|
Name |
Accession |
Description |
Interval |
E-value |
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
64-577 |
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: 675.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 64 DNVAITDHSGSHTFCSLYknskSLAGLITKALTCQSGDLQGKCISFLCANDASYTVAQWAAWMCGGIAVPLYRKHPPGEL 143
Cdd:cd05941 1 DRIAIVDDGDSITYADLV----ARAARLANRLLALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 144 EYVISDSQSSLLVagqpfmdtleplaqklglpclqlpttssldtlqsedirmlpeqnisdwaeRPAMLIYTSGTTGRPKG 223
Cdd:cd05941 77 EYVITDSEPSLVL--------------------------------------------------DPALILYTSGTTGRPKG 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 224 VLHTHSSLQAMVQGLVSEWAWNKDDVILHTLPLHHVHGIVNKLMCPLWVGATCIMLPEFSAQKVWeqlISSKSPMVNVFM 303
Cdd:cd05941 107 VVLTHANLAANVRALVDAWRWTEDDVLLHVLPLHHVHGLVNALLCPLFAGASVEFLPKFDPKEVA---ISRLMPSITVFM 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 304 AVPTIYSKLIEYYDQHFTQPQvqdFIRAVCKERIRLMVSGSAALPQPVLERWAEITGHVLLERYGMTEIGMALSNPLKGS 383
Cdd:cd05941 184 GVPTIYTRLLQYYEAHFTDPQ---FARAAAAERLRLMVSGSAALPVPTLEEWEAITGHTLLERYGMTEIGMALSNPLDGE 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 384 RVPGAVGVPLPGVEVRIMMTNstnaiiaegnskgtRVKAGLEGKEGELLVRGSSVFQKYWNKPQETADTFTEDGWFKTGD 463
Cdd:cd05941 261 RRPGTVGMPLPGVQARIVDEE--------------TGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGWFKTGD 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 464 TALYR-DGVYWIMGRTSVDIIKSGGYKISALDVERHLLAHPDITDVAVIGAPDPTWGQKVTAVVQLKKGK-TLTLSQLQA 541
Cdd:cd05941 327 LGVVDeDGYYWILGRSSVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGAaALSLEELKE 406
|
490 500 510
....*....|....*....|....*....|....*.
gi 2073725801 542 WAREHMAPYTIPTGLILVEEMPRNQMGKVNKKDLLR 577
Cdd:cd05941 407 WAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
58-579 |
2.27e-139 |
|
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: 412.28 E-value: 2.27e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 58 RASVYGDNVAITDHSGSHTFCSLYKNSKSLAGLITkALTCQSGDlqgkCISFLCANDASYTVAQWAAWMCGGIAVPLYRK 137
Cdd:COG0318 8 AAARHPDRPALVFGGRRLTYAELDARARRLAAALR-ALGVGPGD----RVALLLPNSPEFVVAFLAALRAGAVVVPLNPR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 138 HPPGELEYVISDSQSSLLVAgqpfmdtleplaqklglpclqlpttssldtlqsedirmlpeqnisdwaerpAMLIYTSGT 217
Cdd:COG0318 83 LTAEELAYILEDSGARALVT---------------------------------------------------ALILYTSGT 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 218 TGRPKGVLHTHSSLQAMVQGLVSEWAWNKDDVILHTLPLHHVHGIVNKLMCPLWVGATCIMLPEFSAQKVWEQLISSKsp 297
Cdd:COG0318 112 TGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLPRFDPERVLELIERER-- 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 298 mVNVFMAVPTIYSKLIEYYDQHFTqpqvqDFiravckERIRLMVSGSAALPQPVLERWAEITGHVLLERYGMTEIGMALS 377
Cdd:COG0318 190 -VTVLFGVPTMLARLLRHPEFARY-----DL------SSLRLVVSGGAPLPPELLERFEERFGVRIVEGYGLTETSPVVT 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 378 -NPL-KGSRVPGAVGVPLPGVEVRIMmtnstnaiiaegNSKGTRVKAGlegKEGELLVRGSSVFQKYWNKPQETADTFtE 455
Cdd:COG0318 258 vNPEdPGERRPGSVGRPLPGVEVRIV------------DEDGRELPPG---EVGEIVVRGPNVMKGYWNDPEATAEAF-R 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 456 DGWFKTGDTA-LYRDGVYWIMGRTSvDIIKSGGYKISALDVERHLLAHPDITDVAVIGAPDPTWGQKVTAVVQLKKGKTL 534
Cdd:COG0318 322 DGWLRTGDLGrLDEDGYLYIVGRKK-DMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPGAEL 400
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 2073725801 535 TLSQLQAWAREHMAPYTIPTGLILVEEMPRNQMGKVNKKDLLRKF 579
Cdd:COG0318 401 DAEELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRERY 445
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
52-575 |
5.47e-112 |
|
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341259 [Multi-domain] Cd Length: 468 Bit Score: 342.62 E-value: 5.47e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 52 VAPVFSRASV-YGDNVAITDHSGSHTFCSLYKNSKSLAGLItKALTCQSGDLqgkcISFLCANDASYTVAQWAAWMCGGI 130
Cdd:cd05936 1 LADLLEEAARrFPDKTALIFMGRKLTYRELDALAEAFAAGL-QNLGVQPGDR----VALMLPNCPQFPIAYFGALKAGAV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 131 AVPLYRKHPPGELEYVISDSQSSLLVAGQPFMDTLEPLAQKLGLPclqlpttssldTLQSEDIrmlpeqnisdwaerpAM 210
Cdd:cd05936 76 VVPLNPLYTPRELEHILNDSGAKALIVAVSFTDLLAAGAPLGERV-----------ALTPEDV---------------AV 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 211 LIYTSGTTGRPKGVLHTHSSLQAMVQGLvseWAW-----NKDDVILHTLPLHHVHGIVNKLMCPLWVGATCIMLPEFSAQ 285
Cdd:cd05936 130 LQYTSGTTGVPKGAMLTHRNLVANALQI---KAWledllEGDDVVLAALPLFHVFGLTVALLLPLALGATIVLIPRFRPI 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 286 KVWEQLissKSPMVNVFMAVPTIYSKLIEYYDQHFTQPQvqdfiravckeRIRLMVSGSAALPQPVLERWAEITGHVLLE 365
Cdd:cd05936 207 GVLKEI---RKHRVTIFPGVPTMYIALLNAPEFKKRDFS-----------SLRLCISGGAPLPVEVAERFEELTGVPIVE 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 366 RYGMTEIG-MALSNPLKGSRVPGAVGVPLPGVEVRIMmtnstnaiiaegNSKGTRVKaglEGKEGELLVRGSSVFQKYWN 444
Cdd:cd05936 273 GYGLTETSpVVAVNPLDGPRKPGSIGIPLPGTEVKIV------------DDDGEELP---PGEVGELWVRGPQVMKGYWN 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 445 KPQETADTFTeDGWFKTGDTAlYRD--GVYWIMGRTSvDIIKSGGYKISALDVERHLLAHPDITDVAVIGAPDPTWGQKV 522
Cdd:cd05936 338 RPEETAEAFV-DGWLRTGDIG-YMDedGYFFIVDRKK-DMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAV 414
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 2073725801 523 TAVVQLKKGKTLTLSQLQAWAREHMAPYTIPTGLILVEEMPRNQMGKVNKKDL 575
Cdd:cd05936 415 KAFVVLKEGASLTEEEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRREL 467
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
128-577 |
3.02e-106 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 328.76 E-value: 3.02e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 128 GGIAVPLYRKHPPGELEYVISDSQSSLLVAGQPFMDTLEPLAQKLGLPC---LQLPTTSSLDTL---QSEDIRMLPEQni 201
Cdd:PRK07514 77 GAVFLPLNTAYTLAELDYFIGDAEPALVVCDPANFAWLSKIAAAAGAPHvetLDADGTGSLLEAaaaAPDDFETVPRG-- 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 202 sdwAERPAMLIYTSGTTGRPKGVLHTHSSLQAMVQGLVSEWAWNKDDVILHTLPLHHVHGIVNKLMCPLWVGATCIMLPE 281
Cdd:PRK07514 155 ---ADDLAAILYTSGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPDDVLIHALPIFHTHGLFVATNVALLAGASMIFLPK 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 282 FSAQKVWEQLissksPMVNVFMAVPTIYSKLIEyyDQHFTqpqvqdfiRAVCKeRIRLMVSGSAALPQPVLERWAEITGH 361
Cdd:PRK07514 232 FDPDAVLALM-----PRATVMMGVPTFYTRLLQ--EPRLT--------REAAA-HMRLFISGSAPLLAETHREFQERTGH 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 362 VLLERYGMTEIGMALSNPLKGSRVPGAVGVPLPGVEVRImmtnstnaiiaegnskgTRVKAGLE---GKEGELLVRGSSV 438
Cdd:PRK07514 296 AILERYGMTETNMNTSNPYDGERRAGTVGFPLPGVSLRV-----------------TDPETGAElppGEIGMIEVKGPNV 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 439 FQKYWNKPQETADTFTEDGWFKTGDTALY-RDGVYWIMGRtSVDIIKSGGYKISALDVERHLLAHPDITDVAVIGAPDPT 517
Cdd:PRK07514 359 FKGYWRMPEKTAEEFRADGFFITGDLGKIdERGYVHIVGR-GKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPD 437
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 518 WGQKVTAVVQLKKGKTLTLSQLQAWAREHMAPYTIPTGLILVEEMPRNQMGKVnKKDLLR 577
Cdd:PRK07514 438 FGEGVTAVVVPKPGAALDEAAILAALKGRLARFKQPKRVFFVDELPRNTMGKV-QKNLLR 496
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
119-577 |
1.08e-104 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 323.87 E-value: 1.08e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 119 VAQWAAWMCGGIAVPLYRKHPPGELEYVISDSQSSLLVAGQPfmdtleplaqklglpclqlpttSSLDTLQSEDIRM--- 195
Cdd:PRK07787 60 LAVVGALIAGVPVVPVPPDSGVAERRHILADSGAQAWLGPAP----------------------DDPAGLPHVPVRLhar 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 196 ----LPEQNisdwAERPAMLIYTSGTTGRPKGVLHTHSSLQAMVQGLVSEWAWNKDDVILHTLPLHHVHGIVNKLMCPLW 271
Cdd:PRK07787 118 swhrYPEPD----PDAPALIVYTSGTTGPPKGVVLSRRAIAADLDALAEAWQWTADDVLVHGLPLFHVHGLVLGVLGPLR 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 272 VGATCIMLPEFSAQKVWEQLISSKSpmvnVFMAVPTIYSKLIEyydqhftqpqVQDFIRAVckERIRLMVSGSAALPQPV 351
Cdd:PRK07787 194 IGNRFVHTGRPTPEAYAQALSEGGT----LYFGVPTVWSRIAA----------DPEAARAL--RGARLLVSGSAALPVPV 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 352 LERWAEITGHVLLERYGMTEIGMALSNPLKGSRVPGAVGVPLPGVEVRIMmtnstnaiiaegNSKGTRVKAGLEgKEGEL 431
Cdd:PRK07787 258 FDRLAALTGHRPVERYGMTETLITLSTRADGERRPGWVGLPLAGVETRLV------------DEDGGPVPHDGE-TVGEL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 432 LVRGSSVFQKYWNKPQETADTFTEDGWFKTGDTALYR-DGVYWIMGRTSVDIIKSGGYKISALDVERHLLAHPDITDVAV 510
Cdd:PRK07787 325 QVRGPTLFDGYLNRPDATAAAFTADGWFRTGDVAVVDpDGMHRIVGRESTDLIKSGGYRIGAGEIETALLGHPGVREAAV 404
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2073725801 511 IGAPDPTWGQKVTAVVQlkKGKTLTLSQLQAWAREHMAPYTIPTGLILVEEMPRNQMGKVNKKDLLR 577
Cdd:PRK07787 405 VGVPDDDLGQRIVAYVV--GADDVAADELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLLS 469
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
207-570 |
4.20e-102 |
|
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: 312.30 E-value: 4.20e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 207 RPAMLIYTSGTTGRPKGVLHTHSSLQAMVQGLVSEWAWNKDDVILHTLPLHHVHGIvNKLMCPLWVGATCIMLPEFSAQK 286
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGL-FGLLGALLAGGTVVLLPKFDPEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 287 VWEQLISSKspmVNVFMAVPTIYSKLIEYYDQHftqPQVQDFIRAVCkerirlmvSGSAALPQPVLERWAEITGHVLLER 366
Cdd:cd04433 80 ALELIEREK---VTILLGVPTLLARLLKAPESA---GYDLSSLRALV--------SGGAPLPPELLERFEEAPGIKLVNG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 367 YGMTEIG--MALSNPLKGSRVPGAVGVPLPGVEVRImmtnstnaIIAEGNSKGtrvkaglEGKEGELLVRGSSVFQKYWN 444
Cdd:cd04433 146 YGLTETGgtVATGPPDDDARKPGSVGRPVPGVEVRI--------VDPDGGELP-------PGEIGELVVRGPSVMKGYWN 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 445 KPQETADtFTEDGWFKTGDTAlYRD--GVYWIMGRTSvDIIKSGGYKISALDVERHLLAHPDITDVAVIGAPDPTWGQKV 522
Cdd:cd04433 211 NPEATAA-VDEDGWYRTGDLG-RLDedGYLYIVGRLK-DMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERV 287
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 2073725801 523 TAVVQLKKGKTLTLSQLQAWAREHMAPYTIPTGLILVEEMPRNQMGKV 570
Cdd:cd04433 288 VAVVVLRPGADLDAEELRAHVRERLAPYKVPRRVVFVDALPRTASGKI 335
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
58-572 |
1.57e-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: 311.85 E-value: 1.57e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 58 RASVYGDNVAITDHSGSHTFCSLYKNSKSLAGLITkALTCQSGDlqgkCISFLCANDASYTVAQWAAWMCGGIAVPL-YR 136
Cdd:cd17631 4 RARRHPDRTALVFGGRSLTYAELDERVNRLAHALR-ALGVAKGD----RVAVLSKNSPEFLELLFAAARLGAVFVPLnFR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 137 KHPPgELEYVISDSQSSLLvagqpFMDtleplaqklglpclqlpttssldtlqsedirmlpeqnisdwaerPAMLIYTSG 216
Cdd:cd17631 79 LTPP-EVAYILADSGAKVL-----FDD--------------------------------------------LALLMYTSG 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 217 TTGRPKGVLHTHSSLQAMVQGLVSEWAWNKDDVILHTLPLHHVHGIVNKLMCPLWVGATCIMLPEFSAQKVWEQLISSKs 296
Cdd:cd17631 109 TTGRPKGAMLTHRNLLWNAVNALAALDLGPDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVILRKFDPETVLDLIERHR- 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 297 pmVNVFMAVPTIYSKLIeyydQHfTQPQVQDFiravckERIRLMVSGSAALPQPVLERWAEItGHVLLERYGMTEIGMAL 376
Cdd:cd17631 188 --VTSFFLVPTMIQALL----QH-PRFATTDL------SSLRAVIYGGAPMPERLLRALQAR-GVKFVQGYGMTETSPGV 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 377 S--NPLKGSRVPGAVGVPLPGVEVRIMmtnstnaiiaegNSKGTRVKAGlegKEGELLVRGSSVFQKYWNKPQETADTFt 454
Cdd:cd17631 254 TflSPEDHRRKLGSAGRPVFFVEVRIV------------DPDGREVPPG---EVGEIVVRGPHVMAGYWNRPEATAAAF- 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 455 EDGWFKTGDTA-LYRDGVYWIMGRTSvDIIKSGGYKISALDVERHLLAHPDITDVAVIGAPDPTWGQKVTAVVQLKKGKT 533
Cdd:cd17631 318 RDGWFHTGDLGrLDEDGYLYIVDRKK-DMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPGAE 396
|
490 500 510
....*....|....*....|....*....|....*....
gi 2073725801 534 LTLSQLQAWAREHMAPYTIPTGLILVEEMPRNQMGKVNK 572
Cdd:cd17631 397 LDEDELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
59-575 |
2.71e-99 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 311.35 E-value: 2.71e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 59 ASVYGDNVAITDHSGSHTFCSLYKNSKSLAglitKALTcQSGDLQGKCISFLCANDASYTVAQWAAWMCGGIAVPL-YRK 137
Cdd:PRK06187 16 ARKHPDKEAVYFDGRRTTYAELDERVNRLA----NALR-ALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPInIRL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 138 HPPgELEYVISDSQSSLLVAGQPFMDTLEPLAQklglpclQLPTTSSLDTLQSEDIRMLPEQNIS------------DWA 205
Cdd:PRK06187 91 KPE-EIAYILNDAEDRVVLVDSEFVPLLAAILP-------QLPTVRTVIVEGDGPAAPLAPEVGEyeellaaasdtfDFP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 206 ER----PAMLIYTSGTTGRPKGVLHTHSSLQAMVQGLVSEWAWNKDDVILHTLPLHHVHGivnkLMCP---LWVGATCIM 278
Cdd:PRK06187 163 DIdendAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVPMFHVHA----WGLPylaLMAGAKQVI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 279 LPEFSAQKVWEQLISSKspmVNVFMAVPTIYSKLIEYYDQHFtqpqvQDFiravckERIRLMVSGSAALPQPVLERWAEI 358
Cdd:PRK06187 239 PRRFDPENLLDLIETER---VTFFFAVPTIWQMLLKAPRAYF-----VDF------SSLRLVIYGGAALPPALLREFKEK 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 359 TGHVLLERYGMTEIGMALS-NPLK-----GSRVPGAVGVPLPGVEVRIMmtnstnaiiaegNSKGTRVKAglEGKE-GEL 431
Cdd:PRK06187 305 FGIDLVQGYGMTETSPVVSvLPPEdqlpgQWTKRRSAGRPLPGVEARIV------------DDDGDELPP--DGGEvGEI 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 432 LVRGSSVFQKYWNKPQETADTFtEDGWFKTGDTAlYRD--GVYWIMGRTSvDIIKSGGYKISALDVERHLLAHPDITDVA 509
Cdd:PRK06187 371 IVRGPWLMQGYWNRPEATAETI-DGGWLHTGDVG-YIDedGYLYITDRIK-DVIISGGENIYPRELEDALYGHPAVAEVA 447
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2073725801 510 VIGAPDPTWGQKVTAVVQLKKGKTLTLSQLQAWAREHMAPYTIPTGLILVEEMPRNQMGKVNKKDL 575
Cdd:PRK06187 448 VIGVPDEKWGERPVAVVVLKPGATLDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVL 513
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
66-570 |
1.36e-88 |
|
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: 282.66 E-value: 1.36e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 66 VAITDHSGSHTFCSLYKNSKSLAGLITKAltcqsGDLQGKCISFLCANDASYTVAQWAAWMCGGIAVPLYRKHPPGELEY 145
Cdd:cd05926 6 LVVPGSTPALTYADLAELVDDLARQLAAL-----GIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 146 VISDSQSSLLVAGQPFMDTLEPLAQKLGLPCLQL--PTTSSLDTLQSEDIRMLPEQNISDWAERP------AMLIYTSGT 217
Cdd:cd05926 81 YLADLGSKLVLTPKGELGPASRAASKLGLAILELalDVGVLIRAPSAESLSNLLADKKNAKSEGVplpddlALILHTSGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 218 TGRPKGVLHTHSSLQAMVQGLVSEWAWNKDDVILHTLPLHHVHGIVNKLMCPLWVGATCIMLPEFSAQKVWEQLISSKsp 297
Cdd:cd05926 161 TGRPKGVPLTHRNLAASATNITNTYKLTPDDRTLVVMPLFHVHGLVASLLSTLAAGGSVVLPPRFSASTFWPDVRDYN-- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 298 mVNVFMAVPTIYSKLIEYYDQHFTQPqvqdfiravcKERIRLMVSGSAALPQPVLERWAEITGHVLLERYGMTEIG--MA 375
Cdd:cd05926 239 -ATWYTAVPTIHQILLNRPEPNPESP----------PPKLRFIRSCSASLPPAVLEALEATFGAPVLEAYGMTEAAhqMT 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 376 lSNPLKGS-RVPGAVGVPLpGVEVRIMmtnstnaiiaegNSKGTRVKAGlegKEGELLVRGSSVFQKYWNKPQETADTFT 454
Cdd:cd05926 308 -SNPLPPGpRKPGSVGKPV-GVEVRIL------------DEDGEILPPG---VVGEICLRGPNVTRGYLNNPEANAEAAF 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 455 EDGWFKTGDT-ALYRDGVYWIMGRTSvDIIKSGGYKISALDVERHLLAHPDITDVAVIGAPDPTWGQKVTAVVQLKKGKT 533
Cdd:cd05926 371 KDGWFRTGDLgYLDADGYLFLTGRIK-ELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGAS 449
|
490 500 510
....*....|....*....|....*....|....*..
gi 2073725801 534 LTLSQLQAWAREHMAPYTIPTGLILVEEMPRNQMGKV 570
Cdd:cd05926 450 VTEEELRAFCRKHLAAFKVPKKVYFVDELPKTATGKI 486
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
55-578 |
3.96e-84 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 271.78 E-value: 3.96e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 55 VFSRASVYGDNVAITDHSGSHTFCSLYKNSKSLA-GLItkaltcQSGDLQGKCISFLCANDASYTVAQWAAWMCGGIAVP 133
Cdd:PRK07656 11 LARAARRFGDKEAYVFGDQRLTYAELNARVRRAAaALA------ALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 134 LYRKHPPGELEYVISDSQSSLLVAGQPFMDTLEPLAQklGLPCLQLPTTSSLDTLQSEDIRMLPEQNI---SDWAER--- 207
Cdd:PRK07656 85 LNTRYTADEAAYILARGDAKALFVLGLFLGVDYSATT--RLPALEHVVICETEEDDPHTEKMKTFTDFlaaGDPAERape 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 208 -----PAMLIYTSGTTGRPKGVLHTHSSLQAMVQglvsEWA----WNKDDVILHTLPLHHVHGIVNKLMCPLWVGATCIM 278
Cdd:PRK07656 163 vdpddVADILFTSGTTGRPKGAMLTHRQLLSNAA----DWAeylgLTEGDRYLAANPFFHVFGYKAGVNAPLMRGATILP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 279 LPEFSAQKVWeQLISSKSpmVNVFMAVPTIYSKLIEYYDQHFTqpqvqDFiravckERIRLMVSGSAALPQPVLERW-AE 357
Cdd:PRK07656 239 LPVFDPDEVF-RLIETER--ITVLPGPPTMYNSLLQHPDRSAE-----DL------SSLRLAVTGAASMPVALLERFeSE 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 358 ITGHVLLERYGMTE-IGMALSNPLKGSR--VPGAVGVPLPGVEVRIMmtnstnaiiaegNSKGTRVKAGlegKEGELLVR 434
Cdd:PRK07656 305 LGVDIVLTGYGLSEaSGVTTFNRLDDDRktVAGTIGTAIAGVENKIV------------NELGEEVPVG---EVGELLVR 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 435 GSSVFQKYWNKPQETADTFTEDGWFKTGDTA-LYRDGVYWIMGRTSvDIIKSGGYKISALDVERHLLAHPDITDVAVIGA 513
Cdd:PRK07656 370 GPNVMKGYYDDPEATAAAIDADGWLHTGDLGrLDEEGYLYIVDRKK-DMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGV 448
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2073725801 514 PDPTWGQKVTAVVQLKKGKTLTLSQLQAWAREHMAPYTIPTGLILVEEMPRNQMGKVnKKDLLRK 578
Cdd:PRK07656 449 PDERLGEVGKAYVVLKPGAELTEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKV-LKRALRE 512
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
56-570 |
1.81e-82 |
|
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: 267.31 E-value: 1.81e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 56 FSRASVYGDNVAITDHSGSHTFCSLYKNSKSLAG-LITKALTcqsgdlQGKCISFLCANDASYTVAQWAAWMCGGIAVPL 134
Cdd:cd05959 11 LNLNEGRGDKTAFIDDAGSLTYAELEAEARRVAGaLRALGVK------REERVLLIMLDTVDFPTAFLGAIRAGIVPVPV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 135 YRKHPPGELEYVISDSQSSLLVAGQPFmdtLEPLAQKLGLPCLQLPTTSSLDTLQSEDIRMLPEQNISD----------W 204
Cdd:cd05959 85 NTLLTPDDYAYYLEDSRARVVVVSGEL---APVLAAALTKSEHTLVVLIVSGGAGPEAGALLLAELVAAeaeqlkpaatH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 205 AERPAMLIYTSGTTGRPKGVLHTHSSLQAMVQGLVSE-WAWNKDDVILHTLPLHHVHGIVNKLMCPLWVGATCIMLPEFS 283
Cdd:cd05959 162 ADDPAFWLYSSGSTGRPKGVVHLHADIYWTAELYARNvLGIREDDVCFSAAKLFFAYGLGNSLTFPLSVGATTVLMPERP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 284 AQKVWEQLISSKSPmvNVFMAVPTIYSKLIEYYDqhftqPQVQDFIravckeRIRLMVSGSAALPQPVLERWAEITGHVL 363
Cdd:cd05959 242 TPAAVFKRIRRYRP--TVFFGVPTLYAAMLAAPN-----LPSRDLS------SLRLCVSAGEALPAEVGERWKARFGLDI 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 364 LERYGMTEIG-MALSNpLKGSRVPGAVGVPLPGVEVRIMmtnstnaiiaegNSKGTRVKAgleGKEGELLVRGSSVFQKY 442
Cdd:cd05959 309 LDGIGSTEMLhIFLSN-RPGRVRYGTTGKPVPGYEVELR------------DEDGGDVAD---GEPGELYVRGPSSATMY 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 443 WNKPQETADTFtEDGWFKTGDTALYR-DGVYWIMGRTSvDIIKSGGYKISALDVERHLLAHPDITDVAVIGAPDPTWGQK 521
Cdd:cd05959 373 WNNRDKTRDTF-QGEWTRTGDKYVRDdDGFYTYAGRAD-DMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTK 450
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 2073725801 522 VTAVVQLKKGKTLT---LSQLQAWAREHMAPYTIPTGLILVEEMPRNQMGKV 570
Cdd:cd05959 451 PKAFVVLRPGYEDSealEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKI 502
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
58-486 |
1.40e-81 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 261.86 E-value: 1.40e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 58 RASVYGDNVAITDHSG-SHTFCSLYKNSKSLA-GLitKALTCQSGDlqgkCISFLCANDASYTVAQWAAWMCGGIAVPLY 135
Cdd:pfam00501 4 QAARTPDKTALEVGEGrRLTYRELDERANRLAaGL--RALGVGKGD----RVAILLPNSPEWVVAFLACLKAGAVYVPLN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 136 RKHPPGELEYVISDSQSSLLVAGQPF--------MDTLEPLAQKLGLPCLQLPTTSSLDTLqSEDIRMLPEQNISDWAER 207
Cdd:pfam00501 78 PRLPAEELAYILEDSGAKVLITDDALkleelleaLGKLEVVKLVLVLDRDPVLKEEPLPEE-AKPADVPPPPPPPPDPDD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 208 PAMLIYTSGTTGRPKGVLHTHSSLQAMVQGLVSEWAW----NKDDVILHTLPLHHVHGIVNKLMCPLWVGATCIMLPEFS 283
Cdd:pfam00501 157 LAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPRgfglGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVVLPPGFP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 284 AQKV--WEQLISSKSPmvNVFMAVPTIYSKLIEyydqhftqpqvQDFIRAVCKERIRLMVSGSAALPQPVLERWAEITGH 361
Cdd:pfam00501 237 ALDPaaLLELIERYKV--TVLYGVPTLLNMLLE-----------AGAPKRALLSSLRLVLSGGAPLPPELARRFRELFGG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 362 VLLERYGMTEIGMALSNPLKGS---RVPGAVGVPLPGVEVRIMMtnstnaiIAEGNSKGTrvkagleGKEGELLVRGSSV 438
Cdd:pfam00501 304 ALVNGYGLTETTGVVTTPLPLDedlRSLGSVGRPLPGTEVKIVD-------DETGEPVPP-------GEPGELCVRGPGV 369
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 2073725801 439 FQKYWNKPQETADTFTEDGWFKTGDTALYR-DGVYWIMGRTSvDIIKSG 486
Cdd:pfam00501 370 MKGYLNDPELTAEAFDEDGWYRTGDLGRRDeDGYLEIVGRKK-DQIKLG 417
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
45-579 |
1.82e-80 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 263.78 E-value: 1.82e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 45 ISPGVGRVAPVFSRA-SVYGDNVAITDHSGSHTFCSLYKN-SKSLAGLitKALTCQSGDLqgkcISFLCANDASYTVAQW 122
Cdd:PRK05605 27 LDYGDTTLVDLYDNAvARFGDRPALDFFGATTTYAELGKQvRRAAAGL--RALGVRPGDR----VAIVLPNCPQHIVAFY 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 123 AAWMCGGIAV---PLYRKHppgELEYVISDSQSSLLVAGQPFMDTLEPLAQKLGLP-----------------CLQLP-- 180
Cdd:PRK05605 101 AVLRLGAVVVehnPLYTAH---ELEHPFEDHGARVAIVWDKVAPTVERLRRTTPLEtivsvnmiaampllqrlALRLPip 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 181 ---------TTSSLDTLQSEDI---RMLPEQNISDWAER----PAMLIYTSGTTGRPKGVLHTHSSLQA-MVQGLvsewA 243
Cdd:PRK05605 178 alrkaraalTGPAPGTVPWETLvdaAIGGDGSDVSHPRPtpddVALILYTSGTTGKPKGAQLTHRNLFAnAAQGK----A 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 244 W-----NKDDVILHTLPLHHVHGIVNKLMCPLWVGATCIMLPEFSAQKVWEQLissKSPMVNVFMAVPTIYSKlieyydq 318
Cdd:PRK05605 254 WvpglgDGPERVLAALPMFHAYGLTLCLTLAVSIGGELVLLPAPDIDLILDAM---KKHPPTWLPGVPPLYEK------- 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 319 hftqpqvqdfIRAVCKER------IRLMVSGSAALPQPVLERWAEITGHVLLERYGMTEIG-MALSNPLKGSRVPGAVGV 391
Cdd:PRK05605 324 ----------IAEAAEERgvdlsgVRNAFSGAMALPVSTVELWEKLTGGLLVEGYGLTETSpIIVGNPMSDDRRPGYVGV 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 392 PLPGVEVRIMmtNSTNAiiaegnskgTRVKAglEGKEGELLVRGSSVFQKYWNKPQETADTFtEDGWFKTGDTA-LYRDG 470
Cdd:PRK05605 394 PFPDTEVRIV--DPEDP---------DETMP--DGEEGELLVRGPQVFKGYWNRPEETAKSF-LDGWFRTGDVVvMEEDG 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 471 VYWIMGRTSvDIIKSGGYKISALDVERHLLAHPDITDVAVIGAPDPTWGQKVTAVVQLKKGKTLTLSQLQAWAREHMAPY 550
Cdd:PRK05605 460 FIRIVDRIK-ELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEPGAALDPEGLRAYCREHLTRY 538
|
570 580 590
....*....|....*....|....*....|...
gi 2073725801 551 TIPTGLILVEEMPRNQMGKVN----KKDLLRKF 579
Cdd:PRK05605 539 KVPRRFYHVDELPRDQLGKVRrrevREELLEKL 571
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
76-571 |
1.65e-78 |
|
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341237 [Multi-domain] Cd Length: 486 Bit Score: 255.99 E-value: 1.65e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 76 TFCSLYKNSKSLA-GLitKALtcqsGDLQGKCISFLCANDASYTVAQWAAWMCGGIAVPLYRKHPPGELEYVISDSQSSL 154
Cdd:cd05911 12 TYAQLRTLSRRLAaGL--RKL----GLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 155 LVAGQPFMDTLEPLAQKLG-----------LPCLQLPTTSSLDTLQSEDIRMLPEQNISDwaERPAMLIYTSGTTGRPKG 223
Cdd:cd05911 86 IFTDPDGLEKVKEAAKELGpkdkiivlddkPDGVLSIEDLLSPTLGEEDEDLPPPLKDGK--DDTAAILYSSGTTGLPKG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 224 VLHTHSSLQA---MVQGLVSEWAWnKDDVILHTLPLHHVHGIVNKLMCPLwVGATCIMLPEFSAQkVWEQLISSKSpmVN 300
Cdd:cd05911 164 VCLSHRNLIAnlsQVQTFLYGNDG-SNDVILGFLPLYHIYGLFTTLASLL-NGATVIIMPKFDSE-LFLDLIEKYK--IT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 301 VFMAVPTIYSKLIEYydqhftqPQVQdfiravcKER---IRLMVSGSAALPQPVLERWAEITGHV-LLERYGMTEIGMAL 376
Cdd:cd05911 239 FLYLVPPIAAALAKS-------PLLD-------KYDlssLRVILSGGAPLSKELQELLAKRFPNAtIKQGYGMTETGGIL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 377 SNPLKGSRVPGAVGVPLPGVEVRIMmtnstnaiiaegNSKGTrvKAGLEGKEGELLVRGSSVFQKYWNKPQETADTFTED 456
Cdd:cd05911 305 TVNPDGDDKPGSVGRLLPNVEAKIV------------DDDGK--DSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDED 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 457 GWFKTGDTALYR-DGVYWIMGRtSVDIIKSGGYKISALDVERHLLAHPDITDVAVIGAPDPTWGQKVTAVVQLKKGKTLT 535
Cdd:cd05911 371 GWLHTGDIGYFDeDGYLYIVDR-KKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGEKLT 449
|
490 500 510
....*....|....*....|....*....|....*..
