|
Name |
Accession |
Description |
Interval |
E-value |
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
79-591 |
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: 686.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 79 DRLAIIDSSGSHSYKQLYCSSFGLAGRISAALNSdfggLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLYRKHPQEEL 158
Cdd:cd05941 1 DRIAIVDDGDSITYADLVARAARLANRLLALGKD----LRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 159 EYIISDSQSSLLVagnsfaktleplalklglpcltlpptsnlstldgtdsqeeeaaitdwadRPAMIIYTSGTTGRPKGV 238
Cdd:cd05941 77 EYVITDSEPSLVL-------------------------------------------------DPALILYTSGTTGRPKGV 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 239 LHTHSSIQAMVQCLVSEWAWTRDDVILHTLPLHHVHGIVNKLLCPLWVGATCIMLPEFQPQKVWEILLTskaPMVNVFMA 318
Cdd:cd05941 108 VLTHANLAANVRALVDAWRWTEDDVLLHVLPLHHVHGLVNALLCPLFAGASVEFLPKFDPKEVAISRLM---PSITVFMG 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 319 VPTIYSKLIQYYDQHFTQPhvkDFVKAVCKQRIRLMVSGSAALPLPTLQRWEEITGHTLLERYGMTEIGMALSNPLKGPR 398
Cdd:cd05941 185 VPTIYTRLLQYYEAHFTDP---QFARAAAAERLRLMVSGSAALPVPTLEEWEAITGHTLLERYGMTEIGMALSNPLDGER 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 399 IPGAVGSPLPGVEIRIVMsnatnttiveanhrETRVRSGLEGKEGELLVRGPSVFKEYWNKHQETRESFTDSGWFKTGDT 478
Cdd:cd05941 262 RPGTVGMPLPGVQARIVD--------------EETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGWFKTGDL 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 479 A-IHKDGVFWIMGRTSVDIIKSGGYKISALEVERHLLAHPAIADVAVIGPPDAIWGQKVTAVMQLKRG-HRLTLPELKIW 556
Cdd:cd05941 328 GvVDEDGYYWILGRSSVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGaAALSLEELKEW 407
|
490 500 510
....*....|....*....|....*....|....*
gi 2105456023 557 AREHMAPYIIPTGLVLVEELPRNQMGKVNKKDLLR 591
Cdd:cd05941 408 AKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
73-593 |
6.15e-141 |
|
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: 416.52 E-value: 6.15e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 73 RAPAFGDRLAIIDSSGSHSYKQLYcssfGLAGRISAALnSDFGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLYRK 152
Cdd:COG0318 8 AAARHPDRPALVFGGRRLTYAELD----ARARRLAAAL-RALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 153 HPQEELEYIISDSQSSLLVAgnsfaktleplalklglpcltlpptsnlstldgtdsqeeeaaitdwadrpAMIIYTSGTT 232
Cdd:COG0318 83 LTAEELAYILEDSGARALVT--------------------------------------------------ALILYTSGTT 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 233 GRPKGVLHTHSSIQAMVQCLVSEWAWTRDDVILHTLPLHHVHGIVNKLLCPLWVGATCIMLPEFQPQKVWEILLTSKapm 312
Cdd:COG0318 113 GRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLPRFDPERVLELIERER--- 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 313 VNVFMAVPTIYSKLIQYYDQHFTQPHvkdfvkavckqRIRLMVSGSAALPLPTLQRWEEITGHTLLERYGMTEIGMALS- 391
Cdd:COG0318 190 VTVLFGVPTMLARLLRHPEFARYDLS-----------SLRLVVSGGAPLPPELLERFEERFGVRIVEGYGLTETSPVVTv 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 392 NPL-KGPRIPGAVGSPLPGVEIRIVmsnatnttivEANHRETRVrsgleGKEGELLVRGPSVFKEYWNKHQETRESFTDs 470
Cdd:COG0318 259 NPEdPGERRPGSVGRPLPGVEVRIV----------DEDGRELPP-----GEVGEIVVRGPNVMKGYWNDPEATAEAFRD- 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 471 GWFKTGDTA-IHKDGVFWIMGRTSvDIIKSGGYKISALEVERHLLAHPAIADVAVIGPPDAIWGQKVTAVMQLKRGHRLT 549
Cdd:COG0318 323 GWLRTGDLGrLDEDGYLYIVGRKK-DMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPGAELD 401
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 2105456023 550 LPELKIWAREHMAPYIIPTGLVLVEELPRNQMGKVNKKDLLRHF 593
Cdd:COG0318 402 AEELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRERY 445
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
77-589 |
4.64e-116 |
|
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: 353.41 E-value: 4.64e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 77 FGDRLAIIDSSGSHSYKQLYcssfGLAGRISAAL-NSDFGglEGKRISFLCANDASYTVAQWAAWMSGGTAVPLyrkHPQ 155
Cdd:cd05936 12 FPDKTALIFMGRKLTYRELD----ALAEAFAAGLqNLGVQ--PGDRVALMLPNCPQFPIAYFGALKAGAVVVPL---NPL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 156 ---EELEYIISDSQSSLLVAGNSFAKTLEPLALKLGLPCLTlpptsnlstldgtdsqeeeaaitdwADRPAMIIYTSGTT 232
Cdd:cd05936 83 ytpRELEHILNDSGAKALIVAVSFTDLLAAGAPLGERVALT-------------------------PEDVAVLQYTSGTT 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 233 GRPKGVLHTHSSIQA-MVQClvseWAW-----TRDDVILHTLPLHHVHGIVNKLLCPLWVGATCIMLPEFQPQKVWEILl 306
Cdd:cd05936 138 GVPKGAMLTHRNLVAnALQI----KAWledllEGDDVVLAALPLFHVFGLTVALLLPLALGATIVLIPRFRPIGVLKEI- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 307 tsKAPMVNVFMAVPTIYSKLIqyydqhftqpHVKDFVKAVcKQRIRLMVSGSAALPLPTLQRWEEITGHTLLERYGMTEI 386
Cdd:cd05936 213 --RKHRVTIFPGVPTMYIALL----------NAPEFKKRD-FSSLRLCISGGAPLPVEVAERFEELTGVPIVEGYGLTET 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 387 G-MALSNPLKGPRIPGAVGSPLPGVEIRIVMSNatnTTIVEanhretrvrsglEGKEGELLVRGPSVFKEYWNKHQETRE 465
Cdd:cd05936 280 SpVVAVNPLDGPRKPGSIGIPLPGTEVKIVDDD---GEELP------------PGEVGELWVRGPQVMKGYWNRPEETAE 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 466 SFTDsGWFKTGDTA-IHKDGVFWIMGRTSvDIIKSGGYKISALEVERHLLAHPAIADVAVIGPPDAIWGQKVTAVMQLKR 544
Cdd:cd05936 345 AFVD-GWLRTGDIGyMDEDGYFFIVDRKK-DMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKE 422
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 2105456023 545 GHRLTLPELKIWAREHMAPYIIPTGLVLVEELPRNQMGKVNKKDL 589
Cdd:cd05936 423 GASLTEEEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRREL 467
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
79-591 |
5.62e-107 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 331.07 E-value: 5.62e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 79 DRLAIIDSSGSH-SYKQLycssFGLAGRISAALNSdFGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLYRKHPQEE 157
Cdd:PRK07514 17 DAPFIETPDGLRyTYGDL----DAASARLANLLVA-LGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 158 LEYIISDSQSSLLVAGNSFAKTLEPLALKLGlpcltlppTSNLSTLD----GTDSQEEEAAITDWADRP------AMIIY 227
Cdd:PRK07514 92 LDYFIGDAEPALVVCDPANFAWLSKIAAAAG--------APHVETLDadgtGSLLEAAAAAPDDFETVPrgaddlAAILY 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 228 TSGTTGRPKGVLHTHSSIQAMVQCLVSEWAWTRDDVILHTLPLHHVHGIVNKLLCPLWVGATCIMLPEFQPQKVWEILlt 307
Cdd:PRK07514 164 TSGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPDDVLIHALPIFHTHGLFVATNVALLAGASMIFLPKFDPDAVLALM-- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 308 skaPMVNVFMAVPTIYSKLIQyyDQHFTQPHVkdfvkavckQRIRLMVSGSAALPLPTLQRWEEITGHTLLERYGMTEIG 387
Cdd:PRK07514 242 ---PRATVMMGVPTFYTRLLQ--EPRLTREAA---------AHMRLFISGSAPLLAETHREFQERTGHAILERYGMTETN 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 388 MALSNPLKGPRIPGAVGSPLPGVEIRIVmSNATNTTIVEanhretrvrsgleGKEGELLVRGPSVFKEYWNKHQETRESF 467
Cdd:PRK07514 308 MNTSNPYDGERRAGTVGFPLPGVSLRVT-DPETGAELPP-------------GEIGMIEVKGPNVFKGYWRMPEKTAEEF 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 468 TDSGWFKTGDTA-IHKDGVFWIMGRtSVDIIKSGGYKISALEVERHLLAHPAIADVAVIGPPDAIWGQKVTAVMQLKRGH 546
Cdd:PRK07514 374 RADGFFITGDLGkIDERGYVHIVGR-GKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKPGA 452
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 2105456023 547 RLTLPELKIWAREHMAPYIIPTGLVLVEELPRNQMGKVnKKDLLR 591
Cdd:PRK07514 453 ALDEAAILAALKGRLARFKQPKRVFFVDELPRNTMGKV-QKNLLR 496
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
63-591 |
4.91e-104 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 322.32 E-value: 4.91e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 63 MRINQKPVfvrAPAFGDRLAIIDSSGSHSYKQLYCSSFGLAGRISAAlnsdfgglegKRISFLCANDASYTVAQWAAWMS 142
Cdd:PRK07787 2 ASLNPAAV---AAAADIADAVRIGGRVLSRSDLAGAATAVAERVAGA----------RRVAVLATPTLATVLAVVGALIA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 143 GGTAVPLYRKHPQEELEYIISDSQSSLLVAgnsfaktlEPLALKLGLPCLTLPPTSnlstldGTDSQEEEAAitdwADRP 222
Cdd:PRK07787 69 GVPVVPVPPDSGVAERRHILADSGAQAWLG--------PAPDDPAGLPHVPVRLHA------RSWHRYPEPD----PDAP 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 223 AMIIYTSGTTGRPKGVLHTHSSIQAMVQCLVSEWAWTRDDVILHTLPLHHVHGIVNKLLCPLWVGATCIMLPEFQPQKVW 302
Cdd:PRK07787 131 ALIVYTSGTTGPPKGVVLSRRAIAADLDALAEAWQWTADDVLVHGLPLFHVHGLVLGVLGPLRIGNRFVHTGRPTPEAYA 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 303 EIlLTSKAPMvnvFMAVPTIYSKLiqyydqhftqphVKDFVKAVCKQRIRLMVSGSAALPLPTLQRWEEITGHTLLERYG 382
Cdd:PRK07787 211 QA-LSEGGTL---YFGVPTVWSRI------------AADPEAARALRGARLLVSGSAALPVPVFDRLAALTGHRPVERYG 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 383 MTEIGMALSNPLKGPRIPGAVGSPLPGVEIRIVMSNATnttivEANHRETRVrsglegkeGELLVRGPSVFKEYWNKHQE 462
Cdd:PRK07787 275 MTETLITLSTRADGERRPGWVGLPLAGVETRLVDEDGG-----PVPHDGETV--------GELQVRGPTLFDGYLNRPDA 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 463 TRESFTDSGWFKTGDTA-IHKDGVFWIMGRTSVDIIKSGGYKISALEVERHLLAHPAIADVAVIGPPDAIWGQKVTAVmq 541
Cdd:PRK07787 342 TAAAFTADGWFRTGDVAvVDPDGMHRIVGRESTDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAY-- 419
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 2105456023 542 LKRGHRLTLPELKIWAREHMAPYIIPTGLVLVEELPRNQMGKVNKKDLLR 591
Cdd:PRK07787 420 VVGADDVAADELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLLS 469
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
221-584 |
1.94e-101 |
|
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: 310.76 E-value: 1.94e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 221 RPAMIIYTSGTTGRPKGVLHTHSSIQAMVQCLVSEWAWTRDDVILHTLPLHHVHGIvNKLLCPLWVGATCIMLPEFQPQK 300
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGL-FGLLGALLAGGTVVLLPKFDPEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 301 VWEILLTSKapmVNVFMAVPTIYSKLIQyydqhftQPHVKDFVKAvckqRIRLMVSGSAALPLPTLQRWEEITGHTLLER 380
Cdd:cd04433 80 ALELIEREK---VTILLGVPTLLARLLK-------APESAGYDLS----SLRALVSGGAPLPPELLERFEEAPGIKLVNG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 381 YGMTEIG--MALSNPLKGPRIPGAVGSPLPGVEIRIVmsnATNTTIVEanhretrvrsglEGKEGELLVRGPSVFKEYWN 458
Cdd:cd04433 146 YGLTETGgtVATGPPDDDARKPGSVGRPVPGVEVRIV---DPDGGELP------------PGEIGELVVRGPSVMKGYWN 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 459 kHQETRESFTDSGWFKTGDTA-IHKDGVFWIMGRTSvDIIKSGGYKISALEVERHLLAHPAIADVAVIGPPDAIWGQKVT 537
Cdd:cd04433 211 -NPEATAAVDEDGWYRTGDLGrLDEDGYLYIVGRLK-DMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVV 288
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 2105456023 538 AVMQLKRGHRLTLPELKIWAREHMAPYIIPTGLVLVEELPRNQMGKV 584
Cdd:cd04433 289 AVVVLRPGADLDAEELRAHVRERLAPYKVPRRVVFVDALPRTASGKI 335
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
71-589 |
8.10e-101 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 315.59 E-value: 8.10e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 71 FVRAPA--FGDRLAIIDSSGSHSYKQLYcssfGLAGRISAALnSDFGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVP 148
Cdd:PRK06187 11 ILRHGArkHPDKEAVYFDGRRTTYAELD----ERVNRLANAL-RALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 149 LYRKHPQEELEYIISDSQSSLLVAGNSFAKTLEPLALKL----------GLPCLTLPPTS-NLST-LDGTDSQEEEAAIT 216
Cdd:PRK06187 86 INIRLKPEEIAYILNDAEDRVVLVDSEFVPLLAAILPQLptvrtvivegDGPAAPLAPEVgEYEElLAAASDTFDFPDID 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 217 dwADRPAMIIYTSGTTGRPKGVLHTHSSIQAMVQCLVSEWAWTRDDVILHTLPLHHVHGIVNKLLcPLWVGATCIMLPEF 296
Cdd:PRK06187 166 --ENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVPMFHVHAWGLPYL-ALMAGAKQVIPRRF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 297 QPQKVWEILLTSKapmVNVFMAVPTIYSKLIQYYDQHFtqphvKDFvkavckQRIRLMVSGSAALPLPTLQRWEEITGHT 376
Cdd:PRK06187 243 DPENLLDLIETER---VTFFFAVPTIWQMLLKAPRAYF-----VDF------SSLRLVIYGGAALPPALLREFKEKFGID 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 377 LLERYGMTEIGMALS-NPLK-----GPRIPGAVGSPLPGVEIRIVMSNATnttIVEANHRETrvrsglegkeGELLVRGP 450
Cdd:PRK06187 309 LVQGYGMTETSPVVSvLPPEdqlpgQWTKRRSAGRPLPGVEARIVDDDGD---ELPPDGGEV----------GEIIVRGP 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 451 SVFKEYWNKHQETRESFtDSGWFKTGDTA-IHKDGVFWIMGRTSvDIIKSGGYKISALEVERHLLAHPAIADVAVIGPPD 529
Cdd:PRK06187 376 WLMQGYWNRPEATAETI-DGGWLHTGDVGyIDEDGYLYITDRIK-DVIISGGENIYPRELEDALYGHPAVAEVAVIGVPD 453
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 530 AIWGQKVTAVMQLKRGHRLTLPELKIWAREHMAPYIIPTGLVLVEELPRNQMGKVNKKDL 589
Cdd:PRK06187 454 EKWGERPVAVVVLKPGATLDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVL 513
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
73-586 |
1.56e-100 |
|
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: 312.24 E-value: 1.56e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 73 RAPAFGDRLAIIDSSGSHSYKQLYcssfGLAGRISAALnSDFGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPL-YR 151
Cdd:cd17631 4 RARRHPDRTALVFGGRSLTYAELD----ERVNRLAHAL-RALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLnFR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 152 KHPqEELEYIISDSQSSLLVagnsfaktleplalklglpcltlpptsnlstldgtdsqeeeaaitdwaDRPAMIIYTSGT 231
Cdd:cd17631 79 LTP-PEVAYILADSGAKVLF------------------------------------------------DDLALLMYTSGT 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 232 TGRPKGVLHTHSSIQAMVQCLVSEWAWTRDDVILHTLPLHHVHGIVNKLLCPLWVGATCIMLPEFQPQKVWEillTSKAP 311
Cdd:cd17631 110 TGRPKGAMLTHRNLLWNAVNALAALDLGPDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVILRKFDPETVLD---LIERH 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 312 MVNVFMAVPTIYSKLIQYYDqhFTQPhvkDFvkavckQRIRLMVSGSAALPLPTLQRWEEItGHTLLERYGMTEIGMALS 391
Cdd:cd17631 187 RVTSFFLVPTMIQALLQHPR--FATT---DL------SSLRAVIYGGAPMPERLLRALQAR-GVKFVQGYGMTETSPGVT 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 392 npLKGP----RIPGAVGSPLPGVEIRIVmsnATNTTIVEAnhretrvrsgleGKEGELLVRGPSVFKEYWNKHQETRESF 467
Cdd:cd17631 255 --FLSPedhrRKLGSAGRPVFFVEVRIV---DPDGREVPP------------GEVGEIVVRGPHVMAGYWNRPEATAAAF 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 468 TDsGWFKTGDTA-IHKDGVFWIMGRTSvDIIKSGGYKISALEVERHLLAHPAIADVAVIGPPDAIWGQKVTAVMQLKRGH 546
Cdd:cd17631 318 RD-GWFHTGDLGrLDEDGYLYIVDRKK-DMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPGA 395
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 2105456023 547 RLTLPELKIWAREHMAPYIIPTGLVLVEELPRNQMGKVNK 586
Cdd:cd17631 396 ELDEDELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
79-584 |
5.13e-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: 289.21 E-value: 5.13e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 79 DRLAIIDSSGSHSYKQLYcssfGLAGRISAALNSDfGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLYRKHPQEEL 158
Cdd:cd05926 4 PALVVPGSTPALTYADLA----ELVDDLARQLAAL-GIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 159 EYIISDSQSSLLVAGNSF-------AKTLEPLALKLGLP---CLTLPPTSNLSTLDGTDSQEEEAAITDwADRPAMIIYT 228
Cdd:cd05926 79 EFYLADLGSKLVLTPKGElgpasraASKLGLAILELALDvgvLIRAPSAESLSNLLADKKNAKSEGVPL-PDDLALILHT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 229 SGTTGRPKGVLHTHSSIQAMVQCLVSEWAWTRDDVILHTLPLHHVHGIVNKLLCPLWVGATCIMLPEFQPQKVWEillTS 308
Cdd:cd05926 158 SGTTGRPKGVPLTHRNLAASATNITNTYKLTPDDRTLVVMPLFHVHGLVASLLSTLAAGGSVVLPPRFSASTFWP---DV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 309 KAPMVNVFMAVPTIYSKLIQYYDQHFTQPHVKdfvkavckqrIRLMVSGSAALPLPTLQRWEEITGHTLLERYGMTEIG- 387
Cdd:cd05926 235 RDYNATWYTAVPTIHQILLNRPEPNPESPPPK----------LRFIRSCSASLPPAVLEALEATFGAPVLEAYGMTEAAh 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 388 -MAlSNPLK-GPRIPGAVGSPLpGVEIRIVMSNAtnttiveanhretrvRSGLEGKEGELLVRGPSVFKEYWNKHQETRE 465
Cdd:cd05926 305 qMT-SNPLPpGPRKPGSVGKPV-GVEVRILDEDG---------------EILPPGVVGEICLRGPNVTRGYLNNPEANAE 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 466 SFTDSGWFKTGDT-AIHKDGVFWIMGRTSvDIIKSGGYKISALEVERHLLAHPAIADVAVIGPPDAIWGQKVTAVMQLKR 544
Cdd:cd05926 368 AAFKDGWFRTGDLgYLDADGYLFLTGRIK-ELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLRE 446
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 2105456023 545 GHRLTLPELKIWAREHMAPYIIPTGLVLVEELPRNQMGKV 584
Cdd:cd05926 447 GASVTEEELRAFCRKHLAAFKVPKKVYFVDELPKTATGKI 486
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
74-589 |
4.72e-89 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 284.87 E-value: 4.72e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 74 APAFGDRLAIIDSSGSHSYKQLycssfglAGRISAALNS--DFGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLYR 151
Cdd:PRK07656 15 ARRFGDKEAYVFGDQRLTYAEL-------NARVRRAAAAlaALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 152 KHPQEELEYIISDSQSSLLVAGNSFAKTLEPLalKLGLPCLTL----------PPTSNLSTLD----GTDSQEEEAAITD 217
Cdd:PRK07656 88 RYTADEAAYILARGDAKALFVLGLFLGVDYSA--TTRLPALEHvviceteeddPHTEKMKTFTdflaAGDPAERAPEVDP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 218 waDRPAMIIYTSGTTGRPKGVLHTHssiqamVQCL--VSEWA----WTRDDVILHTLPLHHVHGIVNKLLCPLWVGATCI 291
Cdd:PRK07656 166 --DDVADILFTSGTTGRPKGAMLTH------RQLLsnAADWAeylgLTEGDRYLAANPFFHVFGYKAGVNAPLMRGATIL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 292 MLPEFQPQKVWEILLTSKApmvNVFMAVPTIYSKLIQYYDQHFTqphvkDFvkavckQRIRLMVSGSAALPLPTLQRWEE 371
Cdd:PRK07656 238 PLPVFDPDEVFRLIETERI---TVLPGPPTMYNSLLQHPDRSAE-----DL------SSLRLAVTGAASMPVALLERFES 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 372 ITG-HTLLERYGMTE-IGMALSNPLKGPR--IPGAVGSPLPGVEIRIVmsnatnttivEANHRETRVrsgleGKEGELLV 447
Cdd:PRK07656 304 ELGvDIVLTGYGLSEaSGVTTFNRLDDDRktVAGTIGTAIAGVENKIV----------NELGEEVPV-----GEVGELLV 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 448 RGPSVFKEYWNKHQETRESFTDSGWFKTGDTA-IHKDGVFWIMGRTSvDIIKSGGYKISALEVERHLLAHPAIADVAVIG 526
Cdd:PRK07656 369 RGPNVMKGYYDDPEATAAAIDADGWLHTGDLGrLDEEGYLYIVDRKK-DMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIG 447
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2105456023 527 PPDAIWGQKVTAVMQLKRGHRLTLPELKIWAREHMAPYIIPTGLVLVEELPRNQMGKVNKKDL 589
Cdd:PRK07656 448 VPDERLGEVGKAYVVLKPGAELTEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRAL 510
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
70-500 |
4.22e-88 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 279.20 E-value: 4.22e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 70 VFVRAPAFGDRLAIIDSSG-SHSYKQLYCssfgLAGRISAALNSDfgGLE-GKRISFLCANDASYTVAQWAAWMSGGTAV 147
Cdd:pfam00501 1 LERQAARTPDKTALEVGEGrRLTYRELDE----RANRLAAGLRAL--GVGkGDRVAILLPNSPEWVVAFLACLKAGAVYV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 148 PLYRKHPQEELEYIISDSQSSLLVA--------GNSFAKTLEPLALKLGLPCLTLPPTSNLSTLDGTDSQEEEAAITDWA 219
Cdd:pfam00501 75 PLNPRLPAEELAYILEDSGAKVLITddalkleeLLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVPPPPPPPPDP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 220 DRPAMIIYTSGTTGRPKGVLHTH----SSIQAMVQCLVSEWAWTRDDVILHTLPLHHVHGIVNKLLCPLWVGATCIMLPE 295
Cdd:pfam00501 155 DDLAYIIYTSGTTGKPKGVMLTHrnlvANVLSIKRVRPRGFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVVLPPG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 296 FQPQKVWEILLTSKAPMVNVFMAVPTIYSKLIQyydqhftqphvKDFVKAVCKQRIRLMVSGSAALPLPTLQRWEEITGH 375
Cdd:pfam00501 235 FPALDPAALLELIERYKVTVLYGVPTLLNMLLE-----------AGAPKRALLSSLRLVLSGGAPLPPELARRFRELFGG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 376 TLLERYGMTEIGMALSNPLKGP---RIPGAVGSPLPGVEIRIVmsnatnttivEANHRETRVRsgleGKEGELLVRGPSV 452
Cdd:pfam00501 304 ALVNGYGLTETTGVVTTPLPLDedlRSLGSVGRPLPGTEVKIV----------DDETGEPVPP----GEPGELCVRGPGV 369
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 2105456023 453 FKEYWNKHQETRESFTDSGWFKTGDTA-IHKDGVFWIMGRTSvDIIKSG 500
Cdd:pfam00501 370 MKGYLNDPELTAEAFDEDGWYRTGDLGrRDEDGYLEIVGRKK-DQIKLG 417
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
74-584 |
1.07e-84 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 275.07 E-value: 1.07e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 74 APAFGDRLAII--DSSGSH---SYKQLYcssfGLAGRISAALNSDfgGLE-GKRISFLCANDASYTVAQWAAWMSGGTAV 147
Cdd:COG0365 19 AEGRGDKVALIweGEDGEErtlTYAELR----REVNRFANALRAL--GVKkGDRVAIYLPNIPEAVIAMLACARIGAVHS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 148 PLYrkhPQ---EELEYIISDSQSSLLVAGNSFAKTLEPLALK-------LGLP----CLTLPPTSNLSTLDG-------- 205
Cdd:COG0365 93 PVF---PGfgaEALADRIEDAEAKVLITADGGLRGGKVIDLKekvdealEELPslehVIVVGRTGADVPMEGdldwdell 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 206 -TDSQEEEAAITDwADRPAMIIYTSGTTGRPKGVLHTHSSIqaMVQCLVSEWAW---TRDDVILHTLPLHHVHGIVNKLL 281
Cdd:COG0365 170 aAASAEFEPEPTD-ADDPLFILYTSGTTGKPKGVVHTHGGY--LVHAATTAKYVldlKPGDVFWCTADIGWATGHSYIVY 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 282 CPLWVGATCIML---PEFQ-PQKVWEILLTSKapmVNVFMAVPTIYSKLIQYYDqhftqphvkDFVKAVCKQRIRLMVSG 357
Cdd:COG0365 247 GPLLNGATVVLYegrPDFPdPGRLWELIEKYG---VTVFFTAPTAIRALMKAGD---------EPLKKYDLSSLRLLGSA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 358 SAALPLPTLQRWEEITGHTLLERYGMTEIGMA-LSNPLKGPRIPGAVGSPLPGVEIRIVmsNATNTTIVEanhretrvrs 436
Cdd:COG0365 315 GEPLNPEVWEWWYEAVGVPIVDGWGQTETGGIfISNLPGLPVKPGSMGKPVPGYDVAVV--DEDGNPVPP---------- 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 437 gleGKEGELLVRG--PSVFKEYWNKHQETRESF--TDSGWFKTGDTA-IHKDGVFWIMGRTSvDIIKSGGYKISALEVER 511
Cdd:COG0365 383 ---GEEGELVIKGpwPGMFRGYWNDPERYRETYfgRFPGWYRTGDGArRDEDGYFWILGRSD-DVINVSGHRIGTAEIES 458
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2105456023 512 HLLAHPAIADVAVIGPPDAIWGQKVTAVMQLKRGHRLT--LP-ELKIWAREHMAPYIIPTGLVLVEELPRNQMGKV 584
Cdd:COG0365 459 ALVSHPAVAEAAVVGVPDEIRGQVVKAFVVLKPGVEPSdeLAkELQAHVREELGPYAYPREIEFVDELPKTRSGKI 534
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
78-584 |
3.01e-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: 269.62 E-value: 3.01e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 78 GDRLAIIDSSGSHSYKQLYCSSFGLAGRIsAALnsdfgGLE-GKRISFLCANDASYTVAQWAAWMSGGTAVPLYRKHPQE 156
Cdd:cd05959 18 GDKTAFIDDAGSLTYAELEAEARRVAGAL-RAL-----GVKrEERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 157 ELEYIISDSQSSLLVAGNSFAKTLEPLALKLGLPCLTL---------PPTSNLSTLDGTDSQEEEAAITdWADRPAMIIY 227
Cdd:cd05959 92 DYAYYLEDSRARVVVVSGELAPVLAAALTKSEHTLVVLivsggagpeAGALLLAELVAAEAEQLKPAAT-HADDPAFWLY 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 228 TSGTTGRPKGVLHTHSSIQAMVQCLVSE-WAWTRDDVILHTLPLHHVHGIVNKLLCPLWVGATCIMLPEF-QPQKVWEIL 305
Cdd:cd05959 171 SSGSTGRPKGVVHLHADIYWTAELYARNvLGIREDDVCFSAAKLFFAYGLGNSLTFPLSVGATTVLMPERpTPAAVFKRI 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 306 LTSKApmvNVFMAVPTIYSKLIQYYDqhftqPHVKDFVkavckqRIRLMVSGSAALPLPTLQRWEEITGHTLLERYGMTE 385
Cdd:cd05959 251 RRYRP---TVFFGVPTLYAAMLAAPN-----LPSRDLS------SLRLCVSAGEALPAEVGERWKARFGLDILDGIGSTE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 386 IG-MALSNpLKGPRIPGAVGSPLPGVEIRIVMSNAtntTIVEAnhretrvrsgleGKEGELLVRGPSVFKEYWNKHQETR 464
Cdd:cd05959 317 MLhIFLSN-RPGRVRYGTTGKPVPGYEVELRDEDG---GDVAD------------GEPGELYVRGPSSATMYWNNRDKTR 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 465 ESFtDSGWFKTGDTAIHK-DGVFWIMGRTSvDIIKSGGYKISALEVERHLLAHPAIADVAVIGPPDAIWGQKVTAVMQLK 543
Cdd:cd05959 381 DTF-QGEWTRTGDKYVRDdDGFYTYAGRAD-DMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLR 458
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 2105456023 544 RGHRLT--LP-ELKIWAREHMAPYIIPTGLVLVEELPRNQMGKV 584
Cdd:cd05959 459 PGYEDSeaLEeELKEFVKDRLAPYKYPRWIVFVDELPKTATGKI 502
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
77-588 |
1.72e-80 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 264.17 E-value: 1.72e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 77 FGDRLAIIDSSGSHSYKQLycssfGLAGRISAALNSDFGGLEGKRISFLCANDASYTVAQWAAWMSGGTAV---PLYRKH 153
Cdd:PRK05605 45 FGDRPALDFFGATTTYAEL-----GKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVehnPLYTAH 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 154 pqeELEYIISDSQSSLLVAGNSFAKTLEPL------------------------ALKLGLP-------CLTLPPTSNL-- 200
Cdd:PRK05605 120 ---ELEHPFEDHGARVAIVWDKVAPTVERLrrttpletivsvnmiaampllqrlALRLPIPalrkaraALTGPAPGTVpw 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 201 -----STLDGTDSQEEEAAITdwADRPAMIIYTSGTTGRPKGVLHTHSSIQA-MVQCLvsewAWT-----RDDVILHTLP 269
Cdd:PRK05605 197 etlvdAAIGGDGSDVSHPRPT--PDDVALILYTSGTTGKPKGAQLTHRNLFAnAAQGK----AWVpglgdGPERVLAALP 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 270 LHHVHGIVNKLLCPLWVGATCIMLPEFQPQKVWEILltsKAPMVNVFMAVPTIYSKLiqyydqhftqphvkdfVKAVCKQ 349
Cdd:PRK05605 271 MFHAYGLTLCLTLAVSIGGELVLLPAPDIDLILDAM---KKHPPTWLPGVPPLYEKI----------------AEAAEER 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 350 R-----IRLMVSGSAALPLPTLQRWEEITGHTLLERYGMTEIG-MALSNPLKGPRIPGAVGSPLPGVEIRIVmsNATNTT 423
Cdd:PRK05605 332 GvdlsgVRNAFSGAMALPVSTVELWEKLTGGLLVEGYGLTETSpIIVGNPMSDDRRPGYVGVPFPDTEVRIV--DPEDPD 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 424 iveanhrETRVrsglEGKEGELLVRGPSVFKEYWNKHQETRESFTDsGWFKTGDTAI-HKDGVFWIMGRTSvDIIKSGGY 502
Cdd:PRK05605 410 -------ETMP----DGEEGELLVRGPQVFKGYWNRPEETAKSFLD-GWFRTGDVVVmEEDGFIRIVDRIK-ELIITGGF 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 503 KISALEVERHLLAHPAIADVAVIGPPDAIWGQKVTAVMQLKRGHRLTLPELKIWAREHMAPYIIPTGLVLVEELPRNQMG 582
Cdd:PRK05605 477 NVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEPGAALDPEGLRAYCREHLTRYKVPRRFYHVDELPRDQLG 556
|
....*.
gi 2105456023 583 KVNKKD 588
Cdd:PRK05605 557 KVRRRE 562
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
82-585 |
2.73e-75 |
|
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: 247.90 E-value: 2.73e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 82 AIIDSSGSH--SYKQLycssFGLAGRISAALNSDfGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLYRKHPQEELE 159
Cdd:cd05911 1 AQIDADTGKelTYAQL----RTLSRRLAAGLRKL-GLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 160 YIISDSQSSLL-VAGNSFAKTLEPLALKLGLPCLTLPPTSNLSTLDGTDSQEEEAAITDW---------ADRPAMIIYTS 229
Cdd:cd05911 76 HQLKISKPKVIfTDPDGLEKVKEAAKELGPKDKIIVLDDKPDGVLSIEDLLSPTLGEEDEdlppplkdgKDDTAAILYSS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 230 GTTGRPKGVLHTHSSIQAMV--QCLVSEWAWTRDDVILHTLPLHHVHGIvNKLLCPLWVGATCIMLPEFQPQKVWEILLT 307
Cdd:cd05911 156 GTTGLPKGVCLSHRNLIANLsqVQTFLYGNDGSNDVILGFLPLYHIYGL-FTTLASLLNGATVIIMPKFDSELFLDLIEK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 308 SKAPMVNVfmaVPTIYSKLIQYydqhftqphvKDFVKAVCkQRIRLMVSGSAALplptLQRWEE-----ITGHTLLERYG 382
Cdd:cd05911 235 YKITFLYL---VPPIAAALAKS----------PLLDKYDL-SSLRVILSGGAPL----SKELQEllakrFPNATIKQGYG 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 383 MTEIGMALSNPLKGPRIPGAVGSPLPGVEIRIVmsNATNTTIVEanhretrvrsglEGKEGELLVRGPSVFKEYWNKHQE 462
Cdd:cd05911 297 MTETGGILTVNPDGDDKPGSVGRLLPNVEAKIV--DDDGKDSLG------------PNEPGEICVRGPQVMKGYYNNPEA 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 463 TRESFTDSGWFKTGDTA-IHKDGVFWIMGRtSVDIIKSGGYKISALEVERHLLAHPAIADVAVIGPPDAIWGQKVTAVMQ 541
Cdd:cd05911 363 TKETFDEDGWLHTGDIGyFDEDGYLYIVDR-KKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVV 441
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 2105456023 542 LKRGHRLTLPELKIWAREHMAPYI-IPTGLVLVEELPRNQMGKVN 585
Cdd:cd05911 442 RKPGEKLTEKEVKDYVAKKVASYKqLRGGVVFVDEIPKSASGKIL 486
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
72-584 |
6.62e-75 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 248.72 E-value: 6.62e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 72 VRAPAFGDRLAIIDSSGSHSYKQLYCSsfglAGRISAALNSDFGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLYR 151
Cdd:PRK08314 18 VSARRYPDKTAIVFYGRAISYRELLEE----AERLAGYLQQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 152 KHPQEELEYIISDSQSSLLVAGNSFAKTLEPLALKLGLPCL-------TLPPTSNLSTLDGTDSQEE-----EAAITDWA 219
Cdd:PRK08314 94 MNREEELAHYVTDSGARVAIVGSELAPKVAPAVGNLRLRHVivaqysdYLPAEPEIAVPAWLRAEPPlqalaPGGVVAWK 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 220 D------RP----------AMIIYTSGTTGRPKGVLHTHSSIQAMVqclVSEWAW---TRDDVILHTLPLHHVHGIVNKL 280
Cdd:PRK08314 174 EalaaglAPpphtagpddlAVLPYTSGTTGVPKGCMHTHRTVMANA---VGSVLWsnsTPESVVLAVLPLFHVTGMVHSM 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 281 LCPLWVGATCIMLPE---------FQPQKV--WeillTSKAPMVNVFMAvptiyskliqyydqhftQPHVKDFvkavCKQ 349
Cdd:PRK08314 251 NAPIYAGATVVLMPRwdreaaarlIERYRVthW----TNIPTMVVDFLA-----------------SPGLAER----DLS 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 350 RIRLMVSGSAALPLPTLQRWEEITGHTLLERYGMTE-IGMALSNPLKGPRiPGAVGSPLPGVEIRIVmsnatnttivean 428
Cdd:PRK08314 306 SLRYIGGGGAAMPEAVAERLKELTGLDYVEGYGLTEtMAQTHSNPPDRPK-LQCLGIPTFGVDARVI------------- 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 429 hretRVRSGLE---GKEGELLVRGPSVFKEYWNKHQETRESFTD-SG--WFKTGDTA-IHKDGVFWIMGRTSvDIIKSGG 501
Cdd:PRK08314 372 ----DPETLEElppGEVGEIVVHGPQVFKGYWNRPEATAEAFIEiDGkrFFRTGDLGrMDEEGYFFITDRLK-RMINASG 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 502 YKISALEVERHLLAHPAIADVAVIGPPDAIWGQKVTAVMQLKRGHRLTLPELKI--WAREHMAPYIIPTGLVLVEELPRN 579
Cdd:PRK08314 447 FKVWPAEVENLLYKHPAIQEACVIATPDPRRGETVKAVVVLRPEARGKTTEEEIiaWAREHMAAYKYPRIVEFVDSLPKS 526
|
....*
gi 2105456023 580 QMGKV 584
Cdd:PRK08314 527 GSGKI 531
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
41-589 |
3.85e-73 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 243.30 E-value: 3.85e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 41 PRRWLLGTVIHRRAHgwtsapsmrinqkpvfvRAPafgDRLAIIDSSGSHSYKQLYcssfGLAGRISAALnSDFGGLEGK 120
Cdd:PRK08316 8 ARRQTIGDILRRSAR-----------------RYP---DKTALVFGDRSWTYAELD----AAVNRVAAAL-LDLGLKKGD 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 121 RISFLCANDASYTVAQWAAWMSGGTAVPLYRKHPQEELEYIISDSQSSLLVAGNSFAKTLEPLALKLGLPCLTLPPTsnl 200
Cdd:PRK08316 63 RVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARAFLVDPALAPTAEAALALLPVDTLILSLV--- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 201 stLDGTDSQEEEAAITDWA--------------DRPAMIIYTSGTTGRPKGVLHTHSSIQA-MVQCLVsEWAWTRDDVIL 265
Cdd:PRK08316 140 --LGGREAPGGWLDFADWAeagsvaepdveladDDLAQILYTSGTESLPKGAMLTHRALIAeYVSCIV-AGDMSADDIPL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 266 HTLPLHHVHGIVNKLLCPLWVGATCIMLPEFQPQkvwEILLTSKAPMVNVFMAVPTIYSKLIQYYDqhFTQPHVKDFVKA 345
Cdd:PRK08316 217 HALPLYHCAQLDVFLGPYLYVGATNVILDAPDPE---LILRTIEAERITSFFAPPTVWISLLRHPD--FDTRDLSSLRKG 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 346 VckqrirlmvSGSAALPLPTLQRweeitghtLLER---------YGMTEIGmalsnPLK---GP----RIPGAVGSPLPG 409
Cdd:PRK08316 292 Y---------YGASIMPVEVLKE--------LRERlpglrfyncYGQTEIA-----PLAtvlGPeehlRRPGSAGRPVLN 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 410 VEirivmsnatnTTIVEANHRETRvrsglEGKEGELLVRGPSVFKEYWNKHQETRESFTDsGWFKTGDTA-IHKDGVFWI 488
Cdd:PRK08316 350 VE----------TRVVDDDGNDVA-----PGEVGEIVHRSPQLMLGYWDDPEKTAEAFRG-GWFHSGDLGvMDEEGYITV 413
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 489 MGRTSvDIIKSGGYKISALEVERHLLAHPAIADVAVIGPPDAIWGQKVTAVMQLKRGHRLTLPELKIWAREHMAPYIIPT 568
Cdd:PRK08316 414 VDRKK-DMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAGATVTEDELIAHCRARLAGFKVPK 492
|
570 580
....*....|....*....|.
gi 2105456023 569 GLVLVEELPRNQMGKVNKKDL 589
Cdd:PRK08316 493 RVIFVDELPRNPSGKILKREL 513
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
101-586 |
3.19e-72 |
|
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: 238.43 E-value: 3.19e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 101 GLAGRISAALNSdFGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPL---YRKHpqeELEYIISDSQSSLLVAGNSFA 177
Cdd:cd05903 9 TRADRLAAGLAA-LGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPIlpfFREH---ELAFILRRAKAKVFVVPERFR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 178 ktleplalklglpcltlpptsnlstldGTDSQEEEAAItdwadrpAMIIYTSGTTGRPKGVLHTHSSIQAMVQCLVSEWA 257
Cdd:cd05903 85 ---------------------------QFDPAAMPDAV-------ALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLG 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 258 WTRDDVILHTLPLHHVHGIVNKLLCPLWVGATCIMLPEFQPQKVWEILLTSKApmvnVFMAVPTiyskliqyydqhftqP 337
Cdd:cd05903 131 LGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQDIWDPDKALALMREHGV----TFMMGAT---------------P 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 338 HVKDFVKAVCKQ-----RIRLMVSGSAALPLPTLQRWEEITGHTLLERYGMTEIGMALSNPLKGP--RIPGAVGSPLPGV 410
Cdd:cd05903 192 FLTDLLNAVEEAgeplsRLRTFVCGGATVPRSLARRAAELLGAKVCSAYGSTECPGAVTSITPAPedRRLYTDGRPLPGV 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 411 EIRIVmsnatnttiveanhrETRVRSGLEGKEGELLVRGPSVFKEYWNKHQETRESFTDsGWFKTGDTA-IHKDGVFWIM 489
Cdd:cd05903 272 EIKVV---------------DDTGATLAPGVEGELLSRGPSVFLGYLDRPDLTADAAPE-GWFRTGDLArLDEDGYLRIT 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 490 GRTSvDIIKSGGYKISALEVERHLLAHPAIADVAVIGPPDAIWGQKVTAVMQLKRGHRLTLPEL-KIWAREHMAPYIIPT 568
Cdd:cd05903 336 GRSK-DIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGALLTFDELvAYLDRQGVAKQYWPE 414
|
490
....*....|....*...
gi 2105456023 569 GLVLVEELPRNQMGKVNK 586
Cdd:cd05903 415 RLVHVDDLPRTPSGKVQK 432
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
79-591 |
4.19e-72 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 239.76 E-value: 4.19e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 79 DRLAIIDSSGSHSYKQLYcssfGLAGRISAALNSDFGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLYRKHPQEEL 158
Cdd:PRK06839 17 DRIAIITEEEEMTYKQLH----EYVSKVAAYLIYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENEL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 159 EYIISDSQSSLLVAGNSFAKTLEPLALKLGLPcltlPPTSnLSTLDGTDSQEEEAAITDWADRPAMIIYTSGTTGRPKGV 238
Cdd:PRK06839 93 IFQLKDSGTTVLFVEKTFQNMALSMQKVSYVQ----RVIS-ITSLKEIEDRKIDNFVEKNESASFIICYTSGTTGKPKGA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 239 LHTHSSIQAMVQCLVSEWAWTRDDVILHTLPLHHVHGIvNKLLCPLWVGATCIMLP-EFQPQKVWEILLTSKapmVNVFM 317
Cdd:PRK06839 168 VLTQENMFWNALNNTFAIDLTMHDRSIVLLPLFHIGGI-GLFAFPTLFAGGVIIVPrKFEPTKALSMIEKHK---VTVVM 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 318 AVPTIYSKLIQYYDqhFTQPHVkdfvkavckQRIRLMVSGSAALPLPTLQRWEEiTGHTLLERYGMTE----IGMALSNP 393
Cdd:PRK06839 244 GVPTIHQALINCSK--FETTNL---------QSVRWFYNGGAPCPEELMREFID-RGFLFGQGFGMTEtsptVFMLSEED 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 394 LKgpRIPGAVGSPLPGVEIRIVmSNATNTTIVeanhretrvrsgleGKEGELLVRGPSVFKEYWNKHQETRESFTDsGWF 473
Cdd:PRK06839 312 AR--RKVGSIGKPVLFCDYELI-DENKNKVEV--------------GEVGELLIRGPNVMKEYWNRPDATEETIQD-GWL 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 474 KTGDTA-IHKDGVFWIMGRTSvDIIKSGGYKISALEVERHLLAHPAIADVAVIGPPDAIWGQKVTAVMQLKRGHRLTLPE 552
Cdd:PRK06839 374 CTGDLArVDEDGFVYIVGRKK-EMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVLIEKD 452
|
490 500 510
....*....|....*....|....*....|....*....
gi 2105456023 553 LKIWAREHMAPYIIPTGLVLVEELPRNQMGKVNKKDLLR 591
Cdd:PRK06839 453 VIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQLVN 491
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
89-589 |
2.87e-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: 235.84 E-value: 2.87e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 89 SHSYKQLYCSSFGLAGRISAAlnsdfGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLYRKHPQEELEYIISDSQSS 168
Cdd:cd05935 1 SLTYLELLEVVKKLASFLSNK-----GVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 169 LLVAGNSfaktLEPLALklglpcltlpptsnlstldgtdsqeeeaaitdwadrpamIIYTSGTTGRPKGVLHTHSSIQAM 248
Cdd:cd05935 76 VAVVGSE----LDDLAL---------------------------------------IPYTSGTTGLPKGCMHTHFSAAAN 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 249 VQCLVSEWAWTRDDVILHTLPLHHVHGIVNKLLCPLWVGATCIMLPEFQPQKVWEILLTSKA-------PMVNVFMAVPT 321
Cdd:cd05935 113 ALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMARWDRETALELIEKYKVtfwtnipTMLVDLLATPE 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 322 IyskliqyydqhftqphvkdfvKAVCKQRIRLMVSGSAALPLPTLQRWEEITGHTLLERYGMTE-IGMALSNPLKGPRIP 400
Cdd:cd05935 193 F---------------------KTRDLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTEtMSQTHTNPPLRPKLQ 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 401 gAVGSPLPGVEIRIVmsnatnttiveanhretRVRSGLE---GKEGELLVRGPSVFKEYWNKHQETRESFT-DSG--WFK 474
Cdd:cd05935 252 -CLGIP*FGVDARVI-----------------DIETGRElppNEVGEIVVRGPQIFKGYWNRPEETEESFIeIKGrrFFR 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 475 TGDTA-IHKDGVFWIMGRTSvDIIKSGGYKISALEVERHLLAHPAIADVAVIGPPDAIWGQKVTAVMQLKRGHRLTLPEL 553
Cdd:cd05935 314 TGDLGyMDEEGYFFFVDRVK-RMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEYRGKVTEE 392
|
490 500 510
....*....|....*....|....*....|....*...
gi 2105456023 554 KI--WAREHMAPYIIPTGLVLVEELPRNQMGKVNKKDL 589
Cdd:cd05935 393 DIieWAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
101-589 |
5.67e-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: 234.49 E-value: 5.67e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 101 GLAGRISAALnSDFGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLYRKHPQEELEYIISDSQSSLLVagnsfaktl 180
Cdd:cd05934 11 RESARIAAAL-AALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV--------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 181 eplalklglpcltlpptsnlstldgtdsqeeeaaiTDwadrPAMIIYTSGTTGRPKGVLHTHSsiQAMVQCLVSEW--AW 258
Cdd:cd05934 81 -----------------------------------VD----PASILYTSGTTGPPKGVVITHA--NLTFAGYYSARrfGL 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 259 TRDDVILHTLPLHHVHGIVNKLLCPLWVGATCIMLPEFQPQKVWEILLTSKApmvNVFMAVPTIYSKLIQyydqhfTQPH 338
Cdd:cd05934 120 GEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLLPRFSASRFWSDVRRYGA---TVTNYLGAMLSYLLA------QPPS 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 339 VKDfvkavCKQRIRLmVSGSAALPLpTLQRWEEITGHTLLERYGMTEIGMALSNPLKGPRIPGAVGSPLPGVEIRIVmsn 418
Cdd:cd05934 191 PDD-----RAHRLRA-AYGAPNPPE-LHEEFEERFGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAPGYEVRIV--- 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 419 atnttivEANHRETRVrsgleGKEGELLVR---GPSVFKEYWNKHQETRESFTDsGWFKTGDTAIH-KDGVFWIMGRTSv 494
Cdd:cd05934 261 -------DDDGQELPA-----GEPGELVIRglrGWGFFKGYYNMPEATAEAMRN-GWFHTGDLGYRdADGFFYFVDRKK- 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 495 DIIKSGGYKISALEVERHLLAHPAIADVAVIGPPDAIWGQKVTAVMQLKRGHRLTLPELKIWAREHMAPYIIPTGLVLVE 574
Cdd:cd05934 327 DMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLDPEELFAFCEGQLAYFKVPRYIRFVD 406
|
490
....*....|....*
gi 2105456023 575 ELPRNQMGKVNKKDL 589
Cdd:cd05934 407 DLPKTPTEKVAKAQL 421
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
73-587 |
7.22e-70 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 236.54 E-value: 7.22e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 73 RAPAFGDRLAIIDSSG----SHSYKQLYcssfGLAGRISAALNSdfGGLE-GKRISFLCANDASYTVAQWAAWMSGGTAV 147
Cdd:COG1022 20 RAARFPDRVALREKEDgiwqSLTWAEFA----ERVRALAAGLLA--LGVKpGDRVAILSDNRPEWVIADLAILAAGAVTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 148 PLYRKHPQEELEYIISDSQSSLLVAGNSF-AKTLepLALKLGLPCL---------TLPPTSNLSTLD-----GTDSQEEE 212
Cdd:COG1022 94 PIYPTSSAEEVAYILNDSGAKVLFVEDQEqLDKL--LEVRDELPSLrhivvldprGLRDDPRLLSLDellalGREVADPA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 213 ------AAITdwADRPAMIIYTSGTTGRPKGVLHTHSSIQAMVQCLVSEWAWTRDDVILHTLPLHHVHGIVNKLLCpLWV 286
Cdd:COG1022 172 elearrAAVK--PDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFLPLAHVFERTVSYYA-LAA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 287 GATCI----------MLPEFQPQ------KVWEILLTS-----------KAPMVNVFMAVPTIYSKliqYYDQHFTQPHV 339
Cdd:COG1022 249 GATVAfaespdtlaeDLREVKPTfmlavpRVWEKVYAGiqakaeeagglKRKLFRWALAVGRRYAR---ARLAGKSPSLL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 340 KDFVKAVCKQ------------RIRLMVSGSAALPlPTLQRWEEITGHTLLERYGMTEI-GMALSNPLKGPRIpGAVGSP 406
Cdd:COG1022 326 LRLKHALADKlvfsklrealggRLRFAVSGGAALG-PELARFFRALGIPVLEGYGLTETsPVITVNRPGDNRI-GTVGPP 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 407 LPGVEIRIvmsnatnttiveanhretrvrsgleGKEGELLVRGPSVFKEYWNKHQETRESFTDSGWFKTGDTA-IHKDGV 485
Cdd:COG1022 404 LPGVEVKI-------------------------AEDGEILVRGPNVMKGYYKNPEATAEAFDADGWLHTGDIGeLDEDGF 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 486 FWIMGRTSvDIIK-SGGYKISALEVERHLLAHPAIADVAVIGppDaiwGQK-VTAVMQLKrghrltLPELKIWAREHMAP 563
Cdd:COG1022 459 LRITGRKK-DLIVtSGGKNVAPQPIENALKASPLIEQAVVVG--D---GRPfLAALIVPD------FEALGEWAEENGLP 526
|
570 580
....*....|....*....|....*..
gi 2105456023 564 YIIPTGLV---LVEELPRNQMGKVNKK 587
Cdd:COG1022 527 YTSYAELAqdpEVRALIQEEVDRANAG 553
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
79-589 |
5.84e-69 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 232.18 E-value: 5.84e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 79 DRLAIIDSSGSHSYKQLycssfglAGRIS--AALNSDFGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLyrkHPQE 156
Cdd:PRK06188 27 DRPALVLGDTRLTYGQL-------ADRISryIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTAL---HPLG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 157 ELE---YIISDSQ-SSLLVAGNSFA-KTLEPLALKLGLP-CLTLPPTSNLSTLDGTDSQEEEAAITDWADRP--AMIIYT 228
Cdd:PRK06188 97 SLDdhaYVLEDAGiSTLIVDPAPFVeRALALLARVPSLKhVLTLGPVPDGVDLLAAAAKFGPAPLVAAALPPdiAGLAYT 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 229 SGTTGRPKGVLHTHSSIQAMVQCLVSEWAWTRDDVILHTLPLHHVHGIvnKLLCPLWVGATCIMLPEFQPQKVWEILLTS 308
Cdd:PRK06188 177 GGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLSHAGGA--FFLPTLLRGGTVIVLAKFDPAEVLRAIEEQ 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 309 KapmVNVFMAVPT-IYSKLiqyyDQHftQPHVKDFvkavckQRIRLMVSGSAALPLPTLQRWEEITGHTLLERYGMTEIG 387
Cdd:PRK06188 255 R---ITATFLVPTmIYALL----DHP--DLRTRDL------SSLETVYYGASPMSPVRLAEAIERFGPIFAQYYGQTEAP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 388 MALS------NPLKGPRIPGAVGSPLPGVEIRIVmsnatnttivEANHRETRVrsgleGKEGELLVRGPSVFKEYWNKHQ 461
Cdd:PRK06188 320 MVITylrkrdHDPDDPKRLTSCGRPTPGLRVALL----------DEDGREVAQ-----GEVGEICVRGPLVMDGYWNRPE 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 462 ETRESFTDsGWFKTGDTA-IHKDGVFWIMGRTSvDIIKSGGYKISALEVERHLLAHPAIADVAVIGPPDAIWGQKVTAVM 540
Cdd:PRK06188 385 ETAEAFRD-GWLHTGDVArEDEDGFYYIVDRKK-DMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVV 462
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 2105456023 541 QLKRGHRLTLPELKIWAREHMAPYIIPTGLVLVEELPRNQMGKVNKKDL 589
Cdd:PRK06188 463 VLRPGAAVDAAELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKAL 511
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
70-589 |
2.26e-66 |
|
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: 224.81 E-value: 2.26e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 70 VFVRAPAFGDRLAIIDSSG--SHSYKQLYCSSFGLAgrisAALNSdFGGLEGKRISFLCANDASYTVAQWAAwMSGG--- 144
Cdd:cd05904 11 SFLFASAHPSRPALIDAATgrALTYAELERRVRRLA----AGLAK-RGGRKGDVVLLLSPNSIEFPVAFLAV-LSLGavv 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 145 -TAVPLYRkhpQEELEYIISDSQSSLLVAGNSFAKTLEPLALKLGLpcltLPptsnlSTLDGTDSQEEEAAITDWADRP- 222
Cdd:cd05904 85 tTANPLST---PAEIAKQVKDSGAKLAFTTAELAEKLASLALPVVL----LD-----SAEFDSLSFSDLLFEADEAEPPv 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 223 --------AMIIYTSGTTGRPKGVLHTHSSIQAMVQCLVSEWAWT--RDDVILHTLPLHHVHGIVNKLLCPLWVGATCIM 292
Cdd:cd05904 153 vvikqddvAALLYSSGTTGRSKGVMLTHRNLIAMVAQFVAGEGSNsdSEDVFLCVLPMFHIYGLSSFALGLLRLGATVVV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 293 LPEFQPQKVWEILLTSKapmVNVFMAVPTIYSKLIQyydqhftQPHVKDFVKavckQRIRLMVSGSAALPLPTLQRWEEI 372
Cdd:cd05904 233 MPRFDLEELLAAIERYK---VTHLPVVPPIVLALVK-------SPIVDKYDL----SSLRQIMSGAAPLGKELIEAFRAK 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 373 TGHT-LLERYGMTE---IGMALSNPLKGPRIPGAVGSPLPGVEIRIVmsnATNTTiveanhretrvRSGLEGKEGELLVR 448
Cdd:cd05904 299 FPNVdLGQGYGMTEstgVVAMCFAPEKDRAKYGSVGRLVPNVEAKIV---DPETG-----------ESLPPNQTGELWIR 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 449 GPSVFKEYWNKHQETRESFTDSGWFKTGDTA-IHKDGVFWIMGRTSvDIIKSGGYKISALEVERHLLAHPAIADVAVIGP 527
Cdd:cd05904 365 GPSIMKGYLNNPEATAATIDKEGWLHTGDLCyIDEDGYLFIVDRLK-ELIKYKGFQVAPAELEALLLSHPEILDAAVIPY 443
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2105456023 528 PDAIWGQKVTAVMQLKRGHRLTLPELKIWAREHMAPYIIPTGLVLVEELPRNQMGKVNKKDL 589
Cdd:cd05904 444 PDEEAGEVPMAFVVRKPGSSLTEDEIMDFVAKQVAPYKKVRKVAFVDAIPKSPSGKILRKEL 505
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
78-586 |
4.36e-66 |
|
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ligase, 4-hydroxybenzoate-CoA ligase, 2-aminobenzoate-CoA ligase, etc. Members are related to fatty acid and acetate CoA ligases.
