -VTSFFLVPTMIQALLQHPR--FATT---DL------SSLRAVIYGGAPMPERLLRALQAR-GVKFVQGYGMTETSPGVT 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 384 npLKGP----RIPGAVGSPLPRVEVRIVmnnttnttivlGDhrNTRVCPglEGKEGELLVRGPSVFKEYWNKPQETRESF 459
Cdd:cd17631 255 --FLSPedhrRKLGSAGRPVFFVEVRIV-----------DP--DGREVP--PGEVGEIVVRGPHVMAGYWNRPEATAAAF 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 460 IDGgWFKTGDtVVYKD--GVYWIMGRSSvDIIKSAGYKISALEVERHLLAHPDIIDVAVIGAPDAIWGQKVTAVVQLRKG 537
Cdd:cd17631 318 RDG-WFHTGD-LGRLDedGYLYIVDRKK-DMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPG 394
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1250165799 538 QSMTLPDLKTWAREHMAPYTIPTGLLLVEEMPRNQMGKVNK 578
Cdd:cd17631 395 AELDEDELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
63-581 |
2.07e-97 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 306.73 E-value: 2.07e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 63 FVRAPA--FGDKPAIIDSSGSHSYKQLYcsslGLAGRISTALnLDFGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVP 140
Cdd:PRK06187 11 ILRHGArkHPDKEAVYFDGRRTTYAELD----ERVNRLANAL-RALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 141 L-FRKHPQsELEYIISDSQSSLLVAGHPYAGTLEPLALKLGlpclTLPPTSNLGTLDGTDTQEKEAAITDW-ADRP---- 214
Cdd:PRK06187 86 InIRLKPE-EIAYILNDAEDRVVLVDSEFVPLLAAILPQLP----TVRTVIVEGDGPAAPLAPEVGEYEELlAAASdtfd 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 215 ---------AMIIYTSGTTGRPKGVLHMHSNIQAMVQGLVSEWAWTRDDVILHTLPLHHVHGIVNKLLcPLWVGATCVML 285
Cdd:PRK06187 161 fpdidendaAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVPMFHVHAWGLPYL-ALMAGAKQVIP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 286 PEFQPQKVWEMLLSSKapmVNVFMAVPTIYSKLIQYYDQHFtqphvKDFVRavckerIRLMVSGSAALPLPTLQRWEEIT 365
Cdd:PRK06187 240 RRFDPENLLDLIETER---VTFFFAVPTIWQMLLKAPRAYF-----VDFSS------LRLVIYGGAALPPALLREFKEKF 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 366 GHTLLERYGMTEIGMALS-NPLK-----GPRIPGAVGSPLPRVEVRIVmnnttnttivlGDHRNtrVCPGLEGKEGELLV 439
Cdd:PRK06187 306 GIDLVQGYGMTETSPVVSvLPPEdqlpgQWTKRRSAGRPLPGVEARIV-----------DDDGD--ELPPDGGEVGEIIV 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 440 RGPSVFKEYWNKPQETREsFIDGGWFKTGDtVVY--KDGVYWIMGRSSvDIIKSAGYKISALEVERHLLAHPDIIDVAVI 517
Cdd:PRK06187 373 RGPWLMQGYWNRPEATAE-TIDGGWLHTGD-VGYidEDGYLYITDRIK-DVIISGGENIYPRELEDALYGHPAVAEVAVI 449
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1250165799 518 GAPDAIWGQKVTAVVQLRKGQSMTLPDLKTWAREHMAPYTIPTGLLLVEEMPRNQMGKVNKKDL 581
Cdd:PRK06187 450 GVPDEKWGERPVAVVVLKPGATLDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVL 513
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
71-576 |
1.03e-91 |
|
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: 290.75 E-value: 1.03e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 71 DKPAIIDSSGSH--SYKQLYCSSLGLAGRIsTALNLdfggLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLFRKHPQS 148
Cdd:cd05926 2 DAPALVVPGSTPalTYADLAELVDDLARQL-AALGI----KKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 149 ELEYIISDSQSSLLVAGHPYAGTLEPLALKLGLPCLTL----------PPTSNLGTLDGTDTQEKEAAITDwADRPAMII 218
Cdd:cd05926 77 EFEFYLADLGSKLVLTPKGELGPASRAASKLGLAILELaldvgvliraPSAESLSNLLADKKNAKSEGVPL-PDDLALIL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 219 YTSGTTGRPKGVLHMHSNIQAMVQGLVSEWAWTRDDVILHTLPLHHVHGIVNKLLCPLWVGATCVMLPEFQPQKVWEmll 298
Cdd:cd05926 156 HTSGTTGRPKGVPLTHRNLAASATNITNTYKLTPDDRTLVVMPLFHVHGLVASLLSTLAAGGSVVLPPRFSASTFWP--- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 299 SSKAPMVNVFMAVPTIYSKLIQYYDQHFTQPHVKdfvravckerIRLMVSGSAALPLPTLQRWEEITGHTLLERYGMTEI 378
Cdd:cd05926 233 DVRDYNATWYTAVPTIHQILLNRPEPNPESPPPK----------LRFIRSCSASLPPAVLEALEATFGAPVLEAYGMTEA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 379 G--MAlSNPLK-GPRIPGAVGSPLPrVEVRIvmnnttnttivLGDHRNtrvcPGLEGKEGELLVRGPSVFKEYWNKPQET 455
Cdd:cd05926 303 AhqMT-SNPLPpGPRKPGSVGKPVG-VEVRI-----------LDEDGE----ILPPGVVGEICLRGPNVTRGYLNNPEAN 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 456 RESFIDGGWFKTGDT-VVYKDGVYWIMGRSSvDIIKSAGYKISALEVERHLLAHPDIIDVAVIGAPDAIWGQKVTAVVQL 534
Cdd:cd05926 366 AEAAFKDGWFRTGDLgYLDADGYLFLTGRIK-ELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVL 444
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1250165799 535 RKGQSMTLPDLKTWAREHMAPYTIPTGLLLVEEMPRNQMGKV 576
Cdd:cd05926 445 REGASVTEEELRAFCRKHLAAFKVPKKVYFVDELPKTATGKI 486
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
66-581 |
5.32e-87 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 279.10 E-value: 5.32e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 66 APAFGDKPAIIDSSGSHSYKQLYCSSLGLAGristALnLDFGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLFRKH 145
Cdd:PRK07656 15 ARRFGDKEAYVFGDQRLTYAELNARVRRAAA----AL-AALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 146 PQSELEYIISDSQSSLLVA-----GHPYAGTLEPLALKLGLPCLT---LPPTSNLGTLD----GTDTQEKEAAITDwaDR 213
Cdd:PRK07656 90 TADEAAYILARGDAKALFVlglflGVDYSATTRLPALEHVVICETeedDPHTEKMKTFTdflaAGDPAERAPEVDP--DD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 214 PAMIIYTSGTTGRPKGVLHMHSNIQAMVQglvsEWA----WTRDDVILHTLPLHHVHGIVNKLLCPLWVGATCVMLPEFQ 289
Cdd:PRK07656 168 VADILFTSGTTGRPKGAMLTHRQLLSNAA----DWAeylgLTEGDRYLAANPFFHVFGYKAGVNAPLMRGATILPLPVFD 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 290 PQKVWEMLLSSKApmvNVFMAVPTIYSKLIQYYDQHFTqphvkDFvravckERIRLMVSGSAALPLPTLQRWEEITG-HT 368
Cdd:PRK07656 244 PDEVFRLIETERI---TVLPGPPTMYNSLLQHPDRSAE-----DL------SSLRLAVTGAASMPVALLERFESELGvDI 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 369 LLERYGMTE-IGMALSNPLKGPR--IPGAVGSPLPRVEVRIVmnnttnttivlgdhrNTRVCPGLEGKEGELLVRGPSVF 445
Cdd:PRK07656 310 VLTGYGLSEaSGVTTFNRLDDDRktVAGTIGTAIAGVENKIV---------------NELGEEVPVGEVGELLVRGPNVM 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 446 KEYWNKPQETRESfIDG-GWFKTGDT-VVYKDGVYWIMGRSSvDIIKSAGYKISALEVERHLLAHPDIIDVAVIGAPDAI 523
Cdd:PRK07656 375 KGYYDDPEATAAA-IDAdGWLHTGDLgRLDEEGYLYIVDRKK-DMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDER 452
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1250165799 524 WGQKVTAVVQLRKGQSMTLPDLKTWAREHMAPYTIPTGLLLVEEMPRNQMGKVNKKDL 581
Cdd:PRK07656 453 LGEVGKAYVVLKPGAELTEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRAL 510
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
62-492 |
2.05e-86 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 274.57 E-value: 2.05e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 62 VFVRAPAFGDKPAIIDSSG-SHSYKQLYCsslgLAGRISTALnLDFGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVP 140
Cdd:pfam00501 1 LERQAARTPDKTALEVGEGrRLTYRELDE----RANRLAAGL-RALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 141 LFRKHPQSELEYIISDSQSSLLVAGH--------PYAGTLEPLALKLGLPCLTLPPTSNLGTLDGTDTQEKEAAITDWAD 212
Cdd:pfam00501 76 LNPRLPAEELAYILEDSGAKVLITDDalkleellEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVPPPPPPPPDPD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 213 RPAMIIYTSGTTGRPKGVLHMHSNIQAMVQGLVSEWAW----TRDDVILHTLPLHHVHGIVNKLLCPLWVGATCVMLPEF 288
Cdd:pfam00501 156 DLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPRgfglGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVVLPPGF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 289 QPQKVWEMLLSSKAPMVNVFMAVPTIYSKLIQyydqhftQPHVKDFVRAvckeRIRLMVSGSAALPLPTLQRWEEITGHT 368
Cdd:pfam00501 236 PALDPAALLELIERYKVTVLYGVPTLLNMLLE-------AGAPKRALLS----SLRLVLSGGAPLPPELARRFRELFGGA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 369 LLERYGMTEIGMALSNPLKGP---RIPGAVGSPLPRVEVRIVmnnttnttivlgDHRNTRVCPglEGKEGELLVRGPSVF 445
Cdd:pfam00501 305 LVNGYGLTETTGVVTTPLPLDedlRSLGSVGRPLPGTEVKIV------------DDETGEPVP--PGEPGELCVRGPGVM 370
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1250165799 446 KEYWNKPQETRESFIDGGWFKTGDTVVY-KDGVYWIMGRSSvDIIKSA 492
Cdd:pfam00501 371 KGYLNDPELTAEAFDEDGWYRTGDLGRRdEDGYLEIVGRKK-DQIKLG 417
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
70-576 |
3.66e-83 |
|
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: 269.24 E-value: 3.66e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 70 GDKPAIIDSSGSHSYKQLYCSSLGLAGRISTAlnldfgGLE-GKRISFLCANDASYTVAQWAAWMSGGTAVPLFRKHPQS 148
Cdd:cd05959 18 GDKTAFIDDAGSLTYAELEAEARRVAGALRAL------GVKrEERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 149 ELEYIISDSQSSLLVAGHPYAGTLEPLALKLGLPCLTL---------PPTSNLGTLDGTDTQEKEAAITdWADRPAMIIY 219
Cdd:cd05959 92 DYAYYLEDSRARVVVVSGELAPVLAAALTKSEHTLVVLivsggagpeAGALLLAELVAAEAEQLKPAAT-HADDPAFWLY 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 220 TSGTTGRPKGVLHMHSNIQAMVQGLVSE-WAWTRDDVILHTLPLHHVHGIVNKLLCPLWVGATCVMLPEF-QPQKVWEML 297
Cdd:cd05959 171 SSGSTGRPKGVVHLHADIYWTAELYARNvLGIREDDVCFSAAKLFFAYGLGNSLTFPLSVGATTVLMPERpTPAAVFKRI 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 298 LSSKApmvNVFMAVPTIYSKLIQYYDqhftqPHVKDFVRavckerIRLMVSGSAALPLPTLQRWEEITGHTLLERYGMTE 377
Cdd:cd05959 251 RRYRP---TVFFGVPTLYAAMLAAPN-----LPSRDLSS------LRLCVSAGEALPAEVGERWKARFGLDILDGIGSTE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 378 IG-MALSNpLKGPRIPGAVGSPLPRVEVRIVMNNTTNTTivlgdhrntrvcpglEGKEGELLVRGPSVFKEYWNKPQETR 456
Cdd:cd05959 317 MLhIFLSN-RPGRVRYGTTGKPVPGYEVELRDEDGGDVA---------------DGEPGELYVRGPSSATMYWNNRDKTR 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 457 ESFiDGGWFKTGDT-VVYKDGVYWIMGRSSvDIIKSAGYKISALEVERHLLAHPDIIDVAVIGAPDAIWGQKVTAVVQLR 535
Cdd:cd05959 381 DTF-QGEWTRTGDKyVRDDDGFYTYAGRAD-DMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLR 458
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1250165799 536 KGQSMT--LPD-LKTWAREHMAPYTIPTGLLLVEEMPRNQMGKV 576
Cdd:cd05959 459 PGYEDSeaLEEeLKEFVKDRLAPYKYPRWIVFVDELPKTATGKI 502
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
69-580 |
2.76e-80 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 263.40 E-value: 2.76e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 69 FGDKPAIIDSSGSHSYKQLycssLGLAGRISTALNlDFGGLEGKRISFLCANDASYTVAQWAAWMSGGTAV---PLFRKH 145
Cdd:PRK05605 45 FGDRPALDFFGATTTYAEL----GKQVRRAAAGLR-ALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVehnPLYTAH 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 146 pqsELEYIISDSQSSLLVAGHPYAGTLEPL------------------------ALKLGLP-------CLTLPP------ 188
Cdd:PRK05605 120 ---ELEHPFEDHGARVAIVWDKVAPTVERLrrttpletivsvnmiaampllqrlALRLPIPalrkaraALTGPApgtvpw 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 189 ---TSNLGTLDGTDTQEKEAAITDwadrPAMIIYTSGTTGRPKGVLHMHSNIQA-MVQGLvsewAWT-----RDDVILHT 259
Cdd:PRK05605 197 etlVDAAIGGDGSDVSHPRPTPDD----VALILYTSGTTGKPKGAQLTHRNLFAnAAQGK----AWVpglgdGPERVLAA 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 260 LPLHHVHGIVNKLLCPLWVGATCVMLPEFQPQKVWEMLlssKAPMVNVFMAVPTIYSKLiqyydqhftqphvkdfvRAVC 339
Cdd:PRK05605 269 LPMFHAYGLTLCLTLAVSIGGELVLLPAPDIDLILDAM---KKHPPTWLPGVPPLYEKI-----------------AEAA 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 340 KER------IRLMVSGSAALPLPTLQRWEEITGHTLLERYGMTEIG-MALSNPLKGPRIPGAVGSPLPRVEVRIVmnNTT 412
Cdd:PRK05605 329 EERgvdlsgVRNAFSGAMALPVSTVELWEKLTGGLLVEGYGLTETSpIIVGNPMSDDRRPGYVGVPFPDTEVRIV--DPE 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 413 NTTIVLGDhrntrvcpgleGKEGELLVRGPSVFKEYWNKPQETRESFIDGgWFKTGDTVVYK-DGVYWIMGRSSvDIIKS 491
Cdd:PRK05605 407 DPDETMPD-----------GEEGELLVRGPQVFKGYWNRPEETAKSFLDG-WFRTGDVVVMEeDGFIRIVDRIK-ELIIT 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 492 AGYKISALEVERHLLAHPDIIDVAVIGAPDAIWGQKVTAVVQLRKGQSMTLPDLKTWAREHMAPYTIPTGLLLVEEMPRN 571
Cdd:PRK05605 474 GGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEPGAALDPEGLRAYCREHLTRYKVPRRFYHVDELPRD 553
|
....*....
gi 1250165799 572 QMGKVNKKD 580
Cdd:PRK05605 554 QLGKVRRRE 562
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
66-576 |
3.81e-79 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 260.04 E-value: 3.81e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 66 APAFGDKPAII--DSSGSH---SYKQLYcsslGLAGRISTALnLDFGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVP 140
Cdd:COG0365 19 AEGRGDKVALIweGEDGEErtlTYAELR----REVNRFANAL-RALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 141 ---LFRKHpqsELEYIISDSQSSLLVA--GHPYAGTLEPLALKL-----GLP----CLTLPPTSNLGTLDGT-------D 199
Cdd:COG0365 94 vfpGFGAE---ALADRIEDAEAKVLITadGGLRGGKVIDLKEKVdealeELPslehVIVVGRTGADVPMEGDldwdellA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 200 TQEKEAAITD-WADRPAMIIYTSGTTGRPKGVLHMHSNIQAMVQGLVSEWA-WTRDDVILHTLPLHHVHGIVNKLLCPLW 277
Cdd:COG0365 171 AASAEFEPEPtDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYVLdLKPGDVFWCTADIGWATGHSYIVYGPLL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 278 VGATCVML---PEFQ-PQKVWEMLlsSKAPmVNVFMAVPTIYSKLIQYYDQHFTQPhvkDFVRavckerIRLMVSGSAAL 353
Cdd:COG0365 251 NGATVVLYegrPDFPdPGRLWELI--EKYG-VTVFFTAPTAIRALMKAGDEPLKKY---DLSS------LRLLGSAGEPL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 354 PLPTLQRWEEITGHTLLERYGMTEIGMA-LSNPLKGPRIPGAVGSPLPRVEVRIVmnnttnttivlgDHrNTRVCPGleG 432
Cdd:COG0365 319 NPEVWEWWYEAVGVPIVDGWGQTETGGIfISNLPGLPVKPGSMGKPVPGYDVAVV------------DE-DGNPVPP--G 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 433 KEGELLVRG--PSVFKEYWNKPQETRESFID--GGWFKTGDTVVY-KDGVYWIMGRSSvDIIKSAGYKISALEVERHLLA 507
Cdd:COG0365 384 EEGELVIKGpwPGMFRGYWNDPERYRETYFGrfPGWYRTGDGARRdEDGYFWILGRSD-DVINVSGHRIGTAEIESALVS 462
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1250165799 508 HPDIIDVAVIGAPDAIWGQKVTAVVQLRKGQsmTLPD-----LKTWAREHMAPYTIPTGLLLVEEMPRNQMGKV 576
Cdd:COG0365 463 HPAVAEAAVVGVPDEIRGQVVKAFVVLKPGV--EPSDelakeLQAHVREELGPYAYPREIEFVDELPKTRSGKI 534
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
74-577 |
5.12e-74 |
|
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: 244.43 E-value: 5.12e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 74 AIIDSSGSH--SYKQLycssLGLAGRISTALNlDFGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLFRKHPQSELE 151
Cdd:cd05911 1 AQIDADTGKelTYAQL----RTLSRRLAAGLR-KLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 152 YIISDSQSSLL-VAGHPYAGTLEPLALKLGLPCLTLPPTSNLGTLDGTDTQEKEAAITDW---------ADRPAMIIYTS 221
Cdd:cd05911 76 HQLKISKPKVIfTDPDGLEKVKEAAKELGPKDKIIVLDDKPDGVLSIEDLLSPTLGEEDEdlppplkdgKDDTAAILYSS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 222 GTTGRPKGVLHMHSNIQA---MVQGLVSEWAWtRDDVILHTLPLHHVHGIvNKLLCPLWVGATCVMLPEFQPQKVWEMLL 298
Cdd:cd05911 156 GTTGLPKGVCLSHRNLIAnlsQVQTFLYGNDG-SNDVILGFLPLYHIYGL-FTTLASLLNGATVIIMPKFDSELFLDLIE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 299 SSKAPMVNVfmaVPTIYSKLIQYydqhftqphvKDFVRAVCKErIRLMVSGSAALplptLQRWEE-----ITGHTLLERY 373
Cdd:cd05911 234 KYKITFLYL---VPPIAAALAKS----------PLLDKYDLSS-LRVILSGGAPL----SKELQEllakrFPNATIKQGY 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 374 GMTEIGMALSNPLKGPRIPGAVGSPLPRVEVRIVmnnTTNTTIVLGDhrntrvcpgleGKEGELLVRGPSVFKEYWNKPQ 453
Cdd:cd05911 296 GMTETGGILTVNPDGDDKPGSVGRLLPNVEAKIV---DDDGKDSLGP-----------NEPGEICVRGPQVMKGYYNNPE 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 454 ETRESFIDGGWFKTGDtVVY--KDGVYWIMGRSSvDIIKSAGYKISALEVERHLLAHPDIIDVAVIGAPDAIWGQKVTAV 531
Cdd:cd05911 362 ATKETFDEDGWLHTGD-IGYfdEDGYLYIVDRKK-ELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAY 439
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1250165799 532 VQLRKGQSMTLPDLKTWAREHMAPYT-IPTGLLLVEEMPRNQMGKVN 577
Cdd:cd05911 440 VVRKPGEKLTEKEVKDYVAKKVASYKqLRGGVVFVDEIPKSASGKIL 486
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
64-576 |
6.27e-74 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 245.64 E-value: 6.27e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 64 VRAPAFGDKPAIIDSSGSHSYKQLYCSSLGLAGRISTALnldfGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLFR 143
Cdd:PRK08314 18 VSARRYPDKTAIVFYGRAISYRELLEEAERLAGYLQQEC----GVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 144 KHPQSELEYIISDSQSSLLVAGHPYAGTLEPLALKLGLPCL-------TLPPTSNLGTLDGTDTQ-----EKEAAITDWA 211
Cdd:PRK08314 94 MNREEELAHYVTDSGARVAIVGSELAPKVAPAVGNLRLRHVivaqysdYLPAEPEIAVPAWLRAEpplqaLAPGGVVAWK 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 212 D------RP----------AMIIYTSGTTGRPKGVLHMHSNIQAMVQGLVsewAW---TRDDVILHTLPLHHVHGIVNKL 272
Cdd:PRK08314 174 EalaaglAPpphtagpddlAVLPYTSGTTGVPKGCMHTHRTVMANAVGSV---LWsnsTPESVVLAVLPLFHVTGMVHSM 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 273 LCPLWVGATCVMLPEfqpqkvWEMLLSSKA---PMVNVFMAVPTIyskLIQYydqhFTQPHVKDFvravCKERIRLMVSG 349
Cdd:PRK08314 251 NAPIYAGATVVLMPR------WDREAAARLierYRVTHWTNIPTM---VVDF----LASPGLAER----DLSSLRYIGGG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 350 SAALPLPTLQRWEEITGHTLLERYGMTE-IGMALSNPLKGPRiPGAVGSPLPRVEVRIVmnnttnttivlgDHRNTRVCP 428
Cdd:PRK08314 314 GAAMPEAVAERLKELTGLDYVEGYGLTEtMAQTHSNPPDRPK-LQCLGIPTFGVDARVI------------DPETLEELP 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 429 glEGKEGELLVRGPSVFKEYWNKPQETRESFI--DGG-WFKTGDTVVYKDGVYWIMgrssVDIIK----SAGYKISALEV 501
Cdd:PRK08314 381 --PGEVGEIVVHGPQVFKGYWNRPEATAEAFIeiDGKrFFRTGDLGRMDEEGYFFI----TDRLKrminASGFKVWPAEV 454
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1250165799 502 ERHLLAHPDIIDVAVIGAPDAIWGQKVTAVVQLRKGQ--SMTLPDLKTWAREHMAPYTIPTGLLLVEEMPRNQMGKV 576
Cdd:PRK08314 455 ENLLYKHPAIQEACVIATPDPRRGETVKAVVVLRPEArgKTTEEEIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKI 531
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
88-581 |
1.32e-71 |
|
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: 236.03 E-value: 1.32e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 88 YCSSLGLAGRISTALnLDFGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLFRKHPQSELEYIISDSQSSLLVaghp 167
Cdd:cd05934 6 YAELLRESARIAAAL-AALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 168 yagtleplalklglpcltlpptsnlgtldgtdtqekeaaiTDwadrPAMIIYTSGTTGRPKGVLHMHSNIQAMVQGLVSE 247
Cdd:cd05934 81 ----------------------------------------VD----PASILYTSGTTGPPKGVVITHANLTFAGYYSARR 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 248 WAWTRDDVILHTLPLHHVHGIVNKLLCPLWVGATCVMLPEFQPQKVWEMLLSSKAPMVNVFMAVPTIYSKliqyydqhfT 327
Cdd:cd05934 117 FGLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLLPRFSASRFWSDVRRYGATVTNYLGAMLSYLLA---------Q 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 328 QPHVKDfvravCKERIRLmVSGSAALPLpTLQRWEEITGHTLLERYGMTEIGMALSNPLKGPRIPGAVGSPLPRVEVRIV 407
Cdd:cd05934 188 PPSPDD-----RAHRLRA-AYGAPNPPE-LHEEFEERFGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAPGYEVRIV 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 408 mnnttnttivlGDHrnTRVCPglEGKEGELLVR---GPSVFKEYWNKPQETRESFiDGGWFKTGDTVVY-KDGVYWIMGR 483
Cdd:cd05934 261 -----------DDD--GQELP--AGEPGELVIRglrGWGFFKGYYNMPEATAEAM-RNGWFHTGDLGYRdADGFFYFVDR 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 484 SSvDIIKSAGYKISALEVERHLLAHPDIIDVAVIGAPDAIWGQKVTAVVQLRKGQSMTLPDLKTWAREHMAPYTIPTGLL 563
Cdd:cd05934 325 KK-DMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLDPEELFAFCEGQLAYFKVPRYIR 403
|
490
....*....|....*...
gi 1250165799 564 LVEEMPRNQMGKVNKKDL 581
Cdd:cd05934 404 FVDDLPKTPTEKVAKAQL 421
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
81-581 |
4.98e-71 |
|
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: 234.68 E-value: 4.98e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 81 SHSYKQLYCSSLGLAGRIStalnlDFGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLFRKHPQSELEYIISDSQSS 160
Cdd:cd05935 1 SLTYLELLEVVKKLASFLS-----NKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 161 LLVAGhpyaGTLEPLALklglpcltlpptsnlgtldgtdtqekeaaitdwadrpamIIYTSGTTGRPKGVLHMHSNIQAM 240
Cdd:cd05935 76 VAVVG----SELDDLAL---------------------------------------IPYTSGTTGLPKGCMHTHFSAAAN 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 241 VQGLVSEWAWTRDDVILHTLPLHHVHGIVNKLLCPLWVGATCVMLPEFQPQKVWEMLLSSKA-------PMVNVFMAVPT 313
Cdd:cd05935 113 ALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMARWDRETALELIEKYKVtfwtnipTMLVDLLATPE 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 314 IyskliqyydqhftqphvkdfvRAVCKERIRLMVSGSAALPLPTLQRWEEITGHTLLERYGMTE-IGMALSNPLKGPRIP 392
Cdd:cd05935 193 F---------------------KTRDLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTEtMSQTHTNPPLRPKLQ 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 393 gAVGSPLPRVEVRIVmnnTTNTTIVLGDhrntrvcpgleGKEGELLVRGPSVFKEYWNKPQETRESFI-DGG--WFKTGD 469
Cdd:cd05935 252 -CLGIP*FGVDARVI---DIETGRELPP-----------NEVGEIVVRGPQIFKGYWNRPEETEESFIeIKGrrFFRTGD 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 470 tVVYKD--GVYWIMGRSSvDIIKSAGYKISALEVERHLLAHPDIIDVAVIGAPDAIWGQKVTAVVQLRKGQSMTLP--DL 545
Cdd:cd05935 317 -LGYMDeeGYFFFVDRVK-RMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEYRGKVTeeDI 394
|
490 500 510
....*....|....*....|....*....|....*.
gi 1250165799 546 KTWAREHMAPYTIPTGLLLVEEMPRNQMGKVNKKDL 581
Cdd:cd05935 395 IEWAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
71-583 |
5.08e-71 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 236.68 E-value: 5.08e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 71 DKPAIIDSSGSHSYKQLYcsslGLAGRISTALNLDFGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLFRKHPQSEL 150
Cdd:PRK06839 17 DRIAIITEEEEMTYKQLH----EYVSKVAAYLIYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENEL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 151 EYIISDSQSSLLVAGHPYAGTLEPLALKLGLPcltlPPTSnLGTLDGTDTQEKEAAITDWADRPAMIIYTSGTTGRPKGV 230
Cdd:PRK06839 93 IFQLKDSGTTVLFVEKTFQNMALSMQKVSYVQ----RVIS-ITSLKEIEDRKIDNFVEKNESASFIICYTSGTTGKPKGA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 231 LHMHSNIQAMVQGLVSEWAWTRDDVILHTLPLHHVHGIvNKLLCPLWVGATCVMLP-EFQPQKVWEMLLSSKapmVNVFM 309
Cdd:PRK06839 168 VLTQENMFWNALNNTFAIDLTMHDRSIVLLPLFHIGGI-GLFAFPTLFAGGVIIVPrKFEPTKALSMIEKHK---VTVVM 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 310 AVPTIYSKLIQYYDqhFTQPHVkdfvravckERIRLMVSGSAALPLPTLQRWEEiTGHTLLERYGMTE----IGMALSNP 385
Cdd:PRK06839 244 GVPTIHQALINCSK--FETTNL---------QSVRWFYNGGAPCPEELMREFID-RGFLFGQGFGMTEtsptVFMLSEED 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 386 LKgpRIPGAVGSPLPRVEVRIVMNNTTNTTIvlgdhrntrvcpgleGKEGELLVRGPSVFKEYWNKPQETRESfIDGGWF 465
Cdd:PRK06839 312 AR--RKVGSIGKPVLFCDYELIDENKNKVEV---------------GEVGELLIRGPNVMKEYWNRPDATEET-IQDGWL 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 466 KTGDTV-VYKDGVYWIMGRSSvDIIKSAGYKISALEVERHLLAHPDIIDVAVIGAPDAIWGQKVTAVVQLRKGQSMTLPD 544
Cdd:PRK06839 374 CTGDLArVDEDGFVYIVGRKK-EMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVLIEKD 452
|
490 500 510
....*....|....*....|....*....|....*....
gi 1250165799 545 LKTWAREHMAPYTIPTGLLLVEEMPRNQMGKVNKKDLLR 583
Cdd:PRK06839 453 VIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQLVN 491
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
62-581 |
1.14e-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: 233.28 E-value: 1.14e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 62 VFVRAPAFGDKPAIIDSSG--SHSYKQLYCSSLGLAGRISTAlnldfGGLEGKRISFLCANDASYTVAQWAAwMSGG--- 136
Cdd:cd05904 11 SFLFASAHPSRPALIDAATgrALTYAELERRVRRLAAGLAKR-----GGRKGDVVLLLSPNSIEFPVAFLAV-LSLGavv 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 137 -TAVPLFRkhpQSELEYIISDSQSSLLVAGHPYAGTLEPLALKLGL--PCLTLPPTSNLGTLDGTDTQEKEAAITdwADR 213
Cdd:cd05904 85 tTANPLST---PAEIAKQVKDSGAKLAFTTAELAEKLASLALPVVLldSAEFDSLSFSDLLFEADEAEPPVVVIK--QDD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 214 PAMIIYTSGTTGRPKGVLHMHSNIQAMVQGLVSEWAWT--RDDVILHTLPLHHVHGIVNKLLCPLWVGATCVMLPEFQPQ 291
Cdd:cd05904 160 VAALLYSSGTTGRSKGVMLTHRNLIAMVAQFVAGEGSNsdSEDVFLCVLPMFHIYGLSSFALGLLRLGATVVVMPRFDLE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 292 KVWEMLLSSKapmVNVFMAVPTIYSKLIQyydqhftQPHVKDFVRAvckeRIRLMVSGSAALPLPTLQRWEEITGHT-LL 370
Cdd:cd05904 240 ELLAAIERYK---VTHLPVVPPIVLALVK-------SPIVDKYDLS----SLRQIMSGAAPLGKELIEAFRAKFPNVdLG 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 371 ERYGMTE---IGMALSNPLKGPRIPGAVGSPLPRVEVRIVmnnTTNTTIVLGdhrntrvcpglEGKEGELLVRGPSVFKE 447
Cdd:cd05904 306 QGYGMTEstgVVAMCFAPEKDRAKYGSVGRLVPNVEAKIV---DPETGESLP-----------PNQTGELWIRGPSIMKG 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 448 YWNKPQETRESFIDGGWFKTGDtVVY--KDGVYWIMGRSSvDIIKSAGYKISALEVERHLLAHPDIIDVAVIGAPDAIWG 525
Cdd:cd05904 372 YLNNPEATAATIDKEGWLHTGD-LCYidEDGYLFIVDRLK-ELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAG 449
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1250165799 526 QKVTAVVQLRKGQSMTLPDLKTWAREHMAPYTIPTGLLLVEEMPRNQMGKVNKKDL 581
Cdd:cd05904 450 EVPMAFVVRKPGSSLTEDEIMDFVAKQVAPYKKVRKVAFVDAIPKSPSGKILRKEL 505
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
111-578 |
4.39e-69 |
|
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: 229.96 E-value: 4.39e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 111 GKRISFLCANDASYTVAQWAAWMSGGTAVPL---FRKHpqsELEYIISDSQSSLLVAGHPYAGTlEPLALklglpcltlp 187
Cdd:cd05903 26 GDVVAFQLPNWWEFAVLYLACLRIGAVTNPIlpfFREH---ELAFILRRAKAKVFVVPERFRQF-DPAAM---------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 188 ptsnlgtldgtdtqekeaaitdwADRPAMIIYTSGTTGRPKGVLHMHSNIQAMVQGLVSEWAWTRDDVILHTLPLHHVHG 267
Cdd:cd05903 92 -----------------------PDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPGDVFLVASPMAHQTG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 268 IVNKLLCPLWVGATCVMLPEFQPQKVWEMLLSSKapmVNVFMAVPTIYSKLIQyydqhftqpHVKDFVRAVCkeRIRLMV 347
Cdd:cd05903 149 FVYGFTLPLLLGAPVVLQDIWDPDKALALMREHG---VTFMMGATPFLTDLLN---------AVEEAGEPLS--RLRTFV 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 348 SGSAALPLPTLQRWEEITGHTLLERYGMTEIGMALSNPLKGP--RIPGAVGSPLPRVEVRIVmnnttnttivlgDHRNTR 425
Cdd:cd05903 215 CGGATVPRSLARRAAELLGAKVCSAYGSTECPGAVTSITPAPedRRLYTDGRPLPGVEIKVV------------DDTGAT 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 426 VCPGlegKEGELLVRGPSVFKEYWNKPQETRESFiDGGWFKTGDTVVYKDGVYW-IMGRSSvDIIKSAGYKISALEVERH 504
Cdd:cd05903 283 LAPG---VEGELLSRGPSVFLGYLDRPDLTADAA-PEGWFRTGDLARLDEDGYLrITGRSK-DIIIRGGENIPVLEVEDL 357
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1250165799 505 LLAHPDIIDVAVIGAPDAIWGQKVTAVVQLRKGQSMTLPDLKTW-AREHMAPYTIPTGLLLVEEMPRNQMGKVNK 578
Cdd:cd05903 358 LLGHPGVIEAAVVALPDERLGERACAVVVTKSGALLTFDELVAYlDRQGVAKQYWPERLVHVDDLPRTPSGKVQK 432
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
33-581 |
1.80e-68 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 230.59 E-value: 1.80e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 33 PGQWLLGSVVHRRAHRwtaaqssrinqkpvfvrapaFGDKPAIIDSSGSHSYKQLYcsslGLAGRISTALnLDFGGLEGK 112
Cdd:PRK08316 8 ARRQTIGDILRRSARR--------------------YPDKTALVFGDRSWTYAELD----AAVNRVAAAL-LDLGLKKGD 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 113 RISFLCANDASYTVAQWAAWMSGGTAVPLFRKHPQSELEYIISDSQSSLLVAGHPYAGTLEPLALKLGLPCLTLPPTsnl 192
Cdd:PRK08316 63 RVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARAFLVDPALAPTAEAALALLPVDTLILSLV--- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 193 gtLDGTDTQEKEAAITDWA--------------DRPAMIIYTSGTTGRPKGVLHMHSNIQAMVQGLVSEWAWTRDDVILH 258
Cdd:PRK08316 140 --LGGREAPGGWLDFADWAeagsvaepdveladDDLAQILYTSGTESLPKGAMLTHRALIAEYVSCIVAGDMSADDIPLH 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 259 TLPLHHVHGIVNKLLCPLWVGATCVMLPEFQPQKVWEMLLSSKAPMvnvFMAVPTIYSKLIQY--YDQHFTQPHVKDFVr 336
Cdd:PRK08316 218 ALPLYHCAQLDVFLGPYLYVGATNVILDAPDPELILRTIEAERITS---FFAPPTVWISLLRHpdFDTRDLSSLRKGYY- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 337 avckerirlmvsGSAALPLPTLQRweeitghtLLER---------YGMTEIGmalsnPLK---GP----RIPGAVGSPLP 400
Cdd:PRK08316 294 ------------GASIMPVEVLKE--------LRERlpglrfyncYGQTEIA-----PLAtvlGPeehlRRPGSAGRPVL 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 401 RVEVRIVmnnttnttivlgDHRNTRVCPGLEGkegELLVRGPSVFKEYWNKPQETRESFiDGGWFKTGDTVVY-KDGVYW 479
Cdd:PRK08316 349 NVETRVV------------DDDGNDVAPGEVG---EIVHRSPQLMLGYWDDPEKTAEAF-RGGWFHSGDLGVMdEEGYIT 412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 480 IMGRSSvDIIKSAGYKISALEVERHLLAHPDIIDVAVIGAPDAIWGQKVTAVVQLRKGQSMTLPDLKTWAREHMAPYTIP 559
Cdd:PRK08316 413 VVDRKK-DMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAGATVTEDELIAHCRARLAGFKVP 491
|
570 580
....*....|....*....|..
gi 1250165799 560 TGLLLVEEMPRNQMGKVNKKDL 581
Cdd:PRK08316 492 KRVIFVDELPRNPSGKILKREL 513
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
65-579 |
2.67e-67 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 229.60 E-value: 2.67e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 65 RAPAFGDKPAIIDSSG----SHSYKQLYcsslGLAGRISTAL-NLdfgGLE-GKRISFLCANDASYTVAQWAAWMSGGTA 138
Cdd:COG1022 20 RAARFPDRVALREKEDgiwqSLTWAEFA----ERVRALAAGLlAL---GVKpGDRVAILSDNRPEWVIADLAILAAGAVT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 139 VPLFRKHPQSELEYIISDSQSSLLVAGHPY-AGTLepLALKLGLPCL---------TLPPTSNLGTLD-----GTDTQEK 203
Cdd:COG1022 93 VPIYPTSSAEEVAYILNDSGAKVLFVEDQEqLDKL--LEVRDELPSLrhivvldprGLRDDPRLLSLDellalGREVADP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 204 E------AAITdwADRPAMIIYTSGTTGRPKGVLHMHSNIQAMVQGLVSEWAWTRDDVILHTLPLHHVHGIVNKLLCpLW 277
Cdd:COG1022 171 AelearrAAVK--PDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFLPLAHVFERTVSYYA-LA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 278 VGATCV----------MLPEFQPQ------KVWEMLLSS-----------KAPMVNVFMAVPTIYSKliqYYDQHFTQPH 330
Cdd:COG1022 248 AGATVAfaespdtlaeDLREVKPTfmlavpRVWEKVYAGiqakaeeagglKRKLFRWALAVGRRYAR---ARLAGKSPSL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 331 VKDFVRAVC--------KE----RIRLMVSGSAALPlPTLQRWEEITGHTLLERYGMTEI-GMALSNPLKGPRIpGAVGS 397
Cdd:COG1022 325 LLRLKHALAdklvfsklREalggRLRFAVSGGAALG-PELARFFRALGIPVLEGYGLTETsPVITVNRPGDNRI-GTVGP 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 398 PLPRVEVRIvmnnttnttivlgdhrntrvcpgleGKEGELLVRGPSVFKEYWNKPQETRESFIDGGWFKTGDtVVY--KD 475
Cdd:COG1022 403 PLPGVEVKI-------------------------AEDGEILVRGPNVMKGYYKNPEATAEAFDADGWLHTGD-IGEldED 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 476 GVYWIMGRSSvDIIK-SAGYKISALEVERHLLAHPDIIDVAVIGApdaiwGQK-VTAVVQLRkgqsmtlPD-LKTWAREH 552
Cdd:COG1022 457 GFLRITGRKK-DLIVtSGGKNVAPQPIENALKASPLIEQAVVVGD-----GRPfLAALIVPD-------FEaLGEWAEEN 523
|
570 580 590
....*....|....*....|....*....|
gi 1250165799 553 MAPYTIPTGLL---LVEEMPRNQMGKVNKK 579
Cdd:COG1022 524 GLPYTSYAELAqdpEVRALIQEEVDRANAG 553
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
70-578 |
1.29e-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: 225.49 E-value: 1.29e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 70 GDKPAIIDSSGSHSYKQLYCSSLGLAGRISTAlnldfgGLEGK-RISFLCANDASYTVAQWAAWMSGGTAVPLFRKHPQS 148
Cdd:TIGR02262 19 GGKTAFIDDISSLSYGELEAQVRRLAAALRRL------GVKREeRVLLLMLDGVDFPIAFLGAIRAGIVPVALNTLLTAD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 149 ELEYIISDSQSSLLVAGHPYAGTLEPLALKLglPCL--------TLPPTSNLGTLDGTDTQEKEAAITDwADRPAMIIYT 220
Cdd:TIGR02262 93 DYAYMLEDSRARVVFVSGALLPVIKAALGKS--PHLehrvvvgrPEAGEVQLAELLATESEQFKPAATQ-ADDPAFWLYS 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 221 SGTTGRPKGVLHMHSNIQAMVQGLVSEWAWTR-DDVILHTLPLHHVHGIVNKLLCPLWVGATCVMLPEF-QPQKVWEMLL 298
Cdd:TIGR02262 170 SGSTGMPKGVVHTHSNPYWTAELYARNTLGIReDDVCFSAAKLFFAYGLGNALTFPMSVGATTVLMGERpTPDAVFDRLR 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 299 SSKApmvNVFMAVPTIYSKLIQYYDqhftqphvkdfVRAVCKERIRLMVSGSAALPLPTLQRWEEITGHTLLERYGMTEI 378
Cdd:TIGR02262 250 RHQP---TIFYGVPTLYAAMLADPN-----------LPSEDQVRLRLCTSAGEALPAEVGQRWQARFGVDIVDGIGSTEM 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 379 G-MALSNplkgprIPGAV-----GSPLPRVEVRIVMNNTTNTTivlgdhrntrvcpglEGKEGELLVRGPSVFKEYWNKP 452
Cdd:TIGR02262 316 LhIFLSN------LPGDVrygtsGKPVPGYRLRLVGDGGQDVA---------------DGEPGELLISGPSSATMYWNNR 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 453 QETRESFIdGGWFKTGDT-VVYKDGVYWIMGRSSvDIIKSAGYKISALEVERHLLAHPDIIDVAVIGAPDAIWGQKVTAV 531
Cdd:TIGR02262 375 AKSRDTFQ-GEWTRSGDKyVRNDDGSYTYAGRTD-DMLKVSGIYVSPFEIESALIQHPAVLEAAVVGVADEDGLIKPKAF 452
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1250165799 532 VQLRKGQSMTLPDLKTWAREHMAPYTIPTGLLLVEEMPRNQMGKVNK 578
Cdd:TIGR02262 453 VVLRPGQTALETELKEHVKDRLAPYKYPRWIVFVDDLPKTATGKIQR 499
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
108-579 |
1.97e-64 |
|
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: 217.85 E-value: 1.97e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 108 GLE-GKRISFLCANDASYTVAQWAAWMSGGTAVPLFRKHPQSELEYIISDSQSSLLVAGHPyagtleplalklglpcltl 186
Cdd:cd05907 26 GVEpGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFVEDP------------------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 187 pptsnlgtldgtdtqekeaaitdwaDRPAMIIYTSGTTGRPKGVLHMHSNIQAMVQGLVSEWAWTRDDVILHTLPLHHVH 266
Cdd:cd05907 87 -------------------------DDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPATEGDRHLSFLPLAHVF 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 267 GIVNKLLCPLWVGATCV----------MLPEFQPQkvwemllsskapmvnVFMAVPTIYSKLIQYYDQHFTQPHVKDFVR 336
Cdd:cd05907 142 ERRAGLYVPLLAGARIYfassaetlldDLSEVRPT---------------VFLAVPRVWEKVYAAIKVKAVPGLKRKLFD 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 337 AVCKERIRLMVSGSAALPLPTLQRWEEItGHTLLERYGMTEIGMALS-NPLKGPRIpGAVGSPLPRVEVRIvmnnttntt 415
Cdd:cd05907 207 LAVGGRLRFAASGGAPLPAELLHFFRAL-GIPVYEGYGLTETSAVVTlNPPGDNRI-GTVGKPLPGVEVRI--------- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 416 ivlgdhrntrvcpgleGKEGELLVRGPSVFKEYWNKPQETRESFIDGGWFKTGDTVVYK-DGVYWIMGRSSvDIIKSAGY 494
Cdd:cd05907 276 ----------------ADDGEILVRGPNVMLGYYKNPEATAEALDADGWLHTGDLGEIDeDGFLHITGRKK-DLIITSGG 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 495 K-ISALEVERHLLAHPDIIDVAVIGApdaiwGQK-VTAVVQLRKGQsmtlpdLKTWAREHMAPYTIPTGLL---LVEEMP 569
Cdd:cd05907 339 KnISPEPIENALKASPLISQAVVIGD-----GRPfLVALIVPDPEA------LEAWAEEHGIAYTDVAELAanpAVRAEI 407
|
490
....*....|
gi 1250165799 570 RNQMGKVNKK 579
Cdd:cd05907 408 EAAVEAANAR 417
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
71-581 |
4.28e-64 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 219.09 E-value: 4.28e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 71 DKPAIIDSSGSHSYKQLycsslglAGRISTALNL--DFGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLfrkHPQS 148
Cdd:PRK06188 27 DRPALVLGDTRLTYGQL-------ADRISRYIQAfeALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTAL---HPLG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 149 ELE---YIISDSQ-SSLLVAGHPYAG-TLEPLALKLGLP-CLTLPPTSNLGTLDGTDTQEKEAAITDWADRP--AMIIYT 220
Cdd:PRK06188 97 SLDdhaYVLEDAGiSTLIVDPAPFVErALALLARVPSLKhVLTLGPVPDGVDLLAAAAKFGPAPLVAAALPPdiAGLAYT 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 221 SGTTGRPKGVLHMHSNIQAMVQGLVSEWAWTRDDVILHTLPLHHVHGIvnKLLCPLWVGATCVMLPEFQPQKVWEMLLSS 300
Cdd:PRK06188 177 GGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLSHAGGA--FFLPTLLRGGTVIVLAKFDPAEVLRAIEEQ 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 301 KapmVNVFMAVPT-IYSKLiqyyDQHftQPHVKDFvravckERIRLMVSGSAALPLPTLQRWEEITGHTLLERYGMTEIG 379
Cdd:PRK06188 255 R---ITATFLVPTmIYALL----DHP--DLRTRDL------SSLETVYYGASPMSPVRLAEAIERFGPIFAQYYGQTEAP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 380 MALS------NPLKGPRIPGAVGSPLPRVEVRIvmnnttnttivLGDHRNtrvcPGLEGKEGELLVRGPSVFKEYWNKPQ 453
Cdd:PRK06188 320 MVITylrkrdHDPDDPKRLTSCGRPTPGLRVAL-----------LDEDGR----EVAQGEVGEICVRGPLVMDGYWNRPE 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 454 ETRESFiDGGWFKTGDtVVYKD--GVYWIMGRSSvDIIKSAGYKISALEVERHLLAHPDIIDVAVIGAPDAIWGQKVTAV 531
Cdd:PRK06188 385 ETAEAF-RDGWLHTGD-VAREDedGFYYIVDRKK-DMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAV 461
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1250165799 532 VQLRKGQSMTLPDLKTWAREHMAPYTIPTGLLLVEEMPRNQMGKVNKKDL 581
Cdd:PRK06188 462 VVLRPGAAVDAAELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKAL 511
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
176-581 |
4.51e-63 |
|
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: 213.74 E-value: 4.51e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 176 ALKLGLpcLTLPPTSNLGTLDGTDTQEK---EAAITDwADRPAMIIYTSGTTGRPKGVLHMHSniqAMVQGLVSEWAWT- 251
Cdd:cd05972 45 VIKLGA--VYVPLTTLLGPKDIEYRLEAagaKAIVTD-AEDPALIYFTSGTTGLPKGVLHTHS---YPLGHIPTAAYWLg 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 252 --RDDVILHTLPLHHVHGIVNKLLCPLWVGATCVM--LPEFQPQKVWEMLLSSKapmVNVFMAVPTIYSKLIQyydqhfT 327
Cdd:cd05972 119 lrPDDIHWNIADPGWAKGAWSSFFGPWLLGATVFVyeGPRFDAERILELLERYG---VTSFCGPPTAYRMLIK------Q 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 328 QPHVKDFvravckERIRLMVSGSAALPLPTLQRWEEITGHTLLERYGMTEIGMALSNPLKGPRIPGAVGSPLPRVEVRIV 407
Cdd:cd05972 190 DLSSYKF------SHLRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGLTVGNFPDMPVKPGSMGRPTPGYDVAII 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 408 mnnttnttivlgdHRNTRVCPglEGKEGELLVR--GPSVFKEYWNKPQETRESFIdGGWFKTGDTVVY-KDGVYWIMGRS 484
Cdd:cd05972 264 -------------DDDGRELP--PGEEGDIAIKlpPPGLFLGYVGDPEKTEASIR-GDYYLTGDRAYRdEDGYFWFVGRA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 485 SvDIIKSAGYKISALEVERHLLAHPDIIDVAVIGAPDAIWGQKVTAVVQLRKG---QSMTLPDLKTWAREHMAPYTIPTG 561
Cdd:cd05972 328 D-DIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGyepSEELAEELQGHVKKVLAPYKYPRE 406
|
410 420
....*....|....*....|
gi 1250165799 562 LLLVEEMPRNQMGKVNKKDL 581
Cdd:cd05972 407 IEFVEELPKTISGKIRRVEL 426
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
71-578 |
9.57e-63 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 216.07 E-value: 9.57e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 71 DKPAIIDSSGSH------SYKQLYCsslgLAGRISTALnLDFGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPL--- 141
Cdd:PRK13295 39 DKTAVTAVRLGTgaprrfTYRELAA----LVDRVAVGL-ARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLmpi 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 142 FRKHpqsELEYIISDSQSSLLVA-----GHPYAGTLEplALKLGLPCLtlpptSNLGTL--DGTDTQEKEAAITDW---- 210
Cdd:PRK13295 114 FRER---ELSFMLKHAESKVLVVpktfrGFDHAAMAR--RLRPELPAL-----RHVVVVggDGADSFEALLITPAWeqep 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 211 -------ADRP-----AMIIYTSGTTGRPKGVLHMH----SNIQAMVQGLvsewAWTRDDVILHTLPLHHVHGIVNKLLC 274
Cdd:PRK13295 184 dapailaRLRPgpddvTQLIYTSGTTGEPKGVMHTAntlmANIVPYAERL----GLGADDVILMASPMAHQTGFMYGLMM 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 275 PLWVGATCVMlpefqpQKVWEmllsskapmvnvfmavPTIYSKLIQYYDQHFTQ---PHVKDFVRAVcKER------IRL 345
Cdd:PRK13295 260 PVMLGATAVL------QDIWD----------------PARAAELIRTEGVTFTMastPFLTDLTRAV-KESgrpvssLRT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 346 MVSGSAALPLPTLQRWEEITGHTLLERYGMTEIGMA----LSNPLKgpRIPGAVGSPLPRVEVRIVmnnttnttivlgDH 421
Cdd:PRK13295 317 FLCAGAPIPGALVERARAALGAKIVSAWGMTENGAVtltkLDDPDE--RASTTDGCPLPGVEVRVV------------DA 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 422 RNTRVCPGlegKEGELLVRGPSVFKEYWNKPQETRESFidGGWFKTGDTV-VYKDGVYWIMGRSSvDIIKSAGYKISALE 500
Cdd:PRK13295 383 DGAPLPAG---QIGRLQVRGCSNFGGYLKRPQLNGTDA--DGWFDTGDLArIDADGYIRISGRSK-DVIIRGGENIPVVE 456
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1250165799 501 VERHLLAHPDIIDVAVIGAPDAIWGQKVTAVVQLRKGQSMTLPDLKTWAREH-MAPYTIPTGLLLVEEMPRNQMGKVNK 578
Cdd:PRK13295 457 IEALLYRHPAIAQVAIVAYPDERLGERACAFVVPRPGQSLDFEEMVEFLKAQkVAKQYIPERLVVRDALPRTPSGKIQK 535
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
65-583 |
1.72e-62 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 215.38 E-value: 1.72e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 65 RAPAFGDKPAIIDSSG-SHSYKQLYCsslgLAGRISTALnLDFGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLFR 143
Cdd:PRK06087 32 TARAMPDKIAVVDNHGaSYTYSALDH----AASRLANWL-LAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 144 KHPQSELEYIISDSQSSLLVAGHPYAGT---LEPLALKLGLPCLT-------LPPTSNLGTLDG--TDTQEKEAAITDWA 211
Cdd:PRK06087 107 SWREAELVWVLNKCQAKMFFAPTLFKQTrpvDLILPLQNQLPQLQqivgvdkLAPATSSLSLSQiiADYEPLTTAITTHG 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 212 DRPAMIIYTSGTTGRPKGVLHMHSNIQAMVQGLVSEWAWTRDDVILHTLPLHHVHGIVNKLLCPLWVGATCVMLPEFQPQ 291
Cdd:PRK06087 187 DELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVLLDIFTPD 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 292 KVWEMLLSSKAPMvnVFMAVPTIYSkLIQYYDQHftQPHVkdfvravckERIRLMVSGSAALPLPTLQRWEEiTGHTLLE 371
Cdd:PRK06087 267 ACLALLEQQRCTC--MLGATPFIYD-LLNLLEKQ--PADL---------SALRFFLCGGTTIPKKVARECQQ-RGIKLLS 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 372 RYGMTE----IGMALSNPLkgPRIPGAVGSPLPRVEVRIVmnnttnttivlGDHRNTRVCpgleGKEGELLVRGPSVFKE 447
Cdd:PRK06087 332 VYGSTEssphAVVNLDDPL--SRFMHTDGYAAAGVEIKVV-----------DEARKTLPP----GCEGEEASRGPNVFMG 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 448 YWNKPQETRESFIDGGWFKTGD-TVVYKDGVYWIMGRSSvDIIKSAGYKISALEVERHLLAHPDIIDVAVIGAPDAIWGQ 526
Cdd:PRK06087 395 YLDEPELTARALDEEGWYYSGDlCRMDEAGYIKITGRKK-DIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGE 473
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1250165799 527 KVTAVVQLRKG-QSMTLPDLKTW-AREHMAPYTIPTGLLLVEEMPRNQMGKVNK----KDLLR 583
Cdd:PRK06087 474 RSCAYVVLKAPhHSLTLEEVVAFfSRKRVAKYKYPEHIVVIDKLPRTASGKIQKfllrKDIMR 536
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
72-581 |
7.39e-61 |
|
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: 208.10 E-value: 7.39e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 72 KPAIIDSSGSHSYKQLycssLGLAGRISTALNLDFGGLEGKRISFLCANDASYTVAQWAAWMSGGTAV---PLFRKhpqS 148
Cdd:cd05958 1 RTCLRSPEREWTYRDL----LALANRIANVLVGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVatmPLLRP---K 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 149 ELEYIISDSQSSLLVAGHpyagtleplalklglpcltlpptsnlgtldgtdtqeKEAAitdwADRPAMIIYTSGTTGRPK 228
Cdd:cd05958 74 ELAYILDKARITVALCAH------------------------------------ALTA----SDDICILAFTSGTTGAPK 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 229 GVLHMHSNIQAMVQGlvseWA-----WTRDDVILHTLPLHHVHGIVNKLLCPLWVGATCVMLPEFQPQKVWEMLLSSKap 303
Cdd:cd05958 114 ATMHFHRDPLASADR----YAvnvlrLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEEATPDLLLSAIARYK-- 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 304 mVNVFMAVPTIYSKLIQYYDqhFTQPHVKDfvravckerIRLMVSGSAALPLPTLQRWEEITGHTLLERYGMTE-IGMAL 382
Cdd:cd05958 188 -PTVLFTAPTAYRAMLAHPD--AAGPDLSS---------LRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEmFHIFI 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 383 SNPLKGPRiPGAVGSPLPRVEVRIVmnnttnttivlgDHRNTRVCPGlegKEGELLVRGPSVfkeYWNKPQETRESFIDG 462
Cdd:cd05958 256 SARPGDAR-PGATGKPVPGYEAKVV------------DDEGNPVPDG---TIGRLAVRGPTG---CRYLADKRQRTYVQG 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 463 GWFKTGDT-VVYKDGVYWIMGRSSvDIIKSAGYKISALEVERHLLAHPDIIDVAVIGAPDAIWGQKVTAVVQLRKGQS-- 539
Cdd:cd05958 317 GWNITGDTySRDPDGYFRHQGRSD-DMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIpg 395
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1250165799 540 -MTLPDLKTWAREHMAPYTIPTGLLLVEEMPRNQMGKVNKKDL 581
Cdd:cd05958 396 pVLARELQDHAKAHIAPYKYPRAIEFVTELPRTATGKLQRFAL 438
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
71-585 |
2.74e-60 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 209.25 E-value: 2.74e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 71 DKPAIIDSSGSHSYKQLYCSSLGLAGRIStALNLDFGglegKRISFLCANDASYTVAQWAAWMSGGTAVPL-FRKHPqSE 149
Cdd:PRK07786 32 DAPALRFLGNTTTWRELDDRVAALAGALS-RRGVGFG----DRVLILMLNRTEFVESVLAANMLGAIAVPVnFRLTP-PE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 150 LEYIISDSQSSLLVAghpyAGTLEPLALKL-----GLPCLTLPPTSNLGTLDGTDTQEKEA----AITDWA-DRPAMIIY 219
Cdd:PRK07786 106 IAFLVSDCGAHVVVT----EAALAPVATAVrdivpLLSTVVVAGGSSDDSVLGYEDLLAEAgpahAPVDIPnDSPALIMY 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 220 TSGTTGRPKGVLHMHSNIQAMVQGLVSEW-AWTRDDVILHTLPLHHVHGIVNkLLCPLWVGATCVMLP--EFQPQKVWEM 296
Cdd:PRK07786 182 TSGTTGRPKGAVLTHANLTGQAMTCLRTNgADINSDVGFVGVPLFHIAGIGS-MLPGLLLGAPTVIYPlgAFDPGQLLDV 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 297 LLSSKApmVNVFMaVPTiyskliQYydqhftqphvkdfvRAVCKE--------RIRLMVSGSAALPlPTLQR--WEEITG 366
Cdd:PRK07786 261 LEAEKV--TGIFL-VPA------QW--------------QAVCAEqqarprdlALRVLSWGAAPAS-DTLLRqmAATFPE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 367 HTLLERYGMTEIGmALSNPLKGP---RIPGAVGSPLPRVEVRIVMNNTTNTTIvlgdhrntrvcpgleGKEGELLVRGPS 443
Cdd:PRK07786 317 AQILAAFGQTEMS-PVTCMLLGEdaiRKLGSVGKVIPTVAARVVDENMNDVPV---------------GEVGEIVYRAPT 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 444 VFKEYWNKPQETRESFiDGGWFKTGDTV-VYKDGVYWIMGRSSvDIIKSAGYKISALEVERHLLAHPDIIDVAVIGAPDA 522
Cdd:PRK07786 381 LMSGYWNNPEATAEAF-AGGWFHSGDLVrQDEEGYVWVVDRKK-DMIISGGENIYCAEVENVLASHPDIVEVAVIGRADE 458
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1250165799 523 IWGQKVTAVVQLRKG-QSMTLPDLKTWAREHMAPYTIPTGLLLVEEMPRNQMGKVNKKDLLRHF 585
Cdd:PRK07786 459 KWGEVPVAVAAVRNDdAALTLEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKVLKTELRERY 522
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
71-581 |
2.89e-60 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 207.74 E-value: 2.89e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 71 DKPAIIDSSGSHSYKqlYCSSLGLAGRISTALNlDFGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLFRKHPQSEL 150
Cdd:PRK09088 10 QRLAAVDLALGRRWT--YAELDALVGRLAAVLR-RRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASEL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 151 EYIISDSQSSLLVA-GHPYAGTLEPLALklglpcltlppTSNLGTLDGTDTQEKEAAItdwADRPAMIIYTSGTTGRPKG 229
Cdd:PRK09088 87 DALLQDAEPRLLLGdDAVAAGRTDVEDL-----------AAFIASADALEPADTPSIP---PERVSLILFTSGTSGQPKG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 230 VLHMHSNIQAMVQGLVSEWAWTRDDVILHTLPLHHVHGIVNKLLCPLWVGATCVMLPEFQPQKV--WemlLSSKAPMVNV 307
Cdd:PRK09088 153 VMLSERNLQQTAHNFGVLGRVDAHSSFLCDAPMFHIIGLITSVRPVLAVGGSILVSNGFEPKRTlgR---LGDPALGITH 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 308 FMAVPtiyskliQYYDQHFTQPhvkDFVRAVCKeRIRLMVSGSAALPLPTLQRWEEiTGHTLLERYGMTEIGMALSNPLK 387
Cdd:PRK09088 230 YFCVP-------QMAQAFRAQP---GFDAAALR-HLTALFTGGAPHAAEDILGWLD-DGIPMVDGFGMSEAGTVFGMSVD 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 388 GPRIP---GAVGSPLPRVEVRIVMNNTtnttivlgdhrntRVCPGleGKEGELLVRGPSVFKEYWNKPQETRESFIDGGW 464
Cdd:PRK09088 298 CDVIRakaGAAGIPTPTVQTRVVDDQG-------------NDCPA--GVPGELLLRGPNLSPGYWRRPQATARAFTGDGW 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 465 FKTGDTVVYK-DGVYWIMGRSSvDIIKSAGYKISALEVERHLLAHPDIIDVAVIGAPDAIWGQKVTAVVQLRKGQSMTLP 543
Cdd:PRK09088 363 FRTGDIARRDaDGFFWVVDRKK-DMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADGAPLDLE 441
|
490 500 510
....*....|....*....|....*....|....*...