gi 2073725801 536 LSQLQAWAREHMAPYT-IPTGLILVEEMPRNQMGKVN 571
Cdd:cd05911 450 EKEVKDYVAKKVASYKqLRGGVVFVDEIPKSASGKIL 486
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
62-570 |
2.91e-76 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 251.80 E-value: 2.91e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 62 YGDNVAITDHSGSHTFCSLYKNSKSLAGLITKALTCQSGD-----LQgkcisflcaNDASYTVAQWAAWMCGGIAVPLYR 136
Cdd:PRK08314 23 YPDKTAIVFYGRAISYRELLEEAERLAGYLQQECGVRKGDrvllyMQ---------NSPQFVIAYYAILRANAVVVPVNP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 137 KHPPGELEYVISDSQSSLLVAGQPFMDTLEPLAQKLGLPCL-------QLPTTSSL---DTLQSE-DIRMLPEQNISDWA 205
Cdd:PRK08314 94 MNREEELAHYVTDSGARVAIVGSELAPKVAPAVGNLRLRHVivaqysdYLPAEPEIavpAWLRAEpPLQALAPGGVVAWK 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 206 E------RP----------AMLIYTSGTTGRPKGVLHTHSSLQAMVQGLVsewAWN---KDDVILHTLPLHHVHGIVNKL 266
Cdd:PRK08314 174 EalaaglAPpphtagpddlAVLPYTSGTTGVPKGCMHTHRTVMANAVGSV---LWSnstPESVVLAVLPLFHVTGMVHSM 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 267 MCPLWVGATCIMLPEfsaqkvWE-----QLISSKSpmVNVFMAVPTIyskLIEYydqhFTQPQVQDFiravCKERIRLMV 341
Cdd:PRK08314 251 NAPIYAGATVVLMPR------WDreaaaRLIERYR--VTHWTNIPTM---VVDF----LASPGLAER----DLSSLRYIG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 342 SGSAALPQPVLERWAEITGHVLLERYGMTE-IGMALSNPLKGSRvPGAVGVPLPGVEVRIMMTNStnaiiaegnskgtrv 420
Cdd:PRK08314 312 GGGAAMPEAVAERLKELTGLDYVEGYGLTEtMAQTHSNPPDRPK-LQCLGIPTFGVDARVIDPET--------------- 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 421 kagLE----GKEGELLVRGSSVFQKYWNKPQETADTFTE-DG--WFKTGDTALYRDGVYWIMgrtsVDIIK----SGGYK 489
Cdd:PRK08314 376 ---LEelppGEVGEIVVHGPQVFKGYWNRPEATAEAFIEiDGkrFFRTGDLGRMDEEGYFFI----TDRLKrminASGFK 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 490 ISALDVERHLLAHPDITDVAVIGAPDPTWGQKVTAVVQLK---KGKTlTLSQLQAWAREHMAPYTIPTGLILVEEMPRNQ 566
Cdd:PRK08314 449 VWPAEVENLLYKHPAIQEACVIATPDPRRGETVKAVVVLRpeaRGKT-TEEEIIAWAREHMAAYKYPRIVEFVDSLPKSG 527
|
....
gi 2073725801 567 MGKV 570
Cdd:PRK08314 528 SGKI 531
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
119-578 |
7.14e-76 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 251.18 E-value: 7.14e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 119 VAQWAAWMCGGIAVPLYrkhP---PGELEYVISDSQSSLLVA--GQPFMDTLEPLAQKL-----GLPCLQ---------- 178
Cdd:COG0365 79 IAMLACARIGAVHSPVF---PgfgAEALADRIEDAEAKVLITadGGLRGGKVIDLKEKVdealeELPSLEhvivvgrtga 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 179 ---LPTTSSLDTL---QSEDIRmlPEQNisdWAERPAMLIYTSGTTGRPKGVLHTHSSLQAMVQGLVSEWA-WNKDDVIL 251
Cdd:COG0365 156 dvpMEGDLDWDELlaaASAEFE--PEPT---DADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYVLdLKPGDVFW 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 252 HTLPLHHVHGIVNKLMCPLWVGATCIML---PEF-SAQKVWEQLISSKspmVNVFMAVPTIYSKLIEYYDQHFTQPqvqD 327
Cdd:COG0365 231 CTADIGWATGHSYIVYGPLLNGATVVLYegrPDFpDPGRLWELIEKYG---VTVFFTAPTAIRALMKAGDEPLKKY---D 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 328 FiravckERIRLMVSGSAALPQPVLERWAEITGHVLLERYGMTEIGMALSNPLKGSRV-PGAVGVPLPGVEVRIMmtnst 406
Cdd:COG0365 305 L------SSLRLLGSAGEPLNPEVWEWWYEAVGVPIVDGWGQTETGGIFISNLPGLPVkPGSMGKPVPGYDVAVV----- 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 407 naiiaegNSKGTRVKAGlegKEGELLVRGS--SVFQKYWNKPQETADTF--TEDGWFKTGDTAlYRD--GVYWIMGRTSv 480
Cdd:COG0365 374 -------DEDGNPVPPG---EEGELVIKGPwpGMFRGYWNDPERYRETYfgRFPGWYRTGDGA-RRDedGYFWILGRSD- 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 481 DIIKSGGYKISALDVERHLLAHPDITDVAVIGAPDPTWGQKVTAVVQLKKGKTLT---LSQLQAWAREHMAPYTIPTGLI 557
Cdd:COG0365 442 DVINVSGHRIGTAEIESALVSHPAVAEAAVVGVPDEIRGQVVKAFVVLKPGVEPSdelAKELQAHVREELGPYAYPREIE 521
|
490 500
....*....|....*....|.
gi 2073725801 558 LVEEMPRNQMGKVnKKDLLRK 578
Cdd:COG0365 522 FVDELPKTRSGKI-MRRLLRK 541
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
55-573 |
2.55e-75 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 250.79 E-value: 2.55e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 55 VFSRASVYGDNVAITDHSG----SHTFCSLYKNSKSLA-GLItkALTCQSGDlqgkCISFLCANDASYTVAQWAAWMCGG 129
Cdd:COG1022 17 LRRRAARFPDRVALREKEDgiwqSLTWAEFAERVRALAaGLL--ALGVKPGD----RVAILSDNRPEWVIADLAILAAGA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 130 IAVPLYRKHPPGELEYVISDSQSSLLVAGQPFM-DTLEPLAQKLglPCLQL------------PTTSSLDTLQSEDIRML 196
Cdd:COG1022 91 VTVPIYPTSSAEEVAYILNDSGAKVLFVEDQEQlDKLLEVRDEL--PSLRHivvldprglrddPRLLSLDELLALGREVA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 197 PEQNISDWAER-----PAMLIYTSGTTGRPKGVLHTHSSLQAMVQGLVSEWAWNKDDVILHTLPLHHVHGIVNKLMCpLW 271
Cdd:COG1022 169 DPAELEARRAAvkpddLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFLPLAHVFERTVSYYA-LA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 272 VGATCIMLPefSAQKVWEQLISSKsPmvNVFMAVPTIYSKL--------------------------IEYYDQHFTQPQV 325
Cdd:COG1022 248 AGATVAFAE--SPDTLAEDLREVK-P--TFMLAVPRVWEKVyagiqakaeeagglkrklfrwalavgRRYARARLAGKSP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 326 QDF---------------IRAVCKERIRLMVSGSAALPqPVLERWAEITGHVLLERYGMTEI-GMALSNPLKGSRvPGAV 389
Cdd:COG1022 323 SLLlrlkhaladklvfskLREALGGRLRFAVSGGAALG-PELARFFRALGIPVLEGYGLTETsPVITVNRPGDNR-IGTV 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 390 GVPLPGVEVRImmtnstnaiiaegnskgtrvkagleGKEGELLVRGSSVFQKYWNKPQETADTFTEDGWFKTGDTA-LYR 468
Cdd:COG1022 401 GPPLPGVEVKI-------------------------AEDGEILVRGPNVMKGYYKNPEATAEAFDADGWLHTGDIGeLDE 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 469 DGVYWIMGRTSvDIIK-SGGYKISALDVERHLLAHPDITDVAVIGApdptwGQK-VTAVVqlkkgkTLTLSQLQAWAREH 546
Cdd:COG1022 456 DGFLRITGRKK-DLIVtSGGKNVAPQPIENALKASPLIEQAVVVGD-----GRPfLAALI------VPDFEALGEWAEEN 523
|
570 580 590
....*....|....*....|....*....|
gi 2073725801 547 MAPYTIPTGLI---LVEEMPRNQMGKVNKK 573
Cdd:COG1022 524 GLPYTSYAELAqdpEVRALIQEEVDRANAG 553
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
76-572 |
2.81e-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: 2.81e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 76 TFCSLYKNSKSLAGLItKALTCQSGDLqgkcISFLCANDASYTVAQWAAWMCGGIAVPL---YRKHppgELEYVISDSQS 152
Cdd:cd05903 3 TYSELDTRADRLAAGL-AALGVGPGDV----VAFQLPNWWEFAVLYLACLRIGAVTNPIlpfFREH---ELAFILRRAKA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 153 SLLVAGQPFmdtleplaqklglpclqlpttssldtlQSEDIRMLPEQnisdwaerPAMLIYTSGTTGRPKGVLHTHSSLQ 232
Cdd:cd05903 75 KVFVVPERF---------------------------RQFDPAAMPDA--------VALLLFTSGTTGEPKGVMHSHNTLS 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 233 AMVQGLVSEWAWNKDDVILHTLPLHHVHGIVNKLMCPLWVGATCIMLPEFSAQKVWEqLISSKSpmVNVFMAVPtiyskl 312
Cdd:cd05903 120 ASIRQYAERLGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQDIWDPDKALA-LMREHG--VTFMMGAT------ 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 313 ieyydqhftqPQVQDFIRAVCKE-----RIRLMVSGSAALPQPVLERWAEITGHVLLERYGMTEIGMALSNPLKG--SRV 385
Cdd:cd05903 191 ----------PFLTDLLNAVEEAgeplsRLRTFVCGGATVPRSLARRAAELLGAKVCSAYGSTECPGAVTSITPApeDRR 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 386 PGAVGVPLPGVEVRImmTNSTNAIIAEGnskgtrvkaglegKEGELLVRGSSVFQKYWNKPQETADTFtEDGWFKTGDTA 465
Cdd:cd05903 261 LYTDGRPLPGVEIKV--VDDTGATLAPG-------------VEGELLSRGPSVFLGYLDRPDLTADAA-PEGWFRTGDLA 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 466 LYRDGVYW-IMGRTSvDIIKSGGYKISALDVERHLLAHPDITDVAVIGAPDPTWGQKVTAVVQLKKGKTLTLSQLQAW-A 543
Cdd:cd05903 325 RLDEDGYLrITGRSK-DIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGALLTFDELVAYlD 403
|
490 500
....*....|....*....|....*....
gi 2073725801 544 REHMAPYTIPTGLILVEEMPRNQMGKVNK 572
Cdd:cd05903 404 RQGVAKQYWPERLVHVDDLPRTPSGKVQK 432
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
55-575 |
2.94e-71 |
|
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: 237.52 E-value: 2.94e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 55 VFSRASVYGDNVAITDHSG--SHTFCSLYKNSKSLAGlitkALTCQSGdLQGKCISFLCANDASYTVAQWAAWMCGGIAV 132
Cdd:cd05904 11 SFLFASAHPSRPALIDAATgrALTYAELERRVRRLAA----GLAKRGG-RKGDVVLLLSPNSIEFPVAFLAVLSLGAVVT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 133 PLyrkHP---PGELEYVISDSQSSLLVAGQPFMDTLEPLAQKLGLpclqlpttssLDTLQSEDIRMLPEQNISDWAERP- 208
Cdd:cd05904 86 TA---NPlstPAEIAKQVKDSGAKLAFTTAELAEKLASLALPVVL----------LDSAEFDSLSFSDLLFEADEAEPPv 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 209 --------AMLIYTSGTTGRPKGVLHTHSSLQAMVQGLVSEWAWN--KDDVILHTLPLHHVHGIVNKLMCPLWVGATCIM 278
Cdd:cd05904 153 vvikqddvAALLYSSGTTGRSKGVMLTHRNLIAMVAQFVAGEGSNsdSEDVFLCVLPMFHIYGLSSFALGLLRLGATVVV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 279 LPEFSAQKVWEQLISSKspmVNVFMAVPTIYSKLIEyydqhftQPQVQDFIRAvckeRIRLMVSGSAALPQPVLERWAEI 358
Cdd:cd05904 233 MPRFDLEELLAAIERYK---VTHLPVVPPIVLALVK-------SPIVDKYDLS----SLRQIMSGAAPLGKELIEAFRAK 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 359 TGHV-LLERYGMTE---IGMALSNPLKGSRVPGAVGVPLPGVEVRIMMTNStnaiiaeGNSKGTrvkagleGKEGELLVR 434
Cdd:cd05904 299 FPNVdLGQGYGMTEstgVVAMCFAPEKDRAKYGSVGRLVPNVEAKIVDPET-------GESLPP-------NQTGELWIR 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 435 GSSVFQKYWNKPQETADTFTEDGWFKTGDTAlY--RDGVYWIMGRTSvDIIKSGGYKISALDVERHLLAHPDITDVAVIG 512
Cdd:cd05904 365 GPSIMKGYLNNPEATAATIDKEGWLHTGDLC-YidEDGYLFIVDRLK-ELIKYKGFQVAPAELEALLLSHPEILDAAVIP 442
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2073725801 513 APDPTWGQKVTAVVQLKKGKTLTLSQLQAWAREHMAPYTIPTGLILVEEMPRNQMGKVNKKDL 575
Cdd:cd05904 443 YPDEEAGEVPMAFVVRKPGSSLTEDEIMDFVAKQVAPYKKVRKVAFVDAIPKSPSGKILRKEL 505
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
119-575 |
4.46e-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: 4.46e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 119 VAQWAAW-MCGGIAVPLYRKHPPGELEYVISDSQSSLLVAGqpfmdtleplaqklglpclqlpttssldtlqsedirmlp 197
Cdd:cd05934 42 LFAWFALaKLGAVLVPINTALRGDELAYIIDHSGAQLVVVD--------------------------------------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 198 eqnisdwaerPAMLIYTSGTTGRPKGVLHTHSSLQAMVQGLVSEWAWNKDDVILHTLPLHHVHGIVNKLMCPLWVGATCI 277
Cdd:cd05934 83 ----------PASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 278 MLPEFSAQKVWEQLISSKSPMVNVFMAVPTIYSKlieyydqhfTQPQVQDfiravCKERIRLmVSGSAALPQ---PVLER 354
Cdd:cd05934 153 LLPRFSASRFWSDVRRYGATVTNYLGAMLSYLLA---------QPPSPDD-----RAHRLRA-AYGAPNPPElheEFEER 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 355 WaeitGHVLLERYGMTEIGMALSNPLKGSRVPGAVGVPLPGVEVRIMmtnstnaiiaegNSKGTRVKAGlegKEGELLVR 434
Cdd:cd05934 218 F----GVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAPGYEVRIV------------DDDGQELPAG---EPGELVIR 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 435 ---GSSVFQKYWNKPQETADTFtEDGWFKTGDTAlYRD--GVYWIMGRTSvDIIKSGGYKISALDVERHLLAHPDITDVA 509
Cdd:cd05934 279 glrGWGFFKGYYNMPEATAEAM-RNGWFHTGDLG-YRDadGFFYFVDRKK-DMIRRRGENISSAEVERAILRHPAVREAA 355
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2073725801 510 VIGAPDPTWGQKVTAVVQLKKGKTLTLSQLQAWAREHMAPYTIPTGLILVEEMPRNQMGKVNKKDL 575
Cdd:cd05934 356 VVAVPDEVGEDEVKAVVVLRPGETLDPEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQL 421
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
113-579 |
3.06e-70 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 235.21 E-value: 3.06e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 113 NDASYTVAQWAAWMCGGIAVPLYRKHPPGELEYVISDSQSSLLVAGQPFMDTLEPLAQKLG-----LPCLQLPTTS---- 183
Cdd:PRK08316 70 NSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARAFLVDPALAPTAEAALALLPvdtliLSLVLGGREApggw 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 184 -SLDTLQSEDIRMLPEQNISDwaERPAMLIYTSGTTGRPKGVLHTHSSLQAMVQGLVSEWAWNKDDVILHTLPLHHVHGI 262
Cdd:PRK08316 150 lDFADWAEAGSVAEPDVELAD--DDLAQILYTSGTESLPKGAMLTHRALIAEYVSCIVAGDMSADDIPLHALPLYHCAQL 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 263 VNKLMCPLWVGATCIMLPEFSAQKVWEQLISSKspmVNVFMAVPTIYSKLIeyydQHftqPqvqDFiravckERIRLmvS 342
Cdd:PRK08316 228 DVFLGPYLYVGATNVILDAPDPELILRTIEAER---ITSFFAPPTVWISLL----RH---P---DF------DTRDL--S 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 343 -------GSAALPQPVLERwaeitghvLLER---------YGMTEIG---MALsNPLKGSRVPGAVGVPLPGVEVRIMmt 403
Cdd:PRK08316 287 slrkgyyGASIMPVEVLKE--------LRERlpglrfyncYGQTEIAplaTVL-GPEEHLRRPGSAGRPVLNVETRVV-- 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 404 nstnaiiaegNSKGTRVKAGLEGkegELLVRGSSVFQKYWNKPQETADTFtEDGWFKTGDTA-LYRDGVYWIMGRTSvDI 482
Cdd:PRK08316 356 ----------DDDGNDVAPGEVG---EIVHRSPQLMLGYWDDPEKTAEAF-RGGWFHSGDLGvMDEEGYITVVDRKK-DM 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 483 IKSGGYKISALDVERHLLAHPDITDVAVIGAPDPTWGQKVTAVVQLKKGKTLTLSQLQAWAREHMAPYTIPTGLILVEEM 562
Cdd:PRK08316 421 IKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAGATVTEDELIAHCRARLAGFKVPKRVIFVDEL 500
|
490
....*....|....*..
gi 2073725801 563 PRNQMGKVNKKDLLRKF 579
Cdd:PRK08316 501 PRNPSGKILKRELRERY 517
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
74-575 |
6.66e-69 |
|
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.
Pssm-ID: 341258 [Multi-domain] Cd Length: 430 Bit Score: 229.29 E-value: 6.66e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 74 SHTFCSLYKNSKSLAGLITkALTCQSGDLQGKCISflcaNDASYTVAQWAAWMCGGIAVPLYRKHPPGELEYVISDSQSS 153
Cdd:cd05935 1 SLTYLELLEVVKKLASFLS-NKGVRKGDRVGICLQ----NSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 154 LLVAGqpfmdtleplaqklglpclqlpttSSLDtlqseDIRMLPeqnisdwaerpamliYTSGTTGRPKGVLHTHSSLQA 233
Cdd:cd05935 76 VAVVG------------------------SELD-----DLALIP---------------YTSGTTGLPKGCMHTHFSAAA 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 234 MVQGLVSEWAWNKDDVILHTLPLHHVHGIVNKLMCPLWVGATCIMLPEFSAQKVWEQLISSK-------SPMVNVFMAVP 306
Cdd:cd05935 112 NALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMARWDRETALELIEKYKvtfwtniPTMLVDLLATP 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 307 TiysklieyydqhftqpqvqdfIRAVCKERIRLMVSGSAALPQPVLERWAEITGHVLLERYGMTE-IGMALSNPLKGSRV 385
Cdd:cd05935 192 E---------------------FKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTEtMSQTHTNPPLRPKL 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 386 PgAVGVPLPGVEVRIMmtnstnaiiaegnskgtRVKAGLE---GKEGELLVRGSSVFQKYWNKPQETADTFTEDG---WF 459
Cdd:cd05935 251 Q-CLGIP*FGVDARVI-----------------DIETGRElppNEVGEIVVRGPQIFKGYWNRPEETEESFIEIKgrrFF 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 460 KTGDTAlYRD--GVYWIMGRTSvDIIKSGGYKISALDVERHLLAHPDITDVAVIGAPDPTWGQKVTAVVQLK---KGKTl 534
Cdd:cd05935 313 RTGDLG-YMDeeGYFFFVDRVK-RMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRpeyRGKV- 389
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 2073725801 535 TLSQLQAWAREHMAPYTIPTGLILVEEMPRNQMGKVNKKDL 575
Cdd:cd05935 390 TEEDIIEWAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
103-583 |
1.78e-66 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 225.25 E-value: 1.78e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 103 QGKCISFLCANDASYTVAQWAAWMCGGIAVPLyrkHPPGELE---YVISDSQ-SSLLVAGQPFMD-TLEPLAQKLGLPcl 177
Cdd:PRK06188 61 TGDAVALLSLNRPEVLMAIGAAQLAGLRRTAL---HPLGSLDdhaYVLEDAGiSTLIVDPAPFVErALALLARVPSLK-- 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 178 QLPTTSSLDTLQ--SEDIRMLPEQNISDWAERP--AMLIYTSGTTGRPKGVLHTHSSLQAMVQGLVSEWAWNKDDVILHT 253
Cdd:PRK06188 136 HVLTLGPVPDGVdlLAAAAKFGPAPLVAAALPPdiAGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMC 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 254 LPLHHVHGIvnKLMCPLWVGATCIMLPEFSAQKVWEQLISSKspmVNVFMAVPTIYSKLIEYYDQHFTqpqvqDFiravc 333
Cdd:PRK06188 216 TPLSHAGGA--FFLPTLLRGGTVIVLAKFDPAEVLRAIEEQR---ITATFLVPTMIYALLDHPDLRTR-----DL----- 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 334 kERIRLMVSGSAALpQPVleRWAE---ITGHVLLERYGMTEIGMALS------NPLKGSRVPGAVGVPLPGVEVRIMmtn 404
Cdd:PRK06188 281 -SSLETVYYGASPM-SPV--RLAEaieRFGPIFAQYYGQTEAPMVITylrkrdHDPDDPKRLTSCGRPTPGLRVALL--- 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 405 stnaiiaegNSKGTRVKAGlegKEGELLVRGSSVFQKYWNKPQETADTFtEDGWFKTGDTAlYRD--GVYWIMGRTSvDI 482
Cdd:PRK06188 354 ---------DEDGREVAQG---EVGEICVRGPLVMDGYWNRPEETAEAF-RDGWLHTGDVA-REDedGFYYIVDRKK-DM 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 483 IKSGGYKISALDVERHLLAHPDITDVAVIGAPDPTWGQKVTAVVQLKKGKTLTLSQLQAWAREHMAPYTIPTGLILVEEM 562
Cdd:PRK06188 419 IVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRPGAAVDAAELQAHVKERKGSVHAPKQVDFVDSL 498
|
490 500
....*....|....*....|.
gi 2073725801 563 PRNQMGKVNKKDLLRKFFPTR 583
Cdd:PRK06188 499 PLTALGKPDKKALRARYWEGR 519
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
103-572 |
3.96e-66 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 224.93 E-value: 3.96e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 103 QGKCISFLCANDASYTVAQWAAWMCGGIAVPL---YRKHppgELEYVISDSQSSLLVAGQPFMD-TLEPLAQKL--GLPC 176
Cdd:PRK13295 79 RGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLmpiFRER---ELSFMLKHAESKVLVVPKTFRGfDHAAMARRLrpELPA 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 177 LQLPTTSSLDTLQS-EDIRMLPE-------QNISDwAERP-----AMLIYTSGTTGRPKGVLHTHSSLQAMVQGLVSEWA 243
Cdd:PRK13295 156 LRHVVVVGGDGADSfEALLITPAweqepdaPAILA-RLRPgpddvTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLG 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 244 WNKDDVILHTLPLHHVHGIVNKLMCPLWVGATCIMlpefsaQKVWEqlisskspmvnvfmavPTIYSKLIEYYDQHFTQ- 322
Cdd:PRK13295 235 LGADDVILMASPMAHQTGFMYGLMMPVMLGATAVL------QDIWD----------------PARAAELIRTEGVTFTMa 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 323 --PQVQDFIRAVcKER------IRLMVSGSAALPQPVLERWAEITGHVLLERYGMTEIGMA----LSNPLKgsRVPGAVG 390
Cdd:PRK13295 293 stPFLTDLTRAV-KESgrpvssLRTFLCAGAPIPGALVERARAALGAKIVSAWGMTENGAVtltkLDDPDE--RASTTDG 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 391 VPLPGVEVRIMmtnstnaiiaegNSKGTRVKAGlegKEGELLVRGSSVFQKYWNKPQETADTFteDGWFKTGDTA-LYRD 469
Cdd:PRK13295 370 CPLPGVEVRVV------------DADGAPLPAG---QIGRLQVRGCSNFGGYLKRPQLNGTDA--DGWFDTGDLArIDAD 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 470 GVYWIMGRTSvDIIKSGGYKISALDVERHLLAHPDITDVAVIGAPDPTWGQKVTAVVQLKKGKTLTLSQLQAWAREH-MA 548
Cdd:PRK13295 433 GYIRISGRSK-DVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPRPGQSLDFEEMVEFLKAQkVA 511
|
490 500
....*....|....*....|....
gi 2073725801 549 PYTIPTGLILVEEMPRNQMGKVNK 572
Cdd:PRK13295 512 KQYIPERLVVRDALPRTPSGKIQK 535
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
103-573 |
4.00e-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: 219.77 E-value: 4.00e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 103 QGKCISFLCANDASYTVAQWAAWMCGGIAVPLYRKHPPGELEYVISDSQSSLLVAGQPfmdtleplaqklglpclqlptt 182
Cdd:cd05907 29 PGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFVEDP---------------------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 183 ssldtlqsEDirmlpeqnisdwaerPAMLIYTSGTTGRPKGVLHTHSSLQAMVQGLVSEWAWNKDDVILHTLPLHHVHGI 262
Cdd:cd05907 87 --------DD---------------LATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPATEGDRHLSFLPLAHVFER 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 263 VNKLMCPLWVGAtCIMLPEfSAQKVWEQLiSSKSPmvNVFMAVPTIYSKLIEYYDQHfTQPQVQDFIRAVCK-ERIRLMV 341
Cdd:cd05907 144 RAGLYVPLLAGA-RIYFAS-SAETLLDDL-SEVRP--TVFLAVPRVWEKVYAAIKVK-AVPGLKRKLFDLAVgGRLRFAA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 342 SGSAALPQPVLeRWAEITGHVLLERYGMTEIGMALS-NPLKGSRvPGAVGVPLPGVEVRImmtnstnaiiaegnskgtrv 420
Cdd:cd05907 218 SGGAPLPAELL-HFFRALGIPVYEGYGLTETSAVVTlNPPGDNR-IGTVGKPLPGVEVRI-------------------- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 421 kagleGKEGELLVRGSSVFQKYWNKPQETADTFTEDGWFKTGDTA-LYRDGVYWIMGRtSVDIIK-SGGYKISALDVERH 498
Cdd:cd05907 276 -----ADDGEILVRGPNVMLGYYKNPEATAEALDADGWLHTGDLGeIDEDGFLHITGR-KKDLIItSGGKNISPEPIENA 349
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2073725801 499 LLAHPDITDVAVIGAPDPtwgqKVTAVVQLKKgktltlSQLQAWAREHMAPYTIPTGLI---LVEEMPRNQMGKVNKK 573
Cdd:cd05907 350 LKASPLISQAVVIGDGRP----FLVALIVPDP------EALEAWAEEHGIAYTDVAELAanpAVRAEIEAAVEAANAR 417
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
58-577 |
4.40e-65 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 220.89 E-value: 4.40e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 58 RASVYGDNVAITDHSGSHTFCSLYKNSKSLAGLITKALTCQSGDLqgkcISFLCANDASYTVAQWAAWMCGGIAVPLYRK 137
Cdd:PRK06839 11 RAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIYELNVKKGER----IAILSQNSLEYIVLLFAIAKVECIAVPLNIR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 138 HPPGELEYVISDSQSSLLVAGQPFMDTLEPLAQKLGL-PCLQLptTSSLDTLQSEDIRMLPEQNisdwaERPAMLIYTSG 216
Cdd:PRK06839 87 LTENELIFQLKDSGTTVLFVEKTFQNMALSMQKVSYVqRVISI--TSLKEIEDRKIDNFVEKNE-----SASFIICYTSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 217 TTGRPKGVLHTHSSLQAMVQGLVSEWAWNKDDVILHTLPLHHVHGIvNKLMCPLWVGATCIMLP-EFSAQKVWeQLISSK 295
Cdd:PRK06839 160 TTGKPKGAVLTQENMFWNALNNTFAIDLTMHDRSIVLLPLFHIGGI-GLFAFPTLFAGGVIIVPrKFEPTKAL-SMIEKH 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 296 SpmVNVFMAVPTIYSKLIEYYDqhFTQPQVQDfiravckerIRLMVSGSAALPQPVLERWAEiTGHVLLERYGMTEIGMA 375
Cdd:PRK06839 238 K--VTVVMGVPTIHQALINCSK--FETTNLQS---------VRWFYNGGAPCPEELMREFID-RGFLFGQGFGMTETSPT 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 376 LSNPLK--GSRVPGAVGVPLPGVEVRImmtnstnaIIAEGNSKGtrvkaglEGKEGELLVRGSSVFQKYWNKPQETADTF 453
Cdd:PRK06839 304 VFMLSEedARRKVGSIGKPVLFCDYEL--------IDENKNKVE-------VGEVGELLIRGPNVMKEYWNRPDATEETI 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 454 tEDGWFKTGDTALY-RDGVYWIMGRTSvDIIKSGGYKISALDVERHLLAHPDITDVAVIGAPDPTWGQKVTAVVQLKKGK 532
Cdd:PRK06839 369 -QDGWLCTGDLARVdEDGFVYIVGRKK-EMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSS 446
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 2073725801 533 TLTLSQLQAWAREHMAPYTIPTGLILVEEMPRNQMGKVNKKDLLR 577
Cdd:PRK06839 447 VLIEKDVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQLVN 491
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
59-578 |
8.92e-64 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.