Pssm-ID: 274059 [Multi-domain] Cd Length: 505 Bit Score: 223.95 E-value: 4.36e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 78 GDRLAIIDSSGSHSYKQLYCSSfglaGRISAALNSdFGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLYRKHPQEE 157
Cdd:TIGR02262 19 GGKTAFIDDISSLSYGELEAQV----RRLAAALRR-LGVKREERVLLLMLDGVDFPIAFLGAIRAGIVPVALNTLLTADD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 158 LEYIISDSQSSLLVAGNSFAKTLEPLALKLglPCL--------TLPPTSNLSTLDGTDSQEEEAAITDwADRPAMIIYTS 229
Cdd:TIGR02262 94 YAYMLEDSRARVVFVSGALLPVIKAALGKS--PHLehrvvvgrPEAGEVQLAELLATESEQFKPAATQ-ADDPAFWLYSS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 230 GTTGRPKGVLHTHSSIQAMVQCLVSEWAWTR-DDVILHTLPLHHVHGIVNKLLCPLWVGATCIMLPEF-QPQKVWEILLT 307
Cdd:TIGR02262 171 GSTGMPKGVVHTHSNPYWTAELYARNTLGIReDDVCFSAAKLFFAYGLGNALTFPMSVGATTVLMGERpTPDAVFDRLRR 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 308 SKApmvNVFMAVPTIYSKLIQYYDqhftqphvkdfVKAVCKQRIRLMVSGSAALPLPTLQRWEEITGHTLLERYGMTEIG 387
Cdd:TIGR02262 251 HQP---TIFYGVPTLYAAMLADPN-----------LPSEDQVRLRLCTSAGEALPAEVGQRWQARFGVDIVDGIGSTEML 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 388 -MALSNplkgprIPGAV-----GSPLPGVEIRIVMSNATNTTiveanhretrvrsglEGKEGELLVRGPSVFKEYWNKHQ 461
Cdd:TIGR02262 317 hIFLSN------LPGDVrygtsGKPVPGYRLRLVGDGGQDVA---------------DGEPGELLISGPSSATMYWNNRA 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 462 ETRESFTdSGWFKTGDTAIHK-DGVFWIMGRTSvDIIKSGGYKISALEVERHLLAHPAIADVAVIGPPDAIWGQKVTAVM 540
Cdd:TIGR02262 376 KSRDTFQ-GEWTRSGDKYVRNdDGSYTYAGRTD-DMLKVSGIYVSPFEIESALIQHPAVLEAAVVGVADEDGLIKPKAFV 453
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 2105456023 541 QLKRGHRLTLPELKIWAREHMAPYIIPTGLVLVEELPRNQMGKVNK 586
Cdd:TIGR02262 454 VLRPGQTALETELKEHVKDRLAPYKYPRWIVFVDDLPKTATGKIQR 499
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
116-587 |
2.54e-65 |
|
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: 220.54 E-value: 2.54e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 116 GLE-GKRISFLCANDASYTVAQWAAWMSGGTAVPLYRKHPQEELEYIISDSQSSLLvagnsfaktleplalklglpcltl 194
Cdd:cd05907 26 GVEpGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKAL------------------------ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 195 pptsnlstldgtdsqeeeaaITDWADRPAMIIYTSGTTGRPKGVLHTHSSIQAMVQCLVSEWAWTRDDVILHTLPLHHVH 274
Cdd:cd05907 82 --------------------FVEDPDDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPATEGDRHLSFLPLAHVF 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 275 GIVNKLLCPLWVGATC----------IMLPEFQPQkvweilltskapmvnVFMAVPTIYSKLIQYYDQHFTQPHVKDFVK 344
Cdd:cd05907 142 ERRAGLYVPLLAGARIyfassaetllDDLSEVRPT---------------VFLAVPRVWEKVYAAIKVKAVPGLKRKLFD 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 345 AVCKQRIRLMVSGSAALPLPTLQRWEEItGHTLLERYGMTEIGMALS-NPLKGPRIpGAVGSPLPGVEIRIvmsnatntt 423
Cdd:cd05907 207 LAVGGRLRFAASGGAPLPAELLHFFRAL-GIPVYEGYGLTETSAVVTlNPPGDNRI-GTVGKPLPGVEVRI--------- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 424 iveanhretrvrsgleGKEGELLVRGPSVFKEYWNKHQETRESFTDSGWFKTGDTA-IHKDGVFWIMGRtSVDIIK-SGG 501
Cdd:cd05907 276 ----------------ADDGEILVRGPNVMLGYYKNPEATAEALDADGWLHTGDLGeIDEDGFLHITGR-KKDLIItSGG 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 502 YKISALEVERHLLAHPAIADVAVIGppDaiwGQK-VTAVMQLKrghrltlPE-LKIWAREHMAPYIIPTGLV---LVEEL 576
Cdd:cd05907 339 KNISPEPIENALKASPLISQAVVIG--D---GRPfLVALIVPD-------PEaLEAWAEEHGIAYTDVAELAanpAVRAE 406
|
490
....*....|.
gi 2105456023 577 PRNQMGKVNKK 587
Cdd:cd05907 407 IEAAVEAANAR 417
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
79-586 |
3.15e-65 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 223.01 E-value: 3.15e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 79 DRLAIIDSSGSH------SYKQLYCssfgLAGRISAALnSDFGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPL--- 149
Cdd:PRK13295 39 DKTAVTAVRLGTgaprrfTYRELAA----LVDRVAVGL-ARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLmpi 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 150 YRKHpqeELEYIISDSQSSLLVAGNSF--------AKTLEPLalklglpcltLPPTSNLSTL--DGTDSQEEEAAITDW- 218
Cdd:PRK13295 114 FRER---ELSFMLKHAESKVLVVPKTFrgfdhaamARRLRPE----------LPALRHVVVVggDGADSFEALLITPAWe 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 219 ----------ADRP-----AMIIYTSGTTGRPKGVLHTHSSIQAMVQCLVSEWAWTRDDVILHTLPLHHVHGIVNKLLCP 283
Cdd:PRK13295 181 qepdapailaRLRPgpddvTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILMASPMAHQTGFMYGLMMP 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 284 LWVGATCIMlpefqpQKVWEilltskapmvnvfmavPTIYSKLIQYYDQHFTQ---PHVKDFVKAVCKQ-----RIRLMV 355
Cdd:PRK13295 261 VMLGATAVL------QDIWD----------------PARAAELIRTEGVTFTMastPFLTDLTRAVKESgrpvsSLRTFL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 356 SGSAALPLPTLQRWEEITGHTLLERYGMTEIGMA----LSNPLKgpRIPGAVGSPLPGVEIRIVmsNATNTTIveanhre 431
Cdd:PRK13295 319 CAGAPIPGALVERARAALGAKIVSAWGMTENGAVtltkLDDPDE--RASTTDGCPLPGVEVRVV--DADGAPL------- 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 432 trvrsgLEGKEGELLVRGPSVFKEYWNKHQETResfTDS-GWFKTGDTA-IHKDGVFWIMGRTSvDIIKSGGYKISALEV 509
Cdd:PRK13295 388 ------PAGQIGRLQVRGCSNFGGYLKRPQLNG---TDAdGWFDTGDLArIDADGYIRISGRSK-DVIIRGGENIPVVEI 457
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2105456023 510 ERHLLAHPAIADVAVIGPPDAIWGQKVTAVMQLKRGHRLTLPELKIWAREH-MAPYIIPTGLVLVEELPRNQMGKVNK 586
Cdd:PRK13295 458 EALLYRHPAIAQVAIVAYPDERLGERACAFVVPRPGQSLDFEEMVEFLKAQkVAKQYIPERLVVRDALPRTPSGKIQK 535
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
213-589 |
3.43e-64 |
|
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: 216.82 E-value: 3.43e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 213 AAITDwADRPAMIIYTSGTTGRPKGVLHTHSsiqAMVQCLVSEWAWT---RDDVILHTLPLHHVHGIVNKLLCPLWVGAT 289
Cdd:cd05972 75 AIVTD-AEDPALIYFTSGTTGLPKGVLHTHS---YPLGHIPTAAYWLglrPDDIHWNIADPGWAKGAWSSFFGPWLLGAT 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 290 CIM--LPEFQPQKVWEILLTSKapmVNVFMAVPTIYSKLIQYYDQHFTQPHVKDFVkavckqrirlmvsgSAALPL--PT 365
Cdd:cd05972 151 VFVyeGPRFDAERILELLERYG---VTSFCGPPTAYRMLIKQDLSSYKFSHLRLVV--------------SAGEPLnpEV 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 366 LQRWEEITGHTLLERYGMTEIGMALSNPLKGPRIPGAVGSPLPGVEIRIVmsnatnttivEANHRETRvrsglEGKEGEL 445
Cdd:cd05972 214 IEWWRAATGLPIRDGYGQTETGLTVGNFPDMPVKPGSMGRPTPGYDVAII----------DDDGRELP-----PGEEGDI 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 446 LVR--GPSVFKEYWNKHQETRESFTDsGWFKTGDTAIH-KDGVFWIMGRTSvDIIKSGGYKISALEVERHLLAHPAIADV 522
Cdd:cd05972 279 AIKlpPPGLFLGYVGDPEKTEASIRG-DYYLTGDRAYRdEDGYFWFVGRAD-DIIKSSGYRIGPFEVESALLEHPAVAEA 356
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 523 AVIGPPDAIWGQKVTAVMQLKRGH---RLTLPELKIWAREHMAPYIIPTGLVLVEELPRNQMGKVNKKDL 589
Cdd:cd05972 357 AVVGSPDPVRGEVVKAFVVLTSGYepsEELAEELQGHVKKVLAPYKYPREIEFVEELPKTISGKIRRVEL 426
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
73-591 |
3.75e-64 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 220.00 E-value: 3.75e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 73 RAPAFGDRLAIIDSSG-SHSYKQLYCssfgLAGRISAALnSDFGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLYR 151
Cdd:PRK06087 32 TARAMPDKIAVVDNHGaSYTYSALDH----AASRLANWL-LAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 152 KHPQEELEYIISDSQSSLLVAGNSFAKT---LEPLALKLGLPCLT-------LPPTSNLSTLDG--TDSQEEEAAITDWA 219
Cdd:PRK06087 107 SWREAELVWVLNKCQAKMFFAPTLFKQTrpvDLILPLQNQLPQLQqivgvdkLAPATSSLSLSQiiADYEPLTTAITTHG 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 220 DRPAMIIYTSGTTGRPKGVLHTHSSIQAMVQCLVSEWAWTRDDVILHTLPLHHVHGIVNKLLCPLWVGATCIMLPEFQPQ 299
Cdd:PRK06087 187 DELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVLLDIFTPD 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 300 KVWEILLTSKAPMvnVFMAVPTIYSkLIQYYDQHftQPHVkdfvkavckQRIRLMVSGSAALPLPTLQRWEEiTGHTLLE 379
Cdd:PRK06087 267 ACLALLEQQRCTC--MLGATPFIYD-LLNLLEKQ--PADL---------SALRFFLCGGTTIPKKVARECQQ-RGIKLLS 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 380 RYGMTE----IGMALSNPLkgPRIPGAVGSPLPGVEIRivmsnatnttIVEANHRETrvrsgLEGKEGELLVRGPSVFKE 455
Cdd:PRK06087 332 VYGSTEssphAVVNLDDPL--SRFMHTDGYAAAGVEIK----------VVDEARKTL-----PPGCEGEEASRGPNVFMG 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 456 YWNKHQETRESFTDSGWFKTGDTA-IHKDGVFWIMGRTSvDIIKSGGYKISALEVERHLLAHPAIADVAVIGPPDAIWGQ 534
Cdd:PRK06087 395 YLDEPELTARALDEEGWYYSGDLCrMDEAGYIKITGRKK-DIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGE 473
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2105456023 535 KVTAVMQLKRG-HRLTLPELKIW-AREHMAPYIIPTGLVLVEELPRNQMGKVNK----KDLLR 591
Cdd:PRK06087 474 RSCAYVVLKAPhHSLTLEEVVAFfSRKRVAKYKYPEHIVVIDKLPRTASGKIQKfllrKDIMR 536
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
169-592 |
7.53e-64 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 220.98 E-value: 7.53e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 169 LLVAGNSFAKTLEPLALKLGLPCLTLPPTSNLSTLDGTDSQEEEAAITDWADRPAMIIYTSGTTGRPKGVLHTHSSIQAM 248
Cdd:PRK07529 162 VEVDLARYLPGPKRLAVPLIRRKAHARILDFDAELARQPGDRLFSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVAN 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 249 VQCLVSEWAWTRDDVILHTLPLHHVHGIVNKLLCPLWVGATCIMLPefqPQ---------KVWEILLTSKapmVNVFMAV 319
Cdd:PRK07529 242 AWLGALLLGLGPGDTVFCGLPLFHVNALLVTGLAPLARGAHVVLAT---PQgyrgpgviaNFWKIVERYR---INFLSGV 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 320 PTIYSKLIQyydqhftQPhvkdfVKAVCKQRIRLMVSGSAALPLPTLQRWEEITGHTLLERYGMTEiGMALS--NPLKGP 397
Cdd:PRK07529 316 PTVYAALLQ-------VP-----VDGHDISSLRYALCGAAPLPVEVFRRFEAATGVRIVEGYGLTE-ATCVSsvNPPDGE 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 398 RIPGAVGSPLPGVEIRIVMSNATNTTIVEAnhretrvrsgLEGKEGELLVRGPSVFKEYWNKHQEtRESFTDSGWFKTGD 477
Cdd:PRK07529 383 RRIGSVGLRLPYQRVRVVILDDAGRYLRDC----------AVDEVGVLCIAGPNVFSGYLEAAHN-KGLWLEDGWLNTGD 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 478 TA-IHKDGVFWIMGRTSvDIIKSGGYKISALEVERHLLAHPAIADVAVIGPPDAIWGQKVTAVMQLKRGHRLTLPELKIW 556
Cdd:PRK07529 452 LGrIDADGYFWLTGRAK-DLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGELPVAYVQLKPGASATEAELLAF 530
|
410 420 430
....*....|....*....|....*....|....*..
gi 2105456023 557 AREHMA-PYIIPTGLVLVEELPRNQMGKVNKKDLLRH 592
Cdd:PRK07529 531 ARDHIAeRAAVPKHVRILDALPKTAVGKIFKPALRRD 567
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
90-589 |
2.54e-62 |
|
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: 214.42 E-value: 2.54e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 90 HSYKQLYCSsfglAGRISAALnSDFGGLEGKRISFLCANDASYTVAQWAAWMSGG---TAVPlyRKHPqEELEYIISDSQ 166
Cdd:cd12119 26 YTYAEVAER----ARRLANAL-RRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAvlhTINP--RLFP-EQIAYIINHAE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 167 SSLLVAGNSFAKTLEPLALKL--------GLPCLTLPPTSNLSTLDGTDSQEEEAAITDWAD----RPAMIIYTSGTTGR 234
Cdd:cd12119 98 DRVVFVDRDFLPLLEAIAPRLptvehvvvMTDDAAMPEPAGVGVLAYEELLAAESPEYDWPDfdenTAAAICYTSGTTGN 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 235 PKGVLHTHSSI--QAMVQCLVSEWAWTRDDVILHTLPLHHVHGIVNKLLCPlWVGATCIML-PEFQPQKVWEILLTSKap 311
Cdd:cd12119 178 PKGVVYSHRSLvlHAMAALLTDGLGLSESDVVLPVVPMFHVNAWGLPYAAA-MVGAKLVLPgPYLDPASLAELIEREG-- 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 312 mVNVFMAVPTIYSKLIQYYDQH-FTQPHVkdfvkavckqriRLMVSGSAALPLPTLQRWEEItGHTLLERYGMTE---IG 387
Cdd:cd12119 255 -VTFAAGVPTVWQGLLDHLEANgRDLSSL------------RRVVIGGSAVPRSLIEAFEER-GVRVIHAWGMTEtspLG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 388 MALSNPLKGPRIPGAV--------GSPLPGVEIRIVmsnATNTTIVEANHRETrvrsglegkeGELLVRGPSVFKEYWNK 459
Cdd:cd12119 321 TVARPPSEHSNLSEDEqlalrakqGRPVPGVELRIV---DDDGRELPWDGKAV----------GELQVRGPWVTKSYYKN 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 460 HQETrESFTDSGWFKTGDTA-IHKDGVFWIMGRTSvDIIKSGGYKISALEVERHLLAHPAIADVAVIGPPDAIWGQKVTA 538
Cdd:cd12119 388 DEES-EALTEDGWLRTGDVAtIDEDGYLTITDRSK-DVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLA 465
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 2105456023 539 VMQLKRGHRLTLPELkiwaREHMAPYI----IPTGLVLVEELPRNQMGKVNKKDL 589
Cdd:cd12119 466 VVVLKEGATVTAEEL----LEFLADKVakwwLPDDVVFVDEIPKTSTGKIDKKAL 516
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
89-589 |
4.05e-62 |
|
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.
Pssm-ID: 341238 [Multi-domain] Cd Length: 411 Bit Score: 211.05 E-value: 4.05e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 89 SHSYKQLYCSSFGLAGRISAalnsdFGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLYRKHPQEELEYIISDSQSS 168
Cdd:cd05912 1 SYTFAELFEEVSRLAEHLAA-----LGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 169 LlvagnsfaktleplalklglpcltlpptsnlstldgtdsqeeeaaitdwaDRPAMIIYTSGTTGRPKGVLHTHSSIQAM 248
Cdd:cd05912 76 L--------------------------------------------------DDIATIMYTSGTTGKPKGVQQTFGNHWWS 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 249 VQCLVSEWAWTRDDVILHTLPLHHVHGIvNKLLCPLWVGATCIMLPEFQPQKVWEILLTSKAPMVNVfmaVPTIYSKLIQ 328
Cdd:cd05912 106 AIGSALNLGLTEDDNWLCALPLFHISGL-SILMRSVIYGMTVYLVDKFDAEQVLHLINSGKVTIISV---VPTMLQRLLE 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 329 YYDQHftqphvkdfvkavCKQRIRLMVSGSAALPLPTLQRWEEiTGHTLLERYGMTEIG--MALSNPLKGPRIPGAVGSP 406
Cdd:cd05912 182 ILGEG-------------YPNNLRCILLGGGPAPKPLLEQCKE-KGIPVYQSYGMTETCsqIVTLSPEDALNKIGSAGKP 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 407 LPGVEIRIVMSNatnttiveanhretrvrsGLEGKEGELLVRGPSVFKEYWNKHQETRESFTDsGWFKTGDTA-IHKDGV 485
Cdd:cd05912 248 LFPVELKIEDDG------------------QPPYEVGEILLKGPNVTKGYLNRPDATEESFEN-GWFKTGDIGyLDEEGF 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 486 FWIMGRTSvDIIKSGGYKISALEVERHLLAHPAIADVAVIGPPDAIWGQKVTAVMQLKRghRLTLPELKIWAREHMAPYI 565
Cdd:cd05912 309 LYVLDRRS-DLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSER--PISEEELIAYCSEKLAKYK 385
|
490 500
....*....|....*....|....
gi 2105456023 566 IPTGLVLVEELPRNQMGKVNKKDL 589
Cdd:cd05912 386 VPKKIYFVDELPRTASGKLLRHEL 409
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
80-589 |
6.36e-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: 208.49 E-value: 6.36e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 80 RLAIIDSSGSHSYKQLycssFGLAGRISAALNSDFGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLYRKHPQEELE 159
Cdd:cd05958 1 RTCLRSPEREWTYRDL----LALANRIANVLVGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 160 YIISdsqssllvagnsfaKTLEPLALklglpcltlpptsnlstLDGTDSQEEEAAItdWAdrpamiiYTSGTTGRPKGVL 239
Cdd:cd05958 77 YILD--------------KARITVAL-----------------CAHALTASDDICI--LA-------FTSGTTGAPKATM 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 240 HTHSSIQAMVQClvseWA-----WTRDDVILHTLPLHHVHGIVNKLLCPLWVGATCIMLPEFQPQKVWEILLTSKapmVN 314
Cdd:cd05958 117 HFHRDPLASADR----YAvnvlrLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEEATPDLLLSAIARYK---PT 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 315 VFMAVPTIYSKLIQYYDqhFTQPHVKDfvkavckqrIRLMVSGSAALPLPTLQRWEEITGHTLLERYGMTE-IGMALSNP 393
Cdd:cd05958 190 VLFTAPTAYRAMLAHPD--AAGPDLSS---------LRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEmFHIFISAR 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 394 LKGPRiPGAVGSPLPGVEIRIVMSNAtnttiveanhretrvRSGLEGKEGELLVRGPSVfkeYWNKHQETRESFTDSGWF 473
Cdd:cd05958 259 PGDAR-PGATGKPVPGYEAKVVDDEG---------------NPVPDGTIGRLAVRGPTG---CRYLADKRQRTYVQGGWN 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 474 KTGDT-AIHKDGVFWIMGRtSVDIIKSGGYKISALEVERHLLAHPAIADVAVIGPPDAIWGQKVTAVMQLKRGHR---LT 549
Cdd:cd05958 320 ITGDTySRDPDGYFRHQGR-SDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIpgpVL 398
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 2105456023 550 LPELKIWAREHMAPYIIPTGLVLVEELPRNQMGKVNKKDL 589
Cdd:cd05958 399 ARELQDHAKAHIAPYKYPRAIEFVTELPRTATGKLQRFAL 438
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
73-589 |
5.62e-60 |
|
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: 208.46 E-value: 5.62e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 73 RAPAFGDRLAIIDSSGSHSYKQLYCSSFGLAGRISAAlnsdfgGLE-GKRISFLCANDASYTVAQWAAWMSGgtAVPLY- 150
Cdd:COG1021 34 RAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLAL------GLRpGDRVVVQLPNVAEFVIVFFALFRAG--AIPVFa 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 151 -RKHPQEELEYIISDSQSSLLVAGNSFAKT-LEPLA--LKLGLPCLTL-------PPTSNLSTLDGTDSQEEEAAITdwA 219
Cdd:COG1021 106 lPAHRRAEISHFAEQSEAVAYIIPDRHRGFdYRALAreLQAEVPSLRHvlvvgdaGEFTSLDALLAAPADLSEPRPD--P 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 220 DRPAMIIYTSGTTGRPKGVLHTHS----SIQAMVQClvseWAWTRDDVILHTLPLHHvhgivN-KLLCP-----LWVGAT 289
Cdd:COG1021 184 DDVAFFQLSGGTTGLPKLIPRTHDdylySVRASAEI----CGLDADTVYLAALPAAH-----NfPLSSPgvlgvLYAGGT 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 290 CIMLPEFQPQKVWEILLTSKapmVNVFMAVPTIYSKLIQYYDQHFTQPhvkdfvkavckQRIRLMVSGSAALPLPTLQRW 369
Cdd:COG1021 255 VVLAPDPSPDTAFPLIERER---VTVTALVPPLALLWLDAAERSRYDL-----------SSLRVLQVGGAKLSPELARRV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 370 EEITGHTLLERYGMTEiGMALSNPLKGPR--IPGAVGSPL-PGVEIRIVmsnatnttivEANHRETRvrsglEGKEGELL 446
Cdd:COG1021 321 RPALGCTLQQVFGMAE-GLVNYTRLDDPEevILTTQGRPIsPDDEVRIV----------DEDGNPVP-----PGEVGELL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 447 VRGPSVFKEYWNKHQETRESFTDSGWFKTGDTA-IHKDGVFWIMGRtSVDIIKSGGYKISALEVERHLLAHPAIADVAVI 525
Cdd:COG1021 385 TRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVrRTPDGYLVVEGR-AKDQINRGGEKIAAEEVENLLLAHPAVHDAAVV 463
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2105456023 526 GPPDAIWGQKVTAVMQLkRGHRLTLPELKIWARE-HMAPYIIPTGLVLVEELPRNQMGKVNKKDL 589
Cdd:COG1021 464 AMPDEYLGERSCAFVVP-RGEPLTLAELRRFLRErGLAAFKLPDRLEFVDALPLTAVGKIDKKAL 527
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
79-592 |
2.95e-59 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 205.20 E-value: 2.95e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 79 DRLAIIDSSGSHSYKQLYCSSFGLAGRISAalnsdFGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLYRKHPQEEL 158
Cdd:PRK03640 17 DRTAIEFEEKKVTFMELHEAVVSVAGKLAA-----LGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREEL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 159 EYIISDSQSSLLVAGNSFAKTLEPLAlklglpcltlppTSNLSTLDGTDSQEEEAaITDWA-DRPAMIIYTSGTTGRPKG 237
Cdd:PRK03640 92 LWQLDDAEVKCLITDDDFEAKLIPGI------------SVKFAELMNGPKEEAEI-QEEFDlDEVATIMYTSGTTGKPKG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 238 VL-----HTHSSIQAMVQCLVSEwawtrDDVILHTLPLHHVHGIvNKLLCPLWVGATCIMLPEFQPQKVWEILLTSKAPM 312
Cdd:PRK03640 159 VIqtygnHWWSAVGSALNLGLTE-----DDCWLAAVPIFHISGL-SILMRSVIYGMRVVLVEKFDAEKINKLLQTGGVTI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 313 VNVfmaVPTIYSKLIQYYDQHFTQPHVkdfvkavckqriRLMVSGSAALPLPTLQRWEEiTGHTLLERYGMTEIG---MA 389
Cdd:PRK03640 233 ISV---VSTMLQRLLERLGEGTYPSSF------------RCMLLGGGPAPKPLLEQCKE-KGIPVYQSYGMTETAsqiVT 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 390 LSNPLKGPRIpGAVGSPLPGVEIRIvmsnatnttiveanhrETRVRSGLEGKEGELLVRGPSVFKEYWNKHQETRESFTD 469
Cdd:PRK03640 297 LSPEDALTKL-GSAGKPLFPCELKI----------------EKDGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQD 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 470 sGWFKTGDTA-IHKDGVFWIMGRTSvDIIKSGGYKISALEVERHLLAHPAIADVAVIGPPDAIWGQkvTAVMQLKRGHRL 548
Cdd:PRK03640 360 -GWFKTGDIGyLDEEGFLYVLDRRS-DLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQ--VPVAFVVKSGEV 435
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 2105456023 549 TLPELKIWAREHMAPYIIPTGLVLVEELPRNQMGKvnkkdLLRH 592
Cdd:PRK03640 436 TEEELRHFCEEKLAKYKVPKRFYFVEELPRNASGK-----LLRH 474
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
220-589 |
2.98e-59 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 201.55 E-value: 2.98e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 220 DRPAMIIYTSGTTGRPKGVLHTHSSIQAMVQCLVSEWAWTRDDVILHTLPLHHVHGIVNKLLCPLWVGATCIMLP----- 294
Cdd:cd05944 2 DDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVVLAGpagyr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 295 -EFQPQKVWEILLTSKapmVNVFMAVPTIYSKLIQyydqhftQPHVKDFvkavckQRIRLMVSGSAALPLPTLQRWEEIT 373
Cdd:cd05944 82 nPGLFDNFWKLVERYR---ITSLSTVPTVYAALLQ-------VPVNADI------SSLRFAMSGAAPLPVELRARFEDAT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 374 GHTLLERYGMTEIGMALS-NPLKGPRIPGAVGSPLPGVEIRIVMSNATNTTIVEANHRETrvrsglegkeGELLVRGPSV 452
Cdd:cd05944 146 GLPVVEGYGLTEATCLVAvNPPDGPKRPGSVGLRLPYARVRIKVLDGVGRLLRDCAPDEV----------GEICVAGPGV 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 453 FKEYWNKhQETRESFTDSGWFKTGDTA-IHKDGVFWIMGRtSVDIIKSGGYKISALEVERHLLAHPAIADVAVIGPPDAI 531
Cdd:cd05944 216 FGGYLYT-EGNKNAFVADGWLNTGDLGrLDADGYLFITGR-AKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAH 293
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2105456023 532 WGQKVTAVMQLKRGHRLTLPELKIWAREHMAPY-IIPTGLVLVEELPRNQMGKVNKKDL 589
Cdd:cd05944 294 AGELPVAYVQLKPGAVVEEEELLAWARDHVPERaAVPKHIEVLEELPVTAVGKVFKPAL 352
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
79-589 |
1.10e-58 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 203.89 E-value: 1.10e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 79 DRLAIIDSSGSHSYKqlYCSSFGLAGRISAALNSdFGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLYRKHPQEEL 158
Cdd:PRK09088 10 QRLAAVDLALGRRWT--YAELDALVGRLAAVLRR-RGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASEL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 159 EYIISDSQSSLLVAGNSFAK-TLEPLALklglpcltlppTSNLSTLDGTDSQEEEAAItdwADRPAMIIYTSGTTGRPKG 237
Cdd:PRK09088 87 DALLQDAEPRLLLGDDAVAAgRTDVEDL-----------AAFIASADALEPADTPSIP---PERVSLILFTSGTSGQPKG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 238 VLHTHSSIQAMVQCLVSEWAWTRDDVILHTLPLHHVHGIVNKLLCPLWVGATCIMLPEFQPQKV--WeilLTSKAPMVNV 315
Cdd:PRK09088 153 VMLSERNLQQTAHNFGVLGRVDAHSSFLCDAPMFHIIGLITSVRPVLAVGGSILVSNGFEPKRTlgR---LGDPALGITH 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 316 FMAVPtiyskliQYYDQHFTQPhvkDFVKAVCKqRIRLMVSGSAALPLPTLQRWEEiTGHTLLERYGMTEIGMALSNPLK 395
Cdd:PRK09088 230 YFCVP-------QMAQAFRAQP---GFDAAALR-HLTALFTGGAPHAAEDILGWLD-DGIPMVDGFGMSEAGTVFGMSVD 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 396 GPRIP---GAVGSPLPGVEIRIVmsnatnttivEANHRETRVrsgleGKEGELLVRGPSVFKEYWNKHQETRESFTDSGW 472
Cdd:PRK09088 298 CDVIRakaGAAGIPTPTVQTRVV----------DDQGNDCPA-----GVPGELLLRGPNLSPGYWRRPQATARAFTGDGW 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 473 FKTGDTAIHK-DGVFWIMGRTSvDIIKSGGYKISALEVERHLLAHPAIADVAVIGPPDAIWGQKVTAVMQLKRGHRLTLP 551
Cdd:PRK09088 363 FRTGDIARRDaDGFFWVVDRKK-DMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADGAPLDLE 441
|
490 500 510
....*....|....*....|....*....|....*...
gi 2105456023 552 ELKIWAREHMAPYIIPTGLVLVEELPRNQMGKVNKKDL 589
Cdd:PRK09088 442 RIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARL 479
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
79-589 |
1.50e-58 |
|
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: 202.37 E-value: 1.50e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 79 DRLAIIDSSGSHSYKQLycssFGLAGRISAALNSDfGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLYRKHPQEEL 158
Cdd:cd05930 2 DAVAVVDGDQSLTYAEL----DARANRLARYLRER-GVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 159 EYIISDSQSSLLvagnsfaktleplalklglpcltlpptsnlstldgtdsqeeeaaITDwADRPAMIIYTSGTTGRPKGV 238
Cdd:cd05930 77 AYILEDSGAKLV--------------------------------------------LTD-PDDLAYVIYTSGSTGKPKGV 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 239 LHTHSSIQAMVQCLVSEWAWTRDDVILHTLPLHHVHGIVNkLLCPLWVGATCIMLPE---FQPQKVWEILLTSKapmVNV 315
Cdd:cd05930 112 MVEHRGLVNLLLWMQEAYPLTPGDRVLQFTSFSFDVSVWE-IFGALLAGATLVVLPEevrKDPEALADLLAEEG---ITV 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 316 FMAVPTIYSKLIQYYDQhftqphvkdfvkAVCKqRIRLMVSGSAALPLPTLQRWEEI-TGHTLLERYGMTEI-GMALSNP 393
Cdd:cd05930 188 LHLTPSLLRLLLQELEL------------AALP-SLRLVLVGGEALPPDLVRRWRELlPGARLVNLYGPTEAtVDATYYR 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 394 LKGPRIPGA---VGSPLPGVEIRIVmsnatnttivEANHRETRVrsgleGKEGELLVRGPSVFKEYWNKHQETRESFTDS 470
Cdd:cd05930 255 VPPDDEEDGrvpIGRPIPNTRVYVL----------DENLRPVPP-----GVPGELYIGGAGLARGYLNRPELTAERFVPN 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 471 GWF------KTGDTAIHK-DGVFWIMGRTSvDIIKSGGYKISALEVERHLLAHPAIADVAVIGPPDAIWGQKVTAVMQLK 543
Cdd:cd05930 320 PFGpgermyRTGDLVRWLpDGNLEFLGRID-DQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPD 398
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 2105456023 544 RGHRLTLPELKIWAREHMAPYIIPTGLVLVEELPRNQMGKVNKKDL 589
Cdd:cd05930 399 EGGELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
108-590 |
1.73e-58 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 205.27 E-value: 1.73e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 108 AALNSDFGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVP---LYRKHpqeELEYIISDSQSSLLVAGNSFAKTLEPLA 184
Cdd:PRK06178 72 AALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPvspLFREH---ELSYELNDAGAEVLLALDQLAPVVEQVR 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 185 LKLGL---------------PCLTLPP------------TSNLSTLDGTdSQEEEAAITDwADRPAMIIYTSGTTGRPKG 237
Cdd:PRK06178 149 AETSLrhvivtsladvlpaePTLPLPDslraprlaaagaIDLLPALRAC-TAPVPLPPPA-LDALAALNYTGGTTGMPKG 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 238 VLHTHSSI--QAMVQCLVSEwAWTRDDVILHTLPLHHVHGIVNKLLCPLWVGATCIMLPEFQPQKVWEILLTSKApmvnv 315
Cdd:PRK06178 227 CEHTQRDMvyTAAAAYAVAV-VGGEDSVFLSFLPEFWIAGENFGLLFPLFSGATLVLLARWDAVAFMAAVERYRV----- 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 316 fmavpTIYSKLIQYYDQHFTQPHVKDFVKAVCKQrIRlMVSGSAALPLPTLQRWEEITGHTLLE-RYGMTE--------I 386
Cdd:PRK06178 301 -----TRTVMLVDNAVELMDHPRFAEYDLSSLRQ-VR-VVSFVKKLNPDYRQRWRALTGSVLAEaAWGMTEthtcdtftA 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 387 GMALSN-PLKGPriPGAVGSPLPGVEIRIVMSNATNTTIVeanhretrvrsgleGKEGELLVRGPSVFKEYWNKHQETRE 465
Cdd:PRK06178 374 GFQDDDfDLLSQ--PVFVGLPVPGTEFKICDFETGELLPL--------------GAEGEIVVRTPSLLKGYWNKPEATAE 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 466 SFTDsGWFKTGDT-AIHKDGVFWIMGRTSvDIIKSGGYKISALEVERHLLAHPAIADVAVIGPPDAIWGQKVTAVMQLKR 544
Cdd:PRK06178 438 ALRD-GWLHTGDIgKIDEQGFLHYLGRRK-EMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKP 515
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 2105456023 545 GHRLTLPELKIWAREHMAPYIIPTgLVLVEELPRNQMGKVNKKDLL 590
Cdd:PRK06178 516 GADLTAAALQAWCRENMAVYKVPE-IRIVDALPMTATGKVRKQDLQ 560
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
222-586 |
6.30e-58 |
|
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341292 [Multi-domain] Cd Length: 333 Bit Score: 197.11 E-value: 6.30e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 222 PAMIIYTSGTTGRPKGVLHTHSSIQAMVQCLVSEWAWTRDDVILHTLPLHHVHGIvNKLLCPLWVGATCIMLPEFQPQKV 301
Cdd:cd17637 2 PFVIIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPLFHIAGL-NLALATFHAGGANVVMEKFDPAEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 302 WEILLTSKapmVNVFMAVPTIYSKLIQYYDQHFTQPhvkDFVKAVckqrirlmvsgsAALPLP-TLQRWEEITGHTLLER 380
Cdd:cd17637 81 LELIEEEK---VTLMGSFPPILSNLLDAAEKSGVDL---SSLRHV------------LGLDAPeTIQRFEETTGATFWSL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 381 YGMTEIGMALSNPLKGPRiPGAVGSPLPGVEIRIVmsnatnttivEANHRETRVrsgleGKEGELLVRGPSVFKEYWNKH 460
Cdd:cd17637 143 YGQTETSGLVTLSPYRER-PGSAGRPGPLVRVRIV----------DDNDRPVPA-----GETGEIVVRGPLVFQGYWNLP 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 461 QETRESFTDsGWFKTGDT-AIHKDGVFWIMGRTSV-DIIKSGGYKISALEVERHLLAHPAIADVAVIGPPDAIWGQKVTA 538
Cdd:cd17637 207 ELTAYTFRN-GWHHTGDLgRFDEDGYLWYAGRKPEkELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKA 285
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 2105456023 539 VMQLKRGHRLTLPELKIWAREHMAPYIIPTGLVLVEELPRNQMGKVNK 586
Cdd:cd17637 286 VCVLKPGATLTADELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
74-586 |
7.68e-58 |
|
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: 201.37 E-value: 7.68e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 74 APAFGDRLAIIDSSGSHSYKQLY--CssfglaGRISAALnSDFGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLYR 151
Cdd:cd12118 14 AAVYPDRTSIVYGDRRYTWRQTYdrC------RRLASAL-AALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 152 KHPQEELEYIISDSQSSLLVAGNSFakTLEPLaLKLGLP-CLTLPPtsnlstldgtdsQEEEAAITdwadrpamIIYTSG 230
Cdd:cd12118 87 RLDAEEIAFILRHSEAKVLFVDREF--EYEDL-LAEGDPdFEWIPP------------ADEWDPIA--------LNYTSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 231 TTGRPKGVLHTHSSiqAMVQCL--VSEWAWTRDDVILHTLPLHHVHGivnklLCPLW----VGATCIMLPEFQPQKVWEI 304
Cdd:cd12118 144 TTGRPKGVVYHHRG--AYLNALanILEWEMKQHPVYLWTLPMFHCNG-----WCFPWtvaaVGGTNVCLRKVDAKAIYDL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 305 LLTSKapmVNVFMAVPTIYSKLIQYydqhftqphvKDFVKAVCKQRIRLMVSGSAAlPLPTLQRWEEItGHTLLERYGMT 384
Cdd:cd12118 217 IEKHK---VTHFCGAPTVLNMLANA----------PPSDARPLPHRVHVMTAGAPP-PAAVLAKMEEL-GFDVTHVYGLT 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 385 EI-GMALSNPLKgpriPGAVGSPLP---------GVeiRIVMSNAtnttiVEANHRETRVRSGLEGKE-GELLVRGPSVF 453
Cdd:cd12118 282 ETyGPATVCAWK----PEWDELPTEerarlkarqGV--RYVGLEE-----VDVLDPETMKPVPRDGKTiGEIVFRGNIVM 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 454 KEYWNKHQETRESFTDsGWFKTGDTA-IHKDGVFWIMGRtSVDIIKSGGYKISALEVERHLLAHPAIADVAVIGPPDAIW 532
Cdd:cd12118 351 KGYLKNPEATAEAFRG-GWFHSGDLAvIHPDGYIEIKDR-SKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKW 428
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 2105456023 533 GQKVTAVMQLKRGHRLTLPELKIWAREHMAPYIIPTGLVlVEELPRNQMGKVNK 586
Cdd:cd12118 429 GEVPCAFVELKEGAKVTEEEIIAFCREHLAGFMVPKTVV-FGELPKTSTGKIQK 481
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
91-589 |
4.81e-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: 198.06 E-value: 4.81e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 91 SYKQLYCSSFGLAGRISAalnsdFGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLYRKHPQEELEYIISDSQSSLL 170
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKA-----QGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 171 VAGNSFakTLEPLAlklglpcltlppTSNLSTLDGTDSQEEEAAITDWADRPAMIIYTSGTTGRPKGVLHTHSSIQAMVQ 250
Cdd:TIGR01923 76 LTDSLL--EEKDFQ------------ADSLDRIEAAGRYETSLSASFNMDQIATLMFTSGTTGKPKAVPHTFRNHYASAV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 251 CLVSEWAWTRDDVILHTLPLHHVHGiVNKLLCPLWVGATCIMlpefqPQKVWEILLTSKAPMVNVFMAVPTIYSKLIQyy 330
Cdd:TIGR01923 142 GSKENLGFTEDDNWLLSLPLYHISG-LSILFRWLIEGATLRI-----VDKFNQLLEMIANERVTHISLVPTQLNRLLD-- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 331 dqhftqphvkdfvKAVCKQRIRLMVSGSAALPLPTLQRWEEiTGHTLLERYGMTEIG---MALSNPLKGPRipGAVGSPL 407
Cdd:TIGR01923 214 -------------EGGHNENLRKILLGGSAIPAPLIEEAQQ-YGLPIYLSYGMTETCsqvTTATPEMLHAR--PDVGRPL 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 408 PGVEIRIVmsnatnttiveanhretrvRSGLEGkEGELLVRGPSVFKEYWNKhQETRESFTDSGWFKTGDTA-IHKDGVF 486
Cdd:TIGR01923 278 AGREIKIK-------------------VDNKEG-HGEIMVKGANLMKGYLYQ-GELTPAFEQQGWFNTGDIGeLDGEGFL 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 487 WIMGRTSvDIIKSGGYKISALEVERHLLAHPAIADVAVIGPPDAIWGQKVTAVMQLKRghRLTLPELKIWAREHMAPYII 566
Cdd:TIGR01923 337 YVLGRRD-DLIISGGENIYPEEIETVLYQHPGIQEAVVVPKPDAEWGQVPVAYIVSES--DISQAKLIAYLTEKLAKYKV 413
|
490 500
....*....|....*....|...
gi 2105456023 567 PTGLVLVEELPRNQMGKVNKKDL 589
Cdd:TIGR01923 414 PIAFEKLDELPYNASGKILRNQL 436
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
143-589 |
3.52e-56 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 197.60 E-value: 3.52e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 143 GGTAVPLYRKHPQEELEYIISDSQSSLLVAGNSFAKTLEPLALKLGLP----CLT------LPPTSNLSTLDGTDSQEEE 212
Cdd:PRK08008 86 GAIMVPINARLLREESAWILQNSQASLLVTSAQFYPMYRQIQQEDATPlrhiCLTrvalpaDDGVSSFTQLKAQQPATLC 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 213 AAITDWADRPAMIIYTSGTTGRPKGVLHTHSSIQamVQCLVSEW--AWTRDDVILHTLPLHHVHGIVNKLLCPLWVGATC 290
Cdd:PRK08008 166 YAPPLSTDDTAEILFTSGTTSRPKGVVITHYNLR--FAGYYSAWqcALRDDDVYLTVMPAFHIDCQCTAAMAAFSAGATF 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 291 IMLPEFQPQKVWEILLTSKApmvNVFMAVPTIYSKLIqyydqhfTQPhVKDFVKAVCKQRIRLMVSGSAALPLPTLQRWe 370
Cdd:PRK08008 244 VLLEKYSARAFWGQVCKYRA---TITECIPMMIRTLM-------VQP-PSANDRQHCLREVMFYLNLSDQEKDAFEERF- 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 371 eitGHTLLERYGMTE-IGMALSNPLKGPRIPGAVGSPLPGVEIRIVmsnatnttivEANHRETRVrsgleGKEGELLVRG 449
Cdd:PRK08008 312 ---GVRLLTSYGMTEtIVGIIGDRPGDKRRWPSIGRPGFCYEAEIR----------DDHNRPLPA-----GEIGEICIKG 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 450 ---PSVFKEYWNKHQETRESFTDSGWFKTGDTA-IHKDGVFWIMGRtSVDIIKSGGYKISALEVERHLLAHPAIADVAVI 525
Cdd:PRK08008 374 vpgKTIFKEYYLDPKATAKVLEADGWLHTGDTGyVDEEGFFYFVDR-RCNMIKRGGENVSCVELENIIATHPKIQDIVVV 452
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2105456023 526 GPPDAIWGQKVTAVMQLKRGHRLTLPELKIWAREHMAPYIIPTGLVLVEELPRNQMGKVNKKDL 589
Cdd:PRK08008 453 GIKDSIRDEAIKAFVVLNEGETLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNL 516
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
102-589 |
8.44e-56 |
|
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: 195.03 E-value: 8.44e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 102 LAGRISAALnSDFGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLYRKHPQEELEYIISDSQSSLLVAGNSFAKTLE 181
Cdd:cd05969 9 LSARFANVL-KSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTEELYERTD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 182 PlalklglpcltlpptsnlstldgtdsqeeeaaitdwaDRPAMIIYTSGTTGRPKGVLHTHSsiqAMVQCLVSEwAWT-- 259
Cdd:cd05969 88 P-------------------------------------EDPTLLHYTSGTTGTPKGVLHVHD---AMIFYYFTG-KYVld 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 260 --RDDVILHTLPLHHVHGIVNKLLCPLWVGATCIMLP-EFQPQKVWEILLTSKapmVNVFMAVPTIYSKLIQYYDQhftq 336
Cdd:cd05969 127 lhPDDIYWCTADPGWVTGTVYGIWAPWLNGVTNVVYEgRFDAESWYGIIERVK---VTVWYTAPTAIRMLMKEGDE---- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 337 phvkdFVKAVCKQRIRLMVSGSAALPlPTLQRW-EEITGHTLLERYGMTEIG-MALSNPLKGPRIPGAVGSPLPGVEIRI 414
Cdd:cd05969 200 -----LARKYDLSSLRFIHSVGEPLN-PEAIRWgMEVFGVPIHDTWWQTETGsIMIANYPCMPIKPGSMGKPLPGVKAAV 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 415 VMSNAtnttiveanhretrvrSGLE-GKEGELLVRG--PSVFKEYWNKHQETRESFTDsGWFKTGDTA-IHKDGVFWIMG 490
Cdd:cd05969 274 VDENG----------------NELPpGTKGILALKPgwPSMFRGIWNDEERYKNSFID-GWYLTGDLAyRDEDGYFWFVG 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 491 RTSvDIIKSGGYKISALEVERHLLAHPAIADVAVIGPPDAIWGQKVTAVMQLKRGHRLTLP---ELKIWAREHMAPYIIP 567
Cdd:cd05969 337 RAD-DIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPSDElkeEIINFVRQKLGAHVAP 415
|
490 500
....*....|....*....|..
gi 2105456023 568 TGLVLVEELPRNQMGKVNKKDL 589
Cdd:cd05969 416 REIEFVDNLPKTRSGKIMRRVL 437
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
80-589 |
8.55e-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: 194.60 E-value: 8.55e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 80 RLAIIDSSGSHSYKQLYCSsfglAGRISAALNSdFGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLYRKHPQEELE 159
Cdd:cd05919 1 KTAFYAADRSVTYGQLHDG----ANRLGSALRN-LGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 160 YIISDSQSSLLVAgnsfaktleplalklglpcltlpptsnlstldgtdsqeEEAAITDWadrpamiIYTSGTTGRPKGVL 239
Cdd:cd05919 76 YIARDCEARLVVT--------------------------------------SADDIAYL-------LYSSGTTGPPKGVM 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 240 HTHSSIQAMVQCLVSEW-AWTRDDVILHTLPLHHVHGIVNKLLCPLWVGATCIMLPEfqPQKVWEILLTSKAPMVNVFMA 318
Cdd:cd05919 111 HAHRDPLLFADAMAREAlGLTPGDRVFSSAKMFFGYGLGNSLWFPLAVGASAVLNPG--WPTAERVLATLARFRPTVLYG 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 319 VPTIYSKLIqyyDQHFTQPHvkDFVKavckqrIRLMVSGSAALPLPTLQRWEEITGHTLLERYGMTEIG-MALSNPLKGP 397
Cdd:cd05919 189 VPTFYANLL---DSCAGSPD--ALRS------LRLCVSAGEALPRGLGERWMEHFGGPILDGIGATEVGhIFLSNRPGAW 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 398 RiPGAVGSPLPGVEIRIVmsnATNTTIVEAnhretrvrsgleGKEGELLVRGPSVFKEYWNKHQETRESFTDsGWFKTGD 477
Cdd:cd05919 258 R-LGSTGRPVPGYEIRLV---DEEGHTIPP------------GEEGDLLVRGPSAAVGYWNNPEKSRATFNG-GWYRTGD 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 478 T-AIHKDGVFWIMGRtSVDIIKSGGYKISALEVERHLLAHPAIADVAVIGPPDAIWGQKVTAVMQLKRG---HRLTLPEL 553
Cdd:cd05919 321 KfCRDADGWYTHAGR-ADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPaapQESLARDI 399
|
490 500 510
....*....|....*....|....*....|....*.
gi 2105456023 554 KIWAREHMAPYIIPTGLVLVEELPRNQMGKVNKKDL 589
Cdd:cd05919 400 HRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKL 435
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
118-590 |
2.90e-55 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 196.41 E-value: 2.90e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 118 EGKRISFLCANDASYTVAQWAAWMSGGTAV---PLYrkhPQEELEYIISDSQSSLL---------VAGNSFAKTLEPLAL 185
Cdd:PRK06710 73 KGDRVAIMLPNCPQAVIGYYGTLLAGGIVVqtnPLY---TERELEYQLHDSGAKVIlcldlvfprVTNVQSATKIEHVIV 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 186 K-----LGLPCLTLPP-----TSNL-------STLDGTDSQEEEA-----AITDWADRPAMIIYTSGTTGRPKGVLHTHS 243
Cdd:PRK06710 150 TriadfLPFPKNLLYPfvqkkQSNLvvkvsesETIHLWNSVEKEVntgveVPCDPENDLALLQYTGGTTGFPKGVMLTHK 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 244 S--------IQAMVQCLVSEwawtrdDVILHTLPLHHVHGIVNKLLCPLWVGATCIMLPEFQPQKVWEILLTSKapmVNV 315
Cdd:PRK06710 230 NlvsntlmgVQWLYNCKEGE------EVVLGVLPFFHVYGMTAVMNLSIMQGYKMVLIPKFDMKMVFEAIKKHK---VTL 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 316 FMAVPTIYSKLIQyydqhftQPHVKDFVKAvckqRIRLMVSGSAALPLPTLQRWEEITGHTLLERYGMTEIG-MALSNPL 394
Cdd:PRK06710 301 FPGAPTIYIALLN-------SPLLKEYDIS----SIRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTESSpVTHSNFL 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 395 KGPRIPGAVGSPLPGVEIRIvMSNATNTTIVEanhretrvrsgleGKEGELLVRGPSVFKEYWNKHQETRESFTDsGWFK 474
Cdd:PRK06710 370 WEKRVPGSIGVPWPDTEAMI-MSLETGEALPP-------------GEIGEIVVKGPQIMKGYWNKPEETAAVLQD-GWLH 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 475 TGDTA-IHKDGVFWIMGRTSvDIIKSGGYKISALEVERHLLAHPAIADVAVIGPPDAIWGQKVTAVMQLKRGHRLTLPEL 553
Cdd:PRK06710 435 TGDVGyMDEDGFFYVKDRKK-DMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVLKEGTECSEEEL 513
|
490 500 510
....*....|....*....|....*....|....*..
gi 2105456023 554 KIWAREHMAPYIIPTGLVLVEELPRNQMGKVNKKDLL 590
Cdd:PRK06710 514 NQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVLI 550
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
119-593 |
5.67e-55 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 195.00 E-value: 5.67e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 119 GKRISFLCANDASYTVAQWAAWMSGGTAVPL-YRKHPQEeLEYIISDSQSSLLVAGNSfaktLEPLA--LKLGLPCLTLP 195
Cdd:PRK07786 67 GDRVLILMLNRTEFVESVLAANMLGAIAVPVnFRLTPPE-IAFLVSDCGAHVVVTEAA----LAPVAtaVRDIVPLLSTV 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 196 PTSNLSTLDGTDSQEEEAAITDWA--------DRPAMIIYTSGTTGRPKGVLHTHSSI--QAMVqCLVSEWAWTRDDVIL 265
Cdd:PRK07786 142 VVAGGSSDDSVLGYEDLLAEAGPAhapvdipnDSPALIMYTSGTTGRPKGAVLTHANLtgQAMT-CLRTNGADINSDVGF 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 266 HTLPLHHVHGIVNkLLCPLWVGATCIMLP--EFQPQKVWEILLTSKApmVNVFMaVPTiyskliQYydqhftqphvkdfv 343
Cdd:PRK07786 221 VGVPLFHIAGIGS-MLPGLLLGAPTVIYPlgAFDPGQLLDVLEAEKV--TGIFL-VPA------QW-------------- 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 344 KAVC-KQRIR------LMVSGSAALPLPTLQR--WEEITGHTLLERYGMTEIGmALSNPLKGP---RIPGAVGSPLPGVE 411
Cdd:PRK07786 277 QAVCaEQQARprdlalRVLSWGAAPASDTLLRqmAATFPEAQILAAFGQTEMS-PVTCMLLGEdaiRKLGSVGKVIPTVA 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 412 IRIVMSNATNTTIveanhretrvrsgleGKEGELLVRGPSVFKEYWNKHQETRESFtDSGWFKTGDTA-IHKDGVFWIMG 490
Cdd:PRK07786 356 ARVVDENMNDVPV---------------GEVGEIVYRAPTLMSGYWNNPEATAEAF-AGGWFHSGDLVrQDEEGYVWVVD 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 491 RTSvDIIKSGGYKISALEVERHLLAHPAIADVAVIGPPDAIWGQKVTAVMQLKRG-HRLTLPELKIWAREHMAPYIIPTG 569
Cdd:PRK07786 420 RKK-DMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRNDdAALTLEDLAEFLTDRLARYKHPKA 498
|
490 500
....*....|....*....|....
gi 2105456023 570 LVLVEELPRNQMGKVNKKDLLRHF 593
Cdd:PRK07786 499 LEIVDALPRNPAGKVLKTELRERY 522
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
79-589 |
2.66e-54 |
|
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: 190.92 E-value: 2.66e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 79 DRLAIIDSSGSHSYKQLYCSSFGLAGRISAAlnsdfGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLYRKHPQEEL 158
Cdd:cd05945 6 DRPAVVEGGRTLTYRELKERADALAAALASL-----GLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 159 EYIISDSQSSLLVAgnsfaktleplalklglpcltlpptsnlstlDGTDsqeeeaaitdwadrPAMIIYTSGTTGRPKGV 238
Cdd:cd05945 81 REILDAAKPALLIA-------------------------------DGDD--------------NAYIIFTSGSTGRPKGV 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 239 LHTHSSIQAMVQCLVSEWAWTRDDVILHTLPLH---HVHGIvnklLCPLWVGATCIMLPEFQPQKVWEILLTSKAPMVNV 315
Cdd:cd05945 116 QISHDNLVSFTNWMLSDFPLGPGDVFLNQAPFSfdlSVMDL----YPALASGATLVPVPRDATADPKQLFRFLAEHGITV 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 316 FMAVPTIYSKLIQyyDQHFTQPHVKdfvkavckqRIRLMVSGSAALPLPTLQRWEEIT-GHTLLERYGMTEIGMALS--- 391
Cdd:cd05945 192 WVSTPSFAAMCLL--SPTFTPESLP---------SLRHFLFCGEVLPHKTARALQQRFpDARIYNTYGPTEATVAVTyie 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 392 ---NPLKG-PRIPgaVGSPLPGVEIrivmsnatntTIVEANHRETRvrsglEGKEGELLVRGPSVFKEYWNKHQETRESF 467
Cdd:cd05945 261 vtpEVLDGyDRLP--IGYAKPGAKL----------VILDEDGRPVP-----PGEKGELVISGPSVSKGYLNNPEKTAAAF 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 468 -TDSG--WFKTGDTA-IHKDGVFWIMGRTSvDIIKSGGYKISALEVERHLLAHPAIADVAVIGPPDAIWGQKVTAVMQLK 543
Cdd:cd05945 324 fPDEGqrAYRTGDLVrLEADGLLFYRGRLD-FQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPK 402
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 2105456023 544 RGHRLTLP-ELKIWAREHMAPYIIPTGLVLVEELPRNQMGKVNKKDL 589
Cdd:cd05945 403 PGAEAGLTkAIKAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
72-589 |
4.47e-54 |
|
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.