gi 1250165799 544 DLKTWAREHMAPYTIPTGLLLVEEMPRNQMGKVNKKDL 581
Cdd:PRK09088 442 RIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARL 479
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
161-584 |
5.75e-60 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 210.58 E-value: 5.75e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 161 LLVAGHPYAGTLEPLALKLGLPCLTLPPTSNLGTLDGTDTQEKEAAITDWADRPAMIIYTSGTTGRPKGVLHMHSNIQAM 240
Cdd:PRK07529 162 VEVDLARYLPGPKRLAVPLIRRKAHARILDFDAELARQPGDRLFSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVAN 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 241 VQGLVSEWAWTRDDVILHTLPLHHVHGIVNKLLCPLWVGATCVMLPefqPQ---------KVWEMLLSSKapmVNVFMAV 311
Cdd:PRK07529 242 AWLGALLLGLGPGDTVFCGLPLFHVNALLVTGLAPLARGAHVVLAT---PQgyrgpgviaNFWKIVERYR---INFLSGV 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 312 PTIYSKLIQyydqhftQPhvkdfVRAVCKERIRLMVSGSAALPLPTLQRWEEITGHTLLERYGMTEiGMALS--NPLKGP 389
Cdd:PRK07529 316 PTVYAALLQ-------VP-----VDGHDISSLRYALCGAAPLPVEVFRRFEAATGVRIVEGYGLTE-ATCVSsvNPPDGE 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 390 RIPGAVGSPLPRVEVRIVmnnttnttIVLGDHRNTRVCPglEGKEGELLVRGPSVFKEYWNKPQEtRESFIDGGWFKTGD 469
Cdd:PRK07529 383 RRIGSVGLRLPYQRVRVV--------ILDDAGRYLRDCA--VDEVGVLCIAGPNVFSGYLEAAHN-KGLWLEDGWLNTGD 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 470 TV-VYKDGVYWIMGRSSvDIIKSAGYKISALEVERHLLAHPDIIDVAVIGAPDAIWGQKVTAVVQLRKGQSMTLPDLKTW 548
Cdd:PRK07529 452 LGrIDADGYFWLTGRAK-DLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGELPVAYVQLKPGASATEAELLAF 530
|
410 420 430
....*....|....*....|....*....|....*..
gi 1250165799 549 AREHMA-PYTIPTGLLLVEEMPRNQMGKVNKKDLLRH 584
Cdd:PRK07529 531 ARDHIAeRAAVPKHVRILDALPKTAVGKIFKPALRRD 567
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
81-581 |
1.29e-59 |
|
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: 204.12 E-value: 1.29e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 81 SHSYKQLYCSSLGLAGRISTalnldFGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLFRKHPQSELEYIISDSQSS 160
Cdd:cd05912 1 SYTFAELFEEVSRLAEHLAA-----LGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 161 LlvaghpyagtleplalklglpcltlpptsnlgtldgtdtqekeaaitdwaDRPAMIIYTSGTTGRPKGVLHMHSNIQAM 240
Cdd:cd05912 76 L--------------------------------------------------DDIATIMYTSGTTGKPKGVQQTFGNHWWS 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 241 VQGLVSEWAWTRDDVILHTLPLHHVHGIvNKLLCPLWVGATCVMLPEFQPQKVWEMLLSSKAPMVNVfmaVPTIYSKLIQ 320
Cdd:cd05912 106 AIGSALNLGLTEDDNWLCALPLFHISGL-SILMRSVIYGMTVYLVDKFDAEQVLHLINSGKVTIISV---VPTMLQRLLE 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 321 YYDQHftqphvkdfvravCKERIRLMVSGSAALPLPTLQRWEEiTGHTLLERYGMTEIG--MALSNPLKGPRIPGAVGSP 398
Cdd:cd05912 182 ILGEG-------------YPNNLRCILLGGGPAPKPLLEQCKE-KGIPVYQSYGMTETCsqIVTLSPEDALNKIGSAGKP 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 399 LPRVEVRIVMNNttnttivlgdhrntrvcpGLEGKEGELLVRGPSVFKEYWNKPQETRESFIDgGWFKTGDtVVYKD--G 476
Cdd:cd05912 248 LFPVELKIEDDG------------------QPPYEVGEILLKGPNVTKGYLNRPDATEESFEN-GWFKTGD-IGYLDeeG 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 477 VYWIMGRSSvDIIKSAGYKISALEVERHLLAHPDIIDVAVIGAPDAIWGQKVTAVVQLRkgQSMTLPDLKTWAREHMAPY 556
Cdd:cd05912 308 FLYVLDRRS-DLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSE--RPISEEELIAYCSEKLAKY 384
|
490 500
....*....|....*....|....*
gi 1250165799 557 TIPTGLLLVEEMPRNQMGKVNKKDL 581
Cdd:cd05912 385 KVPKKIYFVDELPRTASGKLLRHEL 409
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
71-581 |
3.58e-59 |
|
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: 203.91 E-value: 3.58e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 71 DKPAIIDSSGSHSYKQLYCSSLGLAGRISTAlnldfGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLFRKHPQSEL 150
Cdd:cd05930 2 DAVAVVDGDQSLTYAELDARANRLARYLRER-----GVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 151 EYIISDSQSSLLvaghpyagtleplalklglpcltlpptsnlgtldgtdtqekeaaITDwADRPAMIIYTSGTTGRPKGV 230
Cdd:cd05930 77 AYILEDSGAKLV--------------------------------------------LTD-PDDLAYVIYTSGSTGKPKGV 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 231 LHMHSNIQAMVQGLVSEWAWTRDDVILHTLPLHHVHGIVNkLLCPLWVGATCVMLPE---FQPQKVWEMLLSSKapmVNV 307
Cdd:cd05930 112 MVEHRGLVNLLLWMQEAYPLTPGDRVLQFTSFSFDVSVWE-IFGALLAGATLVVLPEevrKDPEALADLLAEEG---ITV 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 308 FMAVPTIYSKLIQYYDqhftqphvkdfvRAVCKeRIRLMVSGSAALPLPTLQRWEEI-TGHTLLERYGMTEI-GMALSNP 385
Cdd:cd05930 188 LHLTPSLLRLLLQELE------------LAALP-SLRLVLVGGEALPPDLVRRWRELlPGARLVNLYGPTEAtVDATYYR 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 386 LKGPRIPGA---VGSPLPRVEVRivmnnttnttiVLGDHRntRVCPglEGKEGELLVRGPSVFKEYWNKPQETRESFID- 461
Cdd:cd05930 255 VPPDDEEDGrvpIGRPIPNTRVY-----------VLDENL--RPVP--PGVPGELYIGGAGLARGYLNRPELTAERFVPn 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 462 --GGW---FKTGDTVVYK-DG--VYwiMGRSSvDIIKSAGYKISALEVERHLLAHPDIIDVAVIGAPDAIWGQKVTAVVQ 533
Cdd:cd05930 320 pfGPGermYRTGDLVRWLpDGnlEF--LGRID-DQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVV 396
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1250165799 534 LRKGQSMTLPDLKTWAREHMAPYTIPTGLLLVEEMPRNQMGKVNKKDL 581
Cdd:cd05930 397 PDEGGELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
71-584 |
6.92e-59 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 204.04 E-value: 6.92e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 71 DKPAIIDSSGSHSYKQLYCSSLGLAGRIStALNLDfgglEGKRISFLCANDASYTVAQWAAWMSGGTAVPLFRKHPQSEL 150
Cdd:PRK03640 17 DRTAIEFEEKKVTFMELHEAVVSVAGKLA-ALGVK----KGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREEL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 151 EYIISDSQSSLLVAGHPYAGTLEPLAlklglpcltlppTSNLGTLDGTDTQEKEAaITDWA-DRPAMIIYTSGTTGRPKG 229
Cdd:PRK03640 92 LWQLDDAEVKCLITDDDFEAKLIPGI------------SVKFAELMNGPKEEAEI-QEEFDlDEVATIMYTSGTTGKPKG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 230 VL-----HMHSNI-QAMVQGLvsewawTRDDVILHTLPLHHVHGIvNKLLCPLWVGATCVMLPEFQPQKVWEMLLSSKAP 303
Cdd:PRK03640 159 VIqtygnHWWSAVgSALNLGL------TEDDCWLAAVPIFHISGL-SILMRSVIYGMRVVLVEKFDAEKINKLLQTGGVT 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 304 MVNVfmaVPTIYSKLIQYYDQHftqphvkdfvraVCKERIRLMVSGSAALPLPTLQRWEEiTGHTLLERYGMTEIG---M 380
Cdd:PRK03640 232 IISV---VSTMLQRLLERLGEG------------TYPSSFRCMLLGGGPAPKPLLEQCKE-KGIPVYQSYGMTETAsqiV 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 381 ALSNPLKGPRIpGAVGSPLPRVEVRIVmnnttnttivlgdhRNTRVCPGLEgkEGELLVRGPSVFKEYWNKPQETRESFI 460
Cdd:PRK03640 296 TLSPEDALTKL-GSAGKPLFPCELKIE--------------KDGVVVPPFE--EGEIVVKGPNVTKGYLNREDATRETFQ 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 461 DGgWFKTGDT-VVYKDGVYWIMGRSSvDIIKSAGYKISALEVERHLLAHPDIIDVAVIGAPDAIWGQKVTAVVqlRKGQS 539
Cdd:PRK03640 359 DG-WFKTGDIgYLDEEGFLYVLDRRS-DLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFV--VKSGE 434
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1250165799 540 MTLPDLKTWAREHMAPYTIPTGLLLVEEMPRNQMGKvnkkdLLRH 584
Cdd:PRK03640 435 VTEEELRHFCEEKLAKYKVPKRFYFVEELPRNASGK-----LLRH 474
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
18-581 |
2.18e-58 |
|
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: 203.84 E-value: 2.18e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 18 PHWKATFHRTYfpSEPGQWL---LGSVVHRRAHRwtaaqssrinqkpvfvrapaFGDKPAIIDSSGSHSYKQLYCSSLGL 94
Cdd:COG1021 6 TPWPEEFAARY--REAGYWRgetLGDLLRRRAER--------------------HPDRIAVVDGERRLSYAELDRRADRL 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 95 AGRISTAlnldfgGLE-GKRISFLCANDASYTVAQWAAWMSGgtAVPLF--RKHPQSELEYIISDSQSSLLVAGHPYAGT 171
Cdd:COG1021 64 AAGLLAL------GLRpGDRVVVQLPNVAEFVIVFFALFRAG--AIPVFalPAHRRAEISHFAEQSEAVAYIIPDRHRGF 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 172 -LEPLA--LKLGLPCLTL-------PPTSNLGTLDGTDTQEKEAAITdwADRPAMIIYTSGTTGRPKGVLHMHS----NI 237
Cdd:COG1021 136 dYRALAreLQAEVPSLRHvlvvgdaGEFTSLDALLAAPADLSEPRPD--PDDVAFFQLSGGTTGLPKLIPRTHDdylySV 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 238 QAMVQglvsEWAWTRDDVILHTLPLHHvhgivN-KLLCP-----LWVGATCVMLPEFQPQKVWEMLLSSKapmVNVFMAV 311
Cdd:COG1021 214 RASAE----ICGLDADTVYLAALPAAH-----NfPLSSPgvlgvLYAGGTVVLAPDPSPDTAFPLIERER---VTVTALV 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 312 PTIYSKLIQYYDQHFTQPhvkdfvravckERIRLMVSGSAALPLPTLQRWEEITGHTLLERYGMTEiGMALSNPLKGPR- 390
Cdd:COG1021 282 PPLALLWLDAAERSRYDL-----------SSLRVLQVGGAKLSPELARRVRPALGCTLQQVFGMAE-GLVNYTRLDDPEe 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 391 -IPGAVGSPL-PRVEVRIVmnnttnttivlgDHRNTRVCPGlegKEGELLVRGPSVFKEYWNKPQETRESFIDGGWFKTG 468
Cdd:COG1021 350 vILTTQGRPIsPDDEVRIV------------DEDGNPVPPG---EVGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTG 414
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 469 DTVVY-KDGVYWIMGRSsVDIIKSAGYKISALEVERHLLAHPDIIDVAVIGAPDAIWGQKVTAVVQLRkGQSMTLPDLKT 547
Cdd:COG1021 415 DLVRRtPDGYLVVEGRA-KDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGERSCAFVVPR-GEPLTLAELRR 492
|
570 580 590
....*....|....*....|....*....|....*
gi 1250165799 548 WARE-HMAPYTIPTGLLLVEEMPRNQMGKVNKKDL 581
Cdd:COG1021 493 FLRErGLAAFKLPDRLEFVDALPLTAVGKIDKKAL 527
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
66-578 |
1.30e-57 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.
Pssm-ID: 341283 [Multi-domain] Cd Length: 486 Bit Score: 200.60 E-value: 1.30e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 66 APAFGDKPAIIDSSGSHSYKQLYCSSLGLAgriSTALNLDFGGleGKRISFLCANDASYTVAQWAAWMSGGTAVPLFRKH 145
Cdd:cd12118 14 AAVYPDRTSIVYGDRRYTWRQTYDRCRRLA---SALAALGISR--GDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 146 PQSELEYIISDSQSSLLVAGHPYAGtlEPLaLKLGLP-CLTLPPtsnlgtldgtdtQEKEAAITdwadrpamIIYTSGTT 224
Cdd:cd12118 89 DAEEIAFILRHSEAKVLFVDREFEY--EDL-LAEGDPdFEWIPP------------ADEWDPIA--------LNYTSGTT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 225 GRPKGVLHMHSNIQAMVQGLVSEWAWTRDDVILHTLPLHHVHGivnklLCPLW----VGATCVMLPEFQPQKVWEMLLSS 300
Cdd:cd12118 146 GRPKGVVYHHRGAYLNALANILEWEMKQHPVYLWTLPMFHCNG-----WCFPWtvaaVGGTNVCLRKVDAKAIYDLIEKH 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 301 KapmVNVFMAVPTIYSKLIQYydqhftqphvKDFVRAVCKERIRLMVSGSAAlPLPTLQRWEEItGHTLLERYGMTEI-G 379
Cdd:cd12118 221 K---VTHFCGAPTVLNMLANA----------PPSDARPLPHRVHVMTAGAPP-PAAVLAKMEEL-GFDVTHVYGLTETyG 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 380 MALSNPLKgpriPGAVGSPLP---RVEVRIVMNNTTNTTIVLGDHRNTRVCPGlEGKE-GELLVRGPSVFKEYWNKPQET 455
Cdd:cd12118 286 PATVCAWK----PEWDELPTEeraRLKARQGVRYVGLEEVDVLDPETMKPVPR-DGKTiGEIVFRGNIVMKGYLKNPEAT 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 456 RESFiDGGWFKTGD-TVVYKDGVYWIMGRSSvDIIKSAGYKISALEVERHLLAHPDIIDVAVIGAPDAIWGQKVTAVVQL 534
Cdd:cd12118 361 AEAF-RGGWFHSGDlAVIHPDGYIEIKDRSK-DIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVEL 438
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1250165799 535 RKGQSMTLPDLKTWAREHMAPYTIPTGlLLVEEMPRNQMGKVNK 578
Cdd:cd12118 439 KEGAKVTEEEIIAFCREHLAGFMVPKT-VVFGELPKTSTGKIQK 481
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
214-578 |
6.14e-57 |
|
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: 194.41 E-value: 6.14e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 214 PAMIIYTSGTTGRPKGVLHMHSNIQAMVQGLVSEWAWTRDDVILHTLPLHHVHGIvNKLLCPLWVGATCVMLPEFQPQKV 293
Cdd:cd17637 2 PFVIIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPLFHIAGL-NLALATFHAGGANVVMEKFDPAEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 294 WEMLLSSKapmVNVFMAVPTIYSKLIqyyDQHFTQPHVKDFVRAVckerirlmvsgsAALPLP-TLQRWEEITGHTLLER 372
Cdd:cd17637 81 LELIEEEK---VTLMGSFPPILSNLL---DAAEKSGVDLSSLRHV------------LGLDAPeTIQRFEETTGATFWSL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 373 YGMTEIGMALSNPLKGPRiPGAVGSPLPRVEVRIVmnnttnttivlgDHRNTRVCPGlegKEGELLVRGPSVFKEYWNKP 452
Cdd:cd17637 143 YGQTETSGLVTLSPYRER-PGSAGRPGPLVRVRIV------------DDNDRPVPAG---ETGEIVVRGPLVFQGYWNLP 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 453 QETRESFiDGGWFKTGDT-VVYKDGVYWIMGRSSV-DIIKSAGYKISALEVERHLLAHPDIIDVAVIGAPDAIWGQKVTA 530
Cdd:cd17637 207 ELTAYTF-RNGWHHTGDLgRFDEDGYLWYAGRKPEkELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKA 285
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1250165799 531 VVQLRKGQSMTLPDLKTWAREHMAPYTIPTGLLLVEEMPRNQMGKVNK 578
Cdd:cd17637 286 VCVLKPGATLTADELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
83-581 |
7.68e-57 |
|
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: 197.29 E-value: 7.68e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 83 SYKQLYCSSLGLAGRISTalnldFGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLFRKHPQSELEYIISDSQSSLL 162
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKA-----QGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 163 VAghpyagtleplALKLGLPCLTlppTSNLGTLDGTDTQEKEAAITDWADRPAMIIYTSGTTGRPKGVLHMHSNIQAMVQ 242
Cdd:TIGR01923 76 LT-----------DSLLEEKDFQ---ADSLDRIEAAGRYETSLSASFNMDQIATLMFTSGTTGKPKAVPHTFRNHYASAV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 243 GLVSEWAWTRDDVILHTLPLHHVHGiVNKLLCPLWVGATCVMLPEFQpqKVWEMLLSSKAPMVNvfmAVPTiysKLIQYY 322
Cdd:TIGR01923 142 GSKENLGFTEDDNWLLSLPLYHISG-LSILFRWLIEGATLRIVDKFN--QLLEMIANERVTHIS---LVPT---QLNRLL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 323 DQHFTQphvkdfvravckERIRLMVSGSAALPLPTLQRWEEiTGHTLLERYGMTEIG---MALSNPLKGPRipGAVGSPL 399
Cdd:TIGR01923 213 DEGGHN------------ENLRKILLGGSAIPAPLIEEAQQ-YGLPIYLSYGMTETCsqvTTATPEMLHAR--PDVGRPL 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 400 PRVEVRIVMnnttnttivlgdhrntrvcPGLEGkEGELLVRGPSVFKEYWNkPQETRESFIDGGWFKTGDTVVYK-DGVY 478
Cdd:TIGR01923 278 AGREIKIKV-------------------DNKEG-HGEIMVKGANLMKGYLY-QGELTPAFEQQGWFNTGDIGELDgEGFL 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 479 WIMGRSSvDIIKSAGYKISALEVERHLLAHPDIIDVAVIGAPDAIWGQKVTAVVQLRKGQSMTlpDLKTWAREHMAPYTI 558
Cdd:TIGR01923 337 YVLGRRD-DLIISGGENIYPEEIETVLYQHPGIQEAVVVPKPDAEWGQVPVAYIVSESDISQA--KLIAYLTEKLAKYKV 413
|
490 500
....*....|....*....|...
gi 1250165799 559 PTGLLLVEEMPRNQMGKVNKKDL 581
Cdd:TIGR01923 414 PIAFEKLDELPYNASGKILRNQL 436
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
65-581 |
1.30e-56 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 198.75 E-value: 1.30e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 65 RAPAFGDKPAII--DSSGS---HSYKQLYcsslglaGRISTALNL--DFGGLEGKRISFLCANDASYTVAQWAAWMSGGT 137
Cdd:PRK08008 16 LADVYGHKTALIfeSSGGVvrrYSYLELN-------EEINRTANLfySLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 138 AVPLFRKHPQSELEYIISDSQSSLLVAGHPYAGTLEPLALKLGLP----CLT------LPPTSNLGTLDGTDTQEKEAAI 207
Cdd:PRK08008 89 MVPINARLLREESAWILQNSQASLLVTSAQFYPMYRQIQQEDATPlrhiCLTrvalpaDDGVSSFTQLKAQQPATLCYAP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 208 TDWADRPAMIIYTSGTTGRPKGVLHMHSNIQamVQGLVSEW--AWTRDDVILHTLPLHHVHGIVNKLLCPLWVGATCVML 285
Cdd:PRK08008 169 PLSTDDTAEILFTSGTTSRPKGVVITHYNLR--FAGYYSAWqcALRDDDVYLTVMPAFHIDCQCTAAMAAFSAGATFVLL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 286 PEFQPQKVWEMLLSSKApmvNVFMAVPTIYSKLIqyydqhfTQPhVKDFVRAVCKERIRLMVSGSAALPLPTLQRWeeit 365
Cdd:PRK08008 247 EKYSARAFWGQVCKYRA---TITECIPMMIRTLM-------VQP-PSANDRQHCLREVMFYLNLSDQEKDAFEERF---- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 366 GHTLLERYGMTE-IGMALSNPLKGPRIPGAVGSPLPRVEVRIVmnnttnttivlgDHRNTRVCPGlegKEGELLVRG--- 441
Cdd:PRK08008 312 GVRLLTSYGMTEtIVGIIGDRPGDKRRWPSIGRPGFCYEAEIR------------DDHNRPLPAG---EIGEICIKGvpg 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 442 PSVFKEYWNKPQETRESFIDGGWFKTGDT-VVYKDGVYWIMGRSsVDIIKSAGYKISALEVERHLLAHPDIIDVAVIGAP 520
Cdd:PRK08008 377 KTIFKEYYLDPKATAKVLEADGWLHTGDTgYVDEEGFFYFVDRR-CNMIKRGGENVSCVELENIIATHPKIQDIVVVGIK 455
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1250165799 521 DAIWGQKVTAVVQLRKGQSMTLPDLKTWAREHMAPYTIPTGLLLVEEMPRNQMGKVNKKDL 581
Cdd:PRK08008 456 DSIRDEAIKAFVVLNEGETLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNL 516
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
212-581 |
4.21e-56 |
|
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: 193.08 E-value: 4.21e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 212 DRPAMIIYTSGTTGRPKGVLHMHSNIQAMVQGLVSEWAWTRDDVILHTLPLHHVHGIVNKLLCPLWVGATCVMLP----- 286
Cdd:cd05944 2 DDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVVLAGpagyr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 287 -EFQPQKVWEMLLSSKapmVNVFMAVPTIYSKLIQyydqhftQPHVKDFvravckERIRLMVSGSAALPLPTLQRWEEIT 365
Cdd:cd05944 82 nPGLFDNFWKLVERYR---ITSLSTVPTVYAALLQ-------VPVNADI------SSLRFAMSGAAPLPVELRARFEDAT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 366 GHTLLERYGMTEIGMALS-NPLKGPRIPGAVGSPLPRVEVRIVMNNttnttivlGDHRNTRVCPGleGKEGELLVRGPSV 444
Cdd:cd05944 146 GLPVVEGYGLTEATCLVAvNPPDGPKRPGSVGLRLPYARVRIKVLD--------GVGRLLRDCAP--DEVGEICVAGPGV 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 445 FKEYWNKpQETRESFIDGGWFKTGDTV-VYKDGVYWIMGRSSvDIIKSAGYKISALEVERHLLAHPDIIDVAVIGAPDAI 523
Cdd:cd05944 216 FGGYLYT-EGNKNAFVADGWLNTGDLGrLDADGYLFITGRAK-DLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAH 293
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1250165799 524 WGQKVTAVVQLRKGQSMTLPDLKTWAREHMAPY-TIPTGLLLVEEMPRNQMGKVNKKDL 581
Cdd:cd05944 294 AGELPVAYVQLKPGAVVEEEELLAWARDHVPERaAVPKHIEVLEELPVTAVGKVFKPAL 352
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
72-581 |
4.58e-56 |
|
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: 195.37 E-value: 4.58e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 72 KPAIIDSSGSHSYKQLYCSslglAGRISTAL-NLDFGGleGKRISFLCANDASYTVAQWAAWMSGGTAVPLFRKHPQSEL 150
Cdd:cd05919 1 KTAFYAADRSVTYGQLHDG----ANRLGSALrNLGVSS--GDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 151 EYIISDSQSSLLVAGhpyagtleplalklglpcltlpptsnlgtldgtdtqekeaaitdwADRPAMIIYTSGTTGRPKGV 230
Cdd:cd05919 75 AYIARDCEARLVVTS---------------------------------------------ADDIAYLLYSSGTTGPPKGV 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 231 LHMHSNIQAMVQGLVSEW-AWTRDDVILHTLPLHHVHGIVNKLLCPLWVGATCVMLPEF-QPQKVWEMLLSSKApmvNVF 308
Cdd:cd05919 110 MHAHRDPLLFADAMAREAlGLTPGDRVFSSAKMFFGYGLGNSLWFPLAVGASAVLNPGWpTAERVLATLARFRP---TVL 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 309 MAVPTIYSKLIqyyDQHFTQPHvkDFVRavckerIRLMVSGSAALPLPTLQRWEEITGHTLLERYGMTEIG-MALSNPLK 387
Cdd:cd05919 187 YGVPTFYANLL---DSCAGSPD--ALRS------LRLCVSAGEALPRGLGERWMEHFGGPILDGIGATEVGhIFLSNRPG 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 388 GPRiPGAVGSPLPRVEVRIVmnnttnttivlgDHRNTRVCPGlegKEGELLVRGPSVFKEYWNKPQETRESFiDGGWFKT 467
Cdd:cd05919 256 AWR-LGSTGRPVPGYEIRLV------------DEEGHTIPPG---EEGDLLVRGPSAAVGYWNNPEKSRATF-NGGWYRT 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 468 GDTV-VYKDGVYWIMGRSSvDIIKSAGYKISALEVERHLLAHPDIIDVAVIGAPDAIWGQKVTAVVQLRKG---QSMTLP 543
Cdd:cd05919 319 GDKFcRDADGWYTHAGRAD-DMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPaapQESLAR 397
|
490 500 510
....*....|....*....|....*....|....*...
gi 1250165799 544 DLKTWAREHMAPYTIPTGLLLVEEMPRNQMGKVNKKDL 581
Cdd:cd05919 398 DIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKL 435
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
71-581 |
7.64e-56 |
|
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: 194.77 E-value: 7.64e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 71 DKPAIIDSSGSHSYKQLYCSSLGLAGRISTAlnldfGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLFRKHPQSEL 150
Cdd:cd05945 6 DRPAVVEGGRTLTYRELKERADALAAALASL-----GLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 151 EYIISDSQSSLLVAghpyagtleplalklglpcltlpptsnlgtlDGTDtqekeaaitdwadrPAMIIYTSGTTGRPKGV 230
Cdd:cd05945 81 REILDAAKPALLIA-------------------------------DGDD--------------NAYIIFTSGSTGRPKGV 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 231 LHMHSNIQAMVQGLVSEWAWTRDDVILHTLPLH---HVHGIvnklLCPLWVGATCVMLPEfqpqkvwEMLLSSKAPM--- 304
Cdd:cd05945 116 QISHDNLVSFTNWMLSDFPLGPGDVFLNQAPFSfdlSVMDL----YPALASGATLVPVPR-------DATADPKQLFrfl 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 305 ----VNVFMAVPTIYSKLIQyyDQHFTQPHVKdfvravckeRIRLMVSGSAALPLPTLQRWEEIT-GHTLLERYGMTEIG 379
Cdd:cd05945 185 aehgITVWVSTPSFAAMCLL--SPTFTPESLP---------SLRHFLFCGEVLPHKTARALQQRFpDARIYNTYGPTEAT 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 380 MALS------NPLKG-PRIPgaVGSPLPrvevrivmnnTTNTTIVLGDHRntrvcPGLEGKEGELLVRGPSVFKEYWNKP 452
Cdd:cd05945 254 VAVTyievtpEVLDGyDRLP--IGYAKP----------GAKLVILDEDGR-----PVPPGEKGELVISGPSVSKGYLNNP 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 453 QETRESF--IDG-GWFKTGDTVVYK-DGVYWIMGRssVDI-IKSAGYKISALEVERHLLAHPDIIDVAVIGAPDAIWGQK 527
Cdd:cd05945 317 EKTAAAFfpDEGqRAYRTGDLVRLEaDGLLFYRGR--LDFqVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTE 394
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1250165799 528 VTAVVQLRKGQSMTLP-DLKTWAREHMAPYTIPTGLLLVEEMPRNQMGKVNKKDL 581
Cdd:cd05945 395 LIAFVVPKPGAEAGLTkAIKAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
110-582 |
2.02e-55 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 196.79 E-value: 2.02e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 110 EGKRISFLCANDASYTVAQWAAWMSGGTAVPLFRKHPQSELEYIISDSQSSLL---------VAGHPYAGTLE------- 173
Cdd:PRK06710 73 KGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVIlcldlvfprVTNVQSATKIEhvivtri 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 174 ----PLALKLGLPCLTLPPTSNLGTLDGTDT--------QEKEAAI---TDWADRPAMIIYTSGTTGRPKGVLHMHSN-I 237
Cdd:PRK06710 153 adflPFPKNLLYPFVQKKQSNLVVKVSESETihlwnsveKEVNTGVevpCDPENDLALLQYTGGTTGFPKGVMLTHKNlV 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 238 QAMVQGLvsEWAWT---RDDVILHTLPLHHVHGIVNKLLCPLWVGATCVMLPEFQPQKVWEMLLSSKapmVNVFMAVPTI 314
Cdd:PRK06710 233 SNTLMGV--QWLYNckeGEEVVLGVLPFFHVYGMTAVMNLSIMQGYKMVLIPKFDMKMVFEAIKKHK---VTLFPGAPTI 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 315 YSKLIQyydqhftQPHVKDFVRAvckeRIRLMVSGSAALPLPTLQRWEEITGHTLLERYGMTEIG-MALSNPLKGPRIPG 393
Cdd:PRK06710 308 YIALLN-------SPLLKEYDIS----SIRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTESSpVTHSNFLWEKRVPG 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 394 AVGSPLPRVEVRIVMNNTTnttivlgdhrntRVCPglEGKEGELLVRGPSVFKEYWNKPQETRESFIDGgWFKTGDT-VV 472
Cdd:PRK06710 377 SIGVPWPDTEAMIMSLETG------------EALP--PGEIGEIVVKGPQIMKGYWNKPEETAAVLQDG-WLHTGDVgYM 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 473 YKDGVYWIMGRSSvDIIKSAGYKISALEVERHLLAHPDIIDVAVIGAPDAIWGQKVTAVVQLRKGQSMTLPDLKTWAREH 552
Cdd:PRK06710 442 DEDGFFYVKDRKK-DMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVLKEGTECSEEELNQFARKY 520
|
490 500 510
....*....|....*....|....*....|
gi 1250165799 553 MAPYTIPTGLLLVEEMPRNQMGKVNKKDLL 582
Cdd:PRK06710 521 LAAYKVPKVYEFRDELPKTTVGKILRRVLI 550
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
71-582 |
2.28e-55 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 196.42 E-value: 2.28e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 71 DKPAIIDSSGSHSYKQLYCSSLGLAgristALNLDFGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVP---LFRKHpq 147
Cdd:PRK06178 48 QRPAIIFYGHVITYAELDELSDRFA-----ALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPvspLFREH-- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 148 sELEYIISDSQSSLLVAGHPYAGTLEPLALKLGL---------------PCLTLPP------------TSNLGTLDGTdT 200
Cdd:PRK06178 121 -ELSYELNDAGAEVLLALDQLAPVVEQVRAETSLrhvivtsladvlpaePTLPLPDslraprlaaagaIDLLPALRAC-T 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 201 QEKEAAITDwADRPAMIIYTSGTTGRPKGVLHMHSNiqaMVQGLVSEWAWT----RDDVILHTLPLHHVHGIVNKLLCPL 276
Cdd:PRK06178 199 APVPLPPPA-LDALAALNYTGGTTGMPKGCEHTQRD---MVYTAAAAYAVAvvggEDSVFLSFLPEFWIAGENFGLLFPL 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 277 WVGATCVMLPEFQPQKVWEmllsskapmvnvfmAVP----TIYSKLIQYYDQHFTQPHVKDF-------VRAVckerirl 345
Cdd:PRK06178 275 FSGATLVLLARWDAVAFMA--------------AVEryrvTRTVMLVDNAVELMDHPRFAEYdlsslrqVRVV------- 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 346 mvSGSAALPLPTLQRWEEITGHTLLE-RYGMTE--------IGMALSN-PLKGPriPGAVGSPLPRVEVRIVmnnttntt 415
Cdd:PRK06178 334 --SFVKKLNPDYRQRWRALTGSVLAEaAWGMTEthtcdtftAGFQDDDfDLLSQ--PVFVGLPVPGTEFKIC-------- 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 416 ivlgDHRNTRVCPglEGKEGELLVRGPSVFKEYWNKPQETRESFIDGgWFKTGDTVVY-KDGVYWIMGRSSvDIIKSAGY 494
Cdd:PRK06178 402 ----DFETGELLP--LGAEGEIVVRTPSLLKGYWNKPEATAEALRDG-WLHTGDIGKIdEQGFLHYLGRRK-EMLKVNGM 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 495 KISALEVERHLLAHPDIIDVAVIGAPDAIWGQKVTAVVQLRKGQSMTLPDLKTWAREHMAPYTIPTgLLLVEEMPRNQMG 574
Cdd:PRK06178 474 SVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPGADLTAAALQAWCRENMAVYKVPE-IRIVDALPMTATG 552
|
....*...
gi 1250165799 575 KVNKKDLL 582
Cdd:PRK06178 553 KVRKQDLQ 560
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
82-581 |
3.61e-53 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.