Pssm-ID: 341283 [Multi-domain] Cd Length: 486 Bit Score: 217.17 E-value: 8.92e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 59 ASVYGDNVAITDHSGSHTFCSLYKNSKSLA-GLITKALtcQSGDLqgkcISFLCANDASYTVAQWAAWMCGGIAVPLYRK 137
Cdd:cd12118 14 AAVYPDRTSIVYGDRRYTWRQTYDRCRRLAsALAALGI--SRGDT----VAVLAPNTPAMYELHFGVPMAGAVLNALNTR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 138 HPPGELEYVISDSQSSLLVAGQPFmdTLEplaqklglpclqlpttsslDTLQSEDIRMLPEQNISDWaeRPAMLIYTSGT 217
Cdd:cd12118 88 LDAEEIAFILRHSEAKVLFVDREF--EYE-------------------DLLAEGDPDFEWIPPADEW--DPIALNYTSGT 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 218 TGRPKGVLHTHSS--LQAMvqGLVSEWAWNKDDVILHTLPLHHVHGivnklMCPLW----VGATCIMLPEFSAQKVWEQL 291
Cdd:cd12118 145 TGRPKGVVYHHRGayLNAL--ANILEWEMKQHPVYLWTLPMFHCNG-----WCFPWtvaaVGGTNVCLRKVDAKAIYDLI 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 292 ISSKspmVNVFMAVPTIYSKLIEYydqhftQPQVQDFIravcKERIRLMVSGSAAlPQPVLERWAEITGHVlLERYGMTE 371
Cdd:cd12118 218 EKHK---VTHFCGAPTVLNMLANA------PPSDARPL----PHRVHVMTAGAPP-PAAVLAKMEELGFDV-THVYGLTE 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 372 I-GMALSNPLKG----------SRVPGAVGVPLPGVE-VRIMMTNSTNAIIAEGNSKgtrvkaglegkeGELLVRGSSVF 439
Cdd:cd12118 283 TyGPATVCAWKPewdelpteerARLKARQGVRYVGLEeVDVLDPETMKPVPRDGKTI------------GEIVFRGNIVM 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 440 QKYWNKPQETADTFtEDGWFKTGDTA-LYRDGVYWIMGRtSVDIIKSGGYKISALDVERHLLAHPDITDVAVIGAPDPTW 518
Cdd:cd12118 351 KGYLKNPEATAEAF-RGGWFHSGDLAvIHPDGYIEIKDR-SKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKW 428
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 519 GQKVTAVVQLKKGKTLTLSQLQAWAREHMAPYTIPTGlILVEEMPRNQMGKVnKKDLLRK 578
Cdd:cd12118 429 GEVPCAFVELKEGAKVTEEEIIAFCREHLAGFMVPKT-VVFGELPKTSTGKI-QKFVLRD 486
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
81-575 |
1.45e-63 |
|
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: 215.42 E-value: 1.45e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 81 YKNSKSLAGLITKALTCQSGDLQGKCISFLCANDASYTVAQWAAWMCGGIAVPLYRKHPPGELEYVISDSQSSLLVagqp 160
Cdd:cd05958 13 YRDLLALANRIANVLVGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDKARITVAL---- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 161 fmdtlepLAQKLglpclqlpTTSsldtlqsEDIrmlpeqnisdwaerpAMLIYTSGTTGRPKGVLHTHSSLQAMVQGlvs 240
Cdd:cd05958 89 -------CAHAL--------TAS-------DDI---------------CILAFTSGTTGAPKATMHFHRDPLASADR--- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 241 eWAWN-----KDDVILHTLPLHHVHGIVNKLMCPLWVGATCIMLPEFSAQKVWEqLISSKSPmvNVFMAVPTIYSKLIEY 315
Cdd:cd05958 129 -YAVNvlrlrEDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEEATPDLLLS-AIARYKP--TVLFTAPTAYRAMLAH 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 316 YDqhFTQPQVQDfiravckerIRLMVSGSAALPQPVLERWAEITGHVLLERYGMTE-IGMALSNPLKGSRvPGAVGVPLP 394
Cdd:cd05958 205 PD--AAGPDLSS---------LRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEmFHIFISARPGDAR-PGATGKPVP 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 395 GVEVRImmtnstnaIIAEGNSkgtrVKAGlegKEGELLVRGSSVfqkYWNKPQETADTFTEDGWFKTGDTALYR-DGVYW 473
Cdd:cd05958 273 GYEAKV--------VDDEGNP----VPDG---TIGRLAVRGPTG---CRYLADKRQRTYVQGGWNITGDTYSRDpDGYFR 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 474 IMGRtSVDIIKSGGYKISALDVERHLLAHPDITDVAVIGAPDPTWGQKVTAVVQLKKGKT---LTLSQLQAWAREHMAPY 550
Cdd:cd05958 335 HQGR-SDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIpgpVLARELQDHAKAHIAPY 413
|
490 500
....*....|....*....|....*
gi 2073725801 551 TIPTGLILVEEMPRNQMGKVNKKDL 575
Cdd:cd05958 414 KYPRAIEFVTELPRTATGKLQRFAL 438
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
76-578 |
8.59e-63 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 216.44 E-value: 8.59e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 76 TFCSLYKNSKSLAGLITKaLTCQSGDLqgkcISFLCANDASYTVAQWAAWMCGGIAV---PLYRKHppgELEYVISDSQS 152
Cdd:PRK06710 51 TFSVFHDKVKRFANYLQK-LGVEKGDR----VAIMLPNCPQAVIGYYGTLLAGGIVVqtnPLYTER---ELEYQLHDSGA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 153 SLL---------VAGQPFMDTLE-----------PLAQKLGLPCLQLPTTSSLDTL-QSEDIRMLP--EQNISDWAERP- 208
Cdd:PRK06710 123 KVIlcldlvfprVTNVQSATKIEhvivtriadflPFPKNLLYPFVQKKQSNLVVKVsESETIHLWNsvEKEVNTGVEVPc 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 209 ------AMLIYTSGTTGRPKGVLHTHSSLQA-MVQGLvsEWAWN---KDDVILHTLPLHHVHGIVNKLMCPLWVGATCIM 278
Cdd:PRK06710 203 dpendlALLQYTGGTTGFPKGVMLTHKNLVSnTLMGV--QWLYNckeGEEVVLGVLPFFHVYGMTAVMNLSIMQGYKMVL 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 279 LPEFSAQKVWEQLissKSPMVNVFMAVPTIYSKLIeyydqhfTQPQVQDFIRAvckeRIRLMVSGSAALPQPVLERWAEI 358
Cdd:PRK06710 281 IPKFDMKMVFEAI---KKHKVTLFPGAPTIYIALL-------NSPLLKEYDIS----SIRACISGSAPLPVEVQEKFETV 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 359 TGHVLLERYGMTEIG-MALSNPLKGSRVPGAVGVPLPGVEVRIMMTNSTNAIiaegnskgtrvkagLEGKEGELLVRGSS 437
Cdd:PRK06710 347 TGGKLVEGYGLTESSpVTHSNFLWEKRVPGSIGVPWPDTEAMIMSLETGEAL--------------PPGEIGEIVVKGPQ 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 438 VFQKYWNKPQETADTFtEDGWFKTGDTA-LYRDGVYWIMGRTSvDIIKSGGYKISALDVERHLLAHPDITDVAVIGAPDP 516
Cdd:PRK06710 413 IMKGYWNKPEETAAVL-QDGWLHTGDVGyMDEDGFFYVKDRKK-DMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDP 490
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2073725801 517 TWGQKVTAVVQLKKGKTLTLSQLQAWAREHMAPYTIPTGLILVEEMPRNQMGKVNKKDLLRK 578
Cdd:PRK06710 491 YRGETVKAFVVLKEGTECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVLIEE 552
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
123-578 |
9.45e-63 |
|
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.
Pssm-ID: 341276 [Multi-domain] Cd Length: 428 Bit Score: 212.97 E-value: 9.45e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 123 AAWMCGGIAVPLYRKHPPGELEYVISDSQSSLLVAGqpfmdtleplaqklglpclqlpttssldtlqsedirmlpeqnis 202
Cdd:cd05972 44 AVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTD-------------------------------------------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 203 dwAERPAMLIYTSGTTGRPKGVLHTHSSLQA------MVQGL--------VSEWAWNKddvilhtlplhhvhGIVNKLMC 268
Cdd:cd05972 80 --AEDPALIYFTSGTTGLPKGVLHTHSYPLGhiptaaYWLGLrpddihwnIADPGWAK--------------GAWSSFFG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 269 PLWVGATCIM--LPEFSAQKVWEQLISSKspmVNVFMAVPTIYSKLIEyydqhftqpqvQDFIRAVcKERIRLMVSGSAA 346
Cdd:cd05972 144 PWLLGATVFVyeGPRFDAERILELLERYG---VTSFCGPPTAYRMLIK-----------QDLSSYK-FSHLRLVVSAGEP 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 347 LPQPVLERWAEITGHVLLERYGMTEIGMALSN----PLKgsrvPGAVGVPLPGVEVRImmtnstnaIIAEGNSKGtrvka 422
Cdd:cd05972 209 LNPEVIEWWRAATGLPIRDGYGQTETGLTVGNfpdmPVK----PGSMGRPTPGYDVAI--------IDDDGRELP----- 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 423 glEGKEGELLVRGS--SVFQKYWNKPQETADTFTEDgWFKTGDTAlYRD--GVYWIMGRTSvDIIKSGGYKISALDVERH 498
Cdd:cd05972 272 --PGEEGDIAIKLPppGLFLGYVGDPEKTEASIRGD-YYLTGDRA-YRDedGYFWFVGRAD-DIIKSSGYRIGPFEVESA 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 499 LLAHPDITDVAVIGAPDPTWGQKVTAVVQLKKGKTLTLS---QLQAWAREHMAPYTIPTGLILVEEMPRNQMGKVnKKDL 575
Cdd:cd05972 347 LLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYEPSEElaeELQGHVKKVLAPYKYPREIEFVEELPKTISGKI-RRVE 425
|
...
gi 2073725801 576 LRK 578
Cdd:cd05972 426 LRD 428
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
128-575 |
2.02e-62 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 214.55 E-value: 2.02e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 128 GGIAVPLYRKHPPGELEYVISDSQSSLLVAGQPFMDTLEPLAQKLGLP----CL------QLPTTSSLDTLQSEDIRMLP 197
Cdd:PRK08008 86 GAIMVPINARLLREESAWILQNSQASLLVTSAQFYPMYRQIQQEDATPlrhiCLtrvalpADDGVSSFTQLKAQQPATLC 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 198 EQ-NISdwAERPAMLIYTSGTTGRPKGVLHTHSSLQamVQGLVSEW--AWNKDDVILHTLPLHHVHGIVNKLMCPLWVGA 274
Cdd:PRK08008 166 YApPLS--TDDTAEILFTSGTTSRPKGVVITHYNLR--FAGYYSAWqcALRDDDVYLTVMPAFHIDCQCTAAMAAFSAGA 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 275 TCIMLPEFSAQKVWEQLISSKSpmvNVFMAVPTIYSKLIeyydqhfTQPQVQDfIRAVCKERIRLMVSGSAALPQPVLER 354
Cdd:PRK08008 242 TFVLLEKYSARAFWGQVCKYRA---TITECIPMMIRTLM-------VQPPSAN-DRQHCLREVMFYLNLSDQEKDAFEER 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 355 WaeitGHVLLERYGMTE-IGMALSNPLKGSRVPGAVGVPLPGVEVRIMmtnstnaiiaegNSKGTRVKAGlegKEGELLV 433
Cdd:PRK08008 311 F----GVRLLTSYGMTEtIVGIIGDRPGDKRRWPSIGRPGFCYEAEIR------------DDHNRPLPAG---EIGEICI 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 434 RG---SSVFQKYWNKPQETADTFTEDGWFKTGDTAlYRD--GVYWIMGRtSVDIIKSGGYKISALDVERHLLAHPDITDV 508
Cdd:PRK08008 372 KGvpgKTIFKEYYLDPKATAKVLEADGWLHTGDTG-YVDeeGFFYFVDR-RCNMIKRGGENVSCVELENIIATHPKIQDI 449
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2073725801 509 AVIGAPDPTWGQKVTAVVQLKKGKTLTLSQLQAWAREHMAPYTIPTGLILVEEMPRNQMGKVNKKDL 575
Cdd:PRK08008 450 VVVGIKDSIRDEAIKAFVVLNEGETLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNL 516
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
59-575 |
4.94e-60 |
|
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: 207.87 E-value: 4.94e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 59 ASVYGDNVAIT-DHSGS---HTFCSLYKNSKSLAGLITKAltcqsGDLQGKCISFLCANDASYTVAQWAAWMCGGIAVPL 134
Cdd:cd12119 6 ARLHGDREIVSrTHEGEvhrYTYAEVAERARRLANALRRL-----GVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 135 YRKHPPGELEYVISDSQSSLLVagqpFMDTLEPLAQKLgLPclQLPTTSSLDTLQSeDIRMLPEQNISDWA--------- 205
Cdd:cd12119 81 NPRLFPEQIAYIINHAEDRVVF----VDRDFLPLLEAI-AP--RLPTVEHVVVMTD-DAAMPEPAGVGVLAyeellaaes 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 206 ---------ER-PAMLIYTSGTTGRPKGVLHTHSS--LQAMVQGLVSEWAWNKDDVILHTLPLHHVHGIVNKLMCPlWVG 273
Cdd:cd12119 153 peydwpdfdENtAAAICYTSGTTGNPKGVVYSHRSlvLHAMAALLTDGLGLSESDVVLPVVPMFHVNAWGLPYAAA-MVG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 274 ATCIMLPEFSAQKVWEQLISSKSPMVNVfmAVPTIYSKLIEYYDQHftqPQVQDFIRAVckerirlmVSGSAALPQPVLE 353
Cdd:cd12119 232 AKLVLPGPYLDPASLAELIEREGVTFAA--GVPTVWQGLLDHLEAN---GRDLSSLRRV--------VIGGSAVPRSLIE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 354 RWAEItgHV-LLERYGMTE---IGMALSNPLKGSRVPGAV--------GVPLPGVEVRIMmTNSTNAIIAEGNSkgtrvk 421
Cdd:cd12119 299 AFEER--GVrVIHAWGMTEtspLGTVARPPSEHSNLSEDEqlalrakqGRPVPGVELRIV-DDDGRELPWDGKA------ 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 422 aglegkEGELLVRGSSVFQKYWNKPqETADTFTEDGWFKTGDTA-LYRDGVYWIMGRTSvDIIKSGGYKISALDVERHLL 500
Cdd:cd12119 370 ------VGELQVRGPWVTKSYYKND-EESEALTEDGWLRTGDVAtIDEDGYLTITDRSK-DVIKSGGEWISSVELENAIM 441
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2073725801 501 AHPDITDVAVIGAPDPTWGQKVTAVVQLKKGKTLTLSQLQAWAREHMAPYTIPTGLILVEEMPRNQMGKVNKKDL 575
Cdd:cd12119 442 AHPAVAEAAVIGVPHPKWGERPLAVVVLKEGATVTAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
74-575 |
7.66e-60 |
|
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.
Pssm-ID: 341238 [Multi-domain] Cd Length: 411 Bit Score: 204.50 E-value: 7.66e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 74 SHTFCSLYKNSKSLAGLITkaltcQSGDLQGKCISFLCANDASYTVAQWAAWMCGGIAVPLYRKHPPGELEYVISDSQSS 153
Cdd:cd05912 1 SYTFAELFEEVSRLAEHLA-----ALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 154 LlvagqpfmdtleplaqklglpclqlpttssldtlqsEDIrmlpeqnisdwaerpAMLIYTSGTTGRPKGVLHTHSSLQA 233
Cdd:cd05912 76 L------------------------------------DDI---------------ATIMYTSGTTGKPKGVQQTFGNHWW 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 234 MVQGLVSEWAWNKDDVILHTLPLHHVHGIvNKLMCPLWVGATCIMLPEFSAQKVWEQLISSKSPMVNVfmaVPTIYSKLI 313
Cdd:cd05912 105 SAIGSALNLGLTEDDNWLCALPLFHISGL-SILMRSVIYGMTVYLVDKFDAEQVLHLINSGKVTIISV---VPTMLQRLL 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 314 EYYDQHftqpqvqdfiravCKERIRLMVSGSAALPQPVLERWAEiTGHVLLERYGMTEIG--MALSNPLKGSRVPGAVGV 391
Cdd:cd05912 181 EILGEG-------------YPNNLRCILLGGGPAPKPLLEQCKE-KGIPVYQSYGMTETCsqIVTLSPEDALNKIGSAGK 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 392 PLPGVEVRIMMTNstnaiiaegnskgtrvkaGLEGKEGELLVRGSSVFQKYWNKPQETADTFtEDGWFKTGDTA-LYRDG 470
Cdd:cd05912 247 PLFPVELKIEDDG------------------QPPYEVGEILLKGPNVTKGYLNRPDATEESF-ENGWFKTGDIGyLDEEG 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 471 VYWIMGRTSvDIIKSGGYKISALDVERHLLAHPDITDVAVIGAPDPTWGQKVTAVVQLKkgKTLTLSQLQAWAREHMAPY 550
Cdd:cd05912 308 FLYVLDRRS-DLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSE--RPISEEELIAYCSEKLAKY 384
|
490 500
....*....|....*....|....*
gi 2073725801 551 TIPTGLILVEEMPRNQMGKVNKKDL 575
Cdd:cd05912 385 KVPKKIYFVDELPRTASGKLLRHEL 409
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
58-575 |
1.08e-59 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 205.97 E-value: 1.08e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 58 RASVYGDNVAITDHSGSHTFCSLYKNSKSLAGLITKAltcqsGDLQGKCISFLCANDASYTVAQWAAWMCGGIAVPLYRK 137
Cdd:PRK03640 11 RAFLTPDRTAIEFEEKKVTFMELHEAVVSVAGKLAAL-----GVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 138 HPPGELEYVISDSQSSLLVAGQPFMDTLEPLAQKlglpclqlpTTSSLDTLQSEDIRmlPEQNISDwaERPAMLIYTSGT 217
Cdd:PRK03640 86 LSREELLWQLDDAEVKCLITDDDFEAKLIPGISV---------KFAELMNGPKEEAE--IQEEFDL--DEVATIMYTSGT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 218 TGRPKGVL-----HTHSSL-QAMVQGLVSEWAWnkddviLHTLPLHHVHGIvNKLMCPLWVGATCIMLPEFSAQKVWEQL 291
Cdd:PRK03640 153 TGKPKGVIqtygnHWWSAVgSALNLGLTEDDCW------LAAVPIFHISGL-SILMRSVIYGMRVVLVEKFDAEKINKLL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 292 ISSKSPMVNVfmaVPTIYSKLIEYYDQHftqpqvqdfiraVCKERIRLMVSGSAALPQPVLERwAEITGHVLLERYGMTE 371
Cdd:PRK03640 226 QTGGVTIISV---VSTMLQRLLERLGEG------------TYPSSFRCMLLGGGPAPKPLLEQ-CKEKGIPVYQSYGMTE 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 372 IG---MALSNPLKGSRVpGAVGVPLPGVEVRImmtnstnaiiaegnskgtrVKAGLEGK---EGELLVRGSSVFQKYWNK 445
Cdd:PRK03640 290 TAsqiVTLSPEDALTKL-GSAGKPLFPCELKI-------------------EKDGVVVPpfeEGEIVVKGPNVTKGYLNR 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 446 PQETADTFtEDGWFKTGDTA-LYRDGVYWIMGRTSvDIIKSGGYKISALDVERHLLAHPDITDVAVIGAPDPTWGQKVTA 524
Cdd:PRK03640 350 EDATRETF-QDGWFKTGDIGyLDEEGFLYVLDRRS-DLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVA 427
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 2073725801 525 VVqlKKGKTLTLSQLQAWAREHMAPYTIPTGLILVEEMPRNQMGKVNKKDL 575
Cdd:PRK03640 428 FV--VKSGEVTEEELRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHEL 476
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
76-575 |
2.07e-59 |
|
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: 204.22 E-value: 2.07e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 76 TFCSLYKNSKSLAglitKALTCQsGDLQGKCISFLCANDASYTVAQWAAWMCGGIAVPLYRKHPPGELEYVISDSQSSLL 155
Cdd:TIGR01923 1 TWQDLDCEAAHLA----KALKAQ-GIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 156 VAGQPFmdTLEPLaQKLGLPclQLPTTSSLDTLQSEDIRMlpeqnisdwaERPAMLIYTSGTTGRPKGVLHTHSSLQAMV 235
Cdd:TIGR01923 76 LTDSLL--EEKDF-QADSLD--RIEAAGRYETSLSASFNM----------DQIATLMFTSGTTGKPKAVPHTFRNHYASA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 236 QGLVSEWAWNKDDVILHTLPLHHVHGiVNKLMCPLWVGATCIMLPEFSaqkvweQLISS-KSPMVNVFMAVPTiysKLIE 314
Cdd:TIGR01923 141 VGSKENLGFTEDDNWLLSLPLYHISG-LSILFRWLIEGATLRIVDKFN------QLLEMiANERVTHISLVPT---QLNR 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 315 YYDQHFTQpqvqdfiravckERIRLMVSGSAALPQPVLERWAEiTGHVLLERYGMTEigMA---LSNPLKGSRVPGAVGV 391
Cdd:TIGR01923 211 LLDEGGHN------------ENLRKILLGGSAIPAPLIEEAQQ-YGLPIYLSYGMTE--TCsqvTTATPEMLHARPDVGR 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 392 PLPGVEVRIMmtnstnaiiaegnskgtrvKAGLEGkEGELLVRGSSVFQKYWNkPQETADTFTEDGWFKTGDTA-LYRDG 470
Cdd:TIGR01923 276 PLAGREIKIK-------------------VDNKEG-HGEIMVKGANLMKGYLY-QGELTPAFEQQGWFNTGDIGeLDGEG 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 471 VYWIMGRTSvDIIKSGGYKISALDVERHLLAHPDITDVAVIGAPDPTWGQKVTAVVQLKkgKTLTLSQLQAWAREHMAPY 550
Cdd:TIGR01923 335 FLYVLGRRD-DLIISGGENIYPEEIETVLYQHPGIQEAVVVPKPDAEWGQVPVAYIVSE--SDISQAKLIAYLTEKLAKY 411
|
490 500
....*....|....*....|....*
gi 2073725801 551 TIPTGLILVEEMPRNQMGKVNKKDL 575
Cdd:TIGR01923 412 KVPIAFEKLDELPYNASGKILRNQL 436
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
63-572 |
6.14e-59 |
|
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: 204.69 E-value: 6.14e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 63 GDNVAITDHSGSHTFCSLYKNSKSLAGLItKALTCQSGDLqgkcISFLCANDASYTVAQWAAWMCGGIAVPLYRKHPPGE 142
Cdd:TIGR02262 19 GGKTAFIDDISSLSYGELEAQVRRLAAAL-RRLGVKREER----VLLLMLDGVDFPIAFLGAIRAGIVPVALNTLLTADD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 143 LEYVISDSQSSLLVAGQPFMDTLEPLAQKLglPCL---------QLPTTSSLDTLQSEDIRMLPEQNISDwaeRPAMLIY 213
Cdd:TIGR02262 94 YAYMLEDSRARVVFVSGALLPVIKAALGKS--PHLehrvvvgrpEAGEVQLAELLATESEQFKPAATQAD---DPAFWLY 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 214 TSGTTGRPKGVLHTHSSLQAMVQGLVSE-WAWNKDDVILHTLPLHHVHGIVNKLMCPLWVGATCIMLPEF-SAQKVWEQL 291
Cdd:TIGR02262 169 SSGSTGMPKGVVHTHSNPYWTAELYARNtLGIREDDVCFSAAKLFFAYGLGNALTFPMSVGATTVLMGERpTPDAVFDRL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 292 ISSKSpmvNVFMAVPTIYSKLIEYYDqhftqpqvqdfIRAVCKERIRLMVSGSAALPQPVLERWAEITGHVLLERYGMTE 371
Cdd:TIGR02262 249 RRHQP---TIFYGVPTLYAAMLADPN-----------LPSEDQVRLRLCTSAGEALPAEVGQRWQARFGVDIVDGIGSTE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 372 IG-MALSNpLKGSRVPGAVGVPLPGVEVRIMmtnstnaiiaegNSKGTRVKAgleGKEGELLVRGSSVFQKYWNKPQETA 450
Cdd:TIGR02262 315 MLhIFLSN-LPGDVRYGTSGKPVPGYRLRLV------------GDGGQDVAD---GEPGELLISGPSSATMYWNNRAKSR 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 451 DTFtEDGWFKTGDTALYR-DGVYWIMGRTSvDIIKSGGYKISALDVERHLLAHPDITDVAVIGAPDPTWGQKVTAVVQLK 529
Cdd:TIGR02262 379 DTF-QGEWTRSGDKYVRNdDGSYTYAGRTD-DMLKVSGIYVSPFEIESALIQHPAVLEAAVVGVADEDGLIKPKAFVVLR 456
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 2073725801 530 KGKTLTLSQLQAWAREHMAPYTIPTGLILVEEMPRNQMGKVNK 572
Cdd:TIGR02262 457 PGQTALETELKEHVKDRLAPYKYPRWIVFVDDLPKTATGKIQR 499
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
100-575 |
1.04e-58 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 203.50 E-value: 1.04e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 100 GDLQGKCISFLCANDASYTVAQWAAWMCGGIAVPLYRKHPPGELEYVISDSQSSLLV------AGQPFMDTLEPLAQKLg 173
Cdd:PRK09088 43 GCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLLLgddavaAGRTDVEDLAAFIASA- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 174 lPCLQLPTTSSLDtlqsedirmlpeqnisdwAERPAMLIYTSGTTGRPKGVLHTHSSLQAMVQGLVSEWAWNKDDVILHT 253
Cdd:PRK09088 122 -DALEPADTPSIP------------------PERVSLILFTSGTSGQPKGVMLSERNLQQTAHNFGVLGRVDAHSSFLCD 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 254 LPLHHVHGIVNKLMCPLWVGATCIMLPEFSAQKVWEQLisskspmvnvfmAVPTIYsklIEYYdqhFTQPQVQDFIR--- 330
Cdd:PRK09088 183 APMFHIIGLITSVRPVLAVGGSILVSNGFEPKRTLGRL------------GDPALG---ITHY---FCVPQMAQAFRaqp 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 331 ---AVCKERIRLMVSGSAALPQPVLERWAEiTGHVLLERYGMTEIGMALSNPLKGSRVP---GAVGVPLPGVEVRIMmtn 404
Cdd:PRK09088 245 gfdAAALRHLTALFTGGAPHAAEDILGWLD-DGIPMVDGFGMSEAGTVFGMSVDCDVIRakaGAAGIPTPTVQTRVV--- 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 405 stnaiiaegNSKGTRVKAGLEGkegELLVRGSSVFQKYWNKPQETADTFTEDGWFKTGDTALY-RDGVYWIMGRTSvDII 483
Cdd:PRK09088 321 ---------DDQGNDCPAGVPG---ELLLRGPNLSPGYWRRPQATARAFTGDGWFRTGDIARRdADGFFWVVDRKK-DMF 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 484 KSGGYKISALDVERHLLAHPDITDVAVIGAPDPTWGQKVTAVVQLKKGKTLTLSQLQAWAREHMAPYTIPTGLILVEEMP 563
Cdd:PRK09088 388 ISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADGAPLDLERIRSHLSTRLAKYKVPKHLRLVDALP 467
|
490
....*....|..
gi 2073725801 564 RNQMGKVNKKDL 575
Cdd:PRK09088 468 RTASGKLQKARL 479
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
154-577 |
1.61e-58 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 206.34 E-value: 1.61e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 154 LLVAGQPFMDTLEPLAQKLGLPCLQLPTTSSLDTLQSE-DIRMLPEQNISdwAERPAMLIYTSGTTGRPKGVLHTHSSLQ 232
Cdd:PRK07529 162 VEVDLARYLPGPKRLAVPLIRRKAHARILDFDAELARQpGDRLFSGRPIG--PDDVAAYFHTGGTTGMPKLAQHTHGNEV 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 233 AMVQGLVSEWAWNKDDVILHTLPLHHVHGIVNKLMCPLWVGATCIMLP------EFSAQKVWEqLISSKSpmVNVFMAVP 306
Cdd:PRK07529 240 ANAWLGALLLGLGPGDTVFCGLPLFHVNALLVTGLAPLARGAHVVLATpqgyrgPGVIANFWK-IVERYR--INFLSGVP 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 307 TIYSKLIEyydqhftQPqvqdfIRAVCKERIRLMVSGSAALPQPVLERWAEITGHVLLERYGMTEiGMALS--NPLKGSR 384
Cdd:PRK07529 317 TVYAALLQ-------VP-----VDGHDISSLRYALCGAAPLPVEVFRRFEAATGVRIVEGYGLTE-ATCVSsvNPPDGER 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 385 VPGAVGVPLPGVEVRIMMtnstnaiiaeGNSKGTRVKAGLEGKEGELLVRGSSVFQKYWNKPQEtADTFTEDGWFKTGDt 464
Cdd:PRK07529 384 RIGSVGLRLPYQRVRVVI----------LDDAGRYLRDCAVDEVGVLCIAGPNVFSGYLEAAHN-KGLWLEDGWLNTGD- 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 465 aLYR---DGVYWIMGRTSvDIIKSGGYKISALDVERHLLAHPDITDVAVIGAPDPTWGQKVTAVVQLKKGKTLTLSQLQA 541
Cdd:PRK07529 452 -LGRidaDGYFWLTGRAK-DLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGELPVAYVQLKPGASATEAELLA 529
|
410 420 430
....*....|....*....|....*....|....*..
gi 2073725801 542 WAREHMA-PYTIPTGLILVEEMPRNQMGKVNKKDLLR 577
Cdd:PRK07529 530 FARDHIAeRAAVPKHVRILDALPKTAVGKIFKPALRR 566
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
104-575 |
1.25e-57 |
|
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: 199.23 E-value: 1.25e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 104 GKCISFLCANDASYTVAQWAAWMCGGIAVPLYRKHPPGELEYVISDSQSSLLVAGQpfmdtleplaqklglpclqlptts 183
Cdd:cd05919 35 GDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVVTSA------------------------ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 184 sldtlqsEDIrmlpeqnisdwaerpAMLIYTSGTTGRPKGVLHTHSSLQAMVQGLVSEW-AWNKDDVILHTLPLHHVHGI 262
Cdd:cd05919 91 -------DDI---------------AYLLYSSGTTGPPKGVMHAHRDPLLFADAMAREAlGLTPGDRVFSSAKMFFGYGL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 263 VNKLMCPLWVGATCIMLPEF-SAQKVWEQLISSKSpmvNVFMAVPTIYSKLIEYYDQHftqpqvQDFIRAvckerIRLMV 341
Cdd:cd05919 149 GNSLWFPLAVGASAVLNPGWpTAERVLATLARFRP---TVLYGVPTFYANLLDSCAGS------PDALRS-----LRLCV 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 342 SGSAALPQPVLERWAEITGHVLLERYGMTEIG-MALSNPLKGSRvPGAVGVPLPGVEVRIMmtnstnaiiaegNSKGTRV 420
Cdd:cd05919 215 SAGEALPRGLGERWMEHFGGPILDGIGATEVGhIFLSNRPGAWR-LGSTGRPVPGYEIRLV------------DEEGHTI 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 421 KAgleGKEGELLVRGSSVFQKYWNKPQETADTFtEDGWFKTGDtaLY---RDGVYWIMGRtSVDIIKSGGYKISALDVER 497
Cdd:cd05919 282 PP---GEEGDLLVRGPSAAVGYWNNPEKSRATF-NGGWYRTGD--KFcrdADGWYTHAGR-ADDMLKVGGQWVSPVEVES 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 498 HLLAHPDITDVAVIGAPDPTWGQKVTAVVQLKKGKTLTLSQLQAWAR---EHMAPYTIPTGLILVEEMPRNQMGKVNKKD 574
Cdd:cd05919 355 LIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPQESLARDIHRhllERLSAHKVPRRIAFVDELPRTATGKLQRFK 434
|
.
gi 2073725801 575 L 575
Cdd:cd05919 435 L 435
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
110-579 |
7.04e-57 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 200.00 E-value: 7.04e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 110 LCANDASYTVAQWAAWMCGGIAVPLYRKHPPGELEYVISDSQSSLLVAGqpfmDTLEPLAQKL--GLPCLQLPTTS---- 183
Cdd:PRK07786 73 LMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAHVVVTE----AALAPVATAVrdIVPLLSTVVVAggss 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 184 -----SLDTLQSEDIRMLPEQNISDwaERPAMLIYTSGTTGRPKGVLHTHSSLQAMVQGLVSEW-AWNKDDVILHTLPLH 257
Cdd:PRK07786 149 ddsvlGYEDLLAEAGPAHAPVDIPN--DSPALIMYTSGTTGRPKGAVLTHANLTGQAMTCLRTNgADINSDVGFVGVPLF 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 258 HVHGIVNklMCP-LWVGATCIMLP--EFSAQKVWEQLISSKspMVNVFMaVPTiysklieyydqhftqpQVQdfirAVCK 334
Cdd:PRK07786 227 HIAGIGS--MLPgLLLGAPTVIYPlgAFDPGQLLDVLEAEK--VTGIFL-VPA----------------QWQ----AVCA 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 335 E--------RIRLMVSGSAALPQPVLERWAEI-TGHVLLERYGMTEIGmALSNPLKGS---RVPGAVGVPLPGVEVRIMM 402
Cdd:PRK07786 282 EqqarprdlALRVLSWGAAPASDTLLRQMAATfPEAQILAAFGQTEMS-PVTCMLLGEdaiRKLGSVGKVIPTVAARVVD 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 403 TNSTNAIIaegnskgtrvkagleGKEGELLVRGSSVFQKYWNKPQETADTFtEDGWFKTGDtaLYR---DGVYWIMGRTS 479
Cdd:PRK07786 361 ENMNDVPV---------------GEVGEIVYRAPTLMSGYWNNPEATAEAF-AGGWFHSGD--LVRqdeEGYVWVVDRKK 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 480 vDIIKSGGYKISALDVERHLLAHPDITDVAVIGAPDPTWGQKVTAVVQLKKG-KTLTLSQLQAWAREHMAPYTIPTGLIL 558
Cdd:PRK07786 423 -DMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRNDdAALTLEDLAEFLTDRLARYKHPKALEI 501
|
490 500
....*....|....*....|.