Pssm-ID: 341244 [Multi-domain] Cd Length: 482 Bit Score: 191.39 E-value: 4.47e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 72 VRAPAFGDRLAIIDSSGSHSYKQLYCSSFGLAGRISaalnsDFGGLEGKRISFLCANDASYTVAqWAAWMSGGT----AV 147
Cdd:cd05920 23 RSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLR-----GLGIRPGDRVVVQLPNVAEFVVL-FFALLRLGAvpvlAL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 148 PLYRKHpqeELEYIISDSQSSLLVAGNSFAKtLEPLALklglpcltlpptsnlstldgtdSQEEEAAITDwadrPAMIIY 227
Cdd:cd05920 97 PSHRRS---ELSAFCAHAEAVAYIVPDRHAG-FDHRAL----------------------ARELAESIPE----VALFLL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 228 TSGTTGRPKGVLHTHSSIQAMVQCLVsEWAW-TRDDVILHTLPLHHvhgivN-KLLCP-----LWVGATCIMLPEFQPQK 300
Cdd:cd05920 147 SGGTTGTPKLIPRTHNDYAYNVRASA-EVCGlDQDTVYLAVLPAAH-----NfPLACPgvlgtLLAGGRVVLAPDPSPDA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 301 VWEILLTSKapmVNVFMAVPTIYSKLIQYYDQHFTQPhvkdfvkavckQRIRLMVSGSAALPLPTLQRWEEITGHTLLER 380
Cdd:cd05920 221 AFPLIEREG---VTVTALVPALVSLWLDAAASRRADL-----------SSLRLLQVGGARLSPALARRVPPVLGCTLQQV 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 381 YGMTEiGM----ALSNPlkGPRIPGAVGSPL-PGVEIRIVmsnatnttivEANHRETRvrsglEGKEGELLVRGPSVFKE 455
Cdd:cd05920 287 FGMAE-GLlnytRLDDP--DEVIIHTQGRPMsPDDEIRVV----------DEEGNPVP-----PGEEGELLTRGPYTIRG 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 456 YWNKHQETRESFTDSGWFKTGDTA-IHKDGVFWIMGRTSvDIIKSGGYKISALEVERHLLAHPAIADVAVIGPPDAIWGQ 534
Cdd:cd05920 349 YYRAPEHNARAFTPDGFYRTGDLVrRTPDGYLVVEGRIK-DQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGE 427
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 2105456023 535 KVTAVMQLkRGHRLTLPELKIWAREH-MAPYIIPTGLVLVEELPRNQMGKVNKKDL 589
Cdd:cd05920 428 RSCAFVVL-RDPPPSAAQLRRFLRERgLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
73-589 |
5.14e-52 |
|
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: 185.79 E-value: 5.14e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 73 RAPafgDRLAIIDSSGSH--SYKQLYCSSFGLAgrisAALNSDfGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLY 150
Cdd:cd05923 13 RAP---DACAIADPARGLrlTYSELRARIEAVA----ARLHAR-GLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALIN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 151 RKHPQEELEYIISDSQSSLLVAGNsfAKTLEPLALKLGLPCLTLpptsnlSTLDGTDSQEEEA-AITDWADRP---AMII 226
Cdd:cd05923 85 PRLKAAELAELIERGEMTAAVIAV--DAQVMDAIFQSGVRVLAL------SDLVGLGEPESAGpLIEDPPREPeqpAFVF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 227 YTSGTTGRPKGVL--HTHSSIQAMVQCLVSEWAWTRDDVILHTLPLHHVHGIVNKLLCPLWVGATCIMLPEFQPQKVWEi 304
Cdd:cd05923 157 YTSGTTGLPKGAVipQRAAESRVLFMSTQAGLRHGRHNVVLGLMPLYHVIGFFAVLVAALALDGTYVVVEEFDPADALK- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 305 lLTSKAPMVNVFmAVPTIYSKLIqyydqhftqpHVKDFVKAVCKQRIRLMVSGsAALPLPTLQRWEEITGHTLLERYGMT 384
Cdd:cd05923 236 -LIEQERVTSLF-ATPTHLDALA----------AAAEFAGLKLSSLRHVTFAG-ATMPDAVLERVNQHLPGEKVNIYGTT 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 385 EIGMALSNPlkGPRiPGAVGSPLPGVEIRIVMSNATNTTIVEAnhretrvrsgleGKEGELLVR--GPSVFKEYWNKHQE 462
Cdd:cd05923 303 EAMNSLYMR--DAR-TGTEMRPGFFSEVRIVRIGGSPDEALAN------------GEEGELIVAaaADAAFTGYLNQPEA 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 463 TRESFTDsGWFKTGDTA-IHKDGVFWIMGRTSvDIIKSGGYKISALEVERHLLAHPAIADVAVIGPPDAIWGQKVTAVMQ 541
Cdd:cd05923 368 TAKKLQD-GWYRTGDVGyVDPSGDVRILGRVD-DMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVV 445
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 2105456023 542 LKRGhRLTLPELKIWARE-HMAPYIIPTGLVLVEELPRNQMGKVNKKDL 589
Cdd:cd05923 446 PREG-TLSADELDQFCRAsELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
220-589 |
1.03e-51 |
|
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: 181.32 E-value: 1.03e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 220 DRPAMIIYTSGTTGRPKGVLHTHSSI--------QAMvqclvsewAWTRDDVILHTLPLHHVHGIVNKLLCPLWVGATCI 291
Cdd:cd05917 2 DDVINIQFTSGTTGSPKGATLTHHNIvnngyfigERL--------GLTEQDRLCIPVPLFHCFGSVLGVLACLTHGATMV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 292 ML-PEFQPQKVWEILLTSKApmvNVFMAVPTIYSKLIQYYDQHFTQPHvkdfvkavckqRIRLMVSGSAALPLPTLQRWE 370
Cdd:cd05917 74 FPsPSFDPLAVLEAIEKEKC---TALHGVPTMFIAELEHPDFDKFDLS-----------SLRTGIMAGAPCPPELMKRVI 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 371 EITGHT-LLERYGMTE----IGMALSNPLKGPRIpGAVGSPLPGVEIRIVMSnatnttiveanhrETRVRSGLeGKEGEL 445
Cdd:cd05917 140 EVMNMKdVTIAYGMTEtspvSTQTRTDDSIEKRV-NTVGRIMPHTEAKIVDP-------------EGGIVPPV-GVPGEL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 446 LVRGPSVFKEYWNKHQETRESFTDSGWFKTGDTAI-HKDGVFWIMGRTSvDIIKSGGYKISALEVERHLLAHPAIADVAV 524
Cdd:cd05917 205 CIRGYSVMKGYWNDPEKTAEAIDGDGWLHTGDLAVmDEDGYCRIVGRIK-DMIIRGGENIYPREIEEFLHTHPKVSDVQV 283
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2105456023 525 IGPPDAIWGQKVTAVMQLKRGHRLTLPELKIWAREHMAPYIIPTGLVLVEELPRNQMGKVNKKDL 589
Cdd:cd05917 284 VGVPDERYGEEVCAWIRLKEGAELTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKL 348
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
91-589 |
3.85e-51 |
|
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: 182.25 E-value: 3.85e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 91 SYKQLYCSSFGLAGRISAAlnsdfgGLE-GKRISFLCANDASYTVAQWAAWMSGGTAVPLYRKHPQEELEYIISDSQSSL 169
Cdd:cd05971 8 TFKELKTASNRFANVLKEI------GLEkGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 170 LVagnsfaktleplalklglpcltlpptsnlstldgtdsqeeeaaiTDWADRPAMIIYTSGTTGRPKGVLHTHS------ 243
Cdd:cd05971 82 LV--------------------------------------------TDGSDDPALIIYTSGTTGPPKGALHAHRvllghl 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 244 -SIQAMVQCL---------VSEWAWtrddvilhtlplhhVHGIVNKLLCPLWVGATCIM--LPEFQPQKVWEILLTSKap 311
Cdd:cd05971 118 pGVQFPFNLFprdgdlywtPADWAW--------------IGGLLDVLLPSLYFGVPVLAhrMTKFDPKAALDLMSRYG-- 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 312 MVNVFMAvPTIYSKLIQYYDQhftqphVKDFvkavcKQRIRLMVSGSAALPLPTLQRWEEITGHTLLERYGMTEIGMALS 391
Cdd:cd05971 182 VTTAFLP-PTALKMMRQQGEQ------LKHA-----QVKLRAIATGGESLGEELLGWAREQFGVEVNEFYGQTECNLVIG 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 392 N-PLKGPRIPGAVGSPLPGVEIRIVMSNATNTTIveanhretrvrsgleGKEGELLVRGPS--VFKEYWNKHQETRESFT 468
Cdd:cd05971 250 NcSALFPIKPGSMGKPIPGHRVAIVDDNGTPLPP---------------GEVGEIAVELPDpvAFLGYWNNPSATEKKMA 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 469 dSGWFKTGDTAIH-KDGVFWIMGRTSvDIIKSGGYKISALEVERHLLAHPAIADVAVIGPPDAIWGQKVTAVMQLKRGHr 547
Cdd:cd05971 315 -GDWLLTGDLGRKdSDGYFWYVGRDD-DVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGE- 391
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 2105456023 548 LTLPELKIWAREH----MAPYIIPTGLVLVEELPRNQMGKVNKKDL 589
Cdd:cd05971 392 TPSDALAREIQELvktrLAAHEYPREIEFVNELPRTATGKIRRREL 437
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
82-589 |
1.38e-49 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 179.33 E-value: 1.38e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 82 AIIDSSG-SHSYKQLYCSSFGLAGRISAAlnsdfgGL-EGKRISFLCANDASYTVAQWAAWMSGGTAVPLYRKHPQEELE 159
Cdd:PRK08276 3 VIMAPSGeVVTYGELEARSNRLAHGLRAL------GLrEGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 160 YIISDSQSSLLVAGNSFAKTLEPLALKLGLPCLTLppTSNLSTLDGTDSQEEEAAI---TDWADRPA--MIIYTSGTTGR 234
Cdd:PRK08276 77 YIVDDSGAKVLIVSAALADTAAELAAELPAGVPLL--LVVAGPVPGFRSYEEALAAqpdTPIADETAgaDMLYSSGTTGR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 235 PKGVLH--THSSI---QAMVQCLVSEWAWTRDD-VILHTLPLHHV-----HGIVNKLlcplwvGATCIMLPEFQPQKVWE 303
Cdd:PRK08276 155 PKGIKRplPGLDPdeaPGMMLALLGFGMYGGPDsVYLSPAPLYHTaplrfGMSALAL------GGTVVVMEKFDAEEALA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 304 ILLTSKapmVNVFMAVPTIYSKLIQYydqhftQPHVKdfvkavckQR-----IRLMVSGSAALPLPTLQRWEEITGHTLL 378
Cdd:PRK08276 229 LIERYR---VTHSQLVPTMFVRMLKL------PEEVR--------ARydvssLRVAIHAAAPCPVEVKRAMIDWWGPIIH 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 379 ERYGMTE-IGMALSNPLKGPRIPGAVGSPLPGvEIRIVmsnatnttivEANHRETRVrsgleGKEGELLVRGPSVFKEYW 457
Cdd:PRK08276 292 EYYASSEgGGVTVITSEDWLAHPGSVGKAVLG-EVRIL----------DEDGNELPP-----GEIGTVYFEMDGYPFEYH 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 458 NKHQETRESFTDSGWFKTGDTA-IHKDGVFWIMGRTSvDIIKSGGYKISALEVERHLLAHPAIADVAVIGPPDAIWGQKV 536
Cdd:PRK08276 356 NDPEKTAAARNPHGWVTVGDVGyLDEDGYLYLTDRKS-DMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERV 434
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 2105456023 537 TAVMQLKRGHRLT---LPELKIWAREHMAPYIIPTGLVLVEELPRNQMGKVNKKDL 589
Cdd:PRK08276 435 KAVVQPADGADAGdalAAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRL 490
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
221-593 |
3.60e-49 |
|
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.
Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 173.67 E-value: 3.60e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 221 RPAMIIYTSGTTGRPKGVLHTHSSIQAMVQCLVSEWAWTRDDVILHTLPLHHVHGIVNKLLCpLWVGATCIMLPEFQPqk 300
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLYHVGGLAILVRS-LLAGAELVLLERNQA-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 301 vweiLLTSKAPMVNVFMA-VPTiysKLIQYYDQHFTQPHVKdfvkavckqRIRLMVSGSAALPLPTLQRWEEiTGHTLLE 379
Cdd:cd17630 78 ----LAEDLAPPGVTHVSlVPT---QLQRLLDSGQGPAALK---------SLRAVLLGGAPIPPELLERAAD-RGIPLYT 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 380 RYGMTEIGMALSNPLKGPRIPGAVGSPLPGVEIRIVmsnatnttiveanhretrvrsglegKEGELLVRGPSVFKEYWNK 459
Cdd:cd17630 141 TYGMTETASQVATKRPDGFGRGGVGVLLPGRELRIV-------------------------EDGEIWVGGASLAMGYLRG 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 460 hqETRESFTDSGWFKTGDTA-IHKDGVFWIMGRTSvDIIKSGGYKISALEVERHLLAHPAIADVAVIGPPDAIWGQKVTA 538
Cdd:cd17630 196 --QLVPEFNEDGWFTTKDLGeLHADGRLTVLGRAD-NMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVA 272
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2105456023 539 VMqlkRGHRLTLP-ELKIWAREHMAPYIIPTGLVLVEELPRNQMGKVNKKDLLRHF 593
Cdd:cd17630 273 VI---VGRGPADPaELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRAWL 325
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
115-589 |
8.09e-49 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 177.39 E-value: 8.09e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 115 GGLEGKRIS------FLCANDASYTVAQWAAWMSGGTAVPLYRKHPQEELEYIISDSQSSLLVAGNSFAKtlePLALKLG 188
Cdd:PRK06145 42 GMLHARGIGqgdvvaLLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYILGDAGAKLLLVDEEFDA---IVALETP 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 189 LPCLTLPPTSNLSTLdgtdSQEEEAAITDWADRPA---MIIYTSGTTGRPKGVLHTHSSIQAMVQCLVSEWAWTRDDVIL 265
Cdd:PRK06145 119 KIVIDAAAQADSRRL----AQGGLEIPPQAAVAPTdlvRLMYTSGTTDRPKGVMHSYGNLHWKSIDHVIALGLTASERLL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 266 HTLPLHHVHGIVNKLLCPLWVGATCIMLPEFQPQKVWEIL----LTSK--AP-MVNVFMAVPTIYSkliqyYDQhftqph 338
Cdd:PRK06145 195 VVGPLYHVGAFDLPGIAVLWVGGTLRIHREFDPEAVLAAIerhrLTCAwmAPvMLSRVLTVPDRDR-----FDL------ 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 339 vkdfvkavckQRIRLMVSGSAALPLPTLQRWEEI-TGHTLLERYGMTEIGMALSNPLKGPRIP--GAVGSPLPGVEIRIv 415
Cdd:PRK06145 264 ----------DSLAWCIGGGEKTPESRIRDFTRVfTRARYIDAYGLTETCSGDTLMEAGREIEkiGSTGRALAHVEIRI- 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 416 msnatnttiveanhRETRVRSGLEGKEGELLVRGPSVFKEYWNKHQETRESFTDsGWFKTGDTA-IHKDGVFWIMGRTSv 494
Cdd:PRK06145 333 --------------ADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYG-DWFRSGDVGyLDEEGFLYLTDRKK- 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 495 DIIKSGGYKISALEVERHLLAHPAIADVAVIGPPDAIWGQKVTAVMQLKRGHRLTLPELKIWAREHMAPYIIPTGLVLVE 574
Cdd:PRK06145 397 DMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPGATLTLEALDRHCRQRLASFKVPRQLKVRD 476
|
490
....*....|....*
gi 2105456023 575 ELPRNQMGKVNKKDL 589
Cdd:PRK06145 477 ELPRNPSGKVLKRVL 491
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
225-586 |
3.41e-48 |
|
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: 171.14 E-value: 3.41e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 225 IIYTSGTTGRPKGVLHTHSsiqamvQCLVSEWAW------TRDDVILHTLPLHHVHGIVNKLLCPLWVGATCIMLPEFQP 298
Cdd:cd17638 5 IMFTSGTTGRSKGVMCAHR------QTLRAAAAWadcadlTEDDRYLIINPFFHTFGYKAGIVACLLTGATVVPVAVFDV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 299 QKVWEILLTSKapmVNVFMAVPTIYSKLIQYydqhftqPHVKDFVKAvckqRIRLMVSGSAALPLPTLQRW-EEITGHTL 377
Cdd:cd17638 79 DAILEAIERER---ITVLPGPPTLFQSLLDH-------PGRKKFDLS----SLRAAVTGAATVPVELVRRMrSELGFETV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 378 LERYGMTEIGMA-LSNPLKGPR-IPGAVGSPLPGVEIRIvmsnatnttiveanhretrvrsgleGKEGELLVRGPSVFKE 455
Cdd:cd17638 145 LTAYGLTEAGVAtMCRPGDDAEtVATTCGRACPGFEVRI-------------------------ADDGEVLVRGYNVMQG 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 456 YWNKHQETRESFTDSGWFKTGDT-AIHKDGVFWIMGRTSvDIIKSGGYKISALEVERHLLAHPAIADVAVIGPPDAIWGQ 534
Cdd:cd17638 200 YLDDPEATAEAIDADGWLHTGDVgELDERGYLRITDRLK-DMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGE 278
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 2105456023 535 KVTAVMQLKRGHRLTLPELKIWAREHMAPYIIPTGLVLVEELPRNQMGKVNK 586
Cdd:cd17638 279 VGKAFVVARPGVTLTEEDVIAWCRERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
102-524 |
1.41e-47 |
|
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: 171.68 E-value: 1.41e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 102 LAGRISAALNSDFGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLYRKHPQEELEYIISDSQSSLLVAGNSFAKTLe 181
Cdd:TIGR01733 8 RANRLARHLRAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDSALASRL- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 182 plalkLGLPCLTLPPTSNLSTLDGTDSQEEEAAITDWADRPAMIIYTSGTTGRPKGVLHTHSSIQAMVQCLVSEWAWTRD 261
Cdd:TIGR01733 87 -----AGLVLPVILLDPLELAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDPD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 262 DVILHTLPLHHvHGIVNKLLCPLWVGATCIMLPEFQ---PQKVWEILLTSKapMVNVFMAVPTIYskliqyydQHFTQPH 338
Cdd:TIGR01733 162 DRVLQFASLSF-DASVEEIFGALLAGATLVVPPEDEerdDAALLAALIAEH--PVTVLNLTPSLL--------ALLAAAL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 339 VKDFvkavckQRIRLMVSGSAALPLPTLQRWEEITGHT-LLERYGMTEI-GMALSNPLKGPRIPGAV----GSPLPGVEI 412
Cdd:TIGR01733 231 PPAL------ASLRLVILGGEALTPALVDRWRARGPGArLINLYGPTETtVWSTATLVDPDDAPRESpvpiGRPLANTRL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 413 RivmsnatnttIVEANHRETRVrsgleGKEGELLVRGPSVFKEYWNKHQETRESFTD--------SGWFKTGDTA-IHKD 483
Cdd:TIGR01733 305 Y----------VLDDDLRPVPV-----GVVGELYIGGPGVARGYLNRPELTAERFVPdpfaggdgARLYRTGDLVrYLPD 369
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 2105456023 484 GVFWIMGRTSvDIIKSGGYKISALEVERHLLAHPAIADVAV 524
Cdd:TIGR01733 370 GNLEFLGRID-DQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
91-525 |
3.45e-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: 171.86 E-value: 3.45e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 91 SYKQL--YCSSFGLAGRISaalnsdfGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLYRKHPQEELEYIISDSQSS 168
Cdd:cd05914 9 TYKDLadNIAKFALLLKIN-------GVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 169 LLVAGNsfaktleplalklglpcltlpptsnlstldgtdsqEEEAAItdwadrpamIIYTSGTTGRPKGVLHTHSSIQAM 248
Cdd:cd05914 82 AIFVSD-----------------------------------EDDVAL---------INYTSGTTGNSKGVMLTYRNIVSN 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 249 VQCLVSEWAWTRDDVILHTLPLHHVHGIVNKLLCPLWVGATCIMLPEFQPQKvweILLTSKAP-----MVNVFMAVPTIY 323
Cdd:cd05914 118 VDGVKEVVLLGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFLDKIPSAK---IIALAFAQvtptlGVPVPLVIEKIF 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 324 SKLIQ-----------YYDQHFTQPHVKDFVKAVCKQ---RIRLMVSGSAALPLPTLQRWEEItGHTLLERYGMTEIGMA 389
Cdd:cd05914 195 KMDIIpkltlkkfkfkLAKKINNRKIRKLAFKKVHEAfggNIKEFVIGGAKINPDVEEFLRTI-GFPYTIGYGMTETAPI 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 390 LSNPLKGPRIPGAVGSPLPGVEIRIVMSNAtnttiveanhretrvrsglEGKEGELLVRGPSVFKEYWNKHQETRESFTD 469
Cdd:cd05914 274 ISYSPPNRIRLGSAGKVIDGVEVRIDSPDP-------------------ATGEGEIIVRGPNVMKGYYKNPEATAEAFDK 334
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 2105456023 470 SGWFKTGDTA-IHKDGVFWIMGRTSVDIIKSGGYKISALEVERHLLAHPAIADVAVI 525
Cdd:cd05914 335 DGWFHTGDLGkIDAEGYLYIRGRKKEMIVLSSGKNIYPEEIEAKINNMPFVLESLVV 391
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
218-591 |
5.16e-47 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 173.45 E-value: 5.16e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 218 WA-DRPAMIIYTSGTTGRPKGVLHTHSSIqaMVQCL--VSEWAWTRDDVILHTLPLHHVHGIvNKLLCPLWVGATCIMLP 294
Cdd:PLN02860 169 WApDDAVLICFTSGTTGRPKGVTISHSAL--IVQSLakIAIVGYGEDDVYLHTAPLCHIGGL-SSALAMLMVGACHVLLP 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 295 EFQPQKVWEILltsKAPMVNVFMAVPTIYSKLIQYYDQHFTQPhvkdfvkavCKQRIRLMVSGSAALPLPTLQRWEEITG 374
Cdd:PLN02860 246 KFDAKAALQAI---KQHNVTSMITVPAMMADLISLTRKSMTWK---------VFPSVRKILNGGGSLSSRLLPDAKKLFP 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 375 HT-LLERYGMTEIG-----MALSNP-LKGPRIPGA-----------------VGSPLPGVEIRIVMSNATnttiveanhr 430
Cdd:PLN02860 314 NAkLFSAYGMTEACssltfMTLHDPtLESPKQTLQtvnqtksssvhqpqgvcVGKPAPHVELKIGLDESS---------- 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 431 etrvrsglegKEGELLVRGPSVFKEYWNKHQETRESFTDSGWFKTGDT-AIHKDGVFWIMGRTSvDIIKSGGYKISALEV 509
Cdd:PLN02860 384 ----------RVGRILTRGPHVMLGYWGQNSETASVLSNDGWLDTGDIgWIDKAGNLWLIGRSN-DRIKTGGENVYPEEV 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 510 ERHLLAHPAIADVAVIGPPDAIWGQKVTAVMQLK------------RGHRLTLPE--LKIWARE-HMAPYIIPTGLVLVE 574
Cdd:PLN02860 453 EAVLSQHPGVASVVVVGVPDSRLTEMVVACVRLRdgwiwsdnekenAKKNLTLSSetLRHHCREkNLSRFKIPKLFVQWR 532
|
410
....*....|....*...
gi 2105456023 575 E-LPRNQMGKVnKKDLLR 591
Cdd:PLN02860 533 KpFPLTTTGKI-RRDEVR 549
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
74-583 |
2.43e-46 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 171.22 E-value: 2.43e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 74 APAFGDRLAIIDSSGSHSYKQLYCSSFGLAGRISAAlnsdfgGLE-GKRISFLCANDASYTVAQWAAWMSGGTAVPL-YR 151
Cdd:PRK07798 13 ADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQ------GLGpGDHVGIYARNRIEYVEAMLGAFKARAVPVNVnYR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 152 KHPqEELEYIISDSQSSLLVAGNSFAKTLEPLalklglpcltLPPTSNLSTL----DGTDSQE-------EEAAITDWAD 220
Cdd:PRK07798 87 YVE-DELRYLLDDSDAVALVYEREFAPRVAEV----------LPRLPKLRTLvvveDGSGNDLlpgavdyEDALAAGSPE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 221 RPA--------MIIYTSGTTGRPKGVLHTHSSI---------QAMVQCLVSEWAWTRDD------VILHTLPLHHVHGIV 277
Cdd:PRK07798 156 RDFgerspddlYLLYTGGTTGMPKGVMWRQEDIfrvllggrdFATGEPIEDEEELAKRAaagpgmRRFPAPPLMHGAGQW 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 278 NKLLCpLWVGATCIMLP--EFQPQKVWEILLTSKA---PMVNVFMAVPTIyskliqyydQHFTQPHVKDFvkavckQRIR 352
Cdd:PRK07798 236 AAFAA-LFSGQTVVLLPdvRFDADEVWRTIEREKVnviTIVGDAMARPLL---------DALEARGPYDL------SSLF 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 353 LMVSGSAALPLPTLQRWEEITGH-TLLERYGMTEIG-MALSNPLKGPRIPGAvgsplPGVEIRivmsnaTNTTIVEANHR 430
Cdd:PRK07798 300 AIASGGALFSPSVKEALLELLPNvVLTDSIGSSETGfGGSGTVAKGAVHTGG-----PRFTIG------PRTVVLDEDGN 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 431 ETRVRSGLEGkegeLLVRGPSVFKEYWNKHQETRESF-TDSG--WFKTGDTA-IHKDGVFWIMGRTSVdIIKSGGYKISA 506
Cdd:PRK07798 369 PVEPGSGEIG----WIARRGHIPLGYYKDPEKTAETFpTIDGvrYAIPGDRArVEADGTITLLGRGSV-CINTGGEKVFP 443
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2105456023 507 LEVERHLLAHPAIADVAVIGPPDAIWGQKVTAVMQLKRGHRLTLPELKIWAREHMAPYIIPTGLVLVEELPRNQMGK 583
Cdd:PRK07798 444 EEVEEALKAHPDVADALVVGVPDERWGQEVVAVVQLREGARPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
77-589 |
2.94e-46 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 170.61 E-value: 2.94e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 77 FGDRLAIIDSSGSHSYKQLYCSSFGLAgrisAALnSDFGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPL-YRKHPq 155
Cdd:PRK07470 20 FPDRIALVWGDRSWTWREIDARVDALA----AAL-AARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTnFRQTP- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 156 EELEYIISDSQSSLLVAGNSFAKTLEplALKLGLPCLTLpptsnLSTLDGTDSQEEEAAITDWA------------DRPA 223
Cdd:PRK07470 94 DEVAYLAEASGARAMICHADFPEHAA--AVRAASPDLTH-----VVAIGGARAGLDYEALVARHlgarvanaavdhDDPC 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 224 MIIYTSGTTGRPKGVLHTHSSIQAMVQCLVSEW--AWTRDDVILHTLPLHHVHGIvnKLLCPLWVGATCIMLP--EFQPQ 299
Cdd:PRK07470 167 WFFFTSGTTGRPKAAVLTHGQMAFVITNHLADLmpGTTEQDASLVVAPLSHGAGI--HQLCQVARGAATVLLPseRFDPA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 300 KVWEilLTSKAPMVNVFmAVPTIYSKLIQYydqhftqPHVKDFVKAvckqRIRLMVSGSAALPLPTLQRWEEITGHTLLE 379
Cdd:PRK07470 245 EVWA--LVERHRVTNLF-TVPTILKMLVEH-------PAVDRYDHS----SLRYVIYAGAPMYRADQKRALAKLGKVLVQ 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 380 RYGMTEIG-------MALSNPLKGP--RIpGAVGSPLPGVEIrivmsnatntTIVEANHRETRvrsglEGKEGELLVRGP 450
Cdd:PRK07470 311 YFGLGEVTgnitvlpPALHDAEDGPdaRI-GTCGFERTGMEV----------QIQDDEGRELP-----PGETGEICVIGP 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 451 SVFKEYWNKHQETRESFTDsGWFKTGDTAiHKD--GVFWIMGRTSvDIIKSGGYKISALEVERHLLAHPAIADVAVIGPP 528
Cdd:PRK07470 375 AVFAGYYNNPEANAKAFRD-GWFRTGDLG-HLDarGFLYITGRAS-DMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVP 451
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2105456023 529 DAIWGQKVTAVMQLKRGHRLTLPELKIWAREHMAPYIIPTGLVLVEELPRNQMGKVNKKDL 589
Cdd:PRK07470 452 DPVWGEVGVAVCVARDGAPVDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMV 512
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
78-589 |
3.84e-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: 169.39 E-value: 3.84e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 78 GDRLAIIDSSGSHSYKQLYcssfGLAGRISAALnSDFGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLYRKHPQEE 157
Cdd:cd12116 1 PDATAVRDDDRSLSYAELD----ERANRLAARL-RARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 158 LEYIISDSQSSLLVAGnsfAKTLEPLALKLGLPCLTLPptsnlstldGTDSQEEEAAITDWADRPAMIIYTSGTTGRPKG 237
Cdd:cd12116 76 LRYILEDAEPALVLTD---DALPDRLPAGLPVLLLALA---------AAAAAPAAPRTPVSPDDLAYVIYTSGSTGRPKG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 238 VLHTHSSIQAMVQCLVSEWAWTRDDVILH-TLPLHHVHGIvnKLLCPLWVGATCIMLPE---FQPQKVWEILltsKAPMV 313
Cdd:cd12116 144 VVVSHRNLVNFLHSMRERLGLGPGDRLLAvTTYAFDISLL--ELLLPLLAGARVVIAPRetqRDPEALARLI---EAHSI 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 314 NVFMAVPTIYSKLIQyydqhfTQPHVKDFVKAVCkqrirlmvsGSAALPlPTLQRWEEITGHTLLERYGMTEI----GMA 389
Cdd:cd12116 219 TVMQATPATWRMLLD------AGWQGRAGLTALC---------GGEALP-PDLAARLLSRVGSLWNLYGPTETtiwsTAA 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 390 LSNPLKGPrIPgaVGSPLPGVEIRIVmsnatnttiveanhrETRVRSGLEGKEGELLVRGPSVFKEYWNKHQETRESFTD 469
Cdd:cd12116 283 RVTAAAGP-IP--IGRPLANTQVYVL---------------DAALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVP 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 470 -------SGWFKTGDTAIHK-DGVFWIMGRTSvDIIKSGGYKISALEVERHLLAHPAIADVAVIGPPDAiWGQKVTAVMQ 541
Cdd:cd12116 345 dpfagpgSRLYRTGDLVRRRaDGRLEYLGRAD-GQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDG-GDRRLVAYVV 422
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 2105456023 542 LKRGHRLTLPELKIWAREHMAPYIIPTGLVLVEELPRNQMGKVNKKDL 589
Cdd:cd12116 423 LKAGAAPDAAALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
77-589 |
8.68e-46 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 169.94 E-value: 8.68e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 77 FGDRLAIIDSSGSHSYKQLYcssfGLAGRISAALNSDFGGLEGKRISFLCANDASYTVAQWAAWMSGGTAV---PLYrkh 153
Cdd:PRK05677 37 FADKPAFSNLGKTLTYGELY----KLSGAFAAWLQQHTDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVntnPLY--- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 154 PQEELEYIISDSQSSLLVAGNSFAKTLEPLALKLGL-------------------------------PCLTLPPTSNLST 202
Cdd:PRK05677 110 TAREMEHQFNDSGAKALVCLANMAHLAEKVLPKTGVkhvivtevadmlpplkrllinavvkhvkkmvPAYHLPQAVKFND 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 203 LDGTDSQEEEAAITDWADRPAMIIYTSGTTGRPKGVLHTHSSIQA-MVQC--LVSEWAWTRDDVILHTLPLHHVHGIVNK 279
Cdd:PRK05677 190 ALAKGAGQPVTEANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVAnMLQCraLMGSNLNEGCEILIAPLPLYHIYAFTFH 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 280 LLCPLWVGATCIMLPEfqPQKVWEILLTSKAPMVNVFMAVPTIYSKLIQyyDQHFTQphvKDFvkavckQRIRLMVSGSA 359
Cdd:PRK05677 270 CMAMMLIGNHNILISN--PRDLPAMVKELGKWKFSGFVGLNTLFVALCN--NEAFRK---LDF------SALKLTLSGGM 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 360 ALPLPTLQRWEEITGHTLLERYGMTEIG-MALSNPLKGPRIpGAVGSPLPGVEIRIVMSNATNTTIveanhretrvrsgl 438
Cdd:PRK05677 337 ALQLATAERWKEVTGCAICEGYGMTETSpVVSVNPSQAIQV-GTIGIPVPSTLCKVIDDDGNELPL-------------- 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 439 eGKEGELLVRGPSVFKEYWNKHQETRESFTDSGWFKTGDTA-IHKDGVFWIMGRTSvDIIKSGGYKISALEVERHLLAHP 517
Cdd:PRK05677 402 -GEVGELCVKGPQVMKGYWQRPEATDEILDSDGWLKTGDIAlIQEDGYMRIVDRKK-DMILVSGFNVYPNELEDVLAALP 479
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2105456023 518 AIADVAVIGPPDAIWGQKVTAVMQLKRGHRLTLPELKIWAREHMAPYIIPTGLVLVEELPRNQMGKVNKKDL 589
Cdd:PRK05677 480 GVLQCAAIGVPDEKSGEAIKVFVVVKPGETLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRREL 551
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
73-593 |
1.30e-45 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 169.30 E-value: 1.30e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 73 RAPAF---GDRLAIidssgshSYKQLYCSSFGLAGRISAAlnsdfGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPL 149
Cdd:PRK05852 31 EAPALvvtADRIAI-------SYRDLARLVDDLAGQLTRS-----GLLPGDRVALRMGSNAEFVVALLAASRADLVVVPL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 150 YRKHP-QEELEYIISDSQSSLLVAGNSFAKTLE------PLALKLGlpCLTLPPTSNLSTLDGTDSQEEEAAITDWADRP 222
Cdd:PRK05852 99 DPALPiAEQRVRSQAAGARVVLIDADGPHDRAEpttrwwPLTVNVG--GDSGPSGGTLSVHLDAATEPTPATSTPEGLRP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 223 --AMIIYTSGTTGRPKGVLHTHSSIQAMVQCLVSEWAWTRDDVILHTLPLHHVHGIVNKLLCPLWVGATcIMLP---EFQ 297
Cdd:PRK05852 177 ddAMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHGHGLIAALLATLASGGA-VLLPargRFS 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 298 PQKVWEILltsKAPMVNVFMAVPTIYSKLIQYYD-QHFTQPHVKdfvkavckqrIRLMVSGSAALPLPTLQRWEEITGHT 376
Cdd:PRK05852 256 AHTFWDDI---KAVGATWYTAVPTIHQILLERAAtEPSGRKPAA----------LRFIRSCSAPLTAETAQALQTEFAAP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 377 LLERYGMTEIG-MALSNPLKG------PRI-PGAVGSPlPGVEIRIVMSNATNTTiveanhretrvrsglEGKEGELLVR 448
Cdd:PRK05852 323 VVCAFGMTEAThQVTTTQIEGigqtenPVVsTGLVGRS-TGAQIRIVGSDGLPLP---------------AGAVGEVWLR 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 449 GPSVFKEYWNKHQETRESFTDsGWFKTGDT-AIHKDGVFWIMGRTSvDIIKSGGYKISALEVERHLLAHPAIADVAVIGP 527
Cdd:PRK05852 387 GTTVVRGYLGDPTITAANFTD-GWLRTGDLgSLSAAGDLSIRGRIK-ELINRGGEKISPERVEGVLASHPNVMEAAVFGV 464
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2105456023 528 PDAIWGQKVTAVMQLKRGHRLTLPELKIWAREHMAPYIIPTGLVLVEELPRNQMGKVNKKDLLRHF 593
Cdd:PRK05852 465 PDQLYGEAVAAVIVPRESAPPTAEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRRAVAEQF 530
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
119-586 |
2.36e-45 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 168.80 E-value: 2.36e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 119 GKRISFLCANDASYTVAQWAAWMSGGTAV---PLYRKhpqEELEYIISDSQSSLLVAGNSFaKTLEPLALKLG------- 188
Cdd:PRK12583 70 GDRVGIWAPNCAEWLLTQFATARIGAILVninPAYRA---SELEYALGQSGVRWVICADAF-KTSDYHAMLQEllpglae 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 189 -----LPCLTLPPTSNLSTLDGTDS---------QEEEAAITDWA----------DRPAMIIYTSGTTGRPKGVLHTHSS 244
Cdd:PRK12583 146 gqpgaLACERLPELRGVVSLAPAPPpgflawhelQARGETVSREAlaerqasldrDDPINIQYTSGTTGFPKGATLSHHN 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 245 IQAMVQCLVSEWAWTRDDVILHTLPLHHVHGIVNKLLCPLWVGAtCIMLP--EFQPQKVWEILLTSKApmvNVFMAVPTI 322
Cdd:PRK12583 226 ILNNGYFVAESLGLTEHDRLCVPVPLYHCFGMVLANLGCMTVGA-CLVYPneAFDPLATLQAVEEERC---TALYGVPTM 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 323 Y-SKLiqyydqhfTQPHVKDFVKAvckqRIRLMVSGSAALPLPTLQR-WEEITGHTLLERYGMTEIG-----MALSNPLk 395
Cdd:PRK12583 302 FiAEL--------DHPQRGNFDLS----SLRTGIMAGAPCPIEVMRRvMDEMHMAEVQIAYGMTETSpvslqTTAADDL- 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 396 gPRIPGAVGSPLPGVEIRIVMSNAtnttiveanhrETRVRsgleGKEGELLVRGPSVFKEYWNKHQETRESFTDSGWFKT 475
Cdd:PRK12583 369 -ERRVETVGRTQPHLEVKVVDPDG-----------ATVPR----GEIGELCTRGYSVMKGYWNNPEATAESIDEDGWMHT 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 476 GDTA-IHKDGVFWIMGRtSVDIIKSGGYKISALEVERHLLAHPAIADVAVIGPPDAIWGQKVTAVMQLKRGHRLTLPELK 554
Cdd:PRK12583 433 GDLAtMDEQGYVRIVGR-SKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRLHPGHAASEEELR 511
|
490 500 510
....*....|....*....|....*....|..
gi 2105456023 555 IWAREHMAPYIIPTGLVLVEELPRNQMGKVNK 586
Cdd:PRK12583 512 EFCKARIAHFKVPRYFRFVDEFPMTVTGKVQK 543
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
70-589 |
5.50e-45 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 168.08 E-value: 5.50e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 70 VFVRA-PAFGDRLAIIDSSGSHSYKQLYCSSFGLAGRISAalNSDFggLEGKRISFLCANDASYTVAQWAAWMSGGTAV- 147
Cdd:PRK12492 29 VFERScKKFADRPAFSNLGVTLSYAELERHSAAFAAYLQQ--HTDL--VPGDRIAVQMPNVLQYPIAVFGALRAGLIVVn 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 148 --PLYrkhPQEELEYIISDSQSSLLVAGNSFAKTLE--------------------PLA-----------LKLGLPCLTL 194
Cdd:PRK12492 105 tnPLY---TAREMRHQFKDSGARALVYLNMFGKLVQevlpdtgieylieakmgdllPAAkgwlvntvvdkVKKMVPAYHL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 195 PPTSNLSTL--DGTDSQEEEAAITdwADRPAMIIYTSGTTGRPKGVLHTHSSIQAMVQCLVSEWAWTRDD---------- 262
Cdd:PRK12492 182 PQAVPFKQAlrQGRGLSLKPVPVG--LDDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVRACLSQLGPDgqplmkegqe 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 263 VILHTLPLHHVHGIVNKLLCPLWVGATCIMLPefQPQKVWEILLTSKAPMVNVFMAVPTIYSKLIQYydqhftqPHVK-- 340
Cdd:PRK12492 260 VMIAPLPLYHIYAFTANCMCMMVSGNHNVLIT--NPRDIPGFIKELGKWRFSALLGLNTLFVALMDH-------PGFKdl 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 341 DFvkavckQRIRLMVSGSAALPLPTLQRWEEITGHTLLERYGMTEIG-MALSNPLKGPRIPGAVGSPLPGVEIRIVMSNa 419
Cdd:PRK12492 331 DF------SALKLTNSGGTALVKATAERWEQLTGCTIVEGYGLTETSpVASTNPYGELARLGTVGIPVPGTALKVIDDD- 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 420 tnttiveanhretrvrsGLE---GKEGELLVRGPSVFKEYWNKHQETRESFTDSGWFKTGDTA-IHKDGVFWIMGRTSvD 495
Cdd:PRK12492 404 -----------------GNElplGERGELCIKGPQVMKGYWQQPEATAEALDAEGWFKTGDIAvIDPDGFVRIVDRKK-D 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 496 IIKSGGYKISALEVERHLLAHPAIADVAVIGPPDAIWGQKVTaVMQLKRGHRLTLPELKIWAREHMAPYIIPTGLVLVEE 575
Cdd:PRK12492 466 LIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVK-LFVVARDPGLSVEELKAYCKENFTGYKVPKHIVLRDS 544
|
570
....*....|....
gi 2105456023 576 LPRNQMGKVNKKDL 589
Cdd:PRK12492 545 LPMTPVGKILRREL 558
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
71-589 |
5.99e-44 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 164.72 E-value: 5.99e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 71 FVRAPAFG-----DRLAIIDSSGSHSYKQLYCSSFGLAGRISAAlnsdfGGLEGKRISFLCANDASYTVAQWAAWMSGGT 145
Cdd:PRK07788 51 FAGLVAHAarrapDRAALIDERGTLTYAELDEQSNALARGLLAL-----GVRAGDGVAVLARNHRGFVLALYAAGKVGAR 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 146 AVPLYRKHPQEELEYIISDSQSSLLVAGNSFAKTLEPLALKLGLpCLTL--------PPTSNLSTLDGTDSQEEEAAITD 217
Cdd:PRK07788 126 IILLNTGFSGPQLAEVAAREGVKALVYDDEFTDLLSALPPDLGR-LRAWggnpdddePSGSTDETLDDLIAGSSTAPLPK 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 218 WADRPAMIIYTSGTTGRPKGVLHTHSSIQAMVQCLVSEWAWTRDDVILHTLPLHHVHGIVNKLLCpLWVGATCIMLPEFQ 297
Cdd:PRK07788 205 PPKPGGIVILTSGTTGTPKGAPRPEPSPLAPLAGLLSRVPFRAGETTLLPAPMFHATGWAHLTLA-MALGSTVVLRRRFD 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 298 PQKVWEILLTSKAPMVnvfMAVPTIYSKLIQYYDQHFTQPHVkdfvkavckQRIRLMVSGSAALPLPTLQRWEEITGHTL 377
Cdd:PRK07788 284 PEATLEDIAKHKATAL---VVVPVMLSRILDLGPEVLAKYDT---------SSLKIIFVSGSALSPELATRALEAFGPVL 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 378 LERYGMTEIGMA-LSNPLKGPRIPGAVGSPLPGVEIRIVmsnatnttivEANHRETRvrsglEGKEGELLVRGPSVFKEY 456
Cdd:PRK07788 352 YNLYGSTEVAFAtIATPEDLAEAPGTVGRPPKGVTVKIL----------DENGNEVP-----RGVVGRIFVGNGFPFEGY 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 457 WN-KHQETREsftdsGWFKTGDTA-IHKDGVFWIMGRTSvDIIKSGGYKISALEVERHLLAHPAIADVAVIGPPDAIWGQ 534
Cdd:PRK07788 417 TDgRDKQIID-----GLLSSGDVGyFDEDGLLFVDGRDD-DMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQ 490
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 2105456023 535 KVTAVMQLKRGHRLTLPELKIWAREHMAPYIIPTGLVLVEELPRNQMGKVNKKDL 589
Cdd:PRK07788 491 RLRAFVVKAPGAALDEDAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKREL 545
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
103-526 |
8.31e-44 |
|
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: 163.41 E-value: 8.31e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 103 AGRISAALNSdFGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLYRKHPQEELEYIISDSQSSLLVAGNSFA-KTLE 181
Cdd:cd05932 16 ARRLAAALRA-LGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFVGKLDDwKAMA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 182 PlALKLGLPCLTLPPTSNLSTLDGTDS-----QEEEAAITDWADRPAMIIYTSGTTGRPKGVLHTHSSIQAMVQCLVSEW 256
Cdd:cd05932 95 P-GVPEGLISISLPPPSAANCQYQWDDliaqhPPLEERPTRFPEQLATLIYTSGTTGQPKGVMLTFGSFAWAAQAGIEHI 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 257 AWTRDDVILHTLPLHHVHGIVNKLLCPLWVGATcIMLPEFQPQKVWEIlltsKAPMVNVFMAVPTIYSKLIQYYDQHFTQ 336
Cdd:cd05932 174 GTEENDRMLSYLPLAHVTERVFVEGGSLYGGVL-VAFAESLDTFVEDV----QRARPTLFFSVPRLWTKFQQGVQDKIPQ 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 337 PHVK-----DFVKAVCKQRI---------RLMVSGSAALPlPTLQRWEEITGHTLLERYGMTEiGMALSNPLK-GPRIPG 401
Cdd:cd05932 249 QKLNlllkiPVVNSLVKRKVlkglgldqcRLAGCGSAPVP-PALLEWYRSLGLNILEAYGMTE-NFAYSHLNYpGRDKIG 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 402 AVGSPLPGVEIRIvmsnatnttiveanhretrvrsgleGKEGELLVRGPSVFKEYWNKHQETRESFTDSGWFKTGDT-AI 480
Cdd:cd05932 327 TVGNAGPGVEVRI-------------------------SEDGEILVRSPALMMGYYKDPEATAEAFTADGFLRTGDKgEL 381
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 2105456023 481 HKDGVFWIMGRTSvDIIK-SGGYKISALEVERHLLAHPAIADVAVIG 526
Cdd:cd05932 382 DADGNLTITGRVK-DIFKtSKGKYVAPAPIENKLAEHDRVEMVCVIG 427
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
77-589 |
1.08e-43 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 164.07 E-value: 1.08e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 77 FGDRLAIIDSSGSHSYKQLYCSSFGLAgrisAALNSDFGGLEGKRISFLCANDASYTVAQWAAWMSGGTAV---PLYRkh 153
Cdd:PRK08974 36 YADQPAFINMGEVMTFRKLEERSRAFA----AYLQNGLGLKKGDRVALMMPNLLQYPIALFGILRAGMIVVnvnPLYT-- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 154 PQEeLEYIISDSQSSLLVAGNSFAKTLEPLALK----------LG---------------------LPCLTLP-PTSNLS 201
Cdd:PRK08974 110 PRE-LEHQLNDSGAKAIVIVSNFAHTLEKVVFKtpvkhviltrMGdqlstakgtlvnfvvkyikrlVPKYHLPdAISFRS 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 202 TLD-GTDSQEEEAAITdwADRPAMIIYTSGTTGRPKGVLHTHSSIQAMVqcLVSEWAW-----TRDDVILHTLPLHHVHG 275
Cdd:PRK08974 189 ALHkGRRMQYVKPELV--PEDLAFLQYTGGTTGVAKGAMLTHRNMLANL--EQAKAAYgpllhPGKELVVTALPLYHIFA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 276 I-VNKLLCpLWVGATCIML--PEFQPQKVWEIlltSKAPMVnVFMAVPTIYSKLIQyyDQHFTQphvKDFvkavckQRIR 352
Cdd:PRK08974 265 LtVNCLLF-IELGGQNLLItnPRDIPGFVKEL---KKYPFT-AITGVNTLFNALLN--NEEFQE---LDF------SSLK 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 353 LMVSGSAALPLPTLQRWEEITGHTLLERYGMTEIGMALS-NPLKGPRIPGAVGSPLPGVEIRIVMSNATNTTIveanhre 431
Cdd:PRK08974 329 LSVGGGMAVQQAVAERWVKLTGQYLLEGYGLTECSPLVSvNPYDLDYYSGSIGLPVPSTEIKLVDDDGNEVPP------- 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 432 trvrsgleGKEGELLVRGPSVFKEYWNKHQETRESFTDsGWFKTGDTA-IHKDGVFWIMGRTSvDIIKSGGYKISALEVE 510
Cdd:PRK08974 402 --------GEPGELWVKGPQVMLGYWQRPEATDEVIKD-GWLATGDIAvMDEEGFLRIVDRKK-DMILVSGFNVYPNEIE 471
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2105456023 511 RHLLAHPAIADVAVIGPPDAIWGQKVTaVMQLKRGHRLTLPELKIWAREHMAPYIIPTGLVLVEELPRNQMGKVNKKDL 589
Cdd:PRK08974 472 DVVMLHPKVLEVAAVGVPSEVSGEAVK-IFVVKKDPSLTEEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRREL 549
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
73-591 |
1.31e-43 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 163.78 E-value: 1.31e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 73 RAPAFGDRLAIIDSSGSHSYKQLYCSSFGLAGRISAAlnsdfGGLEGKRISFLCANDASY-TVAQWAAWMsGGTAVPL-- 149
Cdd:PRK06155 30 QAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAA-----GVKRGDRVALMCGNRIEFlDVFLGCAWL-GAIAVPInt 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 150 -YRKhPQeeLEYIISDSQSSLLVAGNSFA---KTLEPLALKL-------GLPCLTLPPTSNLSTLDGTDSQEEEAAITDw 218
Cdd:PRK06155 104 aLRG-PQ--LEHILRNSGARLLVVEAALLaalEAADPGDLPLpavwlldAPASVSVPAGWSTAPLPPLDAPAPAAAVQP- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 219 ADrPAMIIYTSGTTGRPKGVLHTHSSIQAMVQCLVSEWAWTRDDVILHTLPLHHVHGIvNKLLCPLWVGATCIMLPEFQP 298
Cdd:PRK06155 180 GD-TAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADDVLYTTLPLFHTNAL-NAFFQALLAGATYVLEPRFSA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 299 QKVWEILLTSKA-------PMVNVFMAVPtiyskliqyydqhfTQPHVKDFvkavckqriRLMVSGSAALPLPTLQRWEE 371
Cdd:PRK06155 258 SGFWPAVRRHGAtvtyllgAMVSILLSQP--------------ARESDRAH---------RVRVALGPGVPAALHAAFRE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 372 ITGHTLLERYGMTEIGMALSNPLKGPRiPGAVGSPLPGVEIRIVMSNATNttiVEAnhretrvrsgleGKEGELLVRG-- 449
Cdd:PRK06155 315 RFGVDLLDGYGSTETNFVIAVTHGSQR-PGSMGRLAPGFEARVVDEHDQE---LPD------------GEPGELLLRAde 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 450 PSVFKE-YWNKHQETRESFTDSgWFKTGD-TAIHKDGVFWIMGRTSvDIIKSGGYKISALEVERHLLAHPAIADVAVIGP 527
Cdd:PRK06155 379 PFAFATgYFGMPEKTVEAWRNL-WFHTGDrVVRDADGWFRFVDRIK-DAIRRRGENISSFEVEQVLLSHPAVAAAAVFPV 456
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2105456023 528 PDAIWGQKVTAVMQLKRGHRLTLPELKIWAREHMAPYIIPTGLVLVEELPRNQMGKVnKKDLLR 591
Cdd:PRK06155 457 PSELGEDEVMAAVVLRDGTALEPVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKV-QKFVLR 519
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
103-589 |
1.71e-43 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 162.56 E-value: 1.71e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 103 AGRISAALNSdFGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLYRKHPQEELEYIISDSQSSLLVAGNSFAKTLEP 182
Cdd:PRK12406 21 AARAAGGLAA-LGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAHADLLHGLAS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 183 lALKLGLPCLTLPPTSNLST---LDGTDSQEEEAAItDW--------------ADRPAMIIYTSGTTGRPKGVLHTHSSI 245
Cdd:PRK12406 100 -ALPAGVTVLSVPTPPEIAAayrISPALLTPPAGAI-DWegwlaqqepydgppVPQPQSMIYTSGTTGHPKGVRRAAPTP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 246 -QAMVQCLVSEWAW--TRDDVILHTLPLHH----VHGIVNKLLcplwvGATCIMLPEFQPQKVWEILLTSKapMVNVFMa 318
Cdd:PRK12406 178 eQAAAAEQMRALIYglKPGIRALLTGPLYHsapnAYGLRAGRL-----GGVLVLQPRFDPEELLQLIERHR--ITHMHM- 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 319 VPTIYSKLIQYYDQhftqphvkdfVKAVCK-QRIRLMVSGSAALPLPTLQRWEEITGHTLLERYGMTEIG-MALSNPLKG 396
Cdd:PRK12406 250 VPTMFIRLLKLPEE----------VRAKYDvSSLRHVIHAAAPCPADVKRAMIEWWGPVIYEYYGSTESGaVTFATSEDA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 397 PRIPGAVGSPLPGVEIRIVMSNAtnttiveanhretrvRSGLEGKEGELLVRGPSVFKEYWNKHQETRESFTDSGWFKTG 476
Cdd:PRK12406 320 LSHPGTVGKAAPGAELRFVDEDG---------------RPLPQGEIGEIYSRIAGNPDFTYHNKPEKRAEIDRGGFITSG 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 477 DTA-IHKDGVFWIMGRTSvDIIKSGGYKISALEVERHLLAHPAIADVAVIGPPDAIWGQKVTAVMQLKRGHRLTLPELKI 555
Cdd:PRK12406 385 DVGyLDADGYLFLCDRKR-DMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPGATLDEADIRA 463
|
490 500 510
....*....|....*....|....*....|....