Pssm-ID: 341284 [Multi-domain] Cd Length: 518 Bit Score: 189.38 E-value: 3.61e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 82 HSYKQLYCSslglAGRISTALNlDFGGLEGKRISFLCANDASYTVAQWAAWMSGG---TAVPlfRKHPQsELEYIISDSQ 158
Cdd:cd12119 26 YTYAEVAER----ARRLANALR-RLGVKPGDRVATLAWNTHRHLELYYAVPGMGAvlhTINP--RLFPE-QIAYIINHAE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 159 SSLLVAGHPYAGTLEPLALKL--------GLPCLTLPPTSNLGTLDGTDTQEKEAAITDWAD----RPAMIIYTSGTTGR 226
Cdd:cd12119 98 DRVVFVDRDFLPLLEAIAPRLptvehvvvMTDDAAMPEPAGVGVLAYEELLAAESPEYDWPDfdenTAAAICYTSGTTGN 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 227 PKGVLHMHSNI--QAMVQGLVSEWAWTRDDVILHTLPLHHVHGIVNKLLCPlWVGATCVML-PEFQPQKVWEMLlssKAP 303
Cdd:cd12119 178 PKGVVYSHRSLvlHAMAALLTDGLGLSESDVVLPVVPMFHVNAWGLPYAAA-MVGAKLVLPgPYLDPASLAELI---ERE 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 304 MVNVFMAVPTIYSKLIQYYDQHftqPHVKDFVRAVckerirlmVSGSAALPLPTLQRWEEItGHTLLERYGMTE---IGM 380
Cdd:cd12119 254 GVTFAAGVPTVWQGLLDHLEAN---GRDLSSLRRV--------VIGGSAVPRSLIEAFEER-GVRVIHAWGMTEtspLGT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 381 ALSNPLKGPRIPGAV--------GSPLPRVEVRIVmnnttnttivlgDHrNTRVCPGlEGKE-GELLVRGPSVFKEYWNK 451
Cdd:cd12119 322 VARPPSEHSNLSEDEqlalrakqGRPVPGVELRIV------------DD-DGRELPW-DGKAvGELQVRGPWVTKSYYKN 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 452 PQETrESFIDGGWFKTGD-TVVYKDGVYWIMGRSSvDIIKSAGYKISALEVERHLLAHPDIIDVAVIGAPDAIWGQKVTA 530
Cdd:cd12119 388 DEES-EALTEDGWLRTGDvATIDEDGYLTITDRSK-DVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLA 465
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1250165799 531 VVQLRKGQSMTLPDLKTWAREHMAPYTIPTGLLLVEEMPRNQMGKVNKKDL 581
Cdd:cd12119 466 VVVLKEGATVTAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
83-581 |
4.22e-53 |
|
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: 187.25 E-value: 4.22e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 83 SYKQLYCSSLGLAGRISTAlnldfgGLE-GKRISFLCANDASYTVAQWAAWMSGGTAVPLFRKHPQSELEYIISDSQSSL 161
Cdd:cd05971 8 TFKELKTASNRFANVLKEI------GLEkGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 162 LVaghpyagtleplalklglpcltlpptsnlgtldgtdtqekeaaiTDWADRPAMIIYTSGTTGRPKGVLHMHS------ 235
Cdd:cd05971 82 LV--------------------------------------------TDGSDDPALIIYTSGTTGPPKGALHAHRvllghl 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 236 -NIQaMVQGLV----------SEWAWtrddvilhtlplhhVHGIVNKLLCPLWVGATCVM--LPEFQPQKVWEMLlsSKA 302
Cdd:cd05971 118 pGVQ-FPFNLFprdgdlywtpADWAW--------------IGGLLDVLLPSLYFGVPVLAhrMTKFDPKAALDLM--SRY 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 303 PMVNVFMAvPTIYSKLIQYYDQhftqphVKDFVRavckeRIRLMVSGSAALPLPTLQRWEEITGHTLLERYGMTEIGMAL 382
Cdd:cd05971 181 GVTTAFLP-PTALKMMRQQGEQ------LKHAQV-----KLRAIATGGESLGEELLGWAREQFGVEVNEFYGQTECNLVI 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 383 SN-PLKGPRIPGAVGSPLPRVEVRIVmnnttnttivlgDHRNTRVCPGlegKEGELLVRGPS--VFKEYWNKPQETRESF 459
Cdd:cd05971 249 GNcSALFPIKPGSMGKPIPGHRVAIV------------DDNGTPLPPG---EVGEIAVELPDpvAFLGYWNNPSATEKKM 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 460 IdGGWFKTGDT-VVYKDGVYWIMGRSSvDIIKSAGYKISALEVERHLLAHPDIIDVAVIGAPDAIWGQKVTAVVQLRKGQ 538
Cdd:cd05971 314 A-GDWLLTGDLgRKDSDGYFWYVGRDD-DVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGE 391
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1250165799 539 SMT---LPDLKTWAREHMAPYTIPTGLLLVEEMPRNQMGKVNKKDL 581
Cdd:cd05971 392 TPSdalAREIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRREL 437
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
212-581 |
5.71e-53 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 184.40 E-value: 5.71e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 212 DRPAMIIYTSGTTGRPKGVLHMHSNI--------QAMvqglvsewAWTRDDVILHTLPLHHVHGIVNKLLCPLWVGATCV 283
Cdd:cd05917 2 DDVINIQFTSGTTGSPKGATLTHHNIvnngyfigERL--------GLTEQDRLCIPVPLFHCFGSVLGVLACLTHGATMV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 284 ML-PEFQPQKVWEMLLSSKApmvNVFMAVPTIYSKLIQYYDQHFTQPHvkdfvravckeRIRLMVSGSAALPLPTLQRWE 362
Cdd:cd05917 74 FPsPSFDPLAVLEAIEKEKC---TALHGVPTMFIAELEHPDFDKFDLS-----------SLRTGIMAGAPCPPELMKRVI 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 363 EITGHT-LLERYGMTE----IGMALSNPLKGPRIpGAVGSPLPRVEVRIVmnnttnttivlgDHRNTRVCPglEGKEGEL 437
Cdd:cd05917 140 EVMNMKdVTIAYGMTEtspvSTQTRTDDSIEKRV-NTVGRIMPHTEAKIV------------DPEGGIVPP--VGVPGEL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 438 LVRGPSVFKEYWNKPQETRESfIDG-GWFKTGDT-VVYKDGVYWIMGRSSvDIIKSAGYKISALEVERHLLAHPDIIDVA 515
Cdd:cd05917 205 CIRGYSVMKGYWNDPEKTAEA-IDGdGWLHTGDLaVMDEDGYCRIVGRIK-DMIIRGGENIYPREIEEFLHTHPKVSDVQ 282
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1250165799 516 VIGAPDAIWGQKVTAVVQLRKGQSMTLPDLKTWAREHMAPYTIPTGLLLVEEMPRNQMGKVNKKDL 581
Cdd:cd05917 283 VVGVPDERYGEEVCAWIRLKEGAELTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKL 348
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
105-581 |
2.40e-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: 185.40 E-value: 2.40e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 105 DFGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLFRKHPQSELEYIISDSQSSLLVaghpyagTLEPLALKlglpcl 184
Cdd:cd05969 19 SLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLI-------TTEELYER------ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 185 tlpptsnlgtldgtdtqekeaaiTDWADrPAMIIYTSGTTGRPKGVLHMHSniqAMVQGLVSEwAWT----RDDVILHTL 260
Cdd:cd05969 86 -----------------------TDPED-PTLLHYTSGTTGTPKGVLHVHD---AMIFYYFTG-KYVldlhPDDIYWCTA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 261 PLHHVHGIVNKLLCPLWVGATCVMLP-EFQPQKVWEMLLSSKapmVNVFMAVPTIYSKLIQYYDQhftqphvkdFVRAVC 339
Cdd:cd05969 138 DPGWVTGTVYGIWAPWLNGVTNVVYEgRFDAESWYGIIERVK---VTVWYTAPTAIRMLMKEGDE---------LARKYD 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 340 KERIRLMVSGSAALPlPTLQRW-EEITGHTLLERYGMTEIG-MALSNPLKGPRIPGAVGSPLPRVEVRIVMNNTTNTTiv 417
Cdd:cd05969 206 LSSLRFIHSVGEPLN-PEAIRWgMEVFGVPIHDTWWQTETGsIMIANYPCMPIKPGSMGKPLPGVKAAVVDENGNELP-- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 418 lgdhrntrvcpglEGKEGELLVRG--PSVFKEYWNKPQETRESFIDGgWFKTGDTVvYKD--GVYWIMGRSSvDIIKSAG 493
Cdd:cd05969 283 -------------PGTKGILALKPgwPSMFRGIWNDEERYKNSFIDG-WYLTGDLA-YRDedGYFWFVGRAD-DIIKTSG 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 494 YKISALEVERHLLAHPDIIDVAVIGAPDAIWGQKVTAVVQLRKGQSMTLP---DLKTWAREHMAPYTIPTGLLLVEEMPR 570
Cdd:cd05969 347 HRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPSDElkeEIINFVRQKLGAHVAPREIEFVDNLPK 426
|
490
....*....|.
gi 1250165799 571 NQMGKVNKKDL 581
Cdd:cd05969 427 TRSGKIMRRVL 437
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
71-581 |
2.07e-51 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 184.32 E-value: 2.07e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 71 DKPAIIDSSGSHSYKQLYCSSLGLAGRISTAlnldfGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLFRKHPQSEL 150
Cdd:PRK06145 17 DRAALVYRDQEISYAEFHQRILQAAGMLHAR-----GIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 151 EYIISDSQSSLLVAGHPYAGTLEPLALKLGLPCLTLPPTSNLGtldgtdtQEKEAAITDWADRPA---MIIYTSGTTGRP 227
Cdd:PRK06145 92 AYILGDAGAKLLLVDEEFDAIVALETPKIVIDAAAQADSRRLA-------QGGLEIPPQAAVAPTdlvRLMYTSGTTDRP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 228 KGVLHMHSNIQAMVQGLVSEWAWTRDDVILHTLPLHHVHGIVNKLLCPLWVGATCVMLPEFQPQKVWEMLLSSK------ 301
Cdd:PRK06145 165 KGVMHSYGNLHWKSIDHVIALGLTASERLLVVGPLYHVGAFDLPGIAVLWVGGTLRIHREFDPEAVLAAIERHRltcawm 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 302 AP-MVNVFMAVPTIYSkliqyYDQhftqphvkdfvravckERIRLMVSGSAALPLPTLQRWEEI-TGHTLLERYGMTEIG 379
Cdd:PRK06145 245 APvMLSRVLTVPDRDR-----FDL----------------DSLAWCIGGGEKTPESRIRDFTRVfTRARYIDAYGLTETC 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 380 MALSNPLKGPRIP--GAVGSPLPRVEVRIVmnnttnttivlgDHRNTRVCPGLEGkegELLVRGPSVFKEYWNKPQETRE 457
Cdd:PRK06145 304 SGDTLMEAGREIEkiGSTGRALAHVEIRIA------------DGAGRWLPPNMKG---EICMRGPKVTKGYWKDPEKTAE 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 458 SFIdGGWFKTGDtVVYKD--GVYWIMGRSSvDIIKSAGYKISALEVERHLLAHPDIIDVAVIGAPDAIWGQKVTAVVQLR 535
Cdd:PRK06145 369 AFY-GDWFRSGD-VGYLDeeGFLYLTDRKK-DMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLN 445
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1250165799 536 KGQSMTLPDLKTWAREHMAPYTIPTGLLLVEEMPRNQMGKVNKKDL 581
Cdd:PRK06145 446 PGATLTLEALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVL 491
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
94-516 |
2.43e-51 |
|
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: 181.69 E-value: 2.43e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 94 LAGRISTALNLDFGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLFRKHPQSELEYIISDSQSSLLVAGHPYAGTLe 173
Cdd:TIGR01733 8 RANRLARHLRAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDSALASRL- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 174 plalkLGLPCLTLPPTSNLGTLDGTDTQEKEAAITDWADRPAMIIYTSGTTGRPKGVLHMHSNIQAMVQGLVSEWAWTRD 253
Cdd:TIGR01733 87 -----AGLVLPVILLDPLELAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDPD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 254 DVILHTLPLHHvHGIVNKLLCPLWVGATCVMLPEfQPQKVWEMLLSS--KAPMVNVFMAVPTIYSKLIQyyDQHFTQPHV 331
Cdd:TIGR01733 162 DRVLQFASLSF-DASVEEIFGALLAGATLVVPPE-DEERDDAALLAAliAEHPVTVLNLTPSLLALLAA--ALPPALASL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 332 kdfvravckeriRLMVSGSAALPLPTLQRWEEITGHT-LLERYGMTEI-GMALSNPLKGPRIPGAV----GSPLPRVEVR 405
Cdd:TIGR01733 238 ------------RLVILGGEALTPALVDRWRARGPGArLINLYGPTETtVWSTATLVDPDDAPRESpvpiGRPLANTRLY 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 406 IVmnnttnttivlgdHRNTRVCPglEGKEGELLVRGPSVFKEYWNKPQETRESFID--------GGWFKTGDTVVY-KDG 476
Cdd:TIGR01733 306 VL-------------DDDLRPVP--VGVVGELYIGGPGVARGYLNRPELTAERFVPdpfaggdgARLYRTGDLVRYlPDG 370
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1250165799 477 VYWIMGRSSvDIIKSAGYKISALEVERHLLAHPDIIDVAV 516
Cdd:TIGR01733 371 NLEFLGRID-DQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
34-581 |
5.94e-51 |
|
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: 182.53 E-value: 5.94e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 34 GQWL---LGSVVHRRAHRWtaaqssrinqkpvfvrapafGDKPAIIDSSGSHSYKQLYCSSLGLAGRIStalnlDFGGLE 110
Cdd:cd05920 10 GYWQdepLGDLLARSAARH--------------------PDRIAVVDGDRRLTYRELDRRADRLAAGLR-----GLGIRP 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 111 GKRISFLCANDASYTVAQWAAWMSGgtAVPLFR--KHPQSELEYIISDSQSSLLVAGHPYAGtLEPLALklglpcltlpp 188
Cdd:cd05920 65 GDRVVVQLPNVAEFVVLFFALLRLG--AVPVLAlpSHRRSELSAFCAHAEAVAYIVPDRHAG-FDHRAL----------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 189 tsnlgtldgtdTQEKEAAITDwadrPAMIIYTSGTTGRPKGVLHMHSNIQAMVQGLVsEWAW-TRDDVILHTLPLHHvhg 267
Cdd:cd05920 131 -----------ARELAESIPE----VALFLLSGGTTGTPKLIPRTHNDYAYNVRASA-EVCGlDQDTVYLAVLPAAH--- 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 268 ivN-KLLCP-----LWVGATCVMLPEFQPQKVWEMLLSSKapmVNVFMAVPTIYSKLIQYYDQHFTQPhvkdfvravckE 341
Cdd:cd05920 192 --NfPLACPgvlgtLLAGGRVVLAPDPSPDAAFPLIEREG---VTVTALVPALVSLWLDAAASRRADL-----------S 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 342 RIRLMVSGSAALPLPTLQRWEEITGHTLLERYGMTEiGM----ALSNPlkGPRIPGAVGSPL-PRVEVRIVmnnttntti 416
Cdd:cd05920 256 SLRLLQVGGARLSPALARRVPPVLGCTLQQVFGMAE-GLlnytRLDDP--DEVIIHTQGRPMsPDDEIRVV--------- 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 417 vlgDHRNTRVCPGlegKEGELLVRGPSVFKEYWNKPQETRESFIDGGWFKTGDTV-VYKDGVYWIMGRSSvDIIKSAGYK 495
Cdd:cd05920 324 ---DEEGNPVPPG---EEGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVrRTPDGYLVVEGRIK-DQINRGGEK 396
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 496 ISALEVERHLLAHPDIIDVAVIGAPDAIWGQKVTAVVQLRkGQSMTLPDLKTWAREH-MAPYTIPTGLLLVEEMPRNQMG 574
Cdd:cd05920 397 IAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVLR-DPPPSAAQLRRFLRERgLAAYKLPDRIEFVDSLPLTAVG 475
|
....*..
gi 1250165799 575 KVNKKDL 581
Cdd:cd05920 476 KIDKKAL 482
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
217-578 |
5.43e-50 |
|
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.
Pssm-ID: 341293 [Multi-domain] Cd Length: 330 Bit Score: 175.77 E-value: 5.43e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 217 IIYTSGTTGRPKGVLHMHSniQAMvqGLVSEWA----WTRDDVILHTLPLHHVHGIVNKLLCPLWVGATCVMLPEFQPQK 292
Cdd:cd17638 5 IMFTSGTTGRSKGVMCAHR--QTL--RAAAAWAdcadLTEDDRYLIINPFFHTFGYKAGIVACLLTGATVVPVAVFDVDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 293 VWEMLLSSKapmVNVFMAVPTIYSKLIQYydqhftqPHVKDFVRAvckeRIRLMVSGSAALPLPTLQRW-EEITGHTLLE 371
Cdd:cd17638 81 ILEAIERER---ITVLPGPPTLFQSLLDH-------PGRKKFDLS----SLRAAVTGAATVPVELVRRMrSELGFETVLT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 372 RYGMTEIGMA-LSNPLKGPR-IPGAVGSPLPRVEVRIvmnnttnttivlgdhrntrvcpgleGKEGELLVRGPSVFKEYW 449
Cdd:cd17638 147 AYGLTEAGVAtMCRPGDDAEtVATTCGRACPGFEVRI-------------------------ADDGEVLVRGYNVMQGYL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 450 NKPQETRESFIDGGWFKTGDTVVYKD-GVYWIMGRSSvDIIKSAGYKISALEVERHLLAHPDIIDVAVIGAPDAIWGQKV 528
Cdd:cd17638 202 DDPEATAEAIDADGWLHTGDVGELDErGYLRITDRLK-DMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVG 280
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1250165799 529 TAVVQLRKGQSMTLPDLKTWAREHMAPYTIPTGLLLVEEMPRNQMGKVNK 578
Cdd:cd17638 281 KAFVVARPGVTLTEEDVIAWCRERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
74-581 |
9.57e-49 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 177.02 E-value: 9.57e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 74 AIIDSSG-SHSYKQLYCSSLGLAGRISTAlnldfgGL-EGKRISFLCANDASYTVAQWAAWMSGGTAVPLFRKHPQSELE 151
Cdd:PRK08276 3 VIMAPSGeVVTYGELEARSNRLAHGLRAL------GLrEGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 152 YIISDSQSSLLVAGHPYAGTLEPLALKLGLPCLTLppTSNLGTLDGTDTQEKEAAI---TDWADRPA--MIIYTSGTTGR 226
Cdd:PRK08276 77 YIVDDSGAKVLIVSAALADTAAELAAELPAGVPLL--LVVAGPVPGFRSYEEALAAqpdTPIADETAgaDMLYSSGTTGR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 227 PKGV------LHMHSNIQAMVqGLVSEWAWTRDD-VILHTLPLHHV-----HGIVNKLlcplwvGATCVMLPEFQPQKVW 294
Cdd:PRK08276 155 PKGIkrplpgLDPDEAPGMML-ALLGFGMYGGPDsVYLSPAPLYHTaplrfGMSALAL------GGTVVVMEKFDAEEAL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 295 EMLLSSKapmVNVFMAVPTIYSKLIQYYDQhftqphvkdfVRAvckeR-----IRLMVSGSAALPLPTLQRWEEITGHTL 369
Cdd:PRK08276 228 ALIERYR---VTHSQLVPTMFVRMLKLPEE----------VRA----RydvssLRVAIHAAAPCPVEVKRAMIDWWGPII 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 370 LERYGMTE-IGMALSNPLKGPRIPGAVGSPLpRVEVRIvmnnttnttivLGDHRNTrvCPglEGKEGELLVRGPSVFKEY 448
Cdd:PRK08276 291 HEYYASSEgGGVTVITSEDWLAHPGSVGKAV-LGEVRI-----------LDEDGNE--LP--PGEIGTVYFEMDGYPFEY 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 449 WNKPQETRESFIDGGWFKTGDtVVY--KDGVYWIMGRSSvDIIKSAGYKISALEVERHLLAHPDIIDVAVIGAPDAIWGQ 526
Cdd:PRK08276 355 HNDPEKTAAARNPHGWVTVGD-VGYldEDGYLYLTDRKS-DMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGE 432
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1250165799 527 KVTAVVQLRKGqsmTLPD------LKTWAREHMAPYTIPTGLLLVEEMPRNQMGKVNKKDL 581
Cdd:PRK08276 433 RVKAVVQPADG---ADAGdalaaeLIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRL 490
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
65-581 |
1.01e-48 |
|
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: 176.55 E-value: 1.01e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 65 RAPafgDKPAIIDSSGSH--SYKQLYCSSLGLAGRistalnLDFGGLE-GKRISFLCANDASYTVAQWAAWMSGGTAVPL 141
Cdd:cd05923 13 RAP---DACAIADPARGLrlTYSELRARIEAVAAR------LHARGLRpGQRVAVVLPNSVEAVIALLALHRLGAVPALI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 142 FRKHPQSELEYIIS-DSQSSLLVAghPYAGTLEplALKLGLPCLTlpptsNLGTLDGTDTQEKEA-AITDWADRP---AM 216
Cdd:cd05923 84 NPRLKAAELAELIErGEMTAAVIA--VDAQVMD--AIFQSGVRVL-----ALSDLVGLGEPESAGpLIEDPPREPeqpAF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 217 IIYTSGTTGRPKGVL--HMHSNIQAMVQGLVSEWAWTRDDVILHTLPLHHVHGIVNKLLCPLWVGATCVMLPEFQPQKVW 294
Cdd:cd05923 155 VFYTSGTTGLPKGAVipQRAAESRVLFMSTQAGLRHGRHNVVLGLMPLYHVIGFFAVLVAALALDGTYVVVEEFDPADAL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 295 EMLlsSKAPMVNVFmAVPTIYSKLIQyydqHFTQPHVKdfvravcKERIRLMVSGSAALPLPTLQRWEEITGHTLLERYG 374
Cdd:cd05923 235 KLI--EQERVTSLF-ATPTHLDALAA----AAEFAGLK-------LSSLRHVTFAGATMPDAVLERVNQHLPGEKVNIYG 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 375 MTEIGMALSNPlkGPRiPGAVGSPLPRVEVRIVMnnttnttiVLGdhRNTRVCPglEGKEGELLVR--GPSVFKEYWNKP 452
Cdd:cd05923 301 TTEAMNSLYMR--DAR-TGTEMRPGFFSEVRIVR--------IGG--SPDEALA--NGEEGELIVAaaADAAFTGYLNQP 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 453 QETRESFIDGgWFKTGDT-VVYKDGVYWIMGRSSvDIIKSAGYKISALEVERHLLAHPDIIDVAVIGAPDAIWGQKVTAV 531
Cdd:cd05923 366 EATAKKLQDG-WYRTGDVgYVDPSGDVRILGRVD-DMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTAC 443
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1250165799 532 VQLRKGqSMTLPDLKTWARE-HMAPYTIPTGLLLVEEMPRNQMGKVNKKDL 581
Cdd:cd05923 444 VVPREG-TLSADELDQFCRAsELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
66-578 |
1.06e-48 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 178.04 E-value: 1.06e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 66 APAFGDKPAIIDSSGS--HSYKQLycssLGLAGRISTALnLDFGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLFR 143
Cdd:PRK12583 28 VARFPDREALVVRHQAlrYTWRQL----ADAVDRLARGL-LALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 144 KHPQSELEYIISDSQSSLLVA-----GHPYAGTLEPLA--LKLG----LPCLTLPPTSNLGTLDGTDTQ----------- 201
Cdd:PRK12583 103 AYRASELEYALGQSGVRWVICadafkTSDYHAMLQELLpgLAEGqpgaLACERLPELRGVVSLAPAPPPgflawhelqar 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 202 ----------EKEAAITdwADRPAMIIYTSGTTGRPKGVLHMHSNIQAMVQGLVSEWAWTRDDVILHTLPLHHVHGIVNK 271
Cdd:PRK12583 183 getvsrealaERQASLD--RDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCVPVPLYHCFGMVLA 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 272 LLCPLWVGAtCVMLP--EFQPQKVWEMLLSSKApmvNVFMAVPTIY-SKLiqyydqhfTQPHVKDFVRAvckeRIRLMVS 348
Cdd:PRK12583 261 NLGCMTVGA-CLVYPneAFDPLATLQAVEEERC---TALYGVPTMFiAEL--------DHPQRGNFDLS----SLRTGIM 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 349 GSAALPLPTLQR-WEEITGHTLLERYGMTEIG-----MALSNPLkgPRIPGAVGSPLPRVEVRIVmnNTTNTTIVLGDhr 422
Cdd:PRK12583 325 AGAPCPIEVMRRvMDEMHMAEVQIAYGMTETSpvslqTTAADDL--ERRVETVGRTQPHLEVKVV--DPDGATVPRGE-- 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 423 ntrvcpglegkEGELLVRGPSVFKEYWNKPQETRESFIDGGWFKTGD-TVVYKDGVYWIMGRSSvDIIKSAGYKISALEV 501
Cdd:PRK12583 399 -----------IGELCTRGYSVMKGYWNNPEATAESIDEDGWMHTGDlATMDEQGYVRIVGRSK-DMIIRGGENIYPREI 466
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1250165799 502 ERHLLAHPDIIDVAVIGAPDAIWGQKVTAVVQLRKGQSMTLPDLKTWAREHMAPYTIPTGLLLVEEMPRNQMGKVNK 578
Cdd:PRK12583 467 EEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRLHPGHAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQK 543
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
111-517 |
1.90e-47 |
|
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: 172.63 E-value: 1.90e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 111 GKRISFLCANDASYTVAQWAAWMSGGTAVP-LFRKHPQsELEYIISDSQSSLLVAGHPyagtleplalklglpcltlppt 189
Cdd:cd05914 32 GDRVALMGENRPEWGIAFFAIWTYGAIAVPiLAEFTAD-EVHHILNHSEAKAIFVSDE---------------------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 190 snlgtldgtdtqekeaaitdwaDRPAMIIYTSGTTGRPKGVLHMHSNIQAMVQGLVSEWAWTRDDVILHTLPLHHVHGIV 269
Cdd:cd05914 89 ----------------------DDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLLGKGDKILSILPLHHIYPLT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 270 NKLLCPLWVGATCVMLPEFQPQKVWEMLLSSKAP--MVNVFMAVPTIYSKLIQ-----------YYDQHFTQPHVKDFVR 336
Cdd:cd05914 147 FTLLLPLLNGAHVVFLDKIPSAKIIALAFAQVTPtlGVPVPLVIEKIFKMDIIpkltlkkfkfkLAKKINNRKIRKLAFK 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 337 AVCKE---RIRLMVSGSAALPLPTLQRWEEItGHTLLERYGMTEIGMALSNPLKGPRIPGAVGSPLPRVEVRIVmnnttn 413
Cdd:cd05914 227 KVHEAfggNIKEFVIGGAKINPDVEEFLRTI-GFPYTIGYGMTETAPIISYSPPNRIRLGSAGKVIDGVEVRID------ 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 414 ttivlgdhrntrvCPGLEGKEGELLVRGPSVFKEYWNKPQETRESFIDGGWFKTGD--TVVYKDGVYwIMGRSSVDIIKS 491
Cdd:cd05914 300 -------------SPDPATGEGEIIVRGPNVMKGYYKNPEATAEAFDKDGWFHTGDlgKIDAEGYLY-IRGRKKEMIVLS 365
|
410 420
....*....|....*....|....*.
gi 1250165799 492 AGYKISALEVERHLLAHPDIIDVAVI 517
Cdd:cd05914 366 SGKNIYPEEIEAKINNMPFVLESLVV 391
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
213-585 |
3.15e-46 |
|
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: 165.58 E-value: 3.15e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 213 RPAMIIYTSGTTGRPKGVLHMHSNIQAMVQGLVSEWAWTRDDVILHTLPLHHVHGIVNKLLCpLWVGATCVMLPEFQPqk 292
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLYHVGGLAILVRS-LLAGAELVLLERNQA-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 293 vwemLLSSKAPMVNVFMA-VPTiysKLIQYYDQHFTQPHVKdfvravckeRIRLMVSGSAALPLPTLQRWEEiTGHTLLE 371
Cdd:cd17630 78 ----LAEDLAPPGVTHVSlVPT---QLQRLLDSGQGPAALK---------SLRAVLLGGAPIPPELLERAAD-RGIPLYT 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 372 RYGMTEIGMALSNPLKGPRIPGAVGSPLPRVEVRIVMNnttnttivlgdhrntrvcpglegkeGELLVRGPSVFKEYWNK 451
Cdd:cd17630 141 TYGMTETASQVATKRPDGFGRGGVGVLLPGRELRIVED-------------------------GEIWVGGASLAMGYLRG 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 452 PqeTRESFIDGGWFKTGDTVVY-KDGVYWIMGRSSvDIIKSAGYKISALEVERHLLAHPDIIDVAVIGAPDAIWGQKVTA 530
Cdd:cd17630 196 Q--LVPEFNEDGWFTTKDLGELhADGRLTVLGRAD-NMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVA 272
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1250165799 531 VVQLRKGqsMTLPDLKTWAREHMAPYTIPTGLLLVEEMPRNQMGKVNKKDLLRHF 585
Cdd:cd17630 273 VIVGRGP--ADPAELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRAWL 325
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
65-583 |
3.22e-46 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 170.71 E-value: 3.22e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 65 RAPAFGDKPAIIDSSGSHSYKQLYCSSLGLAGRISTAlnldfGGLEGKRISFLCANDASY-TVAQWAAWMsGGTAVPL-- 141
Cdd:PRK06155 30 QAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAA-----GVKRGDRVALMCGNRIEFlDVFLGCAWL-GAIAVPInt 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 142 FRKHPQseLEYIISDSQSSLLVAGHPYAGTLEPL-ALKLGLPCLTLPPTSNLGTLD-GTDTQE---KEAAITDWADRP-- 214
Cdd:PRK06155 104 ALRGPQ--LEHILRNSGARLLVVEAALLAALEAAdPGDLPLPAVWLLDAPASVSVPaGWSTAPlppLDAPAPAAAVQPgd 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 215 -AMIIYTSGTTGRPKGVLHMHSniQAMVQGLVSEWAW--TRDDVILHTLPLHHVHGIvNKLLCPLWVGATCVMLPEFQPQ 291
Cdd:PRK06155 182 tAAILYTSGTTGPSKGVCCPHA--QFYWWGRNSAEDLeiGADDVLYTTLPLFHTNAL-NAFFQALLAGATYVLEPRFSAS 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 292 KVWEMLLSSKA-------PMVNVFMAVPTiyskliqyydqhftQPHVKDFvravckeriRLMVSGSAALPLPTLQRWEEI 364
Cdd:PRK06155 259 GFWPAVRRHGAtvtyllgAMVSILLSQPA--------------RESDRAH---------RVRVALGPGVPAALHAAFRER 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 365 TGHTLLERYGMTEIGMALSNPLKGPRiPGAVGSPLPRVEVRIVmnnttnttivlgDHRNTRVCPGlegKEGELLVRG--P 442
Cdd:PRK06155 316 FGVDLLDGYGSTETNFVIAVTHGSQR-PGSMGRLAPGFEARVV------------DEHDQELPDG---EPGELLLRAdeP 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 443 SVFKE-YWNKPQETRESFIDGgWFKTGDTVVYK-DGVYWIMGRSSvDIIKSAGYKISALEVERHLLAHPDIIDVAVIGAP 520
Cdd:PRK06155 380 FAFATgYFGMPEKTVEAWRNL-WFHTGDRVVRDaDGWFRFVDRIK-DAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVP 457
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1250165799 521 DAIWGQKVTAVVQLRKGQSMTLPDLKTWAREHMAPYTIPTGLLLVEEMPRNQMGKVnKKDLLR 583
Cdd:PRK06155 458 SELGEDEVMAAVVLRDGTALEPVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKV-QKFVLR 519
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
69-581 |
3.48e-46 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 171.10 E-value: 3.48e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 69 FGDKPAIIDSSGSHSYKQLYCSSLGLAGRISTALNLDfgglEGKRISFLCANDASYTVAQWAAWMSGGTAV---PLFRKH 145
Cdd:PRK05677 37 FADKPAFSNLGKTLTYGELYKLSGAFAAWLQQHTDLK----PGDRIAVQLPNVLQYPVAVFGAMRAGLIVVntnPLYTAR 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 146 pqsELEYIISDSQSSLLVA----GH------PYAGT-----------LEPLA----------LKLGLPCLTLPPTSNLGT 194
Cdd:PRK05677 113 ---EMEHQFNDSGAKALVClanmAHlaekvlPKTGVkhvivtevadmLPPLKrllinavvkhVKKMVPAYHLPQAVKFND 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 195 LDGTDTQEKEAAITDWADRPAMIIYTSGTTGRPKGVLHMHSNI-------QAMVQGLVSEWAwtrdDVILHTLPLHHVHG 267
Cdd:PRK05677 190 ALAKGAGQPVTEANPQADDVAVLQYTGGTTGVAKGAMLTHRNLvanmlqcRALMGSNLNEGC----EILIAPLPLYHIYA 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 268 IVNKLLCPLWVGATCVMLPEfqPQKVWEMLLSSKAPMVNVFMAVPTIYSKLIqyydqhftqpHVKDFvRAVCKERIRLMV 347
Cdd:PRK05677 266 FTFHCMAMMLIGNHNILISN--PRDLPAMVKELGKWKFSGFVGLNTLFVALC----------NNEAF-RKLDFSALKLTL 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 348 SGSAALPLPTLQRWEEITGHTLLERYGMTEIG-MALSNPLKGPRIpGAVGSPLPRVEVRIVMNNTTNTTIvlgdhrntrv 426
Cdd:PRK05677 333 SGGMALQLATAERWKEVTGCAICEGYGMTETSpVVSVNPSQAIQV-GTIGIPVPSTLCKVIDDDGNELPL---------- 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 427 cpgleGKEGELLVRGPSVFKEYWNKPQETRESFIDGGWFKTGD-TVVYKDGVYWIMGRSSvDIIKSAGYKISALEVERHL 505
Cdd:PRK05677 402 -----GEVGELCVKGPQVMKGYWQRPEATDEILDSDGWLKTGDiALIQEDGYMRIVDRKK-DMILVSGFNVYPNELEDVL 475
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1250165799 506 LAHPDIIDVAVIGAPDAIWGQKVTAVVQLRKGQSMTLPDLKTWAREHMAPYTIPTGLLLVEEMPRNQMGKVNKKDL 581
Cdd:PRK05677 476 AALPGVLQCAAIGVPDEKSGEAIKVFVVVKPGETLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRREL 551
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
94-585 |
3.82e-46 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 170.45 E-value: 3.82e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 94 LAGRISTAlnldfGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLFRKHPQSEleyiisdsQSSLLVAghpyAGTLE 173
Cdd:PRK05852 56 LAGQLTRS-----GLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAE--------QRVRSQA----AGARV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 174 PLALKLGlPCLTLPPTSNLGTLD---GTDTQEKEAAI---------------TDWADRP--AMIIYTSGTTGRPKGVLHM 233
Cdd:PRK05852 119 VLIDADG-PHDRAEPTTRWWPLTvnvGGDSGPSGGTLsvhldaateptpatsTPEGLRPddAMIMFTGGTTGLPKMVPWT 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 234 HSNIQAMVQGLVSEWAWTRDDVILHTLPLHHVHGIVNKLLCPLWVGATcVMLP---EFQPQKVWEMLLSSKAPMvnvFMA 310
Cdd:PRK05852 198 HANIASSVRAIITGYRLSPRDATVAVMPLYHGHGLIAALLATLASGGA-VLLPargRFSAHTFWDDIKAVGATW---YTA 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 311 VPTIYSKLIQYYD-QHFTQPHVKdfvravckerIRLMVSGSAALPLPTLQRWEEITGHTLLERYGMTEIgmalSNPLKGP 389
Cdd:PRK05852 274 VPTIHQILLERAAtEPSGRKPAA----------LRFIRSCSAPLTAETAQALQTEFAAPVVCAFGMTEA----THQVTTT 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 390 RIPGAVGSPLPRVEVRIVMNNTTNTTIVLGDhrNTRVCPglEGKEGELLVRGPSVFKEYWNKPQETRESFIDGgWFKTGD 469
Cdd:PRK05852 340 QIEGIGQTENPVVSTGLVGRSTGAQIRIVGS--DGLPLP--AGAVGEVWLRGTTVVRGYLGDPTITAANFTDG-WLRTGD 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 470 T-VVYKDGVYWIMGRSSvDIIKSAGYKISALEVERHLLAHPDIIDVAVIGAPDAIWGQKVTAVVQLRKGQSMTLPDLKTW 548
Cdd:PRK05852 415 LgSLSAAGDLSIRGRIK-ELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIVPRESAPPTAEELVQF 493
|
490 500 510
....*....|....*....|....*....|....*..
gi 1250165799 549 AREHMAPYTIPTGLLLVEEMPRNQMGKVNKKDLLRHF 585
Cdd:PRK05852 494 CRERLAAFEIPASFQEASGLPHTAKGSLDRRAVAEQF 530
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
71-581 |
6.43e-46 |
|
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: 169.58 E-value: 6.43e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 71 DKPAIIDSSGSHSYKQLYCSSLGLAGRISTAlnldfgGLE-GKRISFLCANDASYTVAQWAAWMSGGTAVPL--FRKHPQ 147
Cdd:TIGR03098 15 DATALVHHDRTLTYAALSERVLALASGLRGL------GLArGERVAIYLDKRLETVTAMFGAALAGGVFVPInpLLKAEQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 148 seLEYIISDSQSSLLVAGhpyagtleplALKLGLPCLTLPPTSNLGTLDGTDTQEK------EAAITDWA---------- 211
Cdd:TIGR03098 89 --VAHILADCNVRLLVTS----------SERLDLLHPALPGCHDLRTLIIVGDPAHaseghpGEEPASWPkllalgdadp 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 212 ------DRPAMIIYTSGTTGRPKGVLHMHSNIQAMVQGLVSEWAWTRDDVILHTLPLHHVHGIvNKLLCPLWVGATCVML 285
Cdd:TIGR03098 157 phpvidSDMAAILYTSGSTGRPKGVVLSHRNLVAGAQSVATYLENRPDDRLLAVLPLSFDYGF-NQLTTAFYVGATVVLH 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 286 PEFQPQKVwemLLSSKAPMVNVFMAVPTIYSKLIQYYDQHFTQPHvkdfvravckerIRLMVSGSAALPLPTLQRWEEIT 365
Cdd:TIGR03098 236 DYLLPRDV---LKALEKHGITGLAAVPPLWAQLAQLDWPESAAPS------------LRYLTNSGGAMPRATLSRLRSFL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 366 GHT-LLERYGMTEIGMALS-NPLKGPRIPGAVGSPLPRVEVRIVMNnttnttivLGDHrntrvCpgLEGKEGELLVRGPS 443
Cdd:TIGR03098 301 PNArLFLMYGLTEAFRSTYlPPEEVDRRPDSIGKAIPNAEVLVLRE--------DGSE-----C--APGEEGELVHRGAL 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 444 VFKEYWNKPQETRESF--IDG--GWFKTGDTVVY--------KDGVYWIMGRSSvDIIKSAGYKISALEVERHLLAHPDI 511
Cdd:TIGR03098 366 VAMGYWNDPEKTAERFrpLPPfpGELHLPELAVWsgdtvrrdEEGFLYFVGRRD-EMIKTSGYRVSPTEVEEVAYATGLV 444
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 512 IDVAVIGAPDAIWGQKVTAVVQLRKGQSMTLPDLKTWAREHMAPYTIPTGLLLVEEMPRNQMGKVNKKDL 581
Cdd:TIGR03098 445 AEAVAFGVPDPTLGQAIVLVVTPPGGEELDRAALLAECRARLPNYMVPALIHVRQALPRNANGKIDRKAL 514
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
66-575 |
7.18e-46 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 169.68 E-value: 7.18e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 66 APAFGDKPAIIDSSGSHSYKQLYCSSLGLAgrisTALnLDFGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLFRKH 145
Cdd:PRK07798 13 ADAVPDRVALVCGDRRLTYAELEERANRLA----HYL-IAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 146 PQSELEYIISDSQSSLLVAGHPYAGTLEPLalklglpcltLPPTSNLGTL----DGTDTQEK------EAAITDW-ADRP 214
Cdd:PRK07798 88 VEDELRYLLDDSDAVALVYEREFAPRVAEV----------LPRLPKLRTLvvveDGSGNDLLpgavdyEDALAAGsPERD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 215 A--------MIIYTSGTTGRPKGVLHMHSNIQaMVQG----------LVSEWAWTRDD------VILHTLPLHHVHGIVN 270
Cdd:PRK07798 158 FgerspddlYLLYTGGTTGMPKGVMWRQEDIF-RVLLggrdfatgepIEDEEELAKRAaagpgmRRFPAPPLMHGAGQWA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 271 KLLCpLWVGATCVMLP--EFQPQKVWEMLLSSKA---PMVNVFMAVPTIyskliqyydQHFTQPHVKDFvravckERIRL 345
Cdd:PRK07798 237 AFAA-LFSGQTVVLLPdvRFDADEVWRTIEREKVnviTIVGDAMARPLL---------DALEARGPYDL------SSLFA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 346 MVSGSAALPLPTLQRWEEITGH-TLLERYGMTEIG-MALSNPLKGPRIPGAvgsplPRVEVRivmnnttNTTIVLGDHRN 423
Cdd:PRK07798 301 IASGGALFSPSVKEALLELLPNvVLTDSIGSSETGfGGSGTVAKGAVHTGG-----PRFTIG-------PRTVVLDEDGN 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 424 tRVCPGlEGKEGeLLVRGPSVFKEYWNKPQETRESF--IDG-GWFKTGD-TVVYKDGVYWIMGRSSVdIIKSAGYKISAL 499
Cdd:PRK07798 369 -PVEPG-SGEIG-WIARRGHIPLGYYKDPEKTAETFptIDGvRYAIPGDrARVEADGTITLLGRGSV-CINTGGEKVFPE 444
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1250165799 500 EVERHLLAHPDIIDVAVIGAPDAIWGQKVTAVVQLRKGQSMTLPDLKTWAREHMAPYTIPTGLLLVEEMPRNQMGK 575
Cdd:PRK07798 445 EVEEALKAHPDVADALVVGVPDERWGQEVVAVVQLREGARPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
70-581 |
7.61e-46 |
|
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: 168.24 E-value: 7.61e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 70 GDKPAIIDSSGSHSYKQLYCSSLGLAGRIStalnlDFGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLFRKHPQSE 149
Cdd:cd12116 1 PDATAVRDDDRSLSYAELDERANRLAARLR-----ARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 150 LEYIISDSQSSLLVAGhpyAGTLEPLALKLGLPCLTLPPTSNLGTldgtdtqekEAAITDWADRPAMIIYTSGTTGRPKG 229
Cdd:cd12116 76 LRYILEDAEPALVLTD---DALPDRLPAGLPVLLLALAAAAAAPA---------APRTPVSPDDLAYVIYTSGSTGRPKG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 230 VLHMHSNIQAMVQGLVSEWAWTRDDVILH-TLPLHHVHGIvnKLLCPLWVGATCVMLPE---FQPQKVWEMLlssKAPMV 305
Cdd:cd12116 144 VVVSHRNLVNFLHSMRERLGLGPGDRLLAvTTYAFDISLL--ELLLPLLAGARVVIAPRetqRDPEALARLI---EAHSI 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 306 NVFMAVPTIYSKLIQyydqhfTQPHVKDFVRAVCkerirlmvsGSAALPlPTLQRWEEITGHTLLERYGMTEI----GMA 381
Cdd:cd12116 219 TVMQATPATWRMLLD------AGWQGRAGLTALC---------GGEALP-PDLAARLLSRVGSLWNLYGPTETtiwsTAA 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 382 LSNPLKGPrIPgaVGSPLPrvevrivmnnttNTTIVLGDHRNTRVCPGLegkEGELLVRGPSVFKEYWNKPQETRESFID 461
Cdd:cd12116 283 RVTAAAGP-IP--IGRPLA------------NTQVYVLDAALRPVPPGV---PGELYIGGDGVAQGYLGRPALTAERFVP 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 462 -------GGWFKTGDTVVYK-DGVYWIMGRSSvDIIKSAGYKISALEVERHLLAHPDIIDVAVIGAPDAiWGQKVTAVVQ 533
Cdd:cd12116 345 dpfagpgSRLYRTGDLVRRRaDGRLEYLGRAD-GQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDG-GDRRLVAYVV 422
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1250165799 534 LRKGQSMTLPDLKTWAREHMAPYTIPTGLLLVEEMPRNQMGKVNKKDL 581
Cdd:cd12116 423 LKAGAAPDAAALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
215-581 |
8.80e-46 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 169.85 E-value: 8.80e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 215 AMIIYTSGTTGRPKGVLHMHSNIQAMVqgLVSEWAW-----TRDDVILHTLPLHHVHGI-VNKLLCpLWVGATCVML--P 286
Cdd:PRK08974 209 AFLQYTGGTTGVAKGAMLTHRNMLANL--EQAKAAYgpllhPGKELVVTALPLYHIFALtVNCLLF-IELGGQNLLItnP 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 287 EFQPQKVWEMllsSKAPMVnVFMAVPTIYSKLIQyyDQHFTQphvKDFvravckERIRLMVSGSAALPLPTLQRWEEITG 366
Cdd:PRK08974 286 RDIPGFVKEL---KKYPFT-AITGVNTLFNALLN--NEEFQE---LDF------SSLKLSVGGGMAVQQAVAERWVKLTG 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 367 HTLLERYGMTEIGMALS-NPLKGPRIPGAVGSPLPRVEVRIVMNNTTNTTIvlgdhrntrvcpgleGKEGELLVRGPSVF 445
Cdd:PRK08974 351 QYLLEGYGLTECSPLVSvNPYDLDYYSGSIGLPVPSTEIKLVDDDGNEVPP---------------GEPGELWVKGPQVM 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 446 KEYWNKPQETREsFIDGGWFKTGDTVVY-KDGVYWIMGRSSvDIIKSAGYKISALEVERHLLAHPDIIDVAVIGAPDAIW 524
Cdd:PRK08974 416 LGYWQRPEATDE-VIKDGWLATGDIAVMdEEGFLRIVDRKK-DMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVS 493
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1250165799 525 GQKVTAVVqLRKGQSMTLPDLKTWAREHMAPYTIPTGLLLVEEMPRNQMGKVNKKDL 581
Cdd:PRK08974 494 GEAVKIFV-VKKDPSLTEEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRREL 549
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
93-582 |
4.98e-45 |
|
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: 165.69 E-value: 4.98e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 93 GLAGRISTALNLDfGGLEGKRISFLCANDASYTVAQWAAWMSGGT----AVPLFRKHPQSELEYIISDSQSSLLVAGHPY 168
Cdd:cd05922 1 LGVSAAASALLEA-GGVRGERVVLILPNRFTYIELSFAVAYAGGRlglvFVPLNPTLKESVLRYLVADAGGRIVLADAGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 169 AGTLeplalKLGLPCLTLPPTSnLGTLDGTDTQEKEAAITDWADRPAMIIYTSGTTGRPKGVLHMHSNIQAMVQGLVSEW 248
Cdd:cd05922 80 ADRL-----RDALPASPDPGTV-LDADGIRAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 249 AWTRDDVILHTLPLHHVHGIvNKLLCPLWVGATCVMLPEFQ-PQKVWEMLLSSKAPMvnvFMAVPTIYSKLIQYYDQHFT 327
Cdd:cd05922 154 GITADDRALTVLPLSYDYGL-SVLNTHLLRGATLVLTNDGVlDDAFWEDLREHGATG---LAGVPSTYAMLTRLGFDPAK 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 328 QPHvkdfvravckerIRLMVSGSAALPLPTLQRWEE-ITGHTLLERYGMTEI--GMALSNPLKGPRIPGAVGSPLPRVEV 404
Cdd:cd05922 230 LPS------------LRYLTQAGGRLPQETIARLRElLPGAQVYVMYGQTEAtrRMTYLPPERILEKPGSIGLAIPGGEF 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 405 RIvmnnttnttivlgDHRNTRVCPglEGKEGELLVRGPSVFKEYWNKPQETRESFIDGGWFKTGDTVVY-KDGVYWIMGR 483
Cdd:cd05922 298 EI-------------LDDDGTPTP--PGEPGEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRdEDGFLFIVGR 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 484 SSvDIIKSAGYKISALEVERHLLAHPDIIDVAVIGAPDAIwGQKVTAVVQLRKGqsMTLPDLKTWAREHMAPYTIPTGLL 563
Cdd:cd05922 363 RD-RMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDPL-GEKLALFVTAPDK--IDPKDVLRSLAERLPPYKVPATVR 438
|
490
....*....|....*....
gi 1250165799 564 LVEEMPRNQMGKVNKKDLL 582
Cdd:cd05922 439 VVDELPLTASGKVDYAALR 457
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
210-583 |
7.54e-45 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 167.28 E-value: 7.54e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 210 WA-DRPAMIIYTSGTTGRPKGVLHMHSNIqaMVQGL--VSEWAWTRDDVILHTLPLHHVHGIvNKLLCPLWVGATCVMLP 286
Cdd:PLN02860 169 WApDDAVLICFTSGTTGRPKGVTISHSAL--IVQSLakIAIVGYGEDDVYLHTAPLCHIGGL-SSALAMLMVGACHVLLP 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 287 EFQPQKVWEMLlssKAPMVNVFMAVPTIYSKLIQYYDQHFTQPhvkdfvravCKERIRLMVSGSAALPLPTLQRWEEITG 366
Cdd:PLN02860 246 KFDAKAALQAI---KQHNVTSMITVPAMMADLISLTRKSMTWK---------VFPSVRKILNGGGSLSSRLLPDAKKLFP 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 367 HT-LLERYGMTEIG-----MALSNP-LKGPRIPGA-----------------VGSPLPRVEVRIvmnnttnttivlgdhr 422
Cdd:PLN02860 314 NAkLFSAYGMTEACssltfMTLHDPtLESPKQTLQtvnqtksssvhqpqgvcVGKPAPHVELKI---------------- 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 423 ntrvCPGLEGKEGELLVRGPSVFKEYWNKPQETRESFIDGGWFKTGDT-VVYKDGVYWIMGRSSvDIIKSAGYKISALEV 501
Cdd:PLN02860 378 ----GLDESSRVGRILTRGPHVMLGYWGQNSETASVLSNDGWLDTGDIgWIDKAGNLWLIGRSN-DRIKTGGENVYPEEV 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 502 ERHLLAHPDIIDVAVIGAPDAIWGQKVTAVVQLRKG------------QSMTLP--DLKTWARE-HMAPYTIPTGLLLVE 566
Cdd:PLN02860 453 EAVLSQHPGVASVVVVGVPDSRLTEMVVACVRLRDGwiwsdnekenakKNLTLSseTLRHHCREkNLSRFKIPKLFVQWR 532
|
410
....*....|....*...
gi 1250165799 567 E-MPRNQMGKVnKKDLLR 583
Cdd:PLN02860 533 KpFPLTTTGKI-RRDEVR 549
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
62-581 |
2.39e-44 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 165.77 E-value: 2.39e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 62 VFVRA-PAFGDKPAIIDSSGSHSYKQLYCSSLGLAGRISTALNLdfggLEGKRISFLCANDASYTVAQWAAWMSGGTAV- 139
Cdd:PRK12492 29 VFERScKKFADRPAFSNLGVTLSYAELERHSAAFAAYLQQHTDL----VPGDRIAVQMPNVLQYPIAVFGALRAGLIVVn 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 140 --PL-----------------------FRKH-----PQSELEYIISDSQSSLLVAGHPYAGTLEPLALKLGLPCLTLPPT 189
Cdd:PRK12492 105 tnPLytaremrhqfkdsgaralvylnmFGKLvqevlPDTGIEYLIEAKMGDLLPAAKGWLVNTVVDKVKKMVPAYHLPQA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 190 SNLGTL--DGTDTQEKEAAITdwADRPAMIIYTSGTTGRPKGVLHMHSNIQAMVQGLVSEWAWTRDD----------VIL 257
Cdd:PRK12492 185 VPFKQAlrQGRGLSLKPVPVG--LDDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVRACLSQLGPDgqplmkegqeVMI 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 258 HTLPLHHVHGIVNKLLCPLWVGATCVMLPefQPQKVWEMLLSSKAPMVNVFMAVPTIYSKLIQYydqhftqPHVK--DFv 335
Cdd:PRK12492 263 APLPLYHIYAFTANCMCMMVSGNHNVLIT--NPRDIPGFIKELGKWRFSALLGLNTLFVALMDH-------PGFKdlDF- 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 336 ravckERIRLMVSGSAALPLPTLQRWEEITGHTLLERYGMTEIG-MALSNPLKGPRIPGAVGSPLPRVEVRIVMNNttnt 414
Cdd:PRK12492 333 -----SALKLTNSGGTALVKATAERWEQLTGCTIVEGYGLTETSpVASTNPYGELARLGTVGIPVPGTALKVIDDD---- 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 415 tivlgdhrntrvcpGLE---GKEGELLVRGPSVFKEYWNKPQETRESFIDGGWFKTGD-TVVYKDGVYWIMGRSSvDIIK 490
Cdd:PRK12492 404 --------------GNElplGERGELCIKGPQVMKGYWQQPEATAEALDAEGWFKTGDiAVIDPDGFVRIVDRKK-DLII 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 491 SAGYKISALEVERHLLAHPDIIDVAVIGAPDAIWGQKVTAVVQLRKGqSMTLPDLKTWAREHMAPYTIPTGLLLVEEMPR 570
Cdd:PRK12492 469 VSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVKLFVVARDP-GLSVEELKAYCKENFTGYKVPKHIVLRDSLPM 547
|
570
....*....|.