gi 2073725801 559 VEEMPRNQMGKVNKKDLLRKF 579
Cdd:PRK07786 502 VDALPRNPAGKVLKTELRERY 522
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
64-575 |
1.33e-56 |
|
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: 196.98 E-value: 1.33e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 64 DNVAITDHSGSHTFCSLYKNSKSLAGLItKALTCQSGDLqgkcISFLCANDASYTVAQWAAWMCGGIAVPLYRKHPPGEL 143
Cdd:cd05930 2 DAVAVVDGDQSLTYAELDARANRLARYL-RERGVGPGDL----VAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 144 EYVISDSQSSLLVAGqpfmdtleplaqklglpclqlpttssldtlqsedirmlpeqnisdwAERPAMLIYTSGTTGRPKG 223
Cdd:cd05930 77 AYILEDSGAKLVLTD----------------------------------------------PDDLAYVIYTSGSTGKPKG 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 224 VLHTHSSLQAMVQGLVSEWAWNKDDVILHTLPLHHVHGIVNkLMCPLWVGATCIMLPE---FSAQKVWEQLISSKspmVN 300
Cdd:cd05930 111 VMVEHRGLVNLLLWMQEAYPLTPGDRVLQFTSFSFDVSVWE-IFGALLAGATLVVLPEevrKDPEALADLLAEEG---IT 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 301 VFMAVPTIYSKLIEYydqhftqPQVQDFiravckERIRLMVSGSAALPQPVLERWAEI-TGHVLLERYGMTEIGMA---- 375
Cdd:cd05930 187 VLHLTPSLLRLLLQE-------LELAAL------PSLRLVLVGGEALPPDLVRRWRELlPGARLVNLYGPTEATVDatyy 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 376 --LSNPLKGSRVPgaVGVPLPGVEVRIMmtnstnaiiaegNSKGTRVKAGlegKEGELLVRGSSVFQKYWNKPQETADTF 453
Cdd:cd05930 254 rvPPDDEEDGRVP--IGRPIPNTRVYVL------------DENLRPVPPG---VPGELYIGGAGLARGYLNRPELTAERF 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 454 TEDGWF------KTGDTALYR-DG--VYwiMGRTSvDIIKSGGYKISALDVERHLLAHPDITDVAVIGAPDPTWGQKVTA 524
Cdd:cd05930 317 VPNPFGpgermyRTGDLVRWLpDGnlEF--LGRID-DQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVA 393
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 2073725801 525 VVQLKKGKTLTLSQLQAWAREHMAPYTIPTGLILVEEMPRNQMGKVNKKDL 575
Cdd:cd05930 394 YVVPDEGGELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
76-576 |
4.93e-56 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 198.34 E-value: 4.93e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 76 TFCSLYKNSKSLAGLITkaltcQSGDLQGKCISFLCANDASYTVAQWAAWMCGGIAVP---LYRKHppgELEYVISDSQS 152
Cdd:PRK06178 60 TYAELDELSDRFAALLR-----QRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPvspLFREH---ELSYELNDAGA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 153 SLLVAGQPFMDTLEPLAQKLGL---------------PCLQLP---------TTSSLDTLQSEDIRMLPEQNISDWAERP 208
Cdd:PRK06178 132 EVLLALDQLAPVVEQVRAETSLrhvivtsladvlpaePTLPLPdslraprlaAAGAIDLLPALRACTAPVPLPPPALDAL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 209 AMLIYTSGTTGRPKGVLHTHSSL--QAMVQGLVSEwAWNKDDVILHTLPLHHVHGIVNKLMCPLWVGATCIMLPEFSAQK 286
Cdd:PRK06178 212 AALNYTGGTTGMPKGCEHTQRDMvyTAAAAYAVAV-VGGEDSVFLSFLPEFWIAGENFGLLFPLFSGATLVLLARWDAVA 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 287 VWEqlisskspmvnvfmAVP----TIYSKLIEYYDQHFTQPQVQDF-IRAVCKERIrlmVSGSAALPQPVLERWAEITGH 361
Cdd:PRK06178 291 FMA--------------AVEryrvTRTVMLVDNAVELMDHPRFAEYdLSSLRQVRV---VSFVKKLNPDYRQRWRALTGS 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 362 VLLE-RYGMTE--------IGMALSN-PLKGSrvPGAVGVPLPGVEVRI--MMTNSTNAIiaegnskgtrvkagleGKEG 429
Cdd:PRK06178 354 VLAEaAWGMTEthtcdtftAGFQDDDfDLLSQ--PVFVGLPVPGTEFKIcdFETGELLPL----------------GAEG 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 430 ELLVRGSSVFQKYWNKPQETADTFtEDGWFKTGDTALY-RDGVYWIMGRTSvDIIKSGGYKISALDVERHLLAHPDITDV 508
Cdd:PRK06178 416 EIVVRTPSLLKGYWNKPEATAEAL-RDGWLHTGDIGKIdEQGFLHYLGRRK-EMLKVNGMSVFPSEVEALLGQHPAVLGS 493
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2073725801 509 AVIGAPDPTWGQKVTAVVQLKKGKTLTLSQLQAWAREHMAPYTIPTgLILVEEMPRNQMGKVNKKDLL 576
Cdd:PRK06178 494 AVVGRPDPDKGQVPVAFVQLKPGADLTAAALQAWCRENMAVYKVPE-IRIVDALPMTATGKVRKQDLQ 560
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
58-578 |
5.02e-56 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 197.66 E-value: 5.02e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 58 RASVYGDNVAITDHSG-SHTFCSLYKNSKSLAG-LITKALtcQSGDLqgkcISFLCANDASYTVAQWAAWMCGGIAVPLY 135
Cdd:PRK06087 32 TARAMPDKIAVVDNHGaSYTYSALDHAASRLANwLLAKGI--EPGDR----VAFQLPGWCEFTIIYLACLKVGAVSVPLL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 136 RKHPPGELEYVISDSQSSLLVAGQPFMDT---LEPLAQKLGLPCLQ--------LPTTSSLDTLQS-EDIRMLpEQNISD 203
Cdd:PRK06087 106 PSWREAELVWVLNKCQAKMFFAPTLFKQTrpvDLILPLQNQLPQLQqivgvdklAPATSSLSLSQIiADYEPL-TTAITT 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 204 WAERPAMLIYTSGTTGRPKGVLHTHSSLQAMVQGLVSEWAWNKDDVILHTLPLHHVHGIVNKLMCPLWVGATCIMLPEFS 283
Cdd:PRK06087 185 HGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVLLDIFT 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 284 AQKVWEQLISSKSPMvnVFMAVPTIYSKLIEYYDQHFTQPQvqdfiravckerIRLMVSGSAALPQPVLERwAEITGHVL 363
Cdd:PRK06087 265 PDACLALLEQQRCTC--MLGATPFIYDLLNLLEKQPADLSA------------LRFFLCGGTTIPKKVARE-CQQRGIKL 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 364 LERYGMTE----IGMALSNPLkgSRVPGAVGVPLPGVEVRIMMTNStnaiiaegnskgtrvKAGLEGKEGELLVRGSSVF 439
Cdd:PRK06087 330 LSVYGSTEssphAVVNLDDPL--SRFMHTDGYAAAGVEIKVVDEAR---------------KTLPPGCEGEEASRGPNVF 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 440 QKYWNKPQETADTFTEDGWFKTGDtaLYR---DGVYWIMGRTSvDIIKSGGYKISALDVERHLLAHPDITDVAVIGAPDP 516
Cdd:PRK06087 393 MGYLDEPELTARALDEEGWYYSGD--LCRmdeAGYIKITGRKK-DIIVRGGENISSREVEDILLQHPKIHDACVVAMPDE 469
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2073725801 517 TWGQKVTAVVQLKKG-KTLTLSQLQAW-AREHMAPYTIPTGLILVEEMPRNQMGKVNK----KDLLRK 578
Cdd:PRK06087 470 RLGERSCAYVVLKAPhHSLTLEEVVAFfSRKRVAKYKYPEHIVVIDKLPRTASGKIQKfllrKDIMRR 537
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
208-572 |
9.96e-55 |
|
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: 188.63 E-value: 9.96e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 208 PAMLIYTSGTTGRPKGVLHTHSSLQAMVQGLVSEWAWNKDDVILHTLPLHHVHGIvNKLMCPLWVGATCIMLPEFSAQKV 287
Cdd:cd17637 2 PFVIIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPLFHIAGL-NLALATFHAGGANVVMEKFDPAEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 288 WEqLISSKSpmVNVFMAVPTIYSKLIEYYDQHFTQPqvqDFIRAVckerirlmvsgsAALPQP-VLERWAEITGHVLLER 366
Cdd:cd17637 81 LE-LIEEEK--VTLMGSFPPILSNLLDAAEKSGVDL---SSLRHV------------LGLDAPeTIQRFEETTGATFWSL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 367 YGMTEIgmalSNPLKGSRV---PGAVGVPLPGVEVRIMmtnstnaiiaegNSKGTRVKAGlegKEGELLVRGSSVFQKYW 443
Cdd:cd17637 143 YGQTET----SGLVTLSPYrerPGSAGRPGPLVRVRIV------------DDNDRPVPAG---ETGEIVVRGPLVFQGYW 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 444 NKPQETADTFtEDGWFKTGDT-ALYRDGVYWIMGRTSV-DIIKSGGYKISALDVERHLLAHPDITDVAVIGAPDPTWGQK 521
Cdd:cd17637 204 NLPELTAYTF-RNGWHHTGDLgRFDEDGYLWYAGRKPEkELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEG 282
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 2073725801 522 VTAVVQLKKGKTLTLSQLQAWAREHMAPYTIPTGLILVEEMPRNQMGKVNK 572
Cdd:cd17637 283 IKAVCVLKPGATLTADELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
58-575 |
5.22e-54 |
|
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: 191.90 E-value: 5.22e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 58 RASVYGDNVAITDHSGSHTFCSLYKNSKSLA-GLItkALTCQSGD---LQgkcisfLcANDASYTVAQWAAWMCGGI--- 130
Cdd:COG1021 34 RAERHPDRIAVVDGERRLSYAELDRRADRLAaGLL--ALGLRPGDrvvVQ------L-PNVAEFVIVFFALFRAGAIpvf 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 131 AVPLYRKHppgELEYVISDSQSSLLV--AGQPFMDtLEPLAQKL--GLPCLQL-------PTTSSLDTLQSEDI-RMLPE 198
Cdd:COG1021 105 ALPAHRRA---EISHFAEQSEAVAYIipDRHRGFD-YRALARELqaEVPSLRHvlvvgdaGEFTSLDALLAAPAdLSEPR 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 199 QNISDwaerPAMLIYTSGTTGRPKGVLHTHS----SLQAMVQglvsEWAWNKDDVILHTLPLHHvhgivNKLM-CP---- 269
Cdd:COG1021 181 PDPDD----VAFFQLSGGTTGLPKLIPRTHDdylySVRASAE----ICGLDADTVYLAALPAAH-----NFPLsSPgvlg 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 270 -LWVGATCIMLPEFSAQKVWEqLISSKSpmVNVFMAVPtiysklieyydqhftqPQVQDFIRAVCKER-----IRLMVSG 343
Cdd:COG1021 248 vLYAGGTVVLAPDPSPDTAFP-LIERER--VTVTALVP----------------PLALLWLDAAERSRydlssLRVLQVG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 344 SAALPQPVLERWAEITGHVLLERYGMTEiGMALSNPLKGSR--VPGAVGVPL-PGVEVRImmtnstnaIIAEGNSkgtrV 420
Cdd:COG1021 309 GAKLSPELARRVRPALGCTLQQVFGMAE-GLVNYTRLDDPEevILTTQGRPIsPDDEVRI--------VDEDGNP----V 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 421 KaglEGKEGELLVRGSSVFQKYWNKPQETADTFTEDGWFKTGDtaLYR---DGVYWIMGRtSVDIIKSGGYKISALDVER 497
Cdd:COG1021 376 P---PGEVGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGD--LVRrtpDGYLVVEGR-AKDQINRGGEKIAAEEVEN 449
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2073725801 498 HLLAHPDITDVAVIGAPDPTWGQKVTAVVQLkKGKTLTLSQLQAWARE-HMAPYTIPTGLILVEEMPRNQMGKVNKKDL 575
Cdd:COG1021 450 LLLAHPAVHDAAVVAMPDEYLGERSCAFVVP-RGEPLTLAELRRFLRErGLAAFKLPDRLEFVDALPLTAVGKIDKKAL 527
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
207-579 |
2.36e-53 |
|
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: 184.46 E-value: 2.36e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 207 RPAMLIYTSGTTGRPKGVLHTHSSLQAMVQGLVSEWAWNKDDVILHTLPLHHVHGIVNKLMCpLWVGATCIMLPefsaqK 286
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLYHVGGLAILVRS-LLAGAELVLLE-----R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 287 VWEQLISSKSPMVNVFMAVPTIYSKLIeyyDQHFTQPQVqdfiravckERIRLMVSGSAALPQPVLERwAEITGHVLLER 366
Cdd:cd17630 75 NQALAEDLAPPGVTHVSLVPTQLQRLL---DSGQGPAAL---------KSLRAVLLGGAPIPPELLER-AADRGIPLYTT 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 367 YGMTEIGMALSNPLKGSRVPGAVGVPLPGVEVRIMmtnstnaiiaegnskgtrvkaglegKEGELLVRGSSVFQKYWNKP 446
Cdd:cd17630 142 YGMTETASQVATKRPDGFGRGGVGVLLPGRELRIV-------------------------EDGEIWVGGASLAMGYLRGQ 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 447 QEtaDTFTEDGWFKTGDTA-LYRDGVYWIMGRTSvDIIKSGGYKISALDVERHLLAHPDITDVAVIGAPDPTWGQKVTAV 525
Cdd:cd17630 197 LV--PEFNEDGWFTTKDLGeLHADGRLTVLGRAD-NMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAV 273
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 2073725801 526 VQLKKGktLTLSQLQAWAREHMAPYTIPTGLILVEEMPRNQMGKVNKKDLLRKF 579
Cdd:cd17630 274 IVGRGP--ADPAELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRAWL 325
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
207-575 |
1.57e-52 |
|
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: 183.45 E-value: 1.57e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 207 RPAMLIYTSGTTGRPKGVLHTHSSLQAMVQGLVSEWAWNKDDVILHTLPLHHVHGIVNKLMCPLWVGATCIMLP------ 280
Cdd:cd05944 3 DVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVVLAGpagyrn 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 281 EFSAQKVWeQLISSKSPmvNVFMAVPTIYSKLIEyydqhftQPQVQDFiravckERIRLMVSGSAALPQPVLERWAEITG 360
Cdd:cd05944 83 PGLFDNFW-KLVERYRI--TSLSTVPTVYAALLQ-------VPVNADI------SSLRFAMSGAAPLPVELRARFEDATG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 361 HVLLERYGMTEIGMALS-NPLKGSRVPGAVGVPLPGVEVRIMMTNstnaiiaeGNSKGTRVKAGleGKEGELLVRGSSVF 439
Cdd:cd05944 147 LPVVEGYGLTEATCLVAvNPPDGPKRPGSVGLRLPYARVRIKVLD--------GVGRLLRDCAP--DEVGEICVAGPGVF 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 440 QKYWNKpQETADTFTEDGWFKTGDTA-LYRDGVYWIMGRtSVDIIKSGGYKISALDVERHLLAHPDITDVAVIGAPDPTW 518
Cdd:cd05944 217 GGYLYT-EGNKNAFVADGWLNTGDLGrLDADGYLFITGR-AKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHA 294
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 2073725801 519 GQKVTAVVQLKKGKTLTLSQLQAWAREHMAPY-TIPTGLILVEEMPRNQMGKVNKKDL 575
Cdd:cd05944 295 GELPVAYVQLKPGAVVEEEELLAWARDHVPERaAVPKHIEVLEELPVTAVGKVFKPAL 352
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
58-575 |
1.70e-52 |
|
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: 186.76 E-value: 1.70e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 58 RASVYGDNVAITDHSGSHTFCSLYKNSKSLA-GLITKALTCqsGD---LQgkcisflCANDASYTVAQWAAWMCGGI--- 130
Cdd:cd05920 24 SAARHPDRIAVVDGDRRLTYRELDRRADRLAaGLRGLGIRP--GDrvvVQ-------LPNVAEFVVLFFALLRLGAVpvl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 131 AVPLYRKHppgELEYVISDSQSSLLVAGqpfmdtleplaqklglpclqlpttsslDTLQSEDIRMLPEQNISDWAErPAM 210
Cdd:cd05920 95 ALPSHRRS---ELSAFCAHAEAVAYIVP---------------------------DRHAGFDHRALARELAESIPE-VAL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 211 LIYTSGTTGRPKGVLHTHSSLQAMVQGLVsEWAW-NKDDVILHTLPLHHvhgivN-KLMCP-----LWVGATCIMLPEFS 283
Cdd:cd05920 144 FLLSGGTTGTPKLIPRTHNDYAYNVRASA-EVCGlDQDTVYLAVLPAAH-----NfPLACPgvlgtLLAGGRVVLAPDPS 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 284 AQKVWEqLISSKSpmVNVFMAVPTIYSKLIEYYDQHFTQPQvqdfiravckeRIRLMVSGSAALPQPVLERWAEITGHVL 363
Cdd:cd05920 218 PDAAFP-LIEREG--VTVTALVPALVSLWLDAAASRRADLS-----------SLRLLQVGGARLSPALARRVPPVLGCTL 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 364 LERYGMTEiGM----ALSNPlkGSRVPGAVGVPL-PGVEVRImmtnstnaIIAEGNSKGtrvkaglEGKEGELLVRGSSV 438
Cdd:cd05920 284 QQVFGMAE-GLlnytRLDDP--DEVIIHTQGRPMsPDDEIRV--------VDEEGNPVP-------PGEEGELLTRGPYT 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 439 FQKYWNKPQETADTFTEDGWFKTGDTA-LYRDGVYWIMGRTSvDIIKSGGYKISALDVERHLLAHPDITDVAVIGAPDPT 517
Cdd:cd05920 346 IRGYYRAPEHNARAFTPDGFYRTGDLVrRTPDGYLVVEGRIK-DQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDEL 424
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 2073725801 518 WGQKVTAVVQLkKGKTLTLSQLQAWAREH-MAPYTIPTGLILVEEMPRNQMGKVNKKDL 575
Cdd:cd05920 425 LGERSCAFVVL-RDPPPSAAQLRRFLRERgLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
211-572 |
7.13e-52 |
|
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: 180.77 E-value: 7.13e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 211 LIYTSGTTGRPKGVLHTHssLQAMvqGLVSEWAWN----KDDVILHTLPLHHVHGIVNKLMCPLWVGATCIMLPEFSAQK 286
Cdd:cd17638 5 IMFTSGTTGRSKGVMCAH--RQTL--RAAAAWADCadltEDDRYLIINPFFHTFGYKAGIVACLLTGATVVPVAVFDVDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 287 VWEQLISSKspmVNVFMAVPTIYSKLIEYydqhftqPQVQDFIRAvckeRIRLMVSGSAALPQPVLERW-AEITGHVLLE 365
Cdd:cd17638 81 ILEAIERER---ITVLPGPPTLFQSLLDH-------PGRKKFDLS----SLRAAVTGAATVPVELVRRMrSELGFETVLT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 366 RYGMTEIGMA-LSNPLKGSR-VPGAVGVPLPGVEVRImmtnstnaiiaegnskgtrvkagleGKEGELLVRGSSVFQKYW 443
Cdd:cd17638 147 AYGLTEAGVAtMCRPGDDAEtVATTCGRACPGFEVRI-------------------------ADDGEVLVRGYNVMQGYL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 444 NKPQETADTFTEDGWFKTGDT-ALYRDGVYWIMGRTSvDIIKSGGYKISALDVERHLLAHPDITDVAVIGAPDPTWGQKV 522
Cdd:cd17638 202 DDPEATAEAIDADGWLHTGDVgELDERGYLRITDRLK-DMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVG 280
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 2073725801 523 TAVVQLKKGKTLTLSQLQAWAREHMAPYTIPTGLILVEEMPRNQMGKVNK 572
Cdd:cd17638 281 KAFVVARPGVTLTEEDVIAWCRERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
37-584 |
2.15e-51 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 185.43 E-value: 2.15e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 37 TFASSYLKISPGVGRVAPVFSRASVYGDNVAITDHSG-SHTFCSLYKNSKSLAGLITKALTCQSGDLqgkcISFLCANDA 115
Cdd:PLN02574 28 KHPPVPLPSDPNLDAVSFIFSHHNHNGDTALIDSSTGfSISYSELQPLVKSMAAGLYHVMGVRQGDV----VLLLLPNSV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 116 SYTVAQWAAWMCGGIAVPLYRKHPPGELEYVISDSQSSLLVAGqpfMDTLEPLaQKLGLPCLQLPTTSSLDTLQSE---- 191
Cdd:PLN02574 104 YFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAFTS---PENVEKL-SPLGVPVIGVPENYDFDSKRIEfpkf 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 192 --------DIRMLPEQNISDwaerPAMLIYTSGTTGRPKGVLHTHSSLQAMVQGLV----SEWAW-NKDDVILHTLPLHH 258
Cdd:PLN02574 180 yelikedfDFVPKPVIKQDD----VAAIMYSSGTTGASKGVVLTHRNLIAMVELFVrfeaSQYEYpGSDNVYLAALPMFH 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 259 VHGIVNKLMCPLWVGATCIMLPEFSAQKVWEQLISSKspmVNVFMAVPTIYSKLIeyydqHFTQPqvqdfIRAVCKERIR 338
Cdd:PLN02574 256 IYGLSLFVVGLLSLGSTIVVMRRFDASDMVKVIDRFK---VTHFPVVPPILMALT-----KKAKG-----VCGEVLKSLK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 339 LMVSGSAALPQPVLERWAEITGHV-LLERYGMTE---IGMALSNPLKGSRVpGAVGVPLPGVEVRIMMTnSTNAIIAEGN 414
Cdd:PLN02574 323 QVSCGAAPLSGKFIQDFVQTLPHVdFIQGYGMTEstaVGTRGFNTEKLSKY-SSVGLLAPNMQAKVVDW-STGCLLPPGN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 415 SkgtrvkaglegkeGELLVRGSSVFQKYWNKPQETADTFTEDGWFKTGDTALY-RDGVYWIMGRTSvDIIKSGGYKISAL 493
Cdd:PLN02574 401 C-------------GELWIQGPGVMKGYLNNPKATQSTIDKDGWLRTGDIAYFdEDGYLYIVDRLK-EIIKYKGFQIAPA 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 494 DVERHLLAHPDITDVAVIGAPDPTWGQKVTAVVQLKKGKTLTLSQLQAWAREHMAPYTIPTGLILVEEMPRNQMGKVNKK 573
Cdd:PLN02574 467 DLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQGSTLSQEAVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRR 546
|
570
....*....|.
gi 2073725801 574 DLLRKFFPTRS 584
Cdd:PLN02574 547 ELKRSLTNSVS 557
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
119-575 |
2.20e-51 |
|
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: 182.70 E-value: 2.20e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 119 VAQWAAWMCGGIAVPLYRKHPPGELEYVISDSQSSLLVAGQPFMDTLEPlaqklglpclqlpttssldtlqsedirmlpe 198
Cdd:cd05969 40 FSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTEELYERTDP------------------------------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 199 qnisdwaERPAMLIYTSGTTGRPKGVLHTHSslqAMVQGLVS-EWAWN--KDDVILHTLPLHHVHGIVNKLMCPLWVGAT 275
Cdd:cd05969 89 -------EDPTLLHYTSGTTGTPKGVLHVHD---AMIFYYFTgKYVLDlhPDDIYWCTADPGWVTGTVYGIWAPWLNGVT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 276 CIMLP-EFSAQKVWEQLISSKspmVNVFMAVPTIYSKLIEYYDQhftqpqvqdFIRAVCKERIRLMVSGSAALpQPVLER 354
Cdd:cd05969 159 NVVYEgRFDAESWYGIIERVK---VTVWYTAPTAIRMLMKEGDE---------LARKYDLSSLRFIHSVGEPL-NPEAIR 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 355 WA-EITGHVLLERYGMTEIG-MALSNPLKGSRVPGAVGVPLPGVEvrimmtnstnAIIAEGNSKGTRvkaglEGKEGELL 432
Cdd:cd05969 226 WGmEVFGVPIHDTWWQTETGsIMIANYPCMPIKPGSMGKPLPGVK----------AAVVDENGNELP-----PGTKGILA 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 433 VRGS--SVFQKYWNKPQETADTFTeDGWFKTGDTAlYRD--GVYWIMGRTSvDIIKSGGYKISALDVERHLLAHPDITDV 508
Cdd:cd05969 291 LKPGwpSMFRGIWNDEERYKNSFI-DGWYLTGDLA-YRDedGYFWFVGRAD-DIIKTSGHRVGPFEVESALMEHPAVAEA 367
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 509 AVIGAPDPTWGQKVTAVVQLKKGKTLT---LSQLQAWAREHMAPYTIPTGLILVEEMPRNQMGKVNKKDL 575
Cdd:cd05969 368 GVIGKPDPLRGEIIKAFISLKEGFEPSdelKEEIINFVRQKLGAHVAPREIEFVDNLPKTRSGKIMRRVL 437
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
213-575 |
4.07e-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: 179.40 E-value: 4.07e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 213 YTSGTTGRPKGVLHTHSSL--------QAMvqglvsewAWNKDDVILHTLPLHHVHGIVNKLMCPLWVGATCIML-PEFS 283
Cdd:cd05917 9 FTSGTTGSPKGATLTHHNIvnngyfigERL--------GLTEQDRLCIPVPLFHCFGSVLGVLACLTHGATMVFPsPSFD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 284 AQKVWEQLISSKSpmvNVFMAVPTIYSKLIEyydqHFTQPQVqDFIRavckerIRLMVSGSAALPQPVLERwaeitghvL 363
Cdd:cd05917 81 PLAVLEAIEKEKC---TALHGVPTMFIAELE----HPDFDKF-DLSS------LRTGIMAGAPCPPELMKR--------V 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 364 LERYGMTEI----GMALSNPLKGSRVPGA--------VGVPLPGVEVRIMmtnstnaiiaegnSKGTRVKAGLeGKEGEL 431
Cdd:cd05917 139 IEVMNMKDVtiayGMTETSPVSTQTRTDDsiekrvntVGRIMPHTEAKIV-------------DPEGGIVPPV-GVPGEL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 432 LVRGSSVFQKYWNKPQETADTFTEDGWFKTGDTA-LYRDGVYWIMGRTSvDIIKSGGYKISALDVERHLLAHPDITDVAV 510
Cdd:cd05917 205 CIRGYSVMKGYWNDPEKTAEAIDGDGWLHTGDLAvMDEDGYCRIVGRIK-DMIIRGGENIYPREIEEFLHTHPKVSDVQV 283
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2073725801 511 IGAPDPTWGQKVTAVVQLKKGKTLTLSQLQAWAREHMAPYTIPTGLILVEEMPRNQMGKVNKKDL 575
Cdd:cd05917 284 VGVPDERYGEEVCAWIRLKEGAELTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKL 348
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
103-575 |
2.86e-50 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 181.44 E-value: 2.86e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 103 QGKCISFLCANDASYTVAQWAAWMCGGIAVPLYRKHPPGELEYVISDSQSSLLVAgqpFMDTLEPLAQKL--GLPCLQLP 180
Cdd:PRK12406 35 PGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIA---HADLLHGLASALpaGVTVLSVP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 181 TTSSLDTLQ--SEDIRMLPEQNIsDW--------------AERPAMLIYTSGTTGRPKGVLHTHSSL-QAMVQGLVSEWA 243
Cdd:PRK12406 112 TPPEIAAAYriSPALLTPPAGAI-DWegwlaqqepydgppVPQPQSMIYTSGTTGHPKGVRRAAPTPeQAAAAEQMRALI 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 244 WN--KDDVILHTLPLHH----VHGIVnklmcPLWVGATCIMLPEFSAQKVWeQLISsKSPMVNVFMaVPTIYSKLIEYYD 317
Cdd:PRK12406 191 YGlkPGIRALLTGPLYHsapnAYGLR-----AGRLGGVLVLQPRFDPEELL-QLIE-RHRITHMHM-VPTMFIRLLKLPE 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 318 qhftqpqvqdfirAVcKER-----IRLMVSGSAALPQPVLERWAEITGHVLLERYGMTEIG-MALSNPLKGSRVPGAVGV 391
Cdd:PRK12406 263 -------------EV-RAKydvssLRHVIHAAAPCPADVKRAMIEWWGPVIYEYYGSTESGaVTFATSEDALSHPGTVGK 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 392 PLPGVEVRImmtnstnaIIAEGNSKGTrvkagleGKEGELLVR--GSSVFQkYWNKPQETADTfTEDGWFKTGDTA-LYR 468
Cdd:PRK12406 329 AAPGAELRF--------VDEDGRPLPQ-------GEIGEIYSRiaGNPDFT-YHNKPEKRAEI-DRGGFITSGDVGyLDA 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 469 DGVYWIMGRTSvDIIKSGGYKISALDVERHLLAHPDITDVAVIGAPDPTWGQKVTAVVQLKKGKTLTLSQLQAWAREHMA 548
Cdd:PRK12406 392 DGYLFLCDRKR-DMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPGATLDEADIRAQLKARLA 470
|
490 500
....*....|....*....|....*..
gi 2073725801 549 PYTIPTGLILVEEMPRNQMGKVNKKDL 575
Cdd:PRK12406 471 GYKVPKHIEIMAELPREDSGKIFKRRL 497
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
103-575 |
5.18e-50 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 180.47 E-value: 5.18e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 103 QGKCISFLCANDASYTVAQWAAWMCGGIAVPL-YRKHPPgELEYVISDSQSSLLvagqpFMDtlEPLAQKLGLPCLQLpt 181
Cdd:PRK06145 51 QGDVVALLMKNSAAFLELAFAASYLGAVFLPInYRLAAD-EVAYILGDAGAKLL-----LVD--EEFDAIVALETPKI-- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 182 tsSLDTLQSEDIRML-------PEQNISdwAERPAM-LIYTSGTTGRPKGVLHTHSSLQAMVQGLVSEWAWNKDDVILHT 253
Cdd:PRK06145 121 --VIDAAAQADSRRLaqggleiPPQAAV--APTDLVrLMYTSGTTDRPKGVMHSYGNLHWKSIDHVIALGLTASERLLVV 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 254 LPLHHVHGIVNKLMCPLWVGATCIMLPEFSAQKVWEQLISSK------SP-MVNVFMAVPTIYSklieyYDQhftqpqvq 326
Cdd:PRK06145 197 GPLYHVGAFDLPGIAVLWVGGTLRIHREFDPEAVLAAIERHRltcawmAPvMLSRVLTVPDRDR-----FDL-------- 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 327 dfiravckERIRLMVSGSAALPQPVLERWAEI-TGHVLLERYGMTEI--GMALSNPLKGSRVPGAVGVPLPGVEVRIMmt 403
Cdd:PRK06145 264 --------DSLAWCIGGGEKTPESRIRDFTRVfTRARYIDAYGLTETcsGDTLMEAGREIEKIGSTGRALAHVEIRIA-- 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 404 nstnaiiaegNSKGTRVKAGLEGkegELLVRGSSVFQKYWNKPQETADTFTeDGWFKTGDTA-LYRDGVYWIMGRTSvDI 482
Cdd:PRK06145 334 ----------DGAGRWLPPNMKG---EICMRGPKVTKGYWKDPEKTAEAFY-GDWFRSGDVGyLDEEGFLYLTDRKK-DM 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 483 IKSGGYKISALDVERHLLAHPDITDVAVIGAPDPTWGQKVTAVVQLKKGKTLTLSQLQAWAREHMAPYTIPTGLILVEEM 562
Cdd:PRK06145 399 IISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPGATLTLEALDRHCRQRLASFKVPRQLKVRDEL 478
|
490
....*....|...
gi 2073725801 563 PRNQMGKVNKKDL 575
Cdd:PRK06145 479 PRNPSGKVLKRVL 491
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
122-575 |
7.05e-50 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 180.62 E-value: 7.05e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 122 WAAWMCGGIAVPLYRKHPPGELEYVISDSQSSLLVAGQPFMDTLEPLAQKLGLPCLQLPTTSSLDTLQSEDI------RM 195
Cdd:PRK07470 75 FAAFRLGAVWVPTNFRQTPDEVAYLAEASGARAMICHADFPEHAAAVRAASPDLTHVVAIGGARAGLDYEALvarhlgAR 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 196 LPEQNISdwAERPAMLIYTSGTTGRPKGVLHTHSSLQAMVQGLVSEW--AWNKDDVILHTLPLHHVHGIvnKLMCPLWVG 273
Cdd:PRK07470 155 VANAAVD--HDDPCWFFFTSGTTGRPKAAVLTHGQMAFVITNHLADLmpGTTEQDASLVVAPLSHGAGI--HQLCQVARG 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 274 ATCIMLP--EFSAQKVWeQLISsKSPMVNVFmAVPTIYSKLIEYydqhftqPQVQDFIRAvckeRIRLMVSGSAALPQPV 351
Cdd:PRK07470 231 AATVLLPseRFDPAEVW-ALVE-RHRVTNLF-TVPTILKMLVEH-------PAVDRYDHS----SLRYVIYAGAPMYRAD 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 352 LERWAEITGHVLLERYGMTEIG-------MALSNPLKGSRVP-GAVGVPLPGVEVRIMmtnstnaiiaegNSKGTRVKAG 423
Cdd:PRK07470 297 QKRALAKLGKVLVQYFGLGEVTgnitvlpPALHDAEDGPDARiGTCGFERTGMEVQIQ------------DDEGRELPPG 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 424 legKEGELLVRGSSVFQKYWNKPQETADTFtEDGWFKTGDTA-LYRDGVYWIMGRTSvDIIKSGGYKISALDVERHLLAH 502
Cdd:PRK07470 365 ---ETGEICVIGPAVFAGYYNNPEANAKAF-RDGWFRTGDLGhLDARGFLYITGRAS-DMYISGGSNVYPREIEEKLLTH 439
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2073725801 503 PDITDVAVIGAPDPTWGQKVTAVVQLKKGKTLTLSQLQAWAREHMAPYTIPTGLILVEEMPRNQMGKVNKKDL 575
Cdd:PRK07470 440 PAVSEVAVLGVPDPVWGEVGVAVCVARDGAPVDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMV 512
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
66-583 |
1.55e-48 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 176.25 E-value: 1.55e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 66 VAITDHSG-SHTFCSLYKNSKSLAGLItKALTCQSGDLqgkcISFLCANDASYTVAQWAAWMCGGIAVPLYRKHPPGELE 144
Cdd:PRK08276 2 AVIMAPSGeVVTYGELEARSNRLAHGL-RALGLREGDV----VAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 145 YVISDSQSSLLVAGQPFMDTLEPLAQKLGLPCLQL-------PTTSSLDTLQSEDirmlPEQNISDWAERPAMLiYTSGT 217
Cdd:PRK08276 77 YIVDDSGAKVLIVSAALADTAAELAAELPAGVPLLlvvagpvPGFRSYEEALAAQ----PDTPIADETAGADML-YSSGT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 218 TGRPKGV------LHTHSSLQAMVQGLVSEWAWNKDDVILHTLPLHHV-----HGIVNKLmcplwvGATCIMLPEFSAQK 286
Cdd:PRK08276 152 TGRPKGIkrplpgLDPDEAPGMMLALLGFGMYGGPDSVYLSPAPLYHTaplrfGMSALAL------GGTVVVMEKFDAEE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 287 VWEQLISSKspmVNVFMAVPTIYSKLIeyydqhftqpQVQDFIRAvckeR-----IRLMVSGSAALPQPVLERWAEITGH 361
Cdd:PRK08276 226 ALALIERYR---VTHSQLVPTMFVRML----------KLPEEVRA----RydvssLRVAIHAAAPCPVEVKRAMIDWWGP 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 362 VLLERYGMTE-IGMALSNPLKGSRVPGAVGVPLPGvEVRIMMTNstnaiiaegnskGTRVKAGlegKEGELLVRGSSVFQ 440
Cdd:PRK08276 289 IIHEYYASSEgGGVTVITSEDWLAHPGSVGKAVLG-EVRILDED------------GNELPPG---EIGTVYFEMDGYPF 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 441 KYWNKPQETADTFTEDGWFKTGDTA-LYRDGVYWIMGRTSvDIIKSGGYKISALDVERHLLAHPDITDVAVIGAPDPTWG 519
Cdd:PRK08276 353 EYHNDPEKTAAARNPHGWVTVGDVGyLDEDGYLYLTDRKS-DMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMG 431
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2073725801 520 QKVTAVVQLKKGKTLT---LSQLQAWAREHMAPYTIPTGLILVEEMPRNQMGKVNKKDLLRKFFPTR 583
Cdd:PRK08276 432 ERVKAVVQPADGADAGdalAAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLRDRYWEGR 498
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
64-575 |
1.74e-48 |
|
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.