gi 2105456023 556 WAREHMAPYIIPTGLVLVEELPRNQMGKVNKKDL 589
Cdd:PRK12406 464 QLKARLAGYKVPKHIEIMAELPREDSGKIFKRRL 497
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
222-586 |
6.38e-43 |
|
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: 157.04 E-value: 6.38e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 222 PAMIIYTSGTTGRPKGVLHTHSSIQAMVQCLVSE-WAWTRDDVILHTLPLHHVHGIVNKLLCpLWVGATCIMLPEFQPQK 300
Cdd:cd17635 3 PLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEgLNWVVGDVTYLPLPATHIGGLWWILTC-LIHGGLCVTGGENTTYK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 301 -VWEILLTSKapmVNVFMAVPTIYSKLIQYYdqhftqphvKDFVKAVckQRIRLMVSGSAaLPLPTLQRWEEITGHT-LL 378
Cdd:cd17635 82 sLFKILTTNA---VTTTCLVPTLLSKLVSEL---------KSANATV--PSLRLIGYGGS-RAIAADVRFIEATGLTnTA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 379 ERYGMTEIGMALSNPL-KGPRIPGAVGSPLPGVEIRIVmsnatnttiveanhrETRVRSGLEGKEGELLVRGPSVFKEYW 457
Cdd:cd17635 147 QVYGLSETGTALCLPTdDDSIEINAVGRPYPGVDVYLA---------------ATDGIAGPSASFGTIWIKSPANMLGYW 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 458 NKHQETRESFTDsGWFKTGDTA-IHKDGVFWIMGRTSVDIIKsGGYKISALEVERHLLAHPAIADVAVIGPPDAIWGQKV 536
Cdd:cd17635 212 NNPERTAEVLID-GWVNTGDLGeRREDGFLFITGRSSESINC-GGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELV 289
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 2105456023 537 TAVM---QLKRGHRLTLPELKIwaREHMAPYIIPTGLVLVEELPRNQMGKVNK 586
Cdd:cd17635 290 GLAVvasAELDENAIRALKHTI--RRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
155-589 |
2.57e-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: 159.94 E-value: 2.57e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 155 QEELEYIISDSQSSLLVAGNSFAKTLEPLALKLglPCLT----LPPTS-----NLSTLDGTDSQEEEAAITDWADrPAMI 225
Cdd:cd05928 103 AKDILYRLQASKAKCIVTSDELAPEVDSVASEC--PSLKtkllVSEKSrdgwlNFKELLNEASTEHHCVETGSQE-PMAI 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 226 IYTSGTTGRPKGVLHTHSSIQAMVQCLVSEW-AWTRDDVILHTLPLHHVHGIVNKLLCPlWVGATCIM---LPEFQPQKV 301
Cdd:cd05928 180 YFTSGTTGSPKMAEHSHSSLGLGLKVNGRYWlDLTASDIMWNTSDTGWIKSAWSSLFEP-WIQGACVFvhhLPRFDPLVI 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 302 WEILltSKAPmVNVFMAVPTIYSKLIQyydQHFTQPHVKdfvkavckqRIRLMVSGSAALPLPTLQRWEEITGHTLLERY 381
Cdd:cd05928 259 LKTL--SSYP-ITTFCGAPTVYRMLVQ---QDLSSYKFP---------SLQHCVTGGEPLNPEVLEKWKAQTGLDIYEGY 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 382 GMTEIGMALSNPlKGPRI-PGAVGSPLPGVEIRIVMSNATnttIVEanhretrvrsglEGKEGELLVR-GP----SVFKE 455
Cdd:cd05928 324 GQTETGLICANF-KGMKIkPGSMGKASPPYDVQIIDDNGN---VLP------------PGTEGDIGIRvKPirpfGLFSG 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 456 YWNKHQETRESFTDSGWFkTGDTAI-HKDGVFWIMGRtSVDIIKSGGYKISALEVERHLLAHPAIADVAVIGPPDAIWGQ 534
Cdd:cd05928 388 YVDNPEKTAATIRGDFYL-TGDRGImDEDGYFWFMGR-ADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGE 465
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2105456023 535 KVTAVMQLK---RGH---RLTLpELKIWAREHMAPYIIPTGLVLVEELPRNQMGKVNKKDL 589
Cdd:cd05928 466 VVKAFVVLApqfLSHdpeQLTK-ELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNEL 525
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
101-590 |
2.77e-42 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 158.37 E-value: 2.77e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 101 GLAGRISAALNSDfGGLEGKRISFLCANDASYTVAQWAAWMSGGT----AVPLYRKHPQEELEYIISDSQSSLLVAGNSF 176
Cdd:cd05922 1 LGVSAAASALLEA-GGVRGERVVLILPNRFTYIELSFAVAYAGGRlglvFVPLNPTLKESVLRYLVADAGGRIVLADAGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 177 AKTLeplalKLGLPCLTLPPTSnLSTLDGTDSQEEEAAITDWADRPAMIIYTSGTTGRPKGVLHTHSSIQAMVQCLVSEW 256
Cdd:cd05922 80 ADRL-----RDALPASPDPGTV-LDADGIRAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 257 AWTRDDVILHTLPLHHVHGIvNKLLCPLWVGATCIMLPEFQ-PQKVWEILLTSKAPMvnvFMAVPTIYSKLIQYYDQHFT 335
Cdd:cd05922 154 GITADDRALTVLPLSYDYGL-SVLNTHLLRGATLVLTNDGVlDDAFWEDLREHGATG---LAGVPSTYAMLTRLGFDPAK 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 336 QPHvkdfvkavckqrIRLMVSGSAALPLPTLQRWEE-ITGHTLLERYGMTEI--GMALSNPLKGPRIPGAVGSPLPGVEI 412
Cdd:cd05922 230 LPS------------LRYLTQAGGRLPQETIARLRElLPGAQVYVMYGQTEAtrRMTYLPPERILEKPGSIGLAIPGGEF 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 413 RIVMSNATNTTIVEAnhretrvrsglegkeGELLVRGPSVFKEYWNKHQETRESFTDSGWFKTGDTAIH-KDGVFWIMGR 491
Cdd:cd05922 298 EILDDDGTPTPPGEP---------------GEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRdEDGFLFIVGR 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 492 TSvDIIKSGGYKISALEVERHLLAHPAIADVAVIGPPDAIwGQKVTAVMQLKRGhrLTLPELKIWAREHMAPYIIPTGLV 571
Cdd:cd05922 363 RD-RMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDPL-GEKLALFVTAPDK--IDPKDVLRSLAERLPPYKVPATVR 438
|
490
....*....|....*....
gi 2105456023 572 LVEELPRNQMGKVNKKDLL 590
Cdd:cd05922 439 VVDELPLTASGKVDYAALR 457
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
91-526 |
3.64e-42 |
|
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: 158.29 E-value: 3.64e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 91 SYKQLYCSSFglagRISAALNSdFGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLYRKHPQEELEYIISDSQSSLL 170
Cdd:cd17640 7 TYKDLYQEIL----DFAAGLRS-LGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 171 VAGNSfaktleplalklglpcltlppTSNLSTldgtdsqeeeaaitdwadrpamIIYTSGTTGRPKGVLHTH-------S 243
Cdd:cd17640 82 VVEND---------------------SDDLAT----------------------IIYTSGTTGNPKGVMLTHanllhqiR 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 244 SIQAMVQCLVSewawtrdDVILHTLPLHHVHGIVNKLLCPLWvGATCIM---------LPEFQPQkvweilltskapmvn 314
Cdd:cd17640 119 SLSDIVPPQPG-------DRFLSILPIWHSYERSAEYFIFAC-GCSQAYtsirtlkddLKRVKPH--------------- 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 315 VFMAVPTIYSKLIQ-YYDQHFTQPHVKDFV--KAVCKQRIRLMVSGSAALPlPTLQRWEEITGHTLLERYGMTEIGMALS 391
Cdd:cd17640 176 YIVSVPRLWESLYSgIQKQVSKSSPIKQFLflFFLSGGIFKFGISGGGALP-PHVDTFFEAIGIEVLNGYGLTETSPVVS 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 392 -NPLKGPrIPGAVGSPLPGVEIRIVMSNATNTTIveanhretrvrsglEGKEGELLVRGPSVFKEYWNKHQETRESFTDS 470
Cdd:cd17640 255 aRRLKCN-VRGSVGRPLPGTEIKIVDPEGNVVLP--------------PGEKGIVWVRGPQVMKGYYKNPEATSKVLDSD 319
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 2105456023 471 GWFKTGDTA-IHKDGVFWIMGRTSVDIIKSGGYKISALEVERHLLAHPAIADVAVIG 526
Cdd:cd17640 320 GWFNTGDLGwLTCGGELVLTGRAKDTIVLSNGENVEPQPIEEALMRSPFIEQIMVVG 376
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
221-584 |
5.82e-42 |
|
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain
Pssm-ID: 341288 [Multi-domain] Cd Length: 320 Bit Score: 153.72 E-value: 5.82e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 221 RPAMIIYTSGTTGRPKGVLHTHSSIQAMVQCLVSEWAWTRDDVILHTLPLHHVHGIvNKLLCPLWVGATCIMLPEFQPQK 300
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSHSLFL-YGAISALYLGGTFIGQRKFNPKS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 301 VWEILLTSKApmVNVFMaVPTIYSKLIQYYdqhftQPHVKdfvkavckqrIRLMVSGSAALPLPTLQRWEEITGHT-LLE 379
Cdd:cd17633 80 WIRKINQYNA--TVIYL-VPTMLQALARTL-----EPESK----------IKSIFSSGQKLFESTKKKLKNIFPKAnLIE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 380 RYGMTEIGMALSNPLKGPRIPGAVGSPLPGVEIRIvmsnatnttiveanhretrvRSGLEGKEGELLVRGPSVFKEYWNK 459
Cdd:cd17633 142 FYGTSELSFITYNFNQESRPPNSVGRPFPNVEIEI--------------------RNADGGEIGKIFVKSEMVFSGYVRG 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 460 hqetrESFTDSGWFKTGDTA-IHKDGVFWIMGRTSvDIIKSGGYKISALEVERHLLAHPAIADVAVIGPPDAIWGQKVTA 538
Cdd:cd17633 202 -----GFSNPDGWMSVGDIGyVDEEGYLYLVGRES-DMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVA 275
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 2105456023 539 VMQlkrGHRLTLPELKIWAREHMAPYIIPTGLVLVEELPRNQMGKV 584
Cdd:cd17633 276 LYS---GDKLTYKQLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKI 318
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
210-564 |
1.23e-41 |
|
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: 157.38 E-value: 1.23e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 210 EEEAAITDW-ADRPAMIIYTSGTTGRPKGVLHTHSSIQAMVQCL---VSEWAwTRDDVILHTLPLHHVHGIVNKLLCPLW 285
Cdd:cd17639 77 ECSAIFTDGkPDDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLgdrVPELL-GPDDRYLAYLPLAHIFELAAENVCLYR 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 286 VGATC----------IM------LPEFQPQ------KVWEILltSKAPMVNVfMAVPTI---------YSKLIQY---YD 331
Cdd:cd17639 156 GGTIGygsprtltdkSKrgckgdLTEFKPTlmvgvpAIWDTI--RKGVLAKL-NPMGGLkrtlfwtayQSKLKALkegPG 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 332 QHFTQPHVKDFVKAVCKQRIRLMVSGSAALPLPTlQRWEEITGHTLLERYGMTEI--GMALSNPlkGPRIPGAVGSPLPG 409
Cdd:cd17639 233 TPLLDELVFKKVRAALGGRLRYMLSGGAPLSADT-QEFLNIVLCPVIQGYGLTETcaGGTVQDP--GDLETGRVGPPLPC 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 410 VEIRIVmsnatntTIVEANHR----ETRvrsglegkeGELLVRGPSVFKEYWNKHQETRESFTDSGWFKTGDTA-IHKDG 484
Cdd:cd17639 310 CEIKLV-------DWEEGGYStdkpPPR---------GEILIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGeFHPDG 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 485 VFWIMGRTSvDIIKS--GGYkiSALE-VERHLLAHPAIADVAVIGPPDAiwgQKVTAVMQLKRGHrltlpeLKIWAREHM 561
Cdd:cd17639 374 TLKIIDRKK-DLVKLqnGEY--IALEkLESIYRSNPLVNNICVYADPDK---SYPVAIVVPNEKH------LTKLAEKHG 441
|
...
gi 2105456023 562 APY 564
Cdd:cd17639 442 VIN 444
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
79-589 |
1.59e-41 |
|
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: 157.25 E-value: 1.59e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 79 DRLAIIDSSGSHSYKQLYCSSFGLAGRISAAlnsdfgGLE-GKRISFLCANDASYTVAQWAAWMSGGTAVPLYRKHPQEE 157
Cdd:TIGR03098 15 DATALVHHDRTLTYAALSERVLALASGLRGL------GLArGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLKAEQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 158 LEYIISDSQSSLLVAGNSFAKTLEPlalklglpclTLPPTSNLSTLDGTDSQEE------EAAITDWA------------ 219
Cdd:TIGR03098 89 VAHILADCNVRLLVTSSERLDLLHP----------ALPGCHDLRTLIIVGDPAHaseghpGEEPASWPkllalgdadpph 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 220 ----DRPAMIIYTSGTTGRPKGVLHTHSSIQAMVQCLVSEWAWTRDDVILHTLPLHHVHGIvNKLLCPLWVGATCIMLPE 295
Cdd:TIGR03098 159 pvidSDMAAILYTSGSTGRPKGVVLSHRNLVAGAQSVATYLENRPDDRLLAVLPLSFDYGF-NQLTTAFYVGATVVLHDY 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 296 FQPQkvwEILLTSKAPMVNVFMAVPTIYSKLIQyydqhftqphvkDFVKAVCKQRIRLMVSGSAALPLPTLQRWEEITGH 375
Cdd:TIGR03098 238 LLPR---DVLKALEKHGITGLAAVPPLWAQLAQ------------LDWPESAAPSLRYLTNSGGAMPRATLSRLRSFLPN 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 376 T-LLERYGMTEIGMALS-NPLKGPRIPGAVGSPLPGVEIRIVMSNATNTtiveanhretrvrsgLEGKEGELLVRGPSVF 453
Cdd:TIGR03098 303 ArLFLMYGLTEAFRSTYlPPEEVDRRPDSIGKAIPNAEVLVLREDGSEC---------------APGEEGELVHRGALVA 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 454 KEYWNKHQETRESFTDSGWFK-----------TGDTA-IHKDGVFWIMGRTSvDIIKSGGYKISALEVERHLLAHPAIAD 521
Cdd:TIGR03098 368 MGYWNDPEKTAERFRPLPPFPgelhlpelavwSGDTVrRDEEGFLYFVGRRD-EMIKTSGYRVSPTEVEEVAYATGLVAE 446
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2105456023 522 VAVIGPPDAIWGQKVTAVMQLKRGHRLTLPELKIWAREHMAPYIIPTGLVLVEELPRNQMGKVNKKDL 589
Cdd:TIGR03098 447 AVAFGVPDPTLGQAIVLVVTPPGGEELDRAALLAECRARLPNYMVPALIHVRQALPRNANGKIDRKAL 514
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
118-589 |
1.59e-41 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 158.12 E-value: 1.59e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 118 EGKRISFLCANDASYTVAQWAAWMSGGTAV---PLYRKhpqEELEYIISDSQSSLLVAGNSFAKTLEPL--------ALK 186
Cdd:PRK08751 75 KGDRVALMMPNCLQYPIATFGVLRAGLTVVnvnPLYTP---RELKHQLIDSGASVLVVIDNFGTTVQQViadtpvkqVIT 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 187 LGLPCLTLPPTSNL--------------STLDGTDSQEEEAAITDWADRPAMII---------YTSGTTGRPKGVLHTHS 243
Cdd:PRK08751 152 TGLGDMLGFPKAALvnfvvkyvkklvpeYRINGAIRFREALALGRKHSMPTLQIepddiaflqYTGGTTGVAKGAMLTHR 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 244 SIQAMVQcLVSEWAWTRD------DVILHTLPLHHVHGIVNKLLCPLWVGAT--CIMLPEFQPQKVWEIlltsKAPMVNV 315
Cdd:PRK08751 232 NLVANMQ-QAHQWLAGTGkleegcEVVITALPLYHIFALTANGLVFMKIGGCnhLISNPRDMPGFVKEL----KKTRFTA 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 316 FMAVPTIYSKLIQY--YDQhftqphvKDFvkavckQRIRLMVSGSAALPLPTLQRWEEITGHTLLERYGMTEIG-MALSN 392
Cdd:PRK08751 307 FTGVNTLFNGLLNTpgFDQ-------IDF------SSLKMTLGGGMAVQRSVAERWKQVTGLTLVEAYGLTETSpAACIN 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 393 PLKGPRIPGAVGSPLPGVEIRIVMSNATNTTIveanhretrvrsgleGKEGELLVRGPSVFKEYWNKHQETRESFTDSGW 472
Cdd:PRK08751 374 PLTLKEYNGSIGLPIPSTDACIKDDAGTVLAI---------------GEIGELCIKGPQVMKGYWKRPEETAKVMDADGW 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 473 FKTGDTA-IHKDGVFWIMGRTSvDIIKSGGYKISALEVERHLLAHPAIADVAVIGPPDAIWGQKVTAVMqLKRGHRLTLP 551
Cdd:PRK08751 439 LHTGDIArMDEQGFVYIVDRKK-DMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEIVKVVI-VKKDPALTAE 516
|
490 500 510
....*....|....*....|....*....|....*...
gi 2105456023 552 ELKIWAREHMAPYIIPTGLVLVEELPRNQMGKVNKKDL 589
Cdd:PRK08751 517 DVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRREL 554
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
79-584 |
2.26e-41 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 156.48 E-value: 2.26e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 79 DRLAIIDSSGSHSYKQLYCSSFGLAGrisaALNSDFGglEGKRISFLCANDASYTVAQWAAWMSGGTAVPLYRKHPQEEL 158
Cdd:PRK07638 16 NKIAIKENDRVLTYKDWFESVCKVAN----WLNEKES--KNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 159 EYIISDSQSSLLVAGNSFaktleplalklglpcltlppTSNLSTLDGT--DSQEEEAAITDWADRPAMII---------- 226
Cdd:PRK07638 90 KERLAISNADMIVTERYK--------------------LNDLPDEEGRviEIDEWKRMIEKYLPTYAPIEnvqnapfymg 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 227 YTSGTTGRPKGVLHTHSSIQAMVQCLVSEWAWTRDDVILHTLPLHHVH---GIVNKLlcplWVGATCIMLPEFQPQKVWE 303
Cdd:PRK07638 150 FTSGSTGKPKAFLRAQQSWLHSFDCNVHDFHMKREDSVLIAGTLVHSLflyGAISTL----YVGQTVHLMRKFIPNQVLD 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 304 ILLTSKapmVNVFMAVPTIYSKLIQyydqhftqphvkdfVKAVCKQRIRLMVSGsAALPLPTLQRWEEITGH-TLLERYG 382
Cdd:PRK07638 226 KLETEN---ISVMYTVPTMLESLYK--------------ENRVIENKMKIISSG-AKWEAEAKEKIKNIFPYaKLYEFYG 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 383 MTEIG-MALSNPLKGPRIPGAVGSPLPGVEIRIvmSNATNTTIveanhretrvrsgLEGKEGELLVRGPSVFKEYWNKHQ 461
Cdd:PRK07638 288 ASELSfVTALVDEESERRPNSVGRPFHNVQVRI--CNEAGEEV-------------QKGEIGTVYVKSPQFFMGYIIGGV 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 462 ETREsFTDSGWFKTGDTA-IHKDGVFWIMGRTSvDIIKSGGYKISALEVERHLLAHPAIADVAVIGPPDAIWGQKVTAVM 540
Cdd:PRK07638 353 LARE-LNADGWMTVRDVGyEDEEGFIYIVGREK-NMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAII 430
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 2105456023 541 qlkRGHRlTLPELKIWAREHMAPYIIPTGLVLVEELPRNQMGKV 584
Cdd:PRK07638 431 ---KGSA-TKQQLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKI 470
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
195-584 |
2.63e-41 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 157.75 E-value: 2.63e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 195 PPTSNLSTLDGTDSQEEEAAITDwADRPAMIIYTSGTTGRPKGVLHTHssiQAMVQCLVS-EWA--WTRDDVILHTLPLH 271
Cdd:PRK04319 181 PGTLDFNALMEQASDEFDIEWTD-REDGAILHYTSGSTGKPKGVLHVH---NAMLQHYQTgKYVldLHEDDVYWCTADPG 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 272 HVHGIVNKLLCPLWVGATCIML-PEFQPQKVWEILLTSKapmVNVFMAVPTIYSKLIQYYDqhftqphvkDFVKAVCKQR 350
Cdd:PRK04319 257 WVTGTSYGIFAPWLNGATNVIDgGRFSPERWYRILEDYK---VTVWYTAPTAIRMLMGAGD---------DLVKKYDLSS 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 351 IRLMVS-GSaalPL-PTLQRW-EEITGHTLLERYGMTEIGMAL-----SNPLKgpriPGAVGSPLPGVEIRIVmsnatnt 422
Cdd:PRK04319 325 LRHILSvGE---PLnPEVVRWgMKVFGLPIHDNWWMTETGGIMianypAMDIK----PGSMGKPLPGIEAAIV------- 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 423 tiveanhreTRVRSGLE-GKEGELLVRG--PSVFKEYWNKHQETRESFTDsGWFKTGDTA-IHKDGVFWIMGRTSvDIIK 498
Cdd:PRK04319 391 ---------DDQGNELPpNRMGNLAIKKgwPSMMRGIWNNPEKYESYFAG-DWYVSGDSAyMDEDGYFWFQGRVD-DVIK 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 499 SGGYKISALEVERHLLAHPAIADVAVIGPPDAIWGQKVTAVMQLKRGHRLT---LPELKIWAREHMAPYIIPTGLVLVEE 575
Cdd:PRK04319 460 TSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVALRPGYEPSeelKEEIRGFVKKGLGAHAAPREIEFKDK 539
|
....*....
gi 2105456023 576 LPRNQMGKV 584
Cdd:PRK04319 540 LPKTRSGKI 548
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
220-586 |
2.96e-41 |
|
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: 156.89 E-value: 2.96e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 220 DRPAMIIYTSGTTGRPKGVLHTHSS-----IQAMVqclvseWAWTRDDVILHTLPLHHVHGIVNKLLCPLWVGATCIML- 293
Cdd:cd05970 185 EDILLVYFSSGTTGMPKMVEHDFTYplghiVTAKY------WQNVREGGLHLTVADTGWGKAVWGKIYGQWIAGAAVFVy 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 294 --PEFQPQKVWEILLTSKapmVNVFMAVPTIYSKLIQYYDQHFtqphvkDFVKavckqrIRLMVSGSAALPLPTLQRWEE 371
Cdd:cd05970 259 dyDKFDPKALLEKLSKYG---VTTFCAPPTIYRFLIREDLSRY------DLSS------LRYCTTAGEALNPEVFNTFKE 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 372 ITGHTLLERYGMTEIGMALSN-PLKGPRiPGAVGSPLPGVEIrivmsnatntTIVEANHRETRVrsgleGKEGELLVR-- 448
Cdd:cd05970 324 KTGIKLMEGFGQTETTLTIATfPWMEPK-PGSMGKPAPGYEI----------DLIDREGRSCEA-----GEEGEIVIRts 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 449 -GPSV--FKEYWNKHQETRESFTDsGWFKTGDTA-IHKDGVFWIMGRTSvDIIKSGGYKISALEVERHLLAHPAIADVAV 524
Cdd:cd05970 388 kGKPVglFGGYYKDAEKTAEVWHD-GYYHTGDAAwMDEDGYLWFVGRTD-DLIKSSGYRIGPFEVESALIQHPAVLECAV 465
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2105456023 525 IGPPDAIWGQKVTAVMQLKRGHRLT---LPELKIWAREHMAPYIIPTGLVLVEELPRNQMGKVNK 586
Cdd:cd05970 466 TGVPDPIRGQVVKATIVLAKGYEPSeelKKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRR 530
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
102-593 |
3.84e-41 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 157.25 E-value: 3.84e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 102 LAGRISA---ALNSDFGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLYRKHPQEELEYIISDSQSSLLVAGNSFAK 178
Cdd:PRK05620 44 IGARAAAlahALHDELGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIVADPRLAE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 179 TLEPL---------ALKLGLPCLTLPPTSNLSTLDGTDSQ---EEEAAITDWAD----RPAMIIYTSGTTGRPKGVLHTH 242
Cdd:PRK05620 124 QLGEIlkecpcvraVVFIGPSDADSAAAHMPEGIKVYSYEallDGRSTVYDWPEldetTAAAICYSTGTTGAPKGVVYSH 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 243 SS--IQAMVQCLVSEWAWTRDDVILHTLPLHHV--HGIvnkllcPL--WVGATCIMLP--EFQPQKVWEILLTSkapMVN 314
Cdd:PRK05620 204 RSlyLQSLSLRTTDSLAVTHGESFLCCVPIYHVlsWGV------PLaaFMSGTPLVFPgpDLSAPTLAKIIATA---MPR 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 315 VFMAVPTIYSKLIQYYDQHFTQphvkdfvkavcKQRIRLMVSGSAALPLPTLQRWEEITGHTLLERYGMTEIGMAlsnpl 394
Cdd:PRK05620 275 VAHGVPTLWIQLMVHYLKNPPE-----------RMSLQEIYVGGSAVPPILIKAWEERYGVDVVHVWGMTETSPV----- 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 395 kgpripGAVGSPLPGV--EIRIVMSNATNTTIVEANHR---ETRVRSGLEGKEGELLVRGPSVFKEYWNKHQET------ 463
Cdd:PRK05620 339 ------GTVARPPSGVsgEARWAYRVSQGRFPASLEYRivnDGQVMESTDRNEGEIQVRGNWVTASYYHSPTEEgggaas 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 464 ----------RESFTDSGWFKTGDTA-IHKDGVFWIMGRTSvDIIKSGGYKISALEVERHLLAHPAIADVAVIGPPDAIW 532
Cdd:PRK05620 413 tfrgedvedaNDRFTADGWLRTGDVGsVTRDGFLTIHDRAR-DVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKW 491
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2105456023 533 GQKVTAVMQLKRG---HRLTLPELKIWAREHMAPYIIPTGLVLVEELPRNQMGKVNKKDLLRHF 593
Cdd:PRK05620 492 GERPLAVTVLAPGiepTRETAERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDLRQHL 555
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
74-586 |
5.28e-41 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 156.26 E-value: 5.28e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 74 APAFGDRLAIIDSSGSHSYKQLYCSSFGLAGRISAAlnsdfGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLYRKH 153
Cdd:PRK08162 28 AEVYPDRPAVIHGDRRRTWAETYARCRRLASALARR-----GIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 154 PQEELEYIISDSQSSLLVAGNSFAKTLEPLALKLGLPCLTL--------PPTSNLSTLDgtdsqeEEAAIT------DWA 219
Cdd:PRK08162 103 DAASIAFMLRHGEAKVLIVDTEFAEVAREALALLPGPKPLVidvddpeyPGGRFIGALD------YEAFLAsgdpdfAWT 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 220 dRPA------MIIYTSGTTGRPKGVLHTHSSIQAMVQCLVSEWAWTRDDVILHTLPLHHVHGivnklLCPLW----VGAT 289
Cdd:PRK08162 177 -LPAdewdaiALNYTSGTTGNPKGVVYHHRGAYLNALSNILAWGMPKHPVYLWTLPMFHCNG-----WCFPWtvaaRAGT 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 290 CIMLPEFQPQKVWEILLTSKapmVNVFMAVPTIYSKLIqyydqhftqpHVKDFVKAVCKQRIRLMVSGsAALPLPTLQRW 369
Cdd:PRK08162 251 NVCLRKVDPKLIFDLIREHG---VTHYCGAPIVLSALI----------NAPAEWRAGIDHPVHAMVAG-AAPPAAVIAKM 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 370 EEItGHTLLERYGMTEI-GMALSNPLKGP----------RIPGAVGSPLPGVEIRIVMSNATNTTiVEANHrETRvrsgl 438
Cdd:PRK08162 317 EEI-GFDLTHVYGLTETyGPATVCAWQPEwdalplderaQLKARQGVRYPLQEGVTVLDPDTMQP-VPADG-ETI----- 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 439 egkeGELLVRGPSVFKEYWNKHQETRESFTDsGWFKTGDTAI-HKDGVFWIMGRtSVDIIKSGGYKISALEVERHLLAHP 517
Cdd:PRK08162 389 ----GEIMFRGNIVMKGYLKNPKATEEAFAG-GWFHTGDLAVlHPDGYIKIKDR-SKDIIISGGENISSIEVEDVLYRHP 462
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2105456023 518 AIADVAVIGPPDAIWGQKVTAVMQLKRGHRLTLPELKIWAREHMAPYIIPTGLVLvEELPRNQMGKVNK 586
Cdd:PRK08162 463 AVLVAAVVAKPDPKWGEVPCAFVELKDGASATEEEIIAHCREHLAGFKVPKAVVF-GELPKTSTGKIQK 530
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
73-589 |
1.62e-40 |
|
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: 153.97 E-value: 1.62e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 73 RAPAFGDRLAIIDSSGSHSYKQLYCSSFGLAGRISAAlnsdfGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLYRK 152
Cdd:cd17646 7 QAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRAR-----GVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 153 HPQEELEYIISDSQSSLLVAGnsfAKTLEPLAlklGLPCLTLPPTSNLSTLDGTDSQEEEAAitdwaDRPAMIIYTSGTT 232
Cdd:cd17646 82 YPADRLAYMLADAGPAVVLTT---ADLAARLP---AGGDVALLGDEALAAPPATPPLVPPRP-----DNLAYVIYTSGST 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 233 GRPKGVLHTHSSIQAMVQCLVSEWAWTRDDVILHTLPLhhvhGI---VNKLLCPLWVGATCIML-------PEFQPQKVW 302
Cdd:cd17646 151 GRPKGVMVTHAGIVNRLLWMQDEYPLGPGDRVLQKTPL----SFdvsVWELFWPLVAGARLVVArpgghrdPAYLAALIR 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 303 E--ILLTSKAP-MVNVFMAVPTiyskliqyydqhftqphvkdfvkAVCKQRIRLMVSGSAALPLPTLQRWEEITGHTLLE 379
Cdd:cd17646 227 EhgVTTCHFVPsMLRVFLAEPA-----------------------AGSCASLRRVFCSGEALPPELAARFLALPGAELHN 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 380 RYGMTE--IGM---ALSNPLKGPRIPgaVGSPLPGVEIRIVmsnatnttiveanhrETRVRSGLEGKEGELLVRGPSVFK 454
Cdd:cd17646 284 LYGPTEaaIDVthwPVRGPAETPSVP--IGRPVPNTRLYVL---------------DDALRPVPVGVPGELYLGGVQLAR 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 455 EYWNKHQETRESFTDSgWF-------KTGDTA-IHKDGVFWIMGRTSvDIIKSGGYKISALEVERHLLAHPAIADVAVIG 526
Cdd:cd17646 347 GYLGRPALTAERFVPD-PFgpgsrmyRTGDLArWRPDGALEFLGRSD-DQVKIRGFRVEPGEIEAALAAHPAVTHAVVVA 424
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2105456023 527 PPDAIWGQKVTAVMQLKRGHR-LTLPELKIWAREHMAPYIIPTGLVLVEELPRNQMGKVNKKDL 589
Cdd:cd17646 425 RAAPAGAARLVGYVVPAAGAAgPDTAALRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
219-589 |
2.08e-40 |
|
C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.
Pssm-ID: 341235 [Multi-domain] Cd Length: 490 Bit Score: 153.64 E-value: 2.08e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 219 ADRPAMIIYTSGTTGRPKGVLHTHSSIQAMVQCLVSEWAWTRDDVILHTLPLHHVHGIVNKLLCPLWVGATCIMLPE-FQ 297
Cdd:cd05909 146 PDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPFFHSFGLTGCLWLPLLSGIKVVFHPNpLD 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 298 PQKVWEILLTSKApmvNVFMAVPTIYSKLIQYYdqhftqpHVKDFvkavckQRIRLMVSGSAALPLPTLQRWEEITGHTL 377
Cdd:cd05909 226 YKKIPELIYDKKA---TILLGTPTFLRGYARAA-------HPEDF------SSLRLVVAGAEKLKDTLRQEFQEKFGIRI 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 378 LERYGMTEIGMALS-NPLKGPRIPGAVGSPLPGVEIRIVmsnatnttiveanHRETRVRSGlEGKEGELLVRGPSVFKEY 456
Cdd:cd05909 290 LEGYGTTECSPVISvNTPQSPNKEGTVGRPLPGMEVKIV-------------SVETHEEVP-IGEGGLLLVRGPNVMLGY 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 457 WNKHQETRESFTDsGWFKTGDTA-IHKDGVFWIMGRTSvDIIKSGGYKISALEVERHLLAH-PAIADVAVIGPPDAIWGQ 534
Cdd:cd05909 356 LNEPELTSFAFGD-GWYDTGDIGkIDGEGFLTITGRLS-RFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVPDGRKGE 433
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2105456023 535 KVTAVMQlkrGHRLTLPELKIWAREHMAPYI-IPTGLVLVEELPRNQMGKVNKKDL 589
Cdd:cd05909 434 KIVLLTT---TTDTDPSSLNDILKNAGISNLaKPSYIHQVEEIPLLGTGKPDYVTL 486
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
79-589 |
4.75e-40 |
|
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: 151.69 E-value: 4.75e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 79 DRLAIIDSSGSHSYKQLYCSSFGLAGRISAAlnsdfGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLYRKHPQEEL 158
Cdd:cd17643 2 EAVAVVDEDRRLTYGELDARANRLARTLRAE-----GVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 159 EYIISDSQSSLLvagnsfaktleplalklglpcltlpptsnlstldgtdsqeeeaaITDwADRPAMIIYTSGTTGRPKGV 238
Cdd:cd17643 77 AFILADSGPSLL--------------------------------------------LTD-PDDLAYVIYTSGSTGRPKGV 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 239 LHTHSSIQAMVQCLVSEWAWTRDDVilhTLPLHH---------VHGivnkllcPLWVGATCIMLPEFQ---PQKVWEILl 306
Cdd:cd17643 112 VVSHANVLALFAATQRWFGFNEDDV---WTLFHSyafdfsvweIWG-------ALLHGGRLVVVPYEVarsPEDFARLL- 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 307 tsKAPMVNVFMAVPTIYSKLIQYYDQHFTQPHvkdfvkavckqRIRLMVSGSAALPLPTLQRWEEITGH---TLLERYGM 383
Cdd:cd17643 181 --RDEGVTVLNQTPSAFYQLVEAADRDGRDPL-----------ALRYVIFGGEALEAAMLRPWAGRFGLdrpQLVNMYGI 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 384 TEIGMALS-NPLKGPRIPGA----VGSPLPGVEIRIVmsnatnttivEANHRETRVrsgleGKEGELLVRGPSVFKEYWN 458
Cdd:cd17643 248 TETTVHVTfRPLDAADLPAAaaspIGRPLPGLRVYVL----------DADGRPVPP-----GVVGELYVSGAGVARGYLG 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 459 KHQETRESFTD-------SGWFKTGDTAIHK-DGVFWIMGRTSvDIIKSGGYKISALEVERHLLAHPAIADVAVIGPPDA 530
Cdd:cd17643 313 RPELTAERFVAnpfggpgSRMYRTGDLARRLpDGELEYLGRAD-EQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDE 391
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 2105456023 531 IWGQKVTAVMQLKRGHRLTLPELKIWAREHMAPYIIPTGLVLVEELPRNQMGKVNKKDL 589
Cdd:cd17643 392 PGDTRLVAYVVADDGAAADIAELRALLKELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
73-591 |
1.62e-39 |
|
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: 155.40 E-value: 1.62e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 73 RAPafgDRLAIIDSSGSHSYKQLYCSSFGLAGRISAAlnsdfGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLYRK 152
Cdd:COG1020 488 RTP---DAVAVVFGDQSLTYAELNARANRLAHHLRAL-----GVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPA 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 153 HPQEELEYIISDSQSSLLVAGNSFAKTLEPLalklGLPCLTLpptsNLSTLDGTDSQEEEAAITdwADRPAMIIYTSGTT 232
Cdd:COG1020 560 YPAERLAYMLEDAGARLVLTQSALAARLPEL----GVPVLAL----DALALAAEPATNPPVPVT--PDDLAYVIYTSGST 629
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 233 GRPKGVLHTHSSIQAMVQCLVSEWAWTRDDVILHTLPLHH---VHGIvnklLCPLWVGATCIMLPE---FQPQKVWEILL 306
Cdd:COG1020 630 GRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFASLSFdasVWEI----FGALLSGATLVLAPPearRDPAALAELLA 705
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 307 TSKapmVNVFMAVPTIYSKLIQYYDQHFTQPhvkdfvkavckqriRLMVSGSAALPLPTLQRWEEITGHT-LLERYGMTE 385
Cdd:COG1020 706 RHR---VTVLNLTPSLLRALLDAAPEALPSL--------------RLVLVGGEALPPELVRRWRARLPGArLVNLYGPTE 768
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 386 ------IGMALSNPLKGPRIPgaVGSPLPGVEIRIVmsnatnttivEANHRETRVrsgleGKEGELLVRGPSVFKEYWNK 459
Cdd:COG1020 769 ttvdstYYEVTPPDADGGSVP--IGRPIANTRVYVL----------DAHLQPVPV-----GVPGELYIGGAGLARGYLNR 831
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 460 HQETRESF-----TDSG--WFKTGDTA-IHKDGVFWIMGRTSvDIIKSGGYKISALEVERHLLAHPAIADVAVIGPPDAI 531
Cdd:COG1020 832 PELTAERFvadpfGFPGarLYRTGDLArWLPDGNLEFLGRAD-DQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDAP 910
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 532 WGQKVTAVMQLKRGHRLTLPELKIWAREHMAPYIIPTGLVLVEELPRNQMGKVNKKDLLR 591
Cdd:COG1020 911 GDKRLVAYVVPEAGAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALPA 970
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
73-589 |
1.63e-39 |
|
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341306 [Multi-domain] Cd Length: 491 Bit Score: 150.96 E-value: 1.63e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 73 RAPafgDRLAIIDSSGSHSYKQLYcssfGLAGRISAALNSDfGGLEGKRISfLCAN-DASYTVAQWAAWMSGGTAVPLYR 151
Cdd:cd17651 7 RTP---DAPALVAEGRRLTYAELD----RRANRLAHRLRAR-GVGPGDLVA-LCARrSAELVVALLAILKAGAAYVPLDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 152 KHPQEELEYIISDSQSSLLVA----GNSFAKTLEPLALKLGLPCLTLPPTSNLSTLDgtdsqeeeaaitdwADRPAMIIY 227
Cdd:cd17651 78 AYPAERLAFMLADAGPVLVLThpalAGELAVELVAVTLLDQPGAAAGADAEPDPALD--------------ADDLAYVIY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 228 TSGTTGRPKGVLHTHSSIQAMVQCLVSEWAWTRDDVILHTLPLH---HVHGIVNKLLCplwvGATCIMLPE---FQPQKV 301
Cdd:cd17651 144 TSGSTGRPKGVVMPHRSLANLVAWQARASSLGPGARTLQFAGLGfdvSVQEIFSTLCA----GATLVLPPEevrTDPPAL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 302 WEILltSKAPMVNVFMavPTIYSK-LIQYYDQHFTQPhvkdfvkavckQRIRLMVSGSAALPL-PTLQRW-EEITGHTLL 378
Cdd:cd17651 220 AAWL--DEQRISRVFL--PTVALRaLAEHGRPLGVRL-----------AALRYLLTGGEQLVLtEDLREFcAGLPGLRLH 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 379 ERYGMTE----IGMALSNPLKGPRIPGAVGSPLPGVEIRIVmsnatnttiveanhrETRVRSGLEGKEGELLVRGPSVFK 454
Cdd:cd17651 285 NHYGPTEthvvTALSLPGDPAAWPAPPPIGRPIDNTRVYVL---------------DAALRPVPPGVPGELYIGGAGLAR 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 455 EYWNKHQETRESFTDSGW------FKTGDTA-IHKDGVFWIMGRTSvDIIKSGGYKISALEVERHLLAHPAIADVAVIGP 527
Cdd:cd17651 350 GYLNRPELTAERFVPDPFvpgarmYRTGDLArWLPDGELEFLGRAD-DQVKIRGFRIELGEIEAALARHPGVREAVVLAR 428
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2105456023 528 PDAIWGQKVTAVMQLKRGHRLTLPELKIWAREHMAPYIIPTGLVLVEELPRNQMGKVNKKDL 589
Cdd:cd17651 429 EDRPGEKRLVAYVVGDPEAPVDAAELRAALATHLPEYMVPSAFVLLDALPLTPNGKLDRRAL 490
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
102-591 |
3.52e-39 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 149.21 E-value: 3.52e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 102 LAGRISAALnSDFGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLYRKHPQEELEYIISDSQSSLLVAGnsfaktle 181
Cdd:cd05973 9 LSARFANAL-QELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTD-------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 182 plalklglpcltlppTSNLSTLDgtdsqeeeaaitdwaDRPAMIIYTSGTTGRPKGVLHTHSSIQAMVQCLVSEWAWTRD 261
Cdd:cd05973 80 ---------------AANRHKLD---------------SDPFVMMFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRPE 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 262 DVILHTLPLHHVHGIVNKLLCPLWVGATCIMLP-EFQPQKVWEILLTSKapmVNVFMAVPTIYSKLIQyydqhftqphvk 340
Cdd:cd05973 130 DSFWNAADPGWAYGLYYAITGPLALGHPTILLEgGFSVESTWRVIERLG---VTNLAGSPTAYRLLMA------------ 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 341 DFVKAVCKQRIRLMVSGSAALPL-PTLQRWEEIT-GHTLLERYGMTEIGMALSN--PLKGPRIPGAVGSPLPGVEIrIVM 416
Cdd:cd05973 195 AGAEVPARPKGRLRRVSSAGEPLtPEVIRWFDAAlGVPIHDHYGQTELGMVLANhhALEHPVHAGSAGRAMPGWRV-AVL 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 417 SNATNTTIveanhretrvrsglEGKEGELLV---RGPSV-FKEYWNKHQETresfTDSGWFKTGDTA-IHKDGVFWIMGR 491
Cdd:cd05973 274 DDDGDELG--------------PGEPGRLAIdiaNSPLMwFRGYQLPDTPA----IDGGYYLTGDTVeFDPDGSFSFIGR 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 492 TSvDIIKSGGYKISALEVERHLLAHPAIADVAVIGPPDAIWGQKVTAVMQLKRGHRLT---LPELKIWAREHMAPYIIPT 568
Cdd:cd05973 336 AD-DVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHEGTpalADELQLHVKKRLSAHAYPR 414
|
490 500
....*....|....*....|...
gi 2105456023 569 GLVLVEELPRNQMGKVnKKDLLR 591
Cdd:cd05973 415 TIHFVDELPKTPSGKI-QRFLLR 436
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
91-593 |
5.84e-39 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 150.29 E-value: 5.84e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 91 SYKQLYcssfGLAGRISAALNSDfGGLEGKRISFLCANDASYTVAqWAAWMSGG----TAVPlyRKHPqEELEYIISDSQ 166
Cdd:PRK06018 41 TYAQIH----DRALKVSQALDRD-GIKLGDRVATIAWNTWRHLEA-WYGIMGIGaichTVNP--RLFP-EQIAWIINHAE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 167 SSLLVAGNSFAKTLEPLALKLglPCL----------TLPPTsnlsTLDGTDSQEEEAAITD----WADRP----AMIIYT 228
Cdd:PRK06018 112 DRVVITDLTFVPILEKIADKL--PSVeryvvltdaaHMPQT----TLKNAVAYEEWIAEADgdfaWKTFDentaAGMCYT 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 229 SGTTGRPKGVLHTHSS--IQAMVQCLVSEWAWTRDDVILHTLPLHHVHGIVNKLLCPLwVGATCIML-PEFQPQKVWEIL 305
Cdd:PRK06018 186 SGTTGDPKGVLYSHRSnvLHALMANNGDALGTSAADTMLPVVPLFHANSWGIAFSAPS-MGTKLVMPgAKLDGASVYELL 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 306 LTSKapmVNVFMAVPTIYSKLIQYYDQH-FTQPHVKdfvKAVCkqrirlmvsGSAALPLPTLQRWEEItGHTLLERYGMT 384
Cdd:PRK06018 265 DTEK---VTFTAGVPTVWLMLLQYMEKEgLKLPHLK---MVVC---------GGSAMPRSMIKAFEDM-GVEVRHAWGMT 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 385 EIG-MALSNPLKGP--RIPGAV--------GSPLPGVEIRIVMsnatnttivEANHRETRvrsglEGKE-GELLVRGPSV 452
Cdd:PRK06018 329 EMSpLGTLAALKPPfsKLPGDArldvlqkqGYPPFGVEMKITD---------DAGKELPW-----DGKTfGRLKVRGPAV 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 453 FKEYWNKHQETresFTDSGWFKTGDTA-IHKDGVFWIMGRtSVDIIKSGGYKISALEVERHLLAHPAIADVAVIGPPDAI 531
Cdd:PRK06018 395 AAAYYRVDGEI---LDDDGFFDTGDVAtIDAYGYMRITDR-SKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPK 470
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2105456023 532 WGQKVTAVMQLKRGHRLTLPELKIWAREHMAPYIIPTGLVLVEELPRNQMGKVNKKDLLRHF 593
Cdd:PRK06018 471 WDERPLLIVQLKPGETATREEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALREQF 532
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
222-578 |
6.66e-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: 145.52 E-value: 6.66e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 222 PAMIIYTSGTTGRPKGVLHTHSSIqaMVQCLVSEW--AWTRDDVILHTLPLHHVhGIVNKLLCPLWVGATCIMLPEFQPQ 299
Cdd:cd17636 2 PVLAIYTAAFSGRPNGALLSHQAL--LAQALVLAVlqAIDEGTVFLNSGPLFHI-GTLMFTLATFHAGGTNVFVRRVDAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 300 KVWEILLTSKApmVNVFMAVPTIyskliqyyDQhftqphvkdFVKAVCKQRIRLmvsgSAALPLPTLQRWEEI--TGHTL 377
Cdd:cd17636 79 EVLELIEAERC--THAFLLPPTI--------DQ---------IVELNADGLYDL----SSLRSSPAAPEWNDMatVDTSP 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 378 LER----YGMTEI-GMALSNPLKGPRIPGAvGSPLPGVEIRIVmsnatnttivEANHRETRVrsgleGKEGELLVRGPSV 452
Cdd:cd17636 136 WGRkpggYGQTEVmGLATFAALGGGAIGGA-GRPSPLVQVRIL----------DEDGREVPD-----GEVGEIVARGPTV 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 453 FKEYWNKHQETRESFTDsGWFKTGDTAIHK-DGVFWIMGrTSVDIIKSGGYKISALEVERHLLAHPAIADVAVIGPPDAI 531
Cdd:cd17636 200 MAGYWNRPEVNARRTRG-GWHHTNDLGRREpDGSLSFVG-PKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPR 277
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 2105456023 532 WGQKVTAVMQLKRGHRLTLPELKIWAREHMAPYIIPTGLVLVEELPR 578
Cdd:cd17636 278 WAQSVKAIVVLKPGASVTEAELIEHCRARIASYKKPKSVEFADALPR 324
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
134-589 |
7.19e-39 |
|
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: 148.67 E-value: 7.19e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 134 VAQWAAWMSGGTAVPLYRKHPQEELEYIISDSQSSLLvagnsfaktleplalklglpcltlpptsnlstldgtdsqeeea 213
Cdd:cd17649 52 VALLAILKAGGAYVPLDPEYPAERLRYMLEDSGAGLL------------------------------------------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 214 aITDWADRPAMIIYTSGTTGRPKGVLHTHSSIQAMVQCLVSEWAWTRDDVILHTLPLhHVHGIVNKLLCPLWVGATCIML 293
Cdd:cd17649 89 -LTHHPRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAERYGLTPGDRELQFASF-NFDGAHEQLLPPLICGACVVLR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 294 PEFQPQKVWEILLTSKAPMVNVfMAVPTIY-SKLIQYYDQHFTQPhvkdfvkavcKQRIRLMVSGSAALPLPTLQRWEEI 372
Cdd:cd17649 167 PDELWASADELAEMVRELGVTV-LDLPPAYlQQLAEEADRTGDGR----------PPSLRLYIFGGEALSPELLRRWLKA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 373 tGHTLLERYGMTEigmALSNPL----------KGPRIPgaVGSPLPGVEIRIVmsnatnttiveanhrETRVRSGLEGKE 442
Cdd:cd17649 236 -PVRLFNAYGPTE---ATVTPLvwkceagaarAGASMP--IGRPLGGRSAYIL---------------DADLNPVPVGVT 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 443 GELLVRGPSVFKEYWNKHQETRESFTD-------SGWFKTGDTAIHK-DGVFWIMGRtsVD-IIKSGGYKISALEVERHL 513
Cdd:cd17649 295 GELYIGGEGLARGYLGRPELTAERFVPdpfgapgSRLYRTGDLARWRdDGVIEYLGR--VDhQVKIRGFRIELGEIEAAL 372
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2105456023 514 LAHPAIADVAVIGPPDAIwGQKVTAVMQLKRGHRL--TLPELKIWAREHMAPYIIPTGLVLVEELPRNQMGKVNKKDL 589
Cdd:cd17649 373 LEHPGVREAAVVALDGAG-GKQLVAYVVLRAAAAQpeLRAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKAL 449
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
70-589 |
7.62e-39 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 150.13 E-value: 7.62e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 70 VFVRAPAFGDRLAIIDSSGSHSYkqlycsSFG----LAGRISAALNSdFGGLEGKRISFLCANDASYTVAQWAAWMSGG- 144
Cdd:PLN02246 29 CFERLSEFSDRPCLIDGATGRVY------TYAdvelLSRRVAAGLHK-LGIRQGDVVMLLLPNCPEFVLAFLGASRRGAv 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 145 --TAVPLYRKHpqeELEYIISDSQSSLLVAGNSFAKTLEPLALKLGLPCLTL--PPTSNLSTLDGTDSQEEEAAITDWA- 219
Cdd:PLN02246 102 ttTANPFYTPA---EIAKQAKASGAKLIITQSCYVDKLKGLAEDDGVTVVTIddPPEGCLHFSELTQADENELPEVEISp 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 220 DRPAMIIYTSGTTGRPKGVLHTH----SSIQAMVQCLVSEWAWTRDDVILHTLPLHHVHGIVNKLLCPLWVGATCIMLPE 295
Cdd:PLN02246 179 DDVVALPYSSGTTGLPKGVMLTHkglvTSVAQQVDGENPNLYFHSDDVILCVLPMFHIYSLNSVLLCGLRVGAAILIMPK 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 296 FQPQKVWEILLTSKapmVNVFMAVPTIYSKLIQyydqhftQPHVKDFVKAvckqRIRLMVSGSAalPL-PTLQR--WEEI 372
Cdd:PLN02246 259 FEIGALLELIQRHK---VTIAPFVPPIVLAIAK-------SPVVEKYDLS----SIRMVLSGAA--PLgKELEDafRAKL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 373 TGHTLLERYGMTEIGMALS-------NPLkgPRIPGAVGSPLPGVEIRIVmsnatnttiveanHRETRVRSGlEGKEGEL 445
Cdd:PLN02246 323 PNAVLGQGYGMTEAGPVLAmclafakEPF--PVKSGSCGTVVRNAELKIV-------------DPETGASLP-RNQPGEI 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 446 LVRGPSVFKEYWNKHQETRESFTDSGWFKTGDTA-IHKDGVFWIMGRTSvDIIKSGGYKISALEVERHLLAHPAIADVAV 524
Cdd:PLN02246 387 CIRGPQIMKGYLNDPEATANTIDKDGWLHTGDIGyIDDDDELFIVDRLK-ELIKYKGFQVAPAELEALLISHPSIADAAV 465
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2105456023 525 IGPPDAIWGQKVTAVMQLKRGHRLTLPELKIWAREHMAPYIIPTGLVLVEELPRNQMGKVNKKDL 589
Cdd:PLN02246 466 VPMKDEVAGEVPVAFVVRSNGSEITEDEIKQFVAKQVVFYKRIHKVFFVDSIPKAPSGKILRKDL 530
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
73-589 |
7.74e-39 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.