gi 1250165799 571 NQMGKVNKKDL 581
Cdd:PRK12492 548 TPVGKILRREL 558
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
71-581 |
3.96e-44 |
|
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: 162.86 E-value: 3.96e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 71 DKPAIIDSSGSHSYKQLYCSSLGLAGRIstalnLDFGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLFRKHPQSEL 150
Cdd:cd17643 2 EAVAVVDEDRRLTYGELDARANRLARTL-----RAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 151 EYIISDSQSSLLvaghpyagtleplalklglpcltlpptsnlgtldgtdtqekeaaITDwADRPAMIIYTSGTTGRPKGV 230
Cdd:cd17643 77 AFILADSGPSLL--------------------------------------------LTD-PDDLAYVIYTSGSTGRPKGV 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 231 LHMHSNIQAMVQGLVSEWAWTRDDVilhTLPLHH---------VHGivnkllcPLWVGATCVMLPEFQ---PQKVWEMLL 298
Cdd:cd17643 112 VVSHANVLALFAATQRWFGFNEDDV---WTLFHSyafdfsvweIWG-------ALLHGGRLVVVPYEVarsPEDFARLLR 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 299 SSKapmVNVFMAVPTIYSKLIQYYDQHFTQPHvkdfvravckeRIRLMVSGSAALPLPTLQRWEEITGH---TLLERYGM 375
Cdd:cd17643 182 DEG---VTVLNQTPSAFYQLVEAADRDGRDPL-----------ALRYVIFGGEALEAAMLRPWAGRFGLdrpQLVNMYGI 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 376 TEIGMALS-NPLKGPRIPGA----VGSPLPRVEVRIVmnnttnttivlgDHRNTRVCPGlegKEGELLVRGPSVFKEYWN 450
Cdd:cd17643 248 TETTVHVTfRPLDAADLPAAaaspIGRPLPGLRVYVL------------DADGRPVPPG---VVGELYVSGAGVARGYLG 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 451 KPQETRESFI---DGG----WFKTGDTVVYK-DGVYWIMGRSSvDIIKSAGYKISALEVERHLLAHPDIIDVAVIGAPDA 522
Cdd:cd17643 313 RPELTAERFVanpFGGpgsrMYRTGDLARRLpDGELEYLGRAD-EQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDE 391
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1250165799 523 IWGQKVTAVVQLRKGQSMTLPDLKTWAREHMAPYTIPTGLLLVEEMPRNQMGKVNKKDL 581
Cdd:cd17643 392 PGDTRLVAYVVADDGAAADIAELRALLKELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
69-581 |
2.49e-43 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 162.52 E-value: 2.49e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 69 FGDKPAIIDSSGSHSYKQLYCSSLGLAgrisTALnLDFGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPL-FRKHPQ 147
Cdd:PRK07470 20 FPDRIALVWGDRSWTWREIDARVDALA----AAL-AARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTnFRQTPD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 148 sELEYIISDSQSSLLV-----AGHPYAGTLEPLALKLGLPCLTLPPTSNLGTL--DGTDTQEKEAAITdwADRPAMIIYT 220
Cdd:PRK07470 95 -EVAYLAEASGARAMIchadfPEHAAAVRAASPDLTHVVAIGGARAGLDYEALvaRHLGARVANAAVD--HDDPCWFFFT 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 221 SGTTGRPKGVLHMHSNIQAMVQGLVSEW--AWTRDDVILHTLPLHHVHGIvnKLLCPLWVGATCVMLP--EFQPQKVWEm 296
Cdd:PRK07470 172 SGTTGRPKAAVLTHGQMAFVITNHLADLmpGTTEQDASLVVAPLSHGAGI--HQLCQVARGAATVLLPseRFDPAEVWA- 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 297 lLSSKAPMVNVFmAVPTIYSKLIQYydqhftqPHVKDFVRAvckeRIRLMVSGSAALPLPTLQRWEEITGHTLLERYGMT 376
Cdd:PRK07470 249 -LVERHRVTNLF-TVPTILKMLVEH-------PAVDRYDHS----SLRYVIYAGAPMYRADQKRALAKLGKVLVQYFGLG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 377 EIG-------MALSNPLKGP--RIpGAVGSPLPRVEVRIVmnnttnttivlgDHRNTRVCPGlegKEGELLVRGPSVFKE 447
Cdd:PRK07470 316 EVTgnitvlpPALHDAEDGPdaRI-GTCGFERTGMEVQIQ------------DDEGRELPPG---ETGEICVIGPAVFAG 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 448 YWNKPQETRESFIDGgWFKTGDT-VVYKDGVYWIMGRSSvDIIKSAGYKISALEVERHLLAHPDIIDVAVIGAPDAIWGQ 526
Cdd:PRK07470 380 YYNNPEANAKAFRDG-WFRTGDLgHLDARGFLYITGRAS-DMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGE 457
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1250165799 527 KVTAVVQLRKGQSMTLPDLKTWAREHMAPYTIPTGLLLVEEMPRNQMGKVNKKDL 581
Cdd:PRK07470 458 VGVAVCVARDGAPVDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMV 512
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
202-556 |
5.84e-43 |
|
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: 160.84 E-value: 5.84e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 202 EKEAAITDW-ADRPAMIIYTSGTTGRPKGVLHMHSNIQAMVQGL---VSEWAwTRDDVILHTLPLHHVHGIVNKLLCPLW 277
Cdd:cd17639 77 ECSAIFTDGkPDDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLgdrVPELL-GPDDRYLAYLPLAHIFELAAENVCLYR 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 278 VGATCVMLP----------------EFQPQ------KVWEMLlsSKAPMVNVfMAVPTI---------YSKLIQY---YD 323
Cdd:cd17639 156 GGTIGYGSPrtltdkskrgckgdltEFKPTlmvgvpAIWDTI--RKGVLAKL-NPMGGLkrtlfwtayQSKLKALkegPG 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 324 QHFTQPHVKDFVRAVCKERIRLMVSGSAALPLPTlQRWEEITGHTLLERYGMTEI--GMALSNPlkGPRIPGAVGSPLPR 401
Cdd:cd17639 233 TPLLDELVFKKVRAALGGRLRYMLSGGAPLSADT-QEFLNIVLCPVIQGYGLTETcaGGTVQDP--GDLETGRVGPPLPC 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 402 VEVRIVmnnttntTIVLGDHRNTRVCPglegkEGELLVRGPSVFKEYWNKPQETRESFIDGGWFKTGDTV-VYKDGVYWI 480
Cdd:cd17639 310 CEIKLV-------DWEEGGYSTDKPPP-----RGEILIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGeFHPDGTLKI 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 481 MGRSSvDIIKSAGYKISALE-VERHLLAHPDIIDVAVIGAPDAiwgQKVTAVVqlrkgqsmtLPD---LKTWAREHMAPY 556
Cdd:cd17639 378 IDRKK-DLVKLQNGEYIALEkLESIYRSNPLVNNICVYADPDK---SYPVAIV---------VPNekhLTKLAEKHGVIN 444
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
95-581 |
8.49e-43 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 160.63 E-value: 8.49e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 95 AGRISTALNlDFGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLFRKHPQSELEYIISDSQSSLLVAghpYAGTLEP 174
Cdd:PRK12406 21 AARAAGGLA-ALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIA---HADLLHG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 175 LA--LKLGLPCLTLPP----TSNLGtLDGTDTQEKEAAItDW--------------ADRPAMIIYTSGTTGRPKGVLHMH 234
Cdd:PRK12406 97 LAsaLPAGVTVLSVPTppeiAAAYR-ISPALLTPPAGAI-DWegwlaqqepydgppVPQPQSMIYTSGTTGHPKGVRRAA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 235 SNI-QAMVQGLVSEWAW--TRDDVILHTLPLHH----VHGIVNKLLcplwvGATCVMLPEFQPQKVWEMLLSSKapMVNV 307
Cdd:PRK12406 175 PTPeQAAAAEQMRALIYglKPGIRALLTGPLYHsapnAYGLRAGRL-----GGVLVLQPRFDPEELLQLIERHR--ITHM 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 308 FMaVPTIYSKLIQYYDQhftqphvkdfVRAVCK-ERIRLMVSGSAALPLPTLQRWEEITGHTLLERYGMTEIG-MALSNP 385
Cdd:PRK12406 248 HM-VPTMFIRLLKLPEE----------VRAKYDvSSLRHVIHAAAPCPADVKRAMIEWWGPVIYEYYGSTESGaVTFATS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 386 LKGPRIPGAVGSPLPRVEVRIVmnnttnttivlGDhrNTRVCPglEGKEGELLVRGPSV--FKeYWNKPQETREsfID-G 462
Cdd:PRK12406 317 EDALSHPGTVGKAAPGAELRFV-----------DE--DGRPLP--QGEIGEIYSRIAGNpdFT-YHNKPEKRAE--IDrG 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 463 GWFKTGDtVVY--KDGVYWIMGRSSvDIIKSAGYKISALEVERHLLAHPDIIDVAVIGAPDAIWGQKVTAVVQLRKGQSM 540
Cdd:PRK12406 379 GFITSGD-VGYldADGYLFLCDRKR-DMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPGATL 456
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1250165799 541 TLPDLKTWAREHMAPYTIPTGLLLVEEMPRNQMGKVNKKDL 581
Cdd:PRK12406 457 DEADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRL 497
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
214-581 |
1.45e-42 |
|
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: 160.32 E-value: 1.45e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 214 PAMIIYTSGTTGRPKGVLHMHSN--IQAMVQGlvSEW-AWTRDDVILHTLPLHHVHGIVNKLLCPlWVGATCVM---LPE 287
Cdd:cd05928 176 PMAIYFTSGTTGSPKMAEHSHSSlgLGLKVNG--RYWlDLTASDIMWNTSDTGWIKSAWSSLFEP-WIQGACVFvhhLPR 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 288 FQPQKVWEMLlsSKAPmVNVFMAVPTIYSKLIQyydqhftqphvKDFVRAVCKeRIRLMVSGSAALPLPTLQRWEEITGH 367
Cdd:cd05928 253 FDPLVILKTL--SSYP-ITTFCGAPTVYRMLVQ-----------QDLSSYKFP-SLQHCVTGGEPLNPEVLEKWKAQTGL 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 368 TLLERYGMTEIGMALSNPlKGPRI-PGAVGSPLPRVEVRIVMNNttnttivlGDhrntrVCPglEGKEGELLVR-GP--- 442
Cdd:cd05928 318 DIYEGYGQTETGLICANF-KGMKIkPGSMGKASPPYDVQIIDDN--------GN-----VLP--PGTEGDIGIRvKPirp 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 443 -SVFKEYWNKPQETRESfIDGGWFKTGDT-VVYKDGVYWIMGRSSvDIIKSAGYKISALEVERHLLAHPDIIDVAVIGAP 520
Cdd:cd05928 382 fGLFSGYVDNPEKTAAT-IRGDFYLTGDRgIMDEDGYFWFMGRAD-DVINSSGYRIGPFEVESALIEHPAVVESAVVSSP 459
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1250165799 521 DAIWGQKVTAVVQL------RKGQSMTLpDLKTWAREHMAPYTIPTGLLLVEEMPRNQMGKVNKKDL 581
Cdd:cd05928 460 DPIRGEVVKAFVVLapqflsHDPEQLTK-ELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNEL 525
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
62-585 |
4.97e-42 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 159.24 E-value: 4.97e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 62 VFVRAPAFGDkPAIIDSSG--SHSYKQLycssLGLAGRISTALNLDFGGLEGKRISFLCANDASYTVAQWAAWMSGGTAV 139
Cdd:PLN02574 46 IFSHHNHNGD-TALIDSSTgfSISYSEL----QPLVKSMAAGLYHVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 140 PLFRKHPQSELEYIISDSQSSLLVAGHPYAGTLEPLalklGLPCLTLPPTSNLgtldgtDTQEKEAAITDWA-------- 211
Cdd:PLN02574 121 TMNPSSSLGEIKKRVVDCSVGLAFTSPENVEKLSPL----GVPVIGVPENYDF------DSKRIEFPKFYELikedfdfv 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 212 -------DRPAMIIYTSGTTGRPKGVLHMHSNIQAMVQGLV----SEWAWT-RDDVILHTLPLHHVHGIVNKLLCPLWVG 279
Cdd:PLN02574 191 pkpvikqDDVAAIMYSSGTTGASKGVVLTHRNLIAMVELFVrfeaSQYEYPgSDNVYLAALPMFHIYGLSLFVVGLLSLG 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 280 ATCVMLPEFQpqkVWEMLLSSKAPMVNVFMAVPTIYSKLIqyydqHFTQPhvkdfVRAVCKERIRLMVSGSAALPLPTLQ 359
Cdd:PLN02574 271 STIVVMRRFD---ASDMVKVIDRFKVTHFPVVPPILMALT-----KKAKG-----VCGEVLKSLKQVSCGAAPLSGKFIQ 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 360 RWEEITGHT-LLERYGMTE---IGMALSNPLKGPRIpGAVGSPLPRVEVRIVmnnttnttivlgDHRNTRVCPglEGKEG 435
Cdd:PLN02574 338 DFVQTLPHVdFIQGYGMTEstaVGTRGFNTEKLSKY-SSVGLLAPNMQAKVV------------DWSTGCLLP--PGNCG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 436 ELLVRGPSVFKEYWNKPQETRESFIDGGWFKTGDTVVY-KDGVYWIMGRSSvDIIKSAGYKISALEVERHLLAHPDIIDV 514
Cdd:PLN02574 403 ELWIQGPGVMKGYLNNPKATQSTIDKDGWLRTGDIAYFdEDGYLYIVDRLK-EIIKYKGFQIAPADLEAVLISHPEIIDA 481
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1250165799 515 AVIGAPDAIWGQKVTAVVQLRKGQSMTLPDLKTWAREHMAPYTIPTGLLLVEEMPRNQMGKVNKKDLLRHF 585
Cdd:PLN02574 482 AVTAVPDKECGEIPVAFVVRRQGSTLSQEAVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRRELKRSL 552
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
211-581 |
6.08e-42 |
|
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: 157.88 E-value: 6.08e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 211 ADRPAMIIYTSGTTGRPKGVLHMHSNIQAMVQGLVSEWAWTRDDVILHTLPLHHVHGIVNKLLCPLWVGATCVMLPE-FQ 289
Cdd:cd05909 146 PDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPFFHSFGLTGCLWLPLLSGIKVVFHPNpLD 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 290 PQKVWEMLLSSKApmvNVFMAVPTIYSKLIQYYdqhftqpHVKDFvravckERIRLMVSGSAALPLPTLQRWEEITGHTL 369
Cdd:cd05909 226 YKKIPELIYDKKA---TILLGTPTFLRGYARAA-------HPEDF------SSLRLVVAGAEKLKDTLRQEFQEKFGIRI 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 370 LERYGMTEIGMALS-NPLKGPRIPGAVGSPLPRVEVRIVMNNTTnttivlgdhrntrvCPGLEGKEGELLVRGPSVFKEY 448
Cdd:cd05909 290 LEGYGTTECSPVISvNTPQSPNKEGTVGRPLPGMEVKIVSVETH--------------EEVPIGEGGLLLVRGPNVMLGY 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 449 WNKPQETRESFIDgGWFKTGDtVVYKDGVYW--IMGRSSvDIIKSAGYKISALEVERHLLAH-PDIIDVAVIGAPDAIWG 525
Cdd:cd05909 356 LNEPELTSFAFGD-GWYDTGD-IGKIDGEGFltITGRLS-RFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVPDGRKG 432
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1250165799 526 QKVTAVVQlrkGQSMTLPDLKTWAREHMAP-YTIPTGLLLVEEMPRNQMGKVNKKDL 581
Cdd:cd05909 433 EKIVLLTT---TTDTDPSSLNDILKNAGISnLAKPSYIHQVEEIPLLGTGKPDYVTL 486
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
71-581 |
7.46e-42 |
|
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: 156.76 E-value: 7.46e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 71 DKPAIIDSSGSHSYKQLYCSSLGLAGRISTAlnldfGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLFRKHPQSEL 150
Cdd:cd17649 2 DAVALVFGDQSLSYAELDARANRLAHRLRAL-----GVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 151 EYIISDSQSSLLVAGHPyagtleplalklglpcltlpptsnlgtldgtdtqekeaaitdwaDRPAMIIYTSGTTGRPKGV 230
Cdd:cd17649 77 RYMLEDSGAGLLLTHHP--------------------------------------------RQLAYVIYTSGSTGTPKGV 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 231 LHMHSNIQAMVQGLVSEWAWTRDDVILHTLPLhHVHGIVNKLLCPLWVGATCVMLPEFQPQKVWEMLLSSKAPMVNVfMA 310
Cdd:cd17649 113 AVSHGPLAAHCQATAERYGLTPGDRELQFASF-NFDGAHEQLLPPLICGACVVLRPDELWASADELAEMVRELGVTV-LD 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 311 VPTIY-SKLIQYYDQHFTQPHVkdfvravckeRIRLMVSGSAALPLPTLQRWEEItGHTLLERYGMTEigmALSNPL--- 386
Cdd:cd17649 191 LPPAYlQQLAEEADRTGDGRPP----------SLRLYIFGGEALSPELLRRWLKA-PVRLFNAYGPTE---ATVTPLvwk 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 387 -------KGPRIPgaVGSPLPRVEVRIvmnnttnttivLGDHRNtrvcPGLEGKEGELLVRGPSVFKEYWNKPQETRESF 459
Cdd:cd17649 257 ceagaarAGASMP--IGRPLGGRSAYI-----------LDADLN----PVPVGVTGELYIGGEGLARGYLGRPELTAERF 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 460 I---DGG----WFKTGDTVVYK-DGVYWIMGRssVD-IIKSAGYKISALEVERHLLAHPDIIDVAVIgAPDAIWGQKVTA 530
Cdd:cd17649 320 VpdpFGApgsrLYRTGDLARWRdDGVIEYLGR--VDhQVKIRGFRIELGEIEAALLEHPGVREAAVV-ALDGAGGKQLVA 396
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1250165799 531 VVQLRKG--QSMTLPDLKTWAREHMAPYTIPTGLLLVEEMPRNQMGKVNKKDL 581
Cdd:cd17649 397 YVVLRAAaaQPELRAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKAL 449
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
219-578 |
3.91e-41 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 156.65 E-value: 3.91e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 219 YTSGTTGRPKGVLHMHSNIQAMVQGLVSEWAWTRDDVILHTLPLHHVHGivnklLCPLW----VGATCVMLPEFQPQKVW 294
Cdd:PRK08162 189 YTSGTTGNPKGVVYHHRGAYLNALSNILAWGMPKHPVYLWTLPMFHCNG-----WCFPWtvaaRAGTNVCLRKVDPKLIF 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 295 EMLLSSKapmVNVFMAVPTIYSKLIqyydqhftqpHVKDFVRAVCKERIRLMVSGsAALPLPTLQRWEEItGHTLLERYG 374
Cdd:PRK08162 264 DLIREHG---VTHYCGAPIVLSALI----------NAPAEWRAGIDHPVHAMVAG-AAPPAAVIAKMEEI-GFDLTHVYG 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 375 MTEI-GMALSNPLKGP----------RIPGAVGSPLPRVEVRIVMNNTTNTTiVLGDHRNTrvcpglegkeGELLVRGPS 443
Cdd:PRK08162 329 LTETyGPATVCAWQPEwdalplderaQLKARQGVRYPLQEGVTVLDPDTMQP-VPADGETI----------GEIMFRGNI 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 444 VFKEYWNKPQETRESFiDGGWFKTGD-TVVYKDGVYWIMGRSSvDIIKSAGYKISALEVERHLLAHPDIIDVAVIGAPDA 522
Cdd:PRK08162 398 VMKGYLKNPKATEEAF-AGGWFHTGDlAVLHPDGYIKIKDRSK-DIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDP 475
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1250165799 523 IWGQKVTAVVQLRKGQSMTLPDLKTWAREHMAPYTIPTGLLLvEEMPRNQMGKVNK 578
Cdd:PRK08162 476 KWGEVPCAFVELKDGASATEEEIIAHCREHLAGFKVPKAVVF-GELPKTSTGKIQK 530
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
214-578 |
5.67e-41 |
|
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: 151.64 E-value: 5.67e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 214 PAMIIYTSGTTGRPKGVLHMHSNIQAMVQGLVSE-WAWTRDDVILHTLPLHHVHGIVNKLLCpLWVGATCVMLPEFQPQK 292
Cdd:cd17635 3 PLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEgLNWVVGDVTYLPLPATHIGGLWWILTC-LIHGGLCVTGGENTTYK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 293 -VWEMLLSSKapmVNVFMAVPTIYSKLIQYYdqhftqphvKDFVRAVckERIRLMVSGSAaLPLPTLQRWEEITGHT-LL 370
Cdd:cd17635 82 sLFKILTTNA---VTTTCLVPTLLSKLVSEL---------KSANATV--PSLRLIGYGGS-RAIAADVRFIEATGLTnTA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 371 ERYGMTEIGMALSNPL-KGPRIPGAVGSPLPRVEVRIVmnnttnttivlgdhrNTRVCPGLEGKEGELLVRGPSVFKEYW 449
Cdd:cd17635 147 QVYGLSETGTALCLPTdDDSIEINAVGRPYPGVDVYLA---------------ATDGIAGPSASFGTIWIKSPANMLGYW 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 450 NKPQETRESFIDGgWFKTGDTV-VYKDGVYWIMGRSSVDIIKsAGYKISALEVERHLLAHPDIIDVAVIGAPDAIWGQKV 528
Cdd:cd17635 212 NNPERTAEVLIDG-WVNTGDLGeRREDGFLFITGRSSESINC-GGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELV 289
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1250165799 529 -TAVVQLRKGQSMTLPDLKTWAREHMAPYTIPTGLLLVEEMPRNQMGKVNK 578
Cdd:cd17635 290 gLAVVASAELDENAIRALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
65-581 |
5.93e-41 |
|
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: 155.19 E-value: 5.93e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 65 RAPafgDKPAIIDSSGSHSYKQLYCSSLGLAGRISTAlnldfGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLFRK 144
Cdd:cd17651 7 RTP---DAPALVAEGRRLTYAELDRRANRLAHRLRAR-----GVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 145 HPQSELEYIISDSQSSLLVAGHPYAGTLEPlalKLGLPCLTLPPtsnlGTLDGTDTqEKEAAITdwADRPAMIIYTSGTT 224
Cdd:cd17651 79 YPAERLAFMLADAGPVLVLTHPALAGELAV---ELVAVTLLDQP----GAAAGADA-EPDPALD--ADDLAYVIYTSGST 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 225 GRPKGVLHMHSNIQAMVQGLVSEWAWTRDDVILHTLPLH---HVHGIVNKLLCplwvGATCVMLPE---FQPQKVWEMLl 298
Cdd:cd17651 149 GRPKGVVMPHRSLANLVAWQARASSLGPGARTLQFAGLGfdvSVQEIFSTLCA----GATLVLPPEevrTDPPALAAWL- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 299 sSKAPMVNVFMavPTIYSK-LIQYYDQHFTQPhvkdfvravckERIRLMVSGSAALPL-PTLQRW-EEITGHTLLERYGM 375
Cdd:cd17651 224 -DEQRISRVFL--PTVALRaLAEHGRPLGVRL-----------AALRYLLTGGEQLVLtEDLREFcAGLPGLRLHNHYGP 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 376 TE----IGMALSNPLKGPRIPGAVGSPLPRVEVRivmnnttnttiVLGDHRntRVCPGleGKEGELLVRGPSVFKEYWNK 451
Cdd:cd17651 290 TEthvvTALSLPGDPAAWPAPPPIGRPIDNTRVY-----------VLDAAL--RPVPP--GVPGELYIGGAGLARGYLNR 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 452 PQETRESFIDGGW------FKTGDTVVY-KDGVYWIMGRSSvDIIKSAGYKISALEVERHLLAHPDIIDVAVIGAPDAIW 524
Cdd:cd17651 355 PELTAERFVPDPFvpgarmYRTGDLARWlPDGELEFLGRAD-DQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPG 433
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1250165799 525 GQKVTAVVQLRKGQSMTLPDLKTWAREHMAPYTIPTGLLLVEEMPRNQMGKVNKKDL 581
Cdd:cd17651 434 EKRLVAYVVGDPEAPVDAAELRAALATHLPEYMVPSAFVLLDALPLTPNGKLDRRAL 490
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
63-581 |
7.52e-41 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 155.86 E-value: 7.52e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 63 FVRAPAFG-----DKPAIIDSSGSHSYKQLYCSSLGLAGRISTAlnldfGGLEGKRISFLCANDASYTVAQWAAWMSGGT 137
Cdd:PRK07788 51 FAGLVAHAarrapDRAALIDERGTLTYAELDEQSNALARGLLAL-----GVRAGDGVAVLARNHRGFVLALYAAGKVGAR 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 138 AVPL---FRKhPQseLEYIISDSQSSLLVAGHPYAGTLEPLALKLGLpCLTL--------PPTSNLGTLDG-TDTQEKEA 205
Cdd:PRK07788 126 IILLntgFSG-PQ--LAEVAAREGVKALVYDDEFTDLLSALPPDLGR-LRAWggnpdddePSGSTDETLDDlIAGSSTAP 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 206 AITdWADRPAMIIYTSGTTGRPKGVLHMHSNIQAMVQGLVSEWAWTRDDVILHTLPLHHVHGIVNKLLCpLWVGATCVML 285
Cdd:PRK07788 202 LPK-PPKPGGIVILTSGTTGTPKGAPRPEPSPLAPLAGLLSRVPFRAGETTLLPAPMFHATGWAHLTLA-MALGSTVVLR 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 286 PEFQPQKVWEMLLSSKAPMVnvfMAVPTIYSKLIQYYDQHFTQPHVKdfvravckeRIRLMVSGSAALPLPTLQRWEEIT 365
Cdd:PRK07788 280 RRFDPEATLEDIAKHKATAL---VVVPVMLSRILDLGPEVLAKYDTS---------SLKIIFVSGSALSPELATRALEAF 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 366 GHTLLERYGMTEIGMA-LSNPLKGPRIPGAVGSPLPRVEVRIvmnnttnttivLGDHRNtrvcPGLEGKEGELLVRGPSV 444
Cdd:PRK07788 348 GPVLYNLYGSTEVAFAtIATPEDLAEAPGTVGRPPKGVTVKI-----------LDENGN----EVPRGVVGRIFVGNGFP 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 445 FKEYWNkpqeTRESFIDGGWFKTGDtVVYKD--GVYWIMGRSSvDIIKSAGYKISALEVERHLLAHPDIIDVAVIGAPDA 522
Cdd:PRK07788 413 FEGYTD----GRDKQIIDGLLSSGD-VGYFDedGLLFVDGRDD-DMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDE 486
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1250165799 523 IWGQKVTAVVQLRKGQSMTLPDLKTWAREHMAPYTIPTGLLLVEEMPRNQMGKVNKKDL 581
Cdd:PRK07788 487 EFGQRLRAFVVKAPGAALDEDAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKREL 545
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
62-581 |
2.13e-40 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 154.37 E-value: 2.13e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 62 VFVRAPAFGDKPAIIDSSGSHSYKqlYCSSLGLAGRISTALNlDFGGLEGKRISFLCANDASYTVAQWAAWMSGG---TA 138
Cdd:PLN02246 29 CFERLSEFSDRPCLIDGATGRVYT--YADVELLSRRVAAGLH-KLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAvttTA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 139 VPLFRKHpqsELEYIISDSQSSLLVAGHPYAGTLEPLALKLGLPCLTL--PPTSNLGTLDGTDTQEKEAAITDWA-DRPA 215
Cdd:PLN02246 106 NPFYTPA---EIAKQAKASGAKLIITQSCYVDKLKGLAEDDGVTVVTIddPPEGCLHFSELTQADENELPEVEISpDDVV 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 216 MIIYTSGTTGRPKGVLHMH----SNIQAMVQGLVSEWAWTRDDVILHTLPLHHVHGIVNKLLCPLWVGATCVMLPEFQPQ 291
Cdd:PLN02246 183 ALPYSSGTTGLPKGVMLTHkglvTSVAQQVDGENPNLYFHSDDVILCVLPMFHIYSLNSVLLCGLRVGAAILIMPKFEIG 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 292 KVWEMLLSSKapmVNVFMAVPTIYSKLIQyydqhftQPHVKDFVRAvckeRIRLMVSGSAalPL-PTLQR--WEEITGHT 368
Cdd:PLN02246 263 ALLELIQRHK---VTIAPFVPPIVLAIAK-------SPVVEKYDLS----SIRMVLSGAA--PLgKELEDafRAKLPNAV 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 369 LLERYGMTEIGMALS-------NPLkgPRIPGAVGSPLPRVEVRIVmnnTTNTTIVLGdhRNtrvcpglegKEGELLVRG 441
Cdd:PLN02246 327 LGQGYGMTEAGPVLAmclafakEPF--PVKSGSCGTVVRNAELKIV---DPETGASLP--RN---------QPGEICIRG 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 442 PSVFKEYWNKPQETRESFIDGGWFKTGDT-VVYKDGVYWIMGRSSvDIIKSAGYKISALEVERHLLAHPDIIDVAVIGAP 520
Cdd:PLN02246 391 PQIMKGYLNDPEATANTIDKDGWLHTGDIgYIDDDDELFIVDRLK-ELIKYKGFQVAPAELEALLISHPSIADAAVVPMK 469
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1250165799 521 DAIWGQKVTAVVQLRKGQSMTLPDLKTWAREHMAPYTIPTGLLLVEEMPRNQMGKVNKKDL 581
Cdd:PLN02246 470 DEVAGEVPVAFVVRSNGSEITEDEIKQFVAKQVVFYKRIHKVFFVDSIPKAPSGKILRKDL 530
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
65-583 |
2.22e-40 |
|
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: 157.71 E-value: 2.22e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 65 RAPafgDKPAIIDSSGSHSYKQLYCSSLGLAGRIstalnLDFGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLFRK 144
Cdd:COG1020 488 RTP---DAVAVVFGDQSLTYAELNARANRLAHHL-----RALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPA 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 145 HPQSELEYIISDSQSSLLVAGHPYAGTLEPLalklGLPCLTLpptsNLGTLDGTDTQEKEAAITdwADRPAMIIYTSGTT 224
Cdd:COG1020 560 YPAERLAYMLEDAGARLVLTQSALAARLPEL----GVPVLAL----DALALAAEPATNPPVPVT--PDDLAYVIYTSGST 629
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 225 GRPKGVLHMHSNIQAMVQGLVSEWAWTRDDVILHTLPLHH---VHGIvnklLCPLWVGATCVMLPE---FQPQKVWEMLL 298
Cdd:COG1020 630 GRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFASLSFdasVWEI----FGALLSGATLVLAPPearRDPAALAELLA 705
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 299 SSKapmVNVFMAVPTIYSKLIQYYDQHFTqphvkdfvravckeRIRLMVSGSAALPLPTLQRWEEITGHT-LLERYGMTE 377
Cdd:COG1020 706 RHR---VTVLNLTPSLLRALLDAAPEALP--------------SLRLVLVGGEALPPELVRRWRARLPGArLVNLYGPTE 768
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 378 ------IGMALSNPLKGPRIPgaVGSPLPRVEVRivmnnttnttiVLGDHRntRVCPglEGKEGELLVRGPSVFKEYWNK 451
Cdd:COG1020 769 ttvdstYYEVTPPDADGGSVP--IGRPIANTRVY-----------VLDAHL--QPVP--VGVPGELYIGGAGLARGYLNR 831
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 452 PQETRESFI------DGG-WFKTGDTVVY-KDGVYWIMGRSSvDIIKSAGYKISALEVERHLLAHPDIIDVAVIGAPDAI 523
Cdd:COG1020 832 PELTAERFVadpfgfPGArLYRTGDLARWlPDGNLEFLGRAD-DQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDAP 910
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 524 WGQKVTAVVQLRKGQSMTLPDLKTWAREHMAPYTIPTGLLLVEEMPRNQMGKVNKKDLLR 583
Cdd:COG1020 911 GDKRLVAYVVPEAGAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALPA 970
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
147-578 |
3.45e-40 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 154.20 E-value: 3.45e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 147 QSELEYIISDSQSSLLVA-----GHPYAGTLEPLALKLG-----------LPCLT------------LPPTSNLGTLDGT 198
Cdd:PRK08315 104 LSELEYALNQSGCKALIAadgfkDSDYVAMLYELAPELAtcepgqlqsarLPELRrviflgdekhpgMLNFDELLALGRA 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 199 DTQEKEAAITDW--ADRPAMIIYTSGTTGRPKGVLHMHSNIQ------AMVQGLvsewawTRDDVILHTLPLHHVHGIVN 270
Cdd:PRK08315 184 VDDAELAARQATldPDDPINIQYTSGTTGFPKGATLTHRNILnngyfiGEAMKL------TEEDRLCIPVPLYHCFGMVL 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 271 KLLCPLWVGATCV-MLPEFQPQKVWEMLLSSKAPMVNvfmAVPTIYsklIQYYDQhftqPHVKDF----VR------AVC 339
Cdd:PRK08315 258 GNLACVTHGATMVyPGEGFDPLATLAAVEEERCTALY---GVPTMF---IAELDH----PDFARFdlssLRtgimagSPC 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 340 kerirlmvsgsaalPLPTLQR------WEEITghtllERYGMTEI--GMALSN---PLKgpRIPGAVGSPLPRVEVRIVm 408
Cdd:PRK08315 328 --------------PIEVMKRvidkmhMSEVT-----IAYGMTETspVSTQTRtddPLE--KRVTTVGRALPHLEVKIV- 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 409 nnttnttivlgDHRNTRVCPglEGKEGELLVRGPSVFKEYWNKPQETRESFIDGGWFKTGD-TVVYKDGVYWIMGRSSvD 487
Cdd:PRK08315 386 -----------DPETGETVP--RGEQGELCTRGYSVMKGYWNDPEKTAEAIDADGWMHTGDlAVMDEEGYVNIVGRIK-D 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 488 IIKSAGYKISALEVERHLLAHPDIIDVAVIGAPDAIWGQKVTAVVQLRKGQSMTLPDLKTWAREHMAPYTIPTGLLLVEE 567
Cdd:PRK08315 452 MIIRGGENIYPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRPGATLTEEDVRDFCRGKIAHYKIPRYIRFVDE 531
|
490
....*....|.
gi 1250165799 568 MPRNQMGKVNK 578
Cdd:PRK08315 532 FPMTVTGKIQK 542
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
212-581 |
4.32e-40 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 153.88 E-value: 4.32e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 212 DRPAMIIYTSGTTGRPKGVLHMHSNIQAMVQGlVSEWAWTRD------DVILHTLPLHHVHGIVNKLLCPLWVGAtCVML 285
Cdd:PRK08751 208 DDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQ-AHQWLAGTGkleegcEVVITALPLYHIFALTANGLVFMKIGG-CNHL 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 286 ---PEFQPQKVWEMllssKAPMVNVFMAVPTIYSKLIQY--YDQhftqphvKDFvravckERIRLMVSGSAALPLPTLQR 360
Cdd:PRK08751 286 isnPRDMPGFVKEL----KKTRFTAFTGVNTLFNGLLNTpgFDQ-------IDF------SSLKMTLGGGMAVQRSVAER 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 361 WEEITGHTLLERYGMTEIG-MALSNPLKGPRIPGAVGSPLPRVEVRIvmNNTTNTTIVLGDHrntrvcpglegkeGELLV 439
Cdd:PRK08751 349 WKQVTGLTLVEAYGLTETSpAACINPLTLKEYNGSIGLPIPSTDACI--KDDAGTVLAIGEI-------------GELCI 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 440 RGPSVFKEYWNKPQETRESFIDGGWFKTGDTV-VYKDGVYWIMGRSSvDIIKSAGYKISALEVERHLLAHPDIIDVAVIG 518
Cdd:PRK08751 414 KGPQVMKGYWKRPEETAKVMDADGWLHTGDIArMDEQGFVYIVDRKK-DMILVSGFNVYPNEIEDVIAMMPGVLEVAAVG 492
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1250165799 519 APDAIWGQKVTAVVqLRKGQSMTLPDLKTWAREHMAPYTIPTGLLLVEEMPRNQMGKVNKKDL 581
Cdd:PRK08751 493 VPDEKSGEIVKVVI-VKKDPALTAEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRREL 554
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
212-578 |
1.57e-39 |
|
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: 151.88 E-value: 1.57e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 212 DRPAMIIYTSGTTGRPKGVLHMHS-NIQAMVQGlvSEWAWTRDDVILHTLPLHHVHGIVNKLLCPLWVGATCVML---PE 287
Cdd:cd05970 185 EDILLVYFSSGTTGMPKMVEHDFTyPLGHIVTA--KYWQNVREGGLHLTVADTGWGKAVWGKIYGQWIAGAAVFVydyDK 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 288 FQPQKVWEMLLSSKapmVNVFMAVPTIYSKLIQYYDQHFtqphvkDFvravckERIRLMVSGSAALPLPTLQRWEEITGH 367
Cdd:cd05970 263 FDPKALLEKLSKYG---VTTFCAPPTIYRFLIREDLSRY------DL------SSLRYCTTAGEALNPEVFNTFKEKTGI 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 368 TLLERYGMTEIGMALSN-PLKGPRiPGAVGSPLPRVEVRIVmnnttnttivlgdHRNTRVCPGleGKEGELLVR---GPS 443
Cdd:cd05970 328 KLMEGFGQTETTLTIATfPWMEPK-PGSMGKPAPGYEIDLI-------------DREGRSCEA--GEEGEIVIRtskGKP 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 444 V--FKEYWNKPQETRESFIDGgWFKTGDTV-VYKDGVYWIMGRSSvDIIKSAGYKISALEVERHLLAHPDIIDVAVIGAP 520
Cdd:cd05970 392 VglFGGYYKDAEKTAEVWHDG-YYHTGDAAwMDEDGYLWFVGRTD-DLIKSSGYRIGPFEVESALIQHPAVLECAVTGVP 469
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1250165799 521 DAIWGQKVTAVVQLRK----GQSMTlPDLKTWAREHMAPYTIPTGLLLVEEMPRNQMGKVNK 578
Cdd:cd05970 470 DPIRGQVVKATIVLAKgyepSEELK-KELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRR 530
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
214-570 |
1.73e-39 |
|
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: 147.06 E-value: 1.73e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 214 PAMIIYTSGTTGRPKGVLHMHSNIqaMVQGLVSEW--AWTRDDVILHTLPLHHVhGIVNKLLCPLWVGATCVMLPEFQPQ 291
Cdd:cd17636 2 PVLAIYTAAFSGRPNGALLSHQAL--LAQALVLAVlqAIDEGTVFLNSGPLFHI-GTLMFTLATFHAGGTNVFVRRVDAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 292 KVWEMLLSSKApmVNVFMAVPTIyskliqyyDQhftqphvkdfVRAVCKERIRLMVSGSAALPLPTlqRWEEITGHTLLE 371
Cdd:cd17636 79 EVLELIEAERC--THAFLLPPTI--------DQ----------IVELNADGLYDLSSLRSSPAAPE--WNDMATVDTSPW 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 372 R-----YGMTEI-GMALSNPLKGPRIPGAvGSPLPRVEVRIVmnnttnttivlgDHRNTRVCPGlegKEGELLVRGPSVF 445
Cdd:cd17636 137 GrkpggYGQTEVmGLATFAALGGGAIGGA-GRPSPLVQVRIL------------DEDGREVPDG---EVGEIVARGPTVM 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 446 KEYWNKPQETRESFIdGGWFKTGDtvvykdgvywiMGRSSVD-----------IIKSAGYKISALEVERHLLAHPDIIDV 514
Cdd:cd17636 201 AGYWNRPEVNARRTR-GGWHHTND-----------LGRREPDgslsfvgpktrMIKSGAENIYPAEVERCLRQHPAVADA 268
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1250165799 515 AVIGAPDAIWGQKVTAVVQLRKGQSMTLPDLKTWAREHMAPYTIPTGLLLVEEMPR 570
Cdd:cd17636 269 AVIGVPDPRWAQSVKAIVVLKPGASVTEAELIEHCRARIASYKKPKSVEFADALPR 324
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
210-576 |
2.08e-39 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 151.97 E-value: 2.08e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 210 WADRPAMII--YTSGTTGRPKGVLHMHsniQAMVQGLVS-EWA--WTRDDVILHTLPLHHVHGIVNKLLCPLWVGATCVM 284
Cdd:PRK04319 201 WTDREDGAIlhYTSGSTGKPKGVLHVH---NAMLQHYQTgKYVldLHEDDVYWCTADPGWVTGTSYGIFAPWLNGATNVI 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 285 L-PEFQPQKVWEMLLSSKapmVNVFMAVPTIYSKLIQYYDQHFTQ---PHVKdFVRAVCKerirlmvsgsaalPL-PTLQ 359
Cdd:PRK04319 278 DgGRFSPERWYRILEDYK---VTVWYTAPTAIRMLMGAGDDLVKKydlSSLR-HILSVGE-------------PLnPEVV 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 360 RW-EEITGHTLLERYGMTEIGMAL-----SNPLKgpriPGAVGSPLPRVEVRIVMNNttnttivlGDhrntrvcpGLE-G 432
Cdd:PRK04319 341 RWgMKVFGLPIHDNWWMTETGGIMianypAMDIK----PGSMGKPLPGIEAAIVDDQ--------GN--------ELPpN 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 433 KEGELLVRG--PSVFKEYWNKPQETRESFIdGGWFKTGDtVVYKD--GVYWIMGRSSvDIIKSAGYKISALEVERHLLAH 508
Cdd:PRK04319 401 RMGNLAIKKgwPSMMRGIWNNPEKYESYFA-GDWYVSGD-SAYMDedGYFWFQGRVD-DVIKTSGERVGPFEVESKLMEH 477
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1250165799 509 PDIIDVAVIGAPDAIWGQKVTAVVQLRKG--QSMTLP-DLKTWAREHMAPYTIPTGLLLVEEMPRNQMGKV 576
Cdd:PRK04319 478 PAVAEAGVIGKPDPVRGEIIKAFVALRPGyePSEELKeEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKI 548
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
65-581 |
3.47e-39 |
|
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: 150.12 E-value: 3.47e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 65 RAPAFGDKPAIIDSSGSHSYKQLYCSSLGLAGRISTAlnldfGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLFRK 144
Cdd:cd17646 7 QAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRAR-----GVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 145 HPQSELEYIISDSQSSLLVAGhpyAGTLEPLAlklGLPCLTLPPTSNLGTLDGTDTQEKEAAitdwaDRPAMIIYTSGTT 224
Cdd:cd17646 82 YPADRLAYMLADAGPAVVLTT---ADLAARLP---AGGDVALLGDEALAAPPATPPLVPPRP-----DNLAYVIYTSGST 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 225 GRPKGVLHMHSNIQAMVQGLVSEWAWTRDDVILHTLPLhhvhGI---VNKLLCPLWVGATCVML-PEFQpqkvwemllss 300
Cdd:cd17646 151 GRPKGVMVTHAGIVNRLLWMQDEYPLGPGDRVLQKTPL----SFdvsVWELFWPLVAGARLVVArPGGH----------- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 301 kapmvnvfmAVPTIYSKLIQYYD---QHFTQPHVKDFVRAVCKER---IRLMVSGSAALPLPTLQRWEEITGHTLLERYG 374
Cdd:cd17646 216 ---------RDPAYLAALIREHGvttCHFVPSMLRVFLAEPAAGScasLRRVFCSGEALPPELAARFLALPGAELHNLYG 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 375 MTE--IGM---ALSNPLKGPRIPgaVGSPLPRVEVRivmnnttnttiVLGDHrnTRVCPglEGKEGELLVRGPSVFKEYW 449
Cdd:cd17646 287 PTEaaIDVthwPVRGPAETPSVP--IGRPVPNTRLY-----------VLDDA--LRPVP--VGVPGELYLGGVQLARGYL 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 450 NKPQETRESFI-----DGG-WFKTGDTVVYK-DGVYWIMGRSSvDIIKSAGYKISALEVERHLLAHPDIIDVAVIGAPDA 522
Cdd:cd17646 350 GRPALTAERFVpdpfgPGSrMYRTGDLARWRpDGALEFLGRSD-DQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAP 428
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 523 IWGQKVTAVVQLRKGQSMTLPD-LKTWAREHMAPYTIPTGLLLVEEMPRNQMGKVNKKDL 581
Cdd:cd17646 429 AGAARLVGYVVPAAGAAGPDTAaLRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
101-519 |
7.32e-39 |
|
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: 149.54 E-value: 7.32e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 101 ALNLDfgglEGKRISFLCANDASYTVAQWAAWMSGGTAVPLFRKHPQSELEYIISDSQSSLLVAGHPYAGTLEPLALKLG 180
Cdd:cd05932 25 ALGLE----PGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFVGKLDDWKAMAPGVPEG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 181 LPCLTLPPTSNLGTLDGTDT-----QEKEAAITDWADRPAMIIYTSGTTGRPKGVLHMHSNIQAMVQGLVSEWAWTRDDV 255
Cdd:cd05932 101 LISISLPPPSAANCQYQWDDliaqhPPLEERPTRFPEQLATLIYTSGTTGQPKGVMLTFGSFAWAAQAGIEHIGTEENDR 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 256 ILHTLPLHHVHGIVNKLLCPLWVGATcVMLPEFQPQKVWEMllssKAPMVNVFMAVPTIYSKLIQYYDQHFTQ------- 328
Cdd:cd05932 181 MLSYLPLAHVTERVFVEGGSLYGGVL-VAFAESLDTFVEDV----QRARPTLFFSVPRLWTKFQQGVQDKIPQqklnlll 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 329 --PHVKDFV-RAVCK----ERIRLMVSGSAALPlPTLQRWEEITGHTLLERYGMTEiGMALSNPLK-GPRIPGAVGSPLP 400
Cdd:cd05932 256 kiPVVNSLVkRKVLKglglDQCRLAGCGSAPVP-PALLEWYRSLGLNILEAYGMTE-NFAYSHLNYpGRDKIGTVGNAGP 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 401 RVEVRIvmnnttnttivlgdhrntrvcpgleGKEGELLVRGPSVFKEYWNKPQETRESFIDGGWFKTGDT-VVYKDGVYW 479
Cdd:cd05932 334 GVEVRI-------------------------SEDGEILVRSPALMMGYYKDPEATAEAFTADGFLRTGDKgELDADGNLT 388
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1250165799 480 IMGRSSvDIIKSA-GYKISALEVERHLLAHPDIIDVAVIGA 519
Cdd:cd05932 389 ITGRVK-DIFKTSkGKYVAPAPIENKLAEHDRVEMVCVIGS 428
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
199-583 |
1.05e-38 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 147.66 E-value: 1.05e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 199 DTQEKEAAITDWADR------PAMIIYTSGTTGRPKGVLHMHSNIQAMVQGLVSEWAWTRDDVILHTLPLHHVHGIVNKL 272
Cdd:cd05973 69 RTSGARLVVTDAANRhkldsdPFVMMFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRPEDSFWNAADPGWAYGLYYAI 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 273 LCPLWVGATCVMLP-EFQPQKVWEMLLSSKapmVNVFMAVPTIYSKLIQyydqhftqphvkDFVRAVCKERIRLMVSGSA 351
Cdd:cd05973 149 TGPLALGHPTILLEgGFSVESTWRVIERLG---VTNLAGSPTAYRLLMA------------AGAEVPARPKGRLRRVSSA 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 352 ALPL-PTLQRWEEIT-GHTLLERYGMTEIGMALSN--PLKGPRIPGAVGSPLPRVEVrivmnnttnttIVLGDHRNTrVC 427
Cdd:cd05973 214 GEPLtPEVIRWFDAAlGVPIHDHYGQTELGMVLANhhALEHPVHAGSAGRAMPGWRV-----------AVLDDDGDE-LG 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 428 PGLEGKEGELLVRGPSV-FKEYWNKPQETresfIDGGWFKTGDTV-VYKDGVYWIMGRSSvDIIKSAGYKISALEVERHL 505
Cdd:cd05973 282 PGEPGRLAIDIANSPLMwFRGYQLPDTPA----IDGGYYLTGDTVeFDPDGSFSFIGRAD-DVITMSGYRIGPFDVESAL 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 506 LAHPDIIDVAVIGAPDAIWGQKVTAVVQLRKGQSMT--LPD-LKTWAREHMAPYTIPTGLLLVEEMPRNQMGKVnKKDLL 582
Cdd:cd05973 357 IEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHEGTpaLADeLQLHVKKRLSAHAYPRTIHFVDELPKTPSGKI-QRFLL 435
|
.
gi 1250165799 583 R 583
Cdd:cd05973 436 R 436
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
65-581 |
1.21e-38 |
|
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: 148.50 E-value: 1.21e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 65 RAPAFGDKPAIIDSSGSHSYKQLYCSSLGLAGRISTAlnldfGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLFRK 144
Cdd:cd12117 6 QAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAA-----GVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 145 HPQSELEYIISDSQSSLLVAGHPYAGTLEPLALKLglpcltlpptsnLGTLDGTDTQEKEAAITDWADRPAMIIYTSGTT 224
Cdd:cd12117 81 LPAERLAFMLADAGAKVLLTDRSLAGRAGGLEVAV------------VIDEALDAGPAGNPAVPVSPDDLAYVMYTSGST 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 225 GRPKGVLHMHSNIQAMVQGlvSEWA-WTRDDVILHTLPL------HHVHGivnkllcPLWVGATCVMLPE---FQPQKVW 294
Cdd:cd12117 149 GRPKGVAVTHRGVVRLVKN--TNYVtLGPDDRVLQTSPLafdastFEIWG-------ALLNGARLVLAPKgtlLDPDALG 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 295 EMLLSSKapmVNVFMAVPTIYSKLIQyydqhftqphvkdfVRAVCKERIRLMVSGSAALPLPTLQRWEEITGH-TLLERY 373
Cdd:cd12117 220 ALIAEEG---VTVLWLTAALFNQLAD--------------EDPECFAGLRELLTGGEVVSPPHVRRVLAACPGlRLVNGY 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 374 GMTE-IGMALSNPLK-----GPRIPgaVGSPLPrvevrivmnnttNTTI-VLGDHRntRVCPglEGKEGELLVRGPSVFK 446
Cdd:cd12117 283 GPTEnTTFTTSHVVTeldevAGSIP--IGRPIA------------NTRVyVLDEDG--RPVP--PGVPGELYVGGDGLAL 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 447 EYWNKPQETRESFI-----DGG-WFKTGDTVVYK-DGVYWIMGRSSvDIIKSAGYKISALEVERHLLAHPDIIDVAVIGA 519
Cdd:cd12117 345 GYLNRPALTAERFVadpfgPGErLYRTGDLARWLpDGRLEFLGRID-DQVKIRGFRIELGEIEAALRAHPGVREAVVVVR 423
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1250165799 520 PDAIWGQKVTAVVqlRKGQSMTLPDLKTWAREHMAPYTIPTGLLLVEEMPRNQMGKVNKKDL 581
Cdd:cd12117 424 EDAGGDKRLVAYV--VAEGALDAAELRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
83-518 |
1.75e-38 |
|
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: 147.51 E-value: 1.75e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 83 SYKQLYCSSLglagRISTALnLDFGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLFRKHPQSELEYIISDSQSSLL 162
Cdd:cd17640 7 TYKDLYQEIL----DFAAGL-RSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 163 VaghpyagtLEplalklglpcltlpptsNlgtlDGTDTqekeaaitdwadrpAMIIYTSGTTGRPKGV-------LHMHS 235
Cdd:cd17640 82 V--------VE-----------------N----DSDDL--------------ATIIYTSGTTGNPKGVmlthanlLHQIR 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 236 NIQAMVQGLVSewawtrdDVILHTLPLHHVHGIVNKLLCPLWvGATCVM---------LPEFQPQkvwemllsskapmvn 306
Cdd:cd17640 119 SLSDIVPPQPG-------DRFLSILPIWHSYERSAEYFIFAC-GCSQAYtsirtlkddLKRVKPH--------------- 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 307 VFMAVPTIYSKLIQ-YYDQHFTQPHVKDFV--RAVCKERIRLMVSGSAALPlPTLQRWEEITGHTLLERYGMTEIGMALS 383
Cdd:cd17640 176 YIVSVPRLWESLYSgIQKQVSKSSPIKQFLflFFLSGGIFKFGISGGGALP-PHVDTFFEAIGIEVLNGYGLTETSPVVS 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 384 -NPLKGPrIPGAVGSPLPRVEVRIVmnnttnttivlgDHRNTRVCPglEGKEGELLVRGPSVFKEYWNKPQETRESFIDG 462
Cdd:cd17640 255 aRRLKCN-VRGSVGRPLPGTEIKIV------------DPEGNVVLP--PGEKGIVWVRGPQVMKGYYKNPEATSKVLDSD 319
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1250165799 463 GWFKTGDTV-VYKDGVYWIMGRSSVDIIKSAGYKISALEVERHLLAHPDIIDVAVIG 518
Cdd:cd17640 320 GWFNTGDLGwLTCGGELVLTGRAKDTIVLSNGENVEPQPIEEALMRSPFIEQIMVVG 376
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
69-581 |
2.42e-38 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 148.63 E-value: 2.42e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 69 FGDKPAIIDSSGSHSYKQLycsslglaGRISTALN--LDFGGLE-GKRISFLCANDASYTVAQWAAWMSGGTAV---PLF 142
Cdd:PRK07059 36 YADRPAFICMGKAITYGEL--------DELSRALAawLQSRGLAkGARVAIMMPNVLQYPVAIAAVLRAGYVVVnvnPLY 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 143 RKHpqsELEYIISDSQSSLLVAGHPYAGTLEPL----ALK----------LGL----------------PCLTLPPTSNL 192
Cdd:PRK07059 108 TPR---ELEHQLKDSGAEAIVVLENFATTVQQVlaktAVKhvvvasmgdlLGFkghivnfvvrrvkkmvPAWSLPGHVRF 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 193 GTLDGTDTQEKEAAITDWADRPAMIIYTSGTTGRPKGVLHMHSNIQAMVqgLVSEwAW--------TRDD--VILHTLPL 262
Cdd:PRK07059 185 NDALAEGARQTFKPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANV--LQME-AWlqpafekkPRPDqlNFVCALPL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 263 HHVHGI-VNKLLcPLWVGATCVMLPefQPQKVWEMLLSSKAPMVNVFMAVPTIYSKLIQYYDqhFTQphvKDFvravckE 341
Cdd:PRK07059 262 YHIFALtVCGLL-GMRTGGRNILIP--NPRDIPGFIKELKKYQVHIFPAVNTLYNALLNNPD--FDK---LDF------S 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 342 RIRLMVSGSAALPLPTLQRWEEITGHTLLERYGMTEIG-MALSNPLKGPRIPGAVGSPLPRVEVRIVMNNTTNTTIvlgd 420
Cdd:PRK07059 328 KLIVANGGGMAVQRPVAERWLEMTGCPITEGYGLSETSpVATCNPVDATEFSGTIGLPLPSTEVSIRDDDGNDLPL---- 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 421 hrntrvcpgleGKEGELLVRGPSVFKEYWNKPQETRESFIDGGWFKTGDT-VVYKDGVYWIMGRSSvDIIKSAGYKISAL 499
Cdd:PRK07059 404 -----------GEPGEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVgVMDERGYTKIVDRKK-DMILVSGFNVYPN 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 500 EVERHLLAHPDIIDVAVIGAPDAIWGQKVTAVVqLRKGQSMTLPDLKTWAREHMAPYTIPTGLLLVEEMPRNQMGKVNKK 579
Cdd:PRK07059 472 EIEEVVASHPGVLEVAAVGVPDEHSGEAVKLFV-VKKDPALTEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRR 550
|
..