Pssm-ID: 341247 [Multi-domain] Cd Length: 493 Bit Score: 176.16 E-value: 1.74e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 64 DNVAITDHSGSH--TFCSLY-KNSKSLAGLITKALtcQSGDLqgkcISFLCANDASYTVAQWAAWMCGGIAVPLYRKHPP 140
Cdd:cd05923 16 DACAIADPARGLrlTYSELRaRIEAVAARLHARGL--RPGQR----VAVVLPNSVEAVIALLALHRLGAVPALINPRLKA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 141 GELEYVISDSQ--SSLLVAGQPFMDtleplAQKLGLPCL----QLPTTSSL--DTLQSEDIRMLPEQnisdwaerPAMLI 212
Cdd:cd05923 90 AELAELIERGEmtAAVIAVDAQVMD-----AIFQSGVRVlalsDLVGLGEPesAGPLIEDPPREPEQ--------PAFVF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 213 YTSGTTGRPKGVL--HTHSSLQAMVQGLVSEWAWNKDDVILHTLPLHHVHGIVNKLMCPLWVGATCIMLPEFSAQKVWeQ 290
Cdd:cd05923 157 YTSGTTGLPKGAVipQRAAESRVLFMSTQAGLRHGRHNVVLGLMPLYHVIGFFAVLVAALALDGTYVVVEEFDPADAL-K 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 291 LISsKSPMVNVFmAVPTIYSKLIEYydQHFTQPQVqdfiravckERIRLMVSGSAALPQPVLERWAEITGHVLLERYGMT 370
Cdd:cd05923 236 LIE-QERVTSLF-ATPTHLDALAAA--AEFAGLKL---------SSLRHVTFAGATMPDAVLERVNQHLPGEKVNIYGTT 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 371 EIGMALSNPlkgSRVPGAVGVPLPGVEVRIMMTNstnaiiaegnskGTRVKAGLEGKEGELLVR--GSSVFQKYWNKPQE 448
Cdd:cd05923 303 EAMNSLYMR---DARTGTEMRPGFFSEVRIVRIG------------GSPDEALANGEEGELIVAaaADAAFTGYLNQPEA 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 449 TADTFtEDGWFKTGDTALYR-DGVYWIMGRTSvDIIKSGGYKISALDVERHLLAHPDITDVAVIGAPDPTWGQKVTAVVQ 527
Cdd:cd05923 368 TAKKL-QDGWYRTGDVGYVDpSGDVRILGRVD-DMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVV 445
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 2073725801 528 LKKGkTLTLSQLQAWARE-HMAPYTIPTGLILVEEMPRNQMGKVNKKDL 575
Cdd:cd05923 446 PREG-TLSADELDQFCRAsELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
86-578 |
1.93e-48 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 177.30 E-value: 1.93e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 86 SLA-GLITKALtcQSGDlqgkcISFLCANDASYTVaQW--AAWMCGGIAVPLYRKHPPGELEYVISDSQSSLLVAGQPFM 162
Cdd:PLN02860 44 SLAaGLLRLGL--RNGD-----VVAIAALNSDLYL-EWllAVACAGGIVAPLNYRWSFEEAKSAMLLVRPVMLVTDETCS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 163 DTLEPLaQKLGLPCLQL-------PTTSSLDTLQSEDIRMLPEQNISD------WAERPAMLI-YTSGTTGRPKGVLHTH 228
Cdd:PLN02860 116 SWYEEL-QNDRLPSLMWqvflespSSSVFIFLNSFLTTEMLKQRALGTteldyaWAPDDAVLIcFTSGTTGRPKGVTISH 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 229 SSLqaMVQGL--VSEWAWNKDDVILHTLPLHHVHGIvNKLMCPLWVGATCIMLPEFSAQKVWEQLissKSPMVNVFMAVP 306
Cdd:PLN02860 195 SAL--IVQSLakIAIVGYGEDDVYLHTAPLCHIGGL-SSALAMLMVGACHVLLPKFDAKAALQAI---KQHNVTSMITVP 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 307 TIYSKLIEYYDQHFTQPqvqdfiravCKERIRLMVSGSAALPQPVLERWAEITGHV-LLERYGMTEIG-----MALSNP- 379
Cdd:PLN02860 269 AMMADLISLTRKSMTWK---------VFPSVRKILNGGGSLSSRLLPDAKKLFPNAkLFSAYGMTEACssltfMTLHDPt 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 380 LKGSRVPGA-----------------VGVPLPGVEVRIMMTNSTnaiiaegnskgtrvkaglegKEGELLVRGSSVFQKY 442
Cdd:PLN02860 340 LESPKQTLQtvnqtksssvhqpqgvcVGKPAPHVELKIGLDESS--------------------RVGRILTRGPHVMLGY 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 443 WNKPQETADTFTEDGWFKTGDTALYRD-GVYWIMGRTSvDIIKSGGYKISALDVERHLLAHPDITDVAVIGAPDPTWGQK 521
Cdd:PLN02860 400 WGQNSETASVLSNDGWLDTGDIGWIDKaGNLWLIGRSN-DRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEM 478
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2073725801 522 VTAVVQLKKG------------KTLTLSQ--LQAWARE-HMAPYTIPTGLILVEE-MPRNQMGKVnKKDLLRK 578
Cdd:PLN02860 479 VVACVRLRDGwiwsdnekenakKNLTLSSetLRHHCREkNLSRFKIPKLFVQWRKpFPLTTTGKI-RRDEVRR 550
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
119-575 |
2.67e-48 |
|
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: 174.16 E-value: 2.67e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 119 VAQWAAWMCGGIAVPLYRKHPPGELEYVISDSQSSLLVagqpfmdtleplaqklglpclqlpttssldtlqsedirmlpe 198
Cdd:cd05971 46 IAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALV------------------------------------------ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 199 qniSDWAERPAMLIYTSGTTGRPKGVLHTHSSLQAMVQG--LVSEWAWNKDDVILHTLPLHHVHGIVNKLMCPLWVGATC 276
Cdd:cd05971 84 ---TDGSDDPALIIYTSGTTGPPKGALHAHRVLLGHLPGvqFPFNLFPRDGDLYWTPADWAWIGGLLDVLLPSLYFGVPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 277 IM--LPEFSAQKVWEQLISSKspMVNVFMavPTIYSKLIEyydqhFTQPQVQDFIRavckeRIRLMVSGSAALPQpVLER 354
Cdd:cd05971 161 LAhrMTKFDPKAALDLMSRYG--VTTAFL--PPTALKMMR-----QQGEQLKHAQV-----KLRAIATGGESLGE-ELLG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 355 WA-EITGHVLLERYGMTEIGMALSN-PLKGSRVPGAVGVPLPGVEVRIMmtnstnaiiaegNSKGTRVKaglEGKEGELL 432
Cdd:cd05971 226 WArEQFGVEVNEFYGQTECNLVIGNcSALFPIKPGSMGKPIPGHRVAIV------------DDNGTPLP---PGEVGEIA 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 433 VR--GSSVFQKYWNKPQETADTFTEDgWFKTGDTALY-RDGVYWIMGRTSvDIIKSGGYKISALDVERHLLAHPDITDVA 509
Cdd:cd05971 291 VElpDPVAFLGYWNNPSATEKKMAGD-WLLTGDLGRKdSDGYFWYVGRDD-DVITSSGYRIGPAEIEECLLKHPAVLMAA 368
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2073725801 510 VIGAPDPTWGQKVTAVVQLKKGKTLT---LSQLQAWAREHMAPYTIPTGLILVEEMPRNQMGKVNKKDL 575
Cdd:cd05971 369 VVGIPDPIRGEIVKAFVVLNPGETPSdalAREIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRREL 437
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
55-575 |
7.86e-48 |
|
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: 174.59 E-value: 7.86e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 55 VFSRASVYGDNVAITDHSGSHTFCSLYKNSKSLAGLItKALTCQSGDLQG----KCISFLcandasytVAQWAAWMCGGI 130
Cdd:TIGR03098 6 LEDAAARLPDATALVHHDRTLTYAALSERVLALASGL-RGLGLARGERVAiyldKRLETV--------TAMFGAALAGGV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 131 AVPLYRKHPPGELEYVISDSQSSLLVAGQPFMDTLEPlaqklGLP-CLQLPTTSSLDTLqSEDIRMLPEQNISDWAE--- 206
Cdd:TIGR03098 77 FVPINPLLKAEQVAHILADCNVRLLVTSSERLDLLHP-----ALPgCHDLRTLIIVGDP-AHASEGHPGEEPASWPKlla 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 207 -------------RPAMLIYTSGTTGRPKGVLHTHSSLQAMVQGLVSEWAWNKDDVILHTLPLHHVHGIvNKLMCPLWVG 273
Cdd:TIGR03098 151 lgdadpphpvidsDMAAILYTSGSTGRPKGVVLSHRNLVAGAQSVATYLENRPDDRLLAVLPLSFDYGF-NQLTTAFYVG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 274 ATCIMLPEFSAQKVweqLISSKSPMVNVFMAVPTIYSKLieyydqhftqpqVQDFIRAVCKERIRLMVSGSAALPQPVLE 353
Cdd:TIGR03098 230 ATVVLHDYLLPRDV---LKALEKHGITGLAAVPPLWAQL------------AQLDWPESAAPSLRYLTNSGGAMPRATLS 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 354 RWAEITGHV-LLERYGMTEIGMALS-NPLKGSRVPGAVGVPLPGVEVRIMmtnstnaiiaegNSKGTRVkagLEGKEGEL 431
Cdd:TIGR03098 295 RLRSFLPNArLFLMYGLTEAFRSTYlPPEEVDRRPDSIGKAIPNAEVLVL------------REDGSEC---APGEEGEL 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 432 LVRGSSVFQKYWNKPQETADTFT----EDGWFKTGDTALY--------RDGVYWIMGRTSvDIIKSGGYKISALDVERHL 499
Cdd:TIGR03098 360 VHRGALVAMGYWNDPEKTAERFRplppFPGELHLPELAVWsgdtvrrdEEGFLYFVGRRD-EMIKTSGYRVSPTEVEEVA 438
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2073725801 500 LAHPDITDVAVIGAPDPTWGQKVTAVVQLKKGKTLTLSQLQAWAREHMAPYTIPTGLILVEEMPRNQMGKVNKKDL 575
Cdd:TIGR03098 439 YATGLVAEAVAFGVPDPTLGQAIVLVVTPPGGEELDRAALLAECRARLPNYMVPALIHVRQALPRNANGKIDRKAL 514
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
87-579 |
9.04e-48 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 175.07 E-value: 9.04e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 87 LAGLITKAltcqsGDLQGKCISFLCANDASYTVAQWAAWMCGGIAVPLYRKHPPGELEyvisdSQSSLLVAGQPFMDTLE 166
Cdd:PRK05852 56 LAGQLTRS-----GLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQR-----VRSQAAGARVVLIDADG 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 167 PLAQKLG-LPCLQLPTTSSLDTLQSEDIrmlPEQNISDWAE-----------RP--AMLIYTSGTTGRPKGVLHTHSSLQ 232
Cdd:PRK05852 126 PHDRAEPtTRWWPLTVNVGGDSGPSGGT---LSVHLDAATEptpatstpeglRPddAMIMFTGGTTGLPKMVPWTHANIA 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 233 AMVQGLVSEWAWNKDDVILHTLPLHHVHGIVNKLMCPLWVGATcIMLP---EFSAQKVWEQLissKSPMVNVFMAVPTIY 309
Cdd:PRK05852 203 SSVRAIITGYRLSPRDATVAVMPLYHGHGLIAALLATLASGGA-VLLPargRFSAHTFWDDI---KAVGATWYTAVPTIH 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 310 SKLIEyydqhftQPQVQDFIRAvcKERIRLMVSGSAALPQPVLERWAEITGHVLLERYGMTEIgmalSNPLKGSRVPGAV 389
Cdd:PRK05852 279 QILLE-------RAATEPSGRK--PAALRFIRSCSAPLTAETAQALQTEFAAPVVCAFGMTEA----THQVTTTQIEGIG 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 390 GVPLPGVEVRiMMTNSTNAIIAEGNSKGTRVKAGlegKEGELLVRGSSVFQKYWNKPQETADTFTeDGWFKTGDT-ALYR 468
Cdd:PRK05852 346 QTENPVVSTG-LVGRSTGAQIRIVGSDGLPLPAG---AVGEVWLRGTTVVRGYLGDPTITAANFT-DGWLRTGDLgSLSA 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 469 DGVYWIMGRTSvDIIKSGGYKISALDVERHLLAHPDITDVAVIGAPDPTWGQKVTAVVQLKKGKTLTLSQLQAWAREHMA 548
Cdd:PRK05852 421 AGDLSIRGRIK-ELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIVPRESAPPTAEELVQFCRERLA 499
|
490 500 510
....*....|....*....|....*....|.
gi 2073725801 549 PYTIPTGLILVEEMPRNQMGKVNKKDLLRKF 579
Cdd:PRK05852 500 AFEIPASFQEASGLPHTAKGSLDRRAVAEQF 530
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
62-575 |
4.98e-47 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 173.32 E-value: 4.98e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 62 YGDNVAITDHSGSHTFCSLYKNSKSLAGLITKALTCQSGDLqgkcISFLCANDASYTVAQWAAWMCGGIAV---PLYrkh 138
Cdd:PRK08974 36 YADQPAFINMGEVMTFRKLEERSRAFAAYLQNGLGLKKGDR----VALMMPNLLQYPIALFGILRAGMIVVnvnPLY--- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 139 PPGELEYVISDSQSSLLVAGQPFMDTLEPLAQK----------LG---------------------LPCLQLPTTSSLDT 187
Cdd:PRK08974 109 TPRELEHQLNDSGAKAIVIVSNFAHTLEKVVFKtpvkhviltrMGdqlstakgtlvnfvvkyikrlVPKYHLPDAISFRS 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 188 LQSEDIRML---PEQNISDWAerpaMLIYTSGTTGRPKGVLHTHSSLQAMVqgLVSEWAW-----NKDDVILHTLPLHHV 259
Cdd:PRK08974 189 ALHKGRRMQyvkPELVPEDLA----FLQYTGGTTGVAKGAMLTHRNMLANL--EQAKAAYgpllhPGKELVVTALPLYHI 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 260 HGI-VNklmcplwvgatCIMLPEFSAQKVweqLIS------------SKSPMVnVFMAVPTIYSKLIEyyDQHFTQpqvQ 326
Cdd:PRK08974 263 FALtVN-----------CLLFIELGGQNL---LITnprdipgfvkelKKYPFT-AITGVNTLFNALLN--NEEFQE---L 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 327 DFiravckERIRLMVSGSAALPQPVLERWAEITGHVLLERYGMTEIGMALS-NPLKGSRVPGAVGVPLPGVEVRImmtns 405
Cdd:PRK08974 323 DF------SSLKLSVGGGMAVQQAVAERWVKLTGQYLLEGYGLTECSPLVSvNPYDLDYYSGSIGLPVPSTEIKL----- 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 406 tnaIIAEGNSKGtrvkaglEGKEGELLVRGSSVFQKYWNKPQETADTFtEDGWFKTGDTALY-RDGVYWIMGRTSvDIIK 484
Cdd:PRK08974 392 ---VDDDGNEVP-------PGEPGELWVKGPQVMLGYWQRPEATDEVI-KDGWLATGDIAVMdEEGFLRIVDRKK-DMIL 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 485 SGGYKISALDVERHLLAHPDITDVAVIGAPDPTWGQKVTAVVqLKKGKTLTLSQLQAWAREHMAPYTIPTGLILVEEMPR 564
Cdd:PRK08974 460 VSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAVKIFV-VKKDPSLTEEELITHCRRHLTGYKVPKLVEFRDELPK 538
|
570
....*....|.
gi 2073725801 565 NQMGKVNKKDL 575
Cdd:PRK08974 539 SNVGKILRREL 549
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
119-510 |
5.00e-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: 170.14 E-value: 5.00e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 119 VAQWAAWMCGGIAVPLYRKHPPGELEYVISDSQSSLLVAGQPFMDTLEPLAQKLGLPclqlpttSSLDTLQSEDIRMLPE 198
Cdd:TIGR01733 40 VAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDSALASRLAGLVLPVILL-------DPLELAALDDAPAPPP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 199 QNISDWAERPAMLIYTSGTTGRPKGVLHTHSSLQAMVQGLVSEWAWNKDDVILHTLPLHH---VHGIvnkLMcPLWVGAT 275
Cdd:TIGR01733 113 PDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDPDDRVLQFASLSFdasVEEI---FG-ALLAGAT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 276 CIMLPE---FSAQKVWEQLISSKSpmVNVFMAVPTIYsklieyydQHFTQPQVQDFiravckERIRLMVSGSAALPQPVL 352
Cdd:TIGR01733 189 LVVPPEdeeRDDAALLAALIAEHP--VTVLNLTPSLL--------ALLAAALPPAL------ASLRLVILGGEALTPALV 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 353 ERWAEITGHV-LLERYGMTE-----IGMALSNPLKGSRVPGAVGVPLPGVEVRIMmtnstnaiiaegNSKGTRVKAGLeg 426
Cdd:TIGR01733 253 DRWRARGPGArLINLYGPTEttvwsTATLVDPDDAPRESPVPIGRPLANTRLYVL------------DDDLRPVPVGV-- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 427 kEGELLVRGSSVFQKYWNKPQETADTFTEDG--------WFKTGDTALYR-DGVYWIMGRTSvDIIKSGGYKISALDVER 497
Cdd:TIGR01733 319 -VGELYIGGPGVARGYLNRPELTAERFVPDPfaggdgarLYRTGDLVRYLpDGNLEFLGRID-DQVKIRGYRIELGEIEA 396
|
410
....*....|...
gi 2073725801 498 HLLAHPDITDVAV 510
Cdd:TIGR01733 397 ALLRHPGVREAVV 409
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
69-505 |
6.16e-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: 171.09 E-value: 6.16e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 69 TDHSGSH-TFCSLYKNSKSLAgLITKALTCQSGDLqgkcISFLCANDASYTVAQWAAWMCGGIAVPLYRKHPPGELEYVI 147
Cdd:cd05914 1 LYYGGEPlTYKDLADNIAKFA-LLLKINGVGTGDR----VALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHIL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 148 SDSQSSLLVAGQPfmdtleplaqklglpclqlpttssldtlqsEDIrmlpeqnisdwaerpAMLIYTSGTTGRPKGVLHT 227
Cdd:cd05914 76 NHSEAKAIFVSDE------------------------------DDV---------------ALINYTSGTTGNSKGVMLT 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 228 HSSLQAMVQGLVSEWAWNKDDVILHTLPLHHVHGIVNKLMCPLWVGATCIMLPEFSAQKVWEQLISSKSPMVNVfmAVP- 306
Cdd:cd05914 111 YRNIVSNVDGVKEVVLLGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFLDKIPSAKIIALAFAQVTPTLGV--PVPl 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 307 ---------TIYSKLIEYYDQHFTQPQVQDFIRAVCKE--------RIRLMVSGSAALPQPVLERWAEItGHVLLERYGM 369
Cdd:cd05914 189 viekifkmdIIPKLTLKKFKFKLAKKINNRKIRKLAFKkvheafggNIKEFVIGGAKINPDVEEFLRTI-GFPYTIGYGM 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 370 TEIGMALSNPLKGSRVPGAVGVPLPGVEVRImmtnstnaiiaegnskgtrVKAGLEGKEGELLVRGSSVFQKYWNKPQET 449
Cdd:cd05914 268 TETAPIISYSPPNRIRLGSAGKVIDGVEVRI-------------------DSPDPATGEGEIIVRGPNVMKGYYKNPEAT 328
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 2073725801 450 ADTFTEDGWFKTGDTALYRDGVY-WIMGRTSVDIIKSGGYKISALDVERHLLAHPDI 505
Cdd:cd05914 329 AEAFDKDGWFHTGDLGKIDAEGYlYIRGRKKEMIVLSSGKNIYPEEIEAKINNMPFV 385
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
62-575 |
1.65e-46 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 171.87 E-value: 1.65e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 62 YGDNVAITDHSGSHTFCSLYKNSKSLAGLITKALTCQSGDLqgkcISFLCANDASYTVAQWAAWMCGGIAV---PLYrkh 138
Cdd:PRK05677 37 FADKPAFSNLGKTLTYGELYKLSGAFAAWLQQHTDLKPGDR----IAVQLPNVLQYPVAVFGAMRAGLIVVntnPLY--- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 139 PPGELEYVISDSQSSLLVAGQPFMDTLEPLAQKLGL-------------------------------PCLQLPTTSSLDT 187
Cdd:PRK05677 110 TAREMEHQFNDSGAKALVCLANMAHLAEKVLPKTGVkhvivtevadmlpplkrllinavvkhvkkmvPAYHLPQAVKFND 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 188 LQSEDiRMLPEQNISDWAERPAMLIYTSGTTGRPKGVLHTHSSL-------QAMVQGLVSEWAwnkdDVILHTLPLHHVH 260
Cdd:PRK05677 190 ALAKG-AGQPVTEANPQADDVAVLQYTGGTTGVAKGAMLTHRNLvanmlqcRALMGSNLNEGC----EILIAPLPLYHIY 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 261 GIVNKLMCPLWVGATCIMLP----------EFSAQKVweqlisskspmvNVFMAVPTIYSKLIeyydqhftqpQVQDFiR 330
Cdd:PRK05677 265 AFTFHCMAMMLIGNHNILISnprdlpamvkELGKWKF------------SGFVGLNTLFVALC----------NNEAF-R 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 331 AVCKERIRLMVSGSAALPQPVLERWAEITGHVLLERYGMTEIG-MALSNPLKGSRVpGAVGVPLPGVEVRIMmtnstnai 409
Cdd:PRK05677 322 KLDFSALKLTLSGGMALQLATAERWKEVTGCAICEGYGMTETSpVVSVNPSQAIQV-GTIGIPVPSTLCKVI-------- 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 410 iaegNSKGTRVKAGlegKEGELLVRGSSVFQKYWNKPQETADTFTEDGWFKTGDTALYR-DGVYWIMGRTSvDIIKSGGY 488
Cdd:PRK05677 393 ----DDDGNELPLG---EVGELCVKGPQVMKGYWQRPEATDEILDSDGWLKTGDIALIQeDGYMRIVDRKK-DMILVSGF 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 489 KISALDVERHLLAHPDITDVAVIGAPDPTWGQKVTAVVQLKKGKTLTLSQLQAWAREHMAPYTIPTGLILVEEMPRNQMG 568
Cdd:PRK05677 465 NVYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIKVFVVVKPGETLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVG 544
|
....*..
gi 2073725801 569 KVNKKDL 575
Cdd:PRK05677 545 KILRREL 551
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
59-575 |
3.42e-46 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 170.88 E-value: 3.42e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 59 ASVYGDNVAITDHSGSHTFCSLYKNSKSLA-GLITKALTcqsgdlQGKCISFLCANDASYTVAQWAAWMCGGIAVPLYRK 137
Cdd:PRK07788 59 ARRAPDRAALIDERGTLTYAELDEQSNALArGLLALGVR------AGDGVAVLARNHRGFVLALYAAGKVGARIILLNTG 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 138 HPPGELEYVISDSQSSLLVAGQPFMDTLEPLAQKLG-LPCLQL------PTTSSLDTLQS----EDIRMLPEqnisdWAE 206
Cdd:PRK07788 133 FSGPQLAEVAAREGVKALVYDDEFTDLLSALPPDLGrLRAWGGnpdddePSGSTDETLDDliagSSTAPLPK-----PPK 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 207 RPAMLIYTSGTTGRPKGVLHTHSSLQAMVQGLVSEWAWNKDDVILHTLPLHHVHGIVN-KLMCPLwvGATCIMLPEFSAQ 285
Cdd:PRK07788 208 PGGIVILTSGTTGTPKGAPRPEPSPLAPLAGLLSRVPFRAGETTLLPAPMFHATGWAHlTLAMAL--GSTVVLRRRFDPE 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 286 KVWEQLISSKspmVNVFMAVPTIYSKLIEYYDQHFTQPQVQdfiravckeRIRLMVSGSAALPQPVLERWAEITGHVLLE 365
Cdd:PRK07788 286 ATLEDIAKHK---ATALVVVPVMLSRILDLGPEVLAKYDTS---------SLKIIFVSGSALSPELATRALEAFGPVLYN 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 366 RYGMTEIGMA-LSNPLKGSRVPGAVGVPLPGVEVRIMmtnstnaiiaegNSKGTRVKaglEGKEGELLVRGSSVFQKYWN 444
Cdd:PRK07788 354 LYGSTEVAFAtIATPEDLAEAPGTVGRPPKGVTVKIL------------DENGNEVP---RGVVGRIFVGNGFPFEGYTD 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 445 kpqeTADTFTEDGWFKTGDTA-LYRDGVYWIMGRTSvDIIKSGGYKISALDVERHLLAHPDITDVAVIGAPDPTWGQKVT 523
Cdd:PRK07788 419 ----GRDKQIIDGLLSSGDVGyFDEDGLLFVDGRDD-DMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLR 493
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 2073725801 524 AVVQLKKGKTLTLSQLQAWAREHMAPYTIPTGLILVEEMPRNQMGKVNKKDL 575
Cdd:PRK07788 494 AFVVKAPGAALDEDAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKREL 545
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
52-575 |
4.88e-45 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 167.69 E-value: 4.88e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 52 VAPVFSRA-SVYGDNVAITDHSGSHTFCSLYKNSKSLAGLITKALTCQSGDLqgkcISFLCANDASYTVAQWAAWMCGGI 130
Cdd:PRK12492 26 VVEVFERScKKFADRPAFSNLGVTLSYAELERHSAAFAAYLQQHTDLVPGDR----IAVQMPNVLQYPIAVFGALRAGLI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 131 AV---PLYR----KH------------------------PPGELEYVISDSQSSLLVAGQPFM-DTLEPLAQKLgLPCLQ 178
Cdd:PRK12492 102 VVntnPLYTaremRHqfkdsgaralvylnmfgklvqevlPDTGIEYLIEAKMGDLLPAAKGWLvNTVVDKVKKM-VPAYH 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 179 LPTTSSLDTL--QSEDIRMLP-EQNISDwaerPAMLIYTSGTTGRPKGVLHTHSSLQAMVQGLVSEWAWNKDD------- 248
Cdd:PRK12492 181 LPQAVPFKQAlrQGRGLSLKPvPVGLDD----IAVLQYTGGTTGLAKGAMLTHGNLVANMLQVRACLSQLGPDgqplmke 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 249 ---VILHTLPLHHVHGIVNKLMCPLWVGATCIML------PEFSAQ-KVWEqlisskspmVNVFMAVPTIYSKLIEYydq 318
Cdd:PRK12492 257 gqeVMIAPLPLYHIYAFTANCMCMMVSGNHNVLItnprdiPGFIKElGKWR---------FSALLGLNTLFVALMDH--- 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 319 hftqPQVQ--DFiravckERIRLMVSGSAALPQPVLERWAEITGHVLLERYGMTEIG-MALSNPLKGSRVPGAVGVPLPG 395
Cdd:PRK12492 325 ----PGFKdlDF------SALKLTNSGGTALVKATAERWEQLTGCTIVEGYGLTETSpVASTNPYGELARLGTVGIPVPG 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 396 VEVRImmtnstnaIIAEGNSKGTrvkagleGKEGELLVRGSSVFQKYWNKPQETADTFTEDGWFKTGDTALY-RDGVYWI 474
Cdd:PRK12492 395 TALKV--------IDDDGNELPL-------GERGELCIKGPQVMKGYWQQPEATAEALDAEGWFKTGDIAVIdPDGFVRI 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 475 MGRTSvDIIKSGGYKISALDVERHLLAHPDITDVAVIGAPDPTWGQKVTAVVQLKKGkTLTLSQLQAWAREHMAPYTIPT 554
Cdd:PRK12492 460 VDRKK-DLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVKLFVVARDP-GLSVEELKAYCKENFTGYKVPK 537
|
570 580
....*....|....*....|.