Pssm-ID: 341282 [Multi-domain] Cd Length: 483 Bit Score: 148.89 E-value: 7.74e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 73 RAPAFGDRLAIIDSSGSHSYKQLYCSSFGLAGRISAAlnsdfGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLYRK 152
Cdd:cd12117 6 QAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAA-----GVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 153 HPQEELEYIISDSQSSLLVAGNSFAKTLEPLALKLglpcltlpptsnLSTLDGTDSQEEEAAITDWADRPAMIIYTSGTT 232
Cdd:cd12117 81 LPAERLAFMLADAGAKVLLTDRSLAGRAGGLEVAV------------VIDEALDAGPAGNPAVPVSPDDLAYVMYTSGST 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 233 GRPKGVLHTHSSIQAmvqcLVSEWAW---TRDDVILHTLPL------HHVHGivnkllcPLWVGATCIMLPE---FQPQK 300
Cdd:cd12117 149 GRPKGVAVTHRGVVR----LVKNTNYvtlGPDDRVLQTSPLafdastFEIWG-------ALLNGARLVLAPKgtlLDPDA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 301 VWEILLTSKapmVNVFMAVPTIYSKLIQYYDQHFTQphvkdfvkavckqrIRLMVSGSAALPLPTLQRWEEITGH-TLLE 379
Cdd:cd12117 218 LGALIAEEG---VTVLWLTAALFNQLADEDPECFAG--------------LRELLTGGEVVSPPHVRRVLAACPGlRLVN 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 380 RYGMTE-IGMALSNPLK-----GPRIPgaVGSPLPGVEIRIVmsnATNTTIVEAnhretrvrsgleGKEGELLVRGPSVF 453
Cdd:cd12117 281 GYGPTEnTTFTTSHVVTeldevAGSIP--IGRPIANTRVYVL---DEDGRPVPP------------GVPGELYVGGDGLA 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 454 KEYWNKHQETRESFTDSGW------FKTGDTA-IHKDGVFWIMGRTSvDIIKSGGYKISALEVERHLLAHPAIADVAVIG 526
Cdd:cd12117 344 LGYLNRPALTAERFVADPFgpgerlYRTGDLArWLPDGRLEFLGRID-DQVKIRGFRIELGEIEAALRAHPGVREAVVVV 422
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2105456023 527 PPDAIWGQKVTAVmqLKRGHRLTLPELKIWAREHMAPYIIPTGLVLVEELPRNQMGKVNKKDL 589
Cdd:cd12117 423 REDAGGDKRLVAY--VVAEGALDAAELRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
73-592 |
8.67e-39 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 149.91 E-value: 8.67e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 73 RAPafgDRLAIIDSSGSHSYKQLYCSSFGLAgrisAALNSdFGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLYRK 152
Cdd:PRK13382 55 RCP---DRPGLIDELGTLTWRELDERSDALA----AALQA-LPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTS 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 153 HPQEELEYIISDSQSSLLVAGNSFAKTLePLALKlGLPCLT----LPPTSNLSTLDGTDSQEEEAAITDWADRPAMIIYT 228
Cdd:PRK13382 127 FAGPALAEVVTREGVDTVIYDEEFSATV-DRALA-DCPQATrivaWTDEDHDLTVEVLIAAHAGQRPEPTGRKGRVILLT 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 229 SGTTGRPKGVLHTHSSIQAMVQCLVSEWAWTRDDVILHTLPLHHVHGIVNkLLCPLWVGATCIMLPEFQPQKVWEILLTS 308
Cdd:PRK13382 205 SGTTGTPKGARRSGPGGIGTLKAILDRTPWRAEEPTVIVAPMFHAWGFSQ-LVLAASLACTIVTRRRFDPEATLDLIDRH 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 309 KAPMVNVfmaVPTIYSKLIQYYDQHFTQPHVKD--FVKAvckqrirlmvSGSAaLPLPTLQRWEEITGHTLLERYGMTEI 386
Cdd:PRK13382 284 RATGLAV---VPVMFDRIMDLPAEVRNRYSGRSlrFAAA----------SGSR-MRPDVVIAFMDQFGDVIYNNYNATEA 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 387 GM-ALSNPLKGPRIPGAVGSPLPGVEIRIVmsnatnttivEANHRETRvrsglEGKEGELLVRGPSVFKEYWN-KHQETR 464
Cdd:PRK13382 350 GMiATATPADLRAAPDTAGRPAEGTEIRIL----------DQDFREVP-----TGEVGTIFVRNDTQFDGYTSgSTKDFH 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 465 EsftdsGWFKTGDTAIHKD-GVFWIMGRtSVDIIKSGGYKISALEVERHLLAHPAIADVAVIGPPDAIWGQKVTAVMQLK 543
Cdd:PRK13382 415 D-----GFMASGDVGYLDEnGRLFVVGR-DDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLK 488
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 2105456023 544 RGHRLTLPELKIWAREHMAPYIIPTGLVLVEELPRNQMGKVNKKDLLRH 592
Cdd:PRK13382 489 PGASATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQAR 537
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
74-586 |
1.08e-37 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 146.88 E-value: 1.08e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 74 APAFGDRLAIIDSSGS--HSYKQLYCSSFGLA-GRISAalnsdfgGLE-GKRISFLCANDASYTVAQWAAWMSGGTAV-- 147
Cdd:PRK08315 26 AARYPDREALVYRDQGlrWTYREFNEEVDALAkGLLAL-------GIEkGDRVGIWAPNVPEWVLTQFATAKIGAILVti 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 148 -PLYRKHpqeELEYIISDSQSSLLVAGNSF---------------AKTLEPLALKL-GLPCLT------------LPPTS 198
Cdd:PRK08315 99 nPAYRLS---ELEYALNQSGCKALIAADGFkdsdyvamlyelapeLATCEPGQLQSaRLPELRrviflgdekhpgMLNFD 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 199 NLSTLDGTDSQEEEAAITDW--ADRPAMIIYTSGTTGRPKGVLHTHSSI--------QAMvqclvsewAWTRDDVILHTL 268
Cdd:PRK08315 176 ELLALGRAVDDAELAARQATldPDDPINIQYTSGTTGFPKGATLTHRNIlnngyfigEAM--------KLTEEDRLCIPV 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 269 PLHHVHGIVNKLLCPLWVGAT-CIMLPEFQPQKVweiLLTSKAPMVNVFMAVPTIYsklIQYYDQhftqphvKDFVK--- 344
Cdd:PRK08315 248 PLYHCFGMVLGNLACVTHGATmVYPGEGFDPLAT---LAAVEEERCTALYGVPTMF---IAELDH-------PDFARfdl 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 345 ----------AVC-----KQRIRLMvsgsaalplptlqRWEEITghtllERYGMTEI--GMALSN---PLKgpRIPGAVG 404
Cdd:PRK08315 315 sslrtgimagSPCpievmKRVIDKM-------------HMSEVT-----IAYGMTETspVSTQTRtddPLE--KRVTTVG 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 405 SPLPGVEIRIVmsNATNTTIVEAnhretrvrsgleGKEGELLVRGPSVFKEYWNKHQETRESFTDSGWFKTGDTA-IHKD 483
Cdd:PRK08315 375 RALPHLEVKIV--DPETGETVPR------------GEQGELCTRGYSVMKGYWNDPEKTAEAIDADGWMHTGDLAvMDEE 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 484 GVFWIMGRTSvDIIKSGGYKISALEVERHLLAHPAIADVAVIGPPDAIWGQKVTAVMQLKRGHRLTLPELKIWAREHMAP 563
Cdd:PRK08315 441 GYVNIVGRIK-DMIIRGGENIYPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRPGATLTEEDVRDFCRGKIAH 519
|
570 580
....*....|....*....|...
gi 2105456023 564 YIIPTGLVLVEELPRNQMGKVNK 586
Cdd:PRK08315 520 YKIPRYIRFVDEFPMTVTGKIQK 542
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
77-589 |
1.89e-37 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 146.32 E-value: 1.89e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 77 FGDRLAIIDSSGSHSYKQLYcssfGLAGRISAALNSDfgGLE-GKRISFLCANDASYTVAQWAAWMSGGTAV---PLYRK 152
Cdd:PRK07059 36 YADRPAFICMGKAITYGELD----ELSRALAAWLQSR--GLAkGARVAIMMPNVLQYPVAIAAVLRAGYVVVnvnPLYTP 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 153 HpqeELEYIISDSQSSLLVAGNSFAKTLEPL----ALK----------LGL----------------PCLTLPPTSNLST 202
Cdd:PRK07059 110 R---ELEHQLKDSGAEAIVVLENFATTVQQVlaktAVKhvvvasmgdlLGFkghivnfvvrrvkkmvPAWSLPGHVRFND 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 203 LDGTDSQEEEAAITDWADRPAMIIYTSGTTGRPKGVLHTHSSIQAMVqcLVSEwAW--------TRDD--VILHTLPLHH 272
Cdd:PRK07059 187 ALAEGARQTFKPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANV--LQME-AWlqpafekkPRPDqlNFVCALPLYH 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 273 VHGI-VNKLLcPLWVGATCIMLPefQPQKVWEILLTSKAPMVNVFMAVPTIYSKLIqyydqhftqpHVKDFVKAVCKQrI 351
Cdd:PRK07059 264 IFALtVCGLL-GMRTGGRNILIP--NPRDIPGFIKELKKYQVHIFPAVNTLYNALL----------NNPDFDKLDFSK-L 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 352 RLMVSGSAALPLPTLQRWEEITGHTLLERYGMTEIG-MALSNPLKGPRIPGAVGSPLPGVEIRIvmsnatnttiveanhR 430
Cdd:PRK07059 330 IVANGGGMAVQRPVAERWLEMTGCPITEGYGLSETSpVATCNPVDATEFSGTIGLPLPSTEVSI---------------R 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 431 ETRVRSGLEGKEGELLVRGPSVFKEYWNKHQETRESFTDSGWFKTGDTAI-HKDGVFWIMGRTSvDIIKSGGYKISALEV 509
Cdd:PRK07059 395 DDDGNDLPLGEPGEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVmDERGYTKIVDRKK-DMILVSGFNVYPNEI 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 510 ERHLLAHPAIADVAVIGPPDAIWGQKVTAVMqLKRGHRLTLPELKIWAREHMAPYIIPTGLVLVEELPRNQMGKVNKKDL 589
Cdd:PRK07059 474 EEVVASHPGVLEVAAVGVPDEHSGEAVKLFV-VKKDPALTEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRREL 552
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
84-510 |
1.92e-37 |
|
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: 145.89 E-value: 1.92e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 84 IDSSGSH---SYKQLYCSsfglAGRISAALNSDfGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPL-------YRKH 153
Cdd:cd05906 31 IDADGSEefqSYQDLLED----ARRLAAGLRQL-GLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLtvpptydEPNA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 154 PQEELEYIISDSQSSLLVAGNSFAKTLEPLALKLGLPCLTLPPTSNLStldgtdsqeEEAAITDW----ADRPAMIIYTS 229
Cdd:cd05906 106 RLRKLRHIWQLLGSPVVLTDAELVAEFAGLETLSGLPGIRVLSIEELL---------DTAADHDLpqsrPDDLALLMLTS 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 230 GTTGRPKGVLHTHSSIQAMVQCLVSEWAWTRDDVILHTLPLHHVHGIVNKLLCPLWVGATcimlpefqpqkvweilltsk 309
Cdd:cd05906 177 GSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVPLDHVGGLVELHLRAVYLGCQ-------------------- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 310 apMVNV----FMAVPTIYSKLIQYYDQHFT-QP-----HVKDFVKAVCKQR-----IRLMVSGSAALPLPTLQRWEEitg 374
Cdd:cd05906 237 --QVHVpteeILADPLRWLDLIDRYRVTITwAPnfafaLLNDLLEEIEDGTwdlssLRYLVNAGEAVVAKTIRRLLR--- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 375 htLLERY-----------GMTEI--GMALSNPLKGPRIPGA-----VGSPLPGVEIRIVmsnATNTTIVEanhretrvrs 436
Cdd:cd05906 312 --LLEPYglppdairpafGMTETcsGVIYSRSFPTYDHSQAlefvsLGRPIPGVSMRIV---DDEGQLLP---------- 376
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2105456023 437 glEGKEGELLVRGPSVFKEYWNKHQETRESFTDSGWFKTGDTAIHKDGVFWIMGRTSvDIIKSGGYKISALEVE 510
Cdd:cd05906 377 --EGEVGRLQVRGPVVTKGYYNNPEANAEAFTEDGWFRTGDLGFLDNGNLTITGRTK-DTIIVNGVNYYSHEIE 447
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
85-589 |
5.30e-37 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 144.77 E-value: 5.30e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 85 DSSGSHSYKQLYCSSFGLAGRISAALNSdfgglEGKRISFLCANDASYTVAQWAAWMSGGTAVPLYRKHPQEELEYI--I 162
Cdd:PRK05857 37 DGTSALRYRELVAEVGGLAADLRAQSVS-----RGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLPIAAIERFcqI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 163 SDSQSSLLVAGNSFAKTLEPLALKlGLPCLTLPPTSNLSTLDGTDSQEEEAAITDW-ADRPAMIIYTSGTTGRPKGVLHT 241
Cdd:PRK05857 112 TDPAAALVAPGSKMASSAVPEALH-SIPVIAVDIAAVTRESEHSLDAASLAGNADQgSEDPLAMIFTSGTTGEPKAVLLA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 242 HSSIQAMVQCLVSE---WA-WTRDDVILHTLPLHHVHGIVNKLLCpLWVGATCIMLPEfQPQKVWEILLTSKapmVNVFM 317
Cdd:PRK05857 191 NRTFFAVPDILQKEglnWVtWVVGETTYSPLPATHIGGLWWILTC-LMHGGLCVTGGE-NTTSLLEILTTNA---VATTC 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 318 AVPTIYSKLIqyYDQHFTqphvkdfvkAVCKQRIRLMV-SGSAALPLPTlqRWEEITGHTLLERYGMTEIG-MALSNPLK 395
Cdd:PRK05857 266 LVPTLLSKLV--SELKSA---------NATVPSLRLVGyGGSRAIAADV--RFIEATGVRTAQVYGLSETGcTALCLPTD 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 396 GPRIP----GAVGSPLPGVEIRIVMSNATNTTIVEAnhretrvrsGLEGKEGELLVRGPSVFKEYWNKHQETRESFTDsG 471
Cdd:PRK05857 333 DGSIVkieaGAVGRPYPGVDVYLAATDGIGPTAPGA---------GPSASFGTLWIKSPANMLGYWNNPERTAEVLID-G 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 472 WFKTGD-TAIHKDGVFWIMGRTSvDIIKSGGYKISALEVERHLLAHPAIADVAVIGPPDAIWGQKV-TAVMQLKRGHRLT 549
Cdd:PRK05857 403 WVNTGDlLERREDGFFYIKGRSS-EMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGALVgLAVVASAELDESA 481
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 2105456023 550 LPELK--IWAR-----EHMAPyiiPTGLVLVEELPRNQMGKVNKKDL 589
Cdd:PRK05857 482 ARALKhtIAARfrresEPMAR---PSTIVIVTDIPRTQSGKVMRASL 525
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
9-593 |
6.65e-37 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 144.98 E-value: 6.65e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 9 MLSSLVATASHllkRTLPHWkasfhrtFSPSeprrwllgTVIHRRAHgwtsaPSMRINQKP-------VFVRAPAFGDRl 81
Cdd:PLN02574 1 IMPNLKAQTSH---NNPPFW-------YSPE--------TGIYSSKH-----PPVPLPSDPnldavsfIFSHHNHNGDT- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 82 AIIDSSG--SHSYKQLYCssfgLAGRISAALNSDFGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLYRKHPQEELE 159
Cdd:PLN02574 57 ALIDSSTgfSISYSELQP----LVKSMAAGLYHVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIK 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 160 YIISDSQSSLLVAGNSFAKTLEPLalklGLPCLTLPPTSNLstldgtDSQEEEAAITDWA---------------DRPAM 224
Cdd:PLN02574 133 KRVVDCSVGLAFTSPENVEKLSPL----GVPVIGVPENYDF------DSKRIEFPKFYELikedfdfvpkpvikqDDVAA 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 225 IIYTSGTTGRPKGVLHTHSSIQAMVQCLV----SEWAWT-RDDVILHTLPLHHVHGIVNKLLCPLWVGATCIMLPEFQPQ 299
Cdd:PLN02574 203 IMYSSGTTGASKGVVLTHRNLIAMVELFVrfeaSQYEYPgSDNVYLAALPMFHIYGLSLFVVGLLSLGSTIVVMRRFDAS 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 300 KVWEILLTSKapmVNVFMAVPTIYSKLIqyydqHFTQPhvkdfVKAVCKQRIRLMVSGSAALPLPTLQRWEEITGHT-LL 378
Cdd:PLN02574 283 DMVKVIDRFK---VTHFPVVPPILMALT-----KKAKG-----VCGEVLKSLKQVSCGAAPLSGKFIQDFVQTLPHVdFI 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 379 ERYGMTE---IGMALSNPLKGPRIpGAVGSPLPGVEIRIV-MSNATNTTiveanhretrvrsglEGKEGELLVRGPSVFK 454
Cdd:PLN02574 350 QGYGMTEstaVGTRGFNTEKLSKY-SSVGLLAPNMQAKVVdWSTGCLLP---------------PGNCGELWIQGPGVMK 413
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 455 EYWNKHQETRESFTDSGWFKTGDTA-IHKDGVFWIMGRTSvDIIKSGGYKISALEVERHLLAHPAIADVAVIGPPDAIWG 533
Cdd:PLN02574 414 GYLNNPKATQSTIDKDGWLRTGDIAyFDEDGYLYIVDRLK-EIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECG 492
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 534 QKVTAVMQLKRGHRLTLPELKIWAREHMAPYIIPTGLVLVEELPRNQMGKVNKKDLLRHF 593
Cdd:PLN02574 493 EIPVAFVVRRQGSTLSQEAVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRRELKRSL 552
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
73-584 |
1.62e-36 |
|
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: 143.53 E-value: 1.62e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 73 RAPAFGDRLAII------DSSGSHSYKQLYCSSFGLAGRISAAlnsdfgGLEGKRISFLCANDASYTVAQWAAWMSGGTA 146
Cdd:cd05931 2 RAAARPDRPAYTflddegGREETLTYAELDRRARAIAARLQAV------GKPGDRVLLLAPPGLDFVAAFLGCLYAGAIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 147 VPLY---RKHPQEELEYIISDSQSSLLVAGNSFAKTLE------PLALKLGLPCLTLPPTSnlstlDGTDSQEEEAAITD 217
Cdd:cd05931 76 VPLPpptPGRHAERLAAILADAGPRVVLTTAAALAAVRafaasrPAAGTPRLLVVDLLPDT-----SAADWPPPSPDPDD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 218 wadrPAMIIYTSGTTGRPKGVLHTHSSIQAMVQCLVSEWAWTRDDVILHTLPLHHVHGIVNKLLCPLWVGATCIMLPefq 297
Cdd:cd05931 151 ----IAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGPSVLMS--- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 298 pqkvweilltskaPMvnVFMAVPTIYSKLIQYYDQHFTQphVKDFVKAVCKQRIR-----------LMVSGSAALPL--P 364
Cdd:cd05931 224 -------------PA--AFLRRPLRWLRLISRYRATISA--APNFAYDLCVRRVRdedlegldlssWRVALNGAEPVrpA 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 365 TLQRWEEITG------HTLLERYGMTEIGMALSNP---------------------LKGPRIPGAV-----GSPLPGVEI 412
Cdd:cd05931 287 TLRRFAEAFApfgfrpEAFRPSYGLAEATLFVSGGppgtgpvvlrvdrdalagravAVAADDPAARelvscGRPLPDQEV 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 413 RIVmsnatnttiveanHRETRVRSGlEGKEGELLVRGPSVFKEYWNKHQETRESF------TDSGWFKTGDTAIHKDGVF 486
Cdd:cd05931 367 RIV-------------DPETGRELP-DGEVGEIWVRGPSVASGYWGRPEATAETFgalaatDEGGWLRTGDLGFLHDGEL 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 487 WIMGRTSvDIIKSGGYKISALEVERHL-LAHPAI--ADVAVIGPPDAIwGQKVTAVMQLKRG-HRLTLPELK------Iw 556
Cdd:cd05931 433 YITGRLK-DLIIVRGRNHYPQDIEATAeEAHPALrpGCVAAFSVPDDG-EERLVVVAEVERGaDPADLAAIAaairaaV- 509
|
570 580 590
....*....|....*....|....*....|
gi 2105456023 557 AREHMapyIIPTGLVLVE--ELPRNQMGKV 584
Cdd:cd05931 510 AREHG---VAPADVVLVRpgSIPRTSSGKI 536
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
151-593 |
2.49e-36 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 142.92 E-value: 2.49e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 151 RKHPqEELEYIISDSQSSLLVAGNSFAKTLEPLALKL-------------GLPCLTLPPTSNLSTLDGTDSQ------EE 211
Cdd:PRK07008 97 RLFP-EQIAYIVNHAEDRYVLFDLTFLPLVDALAPQCpnvkgwvamtdaaHLPAGSTPLLCYETLVGAQDGDydwprfDE 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 212 EAAitdwadrpAMIIYTSGTTGRPKGVLHTHSS--IQAMVQCLVSEWAWTRDDVILHTLPLHHVHGIVNKLLCPLwVGAT 289
Cdd:PRK07008 176 NQA--------SSLCYTSGTTGNPKGALYSHRStvLHAYGAALPDAMGLSARDAVLPVVPMFHVNAWGLPYSAPL-TGAK 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 290 CIML-PEFQPQKVWEILltsKAPMVNVFMAVPTIYSKLIQYydqhfTQPHVKDFVKavckqrIRLMVSGSAALPLPTLQR 368
Cdd:PRK07008 247 LVLPgPDLDGKSLYELI---EAERVTFSAGVPTVWLGLLNH-----MREAGLRFST------LRRTVIGGSACPPAMIRT 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 369 WEEITGHTLLERYGMTEI---GMALSNPLKGPRIPGAV--------GSPLPGVEIRIVmsnatnttiveanhretrvrsG 437
Cdd:PRK07008 313 FEDEYGVEVIHAWGMTEMsplGTLCKLKWKHSQLPLDEqrkllekqGRVIYGVDMKIV---------------------G 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 438 LEGKE--------GELLVRGPSVFKEYWNKHqetrESFTDSGWFKTGDTA-IHKDGVFWIMGRtSVDIIKSGGYKISALE 508
Cdd:PRK07008 372 DDGRElpwdgkafGDLQVRGPWVIDRYFRGD----ASPLVDGWFPTGDVAtIDADGFMQITDR-SKDVIKSGGEWISSID 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 509 VERHLLAHPAIADVAVIGPPDAIWGQKVTAVMQLKRGHRLTLPELKIWAREHMAPYIIPTGLVLVEELPRNQMGKVNKKD 588
Cdd:PRK07008 447 IENVAVAHPAVAEAACIACAHPKWDERPLLVVVKRPGAEVTREELLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLK 526
|
....*
gi 2105456023 589 LLRHF 593
Cdd:PRK07008 527 LREQF 531
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
73-589 |
9.71e-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: 141.13 E-value: 9.71e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 73 RAPAFGDRLAIIDSSGSHSYkqLYCSSFGLAGRISAALNSdFGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLYRK 152
Cdd:cd17642 26 RYASVPGTIAFTDAHTGVNY--SYAEYLEMSVRLAEALKK-YGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 153 HPQEELEYIISDSQSSLLVAG-------------NSFAKTLEPLALKL---GLPCLTLPPTSNLSTldgtdSQEEEAAIT 216
Cdd:cd17642 103 YNERELDHSLNISKPTIVFCSkkglqkvlnvqkkLKIIKTIIILDSKEdykGYQCLYTFITQNLPP-----GFNEYDFKP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 217 DWADRP---AMIIYTSGTTGRPKGVLHTH--------SSIQAMVQCLVSEwawtrDDVILHTLPLHHVHGIVNkLLCPLW 285
Cdd:cd17642 178 PSFDRDeqvALIMNSSGSTGLPKGVQLTHknivarfsHARDPIFGNQIIP-----DTAILTVIPFHHGFGMFT-TLGYLI 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 286 VGATCIMLPEFQPQKVWEILLTSKAPMVnvfMAVPTIY-----SKLIQYYDQHftqphvkdfvkavckqriRLMVSGSAA 360
Cdd:cd17642 252 CGFRVVLMYKFEEELFLRSLQDYKVQSA---LLVPTLFaffakSTLVDKYDLS------------------NLHEIASGG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 361 LPLptlqrwEEITGHTLLER---------YGMTEIGMALSNPLKGPRIPGAVGSPLPGVEIRIVmsNATNTTIVEANHRe 431
Cdd:cd17642 311 APL------SKEVGEAVAKRfklpgirqgYGLTETTSAILITPEGDDKPGAVGKVVPFFYAKVV--DLDTGKTLGPNER- 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 432 trvrsglegkeGELLVRGPSVFKEYWNKHQETRESFTDSGWFKTGDTAIH-KDGVFWIMGRTSvDIIKSGGYKISALEVE 510
Cdd:cd17642 382 -----------GELCVKGPMIMKGYVNNPEATKALIDKDGWLHSGDIAYYdEDGHFFIVDRLK-SLIKYKGYQVPPAELE 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 511 RHLLAHPAIADVAVIGPPDAIWGQKVTAVMQLKRGHRLTLPELKIWAREHMAPYI-IPTGLVLVEELPRNQMGKVNKKDL 589
Cdd:cd17642 450 SILLQHPKIFDAGVAGIPDEDAGELPAAVVVLEAGKTMTEKEVMDYVASQVSTAKrLRGGVKFVDEVPKGLTGKIDRRKI 529
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
78-584 |
1.04e-35 |
|
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: 141.56 E-value: 1.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 78 GDRLAII------DSSGSHSYKQLYCSSFGLAGRISaalnsDFGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLYR 151
Cdd:cd17634 67 GDRTAIIyegddtSQSRTISYRELHREVCRFAGTLL-----DLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFG 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 152 KHPQEELEYIISDSQSSLLVAGNSFAK-----TLEPLALKLGLPCLTLPPTSNLSTLDGTDSQEEEAAITDW-------- 218
Cdd:cd17634 142 GFAPEAVAGRIIDSSSRLLITADGGVRagrsvPLKKNVDDALNPNVTSVEHVIVLKRTGSDIDWQEGRDLWWrdliakas 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 219 ---------ADRPAMIIYTSGTTGRPKGVLHTH-----SSIQAMVQCL---VSEWAWTRDDVILHTLPLHHVHGivnkll 281
Cdd:cd17634 222 pehqpeamnAEDPLFILYTSGTTGKPKGVLHTTggylvYAATTMKYVFdygPGDIYWCTADVGWVTGHSYLLYG------ 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 282 cPLWVGATCIML---PEF-QPQKVWEILLTSKapmVNVFMAVPTIYSKLIQYYDqhftqphvkdfvKAVCKQRI-RLMVS 356
Cdd:cd17634 296 -PLACGATTLLYegvPNWpTPARMWQVVDKHG---VNILYTAPTAIRALMAAGD------------DAIEGTDRsSLRIL 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 357 GSAALPL-PTLQRW--EEITGH--TLLERYGMTEIGMALSNPLKG--PRIPGAVGSPLPGVEIRIVmSNATNTtiVEAnh 429
Cdd:cd17634 360 GSVGEPInPEAYEWywKKIGKEkcPVVDTWWQTETGGFMITPLPGaiELKAGSATRPVFGVQPAVV-DNEGHP--QPG-- 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 430 retrvrsgleGKEGELLVRG--PSVFKEYWNKHQETRESF--TDSGWFKTGDTA-IHKDGVFWIMGRtSVDIIKSGGYKI 504
Cdd:cd17634 435 ----------GTEGNLVITDpwPGQTRTLFGDHERFEQTYfsTFKGMYFSGDGArRDEDGYYWITGR-SDDVINVAGHRL 503
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 505 SALEVERHLLAHPAIADVAVIGPPDAIWGQKVTAVMQLKRGhrLTLP-----ELKIWAREHMAPYIIPTGLVLVEELPRN 579
Cdd:cd17634 504 GTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLNHG--VEPSpelyaELRNWVRKEIGPLATPDVVHWVDSLPKT 581
|
....*
gi 2105456023 580 QMGKV 584
Cdd:cd17634 582 RSGKI 586
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
36-589 |
1.70e-35 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 140.13 E-value: 1.70e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 36 FSPSEPRRWLlgTVIHRRAHGWTSAPSmrinqkPVFVRAPAFGDRLAIIDSSGSHSYKQLYCSSFGLAGRISAAlnsdfG 115
Cdd:PRK13383 15 LNPPSPRAVL--RLLREASRGGTNPYT------LLAVTAARWPGRTAIIDDDGALSYRELQRATESLARRLTRD-----G 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 116 GLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLYRKHPQEELEYIISDSQSSLLVAGNSFAKTLEplalKLGLPCLTLP 195
Cdd:PRK13383 82 VAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAALRAHHISTVVADNEFAERIA----GADDAVAVID 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 196 PTsnlstldgTDSQEEEAAITDWADRPAMIIYTSGTTGRPKGVLHThSSIQAMVQCLVSEWAWTRDDV---ILHTLPLHH 272
Cdd:PRK13383 158 PA--------TAGAEESGGRPAVAAPGRIVLLTSGTTGKPKGVPRA-PQLRSAVGVWVTILDRTRLRTgsrISVAMPMFH 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 273 VHGIvNKLLCPLWVGATCIMLPEFQPQKVweiLLTSKAPMVNVFMAVPTIYSKLIQYYDQhftqphvkdfVKAVCK-QRI 351
Cdd:PRK13383 229 GLGL-GMLMLTIALGGTVLTHRHFDAEAA---LAQASLHRADAFTAVPVVLARILELPPR----------VRARNPlPQL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 352 RLMVSGSAALPlPTL-QRWEEITGHTLLERYGMTEIGM-ALSNPLKGPRIPGAVGSPLPGVEIRivmsnatnttIVEANH 429
Cdd:PRK13383 295 RVVMSSGDRLD-PTLgQRFMDTYGDILYNGYGSTEVGIgALATPADLRDAPETVGKPVAGCPVR----------ILDRNN 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 430 RETrvrsglegkegellvrGPSVFKEYWNKHQETRESFTD-------SGWFKTGDTA-IHKDGVFWIMGRTSvDIIKSGG 501
Cdd:PRK13383 364 RPV----------------GPRVTGRIFVGGELAGTRYTDgggkavvDGMTSTGDMGyLDNAGRLFIVGRED-DMIISGG 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 502 YKISALEVERHLLAHPAIADVAVIGPPDAIWGQKVTAVMQLKRGHRLTLPELKIWAREHMAPYIIPTGLVLVEELPRNQM 581
Cdd:PRK13383 427 ENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPGSGVDAAQLRDYLKDRVSRFEQPRDINIVSSIPRNPT 506
|
....*...
gi 2105456023 582 GKVNKKDL 589
Cdd:PRK13383 507 GKVLRKEL 514
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
219-591 |
2.72e-35 |
|
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: 140.85 E-value: 2.72e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 219 ADRPAMIIYTSGTTGRPKGVLHThsSIQAMVQCLVSEWaWT---RDDVIL-----------HTlplHHVHGivnkllcPL 284
Cdd:TIGR02188 236 SEDPLFILYTSGSTGKPKGVLHT--TGGYLLYAAMTMK-YVfdiKDGDIFwctadvgwitgHS---YIVYG-------PL 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 285 WVGATCIML---PEF-QPQKVWEILLTSKapmVNVFMAVPTIYSKLIQYYDQHftqphvkdfVKAVCKQRIRLMvsGSAA 360
Cdd:TIGR02188 303 ANGATTVMFegvPTYpDPGRFWEIIEKHK---VTIFYTAPTAIRALMRLGDEW---------VKKHDLSSLRLL--GSVG 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 361 LPL-PTLQRW-EEITGHT---LLERYGMTEIGMALSNPLKG--PRIPGAVGSPLPGVEIRIVmsnATNTTIVEANhretr 433
Cdd:TIGR02188 369 EPInPEAWMWyYKVVGKErcpIVDTWWQTETGGIMITPLPGatPTKPGSATLPFFGIEPAVV---DEEGNPVEGP----- 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 434 vrsgleGKEGELLVRG--PSVFKEYWNKHQETRESFTD--SGWFKTGDTAIH-KDGVFWIMGRTSvDIIKSGGYKISALE 508
Cdd:TIGR02188 441 ------GEGGYLVIKQpwPGMLRTIYGDHERFVDTYFSpfPGYYFTGDGARRdKDGYIWITGRVD-DVINVSGHRLGTAE 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 509 VERHLLAHPAIADVAVIGPPDAIWGQKVTAVMQLKRG---HRLTLPELKIWAREHMAPYIIPTGLVLVEELPRNQMGKVN 585
Cdd:TIGR02188 514 IESALVSHPAVAEAAVVGIPDDIKGQAIYAFVTLKDGyepDDELRKELRKHVRKEIGPIAKPDKIRFVPGLPKTRSGKIM 593
|
....*.
gi 2105456023 586 KKdLLR 591
Cdd:TIGR02188 594 RR-LLR 598
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
222-591 |
3.98e-35 |
|
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: 140.00 E-value: 3.98e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 222 PAMIIYTSGTTGRPKGVLHTHSSIqaMVQCLVS-EWAW-TRDDVIL-----------HTlplHHVHGivnkllcPLWVGA 288
Cdd:cd05966 233 PLFILYTSGSTGKPKGVVHTTGGY--LLYAATTfKYVFdYHPDDIYwctadigwitgHS---YIVYG-------PLANGA 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 289 TCIML---PEF-QPQKVWEILLTSKapmVNVFMAVPTIYSKLIQYYDqhftqphvkDFVKAVCKQRIRLMvsGSAALPL- 363
Cdd:cd05966 301 TTVMFegtPTYpDPGRYWDIVEKHK---VTIFYTAPTAIRALMKFGD---------EWVKKHDLSSLRVL--GSVGEPIn 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 364 PTLQRW-EEITGH---TLLERYGMTEIGMALSNPLKG--PRIPGAVGSPLPGVEIRIVmsnaTNTTIVEANHREtrvrsg 437
Cdd:cd05966 367 PEAWMWyYEVIGKercPIVDTWWQTETGGIMITPLPGatPLKPGSATRPFFGIEPAIL----DEEGNEVEGEVE------ 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 438 legkeGELLVRG--PSVFKEYWNKHQETRESF--TDSGWFKTGDTAIH-KDGVFWIMGRTSvDIIKSGGYKISALEVERH 512
Cdd:cd05966 437 -----GYLVIKRpwPGMARTIYGDHERYEDTYfsKFPGYYFTGDGARRdEDGYYWITGRVD-DVINVSGHRLGTAEVESA 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 513 LLAHPAIADVAVIGPPDAIWGQKVTAVMQLKRGHRLTLP---ELKIWAREHMAPYIIPTGLVLVEELPRNQMGKVNKKdL 589
Cdd:cd05966 511 LVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGEEPSDElrkELRKHVRKEIGPIATPDKIQFVPGLPKTRSGKIMRR-I 589
|
..
gi 2105456023 590 LR 591
Cdd:cd05966 590 LR 591
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
225-585 |
1.48e-34 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 134.43 E-value: 1.48e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 225 IIYTSGTTGRPKGVLHTHSSI--------------QAMVQCLVSEWAWTRDDVILHTLPLHHVHGIVNKLLCPLWVGATC 290
Cdd:cd05924 8 ILYTGGTTGMPKGVMWRQEDIfrmlmggadfgtgeFTPSEDAHKAAAAAAGTVMFPAPPLMHGTGSWTAFGGLLGGQTVV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 291 IMLPEFQPQKVWEILLTSKA---PMVNVFMAVPTIyskliqyydQHFTQPHVKDFvkavckQRIRLMVSGSAALPLPTLQ 367
Cdd:cd05924 88 LPDDRFDPEEVWRTIEKHKVtsmTIVGDAMARPLI---------DALRDAGPYDL------SSLFAISSGGALLSPEVKQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 368 RWEEITGH-TLLERYGMTEIGMalsnplkgpripGAVGSPLPGVEIRIVMSNATNTTIVEANHreTRVRSGLEGKEGELL 446
Cdd:cd05924 153 GLLELVPNiTLVDAFGSSETGF------------TGSGHSAGSGPETGPFTRANPDTVVLDDD--GRVVPPGSGGVGWIA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 447 VRGpSVFKEYWNKHQETRESFTDSG---WFKTGDTA-IHKDGVFWIMGRTSVdIIKSGGYKISALEVERHLLAHPAIADV 522
Cdd:cd05924 219 RRG-HIPLGYYGDEAKTAETFPEVDgvrYAVPGDRAtVEADGTVTLLGRGSV-CINTGGEKVFPEEVEEALKSHPAVYDV 296
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2105456023 523 AVIGPPDAIWGQKVTAVMQLKRGHRLTLPELKIWAREHMAPYIIPTGLVLVEELPRNQMGKVN 585
Cdd:cd05924 297 LVVGRPDERWGQEVVAVVQLREGAGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGKAD 359
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
79-589 |
1.95e-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: 135.46 E-value: 1.95e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 79 DRLAIIDSSGSHSYKQLYcssfGLAGRISAALnSDFGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLYRKHPQEEL 158
Cdd:cd17652 2 DAPAVVFGDETLTYAELN----ARANRLARLL-AARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 159 EYIISDSQSSLLvagnsfaktleplalklglpcLTLPptsnlstldgtdsqeeeaaitdwaDRPAMIIYTSGTTGRPKGV 238
Cdd:cd17652 77 AYMLADARPALL---------------------LTTP------------------------DNLAYVIYTSGSTGRPKGV 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 239 LHTHSSIQAMVQCLVSEWAWTRDDVILHTLPLHhVHGIVNKLLCPLWVGATCIMLPEFqpqkvweiLLTSKAPMVNVfma 318
Cdd:cd17652 112 VVTHRGLANLAAAQIAAFDVGPGSRVLQFASPS-FDASVWELLMALLAGATLVLAPAE--------ELLPGEPLADL--- 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 319 vptiyskLIQYYDQHFTQ-PHVKDFVKAVCKQRIRLMVSGSAALPLPTLQRWEeiTGHTLLERYGMTE--IGMALSNPLK 395
Cdd:cd17652 180 -------LREHRITHVTLpPAALAALPPDDLPDLRTLVVAGEACPAELVDRWA--PGRRMINAYGPTEttVCATMAGPLP 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 396 GPRIPgAVGSPLPGVEIRIVmsnatnttiveanhrETRVRSGLEGKEGELLVRGPSVFKEYWNKHQETRESFT-----DS 470
Cdd:cd17652 251 GGGVP-PIGRPVPGTRVYVL---------------DARLRPVPPGVPGELYIAGAGLARGYLNRPGLTAERFVadpfgAP 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 471 G--WFKTGDTAIHK-DGVFWIMGRTSvDIIKSGGYKISALEVERHLLAHPAIADVAVIGPPDAIWGQKVTAVMQLKRGHR 547
Cdd:cd17652 315 GsrMYRTGDLARWRaDGQLEFLGRAD-DQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAPGAA 393
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 2105456023 548 LTLPELKIWAREHMAPYIIPTGLVLVEELPRNQMGKVNKKDL 589
Cdd:cd17652 394 PTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
142-589 |
3.85e-34 |
|
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: 135.53 E-value: 3.85e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 142 SGGTAVPLYRKHPQEELEYIISDSQSSLLVAgnsfAKTLEPLALKLGLPCLtlpptsnlstLDGTDSQEEEA---AITDW 218
Cdd:cd17655 70 AGGAYLPIDPDYPEERIQYILEDSGADILLT----QSHLQPPIAFIGLIDL----------LDEDTIYHEESenlEPVSK 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 219 ADRPAMIIYTSGTTGRPKGVLHTHSSIQAMVQCLVSEWAWTRDDVILHTLPLH---HVHGIVNKLLCplwvGATCIMLPe 295
Cdd:cd17655 136 SDDLAYVIYTSGSTGKPKGVMIEHRGVVNLVEWANKVIYQGEHLRVALFASISfdaSVTEIFASLLS----GNTLYIVR- 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 296 fqpqkvweilltsKAPMVNVfmavptiySKLIQYYDQH------FTQPHVK--DFVKAVCKQRIRLMVSGSAALPLPTLQ 367
Cdd:cd17655 211 -------------KETVLDG--------QALTQYIRQNritiidLTPAHLKllDAADDSEGLSLKHLIVGGEALSTELAK 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 368 RWEEITGH--TLLERYGMTE------IGMALSNPLKGPRIPgaVGSPLpgveirivmSNaTNTTIVEANHRETRVrsgle 439
Cdd:cd17655 270 KIIELFGTnpTITNAYGPTEttvdasIYQYEPETDQQVSVP--IGKPL---------GN-TRIYILDQYGRPQPV----- 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 440 GKEGELLVRGPSVFKEYWNKHQETRESFTDSGW------FKTGDTA-IHKDGVFWIMGRTSvDIIKSGGYKISALEVERH 512
Cdd:cd17655 333 GVAGELYIGGEGVARGYLNRPELTAEKFVDDPFvpgermYRTGDLArWLPDGNIEFLGRID-HQVKIRGYRIELGEIEAR 411
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2105456023 513 LLAHPAIADVAVIGPPDAIWGQKVTAVMQLKRghRLTLPELKIWAREHMAPYIIPTGLVLVEELPRNQMGKVNKKDL 589
Cdd:cd17655 412 LLQHPDIKEAVVIARKDEQGQNYLCAYIVSEK--ELPVAQLREFLARELPDYMIPSYFIKLDEIPLTPNGKVDRKAL 486
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
108-591 |
7.14e-34 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 135.20 E-value: 7.14e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 108 AALNSDFGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLYRKHPQEELEYIISDSQSSLLVAGNSFAKTLEPLALKL 187
Cdd:PRK13391 38 AHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAAYIVDDSGARALITSAAKLDVARALLKQC 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 188 --GLPCLTLpptSNLSTLDGTDSQEEeaAITDWADRP-------AMIIYTSGTTGRPKGVLH--------THSSIQAMVQ 250
Cdd:PRK13391 118 pgVRHRLVL---DGDGELEGFVGYAE--AVAGLPATPiadeslgTDMLYSSGTTGRPKGIKRplpeqppdTPLPLTAFLQ 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 251 CLvseWAWTRDDVILHTLPLHHVH-----GIVNKLlcplwvGATCIMLPEFQPQKVWEILLTSKapmVNVFMAVPTIYSK 325
Cdd:PRK13391 193 RL---WGFRSDMVYLSPAPLYHSApqravMLVIRL------GGTVIVMEHFDAEQYLALIEEYG---VTHTQLVPTMFSR 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 326 LIQYYDQhftqphvkdfvkavckQRIR-----LMVSGSAALPLPTLQRWEEIT--GHTLLERYGMTE-IGMALSNPLKGP 397
Cdd:PRK13391 261 MLKLPEE----------------VRDKydlssLEVAIHAAAPCPPQVKEQMIDwwGPIIHEYYAATEgLGFTACDSEEWL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 398 RIPGAVGSPLPGVeirivmsnatnTTIVEANHRETRVrsgleGKEGELLVRGPSVFkEYWNKHQETRESFT-DSGWFKTG 476
Cdd:PRK13391 325 AHPGTVGRAMFGD-----------LHILDDDGAELPP-----GEPGTIWFEGGRPF-EYLNDPAKTAEARHpDGTWSTVG 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 477 DTA-IHKDGVFWIMGRTSVDIIkSGGYKISALEVERHLLAHPAIADVAVIGPPDAIWGQKVTAVMQLKRGHRLT---LPE 552
Cdd:PRK13391 388 DIGyVDEDGYLYLTDRAAFMII-SGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPVDGVDPGpalAAE 466
|
490 500 510
....*....|....*....|....*....|....*....
gi 2105456023 553 LKIWAREHMAPYIIPTGLVLVEELPRNQMGKVNKKdLLR 591
Cdd:PRK13391 467 LIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKR-LLR 504
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
114-591 |
7.38e-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: 134.81 E-value: 7.38e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 114 FGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLYRKHPQEELEYIIsdsqssllvagnsfaktlepLALKLGLPCLt 193
Cdd:cd05929 37 EGVWIADGVYIYLINSILTVFAAAAAWKCGACPAYKSSRAPRAEACAII--------------------EIKAAALVCG- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 194 LPPTSNLSTLDGTDSQEEEAA----ITDWAdRPAMIIYTSGTTGRPKGVLHTHSSIQAMVQCLVSeWA----WTRDDVIL 265
Cdd:cd05929 96 LFTGGGALDGLEDYEAAEGGSpetpIEDEA-AGWKMLYSGGTTGRPKGIKRGLPGGPPDNDTLMA-AAlgfgPGADSVYL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 266 HTLPLHHVHGIVNKLLCpLWVGATCIMLPEFQPQkvwEILLTSKAPMVNVFMAVPTIYSKLIQYYDQhftQPHVKDF--V 343
Cdd:cd05929 174 SPAPLYHAAPFRWSMTA-LFMGGTLVLMEKFDPE---EFLRLIERYRVTFAQFVPTMFVRLLKLPEA---VRNAYDLssL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 344 KAVCKqrirlmvsgsAALPLPTL--QRWEEITGHTLLERYGMTE-IGMALSNPLKGPRIPGAVGSPLPGvEIRIVmsnat 420
Cdd:cd05929 247 KRVIH----------AAAPCPPWvkEQWIDWGGPIIWEYYGGTEgQGLTIINGEEWLTHPGSVGRAVLG-KVHIL----- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 421 nttivEANHRETRvrsglEGKEGELLVRGPSVFkEYWNKHQETRESFTDSGWFKTGDTA-IHKDGVFWIMGRTSvDIIKS 499
Cdd:cd05929 311 -----DEDGNEVP-----PGEIGEVYFANGPGF-EYTNDPEKTAAARNEGGWSTLGDVGyLDEDGYLYLTDRRS-DMIIS 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 500 GGYKISALEVERHLLAHPAIADVAVIGPPDAIWGQKVTAVMQ---LKRGHRLTLPELKIWAREHMAPYIIPTGLVLVEEL 576
Cdd:cd05929 379 GGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVQpapGADAGTALAEELIAFLRDRLSRYKCPRSIEFVAEL 458
|
490
....*....|....*
gi 2105456023 577 PRNQMGKVNKKdLLR 591
Cdd:cd05929 459 PRDDTGKLYRR-LLR 472
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
223-593 |
3.45e-33 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 130.55 E-value: 3.45e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 223 AMIIYTSGTTGRPKGVLHTH----SSIQAMVQCLVSEWAWtrddviLHTLPLHHVHGIvNKLLCPLWVGA--TCIMLPE- 295
Cdd:PRK07824 38 ALVVATSGTTGTPKGAMLTAaaltASADATHDRLGGPGQW------LLALPAHHIAGL-QVLVRSVIAGSepVELDVSAg 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 296 FQPqkvweilltSKAPMVNVFMAVPTIYSKLIQyydqhfTQphvkdFVKAV-------CKQRIRLMVSGSAALPLPTLQR 368
Cdd:PRK07824 111 FDP---------TALPRAVAELGGGRRYTSLVP------MQ-----LAKALddpaataALAELDAVLVGGGPAPAPVLDA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 369 WEEItGHTLLERYGMTEIGmalsnplkgpriPGAV--GSPLPGVEIRIVmsnatnttiveanhretrvrsglegkEGELL 446
Cdd:PRK07824 171 AAAA-GINVVRTYGMSETS------------GGCVydGVPLDGVRVRVE--------------------------DGRIA 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 447 VRGPSVFKEYWNkhQETRESFTDSGWFKTGDTAIHKDGVFWIMGRTSvDIIKSGGYKISALEVERHLLAHPAIADVAVIG 526
Cdd:PRK07824 212 LGGPTLAKGYRN--PVDPDPFAEPGWFRTDDLGALDDGVLTVLGRAD-DAISTGGLTVLPQVVEAALATHPAVADCAVFG 288
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2105456023 527 PPDAIWGQKVTAVMQLKRGHRLTLPELKIWAREHMAPYIIPTGLVLVEELPRNQMGKVNKKDLLRHF 593
Cdd:PRK07824 289 LPDDRLGQRVVAAVVGDGGPAPTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALVRRF 355
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
79-589 |
3.32e-32 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 133.36 E-value: 3.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 79 DRLAIIDSSGSHSYKQLYCSSFGLAGRISAAlnsdfGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLYRKHPQEEL 158
Cdd:PRK12467 527 ERPALVFGEQVLSYAELNRQANRLAHVLIAA-----GVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRL 601
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 159 EYIISDSQSSLLVAGNSFAKTLePLALKLGLPCLTLPptsnLSTLDGTDSQEEEAAITdwADRPAMIIYTSGTTGRPKGV 238
Cdd:PRK12467 602 AYMLDDSGVRLLLTQSHLLAQL-PVPAGLRSLCLDEP----ADLLCGYSGHNPEVALD--PDNLAYVIYTSGSTGQPKGV 674
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 239 LHTHSSIQAMVQCLVSEWAWTRDDVILHTLPLhHVHGIVNKLLCPLWVGATCIMLPEFQPQKVWEILLTSKAPMVNVFMA 318
Cdd:PRK12467 675 AISHGALANYVCVIAERLQLAADDSMLMVSTF-AFDLGVTELFGALASGATLHLLPPDCARDAEAFAALMADQGVTVLKI 753
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 319 VPTIYSKLIQyydqhftqphvkDFVKAVCKQRIRLMVSGSaALPLPTLQRWEEIT-GHTLLERYGMTE--IGMALSNPLK 395
Cdd:PRK12467 754 VPSHLQALLQ------------ASRVALPRPQRALVCGGE-ALQVDLLARVRALGpGARLINHYGPTEttVGVSTYELSD 820
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 396 GPRIPGAV--GSPLPGVEIRIvMSNATNTTIVeanhretrvrsgleGKEGELLVRGPSVFKEYWNKHQETRESF------ 467
Cdd:PRK12467 821 EERDFGNVpiGQPLANLGLYI-LDHYLNPVPV--------------GVVGELYIGGAGLARGYHRRPALTAERFvpdpfg 885
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 468 TDSG-WFKTGDTAIH-KDGVFWIMGRTSvDIIKSGGYKISALEVERHLLAHPAIADVAVIGPPDAIWGQKVT----AVMQ 541
Cdd:PRK12467 886 ADGGrLYRTGDLARYrADGVIEYLGRMD-HQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAGLQLVAylvpAAVA 964
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 2105456023 542 LKRGHRLTLPELKIWAREHMAPYIIPTGLVLVEELPRNQMGKVNKKDL 589
Cdd:PRK12467 965 DGAEHQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKAL 1012
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
79-586 |
3.74e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 127.55 E-value: 3.74e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 79 DRLAIIDSSGSHSYKQLYCSSFGLAGRISAAlnsdfGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLYRKHPQEEL 158
Cdd:PRK06164 25 DAVALIDEDRPLSRAELRALVDRLAAWLAAQ-----GVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 159 EYIISDSQSSLLVAGNSFaKTLEPLALKLGLPCLTLPPTSNLSTLDGTDS---------------QEEEAAIT------D 217
Cdd:PRK06164 100 AHILGRGRARWLVVWPGF-KGIDFAAILAAVPPDALPPLRAIAVVDDAADatpapapgarvqlfaLPDPAPPAaageraA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 218 WADRPAMIIYTSGTTGRPKGVLHTHSSIQAMVQCLVSEWAWTRDDVILHTLPLHHVHGIvNKLLCPLWVGATCIMLPEFQ 297
Cdd:PRK06164 179 DPDAGALLFTTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFGF-STLLGALAGGAPLVCEPVFD 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 298 PQKVWEILLTSKapMVNVFmAVPTIYSKLIQyydqhfTQPHVKDFVKAvckqriRLMVSGSAALPLPTLQRWEEITGHTL 377
Cdd:PRK06164 258 AARTARALRRHR--VTHTF-GNDEMLRRILD------TAGERADFPSA------RLFGFASFAPALGELAALARARGVPL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 378 LERYGMTE-IGMALSNPLKGP---RIPGAvGSPL-PGVEIRIvmsnatnttiveanhRETRVRSGLE-GKEGELLVRGPS 451
Cdd:PRK06164 323 TGLYGSSEvQALVALQPATDPvsvRIEGG-GRPAsPEARVRA---------------RDPQDGALLPdGESGEIEIRAPS 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 452 VFKEYWNKHQETRESFTDSGWFKTGDTAIHK-DGVFWIMGRTSvDIIKSGGYKISALEVERHLLAHPAIADVAVIGPpdA 530
Cdd:PRK06164 387 LMRGYLDNPDATARALTDDGYFRTGDLGYTRgDGQFVYQTRMG-DSLRLGGFLVNPAEIEHALEALPGVAAAQVVGA--T 463
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 2105456023 531 IWGQKV-TAVMQLKRGHRLTLPELKIWAREHMAPYIIPTGLVLVEELPRNQMGKVNK 586
Cdd:PRK06164 464 RDGKTVpVAFVIPTDGASPDEAGLMAACREALAGFKVPARVQVVEAFPVTESANGAK 520
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
184-592 |
2.69e-30 |
|
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: 123.45 E-value: 2.69e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 184 ALKLGlpCLTLPPTSNLSTLDGTDSQEEEAAI------TDWADRPAMIIYTSGTTGRPKGVLHTHSSIQAmvqCLVSEWA 257
Cdd:cd05974 45 AMKLG--AVVIPATTLLTPDDLRDRVDRGGAVyaavdeNTHADDPMLLYFTSGTTSKPKLVEHTHRSYPV---GHLSTMY 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 258 WT---RDDVILH-TLPLHHVHGIVNkLLCPLWVGATCIML--PEFQPQKVWEILLTSKapmVNVFMAVPTIYSKLIQyyd 331
Cdd:cd05974 120 WIglkPGDVHWNiSSPGWAKHAWSC-FFAPWNAGATVFLFnyARFDAKRVLAALVRYG---VTTLCAPPTVWRMLIQ--- 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 332 QHFTQPHVKdfvkavckqrIRLMVSGSAALPLPTLQRWEEITGHTLLERYGMTEIGMALSNPLKGPRIPGAVGSPLPGVe 411
Cdd:cd05974 193 QDLASFDVK----------LREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETTALVGNSPGQPVKAGSMGRPLPGY- 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 412 iRIVMSNAtnttiveanhretrvrSGLEGKEGELLV-----RGPSVFKEYWNKHQETRESFTDsGWFKTGDTAIH-KDGV 485
Cdd:cd05974 262 -RVALLDP----------------DGAPATEGEVALdlgdtRPVGLMKGYAGDPDKTAHAMRG-GYYRTGDIAMRdEDGY 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 486 FWIMGRTSvDIIKSGGYKISALEVERHLLAHPAIADVAVIGPPDAIWGQKVTAVMQLKRGHRLTlPELKI----WAREHM 561
Cdd:cd05974 324 LTYVGRAD-DVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGYEPS-PETALeifrFSRERL 401
|
410 420 430
....*....|....*....|....*....|.