gi 1250165799 580 DL 581
Cdd:PRK07059 551 EL 552
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
134-581 |
4.29e-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: 144.01 E-value: 4.29e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 134 SGGTAVPLFRKHPQSELEYIISDSQSSLLVAGHPYAgtleplalklglpcltlPPTSNLGT---LDGTDTQEKEA---AI 207
Cdd:cd17655 70 AGGAYLPIDPDYPEERIQYILEDSGADILLTQSHLQ-----------------PPIAFIGLidlLDEDTIYHEESenlEP 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 208 TDWADRPAMIIYTSGTTGRPKGVLHMHSNIQAMVQGLVSEWAWTRDDVILHTLPLH---HVHGIVNKLLCplwvGATCVM 284
Cdd:cd17655 133 VSKSDDLAYVIYTSGSTGKPKGVMIEHRGVVNLVEWANKVIYQGEHLRVALFASISfdaSVTEIFASLLS----GNTLYI 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 285 LPefqpqkvwemllssKAPMVNVfmavptiySKLIQYYDQH------FTQPHVK--DFVRAVCKERIRLMVSGSAALPLP 356
Cdd:cd17655 209 VR--------------KETVLDG--------QALTQYIRQNritiidLTPAHLKllDAADDSEGLSLKHLIVGGEALSTE 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 357 TLQRWEEITGH--TLLERYGMTE------IGMALSNPLKGPRIPgaVGSPLprvevrivmnntTNTTIVLGDhRNTRVCP 428
Cdd:cd17655 267 LAKKIIELFGTnpTITNAYGPTEttvdasIYQYEPETDQQVSVP--IGKPL------------GNTRIYILD-QYGRPQP 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 429 glEGKEGELLVRGPSVFKEYWNKPQETRESFID------GGWFKTGDTVVY-KDGVYWIMGRSSvDIIKSAGYKISALEV 501
Cdd:cd17655 332 --VGVAGELYIGGEGVARGYLNRPELTAEKFVDdpfvpgERMYRTGDLARWlPDGNIEFLGRID-HQVKIRGYRIELGEI 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 502 ERHLLAHPDIIDVAVIGAPDAIWGQKVTAVVQLRKgqSMTLPDLKTWAREHMAPYTIPTGLLLVEEMPRNQMGKVNKKDL 581
Cdd:cd17655 409 EARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEK--ELPVAQLREFLARELPDYMIPSYFIKLDEIPLTPNGKVDRKAL 486
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
213-576 |
4.59e-37 |
|
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: 140.23 E-value: 4.59e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 213 RPAMIIYTSGTTGRPKGVLHMH-SNIQAMVQGlVSEWAWTRDDVILHTLPLHHVHGIvNKLLCPLWVGATCVMLPEFQPQ 291
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRSErSWIESFVCN-EDLFNISGEDAILAPGPLSHSLFL-YGAISALYLGGTFIGQRKFNPK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 292 KVWEMLLSSKApmVNVFMaVPTIYSKLIQYYdqhftQPHVKdfvravckerIRLMVSGSAALPLPTLQRWEEITGHT-LL 370
Cdd:cd17633 79 SWIRKINQYNA--TVIYL-VPTMLQALARTL-----EPESK----------IKSIFSSGQKLFESTKKKLKNIFPKAnLI 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 371 ERYGMTEIGMALSNPLKGPRIPGAVGSPLPRVEVRIvmnnttnttivlgdhRNTRvcpglEGKEGELLVRGPSVFKEYwn 450
Cdd:cd17633 141 EFYGTSELSFITYNFNQESRPPNSVGRPFPNVEIEI---------------RNAD-----GGEIGKIFVKSEMVFSGY-- 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 451 kpqeTRESFID-GGWFKTGDTVVYK-DGVYWIMGRSSvDIIKSAGYKISALEVERHLLAHPDIIDVAVIGAPDAIWGQKV 528
Cdd:cd17633 199 ----VRGGFSNpDGWMSVGDIGYVDeEGYLYLVGRES-DMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIA 273
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1250165799 529 TAVVqlrKGQSMTLPDLKTWAREHMAPYTIPTGLLLVEEMPRNQMGKV 576
Cdd:cd17633 274 VALY---SGDKLTYKQLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKI 318
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
65-576 |
4.75e-37 |
|
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: 145.07 E-value: 4.75e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 65 RAPAFGDKPAII------DSSGSHSYKQLYCSSLGLAGRISTAlnldfgGLEGKRISFLCANDASYTVAQWAAWMSGGTA 138
Cdd:cd05931 2 RAAARPDRPAYTflddegGREETLTYAELDRRARAIAARLQAV------GKPGDRVLLLAPPGLDFVAAFLGCLYAGAIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 139 VPLFRKHPQSE---LEYIISDSQSSLLVAGHPYAGTLEPLALKlglpcltlPPTSNLGTLDGTDTQEKEAAiTDW----- 210
Cdd:cd05931 76 VPLPPPTPGRHaerLAAILADAGPRVVLTTAAALAAVRAFAAS--------RPAAGTPRLLVVDLLPDTSA-ADWpppsp 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 211 -ADRPAMIIYTSGTTGRPKGVLHMHSNIQAMVQGLVSEWAWTRDDVILHTLPLHHVHGIVNKLLCPLWVGATCVMLPefq 289
Cdd:cd05931 147 dPDDIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGPSVLMS--- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 290 pqkvwemllsskaPMvnVFMAVPTIYSKLIQYYDQHFTQphVKDFVRAVCKERIR-----------LMVSGSAALPL--P 356
Cdd:cd05931 224 -------------PA--AFLRRPLRWLRLISRYRATISA--APNFAYDLCVRRVRdedlegldlssWRVALNGAEPVrpA 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 357 TLQRWEE------ITGHTLLERYGMTEIGMALSNP---------------------LKGPRIPGAV-----GSPLPRVEV 404
Cdd:cd05931 287 TLRRFAEafapfgFRPEAFRPSYGLAEATLFVSGGppgtgpvvlrvdrdalagravAVAADDPAARelvscGRPLPDQEV 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 405 RIVMNNTtnttivlgdhrnTRVCPglEGKEGELLVRGPSVFKEYWNKPQETRESFI------DGGWFKTGDTVVYKDGVY 478
Cdd:cd05931 367 RIVDPET------------GRELP--DGEVGEIWVRGPSVASGYWGRPEATAETFGalaatdEGGWLRTGDLGFLHDGEL 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 479 WIMGRSSvDIIKSAGYKISALEVERHLLAHPDIID---VAVIGAPDAIWGQKVTAVVQLRKGQSMTLPDLK-----TWAR 550
Cdd:cd05931 433 YITGRLK-DLIIVRGRNHYPQDIEATAEEAHPALRpgcVAAFSVPDDGEERLVVVAEVERGADPADLAAIAaairaAVAR 511
|
570 580
....*....|....*....|....*....
gi 1250165799 551 EH-MAPYTIptglLLVE--EMPRNQMGKV 576
Cdd:cd05931 512 EHgVAPADV----VLVRpgSIPRTSSGKI 536
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
217-577 |
1.21e-36 |
|
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: 140.21 E-value: 1.21e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 217 IIYTSGTTGRPKGVLHMHSNIQAMVQG---------LVSEWAWTR-----DDVILHTLPLHHVHGIVNKLLCPLWVGATC 282
Cdd:cd05924 8 ILYTGGTTGMPKGVMWRQEDIFRMLMGgadfgtgefTPSEDAHKAaaaaaGTVMFPAPPLMHGTGSWTAFGGLLGGQTVV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 283 VMLPEFQPQKVWEMLLSSKA---PMVNVFMAVPTIyskliqyydQHFTQPHVKDFvravckERIRLMVSGSAALPLPTLQ 359
Cdd:cd05924 88 LPDDRFDPEEVWRTIEKHKVtsmTIVGDAMARPLI---------DALRDAGPYDL------SSLFAISSGGALLSPEVKQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 360 RWEEITGH-TLLERYGMTEIGMALSnplkgpripGAVGSPLPRVEVRIVMNNTTnttIVLGDHrnTRVCPGLEGKEGELL 438
Cdd:cd05924 153 GLLELVPNiTLVDAFGSSETGFTGS---------GHSAGSGPETGPFTRANPDT---VVLDDD--GRVVPPGSGGVGWIA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 439 VRGpSVFKEYWNKPQETRESF--IDGG-WFKTGD-TVVYKDGVYWIMGRSSVdIIKSAGYKISALEVERHLLAHPDIIDV 514
Cdd:cd05924 219 RRG-HIPLGYYGDEAKTAETFpeVDGVrYAVPGDrATVEADGTVTLLGRGSV-CINTGGEKVFPEEVEEALKSHPAVYDV 296
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1250165799 515 AVIGAPDAIWGQKVTAVVQLRKGQSMTLPDLKTWAREHMAPYTIPTGLLLVEEMPRNQMGKVN 577
Cdd:cd05924 297 LVVGRPDERWGQEVVAVVQLREGAGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGKAD 359
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
65-584 |
5.62e-36 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 141.82 E-value: 5.62e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 65 RAPafgDKPAIIDSSGSHSYKQLYCSSLGLAGRISTalnldFGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLFRK 144
Cdd:PRK13382 55 RCP---DRPGLIDELGTLTWRELDERSDALAAALQA-----LPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTS 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 145 HPQSELEYIISDSQSSLLVAGHPYAGTLePLALKlGLPCLT----LPPTSNLGTLDGTDTQEKEAAITDWADRPAMIIYT 220
Cdd:PRK13382 127 FAGPALAEVVTREGVDTVIYDEEFSATV-DRALA-DCPQATrivaWTDEDHDLTVEVLIAAHAGQRPEPTGRKGRVILLT 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 221 SGTTGRPKGVLHMHSNIQAMVQGLVSEWAWTRDDVILHTLPLHHVHGIVNkLLCPLWVGATCVMLPEFQPQKVWEMLLSS 300
Cdd:PRK13382 205 SGTTGTPKGARRSGPGGIGTLKAILDRTPWRAEEPTVIVAPMFHAWGFSQ-LVLAASLACTIVTRRRFDPEATLDLIDRH 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 301 KAPMVNVfmaVPTIYSKLIQYYDQhftqphvkdfVRAVCKER-IRLMVSGSAALPLPTLQRWEEITGHTLLERYGMTEIG 379
Cdd:PRK13382 284 RATGLAV---VPVMFDRIMDLPAE----------VRNRYSGRsLRFAAASGSRMRPDVVIAFMDQFGDVIYNNYNATEAG 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 380 M-ALSNPLKGPRIPGAVGSPLPRVEVRIVMnnttnttivlGDHRNtrvCPglEGKEGELLVRGPSVFKEYwnKPQETREs 458
Cdd:PRK13382 351 MiATATPADLRAAPDTAGRPAEGTEIRILD----------QDFRE---VP--TGEVGTIFVRNDTQFDGY--TSGSTKD- 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 459 FIDGgWFKTGDTVVYKD-GVYWIMGRSSvDIIKSAGYKISALEVERHLLAHPDIIDVAVIGAPDAIWGQKVTAVVQLRKG 537
Cdd:PRK13382 413 FHDG-FMASGDVGYLDEnGRLFVVGRDD-EMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPG 490
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1250165799 538 QSMTLPDLKTWAREHMAPYTIPTGLLLVEEMPRNQMGKVNKKDLLRH 584
Cdd:PRK13382 491 ASATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQAR 537
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
51-581 |
6.15e-36 |
|
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: 141.51 E-value: 6.15e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 51 AAQSSRINQKPVFVRAPAFGDKPAIIDSSGSHSYkqLYCSSLGLAGRISTALNlDFGGLEGKRISFLCANDASYTVAQWA 130
Cdd:cd17642 12 EDGTAGEQLHKAMKRYASVPGTIAFTDAHTGVNY--SYAEYLEMSVRLAEALK-KYGLKQNDRIAVCSENSLQFFLPVIA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 131 AWMSGGTAVPLFRKHPQSELEYIISDSQSSLLVAGH-------------PYAGTLEPLALKL---GLPCLTLPPTSNLGT 194
Cdd:cd17642 89 GLFIGVGVAPTNDIYNERELDHSLNISKPTIVFCSKkglqkvlnvqkklKIIKTIIILDSKEdykGYQCLYTFITQNLPP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 195 ldGTDTQEKEAAITDWADRPAMIIYTSGTTGRPKGVLHMHSNI--------QAMVQGLVSEwawtrDDVILHTLPLHHVH 266
Cdd:cd17642 169 --GFNEYDFKPPSFDRDEQVALIMNSSGSTGLPKGVQLTHKNIvarfsharDPIFGNQIIP-----DTAILTVIPFHHGF 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 267 GIVNkLLCPLWVGATCVMLPEFQPqkvwEMLLSS--KAPMVNVFMaVPTIY-----SKLIQYYDQHftqphvkdfvravc 339
Cdd:cd17642 242 GMFT-TLGYLICGFRVVLMYKFEE----ELFLRSlqDYKVQSALL-VPTLFaffakSTLVDKYDLS-------------- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 340 keriRLMVSGSAALPLptlqrwEEITGHTLLER---------YGMTEIGMALSNPLKGPRIPGAVGSPLPRVEVRIVMNN 410
Cdd:cd17642 302 ----NLHEIASGGAPL------SKEVGEAVAKRfklpgirqgYGLTETTSAILITPEGDDKPGAVGKVVPFFYAKVVDLD 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 411 TTNTtivLGDHRntrvcpglegkEGELLVRGPSVFKEYWNKPQETRESFIDGGWFKTGDTVVY-KDGVYWIMGRSSvDII 489
Cdd:cd17642 372 TGKT---LGPNE-----------RGELCVKGPMIMKGYVNNPEATKALIDKDGWLHSGDIAYYdEDGHFFIVDRLK-SLI 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 490 KSAGYKISALEVERHLLAHPDIIDVAVIGAPDAIWGQKVTAVVQLRKGQSMTLPDLKTWAREHMAPYT-IPTGLLLVEEM 568
Cdd:cd17642 437 KYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVVLEAGKTMTEKEVMDYVASQVSTAKrLRGGVKFVDEV 516
|
570
....*....|...
gi 1250165799 569 PRNQMGKVNKKDL 581
Cdd:cd17642 517 PKGLTGKIDRRKI 529
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
71-583 |
1.12e-35 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 140.21 E-value: 1.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 71 DKPAII-DSSG-SHSYKQLYCSSLGLAgristALNLDFGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLFRKHPQS 148
Cdd:PRK13391 12 DKPAVImASTGeVVTYRELDERSNRLA-----HLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 149 ELEYIISDSQSSLLVAGHPYAGTLEPLALKL--GLPCLTLpptSNLGTLDG-TDTQEKEAAITDW--ADRP--AMIIYTS 221
Cdd:PRK13391 87 EAAYIVDDSGARALITSAAKLDVARALLKQCpgVRHRLVL---DGDGELEGfVGYAEAVAGLPATpiADESlgTDMLYSS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 222 GTTGRPKGVLHMHS--------NIQAMVQGLvseWAWTRDDVILHTLPLHHVH-----GIVNKLlcplwvGATCVMLPEF 288
Cdd:PRK13391 164 GTTGRPKGIKRPLPeqppdtplPLTAFLQRL---WGFRSDMVYLSPAPLYHSApqravMLVIRL------GGTVIVMEHF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 289 QPQKVWEMLLSSKapmVNVFMAVPTIYSKLIQYYDQHFTQPHVKDFVRAVckerirlmvsgSAALPLPTLQRWEEIT--G 366
Cdd:PRK13391 235 DAEQYLALIEEYG---VTHTQLVPTMFSRMLKLPEEVRDKYDLSSLEVAI-----------HAAAPCPPQVKEQMIDwwG 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 367 HTLLERYGMTE-IGMALSNPLKGPRIPGAVGSPLPRVeVRIvmnnttnttivLGDhrNTRVCPglEGKEGELLVRGPSVF 445
Cdd:PRK13391 301 PIIHEYYAATEgLGFTACDSEEWLAHPGTVGRAMFGD-LHI-----------LDD--DGAELP--PGEPGTIWFEGGRPF 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 446 kEYWNKPQETRES-FIDGGWFKTGDT-VVYKDGVYWIMGRSSVDIIkSAGYKISALEVERHLLAHPDIIDVAVIGAPDAI 523
Cdd:PRK13391 365 -EYLNDPAKTAEArHPDGTWSTVGDIgYVDEDGYLYLTDRAAFMII-SGGVNIYPQEAENLLITHPKVADAAVFGVPNED 442
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1250165799 524 WGQKVTAVVQLRKGQSMTlPD----LKTWAREHMAPYTIPTGLLLVEEMPRNQMGKVNKKdLLR 583
Cdd:PRK13391 443 LGEEVKAVVQPVDGVDPG-PAlaaeLIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKR-LLR 504
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
112-576 |
1.63e-34 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 136.83 E-value: 1.63e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 112 KRISFLCANDASYTVAQWAAWMSGGTAVPLFRKHPQSELEYIISDSQSSLLVAGHPYagtleplalklglpcltlpptsn 191
Cdd:PRK07638 51 KTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKERLAISNADMIVTERYK----------------------- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 192 LGTLDGTDTQ-----EKEAAITDWADRPAMII----------YTSGTTGRPKGVLHMHSNIQAMVQGLVSEWAWTRDDVI 256
Cdd:PRK07638 108 LNDLPDEEGRvieidEWKRMIEKYLPTYAPIEnvqnapfymgFTSGSTGKPKAFLRAQQSWLHSFDCNVHDFHMKREDSV 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 257 LHTLPLHHVH---GIVNKllcpLWVGATCVMLPEFQPQKVWEMLlssKAPMVNVFMAVPTIYSKLIQyydqhftqphvkd 333
Cdd:PRK07638 188 LIAGTLVHSLflyGAIST----LYVGQTVHLMRKFIPNQVLDKL---ETENISVMYTVPTMLESLYK------------- 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 334 fVRAVCKERIRLMVSGsAALPLPTLQRWEEITGH-TLLERYGMTEIG-MALSNPLKGPRIPGAVGSPLPRVEVRIvmnnt 411
Cdd:PRK07638 248 -ENRVIENKMKIISSG-AKWEAEAKEKIKNIFPYaKLYEFYGASELSfVTALVDEESERRPNSVGRPFHNVQVRI----- 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 412 tnttivlgdhRN---TRVCPGLEGKegeLLVRGPSVFKEYWNKPQETRESFIDgGWFKTGDT-VVYKDGVYWIMGRSSvD 487
Cdd:PRK07638 321 ----------CNeagEEVQKGEIGT---VYVKSPQFFMGYIIGGVLARELNAD-GWMTVRDVgYEDEEGFIYIVGREK-N 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 488 IIKSAGYKISALEVERHLLAHPDIIDVAVIGAPDAIWGQKVTAVVqlrKGQSmTLPDLKTWAREHMAPYTIPTGLLLVEE 567
Cdd:PRK07638 386 MILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAII---KGSA-TKQQLKSFCLQRLSSFKIPKEWHFVDE 461
|
....*....
gi 1250165799 568 MPRNQMGKV 576
Cdd:PRK07638 462 IPYTNSGKI 470
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
61-581 |
2.41e-34 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 136.66 E-value: 2.41e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 61 PVFVRAPAFGDKPAIIDSSGSHSYKQLYCSSLGLAGRISTAlnldfGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVP 140
Cdd:PRK13383 40 LLAVTAARWPGRTAIIDDDGALSYRELQRATESLARRLTRD-----GVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVP 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 141 LFRKHPQSELEYIISDSQSSLLVAGHPYAgtlEPLAlKLGLPCLTLPPTsnlgtldgTDTQEKEAAITDWADRPAMIIYT 220
Cdd:PRK13383 115 ISTEFRSDALAAALRAHHISTVVADNEFA---ERIA-GADDAVAVIDPA--------TAGAEESGGRPAVAAPGRIVLLT 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 221 SGTTGRPKGVLHmhsniQAMVQGLVSEWAWTRDDVILHT-------LPLHHVHGIvNKLLCPLWVGATCVMLPEFQPQKV 293
Cdd:PRK13383 183 SGTTGKPKGVPR-----APQLRSAVGVWVTILDRTRLRTgsrisvaMPMFHGLGL-GMLMLTIALGGTVLTHRHFDAEAA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 294 wemLLSSKAPMVNVFMAVPTIYSKLIQYYDQhftqphvkdfVRAVCK-ERIRLMVSGSAALPlPTL-QRWEEITGHTLLE 371
Cdd:PRK13383 257 ---LAQASLHRADAFTAVPVVLARILELPPR----------VRARNPlPQLRVVMSSGDRLD-PTLgQRFMDTYGDILYN 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 372 RYGMTEIGM-ALSNPLKGPRIPGAVGSPLPRVEVRIVmnnttnttivlgDHRNTRVCPGLEGKegeLLVRGPSVFKEYWN 450
Cdd:PRK13383 323 GYGSTEVGIgALATPADLRDAPETVGKPVAGCPVRIL------------DRNNRPVGPRVTGR---IFVGGELAGTRYTD 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 451 KpqeTRESFIDGgWFKTGDtVVYKD--GVYWIMGRSSvDIIKSAGYKISALEVERHLLAHPDIIDVAVIGAPDAIWGQKV 528
Cdd:PRK13383 388 G---GGKAVVDG-MTSTGD-MGYLDnaGRLFIVGRED-DMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRL 461
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1250165799 529 TAVVQLRKGQSMTLPDLKTWAREHMAPYTIPTGLLLVEEMPRNQMGKVNKKDL 581
Cdd:PRK13383 462 AAFVVLHPGSGVDAAQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
106-583 |
2.70e-34 |
|
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: 135.97 E-value: 2.70e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 106 FGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLFRKHPQSELEYIIsdsqssllvagHPYAGTLEPLALKLGlpclt 185
Cdd:cd05929 37 EGVWIADGVYIYLINSILTVFAAAAAWKCGACPAYKSSRAPRAEACAII-----------EIKAAALVCGLFTGG----- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 186 lpptsnlGTLDGTDTQEKEAA------ITDWAdRPAMIIYTSGTTGRPKGVLHMHSNIQAMVQGLVSeWA----WTRDDV 255
Cdd:cd05929 101 -------GALDGLEDYEAAEGgspetpIEDEA-AGWKMLYSGGTTGRPKGIKRGLPGGPPDNDTLMA-AAlgfgPGADSV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 256 ILHTLPLHHVHGIVNKLLCpLWVGATCVMLPEFQPQkvwEMLLSSKAPMVNVFMAVPTIYSKLIQYYDQhftQPHVKDFv 335
Cdd:cd05929 172 YLSPAPLYHAAPFRWSMTA-LFMGGTLVLMEKFDPE---EFLRLIERYRVTFAQFVPTMFVRLLKLPEA---VRNAYDL- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 336 ravckERIRLMVSGSAALPLPTLQRWEEITGHTLLERYGMTE-IGMALSNPLKGPRIPGAVGSPLpRVEVRIvmnnttnt 414
Cdd:cd05929 244 -----SSLKRVIHAAAPCPPWVKEQWIDWGGPIIWEYYGGTEgQGLTIINGEEWLTHPGSVGRAV-LGKVHI-------- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 415 tivLGDhrNTRVCPglEGKEGELLVRGPSVFkEYWNKPQETRESFIDGGWFKTGDtVVY--KDGVYWIMGRSSvDIIKSA 492
Cdd:cd05929 310 ---LDE--DGNEVP--PGEIGEVYFANGPGF-EYTNDPEKTAAARNEGGWSTLGD-VGYldEDGYLYLTDRRS-DMIISG 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 493 GYKISALEVERHLLAHPDIIDVAVIGAPDAIWGQKVTAVVQLRKG---QSMTLPDLKTWAREHMAPYTIPTGLLLVEEMP 569
Cdd:cd05929 380 GVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVQPAPGadaGTALAEELIAFLRDRLSRYKCPRSIEFVAELP 459
|
490
....*....|....
gi 1250165799 570 RNQMGKVNKKdLLR 583
Cdd:cd05929 460 RDDTGKLYRR-LLR 472
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
71-581 |
5.10e-34 |
|
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: 134.30 E-value: 5.10e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 71 DKPAIIDSSGSHSYKQLYcsslGLAGRISTALnLDFGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLFRKHPQSEL 150
Cdd:cd17652 2 DAPAVVFGDETLTYAELN----ARANRLARLL-AARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 151 EYIISDSQSSLLVaghpyagtleplalklglpcltlpptsnlgtldgtdTQekeaaitdwADRPAMIIYTSGTTGRPKGV 230
Cdd:cd17652 77 AYMLADARPALLL------------------------------------TT---------PDNLAYVIYTSGSTGRPKGV 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 231 LHMHSNIQAMVQGLVSEWAWTRDDVILHTLPLHhVHGIVNKLLCPLWVGATCVMLPEfqpqkvwEMLLSSkAPMVNVfma 310
Cdd:cd17652 112 VVTHRGLANLAAAQIAAFDVGPGSRVLQFASPS-FDASVWELLMALLAGATLVLAPA-------EELLPG-EPLADL--- 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 311 vptiyskLIQYYDQHFTQ-PHVKDFVRAVCKERIRLMVSGSAALPLPTLQRWEeiTGHTLLERYGMTE--IGMALSNPLK 387
Cdd:cd17652 180 -------LREHRITHVTLpPAALAALPPDDLPDLRTLVVAGEACPAELVDRWA--PGRRMINAYGPTEttVCATMAGPLP 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 388 GPRIPgAVGSPLPRVEVRivmnnttnttiVLGDHRntRVCPglEGKEGELLVRGPSVFKEYWNKPQETRESFI------D 461
Cdd:cd17652 251 GGGVP-PIGRPVPGTRVY-----------VLDARL--RPVP--PGVPGELYIAGAGLARGYLNRPGLTAERFVadpfgaP 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 462 GG-WFKTGDTVVYK-DGVYWIMGRSSvDIIKSAGYKISALEVERHLLAHPDIIDVAVIGAPDAIWGQKVTAVVQLRKGQS 539
Cdd:cd17652 315 GSrMYRTGDLARWRaDGQLEFLGRAD-DQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAPGAA 393
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1250165799 540 MTLPDLKTWAREHMAPYTIPTGLLLVEEMPRNQMGKVNKKDL 581
Cdd:cd17652 394 PTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
76-502 |
1.49e-33 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 134.72 E-value: 1.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 76 IDSSGSH---SYKQLYCSslglAGRISTALNLDfGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPL----FRKHPQS 148
Cdd:cd05906 31 IDADGSEefqSYQDLLED----ARRLAAGLRQL-GLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLtvppTYDEPNA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 149 ELEYIISDSQ---SSLLVAGHPYAGTLEPLALKLGLPCLTLPPTSNLgtldgtdtqEKEAAITDW----ADRPAMIIYTS 221
Cdd:cd05906 106 RLRKLRHIWQllgSPVVLTDAELVAEFAGLETLSGLPGIRVLSIEEL---------LDTAADHDLpqsrPDDLALLMLTS 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 222 GTTGRPKGVLHMHSNIQAMVQGLVSEWAWTRDDVILHTLPLHHVHGIVNKLLCPLWVGATcvmlpefqpqkvwemllssk 301
Cdd:cd05906 177 GSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVPLDHVGGLVELHLRAVYLGCQ-------------------- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 302 apMVNV----FMAVPTIYSKLIQYYDQHFT-QP-----HVKDFVRAVCKER-----IRLMVSGSAALPLPTLQRWEEitg 366
Cdd:cd05906 237 --QVHVpteeILADPLRWLDLIDRYRVTITwAPnfafaLLNDLLEEIEDGTwdlssLRYLVNAGEAVVAKTIRRLLR--- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 367 htLLERY-----------GMTEI--GMALSNPLKGPRIPGA-----VGSPLPRVEVRIVmnnttnttivlgDHRNTRVcp 428
Cdd:cd05906 312 --LLEPYglppdairpafGMTETcsGVIYSRSFPTYDHSQAlefvsLGRPIPGVSMRIV------------DDEGQLL-- 375
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1250165799 429 gLEGKEGELLVRGPSVFKEYWNKPQETRESFIDGGWFKTGDTVVYKDGVYWIMGRSSvDIIKSAGYKISALEVE 502
Cdd:cd05906 376 -PEGEVGRLQVRGPVVTKGYYNNPEANAEAFTEDGWFRTGDLGFLDNGNLTITGRTK-DTIIVNGVNYYSHEIE 447
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
70-576 |
1.79e-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: 135.01 E-value: 1.79e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 70 GDKPAII------DSSGSHSYKQLYCSSLGLAGRIstalnLDFGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLFR 143
Cdd:cd17634 67 GDRTAIIyegddtSQSRTISYRELHREVCRFAGTL-----LDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFG 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 144 KHPQSELEYIISDSQSSLLVA--GHPYAGTLEPLaLKLGLPCLTL--PPTSNLGTLD--GTDTQEKEAAITDW------- 210
Cdd:cd17634 142 GFAPEAVAGRIIDSSSRLLITadGGVRAGRSVPL-KKNVDDALNPnvTSVEHVIVLKrtGSDIDWQEGRDLWWrdliaka 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 211 ----------ADRPAMIIYTSGTTGRPKGVLHMHSN-IQAMVQGLVSEWAWTRDDVILHTLPLHHVHGIVNKLLCPLWVG 279
Cdd:cd17634 221 spehqpeamnAEDPLFILYTSGTTGKPKGVLHTTGGyLVYAATTMKYVFDYGPGDIYWCTADVGWVTGHSYLLYGPLACG 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 280 ATCVML---PEF-QPQKVWEMLLSSKapmVNVFMAVPTIyskliqyydqhftqphvkdfVRAVCKE---------RIRLM 346
Cdd:cd17634 301 ATTLLYegvPNWpTPARMWQVVDKHG---VNILYTAPTA--------------------IRALMAAgddaiegtdRSSLR 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 347 VSGSAALPL-PTLQRW--EEITGH--TLLERYGMTEIGMALSNPLKG--PRIPGAVGSPLPRVEVRIVmnnttnttivlg 419
Cdd:cd17634 358 ILGSVGEPInPEAYEWywKKIGKEkcPVVDTWWQTETGGFMITPLPGaiELKAGSATRPVFGVQPAVV------------ 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 420 DHRNTRVCPGlegKEGELLVRG--PSVFKEYWNKPQETRESFI---DGGWFkTGDTV-VYKDGVYWIMGRSSvDIIKSAG 493
Cdd:cd17634 426 DNEGHPQPGG---TEGNLVITDpwPGQTRTLFGDHERFEQTYFstfKGMYF-SGDGArRDEDGYYWITGRSD-DVINVAG 500
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 494 YKISALEVERHLLAHPDIIDVAVIGAPDAIWGQKVTAVVQLRKGQ--SMTLPD-LKTWAREHMAPYTIPTGLLLVEEMPR 570
Cdd:cd17634 501 HRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLNHGVepSPELYAeLRNWVRKEIGPLATPDVVHWVDSLPK 580
|
....*.
gi 1250165799 571 NQMGKV 576
Cdd:cd17634 581 TRSGKI 586
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
83-585 |
1.84e-33 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 134.49 E-value: 1.84e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 83 SYKQLYCSSLglagRISTALNLDfGGLEGKRISFLCANDASYTVAqWAAWMSGG----TAVPlfRKHPQsELEYIISDSQ 158
Cdd:PRK06018 41 TYAQIHDRAL----KVSQALDRD-GIKLGDRVATIAWNTWRHLEA-WYGIMGIGaichTVNP--RLFPE-QIAWIINHAE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 159 SSLLVAGHPYAGTLEPLALKLglPCL----------TLPPTSNLGTLDGTDTQEKEAAITDWADRP----AMIIYTSGTT 224
Cdd:PRK06018 112 DRVVITDLTFVPILEKIADKL--PSVeryvvltdaaHMPQTTLKNAVAYEEWIAEADGDFAWKTFDentaAGMCYTSGTT 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 225 GRPKGVLHMH-SNI-QAMVQGLVSEWAWTRDDVILHTLPLHHVHGIVNKLLCPLwVGATCVML-PEFQPQKVWEMLLSSK 301
Cdd:PRK06018 190 GDPKGVLYSHrSNVlHALMANNGDALGTSAADTMLPVVPLFHANSWGIAFSAPS-MGTKLVMPgAKLDGASVYELLDTEK 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 302 apmVNVFMAVPTIYSKLIQYYDQH-FTQPHVKdfvRAVCkerirlmvsGSAALPLPTLQRWEEItGHTLLERYGMTEIG- 379
Cdd:PRK06018 269 ---VTFTAGVPTVWLMLLQYMEKEgLKLPHLK---MVVC---------GGSAMPRSMIKAFEDM-GVEVRHAWGMTEMSp 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 380 MALSNPLKGP--RIPGAV--------GSPLPRVEVRIVmnnttnttivlgDHRNTRVcpGLEGKE-GELLVRGPSVFKEY 448
Cdd:PRK06018 333 LGTLAALKPPfsKLPGDArldvlqkqGYPPFGVEMKIT------------DDAGKEL--PWDGKTfGRLKVRGPAVAAAY 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 449 WnkpQETRESFIDGGWFKTGDT-VVYKDGVYWIMGRSSvDIIKSAGYKISALEVERHLLAHPDIIDVAVIGAPDAIWGQK 527
Cdd:PRK06018 399 Y---RVDGEILDDDGFFDTGDVaTIDAYGYMRITDRSK-DVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDER 474
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1250165799 528 VTAVVQLRKGQSMTLPDLKTWAREHMAPYTIPTGLLLVEEMPRNQMGKVNKKDLLRHF 585
Cdd:PRK06018 475 PLLIVQLKPGETATREEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALREQF 532
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
126-581 |
3.89e-33 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 136.06 E-value: 3.89e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 126 VAQWAAWMSGGTAVPLFRKHPQSELEYIISDSQSSLLVaGHPYagTLEPLALKLGLPCLTLpptsnlgTLDGTDTQEKEA 205
Cdd:PRK12467 577 VGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLL-TQSH--LLAQLPVPAGLRSLCL-------DEPADLLCGYSG 646
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 206 AITDWADRP---AMIIYTSGTTGRPKGVLHMHSNIQAMVQGLVSEWAWTRDDVILHTLPLhHVHGIVNKLLCPLWVGATC 282
Cdd:PRK12467 647 HNPEVALDPdnlAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVSTF-AFDLGVTELFGALASGATL 725
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 283 VMLPEFQPQKVWEMLLSSKAPMVNVFMAVPTIYSKLIQyydqhftqphvkDFVRAVCKERIRLMVSGSaALPLPTLQRWE 362
Cdd:PRK12467 726 HLLPPDCARDAEAFAALMADQGVTVLKIVPSHLQALLQ------------ASRVALPRPQRALVCGGE-ALQVDLLARVR 792
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 363 EIT-GHTLLERYGMTE--IGMALSNPLKGPRIPGAV--GSPLPRVEVRIvMNNTTNTtivlgdhrntrvCPGleGKEGEL 437
Cdd:PRK12467 793 ALGpGARLINHYGPTEttVGVSTYELSDEERDFGNVpiGQPLANLGLYI-LDHYLNP------------VPV--GVVGEL 857
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 438 LVRGPSVFKEYWNKPQETRESFI------DGG-WFKTGDTVVY-KDGVYWIMGRSSvDIIKSAGYKISALEVERHLLAHP 509
Cdd:PRK12467 858 YIGGAGLARGYHRRPALTAERFVpdpfgaDGGrLYRTGDLARYrADGVIEYLGRMD-HQVKIRGFRIELGEIEARLLAQP 936
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1250165799 510 DIIDVAVIGAPDAIWGQKVTAVVQLRKG----QSMTLPDLKTWAREHMAPYTIPTGLLLVEEMPRNQMGKVNKKDL 581
Cdd:PRK12467 937 GVREAVVLAQPGDAGLQLVAYLVPAAVAdgaeHQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKAL 1012
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
95-585 |
3.89e-33 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 133.75 E-value: 3.89e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 95 AGRISTALNLDFGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLFRKHPQSELEYIISDSQSSLLVAGHPYAGTLEP 174
Cdd:PRK05620 48 AAALAHALHDELGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIVADPRLAEQLGE 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 175 L---------ALKLGLPCLTLPPTSNLGTLDGTDTQ---EKEAAITDWAD----RPAMIIYTSGTTGRPKGVLHMHSN-- 236
Cdd:PRK05620 128 IlkecpcvraVVFIGPSDADSAAAHMPEGIKVYSYEallDGRSTVYDWPEldetTAAAICYSTGTTGAPKGVVYSHRSly 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 237 IQAMVQGLVSEWAWTRDDVILHTLPLHHV--HGIvnkllcPL--WVGATCVMLP--EFQPQKVWEMLLSSkapMVNVFMA 310
Cdd:PRK05620 208 LQSLSLRTTDSLAVTHGESFLCCVPIYHVlsWGV------PLaaFMSGTPLVFPgpDLSAPTLAKIIATA---MPRVAHG 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 311 VPTIYSKLIQYYDQHftQPhvkdfvravckERIRL--MVSGSAALPLPTLQRWEEITGHTLLERYGMTE---IGmALSNP 385
Cdd:PRK05620 279 VPTLWIQLMVHYLKN--PP-----------ERMSLqeIYVGGSAVPPILIKAWEERYGVDVVHVWGMTEtspVG-TVARP 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 386 LKGP-------------RIPGAVgsplprvEVRIVmnnttNTTIVLGDH-RNtrvcpglegkEGELLVRGPSVFKEYWNK 451
Cdd:PRK05620 345 PSGVsgearwayrvsqgRFPASL-------EYRIV-----NDGQVMESTdRN----------EGEIQVRGNWVTASYYHS 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 452 PQET----------------RESFIDGGWFKTGDT-VVYKDGVYWIMGRSSvDIIKSAGYKISALEVERHLLAHPDIIDV 514
Cdd:PRK05620 403 PTEEgggaastfrgedvedaNDRFTADGWLRTGDVgSVTRDGFLTIHDRAR-DVIRSGGEWIYSAQLENYIMAAPEVVEC 481
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1250165799 515 AVIGAPDAIWGQKVTAVVQLRKGQS---MTLPDLKTWAREHMAPYTIPTGLLLVEEMPRNQMGKVNKKDLLRHF 585
Cdd:PRK05620 482 AVIGYPDDKWGERPLAVTVLAPGIEptrETAERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDLRQHL 555
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
77-581 |
6.11e-33 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 132.82 E-value: 6.11e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 77 DSSGSHSYKQLYCSSLGLAGRISTAlnldfGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLFRKHPQSELEYI--I 154
Cdd:PRK05857 37 DGTSALRYRELVAEVGGLAADLRAQ-----SVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLPIAAIERFcqI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 155 SDSQSSLLVAGHPYAGTLEPLALKlGLPCLTLPPTSNLGTLDGTDTQEKEAAITDW-ADRPAMIIYTSGTTGRPKGVLHM 233
Cdd:PRK05857 112 TDPAAALVAPGSKMASSAVPEALH-SIPVIAVDIAAVTRESEHSLDAASLAGNADQgSEDPLAMIFTSGTTGEPKAVLLA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 234 HSNIQAMVQGLVSE---WA-WTRDDVILHTLPLHHVHGIVNKLLCpLWVGATCVMLPEfQPQKVWEMLLSSKapmVNVFM 309
Cdd:PRK05857 191 NRTFFAVPDILQKEglnWVtWVVGETTYSPLPATHIGGLWWILTC-LMHGGLCVTGGE-NTTSLLEILTTNA---VATTC 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 310 AVPTIYSKLIqyYDQHFTqphvkdfvrAVCKERIRLMV-SGSAALPLPTlqRWEEITGHTLLERYGMTEIG-MALSNPLK 387
Cdd:PRK05857 266 LVPTLLSKLV--SELKSA---------NATVPSLRLVGyGGSRAIAADV--RFIEATGVRTAQVYGLSETGcTALCLPTD 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 388 GPRIP----GAVGSPLPRVEVRIVMNNTTNTTIVLGdhrntrvcpGLEGKEGELLVRGPSVFKEYWNKPQETRESFIDgG 463
Cdd:PRK05857 333 DGSIVkieaGAVGRPYPGVDVYLAATDGIGPTAPGA---------GPSASFGTLWIKSPANMLGYWNNPERTAEVLID-G 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 464 WFKTGDTVV-YKDGVYWIMGRSSvDIIKSAGYKISALEVERHLLAHPDIIDVAVIGAPDAIWGQKV-TAVVQLRKGQSMT 541
Cdd:PRK05857 403 WVNTGDLLErREDGFFYIKGRSS-EMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGALVgLAVVASAELDESA 481
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1250165799 542 LPDLK--TWAR-----EHMAPytiPTGLLLVEEMPRNQMGKVNKKDL 581
Cdd:PRK05857 482 ARALKhtIAARfrresEPMAR---PSTIVIVTDIPRTQSGKVMRASL 525
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
74-578 |
8.46e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 132.56 E-value: 8.46e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 74 AIIDSSGSHSYKQLYCSSLGLAGRISTAlnldfGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPL---FRKHpqsEL 150
Cdd:PRK06164 28 ALIDEDRPLSRAELRALVDRLAAWLAAQ-----GVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVntrYRSH---EV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 151 EYIISDSQSSLLVA-----GHPYAGTLE--PLALKLGLPCL--------TLP---PTSNLGTLDGTDTQEKEAAITDWA- 211
Cdd:PRK06164 100 AHILGRGRARWLVVwpgfkGIDFAAILAavPPDALPPLRAIavvddaadATPapaPGARVQLFALPDPAPPAAAGERAAd 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 212 -DRPAMIIYTSGTTGRPKGVLHMHSNIQAMVQGLVSEWAWTRDDVILHTLPLHHVHGIvNKLLCPLWVGATCVMLPEFQP 290
Cdd:PRK06164 180 pDAGALLFTTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFGF-STLLGALAGGAPLVCEPVFDA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 291 QKVWEMLLSSKapMVNVFmAVPTIYSKLIQyydqhfTQPHVKDFVRAvckeriRLMVSGSAALPLPTLQRWEEITGHTLL 370
Cdd:PRK06164 259 ARTARALRRHR--VTHTF-GNDEMLRRILD------TAGERADFPSA------RLFGFASFAPALGELAALARARGVPLT 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 371 ERYGMTE-IGMALSNPLKGP---RIPGAvGSPL-PRVEVRIVmnnttnttivlgDHRNTRVCPglEGKEGELLVRGPSVF 445
Cdd:PRK06164 324 GLYGSSEvQALVALQPATDPvsvRIEGG-GRPAsPEARVRAR------------DPQDGALLP--DGESGEIEIRAPSLM 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 446 KEYWNKPQETRESFIDGGWFKTGD-TVVYKDGVYWIMGRSSvDIIKSAGYKISALEVERHLLAHPDIIDVAVIGApdAIW 524
Cdd:PRK06164 389 RGYLDNPDATARALTDDGYFRTGDlGYTRGDGQFVYQTRMG-DSLRLGGFLVNPAEIEHALEALPGVAAAQVVGA--TRD 465
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1250165799 525 GQKV-TAVVQLRKGQSMTLPDLKTWAREHMAPYTIPTGLLLVEEMPRNQMGKVNK 578
Cdd:PRK06164 466 GKTVpVAFVIPTDGASPDEAGLMAACREALAGFKVPARVQVVEAFPVTESANGAK 520
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
211-583 |
1.15e-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: 132.76 E-value: 1.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 211 ADRPAMIIYTSGTTGRPKGVlhMHSNIQAMVQGLVSEWaWT---RDDVIL-----------HTlplHHVHGivnkllcPL 276
Cdd:TIGR02188 236 SEDPLFILYTSGSTGKPKGV--LHTTGGYLLYAAMTMK-YVfdiKDGDIFwctadvgwitgHS---YIVYG-------PL 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 277 WVGATCVML---PEF-QPQKVWEMLLSSKapmVNVFMAVPTIYSKLIQYYDQHftqphvkdfVRAVCKERIRLMvsGSAA 352
Cdd:TIGR02188 303 ANGATTVMFegvPTYpDPGRFWEIIEKHK---VTIFYTAPTAIRALMRLGDEW---------VKKHDLSSLRLL--GSVG 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 353 LPL-PTLQRW-EEITGHT---LLERYGMTEIGMALSNPLKG--PRIPGAVGSPLPRVEVRIVmNNTTNttivlgdhrntr 425
Cdd:TIGR02188 369 EPInPEAWMWyYKVVGKErcpIVDTWWQTETGGIMITPLPGatPTKPGSATLPFFGIEPAVV-DEEGN------------ 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 426 VCPGlEGKEGELLVRG--PSVFKEYWNKPQETRESFIDG--GWFKTGDTVVY-KDGVYWIMGRSSvDIIKSAGYKISALE 500
Cdd:TIGR02188 436 PVEG-PGEGGYLVIKQpwPGMLRTIYGDHERFVDTYFSPfpGYYFTGDGARRdKDGYIWITGRVD-DVINVSGHRLGTAE 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 501 VERHLLAHPDIIDVAVIGAPDAIWGQKVTAVVQLRKGQSMTL---PDLKTWAREHMAPYTIPTGLLLVEEMPRNQMGKVN 577
Cdd:TIGR02188 514 IESALVSHPAVAEAAVVGIPDDIKGQAIYAFVTLKDGYEPDDelrKELRKHVRKEIGPIAKPDKIRFVPGLPKTRSGKIM 593
|
....*.
gi 1250165799 578 KKdLLR 583
Cdd:TIGR02188 594 RR-LLR 598
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
71-581 |
1.25e-32 |
|
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: 130.85 E-value: 1.25e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 71 DKPAIIDSSGSHSYKQLYCSSLGLAGRISTAlnldfGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLFRKHPQSEL 150
Cdd:cd12114 2 DATAVICGDGTLTYGELAERARRVAGALKAA-----GVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 151 EYIISDSQSSLLVAGHPYAGTLEPLalklglPCLTLPPTSNLGTLDgtdtqeKEAAITDWADRPAMIIYTSGTTGRPKGV 230
Cdd:cd12114 77 EAILADAGARLVLTDGPDAQLDVAV------FDVLILDLDALAAPA------PPPPVDVAPDDLAYVIFTSGSTGTPKGV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 231 LHMHSN----IQAMVQglvsEWAWTRDDVILHTLPLHH---VHGIVNkllcPLWVGATCVMLPEFQPQKV--WEMLLSSK 301
Cdd:cd12114 145 MISHRAalntILDINR----RFAVGPDDRVLALSSLSFdlsVYDIFG----ALSAGATLVLPDEARRRDPahWAELIERH 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 302 ApmVNVFMAVPTIYSKLIQYYDQHFTQPHVkdfVRAVckerirlMVSG---SAALPLPTLQRWEEITGHTLlerYGMTEi 378
Cdd:cd12114 217 G--VTLWNSVPALLEMLLDVLEAAQALLPS---LRLV-------LLSGdwiPLDLPARLRALAPDARLISL---GGATE- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 379 GMALSNPLKGPRIPGAVGS-----PLPRVEVRIVmnnttnttivlgdHRNTRVCPglEGKEGELLVRGPSVFKEYWNKPQ 453
Cdd:cd12114 281 ASIWSIYHPIDEVPPDWRSipygrPLANQRYRVL-------------DPRGRDCP--DWVPGELWIGGRGVALGYLGDPE 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 454 ETRESFID----GGWFKTGDTVVYK-DGVYWIMGRssVDI-IKSAGYKISALEVERHLLAHPDIIDVAVIGAPDAIWGQK 527
Cdd:cd12114 346 LTAARFVThpdgERLYRTGDLGRYRpDGTLEFLGR--RDGqVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDPGGKRL 423
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1250165799 528 VTAVVQLRKGQSMTLPDLKTWAREHMAPYTIPTGLLLVEEMPRNQMGKVNKKDL 581
Cdd:cd12114 424 AAFVVPDNDGTPIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
16-583 |
1.13e-31 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 131.62 E-value: 1.13e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 16 ALPHWKATFHRtyFPSEPGqwllgsvVHRRahrwTAAQSSRinqkpvfvrAPafgDKPAIIDSSGSHSYKQLYCSSLGLA 95
Cdd:PRK12316 1988 ILADWDRTPEA--YPRGPG-------VHQR----IAEQAAR---------AP---EAIAVVFGDQHLSYAELDSRANRLA 2042
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 96 GRIstalnLDFGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLFRKHPQSELEYIISDSQSSLLVAGhpyAGTLEPL 175
Cdd:PRK12316 2043 HRL-----RARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQ---RHLLERL 2114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 176 ALKLGLPCLTLPPTSNLgtldgTDTQEKEAAITDWADRPAMIIYTSGTTGRPKGVLHMHSNIQAMVQGLVSEWAWTRDDV 255
Cdd:PRK12316 2115 PLPAGVARLPLDRDAEW-----ADYPDTAPAVQLAGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPADC 2189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 256 ILHTLPLHhVHGIVNKLLCPLWVGATCVMLPEFQ--PQKVWEMLlSSKAPMVNVFMAVptiyskliqyydqhFTQPHVKD 333
Cdd:PRK12316 2190 ELQFMSFS-FDGAHEQWFHPLLNGARVLIRDDELwdPEQLYDEM-ERHGVTILDFPPV--------------YLQQLAEH 2253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 334 FVRAVCKERIRLMVSGSAALPLPTLQR-WEEITGHTLLERYGMTEigmALSNPL---KGPRIP-GAVGSPLPRVevrivm 408
Cdd:PRK12316 2254 AERDGRPPAVRVYCFGGEAVPAASLRLaWEALRPVYLFNGYGPTE---AVVTPLlwkCRPQDPcGAAYVPIGRA------ 2324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 409 nnttnttivLGDHRNTRVCPGLE----GKEGELLVRGPSVFKEYWNKPQETRESFI-------DGGWFKTGDTVVYK-DG 476
Cdd:PRK12316 2325 ---------LGNRRAYILDADLNllapGMAGELYLGGEGLARGYLNRPGLTAERFVpdpfsasGERLYRTGDLARYRaDG 2395
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 477 VYWIMGRssVD-IIKSAGYKISALEVERHLLAHPDIIDVAVIgAPDAIWGQKVTAVVQLRKGQSMTLPDLKTWAREHMAP 555
Cdd:PRK12316 2396 VVEYLGR--IDhQVKIRGFRIELGEIEARLQAHPAVREAVVV-AQDGASGKQLVAYVVPDDAAEDLLAELRAWLAARLPA 2472
|
570 580
....*....|....*....|....*...