gi 2073725801 555 GLILVEEMPRNQMGKVNKKDL 575
Cdd:PRK12492 538 HIVLRDSLPMTPVGKILRREL 558
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
107-569 |
6.71e-45 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 166.98 E-value: 6.71e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 107 ISFLCANDASYTVAQWAAWMCGGIAVPL-YRkHPPGELEYVISDSQSSLLVAGQPFMDTLEPLaqklglpclqLPTTSSL 185
Cdd:PRK07798 56 VGIYARNRIEYVEAMLGAFKARAVPVNVnYR-YVEDELRYLLDDSDAVALVYEREFAPRVAEV----------LPRLPKL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 186 DTL-QSEDIRMLPEQNIS--------------DWAERPA---MLIYTSGTTGRPKGVLHTHSSLQaMVQG---------- 237
Cdd:PRK07798 125 RTLvVVEDGSGNDLLPGAvdyedalaagsperDFGERSPddlYLLYTGGTTGMPKGVMWRQEDIF-RVLLggrdfatgep 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 238 ------LVSEWAWNKDDVILHTLPLHHVHGIVNKLMCpLWVGATCIMLP--EFSAQKVWE-------QLISskspMVNVF 302
Cdd:PRK07798 204 iedeeeLAKRAAAGPGMRRFPAPPLMHGAGQWAAFAA-LFSGQTVVLLPdvRFDADEVWRtierekvNVIT----IVGDA 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 303 MAVPtiyskLIEYYDQhftqpqvqdfiravcKER-----IRLMVSGSAALPQPVLERWAEITGHV-LLERYGMTEIG-MA 375
Cdd:PRK07798 279 MARP-----LLDALEA---------------RGPydlssLFAIASGGALFSPSVKEALLELLPNVvLTDSIGSSETGfGG 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 376 LSNPLKGSRVPGAVgvplpgvevRIMMTNSTnAIIAEgnsKGTRVKAGlEGKEGeLLVRGSSVFQKYWNKPQETADTFTE 455
Cdd:PRK07798 339 SGTVAKGAVHTGGP---------RFTIGPRT-VVLDE---DGNPVEPG-SGEIG-WIARRGHIPLGYYKDPEKTAETFPT 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 456 -DG--WFKTGDTALYR-DGVYWIMGRTSVdIIKSGGYKISALDVERHLLAHPDITDVAVIGAPDPTWGQKVTAVVQLKKG 531
Cdd:PRK07798 404 iDGvrYAIPGDRARVEaDGTITLLGRGSV-CINTGGEKVFPEEVEEALKAHPDVADALVVGVPDERWGQEVVAVVQLREG 482
|
490 500 510
....*....|....*....|....*....|....*...
gi 2073725801 532 KTLTLSQLQAWAREHMAPYTIPTGLILVEEMPRNQMGK 569
Cdd:PRK07798 483 ARPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
113-572 |
9.65e-44 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 164.18 E-value: 9.65e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 113 NDASYTVAQWAAWMCGGIAV---PLYRKHppgELEYVISDSQSSLLVAGQPF--------MDTLEP---LAQKLGLPCLQ 178
Cdd:PRK12583 79 NCAEWLLTQFATARIGAILVninPAYRAS---ELEYALGQSGVRWVICADAFktsdyhamLQELLPglaEGQPGALACER 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 179 LPTTSSLDTLQSE---------DIRMLPEQ-NISDWAERPAML--------IYTSGTTGRPKGVLHTHSSL--------Q 232
Cdd:PRK12583 156 LPELRGVVSLAPApppgflawhELQARGETvSREALAERQASLdrddpiniQYTSGTTGFPKGATLSHHNIlnngyfvaE 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 233 AMvqGLVSEwawnkdDVILHTLPLHHVHGIV-NKLMCpLWVGAtCIMLP--EFSAQKVWeQLISSKSpmVNVFMAVPTIY 309
Cdd:PRK12583 236 SL--GLTEH------DRLCVPVPLYHCFGMVlANLGC-MTVGA-CLVYPneAFDPLATL-QAVEEER--CTALYGVPTMF 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 310 SKLIEYydqhftqPQVQDFIRAvckeRIRLMVSGSAALPQPVLER-WAEITGHVLLERYGMTEIG-----MALSNPLKgS 383
Cdd:PRK12583 303 IAELDH-------PQRGNFDLS----SLRTGIMAGAPCPIEVMRRvMDEMHMAEVQIAYGMTETSpvslqTTAADDLE-R 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 384 RVPgAVGVPLPGVEVRImmtnstnaIIAEGNSKGTrvkagleGKEGELLVRGSSVFQKYWNKPQETADTFTEDGWFKTGD 463
Cdd:PRK12583 371 RVE-TVGRTQPHLEVKV--------VDPDGATVPR-------GEIGELCTRGYSVMKGYWNNPEATAESIDEDGWMHTGD 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 464 TA-LYRDGVYWIMGRtSVDIIKSGGYKISALDVERHLLAHPDITDVAVIGAPDPTWGQKVTAVVQLKKGKTLTLSQLQAW 542
Cdd:PRK12583 435 LAtMDEQGYVRIVGR-SKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRLHPGHAASEEELREF 513
|
490 500 510
....*....|....*....|....*....|
gi 2073725801 543 AREHMAPYTIPTGLILVEEMPRNQMGKVNK 572
Cdd:PRK12583 514 CKARIAHFKVPRYFRFVDEFPMTVTGKVQK 543
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
104-513 |
2.52e-43 |
|
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: 161.87 E-value: 2.52e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 104 GKCISFLCANDASYTVAQWAAWMCGGIAVPLYRKHPPGELEYVISDSQSSLLVAGQpfMDTLEplAQKLGLP-----CLQ 178
Cdd:cd05932 31 GSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFVGK--LDDWK--AMAPGVPeglisISL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 179 LPTTSSLDTLQSEDI--RMLPEQN-ISDWAERPAMLIYTSGTTGRPKGVLHTHSSLQAMVQGLVSEWAWNKDDVILHTLP 255
Cdd:cd05932 107 PPPSAANCQYQWDDLiaQHPPLEErPTRFPEQLATLIYTSGTTGQPKGVMLTFGSFAWAAQAGIEHIGTEENDRMLSYLP 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 256 LHHVHGIVNKLMCPLWVGATcIMLPE-----------------FSAQKVW---EQLISSKSPM--VNVFMAVPTIySKLI 313
Cdd:cd05932 187 LAHVTERVFVEGGSLYGGVL-VAFAEsldtfvedvqrarptlfFSVPRLWtkfQQGVQDKIPQqkLNLLLKIPVV-NSLV 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 314 EyydqhftqpqvQDFIRAVCKERIRLMVSGSAALPQPVLErWAEITGHVLLERYGMTEiGMALSNPLK-GSRVPGAVGVP 392
Cdd:cd05932 265 K-----------RKVLKGLGLDQCRLAGCGSAPVPPALLE-WYRSLGLNILEAYGMTE-NFAYSHLNYpGRDKIGTVGNA 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 393 LPGVEVRImmtnstnaiiaegnskgtrvkagleGKEGELLVRGSSVFQKYWNKPQETADTFTEDGWFKTGDT-ALYRDGV 471
Cdd:cd05932 332 GPGVEVRI-------------------------SEDGEILVRSPALMMGYYKDPEATAEAFTADGFLRTGDKgELDADGN 386
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 2073725801 472 YWIMGRTSvDIIK-SGGYKISALDVERHLLAHPDITDVAVIGA 513
Cdd:cd05932 387 LTITGRVK-DIFKtSKGKYVAPAPIENKLAEHDRVEMVCVIGS 428
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
123-576 |
1.13e-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: 159.14 E-value: 1.13e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 123 AAWMCGGIAVPLYRKHPPGELEYVISDSQSSLLVAGQPFMDTLeplaqKLGLPCLQLPTTSsLDTLQSEDIRMLPEQNIS 202
Cdd:cd05922 41 AGGRLGLVFVPLNPTLKESVLRYLVADAGGRIVLADAGAADRL-----RDALPASPDPGTV-LDADGIRAARASAPAHEV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 203 DwAERPAMLIYTSGTTGRPKGVLHTHSSLQAMVQGLVSEWAWNKDDVILHTLPLHHVHGIvNKLMCPLWVGATCIMLPEF 282
Cdd:cd05922 115 S-HEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADDRALTVLPLSYDYGL-SVLNTHLLRGATLVLTNDG 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 283 S-AQKVWEQLISSKSPMvnvFMAVPTIYSKLIEyydqhftqpqvqdFIRAVCK-ERIRLMVSGSAALPQPVLERWAE-IT 359
Cdd:cd05922 193 VlDDAFWEDLREHGATG---LAGVPSTYAMLTR-------------LGFDPAKlPSLRYLTQAGGRLPQETIARLRElLP 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 360 GHVLLERYGMTEI--GMALSNPLKGSRVPGAVGVPLPGVEVRIMmtnstnaiiaegNSKGTRVKAGlegKEGELLVRGSS 437
Cdd:cd05922 257 GAQVYVMYGQTEAtrRMTYLPPERILEKPGSIGLAIPGGEFEIL------------DDDGTPTPPG---EPGEIVHRGPN 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 438 VFQKYWNKPQETADTFTEDGWFKTGDTALYR-DGVYWIMGRTSvDIIKSGGYKISALDVERHLLAHPDITDVAVIGAPDP 516
Cdd:cd05922 322 VMKGYWNDPPYRRKEGRGGGVLHTGDLARRDeDGFLFIVGRRD-RMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDP 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 517 TwGQKVTAVVQLKKGktLTLSQLQAWAREHMAPYTIPTGLILVEEMPRNQMGKVNKKDLL 576
Cdd:cd05922 401 L-GEKLALFVTAPDK--IDPKDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
52-575 |
1.27e-42 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 161.20 E-value: 1.27e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 52 VAPVFSRASV-YGDNVAITDHSGSHTFCSLYKNSKSLAGLITKALTCQSGDLqgkcISFLCANDASYTVAQWAAwMCGGI 130
Cdd:PRK08751 27 VAEVFATSVAkFADRPAYHSFGKTITYREADQLVEQFAAYLLGELQLKKGDR----VALMMPNCLQYPIATFGV-LRAGL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 131 AV----PLYrkhPPGELEYVISDSQSSLLVAGQPFMDTLEPLAQklGLPCLQLPTTSSLDTLQ----------------- 189
Cdd:PRK08751 102 TVvnvnPLY---TPRELKHQLIDSGASVLVVIDNFGTTVQQVIA--DTPVKQVITTGLGDMLGfpkaalvnfvvkyvkkl 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 190 ------SEDIRM-----------LPEQNISdwAERPAMLIYTSGTTGRPKGVLHTHSSLQAMVQGlVSEWAWNKD----- 247
Cdd:PRK08751 177 vpeyriNGAIRFrealalgrkhsMPTLQIE--PDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQ-AHQWLAGTGkleeg 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 248 -DVILHTLPLHHVHGIVNKLMCPLWVGATcimlpefsaqkvwEQLISSKSPM-----------VNVFMAVPTIYSKLIEY 315
Cdd:PRK08751 254 cEVVITALPLYHIFALTANGLVFMKIGGC-------------NHLISNPRDMpgfvkelkktrFTAFTGVNTLFNGLLNT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 316 --YDQhftqpqvQDFiravckERIRLMVSGSAALPQPVLERWAEITGHVLLERYGMTEIG-MALSNPLKGSRVPGAVGVP 392
Cdd:PRK08751 321 pgFDQ-------IDF------SSLKMTLGGGMAVQRSVAERWKQVTGLTLVEAYGLTETSpAACINPLTLKEYNGSIGLP 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 393 LPgvevrimmtnSTNAIIAEGNSKGTRVkagleGKEGELLVRGSSVFQKYWNKPQETADTFTEDGWFKTGDTA-LYRDGV 471
Cdd:PRK08751 388 IP----------STDACIKDDAGTVLAI-----GEIGELCIKGPQVMKGYWKRPEETAKVMDADGWLHTGDIArMDEQGF 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 472 YWIMGRTSvDIIKSGGYKISALDVERHLLAHPDITDVAVIGAPDPTWGQKVTAVVqLKKGKTLTLSQLQAWAREHMAPYT 551
Cdd:PRK08751 453 VYIVDRKK-DMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEIVKVVI-VKKDPALTAEDVKAHARANLTGYK 530
|
570 580
....*....|....*....|....
gi 2073725801 552 IPTGLILVEEMPRNQMGKVNKKDL 575
Cdd:PRK08751 531 QPRIIEFRKELPKTNVGKILRREL 554
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
63-575 |
1.83e-42 |
|
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: 158.99 E-value: 1.83e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 63 GDNVAITDHSGSHTFCSLYKNSKSLAGLITKALTCQsGDLQGKCISflcaNDASYTVAQWAAWMCGGIAVPLYRKHPPGE 142
Cdd:cd12116 1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGP-GDRVAVYLP----RSARLVAAMLAVLKAGAAYVPLDPDYPADR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 143 LEYVISDSQSSLLVAGQpfmDTLEPLAQKLGLPCLQLPTTSSLDTLQSEDirMLPEQnisdwaerPAMLIYTSGTTGRPK 222
Cdd:cd12116 76 LRYILEDAEPALVLTDD---ALPDRLPAGLPVLLLALAAAAAAPAAPRTP--VSPDD--------LAYVIYTSGSTGRPK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 223 GVLHTHSSLQAMVQGLVSEWAWNKDDVILH-TLPLHHVHGIvnKLMCPLWVGATCIMLPEfSAQKVWEQL---ISSKSPm 298
Cdd:cd12116 143 GVVVSHRNLVNFLHSMRERLGLGPGDRLLAvTTYAFDISLL--ELLLPLLAGARVVIAPR-ETQRDPEALarlIEAHSI- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 299 vNVFMAVPTIYSKLIEyydqhfTQPQVQDFIRAVCkerirlmvsGSAALPQPVLERWAEITGhVLLERYGMTEIGM-ALS 377
Cdd:cd12116 219 -TVMQATPATWRMLLD------AGWQGRAGLTALC---------GGEALPPDLAARLLSRVG-SLWNLYGPTETTIwSTA 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 378 NPLKGSRVPGAVGVPLPGVEVRIMmtnstnaiiaegNSKGTRVKAGLEGkegELLVRGSSVFQKYWNKPQETADTFTEDG 457
Cdd:cd12116 282 ARVTAAAGPIPIGRPLANTQVYVL------------DAALRPVPPGVPG---ELYIGGDGVAQGYLGRPALTAERFVPDP 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 458 -------WFKTGDTALYR-DGVYWIMGRTSvDIIKSGGYKISALDVERHLLAHPDITDVAVIGAPDPTwGQKVTAVVQLK 529
Cdd:cd12116 347 fagpgsrLYRTGDLVRRRaDGRLEYLGRAD-GQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGG-DRRLVAYVVLK 424
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 2073725801 530 KGKTLTLSQLQAWAREHMAPYTIPTGLILVEEMPRNQMGKVNKKDL 575
Cdd:cd12116 425 AGAAPDAAALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
197-578 |
1.94e-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: 1.94e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 197 PEQNISDWAERPAMLIY-TSGTTGRPKGVLHTHSSLQamvQGL-VSEWAW---NKDDVILHTLPLHHVHGIVNKLMCPlW 271
Cdd:cd05928 164 TEHHCVETGSQEPMAIYfTSGTTGSPKMAEHSHSSLG---LGLkVNGRYWldlTASDIMWNTSDTGWIKSAWSSLFEP-W 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 272 VGATCIM---LPEFSAQKVWEQLisSKSPmVNVFMAVPTIYSKLIEyydQHFTQPQVQdfiravckeRIRLMVSGSAALP 348
Cdd:cd05928 240 IQGACVFvhhLPRFDPLVILKTL--SSYP-ITTFCGAPTVYRMLVQ---QDLSSYKFP---------SLQHCVTGGEPLN 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 349 QPVLERWAEITGHVLLERYGMTEIGMALSNPlKGSRV-PGAVGVPLPGVEVRIMmtnstnaiiaegNSKGTRVKaglEGK 427
Cdd:cd05928 305 PEVLEKWKAQTGLDIYEGYGQTETGLICANF-KGMKIkPGSMGKASPPYDVQII------------DDNGNVLP---PGT 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 428 EGELLVRGS-----SVFQKYWNKPQETADTFTEDGWFkTGDTALY-RDGVYWIMGRtSVDIIKSGGYKISALDVERHLLA 501
Cdd:cd05928 369 EGDIGIRVKpirpfGLFSGYVDNPEKTAATIRGDFYL-TGDRGIMdEDGYFWFMGR-ADDVINSSGYRIGPFEVESALIE 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 502 HPDITDVAVIGAPDPTWGQKVTAVVQLKKG------KTLTLsQLQAWAREHMAPYTIPTGLILVEEMPRNQMGKVNKKDL 575
Cdd:cd05928 447 HPAVVESAVVSSPDPIRGEVVKAFVVLAPQflshdpEQLTK-ELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNEL 525
|
...
gi 2073725801 576 LRK 578
Cdd:cd05928 526 RDK 528
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
190-572 |
2.83e-42 |
|
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: 159.58 E-value: 2.83e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 190 SEDIRMlPEQNISDWAERPAMLIYTSGTTGRPKGVLHTHS-SLQAMVQGlvSEWAWNKDDVILHTLPLHHVHGIVNKLMC 268
Cdd:cd05970 170 SPDFER-PTANSYPCGEDILLVYFSSGTTGMPKMVEHDFTyPLGHIVTA--KYWQNVREGGLHLTVADTGWGKAVWGKIY 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 269 PLWVGATCIML---PEFSAQKVWEQLISSKspmVNVFMAVPTIYSKLIEYYDQHFtqpqvqDFiravckERIRLMVSGSA 345
Cdd:cd05970 247 GQWIAGAAVFVydyDKFDPKALLEKLSKYG---VTTFCAPPTIYRFLIREDLSRY------DL------SSLRYCTTAGE 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 346 ALPQPVLERWAEITGHVLLERYGMTEIGMALSNPLKGSRVPGAVGVPLPGVEVRIMmtnstnaiiaegNSKGTRVKAGle 425
Cdd:cd05970 312 ALNPEVFNTFKEKTGIKLMEGFGQTETTLTIATFPWMEPKPGSMGKPAPGYEIDLI------------DREGRSCEAG-- 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 426 gKEGELLVRGSS-----VFQKYWNKPQETADTFtEDGWFKTGDTA-LYRDGVYWIMGRTSvDIIKSGGYKISALDVERHL 499
Cdd:cd05970 378 -EEGEIVIRTSKgkpvgLFGGYYKDAEKTAEVW-HDGYYHTGDAAwMDEDGYLWFVGRTD-DLIKSSGYRIGPFEVESAL 454
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2073725801 500 LAHPDITDVAVIGAPDPTWGQKVTAVVQLKKGKTLTLS---QLQAWAREHMAPYTIPTGLILVEEMPRNQMGKVNK 572
Cdd:cd05970 455 IQHPAVLECAVTGVPDPIRGQVVKATIVLAKGYEPSEElkkELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRR 530
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
59-572 |
3.39e-42 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 159.34 E-value: 3.39e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 59 ASVYGDNVAITDHSGSHTFCSLYKNSKSLAGlitkALTcQSGDLQGKCISFLCANDASYTVAQWAAWMCGGIAVPLYRKH 138
Cdd:PRK08162 28 AEVYPDRPAVIHGDRRRTWAETYARCRRLAS----ALA-RRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 139 PPGELEYVISDSQSSLLVAGQPFMDTLEPLAQKLGLPCL--------QLPTTSSLDTLQSEDirMLPEQNIS-DWaERPA 209
Cdd:PRK08162 103 DAASIAFMLRHGEAKVLIVDTEFAEVAREALALLPGPKPlvidvddpEYPGGRFIGALDYEA--FLASGDPDfAW-TLPA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 210 ------MLIYTSGTTGRPKGVLHTHSSLQAMVQGLVSEWAWNKDDVILHTLPLHHVHGivnklMCPLW----VGATCIML 279
Cdd:PRK08162 180 dewdaiALNYTSGTTGNPKGVVYHHRGAYLNALSNILAWGMPKHPVYLWTLPMFHCNG-----WCFPWtvaaRAGTNVCL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 280 PEFSAQKVWEqLISSKSpmVNVFMAVPTIYSKLIEYYDQHftqpqvqdfiRAVCKERIRLMVSGsAALPQPVLERWAEIt 359
Cdd:PRK08162 255 RKVDPKLIFD-LIREHG--VTHYCGAPIVLSALINAPAEW----------RAGIDHPVHAMVAG-AAPPAAVIAKMEEI- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 360 GHVLLERYGMTEI-GMALSNPLKG----------SRVPGAVGVPLPGVE-VRIMMTNSTNAIIAEGNSKGtrvkaglegk 427
Cdd:PRK08162 320 GFDLTHVYGLTETyGPATVCAWQPewdalplderAQLKARQGVRYPLQEgVTVLDPDTMQPVPADGETIG---------- 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 428 egELLVRGSSVFQKYWNKPQETADTFtEDGWFKTGDTA-LYRDGVYWIMGRtSVDIIKSGGYKISALDVERHLLAHPDIT 506
Cdd:PRK08162 390 --EIMFRGNIVMKGYLKNPKATEEAF-AGGWFHTGDLAvLHPDGYIKIKDR-SKDIIISGGENISSIEVEDVLYRHPAVL 465
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2073725801 507 DVAVIGAPDPTWGQKVTAVVQLKKGKTLTLSQLQAWAREHMAPYTIPTGLILvEEMPRNQMGKVNK 572
Cdd:PRK08162 466 VAAVVAKPDPKWGEVPCAFVELKDGASATEEEIIAHCREHLAGFKVPKAVVF-GELPKTSTGKIQK 530
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
64-575 |
3.53e-42 |
|
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: 157.41 E-value: 3.53e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 64 DNVAITDHSGSHTFCSLYKNSKSLAGLITKAltcqsGDLQGKCISFLCANDASYTVAQWAAWMCGGIAVPLYRKHPPGEL 143
Cdd:cd05945 6 DRPAVVEGGRTLTYRELKERADALAAALASL-----GLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 144 EYVISDSQSSLLVAgqpfmdtleplaqklglpclqlpttssldtlqsedirmlpeqnisDWAErPAMLIYTSGTTGRPKG 223
Cdd:cd05945 81 REILDAAKPALLIA---------------------------------------------DGDD-NAYIIFTSGSTGRPKG 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 224 VLHTHSSLQAMVQGLVSEWAWNKDDVILHTLPLH---HVHGIvnklMCPLWVGATCIMLPEfSAQKVWEQLIS--SKSPm 298
Cdd:cd05945 115 VQISHDNLVSFTNWMLSDFPLGPGDVFLNQAPFSfdlSVMDL----YPALASGATLVPVPR-DATADPKQLFRflAEHG- 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 299 VNVFMAVPTIYSKLIEyyDQHFTQ---PQVQDFIraVCKErirlmvsgsaALPQPVLERWAEIT-GHVLLERYGMTEIGM 374
Cdd:cd05945 189 ITVWVSTPSFAAMCLL--SPTFTPeslPSLRHFL--FCGE----------VLPHKTARALQQRFpDARIYNTYGPTEATV 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 375 ALS------NPLKGS-RVPgaVGVPLPGVEVRIMmtnstnaiiaegNSKGTRVKaglEGKEGELLVRGSSVFQKYWNKPQ 447
Cdd:cd05945 255 AVTyievtpEVLDGYdRLP--IGYAKPGAKLVIL------------DEDGRPVP---PGEKGELVISGPSVSKGYLNNPE 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 448 ETADTFTED---GWFKTGDtALYR--DGVYWIMGRTSvDIIKSGGYKISALDVERHLLAHPDITDVAVIGAPDPTWGQKV 522
Cdd:cd05945 318 KTAAAFFPDegqRAYRTGD-LVRLeaDGLLFYRGRLD-FQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTEL 395
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 2073725801 523 TAVVQLKKGKTLTL-SQLQAWAREHMAPYTIPTGLILVEEMPRNQMGKVNKKDL 575
Cdd:cd05945 396 IAFVVPKPGAEAGLtKAIKAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
128-575 |
3.76e-42 |
|
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341304 [Multi-domain] Cd Length: 450 Bit Score: 157.53 E-value: 3.76e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 128 GGIAVPLYRKHPPGELEYVISDSQSSLLVAGQPfmdtleplaqklglpclqlpttssldtlqsedirmlpeqnisdwaER 207
Cdd:cd17649 61 GGAYVPLDPEYPAERLRYMLEDSGAGLLLTHHP---------------------------------------------RQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 208 PAMLIYTSGTTGRPKGVLHTHSSLQAMVQGLVSEWAWNKDDVILHTLPLhHVHGIVNKLMCPLWVGATCIMLPE---FSA 284
Cdd:cd17649 96 LAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAERYGLTPGDRELQFASF-NFDGAHEQLLPPLICGACVVLRPDelwASA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 285 QKVWEQLISSKspmVNVfMAVPTIY-SKLIEYYDQHFTQPQVqdfiravckeRIRLMVSGSAALPQPVLERWAeiTGHV- 362
Cdd:cd17649 175 DELAEMVRELG---VTV-LDLPPAYlQQLAEEADRTGDGRPP----------SLRLYIFGGEALSPELLRRWL--KAPVr 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 363 LLERYGMTE---IGMALSNPLKGSRVPGAV--GVPLPGVEVRIMmtnstnaiiaegnskGTRVKAGLEGKEGELLVRGSS 437
Cdd:cd17649 239 LFNAYGPTEatvTPLVWKCEAGAARAGASMpiGRPLGGRSAYIL---------------DADLNPVPVGVTGELYIGGEG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 438 VFQKYWNKPQETADTFTEDG-------WFKTGDTALYR-DGVYWIMGRtsVD-IIKSGGYKISALDVERHLLAHPDITDV 508
Cdd:cd17649 304 LARGYLGRPELTAERFVPDPfgapgsrLYRTGDLARWRdDGVIEYLGR--VDhQVKIRGFRIELGEIEAALLEHPGVREA 381
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2073725801 509 AVIGAPDPTwGQKVTAVVQLKKGKTL--TLSQLQAWAREHMAPYTIPTGLILVEEMPRNQMGKVNKKDL 575
Cdd:cd17649 382 AVVALDGAG-GKQLVAYVVLRAAAAQpeLRAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKAL 449
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
119-583 |
9.69e-42 |
|
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: 161.95 E-value: 9.69e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 119 VAQWAAWMCGGIAVPLYRKHPPGELEYVISDSQSSLLVAGQPFMDTLeplaQKLGLPCLQLPTTSSLDtlQSEDirmLPE 198
Cdd:COG1020 541 VALLAVLKAGAAYVPLDPAYPAERLAYMLEDAGARLVLTQSALAARL----PELGVPVLALDALALAA--EPAT---NPP 611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 199 QNISdwAERPAMLIYTSGTTGRPKGVLHTHSSLQAMVQGLVSEWAWNKDDVILHTLPLHH---VHGIvnklMCPLWVGAT 275
Cdd:COG1020 612 VPVT--PDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFASLSFdasVWEI----FGALLSGAT 685
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 276 CIMLPE---FSAQKVWEQLISSKspmVNVFMAVPTIYSKLIEYYDQHFTqpqvqdfiravckeRIRLMVSGSAALPQPVL 352
Cdd:COG1020 686 LVLAPPearRDPAALAELLARHR---VTVLNLTPSLLRALLDAAPEALP--------------SLRLVLVGGEALPPELV 748
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 353 ERWAEITGHV-LLERYGMTE------IGMALSNPLKGSRVPgaVGVPLPGVEVRIMmtnstnaiiaegNSKGTRVKAGLe 425
Cdd:COG1020 749 RRWRARLPGArLVNLYGPTEttvdstYYEVTPPDADGGSVP--IGRPIANTRVYVL------------DAHLQPVPVGV- 813
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 426 gkEGELLVRGSSVFQKYWNKPQETA-----DTFTEDG--WFKTGDTALYR-DGVYWIMGRtsVDI-IKSGGYKISALDVE 496
Cdd:COG1020 814 --PGELYIGGAGLARGYLNRPELTAerfvaDPFGFPGarLYRTGDLARWLpDGNLEFLGR--ADDqVKIRGFRIELGEIE 889
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 497 RHLLAHPDITDVAVIGAPDPTWGQKVTAVVQLKKGKTLTLSQLQAWAREHMAPYTIPTGLILVEEMPRNQMGKVNKKDLL 576
Cdd:COG1020 890 AALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALP 969
|
....*..
gi 2073725801 577 RKFFPTR 583
Cdd:COG1020 970 APAAAAA 976
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
208-564 |
1.08e-41 |
|
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: 153.23 E-value: 1.08e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 208 PAMLIYTSGTTGRPKGVLHTHSSLqaMVQGLVSEW--AWNKDDVILHTLPLHHVhGIVNKLMCPLWVGATCIMLPEFSAQ 285
Cdd:cd17636 2 PVLAIYTAAFSGRPNGALLSHQAL--LAQALVLAVlqAIDEGTVFLNSGPLFHI-GTLMFTLATFHAGGTNVFVRRVDAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 286 KVWEqLISSkspmvnvfmavptiyskliEYYDQHFTQPQVQDFIRAVCKERiRLMVSGSAALPQPVlERWAEITGHVLLE 365
Cdd:cd17636 79 EVLE-LIEA-------------------ERCTHAFLLPPTIDQIVELNADG-LYDLSSLRSSPAAP-EWNDMATVDTSPW 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 366 R-----YGMTEI-GMALSNPLKGSRVPGAvGVPLPGVEVRIMMTnstnaiiaEGNSKGTrvkagleGKEGELLVRGSSVF 439
Cdd:cd17636 137 GrkpggYGQTEVmGLATFAALGGGAIGGA-GRPSPLVQVRILDE--------DGREVPD-------GEVGEIVARGPTVM 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 440 QKYWNKPQETADTFTeDGWFKTGDtaLYR---DGVYWIMGrTSVDIIKSGGYKISALDVERHLLAHPDITDVAVIGAPDP 516
Cdd:cd17636 201 AGYWNRPEVNARRTR-GGWHHTND--LGRrepDGSLSFVG-PKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDP 276
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 2073725801 517 TWGQKVTAVVQLKKGKTLTLSQLQAWAREHMAPYTIPTGLILVEEMPR 564
Cdd:cd17636 277 RWAQSVKAIVVLKPGASVTEAELIEHCRARIASYKKPKSVEFADALPR 324
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
57-575 |
1.10e-41 |
|
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: 157.05 E-value: 1.10e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 57 SRASVYGDNVAITDHSGSHTFCSLYKNSKSLAGLITkALTCQSGDLQGkcisfLCAND-ASYTVAQWAAWMCGGIAVPLY 135
Cdd:cd17646 6 EQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLR-ARGVGPEDRVA-----VLLPRsADLVVALLAVLKAGAAYLPLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 136 RKHPPGELEYVISDSQSSLLVAGQPFMDTLEPLAQKLGLPCLQLPTTSSLDTLQSEDirmlPEQnisdwaerPAMLIYTS 215
Cdd:cd17646 80 PGYPADRLAYMLADAGPAVVLTTADLAARLPAGGDVALLGDEALAAPPATPPLVPPR----PDN--------LAYVIYTS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 216 GTTGRPKGVLHTHSSLQAMVQGLVSEWAWNKDDVILHTLPLhhvhGI---VNKLMCPLWVGATCIML-------PEFSAQ 285
Cdd:cd17646 148 GSTGRPKGVMVTHAGIVNRLLWMQDEYPLGPGDRVLQKTPL----SFdvsVWELFWPLVAGARLVVArpgghrdPAYLAA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 286 KVWEQLISSK---SPMVNVFMAVPtiysklieyydqhftqpqvqdfiRAVCKERIRLMVSGSAALPQPVLERWAEITGHV 362
Cdd:cd17646 224 LIREHGVTTChfvPSMLRVFLAEP-----------------------AAGSCASLRRVFCSGEALPPELAARFLALPGAE 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 363 LLERYGMTE--IGM---ALSNPLKGSRVPgaVGVPLPGVEVRIMmtnstnaiiaegNSKGTRVKAGLEGkegELLVRGSS 437
Cdd:cd17646 281 LHNLYGPTEaaIDVthwPVRGPAETPSVP--IGRPVPNTRLYVL------------DDALRPVPVGVPG---ELYLGGVQ 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 438 VFQKYWNKPQETADTFTEDgWF-------KTGDTALYR-DGVYWIMGRTSvDIIKSGGYKISALDVERHLLAHPDITDVA 509
Cdd:cd17646 344 LARGYLGRPALTAERFVPD-PFgpgsrmyRTGDLARWRpDGALEFLGRSD-DQVKIRGFRVEPGEIEAALAAHPAVTHAV 421
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2073725801 510 VIGAPDPTWGQKVTAVVQLKKGKT-LTLSQLQAWAREHMAPYTIPTGLILVEEMPRNQMGKVNKKDL 575
Cdd:cd17646 422 VVARAAPAGAARLVGYVVPAAGAAgPDTAALRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
47-577 |
1.94e-41 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 157.23 E-value: 1.94e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 47 PGVGRVAPVF--SRASVYGDNVAITDHSGSHTFCSLYKNSKSLAGLITKAltcqsGDLQGKCISFLCANDASY-TVAQWA 123
Cdd:PRK06155 17 PPSERTLPAMlaRQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAA-----GVKRGDRVALMCGNRIEFlDVFLGC 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 124 AWMcGGIAVPLYRKHPPGELEYVISDSQSSLLVAGQPFMDTLEPL-AQKLGLPCLQL---------PTTSSLDTLQSEDI 193
Cdd:PRK06155 92 AWL-GAIAVPINTALRGPQLEHILRNSGARLLVVEAALLAALEAAdPGDLPLPAVWLldapasvsvPAGWSTAPLPPLDA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 194 RmLPEQNISDwaERPAMLIYTSGTTGRPKGVLHTHSSL------QAMVQGLVSewawnkDDVILHTLPLHHVHGIvNKLM 267
Cdd:PRK06155 171 P-APAAAVQP--GDTAAILYTSGTTGPSKGVCCPHAQFywwgrnSAEDLEIGA------DDVLYTTLPLFHTNAL-NAFF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 268 CPLWVGATCIMLPEFSAQKVWEQLISSKS-------PMVNVFMAVPtiysklieyydqhftqPQVQDFIRAVckeRIRLM 340
Cdd:PRK06155 241 QALLAGATYVLEPRFSASGFWPAVRRHGAtvtyllgAMVSILLSQP----------------ARESDRAHRV---RVALG 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 341 VSGSAALPQPVLERwaeiTGHVLLERYGMTEIGMALSNPLkGSRVPGAVGVPLPGVEVRIMmtnstnaiiaegNSKGTRV 420
Cdd:PRK06155 302 PGVPAALHAAFRER----FGVDLLDGYGSTETNFVIAVTH-GSQRPGSMGRLAPGFEARVV------------DEHDQEL 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 421 KAGlegKEGELLVRGSSVF---QKYWNKPQETADTFtEDGWFKTGD-TALYRDGVYWIMGRTSvDIIKSGGYKISALDVE 496
Cdd:PRK06155 365 PDG---EPGELLLRADEPFafaTGYFGMPEKTVEAW-RNLWFHTGDrVVRDADGWFRFVDRIK-DAIRRRGENISSFEVE 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 497 RHLLAHPDITDVAVIGAPDPTWGQKVTAVVQLKKGKTLTLSQLQAWAREHMAPYTIPTGLILVEEMPRNQMGKVnKKDLL 576
Cdd:PRK06155 440 QVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDGTALEPVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKV-QKFVL 518
|
.
gi 2073725801 577 R 577
Cdd:PRK06155 519 R 519
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
119-575 |
2.95e-41 |
|
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: 155.16 E-value: 2.95e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 119 VAQWAAWMCGGIAVPLYRKHPPGELEYVISDSQSSLLVaGQPfmdtleplaqklglpclqlpttssldtlqsedirmlpe 198
Cdd:cd17643 52 VALLAILKAGGAYVPIDPAYPVERIAFILADSGPSLLL-TDP-------------------------------------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 199 qnisdwaERPAMLIYTSGTTGRPKGVLHTHSSLQAMVQGLVSEWAWNKDDVilhTLPLHH---------VHGivnklmcP 269
Cdd:cd17643 93 -------DDLAYVIYTSGSTGRPKGVVVSHANVLALFAATQRWFGFNEDDV---WTLFHSyafdfsvweIWG-------A 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 270 LWVGATCIMLPEF---SAQKVWEQLISSKspmVNVFMAVPTIYSKLIEYYDQHFTQPqvqdfiravckERIRLMVSGSAA 346
Cdd:cd17643 156 LLHGGRLVVVPYEvarSPEDFARLLRDEG---VTVLNQTPSAFYQLVEAADRDGRDP-----------LALRYVIFGGEA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 347 LPQPVLERWAEITGHV---LLERYGMTEIGMALS-NPLKGSRVPGA----VGVPLPGVEVRIMMTNstnaiiaegnskGT 418
Cdd:cd17643 222 LEAAMLRPWAGRFGLDrpqLVNMYGITETTVHVTfRPLDAADLPAAaaspIGRPLPGLRVYVLDAD------------GR 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 419 RVKAGlegKEGELLVRGSSVFQKYWNKPQETADTFTEDGW-------FKTGDTALYR-DGVYWIMGRTSvDIIKSGGYKI 490
Cdd:cd17643 290 PVPPG---VVGELYVSGAGVARGYLGRPELTAERFVANPFggpgsrmYRTGDLARRLpDGELEYLGRAD-EQVKIRGFRI 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 491 SALDVERHLLAHPDITDVAVIGAPDPTWGQKVTAVVQLKKGKTLTLSQLQAWAREHMAPYTIPTGLILVEEMPRNQMGKV 570
Cdd:cd17643 366 ELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVADDGAAADIAELRALLKELLPDYMVPARYVPLDALPLTVNGKL 445
|
....*
gi 2073725801 571 NKKDL 575
Cdd:cd17643 446 DRAAL 450
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
206-572 |
3.70e-41 |
|
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.