gi 2105456023 562 APYIIPTGLVLVeELPRNQMGKVNKKDLLRH 592
Cdd:cd05974 402 APYKRIRRLEFA-ELPKTISGKIRRVELRRR 431
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
219-587 |
5.66e-30 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 125.81 E-value: 5.66e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 219 ADRPAMIIYTSGTTGRPKGVLHTHSSIQAMVQCLVSEWAWTRDDVILHTLPLHHVHGIVNKLLCPLWVGATCIMLPEfqP 298
Cdd:PRK08633 781 PDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSSLPFFHSFGLTVTLWLPLLEGIKVVYHPD--P 858
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 299 QKVWEILLTSKAPMVNVFMAVPT---IYSKliqyydqhFTQPHVKDFvkavckQRIRLMVSGSAALPLPTLQRWEEITGH 375
Cdd:PRK08633 859 TDALGIAKLVAKHRATILLGTPTflrLYLR--------NKKLHPLMF------ASLRLVVAGAEKLKPEVADAFEEKFGI 924
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 376 TLLERYGMTE-----------IGMALSNPLKGPRiPGAVGSPLPGVEIRIVMSNatntTIVEANHretrvrsgleGKEGE 444
Cdd:PRK08633 925 RILEGYGATEtspvasvnlpdVLAADFKRQTGSK-EGSVGMPLPGVAVRIVDPE----TFEELPP----------GEDGL 989
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 445 LLVRGPSVFKEYWNKHQETRESFTD---SGWFKTGDTA-IHKDGVFWIMGRTSvDIIKSGGYKIS--ALEVERHLLAHPA 518
Cdd:PRK08633 990 ILIGGPQVMKGYLGDPEKTAEVIKDidgIGWYVTGDKGhLDEDGFLTITDRYS-RFAKIGGEMVPlgAVEEELAKALGGE 1068
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2105456023 519 IADVAVIGPPDAiwgqkvtavmqlKRGHRL----TLPELKIWA-REHMA-----PYIIPTGLVLVEELPRNQMGKVNKK 587
Cdd:PRK08633 1069 EVVFAVTAVPDE------------KKGEKLvvlhTCGAEDVEElKRAIKesglpNLWKPSRYFKVEALPLLGSGKLDLK 1135
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
91-526 |
1.41e-29 |
|
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: 123.09 E-value: 1.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 91 SYKQLYcssfGLAGRISAALNSDFG-GLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLYRKHPQEELEYIISDSQSSL 169
Cdd:cd05927 7 SYKEVA----ERADNIGSALRSLGGkPAPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 170 LVagnsFAKTLEPLAL----KLG--LPCLTLPPT-SNLSTldgtdsqeeeaaitdwadrpamIIYTSGTTGRPKGVLHTH 242
Cdd:cd05927 83 VF----CDAGVKVYSLeefeKLGkkNKVPPPPPKpEDLAT----------------------ICYTSGTTGNPKGVMLTH 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 243 SSIQAMVQCLVSEW----AWTRDDVILHTLPLHHVHGIVNKLLCpLWVGAtCIMLPEFQPQKVWEILLTSKaPmvNVFMA 318
Cdd:cd05927 137 GNIVSNVAGVFKILeilnKINPTDVYISYLPLAHIFERVVEALF-LYHGA-KIGFYSGDIRLLLDDIKALK-P--TVFPG 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 319 VPTIYSKLiqyYDQHFTQPHVKDFVK------AVCKQ-----------------------------RIRLMVSGSAALPL 363
Cdd:cd05927 212 VPRVLNRI---YDKIFNKVQAKGPLKrklfnfALNYKlaelrsgvvraspfwdklvfnkikqalggNVRLMLTGSAPLSP 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 364 PTLQRWEEITGHTLLERYGMTEI--GMALSNPlkGPRIPGAVGSPLPGVEIRIVmsnatntTIVEANHRETRvrsglEGK 441
Cdd:cd05927 289 EVLEFLRVALGCPVLEGYGQTECtaGATLTLP--GDTSVGHVGGPLPCAEVKLV-------DVPEMNYDAKD-----PNP 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 442 EGELLVRGPSVFKEYWNKHQETRESFTDSGWFKTGDTA-IHKDGVFWIMGRTSvDIIK-SGGYKISALEVERHLLAHPAI 519
Cdd:cd05927 355 RGEVCIRGPNVFSGYYKDPEKTAEALDEDGWLHTGDIGeWLPNGTLKIIDRKK-NIFKlSQGEYVAPEKIENIYARSPFV 433
|
....*..
gi 2105456023 520 ADVAVIG 526
Cdd:cd05927 434 AQIFVYG 440
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
73-591 |
1.82e-29 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 125.07 E-value: 1.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 73 RAPafgDRLAIIDSSGSHSYKQLYCSSFGLAGRISAalnsdFGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLYRK 152
Cdd:PRK12316 2015 RAP---EAIAVVFGDQHLSYAELDSRANRLAHRLRA-----RGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPN 2086
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 153 HPQEELEYIISDSQSSLLVAGNSFaktLEPLALKLGLPCLTLPPTSNLStldgtDSQEEEAAITDWADRPAMIIYTSGTT 232
Cdd:PRK12316 2087 YPAERLAYMLEDSGAALLLTQRHL---LERLPLPAGVARLPLDRDAEWA-----DYPDTAPAVQLAGENLAYVIYTSGST 2158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 233 GRPKGVLHTHSSIQAMVQCLVSEWAWTRDDVILHTLPLhHVHGIVNKLLCPLWVGATCIMLPEFQ--PQKVWEiLLTSKA 310
Cdd:PRK12316 2159 GLPKGVAVSHGALVAHCQAAGERYELSPADCELQFMSF-SFDGAHEQWFHPLLNGARVLIRDDELwdPEQLYD-EMERHG 2236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 311 PMVNVFMAVptiyskliqYYDQHFTQPHVKDfvkavCKQRIRLMVSGSAALPLPTLQR-WEEITGHTLLERYGMTEigmA 389
Cdd:PRK12316 2237 VTILDFPPV---------YLQQLAEHAERDG-----RPPAVRVYCFGGEAVPAASLRLaWEALRPVYLFNGYGPTE---A 2299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 390 LSNPL---KGPRIPGAVGSPLPGVEIrivmsnatnttiveANHRETRVRSGLE----GKEGELLVRGPSVFKEYWNKHQE 462
Cdd:PRK12316 2300 VVTPLlwkCRPQDPCGAAYVPIGRAL--------------GNRRAYILDADLNllapGMAGELYLGGEGLARGYLNRPGL 2365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 463 TRESF-------TDSGWFKTGDTAIHK-DGVFWIMGRtsVD-IIKSGGYKISALEVERHLLAHPAIADVAVIGpPDAIWG 533
Cdd:PRK12316 2366 TAERFvpdpfsaSGERLYRTGDLARYRaDGVVEYLGR--IDhQVKIRGFRIELGEIEARLQAHPAVREAVVVA-QDGASG 2442
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 2105456023 534 QKVTAVMQLKRGHRLTLPELKIWAREHMAPYIIPTGLVLVEELPRNQMGKVNKKDLLR 591
Cdd:PRK12316 2443 KQLVAYVVPDDAAEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPK 2500
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
79-591 |
2.05e-29 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 122.04 E-value: 2.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 79 DRLAII--DSSGSHSYKQLYCSSFGLAGRISaalnsDFGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLYRKHPQE 156
Cdd:PRK13390 12 DRPAVIvaETGEQVSYRQLDDDSAALARVLY-----DAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 157 ELEYIISDSQSSLLVAgnsfAKTLEPLALKLGLPcltLPPTSNLS-TLDGTDSQEEE--AAITDWADRP--AMIIYTSGT 231
Cdd:PRK13390 87 EADYIVGDSGARVLVA----SAALDGLAAKVGAD---LPLRLSFGgEIDGFGSFEAAlaGAGPRLTEQPcgAVMLYSSGT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 232 TGRPKGV---LHTHSSIQA---MVQCLVSEWAWTRDDVILHTLPLHHVH-----GIVNKLlcplwvGATCIMLPEFQPQk 300
Cdd:PRK13390 160 TGFPKGIqpdLPGRDVDAPgdpIVAIARAFYDISESDIYYSSAPIYHAAplrwcSMVHAL------GGTVVLAKRFDAQ- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 301 vwEILLTSKAPMVNVFMAVPTIYSKLIQYYDQHFTQPHVKDfvkavckqrIRLMVSGSAALPLPTLQRWEEITGHTLLER 380
Cdd:PRK13390 233 --ATLGHVERYRITVTQMVPTMFVRLLKLDADVRTRYDVSS---------LRAVIHAAAPCPVDVKHAMIDWLGPIVYEY 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 381 YGMTEI-GMALSNPLKGPRIPGAVGSPLPGveirivmsnatNTTIVEANHRETRVrsgleGKEGELLVRGPSVFKEYWNK 459
Cdd:PRK13390 302 YSSTEAhGMTFIDSPDWLAHPGSVGRSVLG-----------DLHICDDDGNELPA-----GRIGTVYFERDRLPFRYLND 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 460 HQETRESFTDSG--WFKTGDTA-IHKDGVFWIMGRTSVDIIkSGGYKISALEVERHLLAHPAIADVAVIGPPDAIWGQKV 536
Cdd:PRK13390 366 PEKTAAAQHPAHpfWTTVGDLGsVDEDGYLYLADRKSFMII-SGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQV 444
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 2105456023 537 TAVMQLKRGHRLT---LPELKIWAREHMAPYIIPTGLVLVEELPRNQMGKVnKKDLLR 591
Cdd:PRK13390 445 KAVIQLVEGIRGSdelARELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKL-VKGLLR 501
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
61-589 |
2.60e-29 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 124.30 E-value: 2.60e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 61 PSMRINQKPVFVRAPAFGDRLAIIDSSGSHSYKQLYCSsfglAGRISAALNSDFGGLEgKRISFLCANDASYTVAQWAAW 140
Cdd:PRK12316 4548 PATRCVHQLVAERARMTPDAVAVVFDEEKLTYAELNRR----ANRLAHALIARGVGPE-VLVGIAMERSAEMMVGLLAVL 4622
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 141 MSGGTAVPLYRKHPQEELEYIISDSQSSLLVagnSFAKTLEPLALKLGLPCLTLPPTSnlstlDGTDSQEEEAAITDWAD 220
Cdd:PRK12316 4623 KAGGAYVPLDPEYPRERLAYMMEDSGAALLL---TQSHLLQRLPIPDGLASLALDRDE-----DWEGFPAHDPAVRLHPD 4694
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 221 RPAMIIYTSGTTGRPKGVLHTHSSIQAMVQCLVSEWAWTRDDVILHTLPLhHVHGIVNKLLCPLWVGATCIMLPEFQ--P 298
Cdd:PRK12316 4695 NLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSF-SFDGSHEGLYHPLINGASVVIRDDSLwdP 4773
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 299 QKVWEILLTSKAPMVNvfmAVPTIYSKLIQyydqhftqphvkDFVKAVCKQRIRLMVSGSAALPLPTLQRWEEITGHT-L 377
Cdd:PRK12316 4774 ERLYAEIHEHRVTVLV---FPPVYLQQLAE------------HAERDGEPPSLRVYCFGGEAVAQASYDLAWRALKPVyL 4838
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 378 LERYGMTEIGM-ALSNPLKGPRIPGA----VGSPLPGVEIRiVMSNATNTTIVeanhretrvrsgleGKEGELLVRGPSV 452
Cdd:PRK12316 4839 FNGYGPTETTVtVLLWKARDGDACGAaympIGTPLGNRSGY-VLDGQLNPLPV--------------GVAGELYLGGEGV 4903
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 453 FKEYWNKHQETRESFTDSGW-------FKTGDTAIHK-DGVFWIMGRtsVD-IIKSGGYKISALEVERHLLAHPAIADVA 523
Cdd:PRK12316 4904 ARGYLERPALTAERFVPDPFgapggrlYRTGDLARYRaDGVIDYLGR--VDhQVKIRGFRIELGEIEARLREHPAVREAV 4981
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2105456023 524 VIGPPDAIWGQKV-------TAVMQLKRGHRLTLPELKIWAREHMAPYIIPTGLVLVEELPRNQMGKVNKKDL 589
Cdd:PRK12316 4982 VIAQEGAVGKQLVgyvvpqdPALADADEAQAELRDELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRKAL 5054
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
79-589 |
2.60e-29 |
|
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: 121.22 E-value: 2.60e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 79 DRLAIIDSSGSHSYKQLYCSSFGLAGRISAAlnsdfGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLYRKHPQEEL 158
Cdd:cd12114 2 DATAVICGDGTLTYGELAERARRVAGALKAA-----GVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 159 EYIISDSQSSLLVAgnsfakTLEPLALKLGLPCLTLPPTSNLSTLDgtdsqeEEAAITDWADRPAMIIYTSGTTGRPKGV 238
Cdd:cd12114 77 EAILADAGARLVLT------DGPDAQLDVAVFDVLILDLDALAAPA------PPPPVDVAPDDLAYVIFTSGSTGTPKGV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 239 LHTHSSIQAMVQCLVSEWAWTRDDVILHTLPLHH---VHGIVNkllcPLWVGATCIMLPEFQPQKV--W-EILLTSKAPM 312
Cdd:cd12114 145 MISHRAALNTILDINRRFAVGPDDRVLALSSLSFdlsVYDIFG----ALSAGATLVLPDEARRRDPahWaELIERHGVTL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 313 VNvfmAVPTIYSKLIQYYDQHFTQPHvkdfvkavckqRIRL-MVSG---SAALPLPTLQRWEEITGHTLlerYGMTEiGM 388
Cdd:cd12114 221 WN---SVPALLEMLLDVLEAAQALLP-----------SLRLvLLSGdwiPLDLPARLRALAPDARLISL---GGATE-AS 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 389 ALSNPLKGPRIPGAVGS-----PLPGVEIRIVmsnatnttiveanhrETRVRSGLEGKEGELLVRGPSVFKEYWNKHQET 463
Cdd:cd12114 283 IWSIYHPIDEVPPDWRSipygrPLANQRYRVL---------------DPRGRDCPDWVPGELWIGGRGVALGYLGDPELT 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 464 RESF----TDSGWFKTGDTAIHK-DGVFWIMGRtsVDI-IKSGGYKISALEVERHLLAHPAIADVAVIGPPDAiwGQK-V 536
Cdd:cd12114 348 AARFvthpDGERLYRTGDLGRYRpDGTLEFLGR--RDGqVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDP--GGKrL 423
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 2105456023 537 TAVMQLKRGHRLTLPE-LKIWAREHMAPYIIPTGLVLVEELPRNQMGKVNKKDL 589
Cdd:cd12114 424 AAFVVPDNDGTPIAPDaLRAFLAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
134-591 |
4.72e-29 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 123.73 E-value: 4.72e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 134 VAQWAAWMSGGTAVPLYRKHPQEELEYIISDSQSSLLVAGnsfAKTLEPLALKLGLPCLTLPPTSNLstLDGTDSQEEEA 213
Cdd:PRK12467 1639 VGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQ---SHLQARLPLPDGLRSLVLDQEDDW--LEGYSDSNPAV 1713
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 214 AITDwaDRPAMIIYTSGTTGRPKGVLHTHSSIQAMVqCLVSEW-AWTRDDVILHTLPlHHVHGIVNKLLCPLWVGATCIM 292
Cdd:PRK12467 1714 NLAP--QNLAYVIYTSGSTGRPKGAGNRHGALVNRL-CATQEAyQLSAADVVLQFTS-FAFDVSVWELFWPLINGARLVI 1789
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 293 LPEFQPQKVWEILLTSKAPMVNVFMAVPTIYSKLIQyYDQHFTQPhvkdfvkavckQRIRLMVSGSAALPLPTLQRWEEI 372
Cdd:PRK12467 1790 APPGAHRDPEQLIQLIERQQVTTLHFVPSMLQQLLQ-MDEQVEHP-----------LSLRRVVCGGEALEVEALRPWLER 1857
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 373 TGHT-LLERYGMTEIGMALSN-PLKGPRIPGAVGSPlpgveIRIVMSNATnTTIVEANHRETRVrsgleGKEGELLVRGP 450
Cdd:PRK12467 1858 LPDTgLFNLYGPTETAVDVTHwTCRRKDLEGRDSVP-----IGQPIANLS-TYILDASLNPVPI-----GVAGELYLGGV 1926
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 451 SVFKEYWNKHQETRESF-------TDSGWFKTGDTAIHK-DGVFWIMGRtsVD-IIKSGGYKISALEVERHLLAHPAIAD 521
Cdd:PRK12467 1927 GLARGYLNRPALTAERFvadpfgtVGSRLYRTGDLARYRaDGVIEYLGR--IDhQVKIRGFRIELGEIEARLREQGGVRE 2004
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 522 VAVIgPPDAIWGQKVTAVM-------------------QLKRGHRLTLPElkiwarehmapYIIPTGLVLVEELPRNQMG 582
Cdd:PRK12467 2005 AVVI-AQDGANGKQLVAYVvptdpglvdddeaqvalraILKNHLKASLPE-----------YMVPAHLVFLARMPLTPNG 2072
|
....*....
gi 2105456023 583 KVNKKDLLR 591
Cdd:PRK12467 2073 KLDRKALPA 2081
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
138-589 |
5.21e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 120.94 E-value: 5.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 138 AAWMSGGTAVPLYRKHPQEELEYIISDSQSSLLVAGNSFAKTLEPLalKLGLPCL---TLPPTSNLSTLDGTdsqeEEAA 214
Cdd:PRK07867 73 AAALSGIVPVGLNPTRRGAALARDIAHADCQLVLTESAHAELLDGL--DPGVRVInvdSPAWADELAAHRDA----EPPF 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 215 ITDWADRPAMIIYTSGTTGRPKGVLHTHSSIQAMVQCLVSEWAWTRDDVILHTLPLHHVHGIVNKLLCPLWVGATCIMLP 294
Cdd:PRK07867 147 RVADPDDLFMLIFTSGTSGDPKAVRCTHRKVASAGVMLAQRFGLGPDDVCYVSMPLFHSNAVMAGWAVALAAGASIALRR 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 295 EFQPQKVweilltskAPMVNVFMAVPTIY-SKLIQYYDQHFTQPHVKDfvkavckQRIRLMVsGSAALPlPTLQRWEEIT 373
Cdd:PRK07867 227 KFSASGF--------LPDVRRYGATYANYvGKPLSYVLATPERPDDAD-------NPLRIVY-GNEGAP-GDIARFARRF 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 374 GHTLLERYGMTEIGMALSNPLKGPriPGAVGSPLPGVEIRIVmsnATNTTIVEANHRETRVRSGLEGKeGELL-VRGPSV 452
Cdd:PRK07867 290 GCVVVDGFGSTEGGVAITRTPDTP--PGALGPLPPGVAIVDP---DTGTECPPAEDADGRLLNADEAI-GELVnTAGPGG 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 453 FKEYWNKHQETRESFTDsGWFKTGDTAIH-KDGVFWIMGRTSvDIIKSGGYKISALEVERHLLAHPAIADVAVIGPPDAI 531
Cdd:PRK07867 364 FEGYYNDPEADAERMRG-GVYWSGDLAYRdADGYAYFAGRLG-DWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPV 441
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 532 WGQKVTAVMQLKRGHRLTLPELK--IWAREHMAPYIIPTGLVLVEELPRNQMGKVNKKDL 589
Cdd:PRK07867 442 VGDQVMAALVLAPGAKFDPDAFAefLAAQPDLGPKQWPSYVRVCAELPRTATFKVLKRQL 501
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
220-584 |
8.17e-29 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 121.68 E-value: 8.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 220 DRPAMIIYTSGTTGRPKGVLHTHSSIQAMVQCLVSE-WAWTRDDVILHTLPLHHVHGIVNKLLCPLWVGATCIMLPEFQP 298
Cdd:PRK06060 145 DALAYATYTSGTTGPPKAAIHRHADPLTFVDAMCRKaLRLTPEDTGLCSARMYFAYGLGNSVWFPLATGGSAVINSAPVT 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 299 QKVWEILLTSKAPmvNVFMAVPTIYSKLIqyydqhftqphvkDFVKAVCKQRIRLMVSGSAALPLPTLQRWEEITGHT-L 377
Cdd:PRK06060 225 PEAAAILSARFGP--SVLYGVPNFFARVI-------------DSCSPDSFRSLRCVVSAGEALELGLAERLMEFFGGIpI 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 378 LERYGMTEIGMA-LSNPLKGPRiPGAVGSPLPGVEIRIVMSNATnttiveanhretrvrSGLEGKEGELLVRGPSVFKEY 456
Cdd:PRK06060 290 LDGIGSTEVGQTfVSNRVDEWR-LGTLGRVLPPYEIRVVAPDGT---------------TAGPGVEGDLWVRGPAIAKGY 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 457 WNKHQETresFTDSGWFKTGD-TAIHKDGvfWIM-GRTSVDIIKSGGYKISALEVERHLLAHPAIADVAVIGPPDAIWGQ 534
Cdd:PRK06060 354 WNRPDSP---VANEGWLDTRDrVCIDSDG--WVTyRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGAS 428
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2105456023 535 KVTAVM-----------QLKRGHRLTLPELkiwarehmAPYIIPTGLVLVEELPRNQMGKV 584
Cdd:PRK06060 429 TLQAFLvatsgatidgsVMRDLHRGLLNRL--------SAFKVPHRFAVVDRLPRTPNGKL 481
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
130-589 |
1.03e-28 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 122.76 E-value: 1.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 130 ASYTVAQWAAWMSGGTAVPLYRKHPQEELEYIISDSQSSLLVAGNSFAKTLePLALKLGLPCLTLPPtsnlSTLDGTDSQ 209
Cdd:PRK12316 572 IEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQSHLGRKL-PLAAGVQVLDLDRPA----AWLEGYSEE 646
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 210 EEEAAITdwADRPAMIIYTSGTTGRPKGVLHTHSSIQAMVQCLVSEWAWTRDDVILHTLPLHHVHGiVNKLLCPLWVGAT 289
Cdd:PRK12316 647 NPGTELN--PENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVS-VWEFFWPLMSGAR 723
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 290 CIMLPE---FQPQKVWEillTSKAPMVNVFMAVPTIYSKLIQYYDQhftqphvkdfvkAVCKQrIRLMVSGSAALPLPTL 366
Cdd:PRK12316 724 LVVAAPgdhRDPAKLVE---LINREGVDTLHFVPSMLQAFLQDEDV------------ASCTS-LRRIVCSGEALPADAQ 787
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 367 QRWEEITGHT-LLERYGMTE--IGMALSNPLK--GPRIPgaVGSPLPGveirivmsnaTNTTIVEANHRETRVrsgleGK 441
Cdd:PRK12316 788 EQVFAKLPQAgLYNLYGPTEaaIDVTHWTCVEegGDSVP--IGRPIAN----------LACYILDANLEPVPV-----GV 850
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 442 EGELLVRGPSVFKEYWNKHQETRESFTDSGW------FKTGDTAIHK-DGVFWIMGRTSvDIIKSGGYKISALEVERHLL 514
Cdd:PRK12316 851 LGELYLAGRGLARGYHGRPGLTAERFVPSPFvagermYRTGDLARYRaDGVIEYAGRID-HQVKLRGLRIELGEIEARLL 929
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2105456023 515 AHPAIADVAVIgppdAIWGQKVTAVMQLKRGHRLTLPELKIWAREHMAPYIIPTGLVLVEELPRNQMGKVNKKDL 589
Cdd:PRK12316 930 EHPWVREAAVL----AVDGKQLVGYVVLESEGGDWREALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKAL 1000
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
219-584 |
1.13e-28 |
|
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.
Pssm-ID: 341271 [Multi-domain] Cd Length: 617 Bit Score: 120.88 E-value: 1.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 219 ADRPAMIIYTSGTTGRPKGVLHT--------HSSIQAMVQCLVSEWAWTRDD---VILHTLPlhhVHGivnkllcPLWVG 287
Cdd:cd05967 229 ATDPLYILYTSGTTGKPKGVVRDngghavalNWSMRNIYGIKPGDVWWAASDvgwVVGHSYI---VYG-------PLLHG 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 288 ATCIMLpEFQPQKV------WEILLTSKapmVNVFMAVPTIYsKLIQYYDQHftqphvKDFVKAVCKQRIRLMVSGSAAL 361
Cdd:cd05967 299 ATTVLY-EGKPVGTpdpgafWRVIEKYQ---VNALFTAPTAI-RAIRKEDPD------GKYIKKYDLSSLRTLFLAGERL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 362 PLPTLQRWEEITGHTLLERYGMTEIGMALSNPLKG----PRIPGAVGSPLPGVEIRIVmsNATNTtIVEANhretrvrsg 437
Cdd:cd05967 368 DPPTLEWAENTLGVPVIDHWWQTETGWPITANPVGleplPIKAGSPGKPVPGYQVQVL--DEDGE-PVGPN--------- 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 438 legKEGELLVRGP---SVFKEYWNKHQETRESF--TDSGWFKTGDTAIH-KDGVFWIMGRTSvDIIKSGGYKISALEVER 511
Cdd:cd05967 436 ---ELGNIVIKLPlppGCLLTLWKNDERFKKLYlsKFPGYYDTGDAGYKdEDGYLFIMGRTD-DVINVAGHRLSTGEMEE 511
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2105456023 512 HLLAHPAIADVAVIGPPDAIWGQKVTAVMQLKRGHRLTLPEL--KIWA--REHMAPYIIPTGLVLVEELPRNQMGKV 584
Cdd:cd05967 512 SVLSHPAVAECAVVGVRDELKGQVPLGLVVLKEGVKITAEELekELVAlvREQIGPVAAFRLVIFVKRLPKTRSGKI 588
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
134-591 |
1.27e-28 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 122.37 E-value: 1.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 134 VAQWAAWMSGGTAVPLYRKHPQEELEYIISDSQSSLLvagnsfaktleplalkLGLPCLTLPPTSNLSTL----DGTDSQ 209
Cdd:PRK12316 3122 VGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLL----------------LSQSHLRLPLAQGVQVLdldrGDENYA 3185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 210 EEEAAITDWADRPAMIIYTSGTTGRPKGVLHTHSSIQAMVQCLVSEWAWTRDDVILHTLPLhHVHGIVNKLLCPLWVGAT 289
Cdd:PRK12316 3186 EANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTF-SFDVFVEELFWPLMSGAR 3264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 290 CIMLPEFQPQKVWEILLTSKAPMVNVFMAVPTIYSKLIQYYDQHFTQPhvkdfvkavckqrIRLMVSGSAALPLPTLQRW 369
Cdd:PRK12316 3265 VVLAGPEDWRDPALLVELINSEGVDVLHAYPSMLQAFLEEEDAHRCTS-------------LKRIVCGGEALPADLQQQV 3331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 370 eeITGHTLLERYGMTEIGMALSNPLKGPRIPGA--VGSPLPGVEIRIVMSNATNTTIveanhretrvrsgleGKEGELLV 447
Cdd:PRK12316 3332 --FAGLPLYNLYGPTEATITVTHWQCVEEGKDAvpIGRPIANRACYILDGSLEPVPV---------------GALGELYL 3394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 448 RGPSVFKEYWNKHQETRESFTDSGW------FKTGDTAIHK-DGVFWIMGRTSVDiIKSGGYKISALEVERHLLAHPAIA 520
Cdd:PRK12316 3395 GGEGLARGYHNRPGLTAERFVPDPFvpgerlYRTGDLARYRaDGVIEYIGRVDHQ-VKIRGFRIELGEIEARLLEHPWVR 3473
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2105456023 521 DVAVIgppdAIWGQKVTAVMQLKRGHRLTLPELKIWAREHMAPYIIPTGLVLVEELPRNQMGKVNKKDLLR 591
Cdd:PRK12316 3474 EAVVL----AVDGRQLVAYVVPEDEAGDLREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPR 3540
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
73-591 |
1.76e-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: 118.18 E-value: 1.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 73 RAPAFGDRLAIIDSSGSHSYKQLYCSSFGLAGRISaalnsDFGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLYRK 152
Cdd:cd17653 6 IAAAHPDAVAVESLGGSLTYGELDAASNALANRLL-----QLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 153 HPQEELEYIISDSQSSLLVAGNSfaktleplalklglpcltlpptsnlstldgtdsqeeeaaitdwADRPAMIIYTSGTT 232
Cdd:cd17653 81 LPSARIQAILRTSGATLLLTTDS-------------------------------------------PDDLAYIIFTSGST 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 233 GRPKGVLHTHSSIQAMVQclvsewaWTRDDviLHTLP---LHHVHGI-----VNKLLCPLWVGATCIMLPEFQPqkvwei 304
Cdd:cd17653 118 GIPKGVMVPHRGVLNYVS-------QPPAR--LDVGPgsrVAQVLSIafdacIGEIFSTLCNGGTLVLADPSDP------ 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 305 lLTSKAPMVNVFMAVPTIYSKLiqyydqhftqpHVKDFvkavckQRIRLMVSGSAALPLPTLQRWEEitGHTLLERYGMT 384
Cdd:cd17653 183 -FAHVARTVDALMSTPSILSTL-----------SPQDF------PNLKTIFLGGEAVPPSLLDRWSP--GRRLYNAYGPT 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 385 EIGMALSNPLKGPRIPGAVGSPLPGVEIRIVmsnatnttivEANHRETrvrsgLEGKEGELLVRGPSVFKEYWNKHQETR 464
Cdd:cd17653 243 ECTISSTMTELLPGQPVTIGKPIPNSTCYIL----------DADLQPV-----PEGVVGEICISGVQVARGYLGNPALTA 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 465 ESFT-DSGW-----FKTGDTA-IHKDGVFWIMGRTSVDIiKSGGYKISALEVERHLLAHPAIAdvavigppdaiwgQKVT 537
Cdd:cd17653 308 SKFVpDPFWpgsrmYRTGDYGrWTEDGGLEFLGREDNQV-KVRGFRINLEEIEEVVLQSQPEV-------------TQAA 373
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2105456023 538 AVMqlkrgHRLTL-----PE------LKIWAREHMAPYIIPTGLVLVEELPRNQMGKVNKKDLLR 591
Cdd:cd17653 374 AIV-----VNGRLvafvtPEtvdvdgLRSELAKHLPSYAVPDRIIALDSFPLTANGKVDRKALRE 433
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
79-589 |
1.95e-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: 118.34 E-value: 1.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 79 DRLAIIDSSGSHSYKQLYCSSFGLAgRISAALNSDFGGLEGkrisfLCANDASYT-VAQWAAWMSGGTAVPLYRKHPQEE 157
Cdd:cd17650 2 DAIAVSDATRQLTYRELNERANQLA-RTLRGLGVAPGSVVG-----VCADRSLDAiVGLLAVLKAGGAYVPIDPDYPAER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 158 LEYIISDSQSSLLvagnsfaktleplalklglpcLTLPptsnlstldgtdsqeeeaaitdwaDRPAMIIYTSGTTGRPKG 237
Cdd:cd17650 76 LQYMLEDSGAKLL---------------------LTQP------------------------EDLAYVIYTSGTTGKPKG 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 238 VLHTHSSIQAMVQCLVSEWAWTRDDVILHTLPLHHVHGIVNKLLCPLWVGATCIMLPE---FQPQKVWEILLTSKApmvN 314
Cdd:cd17650 111 VMVEHRNVAHAAHAWRREYELDSFPVRLLQMASFSFDVFAGDFARSLLNGGTLVICPDevkLDPAALYDLILKSRI---T 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 315 VFMAVPTIYSKLIQYYDQHFTQPhvkdfvkavckQRIRLMVSGSAALPLptlqRW-----EEITGHT-LLERYGMTE--I 386
Cdd:cd17650 188 LMESTPALIRPVMAYVYRNGLDL-----------SAMRLLIVGSDGCKA----QDfktlaARFGQGMrIINSYGVTEatI 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 387 GMALSNPLKGPRIPGA---VGSPLPGVEIRIVmsnatnttiveanhrETRVRSGLEGKEGELLVRGPSVFKEYWNKHQET 463
Cdd:cd17650 253 DSTYYEEGRDPLGDSAnvpIGRPLPNTAMYVL---------------DERLQPQPVGVAGELYIGGAGVARGYLNRPELT 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 464 RESFTDSGW------FKTGDTAIHK-DGVFWIMGRTSvDIIKSGGYKISALEVERHLLAHPAIADVAVIGPPDAiwGQKV 536
Cdd:cd17650 318 AERFVENPFapgermYRTGDLARWRaDGNVELLGRVD-HQVKIRGFRIELGEIESQLARHPAIDEAVVAVREDK--GGEA 394
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 2105456023 537 TAVMQLKRGHRLTLPELKIWAREHMAPYIIPTGLVLVEELPRNQMGKVNKKDL 589
Cdd:cd17650 395 RLCAYVVAAATLNTAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
79-589 |
2.21e-28 |
|
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: 118.19 E-value: 2.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 79 DRLAIIDSSGSHSYKQLYCSSFGLAGRISAAlnsdfGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLYRKHPQEEL 158
Cdd:cd12115 14 DAIALVCGDESLTYAELNRRANRLAARLRAA-----GVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPERL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 159 EYIISDSQSSLLvagnsfaktleplalklglpcltlpptsnlstldgtdsqeeeaaITDwADRPAMIIYTSGTTGRPKGV 238
Cdd:cd12115 89 RFILEDAQARLV--------------------------------------------LTD-PDDLAYVIYTSGSTGRPKGV 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 239 LHTHSSIQAMVQclvseWAwtrddviLHTLPLHHVHGI-----------VNKLLCPLWVGATCIMLpefqpQKVWEILLT 307
Cdd:cd12115 124 AIEHRNAAAFLQ-----WA-------AAAFSAEELAGVlastsicfdlsVFELFGPLATGGKVVLA-----DNVLALPDL 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 308 SKAPMVNVFMAVPTIYSKLIQyydqhftqphVKDFVKAVckQRIRLmvsgsAALPLPTlQRWEEITGHTLLER----YGM 383
Cdd:cd12115 187 PAAAEVTLINTVPSAAAELLR----------HDALPASV--RVVNL-----AGEPLPR-DLVQRLYARLQVERvvnlYGP 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 384 TE-----IGMALSnplKGPRIPGAVGSPLPGveirivmsnaTNTTIVEANHRETRVrsgleGKEGELLVRGPSVFKEYWN 458
Cdd:cd12115 249 SEdttysTVAPVP---PGASGEVSIGRPLAN----------TQAYVLDRALQPVPL-----GVPGELYIGGAGVARGYLG 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 459 KHQETRESF------TDSGWFKTGDTAIHK-DGVFWIMGRTSvDIIKSGGYKISALEVERHLLAHPAIADVAVIGPPDAI 531
Cdd:cd12115 311 RPGLTAERFlpdpfgPGARLYRTGDLVRWRpDGLLEFLGRAD-NQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAA 389
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 2105456023 532 WGQKVTAVMQLKRGHRLTLPELKIWAREHMAPYIIPTGLVLVEELPRNQMGKVNKKDL 589
Cdd:cd12115 390 GERRLVAYIVAEPGAAGLVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
222-589 |
2.32e-28 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 119.74 E-value: 2.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 222 PAMIIYTSGTTGRPKGVLHTHSSIQAMVQCLVSEWAWTRDDVILHTLPLHHVHGIVNKLLCPLWVGATCIMLPEFQPQKV 301
Cdd:PLN03102 188 PISLNYTSGTTADPKGVVISHRGAYLSTLSAIIGWEMGTCPVYLWTLPMFHCNGWTFTWGTAARGGTSVCMRHVTAPEIY 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 302 WEILLTSKAPMVnvfmAVPTIYSKLIQ--YYDQHFTQPHVKdfvkavckqrirlMVSGSAALPLPTLQRWEEItGHTLLE 379
Cdd:PLN03102 268 KNIEMHNVTHMC----CVPTVFNILLKgnSLDLSPRSGPVH-------------VLTGGSPPPAALVKKVQRL-GFQVMH 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 380 RYGMTEIgmalsnplKGP-----------RIPGAVGSPLpgvEIRIVMSNATnTTIVEANHRETRVRSGLEGKE-GELLV 447
Cdd:PLN03102 330 AYGLTEA--------TGPvlfcewqdewnRLPENQQMEL---KARQGVSILG-LADVDVKNKETQESVPRDGKTmGEIVI 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 448 RGPSVFKEYWNKHQETRESFTdSGWFKTGDTA-IHKDGVFWIMGRtSVDIIKSGGYKISALEVERHLLAHPAIADVAVIG 526
Cdd:PLN03102 398 KGSSIMKGYLKNPKATSEAFK-HGWLNTGDVGvIHPDGHVEIKDR-SKDIIISGGENISSVEVENVLYKYPKVLETAVVA 475
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2105456023 527 PPDAIWGQKVTAVMQLKRGH--------RLTLPE--LKIWAREHMAPYIIPTGLVLVEELPRNQMGKVNKKDL 589
Cdd:PLN03102 476 MPHPTWGETPCAFVVLEKGEttkedrvdKLVTRErdLIEYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKL 548
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
69-591 |
2.66e-28 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 119.31 E-value: 2.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 69 PVFV--RAPAFGDRLAIIDSSGSHSYKqlYCSSFGLAGRISAALNSdFGGLEGKRISFLCANDASYTVAQWAAWMSGGTA 146
Cdd:PLN02330 31 PDFVlqDAELYADKVAFVEAVTGKAVT--YGEVVRDTRRFAKALRS-LGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVF 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 147 VPLYRKHPQEELEYIISDSQSSLLVAGNSFAKTLEplalKLGLPCLTLPPTSNLSTLDGTD-----------SQEEEAAI 215
Cdd:PLN02330 108 SGANPTALESEIKKQAEAAGAKLIVTNDTNYGKVK----GLGLPVIVLGEEKIEGAVNWKElleaadragdtSDNEEILQ 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 216 TDWADRPamiiYTSGTTGRPKGVLHTHSSiqaMVQCLVSEWAWTRDDVI-----LHTLPLHHVHGIVNKLLCPLWVGATC 290
Cdd:PLN02330 184 TDLCALP----FSSGTTGISKGVMLTHRN---LVANLCSSLFSVGPEMIgqvvtLGLIPFFHIYGITGICCATLRNKGKV 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 291 IMLPEFQPQKVWEILLT---SKAPMVnvfmavPTIYSKLIQyydqhftQPHVKDFvkAVCKQRIRLMVSGSAALPLPTLQ 367
Cdd:PLN02330 257 VVMSRFELRTFLNALITqevSFAPIV------PPIILNLVK-------NPIVEEF--DLSKLKLQAIMTAAAPLAPELLT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 368 RWE-EITGHTLLERYGMTE---IGMALSNPLKGPRIP--GAVGSPLPGVEIRIVMSNATnttiveanhretrvRSGLEGK 441
Cdd:PLN02330 322 AFEaKFPGVQVQEAYGLTEhscITLTHGDPEKGHGIAkkNSVGFILPNLEVKFIDPDTG--------------RSLPKNT 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 442 EGELLVRGPSVFKEYWNKHQETRESFTDSGWFKTGDTA-IHKDGVFWIMGRTSvDIIKSGGYKISALEVERHLLAHPAIA 520
Cdd:PLN02330 388 PGELCVRSQCVMQGYYNNKEETDRTIDEDGWLHTGDIGyIDDDGDIFIVDRIK-ELIKYKGFQVAPAELEAILLTHPSVE 466
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2105456023 521 DVAVIGPPDAIWGQKVTAVMQLKRGHRLTLPELKIWAREHMAPYIIPTGLVLVEELPRNQMGKVNKKdLLR 591
Cdd:PLN02330 467 DAAVVPLPDEEAGEIPAACVVINPKAKESEEDILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRR-LLK 536
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
227-591 |
4.98e-27 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 115.33 E-value: 4.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 227 YTSGTTGRPKGVLHTHSSiqAMVQCLVSEWAWTRDD--VILHTLPLHHVHGivnklLCPLWVGA----TCIMLPEFQPQK 300
Cdd:PLN02479 202 YTSGTTASPKGVVLHHRG--AYLMALSNALIWGMNEgaVYLWTLPMFHCNG-----WCFTWTLAalcgTNICLRQVTAKA 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 301 VWEILLTSKapmVNVFMAVPTIYSKLIQY--YDQHFTQPHVkdfvkavckqrIRLMVSGSAalPLPTLQRWEEITGHTLL 378
Cdd:PLN02479 275 IYSAIANYG---VTHFCAAPVVLNTIVNApkSETILPLPRV-----------VHVMTAGAA--PPPSVLFAMSEKGFRVT 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 379 ERYGMTEIGMALS-----------NPLKGPRIPGAVGSPLPGVEIRIVMSNATNTTIVEanhretrvrsglEGKE-GELL 446
Cdd:PLN02479 339 HTYGLSETYGPSTvcawkpewdslPPEEQARLNARQGVRYIGLEGLDVVDTKTMKPVPA------------DGKTmGEIV 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 447 VRGPSVFKEYWNKHQETRESFTDsGWFKTGDTAI-HKDGVFWIMGRtSVDIIKSGGYKISALEVERHLLAHPAIADVAVI 525
Cdd:PLN02479 407 MRGNMVMKGYLKNPKANEEAFAN-GWFHSGDLGVkHPDGYIEIKDR-SKDIIISGGENISSLEVENVVYTHPAVLEASVV 484
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2105456023 526 GPPDAIWGQKVTAVMQLKRG-----HRLTLPELKIWAREHMAPYIIPTGLVLvEELPRNQMGKVnKKDLLR 591
Cdd:PLN02479 485 ARPDERWGESPCAFVTLKPGvdksdEAALAEDIMKFCRERLPAYWVPKSVVF-GPLPKTATGKI-QKHVLR 553
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
219-591 |
9.98e-27 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 114.85 E-value: 9.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 219 ADRPAMIIYTSGTTGRPKGVLHThsSIQAMVQCLVS-EWA---------WTRDDV--IL-HTlplHHVHGivnkllcPLW 285
Cdd:PRK00174 244 AEDPLFILYTSGSTGKPKGVLHT--TGGYLVYAAMTmKYVfdykdgdvyWCTADVgwVTgHS---YIVYG-------PLA 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 286 VGATCIML---PEF-QPQKVWEILLTSKapmVNVFMAVPTIYSKLIQYYDQHftqphvkdfVKAVCKQRIRLMvsGSAAL 361
Cdd:PRK00174 312 NGATTLMFegvPNYpDPGRFWEVIDKHK---VTIFYTAPTAIRALMKEGDEH---------PKKYDLSSLRLL--GSVGE 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 362 PL-PTLQRW-EEITGHtllER------YGMTEIGMALSNPLKG--PRIPGAVGSPLPGVEIRIVMSNATnttIVEAnhre 431
Cdd:PRK00174 378 PInPEAWEWyYKVVGG---ERcpivdtWWQTETGGIMITPLPGatPLKPGSATRPLPGIQPAVVDEEGN---PLEG---- 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 432 trvrsgleGKEGELLVRG--PSVFKEYWNKHQETRESF--TDSGWFKTGDTAIH-KDGVFWIMGRTSvDIIKSGGYKISA 506
Cdd:PRK00174 448 --------GEGGNLVIKDpwPGMMRTIYGDHERFVKTYfsTFKGMYFTGDGARRdEDGYYWITGRVD-DVLNVSGHRLGT 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 507 LEVERHLLAHPAIADVAVIGPPDAIWGQKVTAVMQLKRGHRLTLP---ELKIWAREHMAPYIIPTGLVLVEELPRNQMGK 583
Cdd:PRK00174 519 AEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLKGGEEPSDElrkELRNWVRKEIGPIAKPDVIQFAPGLPKTRSGK 598
|
....*...