gi 1250165799 556 YTIPTGLLLVEEMPRNQMGKVNKKDLLR 583
Cdd:PRK12316 2473 YMVPAHWVVLERLPLNPNGKLDRKALPK 2500
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
71-583 |
8.41e-31 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 125.89 E-value: 8.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 71 DKPAII--DSSGSHSYKQLYCSSLGLAGRIStalnlDFGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLFRKHPQS 148
Cdd:PRK13390 12 DRPAVIvaETGEQVSYRQLDDDSAALARVLY-----DAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 149 ELEYIISDSQSSLLVAghpyAGTLEPLALKLGLPcltLPPTSNLG-TLDGTDTQEKE--AAITDWADRP--AMIIYTSGT 223
Cdd:PRK13390 87 EADYIVGDSGARVLVA----SAALDGLAAKVGAD---LPLRLSFGgEIDGFGSFEAAlaGAGPRLTEQPcgAVMLYSSGT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 224 TGRPKG---------VLHMHSNIQAMVQGLvseWAWTRDDVILHTLPLHHVH-----GIVNKLlcplwvGATCVMLPEFQ 289
Cdd:PRK13390 160 TGFPKGiqpdlpgrdVDAPGDPIVAIARAF---YDISESDIYYSSAPIYHAAplrwcSMVHAL------GGTVVLAKRFD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 290 PQKVWEMLLSSKapmVNVFMAVPTIYSKLIQYYDQHFTQPHVKDfvravckerIRLMVSGSAALPLPTLQRWEEITGHTL 369
Cdd:PRK13390 231 AQATLGHVERYR---ITVTQMVPTMFVRLLKLDADVRTRYDVSS---------LRAVIHAAAPCPVDVKHAMIDWLGPIV 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 370 LERYGMTEI-GMALSNPLKGPRIPGAVGSPlprvevrivmnnttnttiVLGDhrnTRVCP--GLEGKEGELlvrGPSVFK 446
Cdd:PRK13390 299 YEYYSSTEAhGMTFIDSPDWLAHPGSVGRS------------------VLGD---LHICDddGNELPAGRI---GTVYFE 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 447 E------YWNKPQETRES------FidggWFKTGDT-VVYKDGVYWIMGRSSVDIIkSAGYKISALEVERHLLAHPDIID 513
Cdd:PRK13390 355 RdrlpfrYLNDPEKTAAAqhpahpF----WTTVGDLgSVDEDGYLYLADRKSFMII-SGGVNIYPQETENALTMHPAVHD 429
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1250165799 514 VAVIGAPDAIWGQKVTAVVQLRKG--QSMTLP-DLKTWAREHMAPYTIPTGLLLVEEMPRNQMGKVnKKDLLR 583
Cdd:PRK13390 430 VAVIGVPDPEMGEQVKAVIQLVEGirGSDELArELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKL-VKGLLR 501
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
126-581 |
1.86e-30 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 127.77 E-value: 1.86e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 126 VAQWAAWMSGGTAVPLFRKHPQSELEYIISDSQSSLLVAgHPYAgtLEPLALKLGLPCLTLPPTSnlgtlDGTDTQEKEA 205
Cdd:PRK12316 4616 VGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAALLLT-QSHL--LQRLPIPDGLASLALDRDE-----DWEGFPAHDP 4687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 206 AITDWADRPAMIIYTSGTTGRPKGVLHMHSNIQAMVQGLVSEWAWTRDDVILHTLPLhHVHGIVNKLLCPLWVGATCVML 285
Cdd:PRK12316 4688 AVRLHPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSF-SFDGSHEGLYHPLINGASVVIR 4766
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 286 PEFQ--PQKVWEMLLSSKAPMVNvfmAVPTIYSKLIQyydqhftqphvkDFVRAVCKERIRLMVSGSAALPLPTLQRWEE 363
Cdd:PRK12316 4767 DDSLwdPERLYAEIHEHRVTVLV---FPPVYLQQLAE------------HAERDGEPPSLRVYCFGGEAVAQASYDLAWR 4831
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 364 ITGHT-LLERYGMTEIGM-ALSNPLKGPRIPGA----VGSPLPRVevrivmnnttnTTIVLGDHRNtrvcPGLEGKEGEL 437
Cdd:PRK12316 4832 ALKPVyLFNGYGPTETTVtVLLWKARDGDACGAaympIGTPLGNR-----------SGYVLDGQLN----PLPVGVAGEL 4896
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 438 LVRGPSVFKEYWNKPQETRESFI-------DGGWFKTGDTVVYK-DGVYWIMGRssVD-IIKSAGYKISALEVERHLLAH 508
Cdd:PRK12316 4897 YLGGEGVARGYLERPALTAERFVpdpfgapGGRLYRTGDLARYRaDGVIDYLGR--VDhQVKIRGFRIELGEIEARLREH 4974
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 509 PDIIDVAVIGAPDAIWGQKV-------TAVVQLRKGQSMTLPDLKTWAREHMAPYTIPTGLLLVEEMPRNQMGKVNKKDL 581
Cdd:PRK12316 4975 PAVREAVVIAQEGAVGKQLVgyvvpqdPALADADEAQAELRDELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRKAL 5054
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
61-583 |
3.80e-30 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 124.71 E-value: 3.80e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 61 PVFV--RAPAFGDKPAIIDSSGSHSYKqlYCSSLGLAGRISTALNlDFGGLEGKRISFLCANDASYTVAQWAAWMSGGTA 138
Cdd:PLN02330 31 PDFVlqDAELYADKVAFVEAVTGKAVT--YGEVVRDTRRFAKALR-SLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVF 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 139 VPLFRKHPQSELEYIISDSQSSLLVAGHPYAGTLEplalKLGLPCLTLPPTSNLGTLDGTDTQEKEAAITDWADRPAM-- 216
Cdd:PLN02330 108 SGANPTALESEIKKQAEAAGAKLIVTNDTNYGKVK----GLGLPVIVLGEEKIEGAVNWKELLEAADRAGDTSDNEEIlq 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 217 -----IIYTSGTTGRPKGVLHMHSNiqaMVQGLVSEWAWTRDDVI-----LHTLPLHHVHGIVNKLLCPLWVGATCVMLP 286
Cdd:PLN02330 184 tdlcaLPFSSGTTGISKGVMLTHRN---LVANLCSSLFSVGPEMIgqvvtLGLIPFFHIYGITGICCATLRNKGKVVVMS 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 287 EFQPQKVWEMLLS---SKAPMVnvfmavPTIYSKLIQyydqhftQPHVKDFvrAVCKERIRLMVSGSAALPLPTLQRWE- 362
Cdd:PLN02330 261 RFELRTFLNALITqevSFAPIV------PPIILNLVK-------NPIVEEF--DLSKLKLQAIMTAAAPLAPELLTAFEa 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 363 EITGHTLLERYGMTE---IGMALSNPLKGPRIP--GAVGSPLPRVEVRIVmnnttnttivlgDHRNTRVCPglEGKEGEL 437
Cdd:PLN02330 326 KFPGVQVQEAYGLTEhscITLTHGDPEKGHGIAkkNSVGFILPNLEVKFI------------DPDTGRSLP--KNTPGEL 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 438 LVRGPSVFKEYWNKPQETRESFIDGGWFKTGDT-VVYKDGVYWIMGRSSvDIIKSAGYKISALEVERHLLAHPDIIDVAV 516
Cdd:PLN02330 392 CVRSQCVMQGYYNNKEETDRTIDEDGWLHTGDIgYIDDDGDIFIVDRIK-ELIKYKGFQVAPAELEAILLTHPSVEDAAV 470
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1250165799 517 IGAPDAIWGQKVTAVVQLRKGQSMTLPDLKTWAREHMAPYTIPTGLLLVEEMPRNQMGKVNKKdLLR 583
Cdd:PLN02330 471 VPLPDEEAGEIPAACVVINPKAKESEEDILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRR-LLK 536
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
126-583 |
5.16e-30 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 126.43 E-value: 5.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 126 VAQWAAWMSGGTAVPLFRKHPQSELEYIISDSQSSLLVAghpYAGTLEPLALKLGLPCLTLPPTSNLgtLDGTDTQEKEA 205
Cdd:PRK12467 1639 VGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLT---QSHLQARLPLPDGLRSLVLDQEDDW--LEGYSDSNPAV 1713
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 206 AITDwaDRPAMIIYTSGTTGRPKGVLHMHSNIQAMVQGLVSEWAWTRDDVILHTLPlHHVHGIVNKLLCPLWVGATCVML 285
Cdd:PRK12467 1714 NLAP--QNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTS-FAFDVSVWELFWPLINGARLVIA 1790
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 286 PEFQPQKVWEMLLSSKAPMVNVFMAVPTIYSKLIQyYDQHFTQPhvkdfvravckERIRLMVSGSAALPLPTLQRWEEIT 365
Cdd:PRK12467 1791 PPGAHRDPEQLIQLIERQQVTTLHFVPSMLQQLLQ-MDEQVEHP-----------LSLRRVVCGGEALEVEALRPWLERL 1858
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 366 GHT-LLERYGMTEIGM-------ALSNPLKGPRIPgaVGSPLPRVEVRIvMNNTTNttivlgdhrntrvcPGLEGKEGEL 437
Cdd:PRK12467 1859 PDTgLFNLYGPTETAVdvthwtcRRKDLEGRDSVP--IGQPIANLSTYI-LDASLN--------------PVPIGVAGEL 1921
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 438 LVRGPSVFKEYWNKPQETRESFI-------DGGWFKTGDTVVYK-DGVYWIMGRssVD-IIKSAGYKISALEVERHLLAH 508
Cdd:PRK12467 1922 YLGGVGLARGYLNRPALTAERFVadpfgtvGSRLYRTGDLARYRaDGVIEYLGR--IDhQVKIRGFRIELGEIEARLREQ 1999
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 509 PDIIDVAVIgAPDAIWGQKVTAVVqLRKGQSMTLPD---------LKTWAREHMAPYTIPTGLLLVEEMPRNQMGKVNKK 579
Cdd:PRK12467 2000 GGVREAVVI-AQDGANGKQLVAYV-VPTDPGLVDDDeaqvalraiLKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRK 2077
|
....
gi 1250165799 580 DLLR 583
Cdd:PRK12467 2078 ALPA 2081
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
122-581 |
1.16e-29 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 125.45 E-value: 1.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 122 ASYTVAQWAAWMSGGTAVPLFRKHPQSELEYIISDSQSSLLVAGHPYAGTLePLALKLGLPCLTLPPTSnlgtLDGTDTQ 201
Cdd:PRK12316 572 IEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQSHLGRKL-PLAAGVQVLDLDRPAAW----LEGYSEE 646
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 202 EKEAAITdwADRPAMIIYTSGTTGRPKGVLHMHSNIQAMVQGLVSEWAWTRDDVILHTLPLHHVHGiVNKLLCPLWVGAT 281
Cdd:PRK12316 647 NPGTELN--PENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVS-VWEFFWPLMSGAR 723
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 282 CVMLPE---FQPQKVWEMllsSKAPMVNVFMAVPTIYSKLIQYYDqhftqphvkdfVRAVCKERiRLMVSGSaALPLPTL 358
Cdd:PRK12316 724 LVVAAPgdhRDPAKLVEL---INREGVDTLHFVPSMLQAFLQDED-----------VASCTSLR-RIVCSGE-ALPADAQ 787
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 359 QRWEEITGHT-LLERYGMTE--IGMALSNPLK--GPRIPgaVGSPLPRVEVRIVmnnttnttivlgdHRNTRVCPglEGK 433
Cdd:PRK12316 788 EQVFAKLPQAgLYNLYGPTEaaIDVTHWTCVEegGDSVP--IGRPIANLACYIL-------------DANLEPVP--VGV 850
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 434 EGELLVRGPSVFKEYWNKPQETRESFI-----DGG-WFKTGDTVVYK-DGVYWIMGRSSvDIIKSAGYKISALEVERHLL 506
Cdd:PRK12316 851 LGELYLAGRGLARGYHGRPGLTAERFVpspfvAGErMYRTGDLARYRaDGVIEYAGRID-HQVKLRGLRIELGEIEARLL 929
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1250165799 507 AHPDIIDVAVIgapdAIWGQKVTAVVQLRKGQSMTLPDLKTWAREHMAPYTIPTGLLLVEEMPRNQMGKVNKKDL 581
Cdd:PRK12316 930 EHPWVREAAVL----AVDGKQLVGYVVLESEGGDWREALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKAL 1000
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
176-584 |
1.27e-29 |
|
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: 121.52 E-value: 1.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 176 ALKLGlpCLTLPPTSNLGTLDGTDTQEKEAAI------TDWADRPAMIIYTSGTTGRPKGVLHMHSNIQAmvqGLVSEWA 249
Cdd:cd05974 45 AMKLG--AVVIPATTLLTPDDLRDRVDRGGAVyaavdeNTHADDPMLLYFTSGTTSKPKLVEHTHRSYPV---GHLSTMY 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 250 WT---RDDVILH-TLPLHHVHGIVNkLLCPLWVGATCVML--PEFQPQKVWEMLLSSKapmVNVFMAVPTIYSKLIQyyd 323
Cdd:cd05974 120 WIglkPGDVHWNiSSPGWAKHAWSC-FFAPWNAGATVFLFnyARFDAKRVLAALVRYG---VTTLCAPPTVWRMLIQ--- 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 324 qhftqphvKDFVRAvcKERIRLMVSGSAALPLPTLQRWEEITGHTLLERYGMTEIGMALSNPLKGPRIPGAVGSPLPrvE 403
Cdd:cd05974 193 --------QDLASF--DVKLREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETTALVGNSPGQPVKAGSMGRPLP--G 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 404 VRIVMNNTTnttivlgdhrntrvcpGLEGKEGELLV-----RGPSVFKEYWNKPQETRESfIDGGWFKTGDTVVY-KDGV 477
Cdd:cd05974 261 YRVALLDPD----------------GAPATEGEVALdlgdtRPVGLMKGYAGDPDKTAHA-MRGGYYRTGDIAMRdEDGY 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 478 YWIMGRSSvDIIKSAGYKISALEVERHLLAHPDIIDVAVIGAPDAIWGQKVTAVVQLRKGQS---MTLPDLKTWAREHMA 554
Cdd:cd05974 324 LTYVGRAD-DVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGYEpspETALEIFRFSRERLA 402
|
410 420 430
....*....|....*....|....*....|
gi 1250165799 555 PYTIPTGLLLVeEMPRNQMGKVNKKDLLRH 584
Cdd:cd05974 403 PYKRIRRLEFA-ELPKTISGKIRRVELRRR 431
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
214-583 |
3.03e-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: 122.28 E-value: 3.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 214 PAMIIYTSGTTGRPKGVLHMHSNIqaMVQ-GLVSEWAW-TRDDVIL-----------HTlplHHVHGivnkllcPLWVGA 280
Cdd:cd05966 233 PLFILYTSGSTGKPKGVVHTTGGY--LLYaATTFKYVFdYHPDDIYwctadigwitgHS---YIVYG-------PLANGA 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 281 TCVML---PEF-QPQKVWEMLLSSKapmVNVFMAVPTIYSKLIQYYDQHFTQpHvkdfvravckERIRLMVSGSAALPL- 355
Cdd:cd05966 301 TTVMFegtPTYpDPGRYWDIVEKHK---VTIFYTAPTAIRALMKFGDEWVKK-H----------DLSSLRVLGSVGEPIn 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 356 PTLQRW-EEITGH---TLLERYGMTEIGMALSNPLKG--PRIPGAVGSPLPRVEVRIVmnnttnttivlgdHRNTRVCPG 429
Cdd:cd05966 367 PEAWMWyYEVIGKercPIVDTWWQTETGGIMITPLPGatPLKPGSATRPFFGIEPAIL-------------DEEGNEVEG 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 430 leGKEGELLVRG--PSVFKEYWNKPQETRESFI--DGGWFKTGDTVVY-KDGVYWIMGRSSvDIIKSAGYKISALEVERH 504
Cdd:cd05966 434 --EVEGYLVIKRpwPGMARTIYGDHERYEDTYFskFPGYYFTGDGARRdEDGYYWITGRVD-DVINVSGHRLGTAEVESA 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 505 LLAHPDIIDVAVIGAPDAIWGQKVTAVVQLRKGQSMTLP---DLKTWAREHMAPYTIPTGLLLVEEMPRNQMGKVNKKdL 581
Cdd:cd05966 511 LVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGEEPSDElrkELRKHVRKEIGPIATPDKIQFVPGLPKTRSGKIMRR-I 589
|
..
gi 1250165799 582 LR 583
Cdd:cd05966 590 LR 591
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
214-581 |
4.03e-29 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 122.05 E-value: 4.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 214 PAMIIYTSGTTGRPKGVLHMHSNIQAMVQGLVSEWAWTRDDVILHTLPLHHVHGivnkllcplWV--------GATCVML 285
Cdd:PLN03102 188 PISLNYTSGTTADPKGVVISHRGAYLSTLSAIIGWEMGTCPVYLWTLPMFHCNG---------WTftwgtaarGGTSVCM 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 286 PEFQPQKVWEMLlsskaPMVNV--FMAVPTIYSKLIQ--YYDQHFTQPHVKdfvravckerirlMVSGSAALPLPTLQRW 361
Cdd:PLN03102 259 RHVTAPEIYKNI-----EMHNVthMCCVPTVFNILLKgnSLDLSPRSGPVH-------------VLTGGSPPPAALVKKV 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 362 EEItGHTLLERYGMTEIgmalsnplKGP-----------RIPGAVGSPL-PRVEVRIVmnnttntTIVLGDHRNTRVCPG 429
Cdd:PLN03102 321 QRL-GFQVMHAYGLTEA--------TGPvlfcewqdewnRLPENQQMELkARQGVSIL-------GLADVDVKNKETQES 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 430 L--EGKE-GELLVRGPSVFKEYWNKPQETRESFiDGGWFKTGDT-VVYKDGVYWIMGRSSvDIIKSAGYKISALEVERHL 505
Cdd:PLN03102 385 VprDGKTmGEIVIKGSSIMKGYLKNPKATSEAF-KHGWLNTGDVgVIHPDGHVEIKDRSK-DIIISGGENISSVEVENVL 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 506 LAHPDIIDVAVIGAPDAIWGQKVTAVVQLRKGQSMTLP----------DLKTWAREHMAPYTIPTGLLLVEEMPRNQMGK 575
Cdd:PLN03102 463 YKYPKVLETAVVAMPHPTWGETPCAFVVLEKGETTKEDrvdklvtrerDLIEYCRENLPHFMCPRKVVFLQELPKNGNGK 542
|
....*.
gi 1250165799 576 VNKKDL 581
Cdd:PLN03102 543 ILKPKL 548
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
215-585 |
4.92e-29 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 118.22 E-value: 4.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 215 AMIIYTSGTTGRPKGVLHMHSNI----QAMVQGLVSEWAWtrddviLHTLPLHHVHGIvNKLLCPLWVGA--TCVMLPE- 287
Cdd:PRK07824 38 ALVVATSGTTGTPKGAMLTAAALtasaDATHDRLGGPGQW------LLALPAHHIAGL-QVLVRSVIAGSepVELDVSAg 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 288 FQPqkvwemllsSKAPMVNVFMAVPTIYSKLIQyydqhfTQpHVKDFVRAVCKERIRLM---VSGSAALPLPTLQRWEEI 364
Cdd:PRK07824 111 FDP---------TALPRAVAELGGGRRYTSLVP------MQ-LAKALDDPAATAALAELdavLVGGGPAPAPVLDAAAAA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 365 tGHTLLERYGMTEIGmalsnplkgpriPGAV--GSPLPRVEVRIVmnnttNTTIVLGdhrntrvcpglegkegellvrGP 442
Cdd:PRK07824 175 -GINVVRTYGMSETS------------GGCVydGVPLDGVRVRVE-----DGRIALG---------------------GP 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 443 SVFKEYWNKPQEtrESFIDGGWFKTGDTVVYKDGVYWIMGRSSvDIIKSAGYKISALEVERHLLAHPDIIDVAVIGAPDA 522
Cdd:PRK07824 216 TLAKGYRNPVDP--DPFAEPGWFRTDDLGALDDGVLTVLGRAD-DAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDD 292
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1250165799 523 IWGQKVTAVVQLRKGQSMTLPDLKTWAREHMAPYTIPTGLLLVEEMPRNQMGKVNKKDLLRHF 585
Cdd:PRK07824 293 RLGQRVVAAVVGDGGPAPTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALVRRF 355
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
126-583 |
6.51e-29 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 123.14 E-value: 6.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 126 VAQWAAWMSGGTAVPLFRKHPQSELEYIISDSQSSLLvaghpyagtleplalkLGLPCLTLPPTSNLGTL----DGTDTQ 201
Cdd:PRK12316 3122 VGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLL----------------LSQSHLRLPLAQGVQVLdldrGDENYA 3185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 202 EKEAAITDWADRPAMIIYTSGTTGRPKGVLHMHSNIQAMVQGLVSEWAWTRDDVILHTLPLhHVHGIVNKLLCPLWVGAT 281
Cdd:PRK12316 3186 EANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTF-SFDVFVEELFWPLMSGAR 3264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 282 CVMLPEFQ---PQKVWEMLLSSkapMVNVFMAVPTIYSKLIQYydqhftqphvkdfVRAVCKERIRLMVSGSAALPLPTL 358
Cdd:PRK12316 3265 VVLAGPEDwrdPALLVELINSE---GVDVLHAYPSMLQAFLEE-------------EDAHRCTSLKRIVCGGEALPADLQ 3328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 359 QRWeeITGHTLLERYGMTEIGMALSNPLKGPRIPGA--VGSPLPRVEVRIVMNNTTnttivlgdhrntrvcPGLEGKEGE 436
Cdd:PRK12316 3329 QQV--FAGLPLYNLYGPTEATITVTHWQCVEEGKDAvpIGRPIANRACYILDGSLE---------------PVPVGALGE 3391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 437 LLVRGPSVFKEYWNKPQETRESFI------DGGWFKTGDTVVYK-DGVYWIMGRSSVDiIKSAGYKISALEVERHLLAHP 509
Cdd:PRK12316 3392 LYLGGEGLARGYHNRPGLTAERFVpdpfvpGERLYRTGDLARYRaDGVIEYIGRVDHQ-VKIRGFRIELGEIEARLLEHP 3470
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1250165799 510 DIIDVAVIgapdAIWGQKVTAVVQLRKGQSMTLPDLKTWAREHMAPYTIPTGLLLVEEMPRNQMGKVNKKDLLR 583
Cdd:PRK12316 3471 WVREAVVL----AVDGRQLVAYVVPEDEAGDLREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPR 3540
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
211-579 |
7.06e-29 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 122.34 E-value: 7.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 211 ADRPAMIIYTSGTTGRPKGVLHMHSNIQAMVQGLVSEWAWTRDDVILHTLPLHHVHGIVNKLLCPLWVGATCVMLPEfqP 290
Cdd:PRK08633 781 PDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSSLPFFHSFGLTVTLWLPLLEGIKVVYHPD--P 858
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 291 ---QKVWEMLLSSKApmvNVFMAVPT---IYSKliqyydqhFTQPHVKDFvravckERIRLMVSGSAALPLPTLQRWEEI 364
Cdd:PRK08633 859 tdaLGIAKLVAKHRA---TILLGTPTflrLYLR--------NKKLHPLMF------ASLRLVVAGAEKLKPEVADAFEEK 921
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 365 TGHTLLERYGMTE-----------IGMALSNPLKGPRiPGAVGSPLPRVEVRIVmnnttnttivlgDHRNTRVCPglEGK 433
Cdd:PRK08633 922 FGIRILEGYGATEtspvasvnlpdVLAADFKRQTGSK-EGSVGMPLPGVAVRIV------------DPETFEELP--PGE 986
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 434 EGELLVRGPSVFKEYWNKPQETRESF--IDG-GWFKTGDT-VVYKDGVYWIMGRSSvDIIKSAGYKIS--ALEVERHLLA 507
Cdd:PRK08633 987 DGLILIGGPQVMKGYLGDPEKTAEVIkdIDGiGWYVTGDKgHLDEDGFLTITDRYS-RFAKIGGEMVPlgAVEEELAKAL 1065
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1250165799 508 HPDIIDVAVIGAPDAIWGQKVTAVVQLRKGQSMTLpdLKTWAREHMAPYTIPTGLLLVEEMPRNQMGKVNKK 579
Cdd:PRK08633 1066 GGEEVVFAVTAVPDEKKGEKLVVLHTCGAEDVEEL--KRAIKESGLPNLWKPSRYFKVEALPLLGSGKLDLK 1135
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
130-581 |
9.42e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 120.17 E-value: 9.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 130 AAWMSGGTAVPLFRKHPQSELEYIISDSQSSLLVAGHPYAGTLEPLalKLGLPCL---TLPPTSNLGTLDGTDTQEKEAA 206
Cdd:PRK07867 73 AAALSGIVPVGLNPTRRGAALARDIAHADCQLVLTESAHAELLDGL--DPGVRVInvdSPAWADELAAHRDAEPPFRVAD 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 207 itdwADRPAMIIYTSGTTGRPKGVLHMHSNIQAMVQGLVSEWAWTRDDVILHTLPLHHVHGIVNKLLCPLWVGATCVMLP 286
Cdd:PRK07867 151 ----PDDLFMLIFTSGTSGDPKAVRCTHRKVASAGVMLAQRFGLGPDDVCYVSMPLFHSNAVMAGWAVALAAGASIALRR 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 287 EFQPqkvwemllSSKAPMVNVFMAVPTIY-SKLIQYYdqhFTQPHVKDfvravckER---IRLMVsGSAALPlPTLQRWE 362
Cdd:PRK07867 227 KFSA--------SGFLPDVRRYGATYANYvGKPLSYV---LATPERPD-------DAdnpLRIVY-GNEGAP-GDIARFA 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 363 EITGHTLLERYGMTEIGMALSNPLKGPriPGAVGSPLPRVEVRIVMNNTTNTTIVLGDHRNTRVCPGLegkeGELL-VRG 441
Cdd:PRK07867 287 RRFGCVVVDGFGSTEGGVAITRTPDTP--PGALGPLPPGVAIVDPDTGTECPPAEDADGRLLNADEAI----GELVnTAG 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 442 PSVFKEYWNKPQETRESfIDGGWFKTGDtVVYKD--GVYWIMGRSSvDIIKSAGYKISALEVERHLLAHPDIIDVAVIGA 519
Cdd:PRK07867 361 PGGFEGYYNDPEADAER-MRGGVYWSGD-LAYRDadGYAYFAGRLG-DWMRVDGENLGTAPIERILLRYPDATEVAVYAV 437
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1250165799 520 PDAIWGQKVTAVVQLRKGQSMTLPDLKTW--AREHMAPYTIPTGLLLVEEMPRNQMGKVNKKDL 581
Cdd:PRK07867 438 PDPVVGDQVMAALVLAPGAKFDPDAFAEFlaAQPDLGPKQWPSYVRVCAELPRTATFKVLKRQL 501
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
212-576 |
2.26e-28 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 120.14 E-value: 2.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 212 DRPAMIIYTSGTTGRPKGVLHMHSNIQAMVQGLVSE-WAWTRDDVILHTLPLHHVHGIVNKLLCPLWVGATCVMLPEFQP 290
Cdd:PRK06060 145 DALAYATYTSGTTGPPKAAIHRHADPLTFVDAMCRKaLRLTPEDTGLCSARMYFAYGLGNSVWFPLATGGSAVINSAPVT 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 291 QKVWEMLLSSKAPmvNVFMAVPTIYSKLIqyydqhftqphvkDFVRAVCKERIRLMVSGSAALPLPTLQRWEEITGHT-L 369
Cdd:PRK06060 225 PEAAAILSARFGP--SVLYGVPNFFARVI-------------DSCSPDSFRSLRCVVSAGEALELGLAERLMEFFGGIpI 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 370 LERYGMTEIGMA-LSNPLKGPRiPGAVGSPLPRVEVRIVMNNTTNTTivlgdhrntrvcpglEGKEGELLVRGPSVFKEY 448
Cdd:PRK06060 290 LDGIGSTEVGQTfVSNRVDEWR-LGTLGRVLPPYEIRVVAPDGTTAG---------------PGVEGDLWVRGPAIAKGY 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 449 WNKPQETREsfiDGGWFKTGDTVVYKDGVYWIMGRSSVDIIKSAGYKISALEVERHLLAHPDIIDVAVIGAPDAIWGQKV 528
Cdd:PRK06060 354 WNRPDSPVA---NEGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTL 430
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1250165799 529 TAVVQLRKGQSM---TLPDLKTWAREHMAPYTIPTGLLLVEEMPRNQMGKV 576
Cdd:PRK06060 431 QAFLVATSGATIdgsVMRDLHRGLLNRLSAFKVPHRFAVVDRLPRTPNGKL 481
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
65-583 |
3.13e-28 |
|
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: 117.41 E-value: 3.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 65 RAPAFGDKPAIIDSSGSHSYKQLYCSSLGLAGRIstalnLDFGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLFRK 144
Cdd:cd17653 6 IAAAHPDAVAVESLGGSLTYGELDAASNALANRL-----LQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 145 HPQSELEYIISDSQSSLLVAghpyagtleplalklglpcltlpptsnlgtldgtdtqekeaaiTDWADRPAMIIYTSGTT 224
Cdd:cd17653 81 LPSARIQAILRTSGATLLLT-------------------------------------------TDSPDDLAYIIFTSGST 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 225 GRPKGVLHMHSNIQAMVQglvsewaWTRDDviLHTLP---LHHVHGI-----VNKLLCPLWVGATCVMLPEFQPqkvwem 296
Cdd:cd17653 118 GIPKGVMVPHRGVLNYVS-------QPPAR--LDVGPgsrVAQVLSIafdacIGEIFSTLCNGGTLVLADPSDP------ 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 297 lLSSKAPMVNVFMAVPTIYSKLiqyydqhftqpHVKDFvravckERIRLMVSGSAALPLPTLQRWEEitGHTLLERYGMT 376
Cdd:cd17653 183 -FAHVARTVDALMSTPSILSTL-----------SPQDF------PNLKTIFLGGEAVPPSLLDRWSP--GRRLYNAYGPT 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 377 EIGMALSNPLKGPRIPGAVGSPLPRVEVRIVmnnttnttivlgdHRNTRvcPGLEGKEGELLVRGPSVFKEYWNKPQETR 456
Cdd:cd17653 243 ECTISSTMTELLPGQPVTIGKPIPNSTCYIL-------------DADLQ--PVPEGVVGEICISGVQVARGYLGNPALTA 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 457 ESFIDGGW------FKTGDTVVY-KDGVYWIMGRSSVDIiKSAGYKISALEVERHLLAHPDII-DVAVIGAPDAIWGQKV 528
Cdd:cd17653 308 SKFVPDPFwpgsrmYRTGDYGRWtEDGGLEFLGREDNQV-KVRGFRINLEEIEEVVLQSQPEVtQAAAIVVNGRLVAFVT 386
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1250165799 529 TAVVQLRkgqsmtlpDLKTWAREHMAPYTIPTGLLLVEEMPRNQMGKVNKKDLLR 583
Cdd:cd17653 387 PETVDVD--------GLRSELAKHLPSYAVPDRIIALDSFPLTANGKVDRKALRE 433
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
71-581 |
3.55e-28 |
|
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: 117.57 E-value: 3.55e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 71 DKPAIIDSSGSHSYKQLYCSSLGLAgRISTALNLDFGGLEGkrisfLCANDASYT-VAQWAAWMSGGTAVPLFRKHPQSE 149
Cdd:cd17650 2 DAIAVSDATRQLTYRELNERANQLA-RTLRGLGVAPGSVVG-----VCADRSLDAiVGLLAVLKAGGAYVPIDPDYPAER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 150 LEYIISDSQSSLLvaghpyagtleplalklglpcLTLPptsnlgtldgtdtqekeaaitdwaDRPAMIIYTSGTTGRPKG 229
Cdd:cd17650 76 LQYMLEDSGAKLL---------------------LTQP------------------------EDLAYVIYTSGTTGKPKG 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 230 VLHMHSNIQAMVQGLVSEWAWTRDDVILHTLPLHHVHGIVNKLLCPLWVGATCVMLPE---FQPQKVWEMLLSSKApmvN 306
Cdd:cd17650 111 VMVEHRNVAHAAHAWRREYELDSFPVRLLQMASFSFDVFAGDFARSLLNGGTLVICPDevkLDPAALYDLILKSRI---T 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 307 VFMAVPTIYSKLIQYYDQHFTQPhvkdfvravckERIRLMVSGSAALPLPTLQR-WEEITGHT-LLERYGMTE--IGMAL 382
Cdd:cd17650 188 LMESTPALIRPVMAYVYRNGLDL-----------SAMRLLIVGSDGCKAQDFKTlAARFGQGMrIINSYGVTEatIDSTY 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 383 SNPLKGPRIPGA---VGSPLPrvevrivmnnttNTTI-VLGDHRNtrvcPGLEGKEGELLVRGPSVFKEYWNKPQETRES 458
Cdd:cd17650 257 YEEGRDPLGDSAnvpIGRPLP------------NTAMyVLDERLQ----PQPVGVAGELYIGGAGVARGYLNRPELTAER 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 459 FID------GGWFKTGDTVVYK-DGVYWIMGRSSvDIIKSAGYKISALEVERHLLAHPDIIDVAVIGAPDAiwGQKVTAV 531
Cdd:cd17650 321 FVEnpfapgERMYRTGDLARWRaDGNVELLGRVD-HQVKIRGFRIELGEIESQLARHPAIDEAVVAVREDK--GGEARLC 397
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1250165799 532 VQLRKGQSMTLPDLKTWAREHMAPYTIPTGLLLVEEMPRNQMGKVNKKDL 581
Cdd:cd17650 398 AYVVAAATLNTAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
215-469 |
7.84e-28 |
|
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: 117.70 E-value: 7.84e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 215 AMIIYTSGTTGRPKGVLHMHSNIQAMVQGLVSEW----AWTRDDVILHTLPLHHV--HGIVNKLLC-----PLWVGATCV 283
Cdd:cd05927 117 ATICYTSGTTGNPKGVMLTHGNIVSNVAGVFKILeilnKINPTDVYISYLPLAHIfeRVVEALFLYhgakiGFYSGDIRL 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 284 MLPEFQPQKvwemllsskaPmvNVFMAVPTIYSKLiqyYDQHFTQPHVKDFVR------------------AVCKE---- 341
Cdd:cd05927 197 LLDDIKALK----------P--TVFPGVPRVLNRI---YDKIFNKVQAKGPLKrklfnfalnyklaelrsgVVRASpfwd 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 342 -------------RIRLMVSGSAALPLPTLQRWEEITGHTLLERYGMTEI--GMALSNPlkGPRIPGAVGSPLPRVEVRI 406
Cdd:cd05927 262 klvfnkikqalggNVRLMLTGSAPLSPEVLEFLRVALGCPVLEGYGQTECtaGATLTLP--GDTSVGHVGGPLPCAEVKL 339
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1250165799 407 V----MNNTTnttivlgdhrnTRVCPglegkEGELLVRGPSVFKEYWNKPQETRESFIDGGWFKTGD 469
Cdd:cd05927 340 VdvpeMNYDA-----------KDPNP-----RGEVCIRGPNVFSGYYKDPEKTAEALDEDGWLHTGD 390
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
211-576 |
1.30e-27 |
|
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: 117.42 E-value: 1.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 211 ADRPAMIIYTSGTTGRPKGVL-----HM------HSNIQAMVQGLVseWaWTRDD---VILHTLPlhhVHGivnkllcPL 276
Cdd:cd05967 229 ATDPLYILYTSGTTGKPKGVVrdnggHAvalnwsMRNIYGIKPGDV--W-WAASDvgwVVGHSYI---VYG-------PL 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 277 WVGATCVM---LPEFQPQK-VWEMLLSSKApmVNVFMAVPTIYsKLIQYYDQHftqphvKDFVRAVCKERIRLMVSGSAA 352
Cdd:cd05967 296 LHGATTVLyegKPVGTPDPgAFWRVIEKYQ--VNALFTAPTAI-RAIRKEDPD------GKYIKKYDLSSLRTLFLAGER 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 353 LPLPTLQRWEEITGHTLLERYGMTEIGMALSNPLKG----PRIPGAVGSPLPRVEVRIVmnnttnttivlgDHRNTRVCP 428
Cdd:cd05967 367 LDPPTLEWAENTLGVPVIDHWWQTETGWPITANPVGleplPIKAGSPGKPVPGYQVQVL------------DEDGEPVGP 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 429 GlegKEGELLVRGP---SVFKEYWNKPQETRESFI--DGGWFKTGDTVVY-KDGVYWIMGRSSvDIIKSAGYKISALEVE 502
Cdd:cd05967 435 N---ELGNIVIKLPlppGCLLTLWKNDERFKKLYLskFPGYYDTGDAGYKdEDGYLFIMGRTD-DVINVAGHRLSTGEME 510
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1250165799 503 RHLLAHPDIIDVAVIGAPDAIWGQKVTAVVQLRKGQSMTLPDLKT----WAREHMAPYTIPTGLLLVEEMPRNQMGKV 576
Cdd:cd05967 511 ESVLSHPAVAECAVVGVRDELKGQVPLGLVVLKEGVKITAEELEKelvaLVREQIGPVAAFRLVIFVKRLPKTRSGKI 588
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
219-585 |
1.39e-27 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 116.73 E-value: 1.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 219 YTSGTTGRPKGVLHMH--SNIQAMVQGLVSEWAWTRDDVILHTLPLHHVHGIVNKLLCPLwVGATCVML-PEFQPQKVWE 295
Cdd:PRK07008 183 YTSGTTGNPKGALYSHrsTVLHAYGAALPDAMGLSARDAVLPVVPMFHVNAWGLPYSAPL-TGAKLVLPgPDLDGKSLYE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 296 MLLSSKapmVNVFMAVPTIYSKLIQYydqhfTQPHVKDFvravckERIRLMVSGSAALPLPTLQRWEEITGHTLLERYGM 375
Cdd:PRK07008 262 LIEAER---VTFSAGVPTVWLGLLNH-----MREAGLRF------STLRRTVIGGSACPPAMIRTFEDEYGVEVIHAWGM 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 376 TEI---GMALSNPLKGPRIPGAV--------GSPLPRVEVRIVmnnttnttivlgdhrntrvcpGLEGKE--------GE 436
Cdd:PRK07008 328 TEMsplGTLCKLKWKHSQLPLDEqrkllekqGRVIYGVDMKIV---------------------GDDGRElpwdgkafGD 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 437 LLVRGPSVFKEYWNKpqetRESFIDGGWFKTGDTV-VYKDGVYWIMGRSSvDIIKSAGYKISALEVERHLLAHPDIIDVA 515
Cdd:PRK07008 387 LQVRGPWVIDRYFRG----DASPLVDGWFPTGDVAtIDADGFMQITDRSK-DVIKSGGEWISSIDIENVAVAHPAVAEAA 461
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 516 VIGAPDAIWGQKVTAVVQLRKGQSMTLPDLKTWAREHMAPYTIPTGLLLVEEMPRNQMGKVNKKDLLRHF 585
Cdd:PRK07008 462 CIACAHPKWDERPLLVVVKRPGAEVTREELLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKLREQF 531
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
211-552 |
2.93e-27 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 116.15 E-value: 2.93e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 211 ADRPAMIIYTSGTTGRPKGVLHMHSNIQAMVQGLVSEWAWTRDDVILHTLPLHHVHGIVnkllcplwVGATCVmLPEF-- 288
Cdd:PRK09274 173 PDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEIDLPTFPLFALFGPA--------LGMTSV-IPDMdp 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 289 ------QPQKVWEMLLSSKapmVNVFMAVPTIYSKLIQYYDQHftqPHVKDFVRAVckerirlmVSGSAALPLPTLQRWE 362
Cdd:PRK09274 244 trpatvDPAKLFAAIERYG---VTNLFGSPALLERLGRYGEAN---GIKLPSLRRV--------ISAGAPVPIAVIERFR 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 363 EITGHT--LLERYGMTE------IGMalSNPLKGPRI---PGA---VGSPLPRVEVRIVmnNTTNTTIVLGDhrNTRVCP 428
Cdd:PRK09274 310 AMLPPDaeILTPYGATEalpissIES--REILFATRAatdNGAgicVGRPVDGVEVRII--AISDAPIPEWD--DALRLA 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 429 glEGKEGELLVRGPSVFKEYWNKPQETRESFIDGG----WFKTGDtVVYKD--GVYWIMGRSSvDIIKSAGYKISALEVE 502
Cdd:PRK09274 384 --TGEIGEIVVAGPMVTRSYYNRPEATRLAKIPDGqgdvWHRMGD-LGYLDaqGRLWFCGRKA-HRVETAGGTLYTIPCE 459
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1250165799 503 RHLLAHPDIIDVAVIGAPDAIwGQKVTAVVQLRKGQSMTLP----DLKTWAREH 552
Cdd:PRK09274 460 RIFNTHPGVKRSALVGVGVPG-AQRPVLCVELEPGVACSKSalyqELRALAAAH 512
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
71-581 |
6.40e-27 |
|
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: 113.95 E-value: 6.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 71 DKPAIIDSSGSHSYKQLYCSSLGLAGRISTAlnldfGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLFRKHPQSEL 150
Cdd:cd12115 14 DAIALVCGDESLTYAELNRRANRLAARLRAA-----GVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPERL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 151 EYIISDSQSSLLvaghpyagtleplalklglpcltlpptsnlgtldgtdtqekeaaITDwADRPAMIIYTSGTTGRPKGV 230
Cdd:cd12115 89 RFILEDAQARLV--------------------------------------------LTD-PDDLAYVIYTSGSTGRPKGV 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 231 LHMHSNIQAMVQglvseWAwtrddviLHTLPLHHVHGI-----------VNKLLCPLWVGATCVMLpefqpQKVWEMLLS 299
Cdd:cd12115 124 AIEHRNAAAFLQ-----WA-------AAAFSAEELAGVlastsicfdlsVFELFGPLATGGKVVLA-----DNVLALPDL 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 300 SKAPMVNVFMAVPTIYSKLIQyydqhftQPHVKDFVRAVCkerirlmvsgSAALPLPTlQRWEEITGHTLLER----YGM 375
Cdd:cd12115 187 PAAAEVTLINTVPSAAAELLR-------HDALPASVRVVN----------LAGEPLPR-DLVQRLYARLQVERvvnlYGP 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 376 TE-----IGMALSnplKGPRIPGAVGSPLPrvevrivmnnttNTTI-VLGDHRNtrvcPGLEGKEGELLVRGPSVFKEYW 449
Cdd:cd12115 249 SEdttysTVAPVP---PGASGEVSIGRPLA------------NTQAyVLDRALQ----PVPLGVPGELYIGGAGVARGYL 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 450 NKPQETRESFIDGGW------FKTGDTVVYK-DGVYWIMGRSSvDIIKSAGYKISALEVERHLLAHPDIIDVAVIGAPDA 522
Cdd:cd12115 310 GRPGLTAERFLPDPFgpgarlYRTGDLVRWRpDGLLEFLGRAD-NQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDA 388
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1250165799 523 IWGQKVTAVVQLRKGQSMTLPDLKTWAREHMAPYTIPTGLLLVEEMPRNQMGKVNKKDL 581
Cdd:cd12115 389 AGERRLVAYIVAEPGAAGLVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
219-583 |
6.87e-27 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 114.94 E-value: 6.87e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 219 YTSGTTGRPKGVLHMHSNIQAMVQGLVSEWAWTRDDVILHTLPLHHVHGivnklLCPLWVGA----TCVMLPEFQPQKVW 294
Cdd:PLN02479 202 YTSGTTASPKGVVLHHRGAYLMALSNALIWGMNEGAVYLWTLPMFHCNG-----WCFTWTLAalcgTNICLRQVTAKAIY 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 295 EMLLSSKapmVNVFMAVPTIYSKLIQY--YDQHFTQPHVkdfvravckerIRLMVSGSAalPLPTLQRWEEITGHTLLER 372
Cdd:PLN02479 277 SAIANYG---VTHFCAAPVVLNTIVNApkSETILPLPRV-----------VHVMTAGAA--PPPSVLFAMSEKGFRVTHT 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 373 YGMTEIgmalsnplKGP-----------RIPGAVGSPL-PRVEVRIVMNNTTNTTivlgDHRNTRVCPGLEGKEGELLVR 440
Cdd:PLN02479 341 YGLSET--------YGPstvcawkpewdSLPPEEQARLnARQGVRYIGLEGLDVV----DTKTMKPVPADGKTMGEIVMR 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 441 GPSVFKEYWNKPQETRESFiDGGWFKTGDTVV-YKDGVYWIMGRSSvDIIKSAGYKISALEVERHLLAHPDIIDVAVIGA 519
Cdd:PLN02479 409 GNMVMKGYLKNPKANEEAF-ANGWFHSGDLGVkHPDGYIEIKDRSK-DIIISGGENISSLEVENVVYTHPAVLEASVVAR 486
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1250165799 520 PDAIWGQKVTAVVQLRKG-----QSMTLPDLKTWAREHMAPYTIPTGLLLvEEMPRNQMGKVnKKDLLR 583
Cdd:PLN02479 487 PDERWGESPCAFVTLKPGvdksdEAALAEDIMKFCRERLPAYWVPKSVVF-GPLPKTATGKI-QKHVLR 553
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
71-587 |
1.09e-26 |
|
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: 113.41 E-value: 1.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 71 DKPAIIDSSGSHSYKQLYCSSLGLAGRISTAlnldfgGLEGKRISFLCANDASYT-VAQWAAWMSGGTAVPLFRKHPQSE 149
Cdd:cd05918 14 DAPAVCAWDGSLTYAELDRLSSRLAHHLRSL------GVGPGVFVPLCFEKSKWAvVAMLAVLKAGGAFVPLDPSHPLQR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 150 LEYIISDSQSSLLVAGHPyagtleplalklglpcltlpptsnlgtldgtdtqekeaaitdwaDRPAMIIYTSGTTGRPKG 229
Cdd:cd05918 88 LQEILQDTGAKVVLTSSP--------------------------------------------SDAAYVIFTSGSTGKPKG 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 230 VLHMHSNIQAMVQGLVSEWAWTRDDVIL----HTLPLHhvhgiVNKLLCPLWVGAT-CVM--------LPEFqpqkVWEM 296
Cdd:cd05918 124 VVIEHRALSTSALAHGRALGLTSESRVLqfasYTFDVS-----ILEIFTTLAAGGClCIPseedrlndLAGF----INRL 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 297 llsskapMVNVFMAVPTIySKLIQyydqhftqPhvKDFVRavckerIRLMVSGSAALPLPTLQRWEEitGHTLLERYGMT 376
Cdd:cd05918 195 -------RVTWAFLTPSV-ARLLD--------P--EDVPS------LRTLVLGGEALTQSDVDTWAD--RVRLINAYGPA 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 377 E--IGMALSNPLKGPRiPGAVGSPLPrvevrivmnntTNTTIV-LGDHrnTRVCPglEGKEGELLVRGPSVFKEYWNKPQ 453
Cdd:cd05918 249 EctIAATVSPVVPSTD-PRNIGRPLG-----------ATCWVVdPDNH--DRLVP--IGAVGELLIEGPILARGYLNDPE 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 454 ETRESFIDG-GW------------FKTGDTVVY-KDGVYWIMGRSSvDIIKSAGYKISALEVERHLLAHPD---IIDVAV 516
Cdd:cd05918 313 KTAAAFIEDpAWlkqegsgrgrrlYRTGDLVRYnPDGSLEYVGRKD-TQVKIRGQRVELGEIEHHLRQSLPgakEVVVEV 391
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 517 IGAPDAIWGQKVTAVVQLR-------KGQSMTLP----------DLKTWAREHMAPYTIPTGLLLVEEMPRNQMGKVNKK 579
Cdd:cd05918 392 VKPKDGSSSPQLVAFVVLDgsssgsgDGDSLFLEpsdefralvaELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRR 471
|
....*...
gi 1250165799 580 dLLRHFFQ 587
Cdd:cd05918 472 -ALRELAE 478
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
130-581 |
4.01e-26 |
|
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: 111.76 E-value: 4.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 130 AAWMSGGTAVPLFRKHPQSELEYIISDSQSSLLvaghpyagtleplalklglpcLTLPptSNLgtldgtdtqekeaaitd 209
Cdd:cd17644 69 AILKAGGAYVPLDPNYPQERLTYILEDAQISVL---------------------LTQP--ENL----------------- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 210 wadrpAMIIYTSGTTGRPKGVLHMHSNIQAMVQGLVSEWAWTRDDVILHTLPLhHVHGIVNKLLCPLWVGATCVMLPE-- 287
Cdd:cd17644 109 -----AYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEYGITSSDRVLQFASI-AFDVAAEEIYVTLLSGATLVLRPEem 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 288 -FQPQKVWEMLLSSKAPMVNvfmaVPTIYSKLIqyydqhftqphVKDFVRAVCK--ERIRLMVSGSAALPLPTLQRWEEI 364
Cdd:cd17644 183 rSSLEDFVQYIQQWQLTVLS----LPPAYWHLL-----------VLELLLSTIDlpSSLRLVIVGGEAVQPELVRQWQKN 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 365 TGH--TLLERYGMTEIGMA-----LSNPLKGPRIPGAVGSPLPRVEVRIVMNNTTNTTIvlgdhrntrvcpgleGKEGEL 437
Cdd:cd17644 248 VGNfiQLINVYGPTEATIAatvcrLTQLTERNITSVPIGRPIANTQVYILDENLQPVPV---------------GVPGEL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 438 LVRGPSVFKEYWNKPQETRESFIDGGW--------FKTGDTVVY-KDGVYWIMGRssVD-IIKSAGYKISALEVERHLLA 507
Cdd:cd17644 313 HIGGVGLARGYLNRPELTAEKFISHPFnsseserlYKTGDLARYlPDGNIEYLGR--IDnQVKIRGFRIELGEIEAVLSQ 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1250165799 508 HPDIIDVAVIGAPDAIWGQKVTAVVQLRKGQSMTLPDLKTWAREHMAPYTIPTGLLLVEEMPRNQMGKVNKKDL 581
Cdd:cd17644 391 HNDVKTAVVIVREDQPGNKRLVAYIVPHYEESPSTVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
200-576 |
3.01e-25 |
|
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: 110.27 E-value: 3.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 200 TQEKEAAITDwADRPAMIIYTSGTTGRPKGVLHMHSN--IQAmVQGLVSEWAWTRDDVILHTLPLHHVHG---IVNKLLc 274
Cdd:cd05968 225 TAGDGAERTE-SEDPLMIIYTSGTTGKPKGTVHVHAGfpLKA-AQDMYFQFDLKPGDLLTWFTDLGWMMGpwlIFGGLI- 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 275 plwVGATCVM---LPEF-QPQKVWEMLLSSKAPMVNVfmaVPTIYSKLIqyydqhftqPHVKDFVRAVCKERIRLMVS-G 349
Cdd:cd05968 302 ---LGATMVLydgAPDHpKADRLWRMVEDHEITHLGL---SPTLIRALK---------PRGDAPVNAHDLSSLRVLGStG 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 350 SAALPLPTLQRWEEI-TGHTLLERY-GMTEI-GMALSNPLKGPRIPGAVGSPLPRVEVRIVmnnttnttivlgDHRNTRV 426
Cdd:cd05968 367 EPWNPEPWNWLFETVgKGRNPIINYsGGTEIsGGILGNVLIKPIKPSSFNGPVPGMKADVL------------DESGKPA 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 427 CPglegKEGELLVRGP--SVFKEYWNKPQ---ETRESFIDGGWFKtGDTVVY-KDGVYWIMGRSSvDIIKSAGYKISALE 500
Cdd:cd05968 435 RP----EVGELVLLAPwpGMTRGFWRDEDrylETYWSRFDNVWVH-GDFAYYdEEGYFYILGRSD-DTINVAGKRVGPAE 508
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1250165799 501 VERHLLAHPDIIDVAVIGAPDAIWGQKVTAVVQLRKGQSMT---LPDLKTWAREHMAPYTIPTGLLLVEEMPRNQMGKV 576
Cdd:cd05968 509 IESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVLKPGVTPTealAEELMERVADELGKPLSPERILFVKDLPKTRNAKV 587
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
126-587 |
5.73e-25 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 110.64 E-value: 5.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 126 VAQWAAWMSGGTAVPLFRKHPQSELEYIISDSQSSLLVAghpYAGTLEPLALKLGLPCLTLpptsNLGTLDGtDTQEKEA 205
Cdd:PRK12467 3160 VALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLLT---QAHLLEQLPAPAGDTALTL----DRLDLNG-YSENNPS 3231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 206 AITDwADRPAMIIYTSGTTGRPKGVLHMHSNIQAMVQGLVSEWAWTRDDVILHTLPLhHVHGIVNKLLCPLWVGATCVML 285
Cdd:PRK12467 3232 TRVM-GENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDRVLLFMSF-SFDGAQERFLWTLICGGCLVVR 3309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 286 P--EFQPQKVWEMLLsskAPMVNVFMAVPTiyskliqyYDQHFTQPHvkdfVRAVCKeRIRLMVSGSAALPLPTLQRWE- 362
Cdd:PRK12467 3310 DndLWDPEELWQAIH---AHRISIACFPPA--------YLQQFAEDA----GGADCA-SLDIYVFGGEAVPPAAFEQVKr 3373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 363 EITGHTLLERYGMTEigmALSNPL----KGPRIPGAVGSPLPRvevrivmnNTTNTTIVLGDhrnTRVCPGLEGKEGELL 438
Cdd:PRK12467 3374 KLKPRGLTNGYGPTE---AVVTVTlwkcGGDAVCEAPYAPIGR--------PVAGRSIYVLD---GQLNPVPVGVAGELY 3439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 439 VRGPSVFKEYWNKPQETRESFI-------DGGWFKTGDTVVYK-DGVYWIMGRssVD-IIKSAGYKISALEVERHLLAHP 509
Cdd:PRK12467 3440 IGGVGLARGYHQRPSLTAERFVadpfsgsGGRLYRTGDLARYRaDGVIEYLGR--IDhQVKIRGFRIELGEIEARLLQHP 3517
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 510 DIIDVAVIGAPDAIWGQKVTAVV----------QLRKGQSMTLPDlktwarehmapYTIPTGLLLVEEMPRNQMGKVNKK 579
Cdd:PRK12467 3518 SVREAVVLARDGAGGKQLVAYVVpadpqgdwreTLRDHLAASLPD-----------YMVPAQLLVLAAMPLGPNGKVDRK 3586
|
....*...