Pssm-ID: 341290 [Multi-domain] Cd Length: 340 Bit Score: 152.03 E-value: 3.70e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 206 ERPAMLIYTSGTTGRPKGVLHTHSSLQAMVQGLVSE-WAWNKDDVILHTLPLHHVHGIVNKLMCpLWVGATCIMLPEFSA 284
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEgLNWVVGDVTYLPLPATHIGGLWWILTC-LIHGGLCVTGGENTT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 285 QK-VWEQLISSKspmVNVFMAVPTIYSKLIEYYdqhftqpqvQDFIRAVckERIRLMVSGSAaLPQPVLERWAEITGHV- 362
Cdd:cd17635 80 YKsLFKILTTNA---VTTTCLVPTLLSKLVSEL---------KSANATV--PSLRLIGYGGS-RAIAADVRFIEATGLTn 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 363 LLERYGMTEIGMALSNPL-KGSRVPGAVGVPLPGVEVRImmtnstnaiiaegnsKGTRVKAGLEGKEGELLVRGSSVFQK 441
Cdd:cd17635 145 TAQVYGLSETGTALCLPTdDDSIEINAVGRPYPGVDVYL---------------AATDGIAGPSASFGTIWIKSPANMLG 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 442 YWNKPQETADTFTeDGWFKTGDTALYR-DGVYWIMGRTSVDIIKsGGYKISALDVERHLLAHPDITDVAVIGAPDPTWGQ 520
Cdd:cd17635 210 YWNNPERTAEVLI-DGWVNTGDLGERReDGFLFITGRSSESINC-GGVKIAPDEVERIAEGVSGVQECACYEISDEEFGE 287
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 2073725801 521 KVTAVVQLKKGKTLT-LSQLQAWAREHMAPYTIPTGLILVEEMPRNQMGKVNK 572
Cdd:cd17635 288 LVGLAVVASAELDENaIRALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
62-575 |
3.93e-41 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 156.72 E-value: 3.93e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 62 YGDNVAITDHSGSHTFCSLYKNSKSLAGLItkaltcQSGDLQ-GKCISFLCANDASYTVAQWAAWMCGGIAV---PLYrk 137
Cdd:PRK07059 36 YADRPAFICMGKAITYGELDELSRALAAWL------QSRGLAkGARVAIMMPNVLQYPVAIAAVLRAGYVVVnvnPLY-- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 138 hPPGELEYVISDSQSSLLVAGQPFMDTLEPLAQK--------------LGL----------------PCLQLPTTSSLDT 187
Cdd:PRK07059 108 -TPRELEHQLKDSGAEAIVVLENFATTVQQVLAKtavkhvvvasmgdlLGFkghivnfvvrrvkkmvPAWSLPGHVRFND 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 188 LQSEDIRML---PEQNISDwaerPAMLIYTSGTTGRPKGVLHTHSSLQAMVqgLVSEwAW------NKDDV----ILHTL 254
Cdd:PRK07059 187 ALAEGARQTfkpVKLGPDD----VAFLQYTGGTTGVSKGATLLHRNIVANV--LQME-AWlqpafeKKPRPdqlnFVCAL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 255 PLHHVHGI-VNKLMcPLWVGATCIMLP----------EFSAQKVweqlisskspmvNVFMAVPTIYSKLIEYYDqhFTQp 323
Cdd:PRK07059 260 PLYHIFALtVCGLL-GMRTGGRNILIPnprdipgfikELKKYQV------------HIFPAVNTLYNALLNNPD--FDK- 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 324 qvQDFiravckERIRLMVSGSAALPQPVLERWAEITGHVLLERYGMTEIG-MALSNPLKGSRVPGAVGVPLPGVEVRImm 402
Cdd:PRK07059 324 --LDF------SKLIVANGGGMAVQRPVAERWLEMTGCPITEGYGLSETSpVATCNPVDATEFSGTIGLPLPSTEVSI-- 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 403 tnstnaiiaegnskgtRVKAGLE---GKEGELLVRGSSVFQKYWNKPQETADTFTEDGWFKTGDTALY-RDGVYWIMGRT 478
Cdd:PRK07059 394 ----------------RDDDGNDlplGEPGEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMdERGYTKIVDRK 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 479 SvDIIKSGGYKISALDVERHLLAHPDITDVAVIGAPDPTWGQKVTAVVqLKKGKTLTLSQLQAWAREHMAPYTIPTGLIL 558
Cdd:PRK07059 458 K-DMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGEAVKLFV-VKKDPALTEEDVKAFCKERLTNYKRPKFVEF 535
|
570
....*....|....*..
gi 2073725801 559 VEEMPRNQMGKVNKKDL 575
Cdd:PRK07059 536 RTELPKTNVGKILRREL 552
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
207-570 |
1.14e-40 |
|
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: 150.25 E-value: 1.14e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 207 RPAMLIYTSGTTGRPKGVLHTHSS-LQAMVQGlVSEWAWNKDDVILHTLPLHHVHGIvNKLMCPLWVGATCIMLPEFSAQ 285
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRSERSwIESFVCN-EDLFNISGEDAILAPGPLSHSLFL-YGAISALYLGGTFIGQRKFNPK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 286 KVWEQLissKSPMVNVFMAVPTIYSKLIEYYDQHFTqpqvqdfiravckerIRLMVSGSAALPQPVLERWAEITGH-VLL 364
Cdd:cd17633 79 SWIRKI---NQYNATVIYLVPTMLQALARTLEPESK---------------IKSIFSSGQKLFESTKKKLKNIFPKaNLI 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 365 ERYGMTEIGMALSNPLKGSRVPGAVGVPLPGVEVRImmTNSTNaiiaegnskgtrvkagleGKEGELLVRGSSVFQKYWn 444
Cdd:cd17633 141 EFYGTSELSFITYNFNQESRPPNSVGRPFPNVEIEI--RNADG------------------GEIGKIFVKSEMVFSGYV- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 445 kpqeTADTFTEDGWFKTGDTALY-RDGVYWIMGRTSvDIIKSGGYKISALDVERHLLAHPDITDVAVIGAPDPTWGQKVT 523
Cdd:cd17633 200 ----RGGFSNPDGWMSVGDIGYVdEEGYLYLVGRES-DMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAV 274
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 2073725801 524 AVVqlkKGKTLTLSQLQAWAREHMAPYTIPTGLILVEEMPRNQMGKV 570
Cdd:cd17633 275 ALY---SGDKLTYKQLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKI 318
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
76-577 |
3.83e-40 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 153.31 E-value: 3.83e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 76 TFCSLYKNSKSLAGLITKAltcqsGDLQGKCISFLCANDASYTVAQWAAWMCGGIAVPLYRKHPPGELEYVISDSQSSLL 155
Cdd:PRK13391 26 TYRELDERSNRLAHLFRSL-----GLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAAYIVDDSGARAL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 156 VAGQPFMDTLEPLAQKL--GLPCLQLPTTSSLDTLQ--SEDIRMLPEQNISDWAERPAMLiYTSGTTGRPKGVLH----- 226
Cdd:PRK13391 101 ITSAAKLDVARALLKQCpgVRHRLVLDGDGELEGFVgyAEAVAGLPATPIADESLGTDML-YSSGTTGRPKGIKRplpeq 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 227 ---THSSLQAMVQGLvseWAWNKDDVILHTLPLHHVH-----GIVNKLmcplwvGATCIMLPEFSAQKvWEQLISSKSpm 298
Cdd:PRK13391 180 ppdTPLPLTAFLQRL---WGFRSDMVYLSPAPLYHSApqravMLVIRL------GGTVIVMEHFDAEQ-YLALIEEYG-- 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 299 VNVFMAVPTIYSKLIEYYDQhftQPQVQDFiravckERIRLMVSGSAALPQPVLERWAEITGHVLLERYGMTE-IGMALS 377
Cdd:PRK13391 248 VTHTQLVPTMFSRMLKLPEE---VRDKYDL------SSLEVAIHAAAPCPPQVKEQMIDWWGPIIHEYYAATEgLGFTAC 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 378 NPLKGSRVPGAVGVPLPGVeVRIMmtnstnaiiaegNSKGTRVKAGlegKEGELLVRGSSVFQkYWNKPQETADTFTEDG 457
Cdd:PRK13391 319 DSEEWLAHPGTVGRAMFGD-LHIL------------DDDGAELPPG---EPGTIWFEGGRPFE-YLNDPAKTAEARHPDG 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 458 -WFKTGDTA-LYRDGVYWIMGRTSVDIIkSGGYKISALDVERHLLAHPDITDVAVIGAPDPTWGQKVTAVVQLKKG--KT 533
Cdd:PRK13391 382 tWSTVGDIGyVDEDGYLYLTDRAAFMII-SGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPVDGvdPG 460
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 2073725801 534 LTLSQ-LQAWAREHMAPYTIPTGLILVEEMPRNQMGKVNKKdLLR 577
Cdd:PRK13391 461 PALAAeLIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKR-LLR 504
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
211-571 |
4.68e-40 |
|
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: 149.84 E-value: 4.68e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 211 LIYTSGTTGRPKGVLHTHSSL--------------QAMVQGLVSEWAWNKDDVILHTLPLHHVHGIVNKLMCPLWVGATC 276
Cdd:cd05924 8 ILYTGGTTGMPKGVMWRQEDIfrmlmggadfgtgeFTPSEDAHKAAAAAAGTVMFPAPPLMHGTGSWTAFGGLLGGQTVV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 277 IMLPEFSAQKVWEQLISSKspmVNVFMAVPTIYSK-LIEYYDQHFTQPQvqdfiravckERIRLMVSGSAALPQPVLERW 355
Cdd:cd05924 88 LPDDRFDPEEVWRTIEKHK---VTSMTIVGDAMARpLIDALRDAGPYDL----------SSLFAISSGGALLSPEVKQGL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 356 AEITGH-VLLERYGMTEIGMalsnplKGSRVPGAvGVPLPGVEVRImmtNSTNAIIAEgnsKGTRVKAGlEGKEGELLVR 434
Cdd:cd05924 155 LELVPNiTLVDAFGSSETGF------TGSGHSAG-SGPETGPFTRA---NPDTVVLDD---DGRVVPPG-SGGVGWIARR 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 435 GSsVFQKYWNKPQETADTFTE-DG--WFKTGDTALYR-DGVYWIMGRTSVdIIKSGGYKISALDVERHLLAHPDITDVAV 510
Cdd:cd05924 221 GH-IPLGYYGDEAKTAETFPEvDGvrYAVPGDRATVEaDGTVTLLGRGSV-CINTGGEKVFPEEVEEALKSHPAVYDVLV 298
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2073725801 511 IGAPDPTWGQKVTAVVQLKKGKTLTLSQLQAWAREHMAPYTIPTGLILVEEMPRNQMGKVN 571
Cdd:cd05924 299 VGRPDERWGQEVVAVVQLREGAGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGKAD 359
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
55-575 |
1.05e-39 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 152.44 E-value: 1.05e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 55 VFSRASVYGDNVAITDHS--GSHTFCSLYKNSKSLAGLITKAltcqsGDLQGKCISFLCANDASYTVAQWAAWMCGGI-- 130
Cdd:PLN02246 29 CFERLSEFSDRPCLIDGAtgRVYTYADVELLSRRVAAGLHKL-----GIRQGDVVMLLLPNCPEFVLAFLGASRRGAVtt 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 131 -AVPLYrkhPPGELEYVISDSQSSLLVAGQPFMDTLEPLAQKLGLP----------CLqlpttsSLDTLQSEDIRMLPEQ 199
Cdd:PLN02246 104 tANPFY---TPAEIAKQAKASGAKLIITQSCYVDKLKGLAEDDGVTvvtiddppegCL------HFSELTQADENELPEV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 200 NISDwaERPAMLIYTSGTTGRPKGVLHTH----SSLQAMVQGLVSEWAWNKDDVILHTLPLHHVHGIVNKLMCPLWVGAT 275
Cdd:PLN02246 175 EISP--DDVVALPYSSGTTGLPKGVMLTHkglvTSVAQQVDGENPNLYFHSDDVILCVLPMFHIYSLNSVLLCGLRVGAA 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 276 CIMLPEFSAQKVWEQLISSKspmVNVFMAVPTIY-----SKLIEYYDQhftqpqvqdfiravckERIRLMVSGSAALPQP 350
Cdd:PLN02246 253 ILIMPKFEIGALLELIQRHK---VTIAPFVPPIVlaiakSPVVEKYDL----------------SSIRMVLSGAAPLGKE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 351 vLER--WAEITGHVLLERYGMTEIGMALSNPLKGSRVP-----GAVGVPLPGVEVRIMMTNStnaiiaeGNSKGtrvkag 423
Cdd:PLN02246 314 -LEDafRAKLPNAVLGQGYGMTEAGPVLAMCLAFAKEPfpvksGSCGTVVRNAELKIVDPET-------GASLP------ 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 424 lEGKEGELLVRGSSVFQKYWNKPQETADTFTEDGWFKTGDTALY-RDGVYWIMGRTSvDIIKSGGYKISALDVERHLLAH 502
Cdd:PLN02246 380 -RNQPGEICIRGPQIMKGYLNDPEATANTIDKDGWLHTGDIGYIdDDDELFIVDRLK-ELIKYKGFQVAPAELEALLISH 457
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2073725801 503 PDITDVAVIGAPDPTWGQKVTAVVQLKKGKTLTLSQLQAWAREHMAPYTIPTGLILVEEMPRNQMGKVNKKDL 575
Cdd:PLN02246 458 PSIADAAVVPMKDEVAGEVPVAFVVRSNGSEITEDEIKQFVAKQVVFYKRIHKVFFVDSIPKAPSGKILRKDL 530
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
116-572 |
2.23e-39 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 151.89 E-value: 2.23e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 116 SYTVAQWAAWM-----CGGIAV---PLYRKHppgELEYVISDSQSSLLVAGQPF-----MDTLEPLAQKLGlpclqlptT 182
Cdd:PRK08315 75 APNVPEWVLTQfatakIGAILVtinPAYRLS---ELEYALNQSGCKALIAADGFkdsdyVAMLYELAPELA--------T 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 183 SSLDTLQSED-------IRMLPE-----QNISDWAERPAML-----------------I---YTSGTTGRPKGVLHTHSS 230
Cdd:PRK08315 144 CEPGQLQSARlpelrrvIFLGDEkhpgmLNFDELLALGRAVddaelaarqatldpddpIniqYTSGTTGFPKGATLTHRN 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 231 LQ------AMVQGLVSEwawnkdDVILHTLPLHHVHGIVNKLMCPLWVGAT-CIMLPEFSAQKVWEQLISSKSPMVNvfm 303
Cdd:PRK08315 224 ILnngyfiGEAMKLTEE------DRLCIPVPLYHCFGMVLGNLACVTHGATmVYPGEGFDPLATLAAVEEERCTALY--- 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 304 AVPTIYsklIEYYDQhftqPQVQDF--------IRAvckerirlmvsGSAAlPQPVLER------WAEITghvllERYGM 369
Cdd:PRK08315 295 GVPTMF---IAELDH----PDFARFdlsslrtgIMA-----------GSPC-PIEVMKRvidkmhMSEVT-----IAYGM 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 370 TEI--GMALSN---PLKgSRVpGAVGVPLPGVEVRIMmTNSTNAIIAEGNSkgtrvkaglegkeGELLVRGSSVFQKYWN 444
Cdd:PRK08315 351 TETspVSTQTRtddPLE-KRV-TTVGRALPHLEVKIV-DPETGETVPRGEQ-------------GELCTRGYSVMKGYWN 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 445 KPQETADTFTEDGWFKTGDTALYR-DGVYWIMGRTSvDIIKSGGYKISALDVERHLLAHPDITDVAVIGAPDPTWGQKVT 523
Cdd:PRK08315 415 DPEKTAEAIDADGWMHTGDLAVMDeEGYVNIVGRIK-DMIIRGGENIYPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVC 493
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 2073725801 524 AVVQLKKGKTLTLSQLQAWAREHMAPYTIPTGLILVEEMPRNQMGKVNK 572
Cdd:PRK08315 494 AWIILRPGATLTEEDVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGKIQK 542
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
128-570 |
3.92e-39 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 151.20 E-value: 3.92e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 128 GGIAVPLYRKHPPGELEYVISDSQSSLLVagqpfmdTLEPLAQKLG---LPCLQ-----------LPTTSSLDTL---QS 190
Cdd:PRK04319 122 GAIVGPLFEAFMEEAVRDRLEDSEAKVLI-------TTPALLERKPaddLPSLKhvllvgedveeGPGTLDFNALmeqAS 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 191 EDIRMLPEQnisdwAERPAMLIYTSGTTGRPKGVLHTHsslQAMVQGLVS-EWAWN--KDDVILHTLPLHHVHGIVNKLM 267
Cdd:PRK04319 195 DEFDIEWTD-----REDGAILHYTSGSTGKPKGVLHVH---NAMLQHYQTgKYVLDlhEDDVYWCTADPGWVTGTSYGIF 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 268 CPLWVGATCIML-PEFSAQKvWEQLISSKSpmVNVFMAVPTIYSKLIEYYDQHFTQpqvQDFiravckERIRLMVS-GSA 345
Cdd:PRK04319 267 APWLNGATNVIDgGRFSPER-WYRILEDYK--VTVWYTAPTAIRMLMGAGDDLVKK---YDL------SSLRHILSvGEP 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 346 ALPQPVleRWA-EITGHVLLERYGMTEIGMAL-----SNPLKgsrvPGAVGVPLPGVEVrimmtnstnAIIAegnskgtR 419
Cdd:PRK04319 335 LNPEVV--RWGmKVFGLPIHDNWWMTETGGIMianypAMDIK----PGSMGKPLPGIEA---------AIVD-------D 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 420 VKAGLE-GKEGELLVRGS--SVFQKYWNKPQETADTFtEDGWFKTGDTAlYRD--GVYWIMGRTSvDIIKSGGYKISALD 494
Cdd:PRK04319 393 QGNELPpNRMGNLAIKKGwpSMMRGIWNNPEKYESYF-AGDWYVSGDSA-YMDedGYFWFQGRVD-DVIKTSGERVGPFE 469
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2073725801 495 VERHLLAHPDITDVAVIGAPDPTWGQKVTAVVQLKKGKTLT---LSQLQAWAREHMAPYTIPTGLILVEEMPRNQMGKV 570
Cdd:PRK04319 470 VESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVALRPGYEPSeelKEEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKI 548
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
64-575 |
2.76e-38 |
|
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: 147.49 E-value: 2.76e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 64 DNVAITDHSGSHTFCSLYKNSKSLAGLItKALTCQSGDLQGkcisfLCAN-DASYTVAQWAAWMCGGIAVPLYRKHPPGE 142
Cdd:cd17651 10 DAPALVAEGRRLTYAELDRRANRLAHRL-RARGVGPGDLVA-----LCARrSAELVVALLAILKAGAAYVPLDPAYPAER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 143 LEYVISDSQSSLLVAGQPFMDTLEPlAQKLGLPCLQLPTTSSLDTlqSEDIRMLPEqnisdwaeRPAMLIYTSGTTGRPK 222
Cdd:cd17651 84 LAFMLADAGPVLVLTHPALAGELAV-ELVAVTLLDQPGAAAGADA--EPDPALDAD--------DLAYVIYTSGSTGRPK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 223 GVLHTHSSLQAMVQGLVSEWAWNKDDVILHTLPLH---HVHGIVNKLMCplwvGATCIMLPE---FSAQKVWEQLisSKS 296
Cdd:cd17651 153 GVVMPHRSLANLVAWQARASSLGPGARTLQFAGLGfdvSVQEIFSTLCA----GATLVLPPEevrTDPPALAAWL--DEQ 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 297 PMVNVFMavPTIYSK-LIEYYDQHFTQPQvqdfiravckeRIR-LMVSGSAALPQPVLERW-AEITGHVLLERYGMTE-- 371
Cdd:cd17651 227 RISRVFL--PTVALRaLAEHGRPLGVRLA-----------ALRyLLTGGEQLVLTEDLREFcAGLPGLRLHNHYGPTEth 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 372 --IGMALSNPLKGSRVPGAVGVPLPGVEVRImmtnstnaiiaegnskgtrVKAGLE----GKEGELLVRGSSVFQKYWNK 445
Cdd:cd17651 294 vvTALSLPGDPAAWPAPPPIGRPIDNTRVYV-------------------LDAALRpvppGVPGELYIGGAGLARGYLNR 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 446 PQETADTFTEDGW------FKTGDTALY-RDGVYWIMGRTSvDIIKSGGYKISALDVERHLLAHPDITDVAVIGAPDPTW 518
Cdd:cd17651 355 PELTAERFVPDPFvpgarmYRTGDLARWlPDGELEFLGRAD-DQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPG 433
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 2073725801 519 GQKVTAVVQLKKGKTLTLSQLQAWAREHMAPYTIPTGLILVEEMPRNQMGKVNKKDL 575
Cdd:cd17651 434 EKRLVAYVVGDPEAPVDAAELRAALATHLPEYMVPSAFVLLDALPLTPNGKLDRRAL 490
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
205-575 |
4.74e-38 |
|
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: 146.71 E-value: 4.74e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 205 AERPAMLIYTSGTTGRPKGVLHTHSSLQAMVQGLVSEWAWNKDDVILHTLPLHHVHGIVNKLMCPLWVGATCIMLPE-FS 283
Cdd:cd05909 146 PDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPFFHSFGLTGCLWLPLLSGIKVVFHPNpLD 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 284 AQKVWEqLISSKSpmVNVFMAVPTIYSklieYYdqhftqpqvqdfIRAVCKE---RIRLMVSGSAALPQPVLERWAEITG 360
Cdd:cd05909 226 YKKIPE-LIYDKK--ATILLGTPTFLR----GY------------ARAAHPEdfsSLRLVVAGAEKLKDTLRQEFQEKFG 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 361 HVLLERYGMTEIGMALS-NPLKGSRVPGAVGVPLPGVEVRIMmtnstnaiiaegnSKGTRVKAGlEGKEGELLVRGSSVF 439
Cdd:cd05909 287 IRILEGYGTTECSPVISvNTPQSPNKEGTVGRPLPGMEVKIV-------------SVETHEEVP-IGEGGLLLVRGPNVM 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 440 QKYWNKPQETADTFtEDGWFKTGDTA-LYRDGVYWIMGRTSvDIIKSGGYKISALDVERHLLAH-PDITDVAVIGAPDPT 517
Cdd:cd05909 353 LGYLNEPELTSFAF-GDGWYDTGDIGkIDGEGFLTITGRLS-RFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVPDGR 430
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2073725801 518 WGQKVTAVVQlkkGKTLTLSQLQAWAREHMAP-YTIPTGLILVEEMPRNQMGKVNKKDL 575
Cdd:cd05909 431 KGEKIVLLTT---TTDTDPSSLNDILKNAGISnLAKPSYIHQVEEIPLLGTGKPDYVTL 486
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
48-575 |
1.01e-37 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 146.29 E-value: 1.01e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 48 GVGRVAPVFSRASVYGDNVAITDHSGSHTFCSLYKNSKSLAGLITKAltcqsGDLQGKCISFLCANDASYTVAQWAAWMC 127
Cdd:PRK13383 34 GTNPYTLLAVTAARWPGRTAIIDDDGALSYRELQRATESLARRLTRD-----GVAPGRAVGVMCRNGRGFVTAVFAVGLL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 128 GGIAVPLYRKHPPGELEYVISDSQSSLLVAGQPFMDTLEPLAQKLGLpclqlpttssLD--TLQSEDIRMLPEQnisdwA 205
Cdd:PRK13383 109 GADVVPISTEFRSDALAAALRAHHISTVVADNEFAERIAGADDAVAV----------IDpaTAGAEESGGRPAV-----A 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 206 ERPAMLIYTSGTTGRPKGVlhthsSLQAMVQGLVSEWAWNKDDVILHT-------LPLHHVHGIvNKLMCPLWVGATCIM 278
Cdd:PRK13383 174 APGRIVLLTSGTTGKPKGV-----PRAPQLRSAVGVWVTILDRTRLRTgsrisvaMPMFHGLGL-GMLMLTIALGGTVLT 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 279 LPEFSAQKVWEQLISSKSpmvNVFMAVPTIYSKLIEYYDQhftqpqvqdfIRAVCK-ERIRLMVSGSAALPQPVLERWAE 357
Cdd:PRK13383 248 HRHFDAEAALAQASLHRA---DAFTAVPVVLARILELPPR----------VRARNPlPQLRVVMSSGDRLDPTLGQRFMD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 358 ITGHVLLERYGMTEIGM-ALSNPLKGSRVPGAVGVPLPGVEVRIMMTNstnaiiaeGNSKGTRVKaglegkeGELLVRGS 436
Cdd:PRK13383 315 TYGDILYNGYGSTEVGIgALATPADLRDAPETVGKPVAGCPVRILDRN--------NRPVGPRVT-------GRIFVGGE 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 437 SVFQKYwnkpQETADTFTEDGWFKTGDTA-LYRDGVYWIMGRTSvDIIKSGGYKISALDVERHLLAHPDITDVAVIGAPD 515
Cdd:PRK13383 380 LAGTRY----TDGGGKAVVDGMTSTGDMGyLDNAGRLFIVGRED-DMIISGGENVYPRAVENALAAHPAVADNAVIGVPD 454
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 516 PTWGQKVTAVVQLKKGKTLTLSQLQAWAREHMAPYTIPTGLILVEEMPRNQMGKVNKKDL 575
Cdd:PRK13383 455 ERFGHRLAAFVVLHPGSGVDAAQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
64-578 |
1.05e-37 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 146.44 E-value: 1.05e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 64 DNVAITDHSGSHTFCSLYKNSKSLAglitKALTCQSGDlQGKCISFLCANDASYTVAQWAAWMCGGIAVPLYRKHPPGEL 143
Cdd:PRK13382 58 DRPGLIDELGTLTWRELDERSDALA----AALQALPIG-EPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPAL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 144 EYVISDSQSSLLVAGQPFMDTLE------PLAQKLglpclqLPTTSSLDTLQSEDIRMLPE-QNISDWAERPAMLIYTSG 216
Cdd:PRK13382 133 AEVVTREGVDTVIYDEEFSATVDraladcPQATRI------VAWTDEDHDLTVEVLIAAHAgQRPEPTGRKGRVILLTSG 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 217 TTGRPKGVLHTHSSLQAMVQGLVSEWAWNKDDVILHTLPLHHVHGIVNkLMCPLWVGATCIMLPEFSAQKVWeQLISSKS 296
Cdd:PRK13382 207 TTGTPKGARRSGPGGIGTLKAILDRTPWRAEEPTVIVAPMFHAWGFSQ-LVLAASLACTIVTRRRFDPEATL-DLIDRHR 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 297 PmvNVFMAVPTIYSKLIEYYDQHFTQPQVQD--FIRAvckerirlmvSGSAALPQpVLERWAEITGHVLLERYGMTEIGM 374
Cdd:PRK13382 285 A--TGLAVVPVMFDRIMDLPAEVRNRYSGRSlrFAAA----------SGSRMRPD-VVIAFMDQFGDVIYNNYNATEAGM 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 375 -ALSNPLKGSRVPGAVGVPLPGVEVRIMMtnstnaiiAEGNSKGTrvkagleGKEGELLVRGSSVFQKYwnKPQETADTf 453
Cdd:PRK13382 352 iATATPADLRAAPDTAGRPAEGTEIRILD--------QDFREVPT-------GEVGTIFVRNDTQFDGY--TSGSTKDF- 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 454 tEDGWFKTGDTALYRD-GVYWIMGRtSVDIIKSGGYKISALDVERHLLAHPDITDVAVIGAPDPTWGQKVTAVVQLKKGK 532
Cdd:PRK13382 414 -HDGFMASGDVGYLDEnGRLFVVGR-DDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPGA 491
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 2073725801 533 TLTLSQLQAWAREHMAPYTIPTGLILVEEMPRNQMGKVNKKDLLRK 578
Cdd:PRK13382 492 SATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQAR 537
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
76-512 |
1.37e-37 |
|
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: 145.19 E-value: 1.37e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 76 TFCSLYKNSKSLA-GLItkALTCQSGDLqgkcISFLCANDASYTVAQWAAWMCGGIAVPLYRKHPPGELEYVISDSQSSL 154
Cdd:cd17640 7 TYKDLYQEILDFAaGLR--SLGVKAGEK----VALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 155 LVagqpfmdtleplaqklglpclqlpttssLDTlQSEDIrmlpeqnisdwaerpAMLIYTSGTTGRPKGVLHTH------ 228
Cdd:cd17640 81 LV----------------------------VEN-DSDDL---------------ATIIYTSGTTGNPKGVMLTHanllhq 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 229 -SSLQAMVQGLVSewawnkdDVILHTLPLHHVHGIVNKLMCPLWvGATCImlpeFSAQKVWEQLISSKSPmvNVFMAVPT 307
Cdd:cd17640 117 iRSLSDIVPPQPG-------DRFLSILPIWHSYERSAEYFIFAC-GCSQA----YTSIRTLKDDLKRVKP--HYIVSVPR 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 308 IYSKLIE-YYDQHFTQPQVQDFI--RAVCKERIRLMVSGSAALPqPVLERWAEITGHVLLERYGMTEIGMALSNPLKGSR 384
Cdd:cd17640 183 LWESLYSgIQKQVSKSSPIKQFLflFFLSGGIFKFGISGGGALP-PHVDTFFEAIGIEVLNGYGLTETSPVVSARRLKCN 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 385 VPGAVGVPLPGVEVRIMMTNStnaiiaegnskgtrvKAGLE-GKEGELLVRGSSVFQKYWNKPQETADTFTEDGWFKTGD 463
Cdd:cd17640 262 VRGSVGRPLPGTEIKIVDPEG---------------NVVLPpGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGWFNTGD 326
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 2073725801 464 TA-LYRDGVYWIMGRTSVDIIKSGGYKISALDVERHLLAHPDITDVAVIG 512
Cdd:cd17640 327 LGwLTCGGELVLTGRAKDTIVLSNGENVEPQPIEEALMRSPFIEQIMVVG 376
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
57-575 |
2.48e-37 |
|
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341297 [Multi-domain] Cd Length: 532 Bit Score: 145.36 E-value: 2.48e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 57 SRASVYGDNVAITD-HSG-SHTFCSLYKNSKSLAGLITKAltcqsGDLQGKCISFLCANDASYTVAQWAAWMCGGIAVPL 134
Cdd:cd17642 25 KRYASVPGTIAFTDaHTGvNYSYAEYLEMSVRLAEALKKY-----GLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 135 YRKHPPGELEYVISDSQSSLLVAGQPFMDTLEPLAQKL----------------GLPCLQLPTTSSLDTLQSEDIRMLPE 198
Cdd:cd17642 100 NDIYNERELDHSLNISKPTIVFCSKKGLQKVLNVQKKLkiiktiiildskedykGYQCLYTFITQNLPPGFNEYDFKPPS 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 199 qniSDWAERPAMLIYTSGTTGRPKGVLHTHSSLQAMVQGLVSEWAWNK---DDVILHTLPLHHVHGIVNkLMCPLWVGAT 275
Cdd:cd17642 180 ---FDRDEQVALIMNSSGSTGLPKGVQLTHKNIVARFSHARDPIFGNQiipDTAILTVIPFHHGFGMFT-TLGYLICGFR 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 276 CIMLPEFSAQKVWEQLISSKSPMVnvfMAVPTIY-----SKLIEYYDQhftqpqvqdfiravckERIRLMVSGSAALPQP 350
Cdd:cd17642 256 VVLMYKFEEELFLRSLQDYKVQSA---LLVPTLFaffakSTLVDKYDL----------------SNLHEIASGGAPLSKE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 351 VLERWAEITGHVLLER-YGMTEIGMALSNPLKGSRVPGAVGVPLPGVEVRIMMTNStnaiiaeGNSKGTRvkaglegKEG 429
Cdd:cd17642 317 VGEAVAKRFKLPGIRQgYGLTETTSAILITPEGDDKPGAVGKVVPFFYAKVVDLDT-------GKTLGPN-------ERG 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 430 ELLVRGSSVFQKYWNKPQETADTFTEDGWFKTGDTALY-RDGVYWIMGRTSvDIIKSGGYKISALDVERHLLAHPDITDV 508
Cdd:cd17642 383 ELCVKGPMIMKGYVNNPEATKALIDKDGWLHSGDIAYYdEDGHFFIVDRLK-SLIKYKGYQVPPAELESILLQHPKIFDA 461
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2073725801 509 AVIGAPDPTWGQKVTAVVQLKKGKTLTLSQLQAWAREHMAPYT-IPTGLILVEEMPRNQMGKVNKKDL 575
Cdd:cd17642 462 GVAGIPDEDAGELPAAVVVLEAGKTMTEKEVMDYVASQVSTAKrLRGGVKFVDEVPKGLTGKIDRRKI 529
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
209-582 |
2.74e-37 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 145.66 E-value: 2.74e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 209 AMLIYTSGTTGRPKGVLHTHSS--LQAMVQGLVSEWAWNKDDVILHTLPLHHVHGIVNKLMCPLwVGATCIML-PEFSAQ 285
Cdd:PRK06018 180 AGMCYTSGTTGDPKGVLYSHRSnvLHALMANNGDALGTSAADTMLPVVPLFHANSWGIAFSAPS-MGTKLVMPgAKLDGA 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 286 KVWEQLISSKspmVNVFMAVPTIYSKLIEYYDQH-FTQPQvqdfiravckerIRLMVSGSAALPQPVLERWAEITGHVlL 364
Cdd:PRK06018 259 SVYELLDTEK---VTFTAGVPTVWLMLLQYMEKEgLKLPH------------LKMVVCGGSAMPRSMIKAFEDMGVEV-R 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 365 ERYGMTE---IGM--ALSNPLkgSRVPGAV--------GVPLPGVEVRIMmtnstnaiiaegNSKGTRVKAglEGKE-GE 430
Cdd:PRK06018 323 HAWGMTEmspLGTlaALKPPF--SKLPGDArldvlqkqGYPPFGVEMKIT------------DDAGKELPW--DGKTfGR 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 431 LLVRGSSVFQKYWNKPQETADtftEDGWFKTGDTA-LYRDGVYWIMGRtSVDIIKSGGYKISALDVERHLLAHPDITDVA 509
Cdd:PRK06018 387 LKVRGPAVAAAYYRVDGEILD---DDGFFDTGDVAtIDAYGYMRITDR-SKDVIKSGGEWISSIDLENLAVGHPKVAEAA 462
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2073725801 510 VIGAPDPTWGQKVTAVVQLKKGKTLTLSQLQAWAREHMAPYTIPTGLILVEEMPRNQMGKVNKKDLLRKF----FPT 582
Cdd:PRK06018 463 VIGVYHPKWDERPLLIVQLKPGETATREEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALREQFkdykLPT 539
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
59-570 |
2.77e-37 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 144.54 E-value: 2.77e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 59 ASVYGDNVAITDHSGSHTfcslYKNSKSLAGLITKALTCQSGdlQGKCISFLCANDASYTVAQWAAWMCGGIAVPLYRKH 138
Cdd:PRK07638 11 ASLQPNKIAIKENDRVLT----YKDWFESVCKVANWLNEKES--KNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKW 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 139 PPGELEYVISDSQSSLLVAGQPFMDTLeplaqklglPCLQLPTTSSLDTLQSEDIRMLPEQNISDWAERPAMLIYTSGTT 218
Cdd:PRK07638 85 KQDELKERLAISNADMIVTERYKLNDL---------PDEEGRVIEIDEWKRMIEKYLPTYAPIENVQNAPFYMGFTSGST 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 219 GRPKGVLHTHSSLQAMVQGLVSEWAWNKDDVILHTLPLHHVH---GIVNKLmcplWVGATCIMLPEFSAQKVWEQLissK 295
Cdd:PRK07638 156 GKPKAFLRAQQSWLHSFDCNVHDFHMKREDSVLIAGTLVHSLflyGAISTL----YVGQTVHLMRKFIPNQVLDKL---E 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 296 SPMVNVFMAVPTIYSKLIEyydqhftqpqvqdfIRAVCKERIRLMVSGsAALPQPVLERWAEITGHV-LLERYGMTEIG- 373
Cdd:PRK07638 229 TENISVMYTVPTMLESLYK--------------ENRVIENKMKIISSG-AKWEAEAKEKIKNIFPYAkLYEFYGASELSf 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 374 MALSNPLKGSRVPGAVGVPLPGVEVRIMmtnstnaiiaegNSKGTRVKAGLEGKegeLLVRGSSVFQKYWNKpQETADTF 453
Cdd:PRK07638 294 VTALVDEESERRPNSVGRPFHNVQVRIC------------NEAGEEVQKGEIGT---VYVKSPQFFMGYIIG-GVLAREL 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 454 TEDGWFKTGDTA-LYRDGVYWIMGRTSvDIIKSGGYKISALDVERHLLAHPDITDVAVIGAPDPTWGQKVTAVVqlkKGK 532
Cdd:PRK07638 358 NADGWMTVRDVGyEDEEGFIYIVGREK-NMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAII---KGS 433
|
490 500 510
....*....|....*....|....*....|....*...