gi 2105456023 584 VNKKdLLR 591
Cdd:PRK00174 599 IMRR-ILR 605
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
79-589 |
5.48e-26 |
|
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: 111.41 E-value: 5.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 79 DRLAIIDSSGSHSYKQLYCSSFGLAGRISAAlnsdfgGLEGKRISFLCAN-DASYTVAQWAAWMSGGTAVPLYRKHPQEE 157
Cdd:cd17656 3 DAVAVVFENQKLTYRELNERSNQLARFLREK------GVKKDSIVAIMMErSAEMIVGILGILKAGGAFVPIDPEYPEER 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 158 LEYIISDSQSSLLVAGNSfaktleplalklglpcLTLPPTSNLSTL---DGTDSQEEEAAIT--DWADRPAMIIYTSGTT 232
Cdd:cd17656 77 RIYIMLDSGVRVVLTQRH----------------LKSKLSFNKSTIlleDPSISQEDTSNIDyiNNSDDLLYIIYTSGTT 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 233 GRPKGVLHTHSSiqaMVQCLVSEWAWTR----DDVILHTLPLHHV--HGIVNKLLcplwVGATCIMLPEFQPQKVWEIL- 305
Cdd:cd17656 141 GKPKGVQLEHKN---MVNLLHFEREKTNinfsDKVLQFATCSFDVcyQEIFSTLL----SGGTLYIIREETKRDVEQLFd 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 306 LTSKAPMVNVFMavPTIYSKLIQYYDQHFtqPHVKDFVKAVCKQRIRLMVSGsaalplpTLQRWEEITGHTLLERYGMTE 385
Cdd:cd17656 214 LVKRHNIEVVFL--PVAFLKFIFSEREFI--NRFPTCVKHIITAGEQLVITN-------EFKEMLHEHNVHLHNHYGPSE 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 386 ---IGMALSNPlkGPRIP--GAVGSPLPGVEIRIVMSNATNTTIveanhretrvrsgleGKEGELLVRGPSVFKEYWNKH 460
Cdd:cd17656 283 thvVTTYTINP--EAEIPelPPIGKPISNTWIYILDQEQQLQPQ---------------GIVGELYISGASVARGYLNRQ 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 461 QETRESF------TDSGWFKTGDTAIH-KDGVFWIMGRTSvDIIKSGGYKISALEVERHLLAHPAIADVAVIGPPDAIWG 533
Cdd:cd17656 346 ELTAEKFfpdpfdPNERMYRTGDLARYlPDGNIEFLGRAD-HQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGE 424
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 2105456023 534 QKVTA--VMQLKrghrLTLPELKIWAREHMAPYIIPTGLVLVEELPRNQMGKVNKKDL 589
Cdd:cd17656 425 KYLCAyfVMEQE----LNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
138-589 |
2.75e-25 |
|
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: 109.06 E-value: 2.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 138 AAWMSGGTAVPLYRKHPQEELEYIISDSQSSLLvagnsfaktleplalklglpcLTLPptSNLstldgtdsqeeeaaitd 217
Cdd:cd17644 69 AILKAGGAYVPLDPNYPQERLTYILEDAQISVL---------------------LTQP--ENL----------------- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 218 wadrpAMIIYTSGTTGRPKGVLHTHSSIQAMVQCLVSEWAWTRDDVILHTLPLhHVHGIVNKLLCPLWVGATCIMLPE-- 295
Cdd:cd17644 109 -----AYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEYGITSSDRVLQFASI-AFDVAAEEIYVTLLSGATLVLRPEem 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 296 -FQPQKVWEILLTSKAPMVNvfmaVPTIYSKLIqyydqhftqphVKDFVKAVCK--QRIRLMVSGSAALPLPTLQRWEEI 372
Cdd:cd17644 183 rSSLEDFVQYIQQWQLTVLS----LPPAYWHLL-----------VLELLLSTIDlpSSLRLVIVGGEAVQPELVRQWQKN 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 373 TGH--TLLERYGMTEIGMA-----LSNPLKGPRIPGAVGSPLPGVEIRIVMSNATNTTIveanhretrvrsgleGKEGEL 445
Cdd:cd17644 248 VGNfiQLINVYGPTEATIAatvcrLTQLTERNITSVPIGRPIANTQVYILDENLQPVPV---------------GVPGEL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 446 LVRGPSVFKEYWNKHQETRESF--------TDSGWFKTGDTAIH-KDGVFWIMGRTSvDIIKSGGYKISALEVERHLLAH 516
Cdd:cd17644 313 HIGGVGLARGYLNRPELTAEKFishpfnssESERLYKTGDLARYlPDGNIEYLGRID-NQVKIRGFRIELGEIEAVLSQH 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2105456023 517 PAIADVAVIGPPDAIWGQKVTAVMQLKRGHRLTLPELKIWAREHMAPYIIPTGLVLVEELPRNQMGKVNKKDL 589
Cdd:cd17644 392 NDVKTAVVIVREDQPGNKRLVAYIVPHYEESPSTVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
226-589 |
2.81e-25 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 108.93 E-value: 2.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 226 IYTSGTTGRPKGVLHTHSSIQAMVQCLVSEWAWTRddviLHT---LPLHHVHGIVnKLLCPLWVGATCIMLP--EFQPQK 300
Cdd:PRK07445 126 IPTGGSSGQIRFAIHTWETLTASVQGFQRYFQLQQ----VNSfcvLPLYHVSGLM-QFMRSFLTGGKLVILPykRLKSGQ 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 301 VWEILLTskapmvNVFMA-VPTiysKLiqyydQHFTQPHVKDFvkavckQRIRLMVSGSAalplPTlqrWEEitghtLLE 379
Cdd:PRK07445 201 ELPPNPS------DFFLSlVPT---QL-----QRLLQLRPQWL------AQFRTILLGGA----PA---WPS-----LLE 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 380 R-----------YGMTEIG--MALSNP---LKGPRipgAVGSPLPGVEIRIVmSNATNTTIVEAnhretrvrsglegkeg 443
Cdd:PRK07445 249 QarqlqlrlaptYGMTETAsqIATLKPddfLAGNN---SSGQVLPHAQITIP-ANQTGNITIQA---------------- 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 444 ellvrgPSVFKEYWNKHQETRESFT--DSGWFKtgdtaihKDGVFWIMGRTSVDIIkSGGYKISALEVERHLLAHPAIAD 521
Cdd:PRK07445 309 ------QSLALGYYPQILDSQGIFEtdDLGYLD-------AQGYLHILGRNSQKII-TGGENVYPAEVEAAILATGLVQD 374
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2105456023 522 VAVIGPPDAIWGQKVTAVMQLKRGhRLTLPELKIWAREHMAPYIIPTGLVLVEELPRNQMGKVNKKDL 589
Cdd:PRK07445 375 VCVLGLPDPHWGEVVTAIYVPKDP-SISLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQL 441
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
45-589 |
3.72e-25 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 111.41 E-value: 3.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 45 LLGTVIHRRAHGWTSAPSMRINQ---KPVFVRAPAFGDRLAIIDSSGSHSYKQLYCSSFGLAGRISaalnsDFGGLEGKR 121
Cdd:PRK05691 1109 LLDAAERAQLAQWGQAPCAPAQAwlpELLNEQARQTPERIALVWDGGSLDYAELHAQANRLAHYLR-----DKGVGPDVC 1183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 122 ISFLCANDASYTVAQWAAWMSGGTAVPLYRKHPQEELEYIISDSQSSLLVAGNSFAKTLEPLALKLGLPCLTLpptsnls 201
Cdd:PRK05691 1184 VAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELLLTQSHLLERLPQAEGVSAIALDSL------- 1256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 202 TLDGTDSQEEEAAITDwaDRPAMIIYTSGTTGRPKGVLHTHSSIQAMVQCLVSEWAWTRDDVILHTLPLHHvhgIVNKLL 281
Cdd:PRK05691 1257 HLDSWPSQAPGLHLHG--DNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKAPISF---DVSVWE 1331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 282 C--PLWVGATCIMLPEFQ---PQKVweilltskAPMVNVFmAVPTIyskliqyydqHFTQPHVKDFVK----AVCkQRIR 352
Cdd:PRK05691 1332 CfwPLITGCRLVLAGPGEhrdPQRI--------AELVQQY-GVTTL----------HFVPPLLQLFIDeplaAAC-TSLR 1391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 353 LMVSGSAALPLPTLQR-WEEITGHTLLERYGMTEIGMALSN----PLKGPRIPgaVGSPLPGVEIRIVMSNATNTTivea 427
Cdd:PRK05691 1392 RLFSGGEALPAELRNRvLQRLPQVQLHNRYGPTETAINVTHwqcqAEDGERSP--IGRPLGNVLCRVLDAELNLLP---- 1465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 428 nhretrvrsglEGKEGELLVRGPSVFKEYWNKHQETRESFT-----DSG--WFKTGDTAI-HKDGVFWIMGRTSVDiIKS 499
Cdd:PRK05691 1466 -----------PGVAGELCIGGAGLARGYLGRPALTAERFVpdplgEDGarLYRTGDRARwNADGALEYLGRLDQQ-VKL 1533
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 500 GGYKISALEVERHLLAHPAIADVAVIGPPDAIwGQKVTAVMQLKRGHRLTLPELKIWAREHMAPYIIPTGLVLVEELPRN 579
Cdd:PRK05691 1534 RGFRVEPEEIQARLLAQPGVAQAAVLVREGAA-GAQLVGYYTGEAGQEAEAERLKAALAAELPEYMVPAQLIRLDQMPLG 1612
|
570
....*....|
gi 2105456023 580 QMGKVNKKDL 589
Cdd:PRK05691 1613 PSGKLDRRAL 1622
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
134-589 |
1.07e-24 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 109.87 E-value: 1.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 134 VAQWAAWMSGGTAVPLYRKHPQEELEYIISDSQSSLLVagnSFAKTLEPLALKLGLPCLTLpptsNLSTLDGtDSQEEEA 213
Cdd:PRK12467 3160 VALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLL---TQAHLLEQLPAPAGDTALTL----DRLDLNG-YSENNPS 3231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 214 AITDwADRPAMIIYTSGTTGRPKGVLHTHSSIQAMVQCLVSEWAWTRDDVILHTLPLhHVHGIVNKLLCPLWVGATCIML 293
Cdd:PRK12467 3232 TRVM-GENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDRVLLFMSF-SFDGAQERFLWTLICGGCLVVR 3309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 294 P--EFQPQKVWEILLtskAPMVNVFMAVPTiyskliqyYDQHFTQPH-VKDFvkavckQRIRLMVSGSAALPLPTLQRWE 370
Cdd:PRK12467 3310 DndLWDPEELWQAIH---AHRISIACFPPA--------YLQQFAEDAgGADC------ASLDIYVFGGEAVPPAAFEQVK 3372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 371 -EITGHTLLERYGMTEigmALSNPL----KGPRIPGA----VGSPLPGVEIRIVMSNATNTTIveanhretrvrsgleGK 441
Cdd:PRK12467 3373 rKLKPRGLTNGYGPTE---AVVTVTlwkcGGDAVCEApyapIGRPVAGRSIYVLDGQLNPVPV---------------GV 3434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 442 EGELLVRGPSVFKEYWNKHQETRES-----FTDSG--WFKTGDTAIHK-DGVFWIMGRtsVD-IIKSGGYKISALEVERH 512
Cdd:PRK12467 3435 AGELYIGGVGLARGYHQRPSLTAERfvadpFSGSGgrLYRTGDLARYRaDGVIEYLGR--IDhQVKIRGFRIELGEIEAR 3512
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 513 LLAHPAIADVAVIGPPDAIWGQKVTAVM----------QLKRGHRLTLPElkiwarehmapYIIPTGLVLVEELPRNQMG 582
Cdd:PRK12467 3513 LLQHPSVREAVVLARDGAGGKQLVAYVVpadpqgdwreTLRDHLAASLPD-----------YMVPAQLLVLAAMPLGPNG 3581
|
....*..
gi 2105456023 583 KVNKKDL 589
Cdd:PRK12467 3582 KVDRKAL 3588
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
136-491 |
1.90e-24 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 108.14 E-value: 1.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 136 QWAA-----WMSGGTAVPLYRKHPQEELEYIISDSQSSLLVAGNSFAKTLEPLALKLGLP-----CL-TLPPTSN----- 199
Cdd:PTZ00216 158 EWLAsiygiWSQSMVAATVYANLGEDALAYALRETECKAIVCNGKNVPNLLRLMKSGGMPnttiiYLdSLPASVDtegcr 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 200 -LSTLDGTDSQEEEAA-----ITDWADRPAMIIYTSGTTGRPKGVLHTHSSIQAMVQCLvSEW------AWTRDDVILHT 267
Cdd:PTZ00216 238 lVAWTDVVAKGHSAGShhplnIPENNDDLALIMYTSGTTGDPKGVMHTHGSLTAGILAL-EDRlndligPPEEDETYCSY 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 268 LPLHHV--HGIVNKLL---CPLWVGAT----------CIMLPEFQPQkvweilltskapmvnVFMAVPTIY--------S 324
Cdd:PTZ00216 317 LPLAHImeFGVTNIFLargALIGFGSPrtltdtfarpHGDLTEFRPV---------------FLIGVPRIFdtikkaveA 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 325 KLIQ------------Y----------YDQHFTQPHVKDFVKAVCKQRIRLMVSGSAALPLPTlQRWEEITGHTLLERYG 382
Cdd:PTZ00216 382 KLPPvgslkrrvfdhaYqsrlralkegKDTPYWNEKVFSAPRAVLGGRVRAMLSGGGPLSAAT-QEFVNVVFGMVIQGWG 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 383 MTEIGMALSNPLKGPRIPGAVGSPLPGVEIRIVmsnatntTIVEANHRET---RvrsglegkeGELLVRGPSVFKEYWNK 459
Cdd:PTZ00216 461 LTETVCCGGIQRTGDLEPNAVGQLLKGVEMKLL-------DTEEYKHTDTpepR---------GEILLRGPFLFKGYYKQ 524
|
410 420 430
....*....|....*....|....*....|...
gi 2105456023 460 HQETRESFTDSGWFKTGDTA-IHKDGVFWIMGR 491
Cdd:PTZ00216 525 EELTREVLDEDGWFHTGDVGsIAANGTLRIIGR 557
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
200-479 |
4.28e-24 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 106.89 E-value: 4.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 200 LSTLDGTDSQEEEAAITdwADRPAMIIYTSGTTGRPKGVLHTH----SSIQAMVQClvseWAWTRDD--VILHTLPLHHV 273
Cdd:PRK08180 191 LATPPTAAVDAAHAAVG--PDTIAKFLFTSGSTGLPKAVINTHrmlcANQQMLAQT----FPFLAEEppVLVDWLPWNHT 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 274 HGIVNKLLCPLWVGATcIMLPEFQP--QKVWEIL--LTSKAPmvNVFMAVPTIYSKLIQYYDQhftqphvkDfvKAVCK- 348
Cdd:PRK08180 265 FGGNHNLGIVLYNGGT-LYIDDGKPtpGGFDETLrnLREISP--TVYFNVPKGWEMLVPALER--------D--AALRRr 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 349 --QRIRLMVSGSAALPLPTLQRWEEITGHTLLER------YGMTEIG-MALS--NPLKGPripGAVGSPLPGVEIRIVMS 417
Cdd:PRK08180 332 ffSRLKLLFYAGAALSQDVWDRLDRVAEATCGERirmmtgLGMTETApSATFttGPLSRA---GNIGLPAPGCEVKLVPV 408
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2105456023 418 NatnttiveanhretrvrsgleGKEgELLVRGPSVFKEYWNKHQETRESFTDSGWFKTGDTA 479
Cdd:PRK08180 409 G---------------------GKL-EVRVKGPNVTPGYWRAPELTAEAFDEEGYYRSGDAV 448
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
142-589 |
6.69e-24 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 107.56 E-value: 6.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 142 SGGTAVPLYRKHPQEELEYIISDSQSSLLVAGNSFAKTLEPL-------ALKLGLPCLTLPPTSNLSTLDGTDSQeeeaa 214
Cdd:PRK05691 2261 AGGAYVPLDPEYPLERLHYMIEDSGIGLLLSDRALFEALGELpagvarwCLEDDAAALAAYSDAPLPFLSLPQHQ----- 2335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 215 itdwadrpAMIIYTSGTTGRPKGVLHTHSSIQAMVQCLVSEWAWTRDDVILHTLPLhHVHGIVNKLLCPLWVGATCIMlp 294
Cdd:PRK05691 2336 --------AYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIERFGMRADDCELHFYSI-NFDAASERLLVPLLCGARVVL-- 2404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 295 efQPQKVW---EILLTSKAPMVNVFMAVPTIYSKLIQYY-DQHFTQPhvkdfvkavckqrIRLMVSGSAALPLPTLQRWE 370
Cdd:PRK05691 2405 --RAQGQWgaeEICQLIREQQVSILGFTPSYGSQLAQWLaGQGEQLP-------------VRMCITGGEALTGEHLQRIR 2469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 371 EITGHTLL-ERYGMTE-IGMALSNpLKGPRIPGAVGSplpgVEI-RIVmsNATNTTIVEANhretrVRSGLEGKEGELLV 447
Cdd:PRK05691 2470 QAFAPQLFfNAYGPTEtVVMPLAC-LAPEQLEEGAAS----VPIgRVV--GARVAYILDAD-----LALVPQGATGELYV 2537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 448 RGPSVFKEYWNKHQETRESF------TDSG-WFKTGDTA-IHKDGVFWIMGRTSVDiIKSGGYKISALEVERHLLAHPAI 519
Cdd:PRK05691 2538 GGAGLAQGYHDRPGLTAERFvadpfaADGGrLYRTGDLVrLRADGLVEYVGRIDHQ-VKIRGFRIELGEIESRLLEHPAV 2616
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2105456023 520 ADVAVI--GPPDA--IWGQKVTAVMQLKRGHRLTLPE-LKIWAREHMAPYIIPTGLVLVEELPRNQMGKVNKKDL 589
Cdd:PRK05691 2617 REAVVLalDTPSGkqLAGYLVSAVAGQDDEAQAALREaLKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRAL 2691
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
79-594 |
7.57e-24 |
|
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341242 [Multi-domain] Cd Length: 481 Bit Score: 104.93 E-value: 7.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 79 DRLAIIDSSGSHSYKQLYCSSFGLAGRISaalnsDFGGLEGKRISfLCANDASYT-VAQWAAWMSGGTAVPLYRKHPQEE 157
Cdd:cd05918 14 DAPAVCAWDGSLTYAELDRLSSRLAHHLR-----SLGVGPGVFVP-LCFEKSKWAvVAMLAVLKAGGAFVPLDPSHPLQR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 158 LEYIISDSQSSLLvagnsfaktleplalklglpcLTLPPtsnlstldgtdsqeeeaaitdwaDRPAMIIYTSGTTGRPKG 237
Cdd:cd05918 88 LQEILQDTGAKVV---------------------LTSSP-----------------------SDAAYVIFTSGSTGKPKG 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 238 VLHTHSSIQAMVQCLVSEWAWTRDDVIL----HTLPLHhvhgiVNKLLCPLWVGAT-CIM--------LPEFqpqkvwei 304
Cdd:cd05918 124 VVIEHRALSTSALAHGRALGLTSESRVLqfasYTFDVS-----ILEIFTTLAAGGClCIPseedrlndLAGF-------- 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 305 LLTSKapmVNVFMAVPTIySKLIQyydqhftqPhvKDFVkavckqRIRLMVSGSAALPLPTLQRWEEitGHTLLERYGMT 384
Cdd:cd05918 191 INRLR---VTWAFLTPSV-ARLLD--------P--EDVP------SLRTLVLGGEALTQSDVDTWAD--RVRLINAYGPA 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 385 E--IGMALSNPLKGPRiPGAVGSPLPGVeirivmsnatnTTIVEANHRETRVrsgLEGKEGELLVRGPSVFKEYWNKHQE 462
Cdd:cd05918 249 EctIAATVSPVVPSTD-PRNIGRPLGAT-----------CWVVDPDNHDRLV---PIGAVGELLIEGPILARGYLNDPEK 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 463 TRESF-TDSGW------------FKTGDTA-IHKDGVFWIMGRTSvDIIKSGGYKISALEVERHLLAHPAIAD---VAVI 525
Cdd:cd05918 314 TAAAFiEDPAWlkqegsgrgrrlYRTGDLVrYNPDGSLEYVGRKD-TQVKIRGQRVELGEIEHHLRQSLPGAKevvVEVV 392
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 526 GPPDAIWGQKVTAVMQLKR-------GHRLTLP----------ELKIWAREHMAPYIIPTGLVLVEELPRNQMGKVNKKd 588
Cdd:cd05918 393 KPKDGSSSPQLVAFVVLDGsssgsgdGDSLFLEpsdefralvaELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRR- 471
|
....*.
gi 2105456023 589 LLRHFF 594
Cdd:cd05918 472 ALRELA 477
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
219-526 |
8.61e-24 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 105.37 E-value: 8.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 219 ADRPAMIIYTSGTTGRPKGVLHTHSSIQAMVQCLVSEWAWTRDDVILHTLPLHHVHGIVnkllcplwVGATCImLPEF-- 296
Cdd:PRK09274 173 PDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEIDLPTFPLFALFGPA--------LGMTSV-IPDMdp 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 297 ------QPQKVWEILLTSKapmVNVFMAVPTIYSKLIQYydqhftqphvkdfvkavCKQR------IRLMVSGSAALPLP 364
Cdd:PRK09274 244 trpatvDPAKLFAAIERYG---VTNLFGSPALLERLGRY-----------------GEANgiklpsLRRVISAGAPVPIA 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 365 TLQRWEEITGHT--LLERYGMTE------IGMalSNPLKGPRI---PGA---VGSPLPGVEIRIVmsnATNTTIVEANHR 430
Cdd:PRK09274 304 VIERFRAMLPPDaeILTPYGATEalpissIES--REILFATRAatdNGAgicVGRPVDGVEVRII---AISDAPIPEWDD 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 431 ETRVrsgLEGKEGELLVRGPSVFKEYWNKHQETRESFTDSG----WFKTGDTA-IHKDGVFWIMGRTSVDIIKSGG--YK 503
Cdd:PRK09274 379 ALRL---ATGEIGEIVVAGPMVTRSYYNRPEATRLAKIPDGqgdvWHRMGDLGyLDAQGRLWFCGRKAHRVETAGGtlYT 455
|
330 340
....*....|....*....|...
gi 2105456023 504 IsalEVERHLLAHPAIADVAVIG 526
Cdd:PRK09274 456 I---PCERIFNTHPGVKRSALVG 475
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
87-584 |
1.11e-23 |
|
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: 105.26 E-value: 1.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 87 SGSHSYKQLYCSSFGLAGRISAAlnsdfGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLYRKHPQEELEYIISDSQ 166
Cdd:cd05968 89 SRTLTYGELLYEVKRLANGLRAL-----GVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAE 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 167 SSLLVAGNSFAKTLEPLALK---------------------LGLPcLTLPPTSNLSTLDGTDSQEEEAAITDwADRPAMI 225
Cdd:cd05968 164 AKALITADGFTRRGREVNLKeeadkacaqcptvekvvvvrhLGND-FTPAKGRDLSYDEEKETAGDGAERTE-SEDPLMI 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 226 IYTSGTTGRPKGVLHTHS-----SIQAMVQCL----------VSEWAWTRDdvilhtlPLHHVHGIVNKLLCPLWVGAtc 290
Cdd:cd05968 242 IYTSGTTGKPKGTVHVHAgfplkAAQDMYFQFdlkpgdlltwFTDLGWMMG-------PWLIFGGLILGATMVLYDGA-- 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 291 imlPEF-QPQKVWEILLTSKAPMVNVfmaVPTIYSKLIqyydqhftqPHVKDFVKAVCKQRIRLMVS-GSAALPLPTLQR 368
Cdd:cd05968 313 ---PDHpKADRLWRMVEDHEITHLGL---SPTLIRALK---------PRGDAPVNAHDLSSLRVLGStGEPWNPEPWNWL 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 369 WEEI-TGHTLLERY-GMTEI-GMALSNPLKGPRIPGAVGSPLPGVEIRIVmsnatnttiveaNHRETRVRsgleGKEGEL 445
Cdd:cd05968 378 FETVgKGRNPIINYsGGTEIsGGILGNVLIKPIKPSSFNGPVPGMKADVL------------DESGKPAR----PEVGEL 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 446 LVRGP--SVFKEYW---NKHQETRESFTDSGWFKtGDTAIH-KDGVFWIMGRtSVDIIKSGGYKISALEVERHLLAHPAI 519
Cdd:cd05968 442 VLLAPwpGMTRGFWrdeDRYLETYWSRFDNVWVH-GDFAYYdEEGYFYILGR-SDDTINVAGKRVGPAEIESVLNAHPAV 519
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2105456023 520 ADVAVIGPPDAIWGQKVTAVMQLKRGHRLT---LPELKIWAREHMAPYIIPTGLVLVEELPRNQMGKV 584
Cdd:cd05968 520 LESAAIGVPHPVKGEAIVCFVVLKPGVTPTealAEELMERVADELGKPLSPERILFVKDLPKTRNAKV 587
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
223-477 |
2.10e-23 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 104.80 E-value: 2.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 223 AMIIYTSGTTGRPKGVLHTHSSIQAMVQCLVSEWAWTRDDVILHTLPLHHVHGIVNKLLCpLWVGATCimlpEFQPQKVW 302
Cdd:PLN02736 224 ATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTKFYPSDVHISYLPLAHIYERVNQIVM-LHYGVAV----GFYQGDNL 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 303 EILLTSKAPMVNVFMAVPTIYSKLiqyYD----------------------------QHFTQPH------VKDFVKAVCK 348
Cdd:PLN02736 299 KLMDDLAALRPTIFCSVPRLYNRI---YDgitnavkesgglkerlfnaaynakkqalENGKNPSpmwdrlVFNKIKAKLG 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 349 QRIRLMVSGSAALPLPTLQRWEEITGHTLLERYGMTEIGMALSNPLKGPRIPGAVGSPLPGVEIRIVMSNATNTTIVEAN 428
Cdd:PLN02736 376 GRVRFMSSGASPLSPDVMEFLRICFGGRVLEGYGMTETSCVISGMDEGDNLSGHVGSPNPACEVKLVDVPEMNYTSEDQP 455
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2105456023 429 HretrvrsglegKEGELLVRGPSVFKEYWNKHQETRESFTDSGWFKTGD 477
Cdd:PLN02736 456 Y-----------PRGEICVRGPIIFKGYYKDEVQTREVIDEDGWLHTGD 493
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
217-589 |
3.73e-23 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 103.82 E-value: 3.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 217 DWADR--PAMIIYTSGTTGRPKGVLHTHSSIqaMVQCLVS---EWAWTRDDVILHTLPLHHVHGIVNKLLCPLWVGATCI 291
Cdd:PLN02654 270 EWVDAedPLFLLYTSGSTGKPKGVLHTTGGY--MVYTATTfkyAFDYKPTDVYWCTADCGWITGHSYVTYGPMLNGATVL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 292 ML---PEF-QPQKVWEILLTSKapmVNVFMAVPTIYSKLIQYYDQHFTQphvkdfvkavcKQRIRLMVSGSAALPL-PTL 366
Cdd:PLN02654 348 VFegaPNYpDSGRCWDIVDKYK---VTIFYTAPTLVRSLMRDGDEYVTR-----------HSRKSLRVLGSVGEPInPSA 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 367 QRW-EEITGHT---LLERYGMTEIGMALSNPLKG--PRIPGAVGSPLPGVEirivmsnatnTTIVEANHREtrvrsgLEG 440
Cdd:PLN02654 414 WRWfFNVVGDSrcpISDTWWQTETGGFMITPLPGawPQKPGSATFPFFGVQ----------PVIVDEKGKE------IEG 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 441 K-EGELLVRG--PSVFKEYWNKHQ--ETRESFTDSGWFKTGD-TAIHKDGVFWIMGRTSvDIIKSGGYKISALEVERHLL 514
Cdd:PLN02654 478 EcSGYLCVKKswPGAFRTLYGDHEryETTYFKPFAGYYFSGDgCSRDKDGYYWLTGRVD-DVINVSGHRIGTAEVESALV 556
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2105456023 515 AHPAIADVAVIGPPDAIWGQKVTAVMQLKRGHRLTlPELK----IWAREHMAPYIIPTGLVLVEELPRNQMGKVNKKDL 589
Cdd:PLN02654 557 SHPQCAEAAVVGIEHEVKGQGIYAFVTLVEGVPYS-EELRksliLTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRIL 634
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
219-589 |
4.32e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 102.04 E-value: 4.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 219 ADRPAMIIYTSGTTGRPKGVLHTHSSIQAMVQCLVSEWAWTRDDVILHTLPLHHVHGIVNKLLCPLWVGATCIMLPEFQP 298
Cdd:PRK08308 100 AEEPSLLQYSSGTTGEPKLIRRSWTEIDREIEAYNEALNCEQDETPIVACPVTHSYGLICGVLAALTRGSKPVIITNKNP 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 299 QKVWEILLTSKAPMVnvfMAVPTIYSKLIQyydqhFTQPhvkdfvkavcKQRI-RLMVSGsAALPLPTLQRWEEITGHtL 377
Cdd:PRK08308 180 KFALNILRNTPQHIL---YAVPLMLHILGR-----LLPG----------TFQFhAVMTSG-TPLPEAWFYKLRERTTY-M 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 378 LERYGMTEIG-MALSNPLkgpRIPGAVGSPLPGVEIRIVMSnatnttivEANHRETRVRSGlegkegellvrgpsvfkey 456
Cdd:PRK08308 240 MQQYGCSEAGcVSICPDM---KSHLDLGNPLPHVSVSAGSD--------ENAPEEIVVKMG------------------- 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 457 wnkhqeTRESFT-DSGwFKTGDTAIHkdgvfwIMGRTSvDIIKSGGYKISALEVERHLLAHPAIADVAVIGPPDAIWGQK 535
Cdd:PRK08308 290 ------DKEIFTkDLG-YKSERGTLH------FMGRMD-DVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGER 355
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 2105456023 536 VTAvmQLKRGHRLTLPELKIWAREHMAPYIIPTGLVLVEELPRNQMGKVNKKDL 589
Cdd:PRK08308 356 VKA--KVISHEEIDPVQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLL 407
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
73-491 |
7.84e-23 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 104.09 E-value: 7.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 73 RAPAFGDRLAII------DSSGSHSYKQLycssfGLAGR-ISAALNSDFGglEGKRISFLCANDASYTVAQWAAWMSGGT 145
Cdd:PRK05691 18 RAAQTPDRLALRfladdpGEGVVLSYRDL-----DLRARtIAAALQARAS--FGDRAVLLFPSGPDYVAAFFGCLYAGVI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 146 AVPLY-----RKHPQEELEYIISDSQSSLLVAGNSFAKTLeplalkLGLPCLTLPPTSNLSTLDGTDSqeeeAAITDW-- 218
Cdd:PRK05691 91 AVPAYppesaRRHHQERLLSIIADAEPRLLLTVADLRDSL------LQMEELAAANAPELLCVDTLDP----ALAEAWqe 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 219 ----ADRPAMIIYTSGTTGRPKGVLHTHSSIQAmvqclvSEWAWTR--------DDVILHTLPLHHVHGIVNKLLCPLWV 286
Cdd:PRK05691 161 palqPDDIAFLQYTSGSTALPKGVQVSHGNLVA------NEQLIRHgfgidlnpDDVIVSWLPLYHDMGLIGGLLQPIFS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 287 GATCIMLpefqpqkvweilltskAPmvNVFMAVPTIYSKLIQYYDQhfTQPHVKDFVKAVCKQRI-------------RL 353
Cdd:PRK05691 235 GVPCVLM----------------SP--AYFLERPLRWLEAISEYGG--TISGGPDFAYRLCSERVsesalerldlsrwRV 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 354 MVSGSAALPLPTLQRWEE------ITGHTLLERYGMTEIGMALSNPLKGPRIP------------------GAV----GS 405
Cdd:PRK05691 295 AYSGSEPIRQDSLERFAEkfaacgFDPDSFFASYGLAEATLFVSGGRRGQGIPaleldaealarnraepgtGSVlmscGR 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 406 PLPGVEIRIVmsnatnttiveanhrETRVRSGL-EGKEGELLVRGPSVFKEYWNKHQETRESFTDSG---WFKTGDTAIH 481
Cdd:PRK05691 375 SQPGHAVLIV---------------DPQSLEVLgDNRVGEIWASGPSIAHGYWRNPEASAKTFVEHDgrtWLRTGDLGFL 439
|
490
....*....|
gi 2105456023 482 KDGVFWIMGR 491
Cdd:PRK05691 440 RDGELFVTGR 449
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
219-589 |
8.63e-23 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 102.41 E-value: 8.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 219 ADRPAMIIYTSGTTGRPKGVLHTHSSIQAMVQCLVSEWAWTRDDVILHTLPLHHVHGIVNKLLCPLWVGATCIMLPEFQP 298
Cdd:PRK13388 149 AMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLTRDDVCYVSMPLFHSNAVMAGWAPAVASGAAVALPAKFSA 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 299 QKVweilltskAPMVNVFMAVPTIY-SKLIQYYDQHFTQPHVKDfvkavckQRIRLMVsGSAALPlptlqrwEEIT---- 373
Cdd:PRK13388 229 SGF--------LDDVRRYGATYFNYvGKPLAYILATPERPDDAD-------NPLRVAF-GNEASP-------RDIAefsr 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 374 --GHTLLERYGMTEIGMALSNPLKGPriPGAVGSPLPGVEIrivMSNATNTTIVEANHRET-RVRSGLEGKeGELLVR-G 449
Cdd:PRK13388 286 rfGCQVEDGYGSSEGAVIVVREPGTP--PGSIGRGAPGVAI---YNPETLTECAVARFDAHgALLNADEAI-GELVNTaG 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 450 PSVFKEYWNKHQETRESFTDsGWFKTGDTA-IHKDGVFWIMGRTSvDIIKSGGYKISALEVERHLLAHPAIADVAVIGPP 528
Cdd:PRK13388 360 AGFFEGYYNNPEATAERMRH-GMYWSGDLAyRDADGWIYFAGRTA-DWMRVDGENLSAAPIERILLRHPAINRVAVYAVP 437
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2105456023 529 DAIWGQKVTAVMQLKRGHRLTLPELKIW--AREHMAPYIIPTGLVLVEELPRNQMGKVNKKDL 589
Cdd:PRK13388 438 DERVGDQVMAALVLRDGATFDPDAFAAFlaAQPDLGTKAWPRYVRIAADLPSTATNKVLKREL 500
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
191-562 |
2.52e-22 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 100.33 E-value: 2.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 191 CLTLPPTSNLSTLDGTDSQEEEAAIT-DW-ADRPAMIIYTSGTTGRPKGVLHTHSSIQAMVQCLVSEWAWTRDDVILHTL 268
Cdd:PRK09029 104 ALVLEGENTFSALTSLHLQLVEGAHAvAWqPQRLATMTLTSGSTGLPKAAVHTAQAHLASAEGVLSLMPFTAQDSWLLSL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 269 PLHHVHG--IVnkllcplW----VGATcIMLPEFQPqkVWEILL-TSKAPMVnvfmavPTIYSKLIQYYDQHFTQPHVkd 341
Cdd:PRK09029 184 PLFHVSGqgIV-------WrwlyAGAT-LVVRDKQP--LEQALAgCTHASLV------PTQLWRLLDNRSEPLSLKAV-- 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 342 fvkavckqrirLMvsGSAALPLPTLQRWEEITGHTLLErYGMTEigMA------LSNPLKGpripgaVGSPLPGVEIRIV 415
Cdd:PRK09029 246 -----------LL--GGAAIPVELTEQAEQQGIRCWCG-YGLTE--MAstvcakRADGLAG------VGSPLPGREVKLV 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 416 msnatnttiveanhretrvrsglegkEGELLVRGPSVFKEYWnkHQETRESFTDS-GWFKTGDTAIHKDGVFWIMGRTSV 494
Cdd:PRK09029 304 --------------------------DGEIWLRGASLALGYW--RQGQLVPLVNDeGWFATRDRGEWQNGELTILGRLDN 355
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2105456023 495 DIIkSGGYKISALEVERHLLAHPAIADVAVIGPPDAIWGQKVTAVMQLKrgHRLTLPELKIWAREHMA 562
Cdd:PRK09029 356 LFF-SGGEGIQPEEIERVINQHPLVQQVFVVPVADAEFGQRPVAVVESD--SEAAVVNLAEWLQDKLA 420
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
99-526 |
3.80e-22 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 100.89 E-value: 3.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 99 SFGLAGRISAALNS---DFGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPL---YRKHPQE--ELEYIISDSQSSLL 170
Cdd:PRK12582 82 TYGEAKRAVDALAQallDLGLDPGRPVMILSGNSIEHALMTLAAMQAGVPAAPVspaYSLMSHDhaKLKHLFDLVKPRVV 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 171 VA--GNSFAKTLEPLALkLGLPCLTL--PPTSN--------LSTLDGTDSQEEEAAITDwaDRPAMIIYTSGTTGRPKGV 238
Cdd:PRK12582 162 FAqsGAPFARALAALDL-LDVTVVHVtgPGEGIasiafadlAATPPTAAVAAAIAAITP--DTVAKYLFTSGSTGMPKAV 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 239 LHTH---SSIQAMVQCLVSEWAWTRDDVILHTLPLHHVHG---IVNKLLcplWVGATCIM-----LP-EFQP--QKVWEI 304
Cdd:PRK12582 239 INTQrmmCANIAMQEQLRPREPDPPPPVSLDWMPWNHTMGgnaNFNGLL---WGGGTLYIddgkpLPgMFEEtiRNLREI 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 305 lltskAPMVnvFMAVPTIYSKLIQYYDQHftqphvkdfvKAVCK---QRIRLMVSGSAALPLPTLQRWEE----ITGH-- 375
Cdd:PRK12582 316 -----SPTV--YGNVPAGYAMLAEAMEKD----------DALRRsffKNLRLMAYGGATLSDDLYERMQAlavrTTGHri 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 376 TLLERYGMTEIGMALSNPLKGPRIPGAVGSPLPGVEIRIVMSnatnttiveanhretrvrsgleGKEGELLVRGPSVFKE 455
Cdd:PRK12582 379 PFYTGYGATETAPTTTGTHWDTERVGLIGLPLPGVELKLAPV----------------------GDKYEVRVKGPNVTPG 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 456 YWNKHQETRESFTDSGWFKTGDTAIHKDG-------VFwiMGRTSVDIIKSGGYKISALEVERHLLA--HPAIADVAVIG 526
Cdd:PRK12582 437 YHKDPELTAAAFDEEGFYRLGDAARFVDPddpekglIF--DGRVAEDFKLSTGTWVSVGTLRPDAVAacSPVIHDAVVAG 514
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
128-526 |
4.31e-22 |
|
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341256 [Multi-domain] Cd Length: 596 Bit Score: 100.51 E-value: 4.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 128 NDASYTVAQWAAWMSGGTAVPLYRKHPQEELEYIISDSQSSLLVAGNsfAKTLEP-LALKLGLPCLTL---------PPT 197
Cdd:cd05933 42 NSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSEANILVVEN--QKQLQKiLQIQDKLPHLKAiiqykeplkEKE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 198 SNLSTLDG--------TDSQEEEAAITDWADRPAMIIYTSGTTGRPKGVLHTHSSI----QAMVQCLVSEWAWTRDDVIL 265
Cdd:cd05933 120 PNLYSWDEfmelgrsiPDEQLDAIISSQKPNQCCTLIYTSGTTGMPKGVMLSHDNItwtaKAASQHMDLRPATVGQESVV 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 266 HTLPLHHVHG-IVNKLLCPLWVGATC------------IMLPEFQPQK------VWEILLTSkapMVNVFmAVPTIYSKL 326
Cdd:cd05933 200 SYLPLSHIAAqILDIWLPIKVGGQVYfaqpdalkgtlvKTLREVRPTAfmgvprVWEKIQEK---MKAVG-AKSGTLKRK 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 327 IQYYDQ-------------HFTQPHVKDFVKAVCKQRIRLMV---------SGSAALPLPTLQRWEEITgHTLLERYGMT 384
Cdd:cd05933 276 IASWAKgvgletnlklmggESPSPLFYRLAKKLVFKKVRKALgldrcqkffTGAAPISRETLEFFLSLN-IPIMELYGMS 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 385 EIGMA--LSNPlKGPRIpGAVGSPLPGVEIRIVMSNAtnttiveanhretrvrsglEGkEGELLVRGPSVFKEYWNKHQE 462
Cdd:cd05933 355 ETSGPhtISNP-QAYRL-LSCGKALPGCKTKIHNPDA-------------------DG-IGEICFWGRHVFMGYLNMEDK 412
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2105456023 463 TRESFTDSGWFKTGDTA-IHKDGVFWIMGRTSVDIIKSGGYKISALEVERHLLAH-PAIADVAVIG 526
Cdd:cd05933 413 TEEAIDEDGWLHSGDLGkLDEDGFLYITGRIKELIITAGGENVPPVPIEDAVKKElPIISNAMLIG 478
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
79-590 |
1.61e-21 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 98.04 E-value: 1.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 79 DRLAIIDSSGSHSYKQLYCSSFGLAGRISAALNSD------FGGLEGKRI-SFLcandasytvaqwAAWMSGGTAVPLYR 151
Cdd:PRK04813 17 DFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDkspiivFGHMSPEMLaTFL------------GAVKAGHAYIPVDV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 152 KHPQEELEYIISDSQSSLLVAGNSFAKTLEplalklGLPCLTLpptSNLSTLDGTD-SQEEEAAITDwaDRPAMIIYTSG 230
Cdd:PRK04813 85 SSPAERIEMIIEVAKPSLIIATEELPLEIL------GIPVITL---DELKDIFATGnPYDFDHAVKG--DDNYYIIFTSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 231 TTGRPKGVLHTHSSIQAMVQCLVSEWAWTRDDVILHTLPLHHVHGIVNKLLCpLWVGATCIMLPE---FQPQKVWEILLT 307
Cdd:PRK04813 154 TTGKPKGVQISHDNLVSFTNWMLEDFALPEGPQFLNQAPYSFDLSVMDLYPT-LASGGTLVALPKdmtANFKQLFETLPQ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 308 SKapmVNVFMAVPTiyskliqyydqhftqphvkdFVKaVCkqrirLMVSGSAALPLPTLQRW----EEITGHT---LLER 380
Cdd:PRK04813 233 LP---INVWVSTPS--------------------FAD-MC-----LLDPSFNEEHLPNLTHFlfcgEELPHKTakkLLER 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 381 ---------YGMTEIGMALSNPL-------KGPRIPgaVGSPLPGVEIRIVMSNATNTTiveanhretrvrsglEGKEGE 444
Cdd:PRK04813 284 fpsatiyntYGPTEATVAVTSIEitdemldQYKRLP--IGYAKPDSPLLIIDEEGTKLP---------------DGEQGE 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 445 LLVRGPSVFKEYWNKHQETRESF-TDSGW--FKTGDTAIHKDGVFWIMGRtsVDI-IKSGGYKISALEVERHLLAHPAIA 520
Cdd:PRK04813 347 IVISGPSVSKGYLNNPEKTAEAFfTFDGQpaYHTGDAGYLEDGLLFYQGR--IDFqIKLNGYRIELEEIEQNLRQSSYVE 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 521 dVAVIGPPDAiwGQKVT---AVMQLKRGHR---LTLP-----ELKiwarEHMAPYIIPTGLVLVEELPRNQMGKVNKKDL 589
Cdd:PRK04813 425 -SAVVVPYNK--DHKVQyliAYVVPKEEDFereFELTkaikkELK----ERLMEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
|
.
gi 2105456023 590 L 590
Cdd:PRK04813 498 I 498
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
79-589 |
3.57e-21 |
|
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: 96.47 E-value: 3.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 79 DRLAIIDSSGSHSYKQLYCSsfglAGRISAALNsDFGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLYRKHPQEEL 158
Cdd:cd17645 13 DHVAVVDRGQSLTYKQLNEK----ANQLARHLR-GKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGERI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 159 EYIISDSQSSLLvagnsfaktleplalklglpcltlpptsnlstldgtdsqeeeaaITDwADRPAMIIYTSGTTGRPKGV 238
Cdd:cd17645 88 AYMLADSSAKIL--------------------------------------------LTN-PDDLAYVIYTSGSTGLPKGV 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 239 LHTHssiqamvqclvsewawtrddvilhtlplhhvHGIVNklLCpLWVGATCIMLPEFQPQK---------VWEIL--LT 307
Cdd:cd17645 123 MIEH-------------------------------HNLVN--LC-EWHRPYFGVTPADKSLVyasfsfdasAWEIFphLT 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 308 SKAPMVNVFMAVPTIYSKLIQYYDQH-----FTQPHVKDFVKAVCKQRIRLMVSGSaalplPTLQRWEEiTGHTLLERYG 382
Cdd:cd17645 169 AGAALHVVPSERRLDLDALNDYFNQEgitisFLPTGAAEQFMQLDNQSLRVLLTGG-----DKLKKIER-KGYKLVNNYG 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 383 MTEIG-MALSNPLKGPRIPGAVGSPLPGVEIRIvmsnatnttIVEANHRETrvrsglEGKEGELLVRGPSVFKEYWNKHQ 461
Cdd:cd17645 243 PTENTvVATSFEIDKPYANIPIGKPIDNTRVYI---------LDEALQLQP------IGVAGELCIAGEGLARGYLNRPE 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 462 ETRESF------TDSGWFKTGDTA-IHKDGVFWIMGRTSvDIIKSGGYKISALEVERHLLAHPAIADVAVIGPPDAIWGQ 534
Cdd:cd17645 308 LTAEKFivhpfvPGERMYRTGDLAkFLPDGNIEFLGRLD-QQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRK 386
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 2105456023 535 KVTAVMQLKRghRLTLPELKIWAREHMAPYIIPTGLVLVEELPRNQMGKVNKKDL 589
Cdd:cd17645 387 YLVAYVTAPE--EIPHEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
219-526 |
6.36e-21 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 95.99 E-value: 6.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 219 ADRPAMIIYTSGTTGRPKGVLHTHSSIQAMVQCLVSEWAWTRDDVILHTLPLHhvhgivnKLLCPLwVGATCImLPEFQP 298
Cdd:cd05910 84 ADEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGEVDLATFPLF-------ALFGPA-LGLTSV-IPDMDP 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 299 qkvweilltSKAPMVNvfmavPTIYSKLIQYY--DQHFTQPHVKDFVKAVCKQR------IRLMVSGSAALPLPTLQRWE 370
Cdd:cd05910 155 ---------TRPARAD-----PQKLVGAIRQYgvSIVFGSPALLERVARYCAQHgitlpsLRRVLSAGAPVPIALAARLR 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 371 EITGHT--LLERYGMTE---IGMALSNPLKGPRIPGA-------VGSPLPGVEIRIVMSNATNTTIVEANHRETRvrsgl 438
Cdd:cd05910 221 KMLSDEaeILTPYGATEalpVSSIGSRELLATTTAATsggagtcVGRPIPGVRVRIIEIDDEPIAEWDDTLELPR----- 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 439 eGKEGELLVRGPSVFKEYWNKHQETRESFTDSG----WFKTGDTAIHKD-GVFWIMGRTSVDIIKSGGyKISALEVERHL 513
Cdd:cd05910 296 -GEIGEITVTGPTVTPTYVNRPVATALAKIDDNsegfWHRMGDLGYLDDeGRLWFCGRKAHRVITTGG-TLYTEPVERVF 373
|
330
....*....|...
gi 2105456023 514 LAHPAIADVAVIG 526
Cdd:cd05910 374 NTHPGVRRSALVG 386
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
78-526 |
7.16e-21 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 96.83 E-value: 7.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 78 GDRLAIIDSSGSH---SYKQLYCSsfglAGRISAALNSdFGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLYRKHP 154
Cdd:PLN02861 63 GRRQVTDSKVGPYvwlTYKEVYDA----AIRIGSAIRS-RGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLG 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 155 QEELEYIISDSQSSLLVAGNSFAKTLeplalklgLPCLTlPPTSNLSTL----DGTDSQEEEA-----AITDWADRPAM- 224
Cdd:PLN02861 138 ANAVEFIINHAEVSIAFVQESKISSI--------LSCLP-KCSSNLKTIvsfgDVSSEQKEEAeelgvSCFSWEEFSLMg 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 225 ----------------IIYTSGTTGRPKGVLHTHSSIQAMVQC-----LVSEWAWTRDDVILHTLPLHHVHGIVNKLLC- 282
Cdd:PLN02861 209 sldcelppkqktdictIMYTSGTTGEPKGVILTNRAIIAEVLStdhllKVTDRVATEEDSYFSYLPLAHVYDQVIETYCi 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 283 ------PLWVGATCIMLPEFQPQKvweilltskaPmvNVFMAVPTIY------------------SKLIQY--------- 329
Cdd:PLN02861 289 skgasiGFWQGDIRYLMEDVQALK----------P--TIFCGVPRVYdriytgimqkissggmlrKKLFDFaynyklgnl 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 330 ---YDQHFTQPHVKDFVKAVCKQ----RIRLMVSGSAALPLPTLQRWEEITGHTLLERYGMTE-IGMALSNPLKGPRIPG 401
Cdd:PLN02861 357 rkgLKQEEASPRLDRLVFDKIKEglggRVRLLLSGAAPLPRHVEEFLRVTSCSVLSQGYGLTEsCGGCFTSIANVFSMVG 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 402 AVGSPLPGVEIRIVMSNATNTTIVEANHRetrvrsglegkeGELLVRGPSVFKEYWNKHQETRESFTDsGWFKTGDTA-I 480
Cdd:PLN02861 437 TVGVPMTTIEARLESVPEMGYDALSDVPR------------GEICLRGNTLFSGYHKRQDLTEEVLID-GWFHTGDIGeW 503
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 2105456023 481 HKDGVFWIMGRTSvDIIK-SGGYKISALEVERHLLAHPAIADVAVIG 526
Cdd:PLN02861 504 QPNGAMKIIDRKK-NIFKlSQGEYVAVENLENTYSRCPLIASIWVYG 549
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
219-577 |
9.49e-21 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 96.70 E-value: 9.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 219 ADRPAMIIYTSGTTGRPKGVLHTHSSIQAMVQCLVSEWAWTRDDVILHTLPLHHVHGIVNKLLCPLWVGATCIMLP---- 294
Cdd:PRK08043 364 PEDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPsplh 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 295 -EFQPQKVWEILLTskapmvnVFMAVPTIyskLIQYydQHFTQPHvkDFVkavckqRIRLMVSGSAALPLPTLQRWEEIT 373
Cdd:PRK08043 444 yRIVPELVYDRNCT-------VLFGTSTF---LGNY--ARFANPY--DFA------RLRYVVAGAEKLQESTKQLWQDKF 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 374 GHTLLERYGMTEIG--MALSNPLKGPriPGAVGSPLPGVEIRIVMSnatnttiveanhretrvrSGLEgKEGELLVRGPS 451
Cdd:PRK08043 504 GLRILEGYGVTECApvVSINVPMAAK--PGTVGRILPGMDARLLSV------------------PGIE-QGGRLQLKGPN 562
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 452 VFKEYWNKHQ---------ETRESFTDSGWFKTGD-TAIHKDGVFWIMGRTSvDIIKSGGYKISALEVERHLLAHPAIAD 521
Cdd:PRK08043 563 IMNGYLRVEKpgvlevptaENARGEMERGWYDTGDiVRFDEQGFVQIQGRAK-RFAKIAGEMVSLEMVEQLALGVSPDKQ 641
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 2105456023 522 VAVIGPPDAIWGQkvtAVMQLKRGHRLTLPELKIWAREHMAPYI-IPTGLVLVEELP 577
Cdd:PRK08043 642 HATAIKSDASKGE---ALVLFTTDSELTREKLQQYAREHGVPELaVPRDIRYLKQLP 695
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
82-589 |
4.28e-20 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 95.11 E-value: 4.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 82 AIIDSSGSHSYKQLYCSSFGLAGRISAAlnsdfGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLYRKHPQEELEYI 161
Cdd:PRK10252 476 ALADARYQFSYREMREQVVALANLLRER-----GVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMM 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 162 ISDSQSSLLVAGNSFAKTLEplalklGLPCLTLPPTSNLSTLDGTdsqeeEAAITDWADRPAMIIYTSGTTGRPKGVLHT 241
Cdd:PRK10252 551 LEDARPSLLITTADQLPRFA------DVPDLTSLCYNAPLAPQGA-----APLQLSQPHHTAYIIFTSGSTGRPKGVMVG 619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 242 HssiQAMVQCLV---SEWAWTRDDVILHTLPL-HHVHgiVNKLLCPLWVGATCIMLPE------FQPQKV---WEILLTS 308
Cdd:PRK10252 620 Q---TAIVNRLLwmqNHYPLTADDVVLQKTPCsFDVS--VWEFFWPFIAGAKLVMAEPeahrdpLAMQQFfaeYGVTTTH 694
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 309 KAP-MVNVFMAVPTiyskliqyydqhftqphvKDFVKAVCKQRIRLMVSGSAaLPLPTLQRWEEITGHTLLERYGMTEIG 387
Cdd:PRK10252 695 FVPsMLAAFVASLT------------------PEGARQSCASLRQVFCSGEA-LPADLCREWQQLTGAPLHNLYGPTEAA 755
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 388 MALSN-PLKGPRIPGAVGSPLPgveIRIVMSNaTNTTIVEAnhretRVRSGLEGKEGELLVRGPSVFKEYWNKHQETRES 466
Cdd:PRK10252 756 VDVSWyPAFGEELAAVRGSSVP---IGYPVWN-TGLRILDA-----RMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASR 826
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 467 FTDSGW------FKTGDTAI-HKDGVFWIMGRtSVDIIKSGGYKISALEVERHLLAHPAIADVAVI------GPPDAIWG 533
Cdd:PRK10252 827 FIADPFapgermYRTGDVARwLDDGAVEYLGR-SDDQLKIRGQRIELGEIDRAMQALPDVEQAVTHacvinqAAATGGDA 905
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 2105456023 534 QKVTAVMQLKRGHRLTLPELKIWAREHMAPYIIPTGLVLVEELPRNQMGKVNKKDL 589
Cdd:PRK10252 906 RQLVGYLVSQSGLPLDTSALQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKAL 961
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
112-526 |
4.32e-20 |
|
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: 94.03 E-value: 4.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 112 SDFGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLYRKHPQEELEYIISDSQSSLLVAGN--SFAKTLE-----PLA 184
Cdd:cd17641 29 LALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIAEDeeQVDKLLEiadriPSV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 185 LKL------GLPCLTLPPTSNLS-------TLDGTDSQEEEAAITdwADRP---AMIIYTSGTTGRPKGVLHTHSSIQAM 248
Cdd:cd17641 109 RYViycdprGMRKYDDPRLISFEdvvalgrALDRRDPGLYEREVA--AGKGedvAVLCTTSGTTGKPKLAMLSHGNFLGH 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 249 VQCLVSEWAWTRDDVILHTLPLHHVHGIVNKLLCPLWVGaTCIMLPE-----------------FQPQKVWEILLT---- 307
Cdd:cd17641 187 CAAYLAADPLGPGDEYVSVLPLPWIGEQMYSVGQALVCG-FIVNFPEepetmmedlreigptfvLLPPRVWEGIAAdvra 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 308 --SKAPMVNVFMAvpTIYSKL-IQYYDQHFTQPHVKDFVKAVCK----------------QRIRLMVSGSAALPlPTLQR 368
Cdd:cd17641 266 rmMDATPFKRFMF--ELGMKLgLRALDRGKRGRPVSLWLRLASWladallfrplrdrlgfSRLRSAATGGAALG-PDTFR 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 369 WEEITGHTLLERYGMTEIGMALSNPLKGPRIPGAVGSPLPGVEIRIVmsnatnttiveanhretrvrsglegKEGELLVR 448
Cdd:cd17641 343 FFHAIGVPLKQLYGQTELAGAYTVHRDGDVDPDTVGVPFPGTEVRID-------------------------EVGEILVR 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 449 GPSVFKEYWNKHQETRESFTDSGWFKTGDTA-IHKDGVFWIMGRTSvDIIK-SGGYKISALEVERHLLAHPAIADVAVIG 526
Cdd:cd17641 398 SPGVFVGYYKNPEATAEDFDEDGWLHTGDAGyFKENGHLVVIDRAK-DVGTtSDGTRFSPQFIENKLKFSPYIAEAVVLG 476
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
79-589 |
5.35e-20 |
|
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.