gi 1250165799 580 DLLRHFFQ 587
Cdd:PRK12467 3587 ALPDPDAK 3594
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
65-581 |
5.76e-25 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 110.64 E-value: 5.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 65 RAPAFGDKPAIIDSSGSHSYKQLYcsslGLAGRISTALNLDFGGLEgKRISFLCANDASYTVAQWAAWMSGGTAVPLFRK 144
Cdd:PRK05691 2197 QAARTPQAPALTFAGQTLSYAELD----ARANRLARALRERGVGPQ-VRVGLALERSLEMVVGLLAILKAGGAYVPLDPE 2271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 145 HPQSELEYIISDSQSSLLVAGHPYAGTLEPL-------ALKLGLPCLTLPPTSNLGTLDGTDTQekeaaitdwadrpAMI 217
Cdd:PRK05691 2272 YPLERLHYMIEDSGIGLLLSDRALFEALGELpagvarwCLEDDAAALAAYSDAPLPFLSLPQHQ-------------AYL 2338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 218 IYTSGTTGRPKGVLHMHSNIQAMVQGLVSEWAWTRDDVILHTLPLHhVHGIVNKLLCPLWVGATCVMlpefQPQKVW--- 294
Cdd:PRK05691 2339 IYTSGSTGKPKGVVVSHGEIAMHCQAVIERFGMRADDCELHFYSIN-FDAASERLLVPLLCGARVVL----RAQGQWgae 2413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 295 EMLLSSKAPMVNVFMAVPTIYSKLIQYY-DQHFTQPhvkdfvravckerIRLMVSGSAALPLPTLQRWEEITGHTLL-ER 372
Cdd:PRK05691 2414 EICQLIREQQVSILGFTPSYGSQLAQWLaGQGEQLP-------------VRMCITGGEALTGEHLQRIRQAFAPQLFfNA 2480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 373 YGMTE-IGMALSNpLKGPRIPGAVGS-PLPRVevrivmnnttnttivLGDHR----NTRVCPGLEGKEGELLVRGPSVFK 446
Cdd:PRK05691 2481 YGPTEtVVMPLAC-LAPEQLEEGAASvPIGRV---------------VGARVayilDADLALVPQGATGELYVGGAGLAQ 2544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 447 EYWNKPQETRESFI------DGG-WFKTGDTVVYK-DGVYWIMGRSSVDIiKSAGYKISALEVERHLLAHPDIIDVAVIg 518
Cdd:PRK05691 2545 GYHDRPGLTAERFVadpfaaDGGrLYRTGDLVRLRaDGLVEYVGRIDHQV-KIRGFRIELGEIESRLLEHPAVREAVVL- 2622
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1250165799 519 APDAIWGQK-----VTAVVQLRKGQSMTLPD-LKTWAREHMAPYTIPTGLLLVEEMPRNQMGKVNKKDL 581
Cdd:PRK05691 2623 ALDTPSGKQlagylVSAVAGQDDEAQAALREaLKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRAL 2691
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
215-469 |
6.75e-25 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 109.42 E-value: 6.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 215 AMIIYTSGTTGRPKGVLHMHSNIQAMVQGLVSEWAWTRDDVILHTLPLHHVHGIVNKLLCpLWVGATCvmlpEFQPQKVW 294
Cdd:PLN02736 224 ATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTKFYPSDVHISYLPLAHIYERVNQIVM-LHYGVAV----GFYQGDNL 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 295 EMLLSSKAPMVNVFMAVPTIYSKLiqyYD----------------------------QHFTQPH------VKDFVRAVCK 340
Cdd:PLN02736 299 KLMDDLAALRPTIFCSVPRLYNRI---YDgitnavkesgglkerlfnaaynakkqalENGKNPSpmwdrlVFNKIKAKLG 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 341 ERIRLMVSGSAALPLPTLQRWEEITGHTLLERYGMTEIGMALSNPLKGPRIPGAVGSPLPRVEVRIV----MNNTTNtti 416
Cdd:PLN02736 376 GRVRFMSSGASPLSPDVMEFLRICFGGRVLEGYGMTETSCVISGMDEGDNLSGHVGSPNPACEVKLVdvpeMNYTSE--- 452
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1250165799 417 vlgDHRNTRvcpglegkeGELLVRGPSVFKEYWNKPQETRESFIDGGWFKTGD 469
Cdd:PLN02736 453 ---DQPYPR---------GEICVRGPIIFKGYYKDEVQTREVIDEDGWLHTGD 493
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
192-475 |
3.01e-24 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 107.27 E-value: 3.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 192 LGTLDGTDTQEKEAAITdwADRPAMIIYTSGTTGRPKGVLHMHSNIQAMVQGLVSEWAWTRDD--VILHTLPLHHVHGIV 269
Cdd:PRK08180 191 LATPPTAAVDAAHAAVG--PDTIAKFLFTSGSTGLPKAVINTHRMLCANQQMLAQTFPFLAEEppVLVDWLPWNHTFGGN 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 270 NKLLCPLWVGATcVMLPEFQP--QKVWEML--LSSKAPmvNVFMAVPTIYSKLIQYYDQhftqphvKDFVRAVCKERIRL 345
Cdd:PRK08180 269 HNLGIVLYNGGT-LYIDDGKPtpGGFDETLrnLREISP--TVYFNVPKGWEMLVPALER-------DAALRRRFFSRLKL 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 346 MVSGSAALPLPTLQRWEEITGHTLLER------YGMTEIG-MALS--NPLKGPripGAVGSPLPRVEVRIVMNNttntti 416
Cdd:PRK08180 339 LFYAGAALSQDVWDRLDRVAEATCGERirmmtgLGMTETApSATFttGPLSRA---GNIGLPAPGCEVKLVPVG------ 409
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1250165799 417 vlgdhrntrvcpgleGKEgELLVRGPSVFKEYWNKPQETRESFIDGGWFKTGDTVVYKD 475
Cdd:PRK08180 410 ---------------GKL-EVRVKGPNVTPGYWRAPELTAEAFDEEGYYRSGDAVRFVD 452
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
211-583 |
1.08e-23 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 105.61 E-value: 1.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 211 ADRPAMIIYTSGTTGRPKGVLHmhSNIQAMVQGLVS-EWA---------WTRDDV--IL-HTlplHHVHGivnkllcPLW 277
Cdd:PRK00174 244 AEDPLFILYTSGSTGKPKGVLH--TTGGYLVYAAMTmKYVfdykdgdvyWCTADVgwVTgHS---YIVYG-------PLA 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 278 VGATCVML---PEF-QPQKVWEMLLSSKapmVNVFMAVPTIYSKLIQYYDQHftqphVKDFVRAvckeRIRLMvsGSAAL 353
Cdd:PRK00174 312 NGATTLMFegvPNYpDPGRFWEVIDKHK---VTIFYTAPTAIRALMKEGDEH-----PKKYDLS----SLRLL--GSVGE 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 354 PL-PTLQRW-EEITGHtllER------YGMTEIGMALSNPLKG--PRIPGAVGSPLPRVEVRIVmNNTTNttivlgdhrn 423
Cdd:PRK00174 378 PInPEAWEWyYKVVGG---ERcpivdtWWQTETGGIMITPLPGatPLKPGSATRPLPGIQPAVV-DEEGN---------- 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 424 trVCPGleGKEGELLVRG--PSVFKEYWNKPQETRESF---IDGGWFkTGDTVVY-KDGVYWIMGRSSvDIIKSAGYKIS 497
Cdd:PRK00174 444 --PLEG--GEGGNLVIKDpwPGMMRTIYGDHERFVKTYfstFKGMYF-TGDGARRdEDGYYWITGRVD-DVLNVSGHRLG 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 498 ALEVERHLLAHPDIIDVAVIGAPDAIWGQKVTAVVQLRKGQ--SMTLP-DLKTWAREHMAPYTIPTGLLLVEEMPRNQMG 574
Cdd:PRK00174 518 TAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLKGGEepSDELRkELRNWVRKEIGPIAKPDVIQFAPGLPKTRSG 597
|
....*....
gi 1250165799 575 KVNKKdLLR 583
Cdd:PRK00174 598 KIMRR-ILR 605
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
134-581 |
2.76e-23 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 105.64 E-value: 2.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 134 SGGTAVPLFRKHPQSELEYIISDSQSSLLVAGHPYAGTLEPLALKLGLPCLTLpptsnlgTLDGTDTQEKEAAITDwaDR 213
Cdd:PRK05691 1204 AGGAYVPLDPDYPAERLAYMLADSGVELLLTQSHLLERLPQAEGVSAIALDSL-------HLDSWPSQAPGLHLHG--DN 1274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 214 PAMIIYTSGTTGRPKGVLHMHSNIQAMVQGLVSEWAWTRDDVILHTLPLHHvhgIVNKLLC--PLWVGATCVMLPEFQ-- 289
Cdd:PRK05691 1275 LAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKAPISF---DVSVWECfwPLITGCRLVLAGPGEhr 1351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 290 -PQKVWEMLlssKAPMVNVFMAVPTIYSKLIQyydqhftQPHVkdfvrAVCKeRIRLMVSGSAALPLPTLQR-WEEITGH 367
Cdd:PRK05691 1352 dPQRIAELV---QQYGVTTLHFVPPLLQLFID-------EPLA-----AACT-SLRRLFSGGEALPAELRNRvLQRLPQV 1415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 368 TLLERYGMTEIGMALSN----PLKGPRIPgaVGSPLPRVEVRivmnnttnttiVLGDHRNtrvcPGLEGKEGELLVRGPS 443
Cdd:PRK05691 1416 QLHNRYGPTETAINVTHwqcqAEDGERSP--IGRPLGNVLCR-----------VLDAELN----LLPPGVAGELCIGGAG 1478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 444 VFKEYWNKPQETRESFI------DGG-WFKTGDTVVYK-DGVYWIMGRSSVDiIKSAGYKISALEVERHLLAHPDIIDVA 515
Cdd:PRK05691 1479 LARGYLGRPALTAERFVpdplgeDGArLYRTGDRARWNaDGALEYLGRLDQQ-VKLRGFRVEPEEIQARLLAQPGVAQAA 1557
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1250165799 516 VIGAPDAIwGQKVTAVVQLRKGQSMTLPDLKTWAREHMAPYTIPTGLLLVEEMPRNQMGKVNKKDL 581
Cdd:PRK05691 1558 VLVREGAA-GAQLVGYYTGEAGQEAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRAL 1622
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
111-483 |
2.81e-23 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 105.25 E-value: 2.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 111 GKRISFLCANDASYTVAQWAAWMSGGTAVPLF-----RKHPQSELEYIISDSQSSLLVAGhpyAGTLEPLALKLGLPCLT 185
Cdd:PRK05691 64 GDRAVLLFPSGPDYVAAFFGCLYAGVIAVPAYppesaRRHHQERLLSIIADAEPRLLLTV---ADLRDSLLQMEELAAAN 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 186 LPPTSNLGTLDGTDTQEKEAAITDwADRPAMIIYTSGTTGRPKGVLHMHSNIQAmvqglvSEWAWTR--------DDVIL 257
Cdd:PRK05691 141 APELLCVDTLDPALAEAWQEPALQ-PDDIAFLQYTSGSTALPKGVQVSHGNLVA------NEQLIRHgfgidlnpDDVIV 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 258 HTLPLHHVHGIVNKLLCPLWVGATCVmlpefqpqkvwemLLSSkapmvNVFMAVPTIYSKLIQYYDQhfTQPHVKDFVRA 337
Cdd:PRK05691 214 SWLPLYHDMGLIGGLLQPIFSGVPCV-------------LMSP-----AYFLERPLRWLEAISEYGG--TISGGPDFAYR 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 338 VCKERI-------------RLMVSGSAALPLPTLQRWEE------ITGHTLLERYGMTEIGMALSNPLKGPRIP------ 392
Cdd:PRK05691 274 LCSERVsesalerldlsrwRVAYSGSEPIRQDSLERFAEkfaacgFDPDSFFASYGLAEATLFVSGGRRGQGIPalelda 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 393 ------------GAV----GSPLPRVEVRIVmnnTTNTTIVLGDHRntrvcpglegkEGELLVRGPSVFKEYWNKPQETR 456
Cdd:PRK05691 354 ealarnraepgtGSVlmscGRSQPGHAVLIV---DPQSLEVLGDNR-----------VGEIWASGPSIAHGYWRNPEASA 419
|
410 420 430
....*....|....*....|....*....|
gi 1250165799 457 ESFI--DG-GWFKTGDTVVYKDGVYWIMGR 483
Cdd:PRK05691 420 KTFVehDGrTWLRTGDLGFLRDGELFVTGR 449
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
71-581 |
3.37e-23 |
|
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: 102.94 E-value: 3.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 71 DKPAIIDSSGSHSYKQLYCSSLGLAGristalNLDFGGLEGKRISFLCAN-DASYTVAQWAAWMSGGTAVPLFRKHPQSE 149
Cdd:cd17656 3 DAVAVVFENQKLTYRELNERSNQLAR------FLREKGVKKDSIVAIMMErSAEMIVGILGILKAGGAFVPIDPEYPEER 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 150 LEYIISDSQSSLLV--AGHPYAGTLEPLALKLGLPCLTLPPTSNLgtldgtdtqekeaAITDWADRPAMIIYTSGTTGRP 227
Cdd:cd17656 77 RIYIMLDSGVRVVLtqRHLKSKLSFNKSTILLEDPSISQEDTSNI-------------DYINNSDDLLYIIYTSGTTGKP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 228 KGVLHMHSNiqaMVQGLVSEWAWTR----DDVILHTLPLHHV--HGIVNKLLcplwVGATCVMLPEFQPQKVWEML-LSS 300
Cdd:cd17656 144 KGVQLEHKN---MVNLLHFEREKTNinfsDKVLQFATCSFDVcyQEIFSTLL----SGGTLYIIREETKRDVEQLFdLVK 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 301 KAPMVNVFMavPTIYSKLIQYYDQHFtqphvKDFVRAVcKERI----RLMVSGsaalplpTLQRWEEITGHTLLERYGMT 376
Cdd:cd17656 217 RHNIEVVFL--PVAFLKFIFSEREFI-----NRFPTCV-KHIItageQLVITN-------EFKEMLHEHNVHLHNHYGPS 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 377 E---IGMALSNPlkGPRIP--GAVGSPLprvevrivmnntTNTTIVLGDHRNTrvcPGLEGKEGELLVRGPSVFKEYWNK 451
Cdd:cd17656 282 EthvVTTYTINP--EAEIPelPPIGKPI------------SNTWIYILDQEQQ---LQPQGIVGELYISGASVARGYLNR 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 452 PQETRESFI------DGGWFKTGDTVVY-KDGVYWIMGRSSvDIIKSAGYKISALEVERHLLAHPDIIDVAVIGAPDAIW 524
Cdd:cd17656 345 QELTAEKFFpdpfdpNERMYRTGDLARYlPDGNIEFLGRAD-HQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKG 423
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1250165799 525 GQKVTA-VVQLrkgQSMTLPDLKTWAREHMAPYTIPTGLLLVEEMPRNQMGKVNKKDL 581
Cdd:cd17656 424 EKYLCAyFVME---QELNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
218-581 |
1.84e-22 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 100.45 E-value: 1.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 218 IYTSGTTGRPKGVLHMHSNIQAMVQGLVSEWAWTRddviLHT---LPLHHVHGIVnKLLCPLWVGATCVMLP--EFQPQK 292
Cdd:PRK07445 126 IPTGGSSGQIRFAIHTWETLTASVQGFQRYFQLQQ----VNSfcvLPLYHVSGLM-QFMRSFLTGGKLVILPykRLKSGQ 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 293 VWEMLLSskapmvNVFMA-VPTIYSKLIQYYDQHFTQphvkdfVRAVckerirlMVSGSAALPlptlqrweeitghTLLE 371
Cdd:PRK07445 201 ELPPNPS------DFFLSlVPTQLQRLLQLRPQWLAQ------FRTI-------LLGGAPAWP-------------SLLE 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 372 R-----------YGMTEIG--MALSNP---LKGPRipgAVGSPLPRVEVRIVMNNTTNTTIvlgdhrntrvcpglegkeg 435
Cdd:PRK07445 249 QarqlqlrlaptYGMTETAsqIATLKPddfLAGNN---SSGQVLPHAQITIPANQTGNITI------------------- 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 436 ellvRGPSVFKEYWNKPQETRESFI--DGGWFKtgdtvvyKDGVYWIMGRSSVDIIkSAGYKISALEVERHLLAHPDIID 513
Cdd:PRK07445 307 ----QAQSLALGYYPQILDSQGIFEtdDLGYLD-------AQGYLHILGRNSQKII-TGGENVYPAEVEAAILATGLVQD 374
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1250165799 514 VAVIGAPDAIWGQKVTAVVQLrKGQSMTLPDLKTWAREHMAPYTIPTGLLLVEEMPRNQMGKVNKKDL 581
Cdd:PRK07445 375 VCVLGLPDPHWGEVVTAIYVP-KDPSISLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQL 441
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
71-581 |
2.16e-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: 100.32 E-value: 2.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 71 DKPAIIDSSGSHSYKQLYCSslglAGRISTALnLDFGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLFRKHPQSEL 150
Cdd:cd17645 13 DHVAVVDRGQSLTYKQLNEK----ANQLARHL-RGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGERI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 151 EYIISDSQSSLLVaghpyagtleplalklglpcltlpptSNLGTLdgtdtqekeaaitdwadrpAMIIYTSGTTGRPKGV 230
Cdd:cd17645 88 AYMLADSSAKILL--------------------------TNPDDL-------------------AYVIYTSGSTGLPKGV 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 231 LHMHsniqamvqglvsewawtrddvilhtlplhhvHGIVNklLCpLWVGATCVMLPEFQPQK---------VWEML--LS 299
Cdd:cd17645 123 MIEH-------------------------------HNLVN--LC-EWHRPYFGVTPADKSLVyasfsfdasAWEIFphLT 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 300 SKAPMVNVFMAVPTIYSKLIQYYDQH-----FTQPHVKDFVRAVCKERIRLMVSGSaalplPTLQRWEEiTGHTLLERYG 374
Cdd:cd17645 169 AGAALHVVPSERRLDLDALNDYFNQEgitisFLPTGAAEQFMQLDNQSLRVLLTGG-----DKLKKIER-KGYKLVNNYG 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 375 MTEIG-MALSNPLKGPRIPGAVGSPLPRVEVRIVmnnttnttivlgdHRNTRVCPglEGKEGELLVRGPSVFKEYWNKPQ 453
Cdd:cd17645 243 PTENTvVATSFEIDKPYANIPIGKPIDNTRVYIL-------------DEALQLQP--IGVAGELCIAGEGLARGYLNRPE 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 454 ETRESFIDGGW------FKTGDTVVY-KDGVYWIMGRssVD-IIKSAGYKISALEVERHLLAHPDIIDVAVIGAPDAIWG 525
Cdd:cd17645 308 LTAEKFIVHPFvpgermYRTGDLAKFlPDGNIEFLGR--LDqQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGR 385
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1250165799 526 QKVTAVVQLRKgqSMTLPDLKTWAREHMAPYTIPTGLLLVEEMPRNQMGKVNKKDL 581
Cdd:cd17645 386 KYLVAYVTAPE--EIPHEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
114-581 |
2.50e-22 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 100.87 E-value: 2.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 114 ISFLCANDASYTVAQWAAWMSGGTAVPLFRKHPQSELEYIISDSQSSLLVAGHPYAGTLEPLALKlGLPCLTLPPTSNLG 193
Cdd:PRK13388 55 VGVLLGNTPEMLFWLAAAALGGYVLVGLNTTRRGAALAADIRRADCQLLVTDAEHRPLLDGLDLP-GVRVLDVDTPAYAE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 194 TLDGTDTQEKEAAITdwADRPAMIIYTSGTTGRPKGVLHMHSNIQAMVQGLVSEWAWTRDDVILHTLPLHHVHGIVNKLL 273
Cdd:PRK13388 134 LVAAAGALTPHREVD--AMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLTRDDVCYVSMPLFHSNAVMAGWA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 274 CPLWVGATCVMLPEFQPqkvwemllSSKAPMVNVFMAVPTIY-SKLIQYYDQHFTQPHVKD--FVRAVckerirlmvsGS 350
Cdd:PRK13388 212 PAVASGAAVALPAKFSA--------SGFLDDVRRYGATYFNYvGKPLAYILATPERPDDADnpLRVAF----------GN 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 351 AALPlptlqrwEEIT------GHTLLERYGMTEIGMALSNPLKGPriPGAVGSPLPRVEVRIVMNNTTNTTIVLGDHrnT 424
Cdd:PRK13388 274 EASP-------RDIAefsrrfGCQVEDGYGSSEGAVIVVREPGTP--PGSIGRGAPGVAIYNPETLTECAVARFDAH--G 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 425 RVcpgLEGKE--GELLVR-GPSVFKEYWNKPQETRESfIDGGWFKTGDtVVYKDGVYWI--MGRSSvDIIKSAGYKISAL 499
Cdd:PRK13388 343 AL---LNADEaiGELVNTaGAGFFEGYYNNPEATAER-MRHGMYWSGD-LAYRDADGWIyfAGRTA-DWMRVDGENLSAA 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 500 EVERHLLAHPDIIDVAVIGAPDAIWGQKVTAVVQLRKGQSMTLPDLKTW--AREHMAPYTIPTGLLLVEEMPRNQMGKVN 577
Cdd:PRK13388 417 PIERILLRHPAINRVAVYAVPDERVGDQVMAALVLRDGATFDPDAFAAFlaAQPDLGTKAWPRYVRIAADLPSTATNKVL 496
|
....
gi 1250165799 578 KKDL 581
Cdd:PRK13388 497 KREL 500
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
212-483 |
2.56e-22 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 101.59 E-value: 2.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 212 DRPAMIIYTSGTTGRPKGVLHMHSNIQAMVQGLvSEW------AWTRDDVILHTLPLHHV--HGIVNKLL---CPLWVGA 280
Cdd:PTZ00216 264 DDLALIMYTSGTTGDPKGVMHTHGSLTAGILAL-EDRlndligPPEEDETYCSYLPLAHImeFGVTNIFLargALIGFGS 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 281 T----------CVMLPEFQPQkvwemllsskapmvnVFMAVPTIY--------SKLIQ------------Y--------- 321
Cdd:PTZ00216 343 PrtltdtfarpHGDLTEFRPV---------------FLIGVPRIFdtikkaveAKLPPvgslkrrvfdhaYqsrlralke 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 322 -YDQHFTQPHVKDFVRAVCKERIRLMVSGSAALPLPTlQRWEEITGHTLLERYGMTEIGMALSNPLKGPRIPGAVGSPLP 400
Cdd:PTZ00216 408 gKDTPYWNEKVFSAPRAVLGGRVRAMLSGGGPLSAAT-QEFVNVVFGMVIQGWGLTETVCCGGIQRTGDLEPNAVGQLLK 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 401 RVEVRIVMNNTTNTTivlgDHRNTRvcpglegkeGELLVRGPSVFKEYWNKPQETRESFIDGGWFKTGDTV-VYKDGVYW 479
Cdd:PTZ00216 487 GVEMKLLDTEEYKHT----DTPEPR---------GEILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGsIAANGTLR 553
|
....
gi 1250165799 480 IMGR 483
Cdd:PTZ00216 554 IIGR 557
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
202-578 |
3.70e-22 |
|
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: 100.58 E-value: 3.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 202 EKEAAITDWADrPAMIIYTSGTTGRPKGVLHMHSNIQAMVQGLVSEWAWTRDDVILHTLPLHHVHGIVNKLLCPLWVGaT 281
Cdd:cd17641 149 EREVAAGKGED-VAVLCTTSGTTGKPKLAMLSHGNFLGHCAAYLAADPLGPGDEYVSVLPLPWIGEQMYSVGQALVCG-F 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 282 CVMLPE-----------------FQPQKVWEMLLS------SKAPMVNVFMAvpTIYSKL-IQYYDQHFTQPHVKDFVRA 337
Cdd:cd17641 227 IVNFPEepetmmedlreigptfvLLPPRVWEGIAAdvrarmMDATPFKRFMF--ELGMKLgLRALDRGKRGRPVSLWLRL 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 338 VCK----------------ERIRLMVSGSAALPlPTLQRWEEITGHTLLERYGMTEIGMALSNPLKGPRIPGAVGSPLPR 401
Cdd:cd17641 305 ASWladallfrplrdrlgfSRLRSAATGGAALG-PDTFRFFHAIGVPLKQLYGQTELAGAYTVHRDGDVDPDTVGVPFPG 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 402 VEVRIVmnnttnttivlgdhrntrvcpglegKEGELLVRGPSVFKEYWNKPQETRESFIDGGWFKTGDTVVYK-DGVYWI 480
Cdd:cd17641 384 TEVRID-------------------------EVGEILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKeNGHLVV 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 481 MGRSSvDIIKSA-GYKISALEVERHLLAHPDIIDVAVIGApDAIWgqkVTAVVQLRkgqsmtLPDLKTWAREHMAPYTIP 559
Cdd:cd17641 439 IDRAK-DVGTTSdGTRFSPQFIENKLKFSPYIAEAVVLGA-GRPY---LTAFICID------YAIVGKWAEQRGIAFTTY 507
|
410 420
....*....|....*....|..
gi 1250165799 560 TGLLL---VEEMPRNQMGKVNK 578
Cdd:cd17641 508 TDLASrpeVYELIRKEVEKVNA 529
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
71-581 |
4.34e-22 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 101.27 E-value: 4.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 71 DKPAIIDSSGSHSYKQLYCSSLGLAGRISTAlnldfGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLFRKHPQSEL 150
Cdd:PRK10252 473 DAPALADARYQFSYREMREQVVALANLLRER-----GVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRL 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 151 EYIISDSQSSLLVAGHPYAGTLePLALKLGLPCLTLPPTsnlgtldgtdTQEKEAAITDWADRPAMIIYTSGTTGRPKGV 230
Cdd:PRK10252 548 KMMLEDARPSLLITTADQLPRF-ADVPDLTSLCYNAPLA----------PQGAAPLQLSQPHHTAYIIFTSGSTGRPKGV 616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 231 LHMHsniQAMVQGLV---SEWAWTRDDVILHTLPL-HHVHgiVNKLLCPLWVGATCVMLPefqPQkvwemllSSKAPmvn 306
Cdd:PRK10252 617 MVGQ---TAIVNRLLwmqNHYPLTADDVVLQKTPCsFDVS--VWEFFWPFIAGAKLVMAE---PE-------AHRDP--- 678
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 307 VFMAvptiysKLIQYY---DQHFTQPHVKDFVRAVCKERI--------RLMVSGSaALPLPTLQRWEEITGHTLLERYGM 375
Cdd:PRK10252 679 LAMQ------QFFAEYgvtTTHFVPSMLAAFVASLTPEGArqscaslrQVFCSGE-ALPADLCREWQQLTGAPLHNLYGP 751
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 376 TEIGMALSN-PLKGPRIPGAVGSPLPrvevriVMNNTTNTTIVLGDHRNTRVCPGLegkEGELLVRGPSVFKEYWNKPQE 454
Cdd:PRK10252 752 TEAAVDVSWyPAFGEELAAVRGSSVP------IGYPVWNTGLRILDARMRPVPPGV---AGDLYLTGIQLAQGYLGRPDL 822
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 455 TRESFIDGGW------FKTGDTVVYK-DGVYWIMGRSSvDIIKSAGYKISALEVERHLLAHPDIIDVAVI------GAPD 521
Cdd:PRK10252 823 TASRFIADPFapgermYRTGDVARWLdDGAVEYLGRSD-DQLKIRGQRIELGEIDRAMQALPDVEQAVTHacvinqAAAT 901
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 522 AIWGQKVTAVVQLRKGQSMTLPDLKTWAREHMAPYTIPTGLLLVEEMPRNQMGKVNKKDL 581
Cdd:PRK10252 902 GGDARQLVGYLVSQSGLPLDTSALQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKAL 961
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
26-475 |
4.59e-22 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 100.51 E-value: 4.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 26 RTYFPSEPGQWllgSVVHRRAHrWTAAQSSR--INQkpvfvRAPAFGDKPAIidssgshSYKQlycsSLGLAGRISTALn 103
Cdd:PRK12582 39 KSRHPLGPYPR---SIPHLLAK-WAAEAPDRpwLAQ-----REPGHGQWRKV-------TYGE----AKRAVDALAQAL- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 104 LDFGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPL-----FRKHPQSELEYIISDSQSSLLVA--GHPYAGTLEPLA 176
Cdd:PRK12582 98 LDLGLDPGRPVMILSGNSIEHALMTLAAMQAGVPAAPVspaysLMSHDHAKLKHLFDLVKPRVVFAqsGAPFARALAALD 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 177 LkLGLPCLTL--PPTSN--------LGTLDGTDTQEKEAAITDwaDRPAMIIYTSGTTGRPKGVLH----MHSNIqAMVQ 242
Cdd:PRK12582 178 L-LDVTVVHVtgPGEGIasiafadlAATPPTAAVAAAIAAITP--DTVAKYLFTSGSTGMPKAVINtqrmMCANI-AMQE 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 243 GLVSEWAWTRDDVILHTLPLHHVHG---IVNKLlcpLWVGATCVM-----LP-EFQP--QKVWEMllsskAPMvnVFMAV 311
Cdd:PRK12582 254 QLRPREPDPPPPVSLDWMPWNHTMGgnaNFNGL---LWGGGTLYIddgkpLPgMFEEtiRNLREI-----SPT--VYGNV 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 312 PTIYSKLIQYYDQHftqphvKDFVRAVCKeRIRLMVSGSAALPLPTLQRWEE----ITGH--TLLERYGMTEIGMALSNP 385
Cdd:PRK12582 324 PAGYAMLAEAMEKD------DALRRSFFK-NLRLMAYGGATLSDDLYERMQAlavrTTGHriPFYTGYGATETAPTTTGT 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 386 LKGPRIPGAVGSPLPRVEVRIVMNnttnttivlgdhrntrvcpgleGKEGELLVRGPSVFKEYWNKPQETRESFIDGGWF 465
Cdd:PRK12582 397 HWDTERVGLIGLPLPGVELKLAPV----------------------GDKYEVRVKGPNVTPGYHKDPELTAAAFDEEGFY 454
|
490
....*....|
gi 1250165799 466 KTGDTVVYKD 475
Cdd:PRK12582 455 RLGDAARFVD 464
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
211-581 |
6.45e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 98.18 E-value: 6.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 211 ADRPAMIIYTSGTTGRPKGVLHMHSNIQAMVQGLVSEWAWTRDDVILHTLPLHHVHGIVNKLLCPLWVGATCVMLPEFQP 290
Cdd:PRK08308 100 AEEPSLLQYSSGTTGEPKLIRRSWTEIDREIEAYNEALNCEQDETPIVACPVTHSYGLICGVLAALTRGSKPVIITNKNP 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 291 QKVWEMLLSSKAPMVnvfMAVPTIYSKLIQyydqhftqphvkdFVRAvcKERI-RLMVSGsAALPLPTLQRWEEITGHtL 369
Cdd:PRK08308 180 KFALNILRNTPQHIL---YAVPLMLHILGR-------------LLPG--TFQFhAVMTSG-TPLPEAWFYKLRERTTY-M 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 370 LERYGMTEIG-MALSNPLkgpRIPGAVGSPLPRVEVRIVMNnttnttivlgdhrntrvcpglEGKEGELLVrgpsvfkey 448
Cdd:PRK08308 240 MQQYGCSEAGcVSICPDM---KSHLDLGNPLPHVSVSAGSD---------------------ENAPEEIVV--------- 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 449 WNKPQETRESfiDGGWFKtgdtvvyKDGVYWIMGRSSvDIIKSAGYKISALEVERHLLAHPDIIDVAVIGAPDAIWGQKV 528
Cdd:PRK08308 287 KMGDKEIFTK--DLGYKS-------ERGTLHFMGRMD-DVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERV 356
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1250165799 529 TAVVQLRkgQSMTLPDLKTWAREHMAPYTIPTGLLLVEEMPRNQMGKVNKKDL 581
Cdd:PRK08308 357 KAKVISH--EEIDPVQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLL 407
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
211-577 |
1.70e-21 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 99.27 E-value: 1.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 211 ADRPAMIIYTSGTTGRPKGVLHMHSNIQAMVQGLVSEWAWTRDDVILHTLPLHHVHGIVNKLLCPLWVGATCVMLPefQP 290
Cdd:PRK06814 792 PDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARIDFSPEDKVFNALPVFHSFGLTGGLVLPLLSGVKVFLYP--SP 869
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 291 ---QKVWEMLLSSKAPMV---NVFMavpTIYSKLIQYYDQHftqphvkdfvravckeRIRLMVSGSAALPLPTLQRWEEI 364
Cdd:PRK06814 870 lhyRIIPELIYDTNATILfgtDTFL---NGYARYAHPYDFR----------------SLRYVFAGAEKVKEETRQTWMEK 930
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 365 TGHTLLERYGMTEIG--MALSNPLKGPriPGAVGSPLPRVEVRIVmnnttnttivlgdhrntRVcPGL-EGkeGELLVRG 441
Cdd:PRK06814 931 FGIRILEGYGVTETApvIALNTPMHNK--AGTVGRLLPGIEYRLE-----------------PV-PGIdEG--GRLFVRG 988
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 442 PSVFKEYW--NKPQETREsfIDGGWFKTGDTV-VYKDGVYWIMGRSSvDIIKSAGYKISALEVERhlLAH---PDIIDvA 515
Cdd:PRK06814 989 PNVMLGYLraENPGVLEP--PADGWYDTGDIVtIDEEGFITIKGRAK-RFAKIAGEMISLAAVEE--LAAelwPDALH-A 1062
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1250165799 516 VIGAPDAIWGQKvtaVVQLRKGQSMTLPDLKTWAREHMAP-YTIPTGLLLVEEMPRNQMGKVN 577
Cdd:PRK06814 1063 AVSIPDARKGER---IILLTTASDATRAAFLAHAKAAGASeLMVPAEIITIDEIPLLGTGKID 1122
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
211-569 |
2.45e-21 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 98.24 E-value: 2.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 211 ADRPAMIIYTSGTTGRPKGVLHMHSNIQAMVQGLVSEWAWTRDDVILHTLPLHHVHGIVNKLLCPLWVGATCVMLP---- 286
Cdd:PRK08043 364 PEDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPsplh 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 287 -EFQPQKVWEMllsskapmvNVFMAVPTiySKLIQYYDQhFTQPHvkDFVRavckerIRLMVSGSAALPLPTLQRWEEIT 365
Cdd:PRK08043 444 yRIVPELVYDR---------NCTVLFGT--STFLGNYAR-FANPY--DFAR------LRYVVAGAEKLQESTKQLWQDKF 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 366 GHTLLERYGMTEIG--MALSNPLKGPriPGAVGSPLPRVEVRIVmnnttnttivlgdhrntrVCPGLEgKEGELLVRGPS 443
Cdd:PRK08043 504 GLRILEGYGVTECApvVSINVPMAAK--PGTVGRILPGMDARLL------------------SVPGIE-QGGRLQLKGPN 562
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 444 VFKEY--------WNKPQ-ETRESFIDGGWFKTGDTVVYKD-GVYWIMGRSSvDIIKSAGYKISALEVER-HLLAHPDII 512
Cdd:PRK08043 563 IMNGYlrvekpgvLEVPTaENARGEMERGWYDTGDIVRFDEqGFVQIQGRAK-RFAKIAGEMVSLEMVEQlALGVSPDKQ 641
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1250165799 513 DVAVIgAPDAIWGQkvtAVVQLRKGQSMTLPDLKTWAREHMAP-YTIPTGLLLVEEMP 569
Cdd:PRK08043 642 HATAI-KSDASKGE---ALVLFTTDSELTREKLQQYAREHGVPeLAVPRDIRYLKQLP 695
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
71-582 |
3.85e-21 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 96.89 E-value: 3.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 71 DKPAIIDSSGSHSYKQLYCSSLGLAGRIStALNLD-------FGGLEGKRI-SFLcandasytvaqwAAWMSGGTAVPLF 142
Cdd:PRK04813 17 DFPAYDYLGEKLTYGQLKEDSDALAAFID-SLKLPdkspiivFGHMSPEMLaTFL------------GAVKAGHAYIPVD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 143 RKHPQSELEYIISDSQSSLLVAGHPyagtlEPLALkLGLPCLTLpptSNLGTLDGTDTQ-EKEAAITDwaDRPAMIIYTS 221
Cdd:PRK04813 84 VSSPAERIEMIIEVAKPSLIIATEE-----LPLEI-LGIPVITL---DELKDIFATGNPyDFDHAVKG--DDNYYIIFTS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 222 GTTGRPKGVLHMHSNIQAMVQGLVSEWAWTRDDVILHTLPLHHVHGIVNKLLCpLWVGATCVMLPE---FQPQKVWEMLL 298
Cdd:PRK04813 153 GTTGKPKGVQISHDNLVSFTNWMLEDFALPEGPQFLNQAPYSFDLSVMDLYPT-LASGGTLVALPKdmtANFKQLFETLP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 299 SSKapmVNVFMAVPTIYSklIQYYDQHFTQ---PHVKDFVraVCKErirlmvsgsaALPLPTLQrweeitghTLLER--- 372
Cdd:PRK04813 232 QLP---INVWVSTPSFAD--MCLLDPSFNEehlPNLTHFL--FCGE----------ELPHKTAK--------KLLERfps 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 373 ------YGMTEIGMALSNPL-------KGPRIPgaVGSPLPRVEVRIVMNNTTnttivlgdhrntrvcPGLEGKEGELLV 439
Cdd:PRK04813 287 atiyntYGPTEATVAVTSIEitdemldQYKRLP--IGYAKPDSPLLIIDEEGT---------------KLPDGEQGEIVI 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 440 RGPSVFKEYWNKPQETRESF--IDGGW-FKTGDTVVYKDGVYWIMGRssVDI-IKSAGYKISALEVERHLLAHPDIID-V 514
Cdd:PRK04813 350 SGPSVSKGYLNNPEKTAEAFftFDGQPaYHTGDAGYLEDGLLFYQGR--IDFqIKLNGYRIELEEIEQNLRQSSYVESaV 427
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1250165799 515 AVIGAPDaiwgQKVT---AVVQLRKGQ--------SMTLPDLKtwarEHMAPYTIPTGLLLVEEMPRNQMGKVNKKDLL 582
Cdd:PRK04813 428 VVPYNKD----HKVQyliAYVVPKEEDferefeltKAIKKELK----ERLMEYMIPRKFIYRDSLPLTPNGKIDRKALI 498
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
47-581 |
2.71e-20 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 94.29 E-value: 2.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 47 HRWTAAQSSRINQKPVFVRAP--------AFGDKPAIIDSSGSHSYKQLYCSSLGLAGRIS--------TALnLDFGgle 110
Cdd:PRK10946 6 TRWPEEFARRYREKGYWQDLPltdiltrhAASDAIAVICGERQFSYRELNQASDNLACSLRrqgikpgdTAL-VQLG--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 111 gkrisflcaNDASYTVAQWAAWMSGgtAVP---LFrKHPQSELEYIISDSQSSLLVA--GHP-YAGT--LEPLALKLGLP 182
Cdd:PRK10946 82 ---------NVAEFYITFFALLKLG--VAPvnaLF-SHQRSELNAYASQIEPALLIAdrQHAlFSDDdfLNTLVAEHSSL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 183 CLTL----PPTSNLGTLDGTDTQEKEAAITDwADRPAMIIYTSGTTGRPKGVLHMHSNIQAMVQGLVSEWAWTRDDVILH 258
Cdd:PRK10946 150 RVVLllndDGEHSLDDAINHPAEDFTATPSP-ADEVAFFQLSGGSTGTPKLIPRTHNDYYYSVRRSVEICGFTPQTRYLC 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 259 TLPLHHvhgivN-KLLCP-----LWVGATCVMLPEFQPQKVWEMLLSSKapmVNVFMAVPTIYSKLIQyydqHFTQPHVK 332
Cdd:PRK10946 229 ALPAAH-----NyPMSSPgalgvFLAGGTVVLAPDPSATLCFPLIEKHQ---VNVTALVPPAVSLWLQ----AIAEGGSR 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 333 DFVRAvckerIRLMVSGSAALPLPTLQRWEEITGHTLLERYGMTEiGMALSNPLKGP--RIPGAVGSPL-PRVEVRIVMN 409
Cdd:PRK10946 297 AQLAS-----LKLLQVGGARLSETLARRIPAELGCQLQQVFGMAE-GLVNYTRLDDSdeRIFTTQGRPMsPDDEVWVADA 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 410 NTtnttivlgdhrntrvCPGLEGKEGELLVRGPSVFKEYWNKPQETRESFIDGGWFKTGDTVVY-KDGVYWIMGRSSvDI 488
Cdd:PRK10946 371 DG---------------NPLPQGEVGRLMTRGPYTFRGYYKSPQHNASAFDANGFYCSGDLVSIdPDGYITVVGREK-DQ 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 489 IKSAGYKISALEVERHLLAHPDIIDVAVIGAPDAIWGQKVTAVVQLRKgqSMTLPDLKTWAREH-MAPYTIPTGLLLVEE 567
Cdd:PRK10946 435 INRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAFLVVKE--PLKAVQLRRFLREQgIAEFKLPDRVECVDS 512
|
570
....*....|....
gi 1250165799 568 MPRNQMGKVNKKDL 581
Cdd:PRK10946 513 LPLTAVGKVDKKQL 526
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
183-554 |
8.66e-20 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 92.24 E-value: 8.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 183 CLTLPPTSNLGTLDGTDTQEKEAAIT-DW-ADRPAMIIYTSGTTGRPKGVLHMHSNIQAMVQGLVSEWAWTRDDVILHTL 260
Cdd:PRK09029 104 ALVLEGENTFSALTSLHLQLVEGAHAvAWqPQRLATMTLTSGSTGLPKAAVHTAQAHLASAEGVLSLMPFTAQDSWLLSL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 261 PLHHV--HGIVnkllcplW----VGATCVmLPEFQPqkVWEMLLS-SKAPMvnvfmaVPTIYSKLIQYYDQHFTQPHVkd 333
Cdd:PRK09029 184 PLFHVsgQGIV-------WrwlyAGATLV-VRDKQP--LEQALAGcTHASL------VPTQLWRLLDNRSEPLSLKAV-- 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 334 fvravckerirLMvsGSAALPLPTLQRWEEITGHTLLErYGMTEigMA------LSNPLKGpripgaVGSPLPRVEVRIV 407
Cdd:PRK09029 246 -----------LL--GGAAIPVELTEQAEQQGIRCWCG-YGLTE--MAstvcakRADGLAG------VGSPLPGREVKLV 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 408 mnnttnttivlgdhrntrvcpglegkEGELLVRGPSVFKEYWNKPQETreSFIDG-GWFKTGDTVVYKDGVYWIMGRSSV 486
Cdd:PRK09029 304 --------------------------DGEIWLRGASLALGYWRQGQLV--PLVNDeGWFATRDRGEWQNGELTILGRLDN 355
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1250165799 487 DIIkSAGYKISALEVERHLLAHPDIIDVAVIGAPDAIWGQKVTAVVQLRKGQsmTLPDLKTWAREHMA 554
Cdd:PRK09029 356 LFF-SGGEGIQPEEIERVINQHPLVQQVFVVPVADAEFGQRPVAVVESDSEA--AVVNLAEWLQDKLA 420
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
211-518 |
1.50e-19 |
|
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: 91.75 E-value: 1.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 211 ADRPAMIIYTSGTTGRPKGVLHMHSNIQAMVQGLVSEWAWTRDDVILHTLPLHhvhgivnKLLCPLwVGATCVmLPEF-- 288
Cdd:cd05910 84 ADEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGEVDLATFPLF-------ALFGPA-LGLTSV-IPDMdp 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 289 ------QPQKVWEMLLSSKapmVNVFMAVPTIYSKLIQYYDQH-FTQPHVKDF------VRAVCKERIRLMVSGSA---- 351
Cdd:cd05910 155 trparaDPQKLVGAIRQYG---VSIVFGSPALLERVARYCAQHgITLPSLRRVlsagapVPIALAARLRKMLSDEAeilt 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 352 ------ALPLPTLQRWEEITGHTllerygmteigmALSNPLKGPripgAVGSPLPRVEVRIVMNNTTNTTIVLGDHRNTR 425
Cdd:cd05910 232 pygateALPVSSIGSRELLATTT------------AATSGGAGT----CVGRPIPGVRVRIIEIDDEPIAEWDDTLELPR 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 426 vcpgleGKEGELLVRGPSVFKEYWNKPQETRESFIDGG----WFKTGDtVVYKD--GVYWIMGRSSVDIIKSAGyKISAL 499
Cdd:cd05910 296 ------GEIGEITVTGPTVTPTYVNRPVATALAKIDDNsegfWHRMGD-LGYLDdeGRLWFCGRKAHRVITTGG-TLYTE 367
|
330
....*....|....*....
gi 1250165799 500 EVERHLLAHPDIIDVAVIG 518
Cdd:cd05910 368 PVERVFNTHPGVRRSALVG 386
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
212-581 |
4.43e-19 |
|
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: 90.18 E-value: 4.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 212 DRPAMIIYTSGTTGRPKGVLHmhSNIQAMVQG-LVSEWAWTRD-DVILHTLPLHHVHGIVNKLLCPLWVGATCVMLPEFQ 289
Cdd:cd05937 87 DDPAILIYTSGTTGLPKAAAI--SWRRTLVTSnLLSHDLNLKNgDRTYTCMPLYHGTAAFLGACNCLMSGGTLALSRKFS 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 290 PQKVWEMLLSSKApmvNVFMAVptiySKLIQY--------YDQhftqphvkdfvravcKERIRlMVSGSAALPlptlQRW 361
Cdd:cd05937 165 ASQFWKDVRDSGA---TIIQYV----GELCRYllstppspYDR---------------DHKVR-VAWGNGLRP----DIW 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 362 EEITghtllERYGMTEIG---------MALSNPLKGPRIPGAVG--SPLPRVEVR---IVMNNTTNTTIVLGDHRN--TR 425
Cdd:cd05937 218 ERFR-----ERFNVPEIGefyaategvFALTNHNVGDFGAGAIGhhGLIRRWKFEnqvVLVKMDPETDDPIRDPKTgfCV 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 426 VCPglEGKEGELLVRGP----SVFKEYWNKPQET-----RESFIDGG-WFKTGDTVVY-KDGVYWIMGRSSvDIIKSAGY 494
Cdd:cd05937 293 RAP--VGEPGEMLGRVPfknrEAFQGYLHNEDATesklvRDVFRKGDiYFRTGDLLRQdADGRWYFLDRLG-DTFRWKSE 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 495 KISALEVERHLLAHPDIIDVAVIGAP----DaiwGQKVTAVVQLRkgQSMTLPDLKTW------AREHMAPYTIPTGLLL 564
Cdd:cd05937 370 NVSTTEVADVLGAHPDIAEANVYGVKvpghD---GRAGCAAITLE--ESSAVPTEFTKsllaslARKNLPSYAVPLFLRL 444
|
410
....*....|....*..
gi 1250165799 565 VEEMPRNQMGKVNKKDL 581
Cdd:cd05937 445 TEEVATTDNHKQQKGVL 461
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
83-555 |
4.97e-19 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 91.06 E-value: 4.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 83 SYKQLYCSSLglagRISTALNlDFGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLFRKHPQSELEYIISDSQSSL- 161
Cdd:PLN02861 79 TYKEVYDAAI----RIGSAIR-SRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVSIa 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 162 -----------------------LVAGHPYAGTLEPLALKLGLPCLTLPPTSNLGTLDGTDTQEKEAAItdwadrpAMII 218
Cdd:PLN02861 154 fvqeskissilsclpkcssnlktIVSFGDVSSEQKEEAEELGVSCFSWEEFSLMGSLDCELPPKQKTDI-------CTIM 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 219 YTSGTTGRPKGVLHMHSNIQAMVQG-----LVSEWAWTRDDVILHTLPLHHVHGIVNKLLC-------PLWVGATCVMLP 286
Cdd:PLN02861 227 YTSGTTGEPKGVILTNRAIIAEVLStdhllKVTDRVATEEDSYFSYLPLAHVYDQVIETYCiskgasiGFWQGDIRYLME 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 287 EFQPQKvwemllsskaPmvNVFMAVPTIY------------------SKLIQY------------YDQHFTQPHVKDFVR 336
Cdd:PLN02861 307 DVQALK----------P--TIFCGVPRVYdriytgimqkissggmlrKKLFDFaynyklgnlrkgLKQEEASPRLDRLVF 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 337 AVCKE----RIRLMVSGSAALPLPTLQRWEEITGHTLLERYGMTE-IGMALSNPLKGPRIPGAVGSPLPRVEVRIVmnnt 411
Cdd:PLN02861 375 DKIKEglggRVRLLLSGAAPLPRHVEEFLRVTSCSVLSQGYGLTEsCGGCFTSIANVFSMVGTVGVPMTTIEARLE---- 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 412 tnTTIVLGDHRNTRVcpglegKEGELLVRGPSVFKEYWNKPQETRESFIDgGWFKTGDTVVYK-DGVYWIMGRSSvDIIK 490
Cdd:PLN02861 451 --SVPEMGYDALSDV------PRGEICLRGNTLFSGYHKRQDLTEEVLID-GWFHTGDIGEWQpNGAMKIIDRKK-NIFK 520
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1250165799 491 -SAGYKISALEVERHLLAHPDIIDVAVIGapDAIWGQKVTAVVQLRKGqsmtlpdLKTWAREHMAP 555
Cdd:PLN02861 521 lSQGEYVAVENLENTYSRCPLIASIWVYG--NSFESFLVAVVVPDRQA-------LEDWAANNNKT 577
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
209-581 |
8.18e-19 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 90.34 E-value: 8.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 209 DWADR--PAMIIYTSGTTGRPKGVLHMHSNIqaMVQGLVS---EWAWTRDDVILHTLPLHHVHGIVNKLLCPLWVGATCV 283
Cdd:PLN02654 270 EWVDAedPLFLLYTSGSTGKPKGVLHTTGGY--MVYTATTfkyAFDYKPTDVYWCTADCGWITGHSYVTYGPMLNGATVL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 284 ML---PEF-QPQKVWEMLLSSKapmVNVFMAVPTIYSKLIQYYDQHFTQphvkdfvravcKERIRLMVSGSAALPL-PTL 358
Cdd:PLN02654 348 VFegaPNYpDSGRCWDIVDKYK---VTIFYTAPTLVRSLMRDGDEYVTR-----------HSRKSLRVLGSVGEPInPSA 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 359 QRW-EEITGHT---LLERYGMTEIGMALSNPLKG--PRIPGAVGSPLPRVEVRIVmnnttnttivlgDHRNTRvcpgLEG 432
Cdd:PLN02654 414 WRWfFNVVGDSrcpISDTWWQTETGGFMITPLPGawPQKPGSATFPFFGVQPVIV------------DEKGKE----IEG 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 433 K-EGELLVRG--PSVFKEYWNKPQETRESFID--GGWFKTGDTVVY-KDGVYWIMGRSSvDIIKSAGYKISALEVERHLL 506
Cdd:PLN02654 478 EcSGYLCVKKswPGAFRTLYGDHERYETTYFKpfAGYYFSGDGCSRdKDGYYWLTGRVD-DVINVSGHRIGTAEVESALV 556
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1250165799 507 AHPDIIDVAVIGAPDAIWGQKVTAVVQLRKGQSMTlPDLKT----WAREHMAPYTIPTGLLLVEEMPRNQMGKVNKKDL 581
Cdd:PLN02654 557 SHPQCAEAAVVGIEHEVKGQGIYAFVTLVEGVPYS-EELRKslilTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRIL 634
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
192-475 |
9.46e-19 |
|
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: 89.80 E-value: 9.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 192 LGTLDGTDTQEKEAAITdwADRPAMIIYTSGTTGRPKGVLHMHSNIQAMVQGLVSEWAWTRDD--VILHTLPLHHVHGIV 269
Cdd:cd05921 147 AATPPTAAVDAAFAAVG--PDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFFGEEppVLVDWLPWNHTFGGN 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 270 NKLLCPLWVGATcVMLPEFQP--QKVWEMLLSSKAPMVNVFMAVPTIYSKLIQYYDQhftqphvKDFVRAVCKERIRLMV 347
Cdd:cd05921 225 HNFNLVLYNGGT-LYIDDGKPmpGGFEETLRNLREISPTVYFNVPAGWEMLVAALEK-------DEALRRRFFKRLKLMF 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 348 SGSAALPLPTLQRWEEI----TGH--TLLERYGMTEIGMALSNPLKGPRIPGAVGSPLPRVEVRIVMNNttnttivlgdh 421
Cdd:cd05921 297 YAGAGLSQDVWDRLQALavatVGEriPMMAGLGATETAPTATFTHWPTERSGLIGLPAPGTELKLVPSG----------- 365
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1250165799 422 rntrvcpgleGKEgELLVRGPSVFKEYWNKPQETRESFIDGGWFKTGDTVVYKD 475
Cdd:cd05921 366 ----------GKY-EVRVKGPNVTPGYWRQPELTAQAFDEEGFYCLGDAAKLAD 408
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
214-583 |
3.14e-18 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.