Pssm-ID: 341303 [Multi-domain] Cd Length: 453 Bit Score: 92.85 E-value: 5.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 79 DRLAIIDSSGSHSYKQLYCSSFGLAGRI--SAALNSDfgglegKRISFLCANDASYTVAQWAAWMSGGTAVPLYRKHPQE 156
Cdd:cd17648 2 DRVAVVYGDKRLTYRELNERANRLAHYLlsVAEIRPD------DLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 157 ELEYIISDSQSSLLVAGnsfaktleplalklglpcltlppTSNLstldgtdsqeeeaaitdwadrpAMIIYTSGTTGRPK 236
Cdd:cd17648 76 RIQFILEDTGARVVITN-----------------------STDL----------------------AYAIYTSGTTGKPK 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 237 GVLHTHSSIQAMVQCLVSEW--AWTRDDVILhTLPLHHVHGIVNKLLCPLWVGATCIMLPE---FQPQKVWEILLTSKap 311
Cdd:cd17648 111 GVLVEHGSVVNLRTSLSERYfgRDNGDEAVL-FFSNYVFDFFVEQMTLALLNGQKLVVPPDemrFDPDRFYAYINREK-- 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 312 mVNVFMAVPTiyskLIQYYDQHfTQPHVKdfvkavckqriRLMVSGSAaLPLPTLQRWEEITGHTLLERYGMTEIGM-AL 390
Cdd:cd17648 188 -VTYLSGTPS----VLQQYDLA-RLPHLK-----------RVDAAGEE-FTAPVFEKLRSRFAGLIINAYGPTETTVtNH 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 391 SNPLKGP-RIPGAVGSPLPGVEIRIVmsnatnttiveaNHRETRVRSGlegKEGELLVRGPSVFKEYWNKHQETRESF-- 467
Cdd:cd17648 250 KRFFPGDqRFDKSLGRPVRNTKCYVL------------NDAMKRVPVG---AVGELYLGGDGVARGYLNRPELTAERFlp 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 468 ------------TDSGWFKTGDTA-IHKDGVFWIMGRTSVDIiKSGGYKISALEVERHLLAHPAIADVAVIGPPDAIWGQ 534
Cdd:cd17648 315 npfqteqerargRNARLYKTGDLVrWLPSGELEYLGRNDFQV-KIRGQRIEPGEVEAALASYPGVRECAVVAKEDASQAQ 393
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2105456023 535 KVTAvmqlKR--GHRLTLPE------LKIWAREHMAPYIIPTGLVLVEELPRNQMGKVNKKDL 589
Cdd:cd17648 394 SRIQ----KYlvGYYLPEPGhvpesdLLSFLRAKLPRYMVPARLVRLEGIPVTINGKLDVRAL 452
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
219-585 |
1.61e-19 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 93.11 E-value: 1.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 219 ADRPAMIIYTSGTTGRPKGVLHTHSSIQAMVQCLVSEWAWTRDDVILHTLPLHHVHGIVNKLLCPLWVGATCIMLP---- 294
Cdd:PRK06814 792 PDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARIDFSPEDKVFNALPVFHSFGLTGGLVLPLLSGVKVFLYPsplh 871
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 295 -EFQPQKVWEILLTskapmvnVFMAVPTIYSKLIQYydqhftqPHVKDFvkavckQRIRLMVSGSAALPLPTLQRWEEIT 373
Cdd:PRK06814 872 yRIIPELIYDTNAT-------ILFGTDTFLNGYARY-------AHPYDF------RSLRYVFAGAEKVKEETRQTWMEKF 931
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 374 GHTLLERYGMTEIG--MALSNPLKGPriPGAVGSPLPGVEIRIVMsnatnttiVEAnhretrVRSGlegkeGELLVRGPS 451
Cdd:PRK06814 932 GIRILEGYGVTETApvIALNTPMHNK--AGTVGRLLPGIEYRLEP--------VPG------IDEG-----GRLFVRGPN 990
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 452 VFKEYWNK-----HQETREsftdsGWFKTGD-TAIHKDGVFWIMGRTSvDIIKSGGYKISALEVERHLLAHPAIADVAVI 525
Cdd:PRK06814 991 VMLGYLRAenpgvLEPPAD-----GWYDTGDiVTIDEEGFITIKGRAK-RFAKIAGEMISLAAVEELAAELWPDALHAAV 1064
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2105456023 526 GPPDAIWGQKVTAVMQLKRGHRltlPELKIWAREHMAPYI-IPTGLVLVEELPRNQMGKVN 585
Cdd:PRK06814 1065 SIPDARKGERIILLTTASDATR---AAFLAHAKAAGASELmVPAEIITIDEIPLLGTGKID 1122
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
200-483 |
7.37e-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: 90.18 E-value: 7.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 200 LSTLDGTDSQEEEAAITdwADRPAMIIYTSGTTGRPKGVLHTHSSIQAMVQCLVSEWAWTRDD--VILHTLPLHHVHGIV 277
Cdd:cd05921 147 AATPPTAAVDAAFAAVG--PDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFFGEEppVLVDWLPWNHTFGGN 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 278 NKLLCPLWVGATcIMLPEFQP--QKVWEILLTSKAPMVNVFMAVPTIYSKLIQYYDqhftqphvKDfvKAVCK---QRIR 352
Cdd:cd05921 225 HNFNLVLYNGGT-LYIDDGKPmpGGFEETLRNLREISPTVYFNVPAGWEMLVAALE--------KD--EALRRrffKRLK 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 353 LMVSGSAALPLPTLQRWEEI----TGH--TLLERYGMTEIGMALSNPLKGPRIPGAVGSPLPGVEIRIVMSNatnttive 426
Cdd:cd05921 294 LMFYAGAGLSQDVWDRLQALavatVGEriPMMAGLGATETAPTATFTHWPTERSGLIGLPAPGTELKLVPSG-------- 365
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2105456023 427 anhretrvrsgleGKEgELLVRGPSVFKEYWNKHQETRESFTDSGWFKTGDTAIHKD 483
Cdd:cd05921 366 -------------GKY-EVRVKGPNVTPGYWRQPELTAQAFDEEGFYCLGDAAKLAD 408
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
79-589 |
8.65e-19 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 89.66 E-value: 8.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 79 DRLAIIDSSGSHSYKQLYCSSFGLAGRISAAlnsdfGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLYRKHPQEEL 158
Cdd:PRK10946 38 DAIAVICGERQFSYRELNQASDNLACSLRRQ-----GIKPGDTALVQLGNVAEFYITFFALLKLGVAPVNALFSHQRSEL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 159 -EYI--------ISDSQSSLLvAGNSFaktLEPLALKLGLPCLTL----PPTSNLSTLDGTDSQEEEAAITDwADRPAMI 225
Cdd:PRK10946 113 nAYAsqiepallIADRQHALF-SDDDF---LNTLVAEHSSLRVVLllndDGEHSLDDAINHPAEDFTATPSP-ADEVAFF 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 226 IYTSGTTGRPKGVLHTHS----SIQAMVQ-CLVsewawTRDDVILHTLPLHHvhgivN-KLLCP-----LWVGATCIMLP 294
Cdd:PRK10946 188 QLSGGSTGTPKLIPRTHNdyyySVRRSVEiCGF-----TPQTRYLCALPAAH-----NyPMSSPgalgvFLAGGTVVLAP 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 295 EFQPQKVWEILLTSKapmVNVFMAVPTIYSKLIQyydqHFTQPHVKDFVKAvckqrIRLMVSGSAALPLPTLQRWEEITG 374
Cdd:PRK10946 258 DPSATLCFPLIEKHQ---VNVTALVPPAVSLWLQ----AIAEGGSRAQLAS-----LKLLQVGGARLSETLARRIPAELG 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 375 HTLLERYGMTEiGMALSNPLKGP--RIPGAVGSPL-PGVEIRIVMSNATNTTiveanhretrvrsglEGKEGELLVRGPS 451
Cdd:PRK10946 326 CQLQQVFGMAE-GLVNYTRLDDSdeRIFTTQGRPMsPDDEVWVADADGNPLP---------------QGEVGRLMTRGPY 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 452 VFKEYWNKHQETRESFTDSGWFKTGD-TAIHKDGVFWIMGRTSvDIIKSGGYKISALEVERHLLAHPAIADVAVIGPPDA 530
Cdd:PRK10946 390 TFRGYYKSPQHNASAFDANGFYCSGDlVSIDPDGYITVVGREK-DQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDE 468
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 531 IWGQKVTAVMQLKRGhrLTLPELKIWAREH-MAPYIIPTGLVLVEELPRNQMGKVNKKDL 589
Cdd:PRK10946 469 LMGEKSCAFLVVKEP--LKAVQLRRFLREQgIAEFKLPDRVECVDSLPLTAVGKVDKKQL 526
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
59-477 |
4.52e-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: 84.81 E-value: 4.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 59 SAPSMRINQ--KPVFVR---APAFGDR---LAIIDSSGSHSYKQL-------YCSSFGLAGRISAALNSDFGGLEGKRIS 123
Cdd:cd17632 18 RRPGLRLAQiiATVMTGyadRPALGQRateLVTDPATGRTTLRLLprfetitYAELWERVGAVAAAHDPEQPVRPGDFVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 124 FLCANDASYTVAQWAAWMSGGTAVPLYRKHPQEELEYIISDSQSSLLVAGnsfAKTLePLALKLGLPCLT---------- 193
Cdd:cd17632 98 VLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLAVS---AEHL-DLAVEAVLEGGTpprlvvfdhr 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 194 ----------------LPPTSNLSTLDGTDSQEEEAA-------ITDWADRPAMIIYTSGTTGRPKGVLHTHSSIQAMVQ 250
Cdd:cd17632 174 pevdahraalesarerLAAVGIPVTTLTLIAVRGRDLppaplfrPEPDDDPLALLIYTSGSTGTPKGAMYTERLVATFWL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 251 CLVSEWAWTRDDVI-LHTLPLHHVHGiVNKLLCPLWVGATCIMLPEFQPQKVWEILltSKAPMVNVFMaVPTIYSKLIQY 329
Cdd:cd17632 254 KVSSIQDIRPPASItLNFMPMSHIAG-RISLYGTLARGGTAYFAAASDMSTLFDDL--ALVRPTELFL-VPRVCDMLFQR 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 330 Y----DQHFTQPH----VKDFVKAVCKQRI---RLM--VSGSAALPlPTLQRW-EEITGHTLLERYGMTEIGMALSNplk 395
Cdd:cd17632 330 YqaelDRRSVAGAdaetLAERVKAELRERVlggRLLaaVCGSAPLS-AEMKAFmESLLDLDLHDGYGSTEAGAVILD--- 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 396 gpripGAVGSPlPGVEIRIVmsnatntTIVEANHretrVRSGLEGKEGELLVRGPSVFKEYWNKHQETRESFTDSGWFKT 475
Cdd:cd17632 406 -----GVIVRP-PVLDYKLV-------DVPELGY----FRTDRPHPRGELLVKTDTLFPGYYKRPEVTAEVFDEDGFYRT 468
|
..
gi 2105456023 476 GD 477
Cdd:cd17632 469 GD 470
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
508-583 |
9.33e-17 |
|
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.
Pssm-ID: 463804 [Multi-domain] Cd Length: 76 Bit Score: 74.89 E-value: 9.33e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2105456023 508 EVERHLLAHPAIADVAVIGPPDAIWGQKVTAVMQLKRGHRLTLPELKIWAREHMAPYIIPTGLVLVEELPRNQMGK 583
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
220-589 |
1.39e-16 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 82.48 E-value: 1.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 220 DRPAMIIYTSGTTGRPKGVLHTHSSIQAMVQcLVSEWAWTRD-DVILHTLPLHHVHGIVNKLLCPLWVGATCIMLPEFQP 298
Cdd:cd05937 87 DDPAILIYTSGTTGLPKAAAISWRRTLVTSN-LLSHDLNLKNgDRTYTCMPLYHGTAAFLGACNCLMSGGTLALSRKFSA 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 299 QKVWEILLTSKApmvNVFMAVptiySKLIQY--------YDQhftqphvkdfvkavcKQRIRlMVSGSAALPlptlQRWE 370
Cdd:cd05937 166 SQFWKDVRDSGA---TIIQYV----GELCRYllstppspYDR---------------DHKVR-VAWGNGLRP----DIWE 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 371 EITghtllERYGMTEIG---------MALSNPLKGPRIPGAVGspLPGVEIRIVMSNatNTTIVEANHrET-----RVRS 436
Cdd:cd05937 219 RFR-----ERFNVPEIGefyaategvFALTNHNVGDFGAGAIG--HHGLIRRWKFEN--QVVLVKMDP-ETddpirDPKT 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 437 GL-----EGKEGELLVRGP----SVFKEYWNKHQETRESF-TD-----SGWFKTGDTAIH-KDGVFWIMGRTSvDIIKSG 500
Cdd:cd05937 289 GFcvrapVGEPGEMLGRVPfknrEAFQGYLHNEDATESKLvRDvfrkgDIYFRTGDLLRQdADGRWYFLDRLG-DTFRWK 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 501 GYKISALEVERHLLAHPAIADVAVIG---PPDAiwGQKVTAVMQLKRGHR----LTLPELKIWAREHMAPYIIPTGLVLV 573
Cdd:cd05937 368 SENVSTTEVADVLGAHPDIAEANVYGvkvPGHD--GRAGCAAITLEESSAvpteFTKSLLASLARKNLPSYAVPLFLRLT 445
|
410
....*....|....*.
gi 2105456023 574 EELPRNQMGKVNKKDL 589
Cdd:cd05937 446 EEVATTDNHKQQKGVL 461
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
219-511 |
2.01e-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: 82.15 E-value: 2.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 219 ADRPAMIIYTSGTTGRPKGVLHTHSSIQAMVQCLVSEWAWTRDDVILHTLPLHHVHGIVNKLLCPLWVGATCIMLPefqp 298
Cdd:cd05908 105 ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGMNQYLMP---- 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 299 qkvweilltskapmVNVFMAVPTIYSKLIQYYD------QHFTQPHVKDFVKA-----VCKQRIRLMVSGSAALpLPTLq 367
Cdd:cd05908 181 --------------TRLFIRRPILWLKKASEHKativssPNFGYKYFLKTLKPekandWDLSSIRMILNGAEPI-DYEL- 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 368 rWEEITGH---------TLLERYGMTEIGMALSNP----------------LKGPRIPG------------AVGSPLPGV 410
Cdd:cd05908 245 -CHEFLDHmskyglkrnAILPVYGLAEASVGASLPkaqspfktitlgrrhvTHGEPEPEvdkkdsecltfvEVGKPIDET 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 411 EIRIVMsnatnttivEANHretrvrsGL-EGKEGELLVRGPSVFKEYWNKHQETRESFTDSGWFKTGDTAIHKDGVFWIM 489
Cdd:cd05908 324 DIRICD---------EDNK-------ILpDGYIGHIQIRGKNVTPGYYNNPEATAKVFTDDGWLKTGDLGFIRNGRLVIT 387
|
330 340
....*....|....*....|..
gi 2105456023 490 GRTSvDIIKSGGYKISALEVER 511
Cdd:cd05908 388 GREK-DIIFVNGQNVYPHDIER 408
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
222-591 |
3.03e-16 |
|
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: 81.71 E-value: 3.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 222 PAMIIYTSGTTGRPKGVLHTH--SSIQAMVQCLVSEWAWTRDDVILHTLPLHHVHGivnklLCPLWV----GATCIMLPE 295
Cdd:cd05915 155 ACGMAYTTGTTGLPKGVVYSHraLVLHSLAASLVDGTALSEKDVVLPVVPMFHVNA-----WCLPYAatlvGAKQVLPGP 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 296 FQPQKV-WEILLTSKapmVNVFMAVPTIYSKLiqyydqhftqPHVKDFVKAVCKQRIRLMVSGSAalPLPTLQRWEEITG 374
Cdd:cd05915 230 RLDPASlVELFDGEG---VTFTAGVPTVWLAL----------ADYLESTGHRLKTLRRLVVGGSA--APRSLIARFERMG 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 375 HTLLERYGMTEIGMALSNPLKGPRipgavGSPLPGVE-IRIVMSNATN----------TTIVEANHRETRVRSglegkeg 443
Cdd:cd05915 295 VEVRQGYGLTETSPVVVQNFVKSH-----LESLSEEEkLTLKAKTGLPiplvrlrvadEEGRPVPKDGKALGE------- 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 444 eLLVRGPSVFKEYWNKHQETRESFTDSGWFKTGDTA-IHKDGVFWIMGRtSVDIIKSGGYKISALEVERHLLAHPAIADV 522
Cdd:cd05915 363 -VQLKGPWITGGYYGNEEATRSALTPDGFFRTGDIAvWDEEGYVEIKDR-LKDLIKSGGEWISSVDLENALMGHPKVKEA 440
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2105456023 523 AVIGPPDAIWGQKVTAVMQLKRGHRLTLPELKIWAREHMAPYIIPTGLVLVEELPRNQMGKVnKKDLLR 591
Cdd:cd05915 441 AVVAIPHPKWQERPLAVVVPRGEKPTPEELNEHLLKAGFAKWQLPDAYVFAEEIPRTSAGKF-LKRALR 508
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
223-589 |
5.76e-15 |
|
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: 77.51 E-value: 5.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 223 AMIIYTSGTTGRPKGVLHTHSSIQAMVQCLVSEWAWTRDDVILHTLPLHHVHGIVNKLLCpLWVGATCIMLP---EFQPQ 299
Cdd:cd17654 121 AYVIHTSGTTGTPKIVAVPHKCILPNIQHFRSLFNITSEDILFLTSPLTFDPSVVEIFLS-LSSGATLLIVPtsvKVLPS 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 300 KVWEILLtsKAPMVNVFMAVPTIYSKliqyydqhFTQPHVKDFVKAVCKQrIRLMVSGSAALPLPTLQR-W-EEITGHTL 377
Cdd:cd17654 200 KLADILF--KRHRITVLQATPTLFRR--------FGSQSIKSTVLSATSS-LRVLALGGEPFPSLVILSsWrGKGNRTRI 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 378 LERYGMTEIGM-ALSNPLKGPRIPGAVGSPLPGVEIRIVmsnatnttivEANHRETRVRSGLEGKEGELLVRGPSVFKEy 456
Cdd:cd17654 269 FNIYGITEVSCwALAYKVPEEDSPVQLGSPLLGTVIEVR----------DQNGSEGTGQVFLGGLNRVCILDDEVTVPK- 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 457 wnkhqetresftdSGWFKTGDTAIHKDGVFWIMGRTSvDIIKSGGYKISALEVERHLLAHPAIADVAVigppdaiWGQKV 536
Cdd:cd17654 338 -------------GTMRATGDFVTVKDGELFFLGRKD-SQIKRRGKRINLDLIQQVIESCLGVESCAV-------TLSDQ 396
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 2105456023 537 TAVMQLKRGHRLTLPELKIWAREHMAPYIIPTGLVLVEELPRNQMGKVNKKDL 589
Cdd:cd17654 397 QRLIAFIVGESSSSRIHKELQLTLLSSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
191-508 |
9.38e-15 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 77.16 E-value: 9.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 191 CLTLPPTSNLSTLDGTDSQEEEAAItdwadrpamIIYTSGTTGRPKGVLHTHSSIQAMVQCLVSEWAWTRDDVILHTLPL 270
Cdd:PRK06334 163 YMSIPFEWLMRWFGVSDKDPEDVAV---------ILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSFLPP 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 271 HHVHGIVNKLLCPLWVGATCIM-LPEFQPQKVWEILLTSKapmVNVFMAVPTIYSKLIQYYDQHFTqphvkdfvkavCKQ 349
Cdd:PRK06334 234 FHAYGFNSCTLFPLLSGVPVVFaYNPLYPKKIVEMIDEAK---VTFLGSTPVFFDYILKTAKKQES-----------CLP 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 350 RIRLMVSGSAALPLPTLQRWEEITGH-TLLERYGMTEIGMALS-NPLKGPRIPGAVGSPLPGVEIRIVmsnatnttivea 427
Cdd:PRK06334 300 SLRFVVIGGDAFKDSLYQEALKTFPHiQLRQGYGTTECSPVITiNTVNSPKHESCVGMPIRGMDVLIV------------ 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 428 nHRETRVRSGlEGKEGELLVRGPSVFKEYWNKHQEtrESFTDSG---WFKTGDTA-IHKDGVFWIMGRTSvDIIKSGGYK 503
Cdd:PRK06334 368 -SEETKVPVS-SGETGLVLTRGTSLFSGYLGEDFG--QGFVELGgetWYVTGDLGyVDRHGELFLKGRLS-RFVKIGAEM 442
|
....*..
gi 2105456023 504 IS--ALE 508
Cdd:PRK06334 443 VSleALE 449
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
75-491 |
1.14e-14 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 77.37 E-value: 1.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 75 PAFGDRlAIIDSSGSHSYKQLYCSSFGLAGRISAALNSdFGGLEGKRISFLCANDASYTVAQWAAWMSGGTAVPLYRKHP 154
Cdd:PLN02614 62 PMLGRR-EIVDGKPGKYVWQTYQEVYDIVIKLGNSLRS-VGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLG 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 155 QEELEYIISDSQSSLlvagnSFAKTLEPLALKLGLPCLTLPPTSNLSTLDGTDSQEEEA-----AITDWAD--------- 220
Cdd:PLN02614 140 AGAVEFIISHSEVSI-----VFVEEKKISELFKTCPNSTEYMKTVVSFGGVSREQKEEAetfglVIYAWDEflklgegkq 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 221 ------RPA---MIIYTSGTTGRPKGVLHTHSSIQAMVQCLV-----SEWAWTRDDVILHTLPLHHVHGIVNKLlCPLWV 286
Cdd:PLN02614 215 ydlpikKKSdicTIMYTSGTTGDPKGVMISNESIVTLIAGVIrllksANAALTVKDVYLSYLPLAHIFDRVIEE-CFIQH 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 287 GATCimlpEFQPQKVwEILLTSKAPMV-NVFMAVPTI----YSKLIQ-----------YYDQHFT---------QPHVK- 340
Cdd:PLN02614 294 GAAI----GFWRGDV-KLLIEDLGELKpTIFCAVPRVldrvYSGLQKklsdggflkkfVFDSAFSykfgnmkkgQSHVEa 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 341 -----DFVKAVCKQ----RIRLMVSGSAALPLPTLQRWEEITGHTLLERYGMTE--IGMALSNPLKGPRIpGAVGSPLPG 409
Cdd:PLN02614 369 splcdKLVFNKVKQglggNVRIILSGAAPLASHVESFLRVVACCHVLQGYGLTEscAGTFVSLPDELDML-GTVGPPVPN 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 410 VEIRIVMSNATNTTIVEANHRetrvrsglegkeGELLVRGPSVFKEYWNKHQETRESFTDsGWFKTGDTA-IHKDGVFWI 488
Cdd:PLN02614 448 VDIRLESVPEMEYDALASTPR------------GEICIRGKTLFSGYYKREDLTKEVLID-GWLHTGDVGeWQPNGSMKI 514
|
...
gi 2105456023 489 MGR 491
Cdd:PLN02614 515 IDR 517
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
225-526 |
1.23e-14 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 77.16 E-value: 1.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 225 IIYTSGTTGRPKGVLHTHSSIQAMVQ----CLVS-EWAWTRDDVILHTLPLHHV-------------------HGIVNKL 280
Cdd:PLN02430 225 IMYTSGTSGDPKGVVLTHEAVATFVRgvdlFMEQfEDKMTHDDVYLSFLPLAHIldrmieeyffrkgasvgyyHGDLNAL 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 281 ------LCP-LWVGATCIM----------LPEFQPQK--VWEILLTSKAPMVNvfmavptiyskliQYYDQHFTQPhVKD 341
Cdd:PLN02430 305 rddlmeLKPtLLAGVPRVFerihegiqkaLQELNPRRrlIFNALYKYKLAWMN-------------RGYSHKKASP-MAD 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 342 F-----VKAVCKQRIRLMVSGSAALPlPTLQRWEEITGHT-LLERYGMTEI--GMALSNPLKGPRIpGAVGSPLPGVEIR 413
Cdd:PLN02430 371 FlafrkVKAKLGGRLRLLISGGAPLS-TEIEEFLRVTSCAfVVQGYGLTETlgPTTLGFPDEMCML-GTVGAPAVYNELR 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 414 IVMSNATNTTIVEANHRetrvrsglegkeGELLVRGPSVFKEYWNKHQETRESFTDsGWFKTGDTA-IHKDGVFWIMGRT 492
Cdd:PLN02430 449 LEEVPEMGYDPLGEPPR------------GEICVRGKCLFSGYYKNPELTEEVMKD-GWFHTGDIGeILPNGVLKIIDRK 515
|
330 340 350
....*....|....*....|....*....|....*
gi 2105456023 493 SvDIIK-SGGYKISALEVERHLLAHPAIADVAVIG 526
Cdd:PLN02430 516 K-NLIKlSQGEYVALEYLENVYGQNPIVEDIWVYG 549
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
23-576 |
6.20e-14 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 74.91 E-value: 6.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 23 RTLPHWKASFHRTFSPSEPRRWLLGTVIHRRAHgwtsapsmrinqkpvfvrapAFGDRLAIIDSSGSHSYKQLYcssfGL 102
Cdd:PRK08279 16 PDLPGILRGLKRTALITPDSKRSLGDVFEEAAA--------------------RHPDRPALLFEDQSISYAELN----AR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 103 AGRISAALNSDfgGL-EGKRISFLCANDASYtVAQWAAWMSGGTAVPLYRKHPQEE-LEYIISDSQSSLLVAGNSFAKTL 180
Cdd:PRK08279 72 ANRYAHWAAAR--GVgKGDVVALLMENRPEY-LAAWLGLAKLGAVVALLNTQQRGAvLAHSLNLVDAKHLIVGEELVEAF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 181 E---------PLALKLGLPCLTLPPT-SNL---STLDGTDSQEEEAAITdwADRPAMIIYTSGTTGRPKGVLHTHSSIQA 247
Cdd:PRK08279 149 EearadlarpPRLWVAGGDTLDDPEGyEDLaaaAAGAPTTNPASRSGVT--AKDTAFYIYTSGTTGLPKAAVMSHMRWLK 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 248 MVQCLVSEWAWTRDDVILHTLPLHHVHGIVNKLLCPLWVGATCIMLPEFQPQKVWEILLTSKAPMvnvFMAVPTIYSKLI 327
Cdd:PRK08279 227 AMGGFGGLLRLTPDDVLYCCLPLYHNTGGTVAWSSVLAAGATLALRRKFSASRFWDDVRRYRATA---FQYIGELCRYLL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 328 QYYDQHFTQPHvkdfvkavckqRIRLMVsGSAALPlptlQRWEEITG----HTLLERYGMTEIGMALSNPLKgprIPGAV 403
Cdd:PRK08279 304 NQPPKPTDRDH-----------RLRLMI-GNGLRP----DIWDEFQQrfgiPRILEFYAASEGNVGFINVFN---FDGTV 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 404 G-SPLPGVE-IRIV-MSNATNTTIVEANHRETRVRSGlegkE-GELLV----RGPsvFKEYWNKhQET-----RESFTDs 470
Cdd:PRK08279 365 GrVPLWLAHpYAIVkYDVDTGEPVRDADGRCIKVKPG----EvGLLIGritdRGP--FDGYTDP-EASekkilRDVFKK- 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 471 G--WFKTGD-TAIHKDGVFWImgrtsVDII------KsgGYKISALEVERHLLAHPAIADVAVIGP--PDAIwGQKVTAV 539
Cdd:PRK08279 437 GdaWFNTGDlMRDDGFGHAQF-----VDRLgdtfrwK--GENVATTEVENALSGFPGVEEAVVYGVevPGTD-GRAGMAA 508
|
570 580 590
....*....|....*....|....*....|....*..
gi 2105456023 540 MQLKRGHRLTLPELKIWAREHMAPYIIPTGLVLVEEL 576
Cdd:PRK08279 509 IVLADGAEFDLAALAAHLYERLPAYAVPLFVRLVPEL 545
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
142-589 |
1.70e-13 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 74.05 E-value: 1.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 142 SGGTAVPLYRKHPQEELEYIISDSQSSLLVAgnSFAKTLEPLALKLGLPCLTLPPTSNLSTLDGTDSQEEEAAITDWADR 221
Cdd:PRK05691 3793 AGAGYLPLDPGLPAQRLQRIIELSRTPVLVC--SAACREQARALLDELGCANRPRLLVWEEVQAGEVASHNPGIYSGPDN 3870
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 222 PAMIIYTSGTTGRPKGVLHTHSSIQAMVQCLVSEWAWTRDDVILHTLPLHHVHGIVNKLLCPLWvGATCIMLPE---FQP 298
Cdd:PRK05691 3871 LAYVIYTSGSTGLPKGVMVEQRGMLNNQLSKVPYLALSEADVIAQTASQSFDISVWQFLAAPLF-GARVEIVPNaiaHDP 3949
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 299 QKvweILLTSKAPMVNVFMAVPTiyskLIQyydQHFTQPHVKdfvkavcKQRIRLMVSGSAALPlPTL-----QRWEEIT 373
Cdd:PRK05691 3950 QG---LLAHVQAQGITVLESVPS----LIQ---GMLAEDRQA-------LDGLRWMLPTGEAMP-PELarqwlQRYPQIG 4011
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 374 ghtLLERYGMTEIgmalSNPLKGPRIPGAV--GSPLPgveirivMSNATNttiveaNHRETRVRSGLE----GKEGELLV 447
Cdd:PRK05691 4012 ---LVNAYGPAEC----SDDVAFFRVDLAStrGSYLP-------IGSPTD------NNRLYLLDEALElvplGAVGELCV 4071
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 448 RGPSVFKEYWNKHQETRESFTDSGW-------FKTGDTAIH-KDGVFWIMGRtsVD-IIKSGGYKISALEVERHLLAHPA 518
Cdd:PRK05691 4072 AGTGVGRGYVGDPLRTALAFVPHPFgapgerlYRTGDLARRrSDGVLEYVGR--IDhQVKIRGYRIELGEIEARLHEQAE 4149
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2105456023 519 IADVAVI---GPP-DAIWGQKVTAVMQLKRGHRLTlpELKIWAREHMAPYIIPTGLVLVEELPRNQMGKVNKKDL 589
Cdd:PRK05691 4150 VREAAVAvqeGVNgKHLVGYLVPHQTVLAQGALLE--RIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKAL 4222
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
165-303 |
6.44e-13 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 71.17 E-value: 6.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 165 SQSSLLVAGNSFAKTLEPLALKL---GLPCLTLPPTSN----LSTLDGTDSQEEEAAITDWADR-----PAMIIYTSGTT 232
Cdd:cd05938 77 CGAKVLVVAPELQEAVEEVLPALradGVSVWYLSHTSNtegvISLLDKVDAASDEPVPASLRAHvtiksPALYIYTSGTT 156
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2105456023 233 GRPKGVLHTHSSIQAMvQCLVSEWAWTRDDVILHTLPLHHVHGIVNKLLCPLWVGATCIMLPEFQPQKVWE 303
Cdd:cd05938 157 GLPKAARISHLRVLQC-SGFLSLCGVTADDVIYITLPLYHSSGFLLGIGGCIELGATCVLKPKFSASQFWD 226
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
222-552 |
2.42e-12 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 69.59 E-value: 2.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 222 PAMIIYTSGTTGRPKGVL-----HT---HSSIQAMVQCLVSEWAWTRDD---VILHTlplHHVHGivnkllcPLWVGATC 290
Cdd:PRK10524 235 PSYILYTSGTTGKPKGVQrdtggYAvalATSMDTIFGGKAGETFFCASDigwVVGHS---YIVYA-------PLLAGMAT 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 291 IM---LPeFQPQK--VWEILLTSKapmVNVFMAVPTIYsKLIQYYDQHFTQPHVKDFVKAvckqrirLMVSGSaalPL-- 363
Cdd:PRK10524 305 IMyegLP-TRPDAgiWWRIVEKYK---VNRMFSAPTAI-RVLKKQDPALLRKHDLSSLRA-------LFLAGE---PLde 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 364 PTLQRWEEITGHTLLERYGMTEIG---MALSNPL-KGPRIPGAVGSPLPGVEIRIvmsnatnttIVEANHRETRVrsgle 439
Cdd:PRK10524 370 PTASWISEALGVPVIDNYWQTETGwpiLAIARGVeDRPTRLGSPGVPMYGYNVKL---------LNEVTGEPCGP----- 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 440 GKEGELLVRGP---SVFKEYWNkhQETResFTDSGW-------FKTGDTAIH-KDGVFWIMGRTSvDIIKSGGYKISALE 508
Cdd:PRK10524 436 NEKGVLVIEGPlppGCMQTVWG--DDDR--FVKTYWslfgrqvYSTFDWGIRdADGYYFILGRTD-DVINVAGHRLGTRE 510
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 2105456023 509 VERHLLAHPAIADVAVIGPPDAIWGQKVTAVMQLKRGHRLTLPE 552
Cdd:PRK10524 511 IEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPKDSDSLADRE 554
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
223-528 |
4.51e-12 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 68.99 E-value: 4.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 223 AMIIYTSGTTGRPKGVLHTHSSIQAM---VQCLVSEWAwtRDDVILHTLPLHHVhgivnkllcpLWVGATCIML------ 293
Cdd:PLN02387 253 AVIMYTSGSTGLPKGVMMTHGNIVATvagVMTVVPKLG--KNDVYLAYLPLAHI----------LELAAESVMAavgaai 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 294 ----PEFQPQKVWEILLTSK--APMVN--VFMAVPTIYSKL--------------------IQYY--------------- 330
Cdd:PLN02387 321 gygsPLTLTDTSNKIKKGTKgdASALKptLMTAVPAILDRVrdgvrkkvdakgglakklfdIAYKrrlaaiegswfgawg 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 331 -DQHFTQPHVKDFVKAVCKQRIRLMVSGSAALPLPTlQRWEEIT-GHTLLERYGMTEI--GMALSNPlKGPRIpGAVGSP 406
Cdd:PLN02387 401 lEKLLWDALVFKKIRAVLGGRIRFMLSGGAPLSGDT-QRFINIClGAPIGQGYGLTETcaGATFSEW-DDTSV-GRVGPP 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 407 LPGVEIRIVMSNATNTTIveanhretrvrSGLEGKEGELLVRGPSVFKEYWNKHQETRESFT----DSGWFKTGDTA-IH 481
Cdd:PLN02387 478 LPCCYVKLVSWEEGGYLI-----------SDKPMPRGEIVIGGPSVTLGYFKNQEKTDEVYKvderGMRWFYTGDIGqFH 546
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 2105456023 482 KDGVFWIMGRTSvDIIK--SGGYkISALEVERHLLAHPAIADVAVIGPP 528
Cdd:PLN02387 547 PDGCLEIIDRKK-DIVKlqHGEY-VSLGKVEAALSVSPYVDNIMVHADP 593
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
222-594 |
6.53e-12 |
|
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 67.76 E-value: 6.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 222 PAMIIYTSGTTGRPKGVLHTHSSIQAMVQCLVSEWAWTRDDVILHTLPLHHVHGIVNKLLCPLWVGATCIMLPEFQPQKV 301
Cdd:cd05940 83 AALYIYTSGTTGLPKAAIISHRRAWRGGAFFAGSGGALPSDVLYTCLPLYHSTALIVGWSACLASGATLVIRKKFSASNF 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 302 WEILLTSKAPMvnvfmaVPTIySKLIQYYdqhFTQPHvKDFVKavcKQRIRlMVSGSAALPlptlQRWEEITGH----TL 377
Cdd:cd05940 163 WDDIRKYQATI------FQYI-GELCRYL---LNQPP-KPTER---KHKVR-MIFGNGLRP----DIWEEFKERfgvpRI 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 378 LERYGMTEIGMALSNPlkgPRIPGAVGsplpgvEIRIVMSNATNTTIVEANHrET----RVRSGL-----EGKEGELLVR 448
Cdd:cd05940 224 AEFYAATEGNSGFINF---FGKPGAIG------RNPSLLRKVAPLALVKYDL-ESgepiRDAEGRcikvpRGEPGLLISR 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 449 --GPSVFKEYWNKHQETRESFTD-----SGWFKTGD-TAIHKDGVFWIMGRTSvDIIKSGGYKISALEVERHLLAHPAIA 520
Cdd:cd05940 294 inPLEPFDGYTDPAATEKKILRDvfkkgDAWFNTGDlMRLDGEGFWYFVDRLG-DTFRWKGENVSTTEVAAVLGAFPGVE 372
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2105456023 521 DVAVIGP--PDAIwGQKVTAVMQLKRGHRLTLPELKIWAREHMAPYIIPTGLVLVEELPRNQMGKVNKKDLLRHFF 594
Cdd:cd05940 373 EANVYGVqvPGTD-GRAGMAAIVLQPNEEFDLSALAAHLEKNLPGYARPLFLRLQPEMEITGTFKQQKVDLRNEGF 447
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
133-511 |
3.85e-11 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 65.79 E-value: 3.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 133 TVAQwAAWMSGGTAVPLYRKHPQEELEYIISDS-------QSSLLVAGNSFaKTLEPLALKLGLPCLTLpptsnlSTLDG 205
Cdd:PRK07768 69 PTAQ-GLWMRGASLTMLHQPTPRTDLAVWAEDTlrvigmiGAKAVVVGEPF-LAAAPVLEEKGIRVLTV------ADLLA 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 206 TDSQEEEAaITDwaDRPAMIIYTSGTTGRPKGVLHTHSSIQAMVQCLVSEWAWTRD-DVILHTLPLHHVHGIVNKLLCPL 284
Cdd:PRK07768 141 ADPIDPVE-TGE--DDLALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEFDVEtDVMVSWLPLFHDMGMVGFLTVPM 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 285 WVGATcimlpefqpqkvweilLTSKAPMvnVFMAVPTIYSKLIQYYdqHFTQPHVKDFVKAVCKQR-------------- 350
Cdd:PRK07768 218 YFGAE----------------LVKVTPM--DFLRDPLLWAELISKY--RGTMTAAPNFAYALLARRlrrqakpgafdlss 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 351 IRLMVSGSAALPLPTLQRWEEITG------HTLLERYGMTEIGMALSNPLKG--------------------PRIPGAV- 403
Cdd:PRK07768 278 LRFALNGAEPIDPADVEDLLDAGArfglrpEAILPAYGMAEATLAVSFSPCGaglvvdevdadllaalrravPATKGNTr 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 404 -----GSPLPGVEIRIVMSNATNTTiveanhrETRVrsglegkeGELLVRGPSVFKEYwnkhqETRESFT----DSGWFK 474
Cdd:PRK07768 358 rlatlGPPLPGLEVRVVDEDGQVLP-------PRGV--------GVIELRGESVTPGY-----LTMDGFIpaqdADGWLD 417
|
410 420 430
....*....|....*....|....*....|....*...
gi 2105456023 475 TGDTA-IHKDGVFWIMGRTSvDIIKSGGYKISALEVER 511
Cdd:PRK07768 418 TGDLGyLTEEGEVVVCGRVK-DVIIMAGRNIYPTDIER 454
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
92-541 |
7.74e-11 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 64.64 E-value: 7.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 92 YKQLYCSSFGLAGRISAAlnsdfgGLE-GKRISFLCANDASYTVAQWAAWMSGGTAVPLY-------RKHPQEELEYIIS 163
Cdd:PRK09192 52 YQTLRARAEAGARRLLAL------GLKpGDRVALIAETDGDFVEAFFACQYAGLVPVPLPlpmgfggRESYIAQLRGMLA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 164 DSQSSLLVAGNSFAKTLEPLALKLGLPcltlpptsnlSTLDGTDSQEEEAAITDWA----DRPAMIIYTSGTTGRPKGVL 239
Cdd:PRK09192 126 SAQPAAIITPDELLPWVNEATHGNPLL----------HVLSHAWFKALPEADVALPrptpDDIAYLQYSSGSTRFPRGVI 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 240 HTHSSIQAMVQclvsewAWTRD-------DVILHTLPLHHVHGIVNKLLCPLWVGATCIMLP--EF--QPQkVWeILLTS 308
Cdd:PRK09192 196 ITHRALMANLR------AISHDglkvrpgDRCVSWLPFYHDMGLVGFLLTPVATQLSVDYLPtrDFarRPL-QW-LDLIS 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 309 KAPmvnvfmavPTI-YSKLIQYydqhftqphvkdfvkAVCKQRIRlmvsgSAALPLPTLQRW-------EEITGHTL--- 377
Cdd:PRK09192 268 RNR--------GTIsYSPPFGY---------------ELCARRVN-----SKDLAELDLSCWrvagigaDMIRPDVLhqf 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 378 --------------LERYGMTEIGMALS-NPL-KGPRI--------------------PGAV------GSPLPGVEIRIV 415
Cdd:PRK09192 320 aeafapagfddkafMPSYGLAEATLAVSfSPLgSGIVVeevdrdrleyqgkavapgaeTRRVrtfvncGKALPGHEIEIR 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 416 MSNATnttivEANHRETrvrsglegkeGELLVRGPSVFKEYWNKhQETRESFTDSGWFKTGDTAIHKDGVFWIMGRTSvD 495
Cdd:PRK09192 400 NEAGM-----PLPERVV----------GHICVRGPSLMSGYFRD-EESQDVLAADGWLDTGDLGYLLDGYLYITGRAK-D 462
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 2105456023 496 IIKSGGYKISALEVERHLLAHPAI--ADVAVIGPPDAIwGQKVTAVMQ 541
Cdd:PRK09192 463 LIIINGRNIWPQDIEWIAEQEPELrsGDAAAFSIAQEN-GEKIVLLVQ 509
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
132-491 |
3.68e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 59.57 E-value: 3.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 132 YTVAQWAAWMSGGTAVPL---YRKHPQEELEYIISDSQSSLL-----VAGNsFAKTLEPLALKlglpclTLPPTSNLSTL 203
Cdd:PRK05850 72 YIVAFLGALQAGLIAVPLsvpQGGAHDERVSAVLRDTSPSVVlttsaVVDD-VTEYVAPQPGQ------SAPPVIEVDLL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 204 DgTDSQEEEAAITDWADRPAMIIYTSGTTGRPKGVLHTHSSIQAMVQCLVSEW------AWTRDDVILHTLPLHHVHGIV 277
Cdd:PRK05850 145 D-LDSPRGSDARPRDLPSTAYLQYTSGSTRTPAGVMVSHRNVIANFEQLMSDYfgdtggVPPPDTTVVSWLPFYHDMGLV 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 278 NKLLCPLWVGatcimlpefqpqkvWEILLTSkaPMVnvFMAVPTIYSKLIQYYDQHFTQPHVKDFVKAVCKQR------- 350
Cdd:PRK05850 224 LGVCAPILGG--------------CPAVLTS--PVA--FLQRPARWMQLLASNPHAFSAAPNFAFELAVRKTSdddmagl 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 351 ----IRLMVSGSAALPLPTLQRWEE------ITGHTLLERYGMTE--IGMALSNPLKGPRI-----------------PG 401
Cdd:PRK05850 286 dlggVLGIISGSERVHPATLKRFADrfapfnLRETAIRPSYGLAEatVYVATREPGQPPESvrfdyeklsaghakrceTG 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 402 AvGSPLpgveIRIVMSNATNTTIVEAnhrETRVRSGlEGKEGELLVRGPSVFKEYWNKHQETRESF----------TDSG 471
Cdd:PRK05850 366 G-GTPL----VSYGSPRSPTVRIVDP---DTCIECP-AGTVGEIWVHGDNVAAGYWQKPEETERTFgatlvdpspgTPEG 436
|
410 420
....*....|....*....|.
gi 2105456023 472 -WFKTGDTAIHKDGVFWIMGR 491
Cdd:PRK05850 437 pWLRTGDLGFISEGELFIVGR 457
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
222-584 |
7.23e-09 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 58.60 E-value: 7.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 222 PAMIIYTSGTTGRPKGVLHTHSSiqAMVqCLVSEWAWTRDDVILHTLPLHH------VHGIVNKLLCplwVGATCIML-- 293
Cdd:PTZ00237 256 PLYILYTSGTTGNSKAVVRSNGP--HLV-GLKYYWRSIIEKDIPTVVFSHSsigwvsFHGFLYGSLS---LGNTFVMFeg 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 294 ----PEFQPQKVWEILLTSKapmVNVFMAVPTIYSKLIQYyDQHFTQPHVK-DFvkavckQRIRLMVSGSAALPLPTLQR 368
Cdd:PTZ00237 330 giikNKHIEDDLWNTIEKHK---VTHTLTLPKTIRYLIKT-DPEATIIRSKyDL------SNLKEIWCGGEVIEESIPEY 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 369 WEEITGHTLLERYGMTEIGMALSNPLKGPRIP-GAVGSPLPGVEIRIVMSnatnttiveanhretrvrsglEGKE----- 442
Cdd:PTZ00237 400 IENKLKIKSSRGYGQTEIGITYLYCYGHINIPyNATGVPSIFIKPSILSE---------------------DGKElnvne 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 443 -GEL---LVRGPSVFKEYWNKHQETRESFTD-SGWFKTGDTA-IHKDGVFWIMGRtSVDIIKSGGYKISALEVERHLLAH 516
Cdd:PTZ00237 459 iGEVafkLPMPPSFATTFYKNDEKFKQLFSKfPGYYNSGDLGfKDENGYYTIVSR-SDDQIKISGNKVQLNTIETSILKH 537
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2105456023 517 PAIADVAVIGPPDAIWGQKVTAVMQLKRG---HRLTLPELK----IWAREHMAPYIIPTGLVLVEELPRNQMGKV 584
Cdd:PTZ00237 538 PLVLECCSIGIYDPDCYNVPIGLLVLKQDqsnQSIDLNKLKneinNIITQDIESLAVLRKIIIVNQLPKTKTGKI 612
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
222-511 |
1.48e-07 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 54.39 E-value: 1.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 222 PAMIIYTSGTTGRPKGVLHTH----SSIQAMVQCLVSEWAwtrDDVILHTLPLHHVHGIVNkLLCPLWVGATCIMLPE-- 295
Cdd:PRK05851 154 PAVLQGTAGSTGTPRTAILSPgavlSNLRGLNARVGLDAA---TDVGCSWLPLYHDMGLAF-LLTAALAGAPLWLAPTta 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 296 FQ--PQKVWEILLTSKAPMVnvfmAVPTIYSKLIQYYdqhftqphvKDFVKAVCKQRIRLMVSGSAALPLPTLQRWEEIT 373
Cdd:PRK05851 230 FSasPFRWLSWLSDSRATLT----AAPNFAYNLIGKY---------ARRVSDVDLGALRVALNGGEPVDCDGFERFATAM 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 374 GH------TLLERYGMTEIGMALSNPLKG---------------PRIPGAVGSPLPGVEIRIVMSNAtnttiveanhret 432
Cdd:PRK05851 297 APfgfdagAAAPSYGLAESTCAVTVPVPGiglrvdevttddgsgARRHAVLGNPIPGMEVRISPGDG------------- 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 433 rvRSGLEGKE-GELLVRGPSVFKEYWNKhqetrESFTDSGWFKTGDTAIHKDGVFWIMGRTSvDIIKSGGYKISALEVER 511
Cdd:PRK05851 364 --AAGVAGREiGEIEIRGASMMSGYLGQ-----APIDPDDWFPTGDLGYLVDGGLVVCGRAK-ELITVAGRNIFPTEIER 435
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
119-491 |
5.12e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 52.81 E-value: 5.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 119 GKRISFLCANDASYTVAQWAAWMSGGTAVPLYrkHPQE-----ELEYIISDSQSSLLVAGNSFAKTLEplALKLGLPCLT 193
Cdd:PRK07769 79 GDRVAILAPQNLDYLIAFFGALYAGRIAVPLF--DPAEpghvgRLHAVLDDCTPSAILTTTDSAEGVR--KFFRARPAKE 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 194 LP--------PTSNLSTLDGTDSQEEEAAitdwadrpaMIIYTSGTTGRPKGVLHTH----SSIQAMVQCLVSEWawtrD 261
Cdd:PRK07769 155 RPrviavdavPDEVGATWVPPEANEDTIA---------YLQYTSGSTRIPAGVQITHlnlpTNVLQVIDALEGQE----G 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 262 DVILHTLPLHHVHGIVNKLLCPLWVGATCIMLPE-F--QPQKVWEILLTSKAPMVNVFMAVPtiyskliqyydqHFTQPH 338
Cdd:PRK07769 222 DRGVSWLPFFHDMGLITVLLPALLGHYITFMSPAaFvrRPGRWIRELARKPGGTGGTFSAAP------------NFAFEH 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 339 V------KDFVKAVCKQRIRLMVSGSAALPLPTLQRWEEITGHTLLER------YGMTEIGMALSNP------------- 393
Cdd:PRK07769 290 AaarglpKDGEPPLDLSNVKGLLNGSEPVSPASMRKFNEAFAPYGLPPtaikpsYGMAEATLFVSTTpmdeeptviyvdr 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 394 --LKGPRI-------PGAVGSPLPGVEIRivmsnATNTTIVEANHRETRVrsglEGKEGELLVRGPSVFKEYWNKHQETR 464
Cdd:PRK07769 370 deLNAGRFvevpadaPNAVAQVSAGKVGV-----SEWAVIVDPETASELP----DGQIGEIWLHGNNIGTGYWGKPEETA 440
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2105456023 465 ESF-----------------TDSGWFKTGDTAIHKDGVFWIMGR 491
Cdd:PRK07769 441 ATFqnilksrlseshaegapDDALWVRTGDYGVYFDGELYITGR 484
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
225-484 |
7.60e-07 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 52.03 E-value: 7.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 225 IIYTSGTTGRPKGVLHTHSSIQAMVQCLvSEWAWTRD---DVILHTLPLHHVHGIVNKLLCpLWVGATCimlpefqpqKV 301
Cdd:PTZ00342 309 IVYTSGTSGKPKGVMLSNKNLYNTVVPL-CKHSIFKKynpKTHLSYLPISHIYERVIAYLS-FMLGGTI---------NI 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 302 W--------EILLTSKApmvNVFMAVPTIYSKLiqyYDQHFTQ-----PHVKDFVKAV---------------------C 347
Cdd:PTZ00342 378 WskdinyfsKDIYNSKG---NILAGVPKVFNRI---YTNIMTEinnlpPLKRFLVKKIlslrksnnnggfskflegithI 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 348 KQRIR--------LMVSGSAALPlPTLQRweEITghTLL-----ERYGMTEIGMALSNPLKGPRIPGAVGSPL-PGVEIR 413
Cdd:PTZ00342 452 SSKIKdkvnpnleVILNGGGKLS-PKIAE--ELS--VLLnvnyyQGYGLTETTGPIFVQHADDNNTESIGGPIsPNTKYK 526
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2105456023 414 IV---MSNATNTTiveanhretrvrsglegKEGELLVRGPSVFKEYWNKHQETRESFTDSGWFKTGDTA-IHKDG 484
Cdd:PTZ00342 527 VRtweTYKATDTL-----------------PKGELLIKSDSIFSGYFLEKEQTKNAFTEDGYFKTGDIVqINKNG 584
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
119-500 |
1.62e-05 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 47.81 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 119 GKRISFLCANDASYTVAQWAAWMSGGTAVPLYRKHPQ---EELEYIISDSQSSLLVAGNSFAKTLEplALKLGLPCLTLP 195
Cdd:PRK12476 92 GDRVAILAPQGIDYVAGFFAAIKAGTIAVPLFAPELPghaERLDTALRDAEPTVVLTTTAAAEAVE--GFLRNLPRLRRP 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 196 PTSNLSTLDGTDSQEEEAAITDwADRPAMIIYTSGTTGRPKGVLHTHSSIQA-MVQCLVSEWAWTRDDVILHTLPLHHVH 274
Cdd:PRK12476 170 RVIAIDAIPDSAGESFVPVELD-TDDVSHLQYTSGSTRPPVGVEITHRAVGTnLVQMILSIDLLDRNTHGVSWLPLYHDM 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 275 GIVNKLLCPLWVGATCIMLP-EF--QPQKvWEILLTSKAPMVNVFMAVPTIyskLIQYYDQHFTQPHVK--DFVKAVckq 349
Cdd:PRK12476 249 GLSMIGFPAVYGGHSTLMSPtAFvrRPQR-WIKALSEGSRTGRVVTAAPNF---AYEWAAQRGLPAEGDdiDLSNVV--- 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 350 rirlMVSGSAALPLPTLQRWEEITGHTLLER------YGMTEIGMALSN--PLKGP----------------RIPGAVGS 405
Cdd:PRK12476 322 ----LIIGSEPVSIDAVTTFNKAFAPYGLPRtafkpsYGIAEATLFVATiaPDAEPsvvyldreqlgagravRVAADAPN 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 406 PLPGVEIRIVmSNATNTTIVEANhretrvrSGLE---GKEGELLVRGPSVFKEYWNKHQETRESF--------------- 467
Cdd:PRK12476 398 AVAHVSCGQV-ARSQWAVIVDPD-------TGAElpdGEVGEIWLHGDNIGRGYWGRPEETERTFgaklqsrlaegshad 469
|
410 420 430
....*....|....*....|....*....|....*.
gi 2105456023 468 ---TDSGWFKTGDTAIHKDGVFWIMGRTSVDIIKSG 500
Cdd:PRK12476 470 gaaDDGTWLRTGDLGVYLDGELYITGRIADLIVIDG 505
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
226-594 |
2.09e-05 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 47.42 E-value: 2.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 226 IYTSGTTGRPKGVLHTHSSIQAMVQCLVSEWAWTRDDVILHTLPLHH----VHGIVNKLLcplwVGATCIMLPEFQPQKV 301
Cdd:cd05939 110 IYTSGTTGLPKAAVIVHSRYYRIAAGAYYAFGMRPEDVVYDCLPLYHsaggIMGVGQALL----HGSTVVIRKKFSASNF 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 302 WEILLTSKApmvnvfmavpTIysklIQYYDQH----FTQPHVKDfvkaVCKQRIRLMVsGSAALPlptlQRWEEITGH-- 375
Cdd:cd05939 186 WDDCVKYNC----------TI----VQYIGEIcrylLAQPPSEE----EQKHNVRLAV-GNGLRP----QIWEQFVRRfg 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 376 --TLLERYGMTEIGMALSNplkgprIPGAVGS------PLPGV-EIRIVMSN-ATNTTIVEANHRETRVRSGLEGK-EGE 444
Cdd:cd05939 243 ipQIGEFYGATEGNSSLVN------IDNHVGAcgfnsrILPSVyPIRLIKVDeDTGELIRDSDGLCIPCQPGEPGLlVGK 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 445 LLVRGPSV-FKEYWNKHQETRESFTDSgwFKTGDTA------IHKD--GVFWIMGRTSvDIIKSGGYKISALEVERHLLA 515
Cdd:cd05939 317 IIQNDPLRrFDGYVNEGATNKKIARDV--FKKGDSAflsgdvLVMDelGYLYFKDRTG-DTFRWKGENVSTTEVEGILSN 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 516 HPAIADVAVIGP--PDAIWGQKVTAVMQLKRGhrLTLPELKIWAREHMAPYIIPTGLVLVEELPRNQMGKVNKKDLLRHF 593
Cdd:cd05939 394 VLGLEDVVVYGVevPGVEGRAGMAAIVDPERK--VDLDRFSAVLAKSLPPYARPQFIRLLPEVDKTGTFKLQKTDLQKEG 471
|
.
gi 2105456023 594 F 594
Cdd:cd05939 472 Y 472
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
228-392 |
3.78e-04 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 43.21 E-value: 3.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 228 TSGTTGRPKGVLHTHSSIQAmvqclvseWAW-----------TRDDVILHTLPLHhvhgivnkllcpLWV---------- 286
Cdd:COG1541 91 SSGTTGKPTVVGYTRKDLDR--------WAElfarslraagvRPGDRVQNAFGYG------------LFTgglglhygae 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105456023 287 --GATCIMLPEFQPQKVWEILLTSKapmVNVFMAVPTiYSK-LIQYYDQHFTQPhvKDFvkavckqRIRLMVSGSAALPL 363
Cdd:COG1541 151 rlGATVIPAGGGNTERQLRLMQDFG---PTVLVGTPS-YLLyLAEVAEEEGIDP--RDL-------SLKKGIFGGEPWSE 217
|
170 180
....*....|....*....|....*....
gi 2105456023 364 PTLQRWEEITGHTLLERYGMTEIGMALSN 392
Cdd:COG1541 218 EMRKEIEERWGIKAYDIYGLTEVGPGVAY 246
|
|
| |