Pssm-ID: 213283 [Multi-domain] Cd Length: 509 Bit Score: 87.87 E-value: 3.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 214 PAMIIYTSGTTGRPKGVLHMH--SNIQAMVQGLVSEWAWTRDDVILHTLPLHHVHGivnklLCPLWV----GATCVMLPE 287
Cdd:cd05915 155 ACGMAYTTGTTGLPKGVVYSHraLVLHSLAASLVDGTALSEKDVVLPVVPMFHVNA-----WCLPYAatlvGAKQVLPGP 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 288 FQPQKV-WEMLLSSKapmVNVFMAVPTIYSKLiqyydqhftqPHVKDFVRAVCKERIRLMVSGSAalPLPTLQRWEEITG 366
Cdd:cd05915 230 RLDPASlVELFDGEG---VTFTAGVPTVWLAL----------ADYLESTGHRLKTLRRLVVGGSA--APRSLIARFERMG 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 367 HTLLERYGMTEIGMALSNPLKGPRIPGAVGSPLPRVEVRIVMNNTTNTTIVLGDhrnTRVCPGLEGKEGELL-VRGPSVF 445
Cdd:cd05915 295 VEVRQGYGLTETSPVVVQNFVKSHLESLSEEEKLTLKAKTGLPIPLVRLRVADE---EGRPVPKDGKALGEVqLKGPWIT 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 446 KEYWNKPQETRESFIDGGWFKTGDT-VVYKDGVYWIMGRSSvDIIKSAGYKISALEVERHLLAHPDIIDVAVIGAPDAIW 524
Cdd:cd05915 372 GGYYGNEEATRSALTPDGFFRTGDIaVWDEEGYVEIKDRLK-DLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKW 450
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1250165799 525 GQKVTAVVQLRKGQSMTLPDLKTWAREHMAPYTIPTGLLLVEEMPRNQMGKVnKKDLLR 583
Cdd:cd05915 451 QERPLAVVVPRGEKPTPEELNEHLLKAGFAKWQLPDAYVFAEEIPRTSAGKF-LKRALR 508
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
111-471 |
2.59e-17 |
|
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: 85.20 E-value: 2.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 111 GKRISFLCANDASYTVAQWAAWMSGGTAVPLFRKHPQSELEYIISDSQSSLLVAGHPYAgtlePLALKLGLPCLT----- 185
Cdd:cd17632 93 GDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLAVSAEHL----DLAVEAVLEGGTpprlv 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 186 ---------------------LPPTSNLGTLDGTDTQEKEAA-------ITDWADRPAMIIYTSGTTGRPKGVLHMHSNI 237
Cdd:cd17632 169 vfdhrpevdahraalesarerLAAVGIPVTTLTLIAVRGRDLppaplfrPEPDDDPLALLIYTSGSTGTPKGAMYTERLV 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 238 QAMVQGLVSEWAWTRDDVI-LHTLPLHHVHGiVNKLLCPLWVGATCVMLPEFQPQKVWEMLlsSKAPMVNVFMaVPTIYS 316
Cdd:cd17632 249 ATFWLKVSSIQDIRPPASItLNFMPMSHIAG-RISLYGTLARGGTAYFAAASDMSTLFDDL--ALVRPTELFL-VPRVCD 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 317 KLIQYY----DQHFTQPH----VKDFVRAVCKERI---RLM--VSGSAALPlPTLQRW-EEITGHTLLERYGMTEIGMAL 382
Cdd:cd17632 325 MLFQRYqaelDRRSVAGAdaetLAERVKAELRERVlggRLLaaVCGSAPLS-AEMKAFmESLLDLDLHDGYGSTEAGAVI 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 383 SNplkgpripGAVGSPlPRVEVRIVmnnttnTTIVLGDHRNTRVCPglegkEGELLVRGPSVFKEYWNKPQETRESFIDG 462
Cdd:cd17632 404 LD--------GVIVRP-PVLDYKLV------DVPELGYFRTDRPHP-----RGELLVKTDTLFPGYYKRPEVTAEVFDED 463
|
....*....
gi 1250165799 463 GWFKTGDTV 471
Cdd:cd17632 464 GFYRTGDVM 472
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
126-581 |
3.75e-17 |
|
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: 84.37 E-value: 3.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 126 VAQWAAWMSGGTAVPLFRKHPQSELEYIISDSQSSLLVAGhpyagtleplalklglpcltlppTSNLgtldgtdtqekea 205
Cdd:cd17648 53 IAILAVWKAGAAYVPIDPSYPDERIQFILEDTGARVVITN-----------------------STDL------------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 206 aitdwadrpAMIIYTSGTTGRPKGVLHMHSNIQAMVQGLVSEW--AWTRDDVILhTLPLHHVHGIVNKLLCPLWVGATCV 283
Cdd:cd17648 97 ---------AYAIYTSGTTGKPKGVLVEHGSVVNLRTSLSERYfgRDNGDEAVL-FFSNYVFDFFVEQMTLALLNGQKLV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 284 MLPE---FQPQKVWEMLLSSKapmVNVFMAVPTiyskLIQYYDQHfTQPHVKdfvravckeriRLMVSGSAaLPLPTLQR 360
Cdd:cd17648 167 VPPDemrFDPDRFYAYINREK---VTYLSGTPS----VLQQYDLA-RLPHLK-----------RVDAAGEE-FTAPVFEK 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 361 WEEITGHTLLERYGMTEIGM-ALSNPLKGP-RIPGAVGSPLPrvevrivmnnttNTTIVLGDHRNTRVcPglEGKEGELL 438
Cdd:cd17648 227 LRSRFAGLIINAYGPTETTVtNHKRFFPGDqRFDKSLGRPVR------------NTKCYVLNDAMKRV-P--VGAVGELY 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 439 VRGPSVFKEYWNKPQETRESFI--------------DGGWFKTGDTVVYK-DGVYWIMGRSSVDiIKSAGYKISALEVER 503
Cdd:cd17648 292 LGGDGVARGYLNRPELTAERFLpnpfqteqerargrNARLYKTGDLVRWLpSGELEYLGRNDFQ-VKIRGQRIEPGEVEA 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 504 HLLAHPDIIDVAVIGAPDAIWGQK--VTAVVQLRKGQSMTLP--DLKTWAREHMAPYTIPTGLLLVEEMPRNQMGKVNKK 579
Cdd:cd17648 371 ALASYPGVRECAVVAKEDASQAQSriQKYLVGYYLPEPGHVPesDLLSFLRAKLPRYMVPARLVRLEGIPVTINGKLDVR 450
|
..
gi 1250165799 580 DL 581
Cdd:cd17648 451 AL 452
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
120-518 |
3.80e-17 |
|
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: 84.72 E-value: 3.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 120 NDASYTVAQWAAWMSGGTAVPLFRKHPQSELEYIISDSQSSLLVAG--------HPYAGTLEPL--ALKLGLPCLTLPPt 189
Cdd:cd05933 42 NSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSEANILVVEnqkqlqkiLQIQDKLPHLkaIIQYKEPLKEKEP- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 190 sNL--------GTLDGTDTQEKEAAITDWADRPAMIIYTSGTTGRPKGVLHMHSNI----QAMVQGLVSEWAWTRDDVIL 257
Cdd:cd05933 121 -NLyswdefmeLGRSIPDEQLDAIISSQKPNQCCTLIYTSGTTGMPKGVMLSHDNItwtaKAASQHMDLRPATVGQESVV 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 258 HTLPLHHVHGIVNKLLCPLWVGAtCVMLPEFQPQKvWEMLLSSKAPMVNVFMAVPTIYSKLiqyydqhftQPHVKDfVRA 337
Cdd:cd05933 200 SYLPLSHIAAQILDIWLPIKVGG-QVYFAQPDALK-GTLVKTLREVRPTAFMGVPRVWEKI---------QEKMKA-VGA 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 338 VCKERIRLMVSGSAALPLPTLQRW-----EEITGHTLLERYGMTEIGMALSnpLKGPRIPGAVGSPLPR--------VEV 404
Cdd:cd05933 268 KSGTLKRKIASWAKGVGLETNLKLmggesPSPLFYRLAKKLVFKKVRKALG--LDRCQKFFTGAAPISRetlefflsLNI 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 405 RIV----MNNTT--NTTIVLGDHRNT---RVCPGLEGK--------EGELLVRGPSVFKEYWNKPQETRESFIDGGWFKT 467
Cdd:cd05933 346 PIMelygMSETSgpHTISNPQAYRLLscgKALPGCKTKihnpdadgIGEICFWGRHVFMGYLNMEDKTEEAIDEDGWLHS 425
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1250165799 468 GDT-VVYKDGVYWIMGRSSVDIIKSAGYKISALEVERHLLAHPDII-DVAVIG 518
Cdd:cd05933 426 GDLgKLDEDGFLYITGRIKELIITAGGENVPPVPIEDAVKKELPIIsNAMLIG 478
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
215-581 |
5.09e-17 |
|
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: 83.68 E-value: 5.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 215 AMIIYTSGTTGRPKGVLHMHSNIQAMVQGLVSEWAWTRDDVILHTLPLHHVHGIVNKLLCpLWVGATCVMLPEfqPQKVW 294
Cdd:cd17654 121 AYVIHTSGTTGTPKIVAVPHKCILPNIQHFRSLFNITSEDILFLTSPLTFDPSVVEIFLS-LSSGATLLIVPT--SVKVL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 295 EMLLSS---KAPMVNVFMAVPTIYSKliqyydqhFTQPHVKDFVRAVCKErIRLMVSGSAALPLPTLQR-W-EEITGHTL 369
Cdd:cd17654 198 PSKLADilfKRHRITVLQATPTLFRR--------FGSQSIKSTVLSATSS-LRVLALGGEPFPSLVILSsWrGKGNRTRI 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 370 LERYGMTEIGM-ALSNPLKGPRIPGAVGSPLPRVEVRIVMNNTTNTTIVLGDHRNTRVCPglegkegellvrgpsvFKEY 448
Cdd:cd17654 269 FNIYGITEVSCwALAYKVPEEDSPVQLGSPLLGTVIEVRDQNGSEGTGQVFLGGLNRVCI----------------LDDE 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 449 WNKPQETresfidggWFKTGDTVVYKDGVYWIMGRSSvDIIKSAGYKISALEVERHLLAHPDIIDVAVigapdaiWGQKV 528
Cdd:cd17654 333 VTVPKGT--------MRATGDFVTVKDGELFFLGRKD-SQIKRRGKRINLDLIQQVIESCLGVESCAV-------TLSDQ 396
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1250165799 529 TAVVQLRKGQSMTLPDLKTWAREHMAPYTIPTGLLLVEEMPRNQMGKVNKKDL 581
Cdd:cd17654 397 QRLIAFIVGESSSSRIHKELQLTLLSSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
500-575 |
1.13e-16 |
|
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: 74.89 E-value: 1.13e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1250165799 500 EVERHLLAHPDIIDVAVIGAPDAIWGQKVTAVVQLRKGQSMTLPDLKTWAREHMAPYTIPTGLLLVEEMPRNQMGK 575
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
217-585 |
7.38e-16 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 81.01 E-value: 7.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 217 IIYTSGTTGRPKGVLHMHSNIQAMVQGL-----VSEWAWTRDDVILHTLPLHHV-------------------HGIVNKL 272
Cdd:PLN02430 225 IMYTSGTSGDPKGVVLTHEAVATFVRGVdlfmeQFEDKMTHDDVYLSFLPLAHIldrmieeyffrkgasvgyyHGDLNAL 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 273 ------LCP-LWVGATCVMlpefqpQKVWEML---LSSKAPMVNVfmavptIYSKLIQY--------YDQHFTQPhVKDF 334
Cdd:PLN02430 305 rddlmeLKPtLLAGVPRVF------ERIHEGIqkaLQELNPRRRL------IFNALYKYklawmnrgYSHKKASP-MADF 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 335 -----VRAVCKERIRLMVSGSAALPlPTLQRWEEITGHT-LLERYGMTEI--GMALSNPLKGPRIpGAVGSPLPRVEVRi 406
Cdd:PLN02430 372 lafrkVKAKLGGRLRLLISGGAPLS-TEIEEFLRVTSCAfVVQGYGLTETlgPTTLGFPDEMCML-GTVGAPAVYNELR- 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 407 vmnnttnttivLGDHRNTRVCPGLEGKEGELLVRGPSVFKEYWNKPQETRESFIDgGWFKTGDT-VVYKDGVYWIMGRSS 485
Cdd:PLN02430 449 -----------LEEVPEMGYDPLGEPPRGEICVRGKCLFSGYYKNPELTEEVMKD-GWFHTGDIgEILPNGVLKIIDRKK 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 486 vDIIKSAGYKISALEVERHLLAHPDII-DVAVIGapDAIWGQKVtAVVQLRKgqsmtlPDLKTWARE--HMAPYTIPTGL 562
Cdd:PLN02430 517 -NLIKLSQGEYVALEYLENVYGQNPIVeDIWVYG--DSFKSMLV-AVVVPNE------ENTNKWAKDngFTGSFEELCSL 586
|
410 420
....*....|....*....|...
gi 1250165799 563 LLVEEMPRNQMGKVNKKDLLRHF 585
Cdd:PLN02430 587 PELKEHILSELKSTAEKNKLRGF 609
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
83-503 |
7.50e-16 |
|
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: 80.61 E-value: 7.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 83 SYKQLYCSSLGLAGRIStalnlDFGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLfrkhpqseleyiisdsqssll 162
Cdd:cd05908 17 SYRHLREEALGYLGALQ-----ELGIKPGQEVVFQITHNNKFLYLFWACLLGGMIAVPV--------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 163 vaghpYAGTLEPLALKLglpcLTLPPTSNLGTLDGTDTQEKEAAitdwaDRPAMIIYTSGTTGRPKGVLHMHSNIQAMVQ 242
Cdd:cd05908 71 -----SIGSNEEHKLKL----NKVWNTLKNPYLITEEEVLCELA-----DELAFIQFSSGSTGDPKGVMLTHENLVHNMF 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 243 GLVSEWAWTRDDVILHTLPLHHVHGIVNKLLCPLWVGATCVMLPefqpqkvwemllsskapmVNVFMAVPTIYSKLIQYY 322
Cdd:cd05908 137 AILNSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGMNQYLMP------------------TRLFIRRPILWLKKASEH 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 323 D------QHFTQPHVKDFVRAVCKE-----RIRLMVSGSAALpLPTLqrWEEITGH---------TLLERYGMTEIGMAL 382
Cdd:cd05908 199 KativssPNFGYKYFLKTLKPEKANdwdlsSIRMILNGAEPI-DYEL--CHEFLDHmskyglkrnAILPVYGLAEASVGA 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 383 SNP-LKGPRIPGAVGSPLPRVEVRIVMNNTTN----TTIVLG---DHRNTRVC----PGL-EGKEGELLVRGPSVFKEYW 449
Cdd:cd05908 276 SLPkAQSPFKTITLGRRHVTHGEPEPEVDKKDseclTFVEVGkpiDETDIRICdednKILpDGYIGHIQIRGKNVTPGYY 355
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1250165799 450 NKPQETRESFIDGGWFKTGDTVVYKDGVYWIMGRSSvDIIKSAGYKISALEVER 503
Cdd:cd05908 356 NNPEATAKVFTDDGWLKTGDLGFIRNGRLVITGREK-DIIFVNGQNVYPHDIER 408
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
16-568 |
1.42e-15 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 79.92 E-value: 1.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 16 ALPHWKATFHRTYFPSEPGQWLLGSVVHRRAHRWtaaqssrinqkpvfvrapafGDKPAIIDSSGSHSYKQLYcsslGLA 95
Cdd:PRK08279 17 DLPGILRGLKRTALITPDSKRSLGDVFEEAAARH--------------------PDRPALLFEDQSISYAELN----ARA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 96 GRISTALnLDFGGLEGKRISFLCANDASYtVAQWAAWMSGGTAVPLFRKHPQSE-LEYIISDSQSSLLVAGHPYAGTLE- 173
Cdd:PRK08279 73 NRYAHWA-AARGVGKGDVVALLMENRPEY-LAAWLGLAKLGAVVALLNTQQRGAvLAHSLNLVDAKHLIVGEELVEAFEe 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 174 --------PLALKLGLPCLTLPPT-SNLGTL-DGTDTQEKEAAITDWADRPAMIIYTSGTTGRPKGVLHMHSNIQAMVQG 243
Cdd:PRK08279 151 aradlarpPRLWVAGGDTLDDPEGyEDLAAAaAGAPTTNPASRSGVTAKDTAFYIYTSGTTGLPKAAVMSHMRWLKAMGG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 244 LVSEWAWTRDDVILHTLPLHHVHGIVNKLLCPLWVGATCVMLPEFQPQKVWEMLLSSKAPMvnvFMAVPTIYSKLIQyyd 323
Cdd:PRK08279 231 FGGLLRLTPDDVLYCCLPLYHNTGGTVAWSSVLAAGATLALRRKFSASRFWDDVRRYRATA---FQYIGELCRYLLN--- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 324 qhftQPhVKDFVRAvckERIRLMVsGSAALPlptlQRWEEITG----HTLLERYGMTEIGMALSNPLKgprIPGAVG-SP 398
Cdd:PRK08279 305 ----QP-PKPTDRD---HRLRLMI-GNGLRP----DIWDEFQQrfgiPRILEFYAASEGNVGFINVFN---FDGTVGrVP 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 399 LP-RVEVRIVMNNTTNTTIVLGDHRNTRVCPglEGKEGELLV----RGPsvFKEYwNKPQET-----RESFIDG-GWFKT 467
Cdd:PRK08279 369 LWlAHPYAIVKYDVDTGEPVRDADGRCIKVK--PGEVGLLIGritdRGP--FDGY-TDPEASekkilRDVFKKGdAWFNT 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 468 GDtVVYKDG---VYWI--MGrssvDIIKSAGYKISALEVERHLLAHPDIIDVAVIGA--PDAIwGQKVTAVVQLRKGQSM 540
Cdd:PRK08279 444 GD-LMRDDGfghAQFVdrLG----DTFRWKGENVATTEVENALSGFPGVEEAVVYGVevPGTD-GRAGMAAIVLADGAEF 517
|
570 580
....*....|....*....|....*...
gi 1250165799 541 TLPDLKTWAREHMAPYTIPTGLLLVEEM 568
Cdd:PRK08279 518 DLAALAAHLYERLPAYAVPLFVRLVPEL 545
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
214-586 |
2.08e-15 |
|
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: 78.93 E-value: 2.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 214 PAMIIYTSGTTGRPKGVLHMHSNIQAMVQGLVSEWAWTRDDVILHTLPLHHVHGIVNKLLCPLWVGATCVMLPEFQPQKV 293
Cdd:cd05940 83 AALYIYTSGTTGLPKAAIISHRRAWRGGAFFAGSGGALPSDVLYTCLPLYHSTALIVGWSACLASGATLVIRKKFSASNF 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 294 WEMLLSSKAPMvnvfmaVPTIySKLIQYYdqhFTQPHvKDFVRavcKERIRlMVSGSAALPlptlQRWEEITGH----TL 369
Cdd:cd05940 163 WDDIRKYQATI------FQYI-GELCRYL---LNQPP-KPTER---KHKVR-MIFGNGLRP----DIWEEFKERfgvpRI 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 370 LERYGMTEIGMALSNPlkgPRIPGAVG---SPLPRV-EVRIVMNNTTNTTIVLGDHRNTRVCPglEGKEGELLVR--GPS 443
Cdd:cd05940 224 AEFYAATEGNSGFINF---FGKPGAIGrnpSLLRKVaPLALVKYDLESGEPIRDAEGRCIKVP--RGEPGLLISRinPLE 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 444 VFKEYWNkPQET-----RESFIDG-GWFKTGDTVVYKDGVYWIMGRSSVDIIKSAGYKISALEVERHLLAHPDIIDVAVI 517
Cdd:cd05940 299 PFDGYTD-PAATekkilRDVFKKGdAWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVY 377
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1250165799 518 GA--PDAIwGQKVTAVVQLRKGQSMTLPDLKTWAREHMAPYTIPTGLLLVEEMPRNQMGKVNKKDLLRHFF 586
Cdd:cd05940 378 GVqvPGTD-GRAGMAAIVLQPNEEFDLSALAAHLEKNLPGYARPLFLRLQPEMEITGTFKQQKVDLRNEGF 447
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
134-581 |
3.91e-15 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 79.44 E-value: 3.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 134 SGGTAVPLFRKHPQSELEYIISDSQSSLLVAGHpyAGTLEPLALKLGLPCLTLPPTSNLGTLDGTDTQEKEAAITDWADR 213
Cdd:PRK05691 3793 AGAGYLPLDPGLPAQRLQRIIELSRTPVLVCSA--ACREQARALLDELGCANRPRLLVWEEVQAGEVASHNPGIYSGPDN 3870
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 214 PAMIIYTSGTTGRPKGVL----HMHSNIQAMVQGLvsewAWTRDDVILHTLPLHHVHGIVNKLLCPLWvGATCVMLPE-- 287
Cdd:PRK05691 3871 LAYVIYTSGSTGLPKGVMveqrGMLNNQLSKVPYL----ALSEADVIAQTASQSFDISVWQFLAAPLF-GARVEIVPNai 3945
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 288 -FQPQKvweMLLSSKAPMVNVFMAVPTiyskLIQyydqhftqphvkdfvRAVCKERI-----RLMVSGSAALPlPTL--- 358
Cdd:PRK05691 3946 aHDPQG---LLAHVQAQGITVLESVPS----LIQ---------------GMLAEDRQaldglRWMLPTGEAMP-PELarq 4002
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 359 --QRWEEITghtLLERYGMTE---------IGMALSnplKGPRIPgaVGSPlprvevrivmnnTTNTTIVLGDHRNTRVc 427
Cdd:PRK05691 4003 wlQRYPQIG---LVNAYGPAEcsddvaffrVDLAST---RGSYLP--IGSP------------TDNNRLYLLDEALELV- 4061
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 428 PglEGKEGELLVRGPSVFKEYWNKPQETRESFIDGGW-------FKTGDTVVY-KDGVYWIMGRssVD-IIKSAGYKISA 498
Cdd:PRK05691 4062 P--LGAVGELCVAGTGVGRGYVGDPLRTALAFVPHPFgapgerlYRTGDLARRrSDGVLEYVGR--IDhQVKIRGYRIEL 4137
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 499 LEVERHLLAHPDIIDVAViGAPDAIWGQKVTAVV---QLRKGQSMTLPDLKTWAREHMAPYTIPTGLLLVEEMPRNQMGK 575
Cdd:PRK05691 4138 GEIEARLHEQAEVREAAV-AVQEGVNGKHLVGYLvphQTVLAQGALLERIKQRLRAELPDYMVPLHWLWLDRLPLNANGK 4216
|
....*.
gi 1250165799 576 VNKKDL 581
Cdd:PRK05691 4217 LDRKAL 4222
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
215-528 |
3.23e-14 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 75.62 E-value: 3.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 215 AMIIYTSGTTGRPKGVLHMHSNIQAMVQGLVSEWAWTRDDVILHTLPLHHVHGIVNKLLCPLWVGATCVM-LPEFQPQKV 293
Cdd:PRK06334 186 AVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSFLPPFHAYGFNSCTLFPLLSGVPVVFaYNPLYPKKI 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 294 WEMLLSSKapmVNVFMAVPTIYSKLIQYYDQHFTqphvkdfvravCKERIRLMVSGSAALPLPTLQRWEEITGH-TLLER 372
Cdd:PRK06334 266 VEMIDEAK---VTFLGSTPVFFDYILKTAKKQES-----------CLPSLRFVVIGGDAFKDSLYQEALKTFPHiQLRQG 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 373 YGMTEIGMALS-NPLKGPRIPGAVGSPLPRVEVRIVMNNTTnttivlgdhrntrvCPGLEGKEGELLVRGPSVFKEYWNk 451
Cdd:PRK06334 332 YGTTECSPVITiNTVNSPKHESCVGMPIRGMDVLIVSEETK--------------VPVSSGETGLVLTRGTSLFSGYLG- 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 452 pQETRESFID-GG--WFKTGDT-VVYKDGVYWIMGRSSvDIIKSAGYKISALEVERHLLAH------PDIIDVAVIGAPd 521
Cdd:PRK06334 397 -EDFGQGFVElGGetWYVTGDLgYVDRHGELFLKGRLS-RFVKIGAEMVSLEALESILMEGfgqnaaDHAGPLVVCGLP- 473
|
....*..
gi 1250165799 522 aiwGQKV 528
Cdd:PRK06334 474 ---GEKV 477
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
83-513 |
1.62e-13 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 73.52 E-value: 1.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 83 SYKQLYCSSLGLAGRISTAlnldfGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLFRKHPQSELEYIISDSQSSLL 162
Cdd:PLN02614 81 TYQEVYDIVIKLGNSLRSV-----GVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIV 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 163 VAGHPYAGTLEPlalklglpclTLPPTS----NLGTLDGTDTQEKEAA------ITDWAD---------------RPA-- 215
Cdd:PLN02614 156 FVEEKKISELFK----------TCPNSTeymkTVVSFGGVSREQKEEAetfglvIYAWDEflklgegkqydlpikKKSdi 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 216 -MIIYTSGTTGRPKGVLHMHSNIQAMVQGLV-----SEWAWTRDDVILHTLPLHHVHGIVNKLlCPLWVGATCvmlpEFQ 289
Cdd:PLN02614 226 cTIMYTSGTTGDPKGVMISNESIVTLIAGVIrllksANAALTVKDVYLSYLPLAHIFDRVIEE-CFIQHGAAI----GFW 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 290 PQKVwEMLLSSKAPMV-NVFMAVPTI----YSKLIQ-----------YYDQHFT---------QPHVK------DFVRAV 338
Cdd:PLN02614 301 RGDV-KLLIEDLGELKpTIFCAVPRVldrvYSGLQKklsdggflkkfVFDSAFSykfgnmkkgQSHVEasplcdKLVFNK 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 339 CKE----RIRLMVSGSAALPLPTLQRWEEITGHTLLERYGMTE--IGMALSNPLKGPRIpGAVGSPLPRVEVRIVMNNTT 412
Cdd:PLN02614 380 VKQglggNVRIILSGAAPLASHVESFLRVVACCHVLQGYGLTEscAGTFVSLPDELDML-GTVGPPVPNVDIRLESVPEM 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 413 NTTIVLGDHRntrvcpglegkeGELLVRGPSVFKEYWNKPQETRESFIDgGWFKTGDTVVYK-DGVYWIMGRSSvDIIKS 491
Cdd:PLN02614 459 EYDALASTPR------------GEICIRGKTLFSGYYKREDLTKEVLID-GWLHTGDVGEWQpNGSMKIIDRKK-NIFKL 524
|
490 500
....*....|....*....|..
gi 1250165799 492 AGYKISALEVERHLLAHPDIID 513
Cdd:PLN02614 525 SQGEYVAVENIENIYGEVQAVD 546
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
125-503 |
1.75e-13 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 73.11 E-value: 1.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 125 TVAQwAAWMSGGTAVPLFRKHPQSELEYIISDS-------QSSLLVAGHPYAGTLEPLAlKLGLPCLTLppTSNLGTLDG 197
Cdd:PRK07768 69 PTAQ-GLWMRGASLTMLHQPTPRTDLAVWAEDTlrvigmiGAKAVVVGEPFLAAAPVLE-EKGIRVLTV--ADLLAADPI 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 198 TDTQEKEaaitdwaDRPAMIIYTSGTTGRPKGVLHMHSNIQAMVQGLVSEWAWTRD-DVILHTLPLHHVHGIVNKLLCPL 276
Cdd:PRK07768 145 DPVETGE-------DDLALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEFDVEtDVMVSWLPLFHDMGMVGFLTVPM 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 277 WVGATCVmlpefqpqKVwemllsskAPMvnVFMAVPTIYSKLIQYYdqHFTQPHVKDFVRAVCKER-------------- 342
Cdd:PRK07768 218 YFGAELV--------KV--------TPM--DFLRDPLLWAELISKY--RGTMTAAPNFAYALLARRlrrqakpgafdlss 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 343 IRLMVSGSAALPLPTLQRWEEITG------HTLLERYGMTEIGMALSNPLKG--------------------PRIPGAV- 395
Cdd:PRK07768 278 LRFALNGAEPIDPADVEDLLDAGArfglrpEAILPAYGMAEATLAVSFSPCGaglvvdevdadllaalrravPATKGNTr 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 396 -----GSPLPRVEVRIVmnnttnttivlgdHRNTRVCPglEGKEGELLVRGPSVFKEYwnkpqETRESFI----DGGWFK 466
Cdd:PRK07768 358 rlatlGPPLPGLEVRVV-------------DEDGQVLP--PRGVGVIELRGESVTPGY-----LTMDGFIpaqdADGWLD 417
|
410 420 430
....*....|....*....|....*....|....*....
gi 1250165799 467 TGDtVVY--KDGVYWIMGRSSvDIIKSAGYKISALEVER 503
Cdd:PRK07768 418 TGD-LGYltEEGEVVVCGRVK-DVIIMAGRNIYPTDIER 454
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
157-295 |
1.20e-11 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 67.32 E-value: 1.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 157 SQSSLLVAGHPYAGTLEPLALKL---GLPCLTLPPTSNL-GT---LDGTDTQEKEAAITDWADR-----PAMIIYTSGTT 224
Cdd:cd05938 77 CGAKVLVVAPELQEAVEEVLPALradGVSVWYLSHTSNTeGVislLDKVDAASDEPVPASLRAHvtiksPALYIYTSGTT 156
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1250165799 225 GRPKGVLHMHSNIQAMvQGLVSEWAWTRDDVILHTLPLHHVHGIVNKLLCPLWVGATCVMLPEFQPQKVWE 295
Cdd:cd05938 157 GLPKAARISHLRVLQC-SGFLSLCGVTADDVIYITLPLYHSSGFLLGIGGCIELGATCVLKPKFSASQFWD 226
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
215-509 |
5.55e-11 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 65.52 E-value: 5.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 215 AMIIYTSGTTGRPKGVLHMHSNIQAMVQGLVSEW-AWTRDDVILHTLPLHHVhgivnkllcpLWVGATCVML-------- 285
Cdd:PLN02387 253 AVIMYTSGSTGLPKGVMMTHGNIVATVAGVMTVVpKLGKNDVYLAYLPLAHI----------LELAAESVMAavgaaigy 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 286 --PefqpqkvweMLL---SSK--------APMVN--VFMAVPTIYSKL--------------------IQYY-------- 322
Cdd:PLN02387 323 gsP---------LTLtdtSNKikkgtkgdASALKptLMTAVPAILDRVrdgvrkkvdakgglakklfdIAYKrrlaaieg 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 323 --------DQHFTQPHVKDFVRAVCKERIRLMVSGSAALPLPTlQRWEEIT-GHTLLERYGMTEI--GMALSNPlKGPRI 391
Cdd:PLN02387 394 swfgawglEKLLWDALVFKKIRAVLGGRIRFMLSGGAPLSGDT-QRFINIClGAPIGQGYGLTETcaGATFSEW-DDTSV 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 392 pGAVGSPLPRVEVRIVMNNTTNTTIvlGDHRNTRvcpglegkeGELLVRGPSVFKEYWNKPQETRESF-IDGG---WFKT 467
Cdd:PLN02387 472 -GRVGPPLPCCYVKLVSWEEGGYLI--SDKPMPR---------GEIVIGGPSVTLGYFKNQEKTDEVYkVDERgmrWFYT 539
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1250165799 468 GDT-VVYKDGVYWIMGRSSvDIIK-SAGYKISALEVERHLLAHP 509
Cdd:PLN02387 540 GDIgQFHPDGCLEIIDRKK-DIVKlQHGEYVSLGKVEAALSVSP 582
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
214-544 |
6.78e-11 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 64.97 E-value: 6.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 214 PAMIIYTSGTTGRPKGV--------LHMHSNIQAMVQGLVSEWAWTRDD---VILHTlplHHVHGivnkllcPLWVGATC 282
Cdd:PRK10524 235 PSYILYTSGTTGKPKGVqrdtggyaVALATSMDTIFGGKAGETFFCASDigwVVGHS---YIVYA-------PLLAGMAT 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 283 VM---LPEFQPQKVWEMLLSSKApmVNVFMAVPTIYsKLIQYYDQHFTQPHVKDFVRAvckerirLMVSGSaalPL--PT 357
Cdd:PRK10524 305 IMyegLPTRPDAGIWWRIVEKYK--VNRMFSAPTAI-RVLKKQDPALLRKHDLSSLRA-------LFLAGE---PLdePT 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 358 LQRWEEITGHTLLERYGMTEIG---MALSNPL-KGPRIPGAVGSPLPRVEVRIVMNNTtnttivlGDhrntrVCPglEGK 433
Cdd:PRK10524 372 ASWISEALGVPVIDNYWQTETGwpiLAIARGVeDRPTRLGSPGVPMYGYNVKLLNEVT-------GE-----PCG--PNE 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 434 EGELLVRGP---SVFKEYWNkpQETResFIDGgWFKTGDTVVY---------KDGVYWIMGRSSvDIIKSAGYKISALEV 501
Cdd:PRK10524 438 KGVLVIEGPlppGCMQTVWG--DDDR--FVKT-YWSLFGRQVYstfdwgirdADGYYFILGRTD-DVINVAGHRLGTREI 511
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1250165799 502 ERHLLAHPDIIDVAVIGAPDAIWGQKVTAVVQLRKGQSMTLPD 544
Cdd:PRK10524 512 EESISSHPAVAEVAVVGVKDALKGQVAVAFVVPKDSDSLADRE 554
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
124-483 |
1.42e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 63.81 E-value: 1.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 124 YTVAQWAAWMSGGTAVPLFRKHPQSELEYIIS---DSQSSLLVAGHPYAGTLEPLALKLGLPclTLPPTSNLGTLDgTDT 200
Cdd:PRK05850 72 YIVAFLGALQAGLIAVPLSVPQGGAHDERVSAvlrDTSPSVVLTTSAVVDDVTEYVAPQPGQ--SAPPVIEVDLLD-LDS 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 201 QEKEAAITDWADRPAMIIYTSGTTGRPKGVLHMHSNIQAMVQGLVSEW------AWTRDDVILHTLPLHHVHGIVNKLLC 274
Cdd:PRK05850 149 PRGSDARPRDLPSTAYLQYTSGSTRTPAGVMVSHRNVIANFEQLMSDYfgdtggVPPPDTTVVSWLPFYHDMGLVLGVCA 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 275 PLWVGATCVmlpefqpqkvwemLLSskaPMVnvFMAVPTIYSKLIQYYDQHFTQPHVKDFVRAVCKER-----------I 343
Cdd:PRK05850 229 PILGGCPAV-------------LTS---PVA--FLQRPARWMQLLASNPHAFSAAPNFAFELAVRKTSdddmagldlggV 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 344 RLMVSGSAALPLPTLQRWEE------ITGHTLLERYGMTE--IGMALSNPLKGPRI-----------------PGAvGSP 398
Cdd:PRK05850 291 LGIISGSERVHPATLKRFADrfapfnLRETAIRPSYGLAEatVYVATREPGQPPESvrfdyeklsaghakrceTGG-GTP 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 399 L-----PRV-EVRIVmnnttnttivlgDHRNTRVCPglEGKEGELLVRGPSVFKEYWNKPQETRESF-----------ID 461
Cdd:PRK05850 370 LvsygsPRSpTVRIV------------DPDTCIECP--AGTVGEIWVHGDNVAAGYWQKPEETERTFgatlvdpspgtPE 435
|
410 420
....*....|....*....|..
gi 1250165799 462 GGWFKTGDTVVYKDGVYWIMGR 483
Cdd:PRK05850 436 GPWLRTGDLGFISEGELFIVGR 457
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
214-576 |
4.48e-10 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 62.45 E-value: 4.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 214 PAMIIYTSGTTGRPKGVLHmhSNIQAMVqGLVSEWAWTRDDVILHTLPLHH------VHGIVNKLLCplwVGATCVML-- 285
Cdd:PTZ00237 256 PLYILYTSGTTGNSKAVVR--SNGPHLV-GLKYYWRSIIEKDIPTVVFSHSsigwvsFHGFLYGSLS---LGNTFVMFeg 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 286 ----PEFQPQKVWEMLLSSKapmVNVFMAVPTIYSKLIQYyDQHFTQPHVK-DFvravckERIRLMVSGSAALPLPTLQR 360
Cdd:PTZ00237 330 giikNKHIEDDLWNTIEKHK---VTHTLTLPKTIRYLIKT-DPEATIIRSKyDL------SNLKEIWCGGEVIEESIPEY 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 361 WEEITGHTLLERYGMTEIGMALSNPLKGPRIP-GAVGSPLPRVEVRIVmnntTNTTIVLGdhrntrvcpglEGKEGEL-- 437
Cdd:PTZ00237 400 IENKLKIKSSRGYGQTEIGITYLYCYGHINIPyNATGVPSIFIKPSIL----SEDGKELN-----------VNEIGEVaf 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 438 -LVRGPSVFKEYWNKPQETRESFID-GGWFKTGDtVVYKD--GVYWIMGRSSvDIIKSAGYKISALEVERHLLAHPDIID 513
Cdd:PTZ00237 465 kLPMPPSFATTFYKNDEKFKQLFSKfPGYYNSGD-LGFKDenGYYTIVSRSD-DQIKISGNKVQLNTIETSILKHPLVLE 542
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 514 VAVIGAPDAIWGQKVTAVVQLRKGQSMTLPDLKTWARE-------HMAPYTIPTGLLLVEEMPRNQMGKV 576
Cdd:PTZ00237 543 CCSIGIYDPDCYNVPIGLLVLKQDQSNQSIDLNKLKNEinniitqDIESLAVLRKIIIVNQLPKTKTGKI 612
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
84-535 |
1.45e-09 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 60.79 E-value: 1.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 84 YKQLYCSSLGLAGRISTAlnldfgGLE-GKRISFLCANDASYTVAQWAAWMSGGTAVPLF-------RKHPQSELEYIIS 155
Cdd:PRK09192 52 YQTLRARAEAGARRLLAL------GLKpGDRVALIAETDGDFVEAFFACQYAGLVPVPLPlpmgfggRESYIAQLRGMLA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 156 DSQSSLLVAGHPYAGTLEPLALKLGLpCLTLPPTSnLGTLDGTDTQEKEAAitdwADRPAMIIYTSGTTGRPKGVLHMHS 235
Cdd:PRK09192 126 SAQPAAIITPDELLPWVNEATHGNPL-LHVLSHAW-FKALPEADVALPRPT----PDDIAYLQYSSGSTRFPRGVIITHR 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 236 NIQAMVQGLVSEWAWTRD-DVILHTLPLHHVHGIVNKLLCPLWVGATCVMLP--EF--QPQkVWEMLLS-SKApmvnvfm 309
Cdd:PRK09192 200 ALMANLRAISHDGLKVRPgDRCVSWLPFYHDMGLVGFLLTPVATQLSVDYLPtrDFarRPL-QWLDLISrNRG------- 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 310 avpTI-YSKLIQYydqhftqphvkdfvrAVCKERIRlmvsgSAALPLPTLQRW-------EEITGHTL------------ 369
Cdd:PRK09192 272 ---TIsYSPPFGY---------------ELCARRVN-----SKDLAELDLSCWrvagigaDMIRPDVLhqfaeafapagf 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 370 -----LERYGMTEIGMALS-NPL-KGPRI--------------------PGAV------GSPLPRVEVRIVmnntTNTTI 416
Cdd:PRK09192 329 ddkafMPSYGLAEATLAVSfSPLgSGIVVeevdrdrleyqgkavapgaeTRRVrtfvncGKALPGHEIEIR----NEAGM 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 417 VLGDHRNTRVCpglegkegellVRGPSVFKEYWNKPQETRESFIDgGWFKTGDTVVYKDGVYWIMGRSSvDIIKSAGYKI 496
Cdd:PRK09192 405 PLPERVVGHIC-----------VRGPSLMSGYFRDEESQDVLAAD-GWLDTGDLGYLLDGYLYITGRAK-DLIIINGRNI 471
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1250165799 497 SALEVERHLLAHPDII--DVAVIGAPDAIwGQKVTAVVQLR 535
Cdd:PRK09192 472 WPQDIEWIAEQEPELRsgDAAAFSIAQEN-GEKIVLLVQCR 511
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
214-503 |
3.97e-08 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 55.93 E-value: 3.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 214 PAMIIYTSGTTGRPKGVL----HMHSNIQAMVQGLVSEWAwtrDDVILHTLPLHHVHGIVNkLLCPLWVGATCVMLPE-- 287
Cdd:PRK05851 154 PAVLQGTAGSTGTPRTAIlspgAVLSNLRGLNARVGLDAA---TDVGCSWLPLYHDMGLAF-LLTAALAGAPLWLAPTta 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 288 FQ--PQKVWEMLLSSKAPMVnvfmAVPTIYSKLIQYYdqhftqphvKDFVRAVCKERIRLMVSGSAALPLPTLQRWEEIT 365
Cdd:PRK05851 230 FSasPFRWLSWLSDSRATLT----AAPNFAYNLIGKY---------ARRVSDVDLGALRVALNGGEPVDCDGFERFATAM 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 366 GH------TLLERYGMTEIGMALSNPLKG---------------PRIPGAVGSPLPRVEVRIVMnnttnttivlGDHRnt 424
Cdd:PRK05851 297 APfgfdagAAAPSYGLAESTCAVTVPVPGiglrvdevttddgsgARRHAVLGNPIPGMEVRISP----------GDGA-- 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 425 rvcPGLEGKE-GELLVRGPSVFKEYWNKPQetresfID-GGWFKTGDTVVYKDGVYWIMGRSSvDIIKSAGYKISALEVE 502
Cdd:PRK05851 365 ---AGVAGREiGEIEIRGASMMSGYLGQAP------IDpDDWFPTGDLGYLVDGGLVVCGRAK-ELITVAGRNIFPTEIE 434
|
.
gi 1250165799 503 R 503
Cdd:PRK05851 435 R 435
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
111-483 |
9.47e-08 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 55.12 E-value: 9.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 111 GKRISFLCANDASYTVAQWAAWMSGGTAVPLFrkHPQ-----SELEYIISDSQ-SSLLVAGHPYAGTLEPLAlklGLPCL 184
Cdd:PRK07769 79 GDRVAILAPQNLDYLIAFFGALYAGRIAVPLF--DPAepghvGRLHAVLDDCTpSAILTTTDSAEGVRKFFR---ARPAK 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 185 TLP--------PTSNLGTLDGTDTQEkeaaitdwaDRPAMIIYTSGTTGRPKGVLHMH----SNIQAMVQGLVSEWawtr 252
Cdd:PRK07769 154 ERPrviavdavPDEVGATWVPPEANE---------DTIAYLQYTSGSTRIPAGVQITHlnlpTNVLQVIDALEGQE---- 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 253 DDVILHTLPLHHVHGIVNKLLCPLWVGATCVMLPE-F--QPQKvWEMLLSSKAP-MVNVFMAVPtiyskliqyydqHFTQ 328
Cdd:PRK07769 221 GDRGVSWLPFFHDMGLITVLLPALLGHYITFMSPAaFvrRPGR-WIRELARKPGgTGGTFSAAP------------NFAF 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 329 PHVKdfVRAVCKE--------RIRLMVSGSAALPLPTLQRWEEITGHTLLER------YGMTEIGMALSNP--------- 385
Cdd:PRK07769 288 EHAA--ARGLPKDgeppldlsNVKGLLNGSEPVSPASMRKFNEAFAPYGLPPtaikpsYGMAEATLFVSTTpmdeeptvi 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 386 ------LKGPRI-------PGAVgsplPRVEVRIVmnnTTNTTIVLGDHRNTRVCPglEGKEGELLVRGPSVFKEYWNKP 452
Cdd:PRK07769 366 yvdrdeLNAGRFvevpadaPNAV----AQVSAGKV---GVSEWAVIVDPETASELP--DGQIGEIWLHGNNIGTGYWGKP 436
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1250165799 453 QETRESF-----------------IDGGWFKTGDTVVYKDGVYWIMGR 483
Cdd:PRK07769 437 EETAATFqnilksrlseshaegapDDALWVRTGDYGVYFDGELYITGR 484
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
111-483 |
2.10e-07 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 53.98 E-value: 2.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 111 GKRISFLCANDASYTVAQWAAWMSGGTAVPLFRKHPQ---SELEYIISDSQSSLLVAGHPYAGTLEplALKLGLPCLTLP 187
Cdd:PRK12476 92 GDRVAILAPQGIDYVAGFFAAIKAGTIAVPLFAPELPghaERLDTALRDAEPTVVLTTTAAAEAVE--GFLRNLPRLRRP 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 188 --------PTSnlgtlDGTDTQEKEAAItdwaDRPAMIIYTSGTTGRPKGVLHMHSNIQA-MVQGLVSEWAWTRDDVILH 258
Cdd:PRK12476 170 rviaidaiPDS-----AGESFVPVELDT----DDVSHLQYTSGSTRPPVGVEITHRAVGTnLVQMILSIDLLDRNTHGVS 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 259 TLPLHHVHGIVNKLLCPLWVGATCVMLP-EF--QPQKvWEMLLSSKAPMVNVFMAVPTIyskLIQYYDQHFTQPHVKDF- 334
Cdd:PRK12476 241 WLPLYHDMGLSMIGFPAVYGGHSTLMSPtAFvrRPQR-WIKALSEGSRTGRVVTAAPNF---AYEWAAQRGLPAEGDDId 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 335 VRAVckerirLMVSGSAALPLPTLQRWEEITGHTLLER------YGMTEIGMALSN--PLKGPRI--------------- 391
Cdd:PRK12476 317 LSNV------VLIIGSEPVSIDAVTTFNKAFAPYGLPRtafkpsYGIAEATLFVATiaPDAEPSVvyldreqlgagravr 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 392 -----PGAV-----GSPLPRVEVRIVMNNTTNTtivLGDhrntrvcpgleGKEGELLVRGPSVFKEYWNKPQETRESF-- 459
Cdd:PRK12476 391 vaadaPNAVahvscGQVARSQWAVIVDPDTGAE---LPD-----------GEVGEIWLHGDNIGRGYWGRPEETERTFga 456
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1250165799 460 ----------------IDGGWFKTGDTVVYKDGVYWIMGR 483
Cdd:PRK12476 457 klqsrlaegshadgaaDDGTWLRTGDLGVYLDGELYITGR 496
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
217-484 |
2.52e-07 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 53.57 E-value: 2.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 217 IIYTSGTTGRPKGVlhMHSNiQAMVQGLVSEWAWT-----RDDVILHTLPLHHVHGIVNKLLCpLWVGATCvmlpefqpq 291
Cdd:PTZ00342 309 IVYTSGTSGKPKGV--MLSN-KNLYNTVVPLCKHSifkkyNPKTHLSYLPISHIYERVIAYLS-FMLGGTI--------- 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 292 KVW--------EMLLSSKApmvNVFMAVPTIYSKLiqyYDQHFTQ-----PHVKDFVRAVCKERIRLMVSGSAalplptl 358
Cdd:PTZ00342 376 NIWskdinyfsKDIYNSKG---NILAGVPKVFNRI---YTNIMTEinnlpPLKRFLVKKILSLRKSNNNGGFS------- 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 359 qrweeitghTLLEryGMTEIGMALS---NP-----LKGpripGAVGSPLPRVEVRIVMN-------NTTNTT--IVLGDH 421
Cdd:PTZ00342 443 ---------KFLE--GITHISSKIKdkvNPnleviLNG----GGKLSPKIAEELSVLLNvnyyqgyGLTETTgpIFVQHA 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 422 RNTR-------VCPGLEGK--------------EGELLVRGPSVFKEYWNKPQETRESFIDGGWFKTGDTV-VYKDGVYW 479
Cdd:PTZ00342 508 DDNNtesiggpISPNTKYKvrtwetykatdtlpKGELLIKSDSIFSGYFLEKEQTKNAFTEDGYFKTGDIVqINKNGSLT 587
|
....*
gi 1250165799 480 IMGRS 484
Cdd:PTZ00342 588 FLDRS 592
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
218-586 |
4.19e-07 |
|
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: 52.81 E-value: 4.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 218 IYTSGTTGRPKGVLHMHSNIQAMVQGLVSEWAWTRDDVILHTLPLHH----VHGIVNKLLcplwVGATCVMLPEFQPQKV 293
Cdd:cd05939 110 IYTSGTTGLPKAAVIVHSRYYRIAAGAYYAFGMRPEDVVYDCLPLYHsaggIMGVGQALL----HGSTVVIRKKFSASNF 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 294 WEMLLSSKApmvnvfmavpTIysklIQYYDQH----FTQPHVKDfvraVCKERIRLMVsGSAALPlptlQRWEEITGH-- 367
Cdd:cd05939 186 WDDCVKYNC----------TI----VQYIGEIcrylLAQPPSEE----EQKHNVRLAV-GNGLRP----QIWEQFVRRfg 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 368 --TLLERYGMTEIGMALSNplkgprIPGAVGSP--LPRV-----EVRIV-MNNTTNTTIVLGDHRNTRVCPGLEGK-EGE 436
Cdd:cd05939 243 ipQIGEFYGATEGNSSLVN------IDNHVGACgfNSRIlpsvyPIRLIkVDEDTGELIRDSDGLCIPCQPGEPGLlVGK 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 437 LLVRGPSV-FKEYWNKPQET----RESFIDGG-WFKTGDTVVYKDGVYWIMGRSSVDIIKSAGYKISALEVERHLLAHPD 510
Cdd:cd05939 317 IIQNDPLRrFDGYVNEGATNkkiaRDVFKKGDsAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLG 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250165799 511 IIDVAVIGA--PDAIWGQKVTAVVQLRKGQsmtlpDLKTWARE---HMAPYTIPTGLLLVEEMPRNQMGKVNKKDLLRHF 585
Cdd:cd05939 397 LEDVVVYGVevPGVEGRAGMAAIVDPERKV-----DLDRFSAVlakSLPPYARPQFIRLLPEVDKTGTFKLQKTDLQKEG 471
|
.
gi 1250165799 586 F 586
Cdd:cd05939 472 Y 472
|
|
| |