gi 2073725801 533 TlTLSQLQAWAREHMAPYTIPTGLILVEEMPRNQMGKV 570
Cdd:PRK07638 434 A-TKQQLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKI 470
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
196-577 |
3.55e-37 |
|
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: 144.06 E-value: 3.55e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 196 LPEQNISDWAERPAMLiYTSGTTGRPKGVLHTHSSLQAMVQGLVSeWA----WNKDDVILHTLPLHHVHGIVnKLMCPLW 271
Cdd:cd05929 116 SPETPIEDEAAGWKML-YSGGTTGRPKGIKRGLPGGPPDNDTLMA-AAlgfgPGADSVYLSPAPLYHAAPFR-WSMTALF 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 272 VGATCIMLPEFSAQKVWeQLIssKSPMVNVFMAVPTIYSKLIEYYDQhftQPQVQDF--IRAVCKerirlmvsgsAALPQ 349
Cdd:cd05929 193 MGGTLVLMEKFDPEEFL-RLI--ERYRVTFAQFVPTMFVRLLKLPEA---VRNAYDLssLKRVIH----------AAAPC 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 350 PVL--ERWAEITGHVLLERYGMTE-IGMALSNPLKGSRVPGAVGVPLPGvEVRIMMTNstnaiiaeGNSKGTrvkagleG 426
Cdd:cd05929 257 PPWvkEQWIDWGGPIIWEYYGGTEgQGLTIINGEEWLTHPGSVGRAVLG-KVHILDED--------GNEVPP-------G 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 427 KEGELLVRGSSVFQkYWNKPQETADTFTEDGWFKTGDTA-LYRDGVYWIMGRTSvDIIKSGGYKISALDVERHLLAHPDI 505
Cdd:cd05929 321 EIGEVYFANGPGFE-YTNDPEKTAAARNEGGWSTLGDVGyLDEDGYLYLTDRRS-DMIISGGVNIYPQEIENALIAHPKV 398
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2073725801 506 TDVAVIGAPDPTWGQKVTAVVQLKKG---KTLTLSQLQAWAREHMAPYTIPTGLILVEEMPRNQMGKVNKKdLLR 577
Cdd:cd05929 399 LDAAVVGVPDEELGQRVHAVVQPAPGadaGTALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRR-LLR 472
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
209-579 |
4.37e-37 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 141.34 E-value: 4.37e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 209 AMLIYTSGTTGRPKGVLHTHSSL----QAMVQGLVSEWAWnkddviLHTLPLHHVHGIvNKLMCPLWVGATCIMLpEFSA 284
Cdd:PRK07824 38 ALVVATSGTTGTPKGAMLTAAALtasaDATHDRLGGPGQW------LLALPAHHIAGL-QVLVRSVIAGSEPVEL-DVSA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 285 QKVWEQLISSKSPMvnvfmAVPTIYSKLIEyydqhfTQ-PQVQDFIRAVckERIRLM---VSGSAALPQPVLERWAEItG 360
Cdd:PRK07824 110 GFDPTALPRAVAEL-----GGGRRYTSLVP------MQlAKALDDPAAT--AALAELdavLVGGGPAPAPVLDAAAAA-G 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 361 HVLLERYGMTEIGmalsnplkgsrvPGAV--GVPLPGVEVRImmtnstnaiiaegnskgtrvkaglegKEGELLVRGSSV 438
Cdd:PRK07824 176 INVVRTYGMSETS------------GGCVydGVPLDGVRVRV--------------------------EDGRIALGGPTL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 439 FQKYWNKPQEtaDTFTEDGWFKTGDTALYRDGVYWIMGRTSvDIIKSGGYKISALDVERHLLAHPDITDVAVIGAPDPTW 518
Cdd:PRK07824 218 AKGYRNPVDP--DPFAEPGWFRTDDLGALDDGVLTVLGRAD-DAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRL 294
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2073725801 519 GQKVTAVVQLKKGKTLTLSQLQAWAREHMAPYTIPTGLILVEEMPRNQMGKVNKKDLLRKF 579
Cdd:PRK07824 295 GQRVVAAVVGDGGPAPTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALVRRF 355
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
119-575 |
1.49e-36 |
|
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: 142.34 E-value: 1.49e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 119 VAQWAAWMCGGIAVPLYRKHPPGELEYVISDSQSSLLVagqpfmdTLEPLAQKLGLPCLqlpttsSLDTLQSEDIRMLPE 198
Cdd:cd12117 62 VALLAVLKAGAAYVPLDPELPAERLAFMLADAGAKVLL-------TDRSLAGRAGGLEV------AVVIDEALDAGPAGN 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 199 QNISDWAERPAMLIYTSGTTGRPKGVLHTHSSlqamVQGLVSEWAW---NKDDVILHTLPL------HHVHGivnklmcP 269
Cdd:cd12117 129 PAVPVSPDDLAYVMYTSGSTGRPKGVAVTHRG----VVRLVKNTNYvtlGPDDRVLQTSPLafdastFEIWG-------A 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 270 LWVGATCIMLPE---FSAQKVWEQLISSKspmVNVFMAVPTIYSKLIEyydqhfTQPQVQDFIRavckeriRLMVSGSAA 346
Cdd:cd12117 198 LLNGARLVLAPKgtlLDPDALGALIAEEG---VTVLWLTAALFNQLAD------EDPECFAGLR-------ELLTGGEVV 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 347 LPQPV---LERWAEITghvLLERYGMTE-IGMALSNPL-KGSRVPGAV--GVPLPGVEVRIMmtnstnaiiaegNSKGTR 419
Cdd:cd12117 262 SPPHVrrvLAACPGLR---LVNGYGPTEnTTFTTSHVVtELDEVAGSIpiGRPIANTRVYVL------------DEDGRP 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 420 VKAGLEGkegELLVRGSSVFQKYWNKPQETADTFTEDGW------FKTGDTALYR-DGVYWIMGRTSvDIIKSGGYKISA 492
Cdd:cd12117 327 VPPGVPG---ELYVGGDGLALGYLNRPALTAERFVADPFgpgerlYRTGDLARWLpDGRLEFLGRID-DQVKIRGFRIEL 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 493 LDVERHLLAHPDITDVAVI-GAPDPTWGQKVTAVVqlkKGKTLTLSQLQAWAREHMAPYTIPTGLILVEEMPRNQMGKVN 571
Cdd:cd12117 403 GEIEAALRAHPGVREAVVVvREDAGGDKRLVAYVV---AEGALDAAELRAFLRERLPAYMVPAAFVVLDELPLTANGKVD 479
|
....
gi 2073725801 572 KKDL 575
Cdd:cd12117 480 RRAL 483
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
104-578 |
3.38e-36 |
|
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: 140.73 E-value: 3.38e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 104 GKCISFLCANDASYTVAQWAAWMCGGIAVPLYRKHPPGELEYVISDSQSSLLVAGqpfmdtlepLAQKlglpclqlpttS 183
Cdd:cd05973 25 GDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTD---------AANR-----------H 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 184 SLDtlqsedirmlpeqnisdwaERPAMLIYTSGTTGRPKGVLHTHSSLQAMVQGLVSEWAWNKDDVILHTLPLHHVHGIV 263
Cdd:cd05973 85 KLD-------------------SDPFVMMFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRPEDSFWNAADPGWAYGLY 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 264 NKLMCPLWVGATCIMLP-EFSAQKVWEQLISSKspmVNVFMAVPTIYSKLIeyydqhftqpqvQDFIRAVCKERIRLMVS 342
Cdd:cd05973 146 YAITGPLALGHPTILLEgGFSVESTWRVIERLG---VTNLAGSPTAYRLLM------------AAGAEVPARPKGRLRRV 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 343 GSAALP-QPVLERWAEIT-GHVLLERYGMTEIGMALSN------PLKGsrvpGAVGVPLPGVEVRIMMTNSTNAIiaegn 414
Cdd:cd05973 211 SSAGEPlTPEVIRWFDAAlGVPIHDHYGQTELGMVLANhhalehPVHA----GSAGRAMPGWRVAVLDDDGDELG----- 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 415 skgtrvkaglEGKEGELL--VRGSSV--FQKYWNKPQETADtfteDGWFKTGDTA-LYRDGVYWIMGRTSvDIIKSGGYK 489
Cdd:cd05973 282 ----------PGEPGRLAidIANSPLmwFRGYQLPDTPAID----GGYYLTGDTVeFDPDGSFSFIGRAD-DVITMSGYR 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 490 ISALDVERHLLAHPDITDVAVIGAPDPTWGQKVTAVVQLKKGKTLT---LSQLQAWAREHMAPYTIPTGLILVEEMPRNQ 566
Cdd:cd05973 347 IGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHEGTpalADELQLHVKKRLSAHAYPRTIHFVDELPKTP 426
|
490
....*....|..
gi 2073725801 567 MGKVnKKDLLRK 578
Cdd:cd05973 427 SGKI-QRFLLRR 437
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
119-575 |
6.97e-36 |
|
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: 139.70 E-value: 6.97e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 119 VAQWAAWMCGGIAVPLYRKHPPGELEYVISDSQSSLLVagqpfmdtleplaqklglpclqlpTTssldtlqsedirmlpe 198
Cdd:cd17652 52 VAILAVLKAGAAYLPLDPAYPAERIAYMLADARPALLL------------------------TT---------------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 199 qnisdwAERPAMLIYTSGTTGRPKGVLHTHSSLQAMVQGLVSEWAWNKDDVILHTLPLHhVHGIVNKLMCPLWVGATCIM 278
Cdd:cd17652 92 ------PDNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQIAAFDVGPGSRVLQFASPS-FDASVWELLMALLAGATLVL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 279 LPEfsaqkvwEQLISSKsPMVNVfmavptiyskLIEYYDQHFTQ-PQVQDFIRAVCKERIRLMVSGSAALPQPVLERWAe 357
Cdd:cd17652 165 APA-------EELLPGE-PLADL----------LREHRITHVTLpPAALAALPPDDLPDLRTLVVAGEACPAELVDRWA- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 358 iTGHVLLERYGMTE--IGMALSNPLKGSRVPgAVGVPLPGVEVRIMmtnstnaiiaegnskgtrvKAGLE----GKEGEL 431
Cdd:cd17652 226 -PGRRMINAYGPTEttVCATMAGPLPGGGVP-PIGRPVPGTRVYVL-------------------DARLRpvppGVPGEL 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 432 LVRGSSVFQKYWNKPQETADTFTEDGW-------FKTGDTALYR-DGVYWIMGRTSvDIIKSGGYKISALDVERHLLAHP 503
Cdd:cd17652 285 YIAGAGLARGYLNRPGLTAERFVADPFgapgsrmYRTGDLARWRaDGQLEFLGRAD-DQVKIRGFRIELGEVEAALTEHP 363
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2073725801 504 DITDVAVIGAPDPTWGQKVTAVVQLKKGKTLTLSQLQAWAREHMAPYTIPTGLILVEEMPRNQMGKVNKKDL 575
Cdd:cd17652 364 GVAEAVVVVRDDRPGDKRLVAYVVPAPGAAPTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
201-579 |
1.71e-35 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 140.69 E-value: 1.71e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 201 ISDWAE----RPAMLIYTSGTTGRPKGVLHTHSS--LQAMVQGLVSEWAWNKDDVILHTLPLHHV--HGIvnklmcPL-- 270
Cdd:PRK05620 172 VYDWPEldetTAAAICYSTGTTGAPKGVVYSHRSlyLQSLSLRTTDSLAVTHGESFLCCVPIYHVlsWGV------PLaa 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 271 WVGATCIMLP--EFSAQKVwEQLISSKSPmvNVFMAVPTIYSKLIEYYDQHftQPQvqdfiravcKERIRLMVSGSAALP 348
Cdd:PRK05620 246 FMSGTPLVFPgpDLSAPTL-AKIIATAMP--RVAHGVPTLWIQLMVHYLKN--PPE---------RMSLQEIYVGGSAVP 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 349 QPVLERWAEITGHVLLERYGMTEIGMAlsnplkgsrvpGAVGVPLPGV--EVRIMMTNSTNA--------IIAEGnskgt 418
Cdd:PRK05620 312 PILIKAWEERYGVDVVHVWGMTETSPV-----------GTVARPPSGVsgEARWAYRVSQGRfpasleyrIVNDG----- 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 419 RVKAGLEGKEGELLVRGSSVFQKYWNKPQET----------------ADTFTEDGWFKTGDTA-LYRDGVYWIMGRTSvD 481
Cdd:PRK05620 376 QVMESTDRNEGEIQVRGNWVTASYYHSPTEEgggaastfrgedvedaNDRFTADGWLRTGDVGsVTRDGFLTIHDRAR-D 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 482 IIKSGGYKISALDVERHLLAHPDITDVAVIGAPDPTWGQKVTAVVQLKKG---KTLTLSQLQAWAREHMAPYTIPTGLIL 558
Cdd:PRK05620 455 VIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLAVTVLAPGiepTRETAERLRDQLRDRLPNWMLPEYWTF 534
|
410 420
....*....|....*....|.
gi 2073725801 559 VEEMPRNQMGKVNKKDLLRKF 579
Cdd:PRK05620 535 VDEIDKTSVGKFDKKDLRQHL 555
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
115-577 |
4.31e-35 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 142.02 E-value: 4.31e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 115 ASYTVAQWAAWMCGGIAVPLYRKHPPGELEYVISDSQSSLLVAGQPFMDTLePLAQklGLPCLQLPTTSSLDTLQSEDir 194
Cdd:PRK12316 2064 FELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQRHLLERL-PLPA--GVARLPLDRDAEWADYPDTA-- 2138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 195 mlPEQNISdwAERPAMLIYTSGTTGRPKGVLHTHSSLQAMVQGLVSEWAWNKDDVILHTLPLhHVHGIVNKLMCPLWVGA 274
Cdd:PRK12316 2139 --PAVQLA--GENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPADCELQFMSF-SFDGAHEQWFHPLLNGA 2213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 275 TCIM------LPEFSAQKVWEQlisskspMVNVFMAVPTIYSKLIEYYDqhftqpqvqdfiRAVCKERIRLMVSGSAALP 348
Cdd:PRK12316 2214 RVLIrddelwDPEQLYDEMERH-------GVTILDFPPVYLQQLAEHAE------------RDGRPPAVRVYCFGGEAVP 2274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 349 QPVLERWAEITGHV-LLERYGMTEigmALSNPL---KGSRVP-GAVGVPLpgvevrimmtnsTNAIiaeGNSKGTRVKAG 423
Cdd:PRK12316 2275 AASLRLAWEALRPVyLFNGYGPTE---AVVTPLlwkCRPQDPcGAAYVPI------------GRAL---GNRRAYILDAD 2336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 424 LE----GKEGELLVRGSSVFQKYWNKPQETADTFTEDGW-------FKTGDTALYR-DGVYWIMGRtsVD-IIKSGGYKI 490
Cdd:PRK12316 2337 LNllapGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFsasgerlYRTGDLARYRaDGVVEYLGR--IDhQVKIRGFRI 2414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 491 SALDVERHLLAHPDITDVAVIgAPDPTWGQKVTAVVQLKKGKTLTLSQLQAWAREHMAPYTIPTGLILVEEMPRNQMGKV 570
Cdd:PRK12316 2415 ELGEIEARLQAHPAVREAVVV-AQDGASGKQLVAYVVPDDAAEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKL 2493
|
....*..
gi 2073725801 571 NKKDLLR 577
Cdd:PRK12316 2494 DRKALPK 2500
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
42-579 |
4.53e-35 |
|
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: 138.95 E-value: 4.53e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 42 YLKISPGVGRVAP-VFSRASVYGDNVAIT--DHSGSHTFCSlYKNSKSLAGLITKALTcQSGDLQGKCISFLCANDASYT 118
Cdd:cd05906 1 PLHRPEGAPRTLLeLLLRAAERGPTKGITyiDADGSEEFQS-YQDLLEDARRLAAGLR-QLGLRPGDSVILQFDDNEDFI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 119 VAQWAAWMCGGIAVPL-----YRKHPPGE--LEYVISDSQSSLLVAGQPFMDTLEPLAQKLGLPCLQLPTTSSLdtLQSE 191
Cdd:cd05906 79 PAFWACVLAGFVPAPLtvpptYDEPNARLrkLRHIWQLLGSPVVLTDAELVAEFAGLETLSGLPGIRVLSIEEL--LDTA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 192 DIRMLPEQNisdwAERPAMLIYTSGTTGRPKGVLHTHSSLQAMVQGLVSEWAWNKDDVILHTLPLHHVHGIVnklMC--- 268
Cdd:cd05906 157 ADHDLPQSR----PDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVPLDHVGGLV---ELhlr 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 269 PLWVGATCIMLP--EFSAQK-VWEQLISSKSpmVNVFMAVPTIYSKLIEYYDQhfTQPQVQDFiravckERIRLMVSGSA 345
Cdd:cd05906 230 AVYLGCQQVHVPteEILADPlRWLDLIDRYR--VTITWAPNFAFALLNDLLEE--IEDGTWDL------SSLRYLVNAGE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 346 ALPQPVLERWAEitghvLLERY-----------GMTEI--GMALSNPLKGSRVPGA-----VGVPLPGVEVRIMMtnstn 407
Cdd:cd05906 300 AVVAKTIRRLLR-----LLEPYglppdairpafGMTETcsGVIYSRSFPTYDHSQAlefvsLGRPIPGVSMRIVD----- 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 408 aiiAEGNSKgtrvkagLEGKEGELLVRGSSVFQKYWNKPQETADTFTEDGWFKTGDTALYRDGVYWIMGRTSvDIIKSGG 487
Cdd:cd05906 370 ---DEGQLL-------PEGEVGRLQVRGPVVTKGYYNNPEANAEAFTEDGWFRTGDLGFLDNGNLTITGRTK-DTIIVNG 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 488 YKISALDVERHLLAHPDITD--VAVIGAPDPTWGQKVTAVV-----QLKKGKTLTLSQLQAWAREHM---APYTIPTGLi 557
Cdd:cd05906 439 VNYYSHEIEAAVEEVPGVEPsfTAAFAVRDPGAETEELAIFfvpeyDLQDALSETLRAIRSVVSREVgvsPAYLIPLPK- 517
|
570 580
....*....|....*....|..
gi 2073725801 558 lvEEMPRNQMGKVNKKDLLRKF 579
Cdd:cd05906 518 --EEIPKTSLGKIQRSKLKAAF 537
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
128-575 |
7.69e-35 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 138.60 E-value: 7.69e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 128 GGIAVPLYRKHPPGELEYV--ISDSqSSLLVAGQPFMDTLEPLAQKLGLPCLQLPTTSSLDTLQSEDIRMLPEQNISDWA 205
Cdd:PRK05857 90 GAIAVMADGNLPIAAIERFcqITDP-AAALVAPGSKMASSAVPEALHSIPVIAVDIAAVTRESEHSLDAASLAGNADQGS 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 206 ERPAMLIYTSGTTGRPKGVLHTHSSLQAMVQGLVSE---WA-WNKDDVILHTLPLHHVHGIVNKLMCpLWVGATCIMLPE 281
Cdd:PRK05857 169 EDPLAMIFTSGTTGEPKAVLLANRTFFAVPDILQKEglnWVtWVVGETTYSPLPATHIGGLWWILTC-LMHGGLCVTGGE 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 282 FSAQkVWEQLISSKspmVNVFMAVPTIYSKLIeyYDQHFTqpqvqdfirAVCKERIRLMV-SGSAALPQPVleRWAEITG 360
Cdd:PRK05857 248 NTTS-LLEILTTNA---VATTCLVPTLLSKLV--SELKSA---------NATVPSLRLVGyGGSRAIAADV--RFIEATG 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 361 HVLLERYGMTEIG-MALSNPLKGSRVP----GAVGVPLPGVEVRIMmtnstnaiiAEGNSKGTRVKAGLEGKEGELLVRG 435
Cdd:PRK05857 311 VRTAQVYGLSETGcTALCLPTDDGSIVkieaGAVGRPYPGVDVYLA---------ATDGIGPTAPGAGPSASFGTLWIKS 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 436 SSVFQKYWNKPQETADTFTeDGWFKTGDTALYR-DGVYWIMGRTSvDIIKSGGYKISALDVERHLLAHPDITDVAVIGAP 514
Cdd:PRK05857 382 PANMLGYWNNPERTAEVLI-DGWVNTGDLLERReDGFFYIKGRSS-EMIICGGVNIAPDEVDRIAEGVSGVREAACYEIP 459
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2073725801 515 DPTWGQ----KVTAVVQLKKGKTLTLSQ-LQAWAREHMAPYTIPTGLILVEEMPRNQMGKVNKKDL 575
Cdd:PRK05857 460 DEEFGAlvglAVVASAELDESAARALKHtIAARFRRESEPMARPSTIVIVTDIPRTQSGKVMRASL 525
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
92-577 |
8.48e-35 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 138.34 E-value: 8.48e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 92 TKALTCQSGDLQGKCISFLCANDASYTVAQWAAWMCGGIAVPL---YRKHppgELEYVISDSQSSLLVA-----GQPFMD 163
Cdd:PRK06164 48 LAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVntrYRSH---EVAHILGRGRARWLVVwpgfkGIDFAA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 164 TLEPLAQKLgLPCLQ-----------LPTTSSLDTLQSEDIRMLPEQNIS----DWAERPAMLIYTSGTTGRPKGVLHTH 228
Cdd:PRK06164 125 ILAAVPPDA-LPPLRaiavvddaadaTPAPAPGARVQLFALPDPAPPAAAgeraADPDAGALLFTTSGTTSGPKLVLHRQ 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 229 SSLQAMVQGLVSEWAWNKDDVILHTLPLHHVHGIvNKLMCPLWVGATCIMLPEFSAQKVWEQLISSKspMVNVFMAVpti 308
Cdd:PRK06164 204 ATLLRHARAIARAYGYDPGAVLLAALPFCGVFGF-STLLGALAGGAPLVCEPVFDAARTARALRRHR--VTHTFGND--- 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 309 yskliEYYDQ-HFTQPQVQDFIRAvckeriRLM-----VSGSAALPQpvlerWAEITGHVLLERYGMTEI-----GMALS 377
Cdd:PRK06164 278 -----EMLRRiLDTAGERADFPSA------RLFgfasfAPALGELAA-----LARARGVPLTGLYGSSEVqalvaLQPAT 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 378 NPLKGSRVPGavGVPL-PGVEVRIMMTnSTNAIIAEGNSkgtrvkaglegkeGELLVRGSSVFQKYWNKPQETADTFTED 456
Cdd:PRK06164 342 DPVSVRIEGG--GRPAsPEARVRARDP-QDGALLPDGES-------------GEIEIRAPSLMRGYLDNPDATARALTDD 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 457 GWFKTGDTALYR-DGVYWIMGRTSvDIIKSGGYKISALDVERHLLAHPDITDVAVIGApdpTWGQKVTAV--VQLKKGKT 533
Cdd:PRK06164 406 GYFRTGDLGYTRgDGQFVYQTRMG-DSLRLGGFLVNPAEIEHALEALPGVAAAQVVGA---TRDGKTVPVafVIPTDGAS 481
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 2073725801 534 LTLSQLQAWAREHMAPYTIPTGLILVEEMPRNQMGKVNK--KDLLR 577
Cdd:PRK06164 482 PDEAGLMAACREALAGFKVPARVQVVEAFPVTESANGAKiqKHRLR 527
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
148-575 |
9.96e-35 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 137.89 E-value: 9.96e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 148 SDSQssLLVAGQPFMDTLEPLAQklGLPCLQLPT---TSSLDTLQSEDIRMlpeqnISDWAERPAMLIYTSGTTGRPKGV 224
Cdd:PRK07867 100 ADCQ--LVLTESAHAELLDGLDP--GVRVINVDSpawADELAAHRDAEPPF-----RVADPDDLFMLIFTSGTSGDPKAV 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 225 LHTHSSLQAMVQGLVSEWAWNKDDVILHTLPLHHVHGIVNKLMCPLWVGATCIMLPEFSAqkvweqliSSKSPMVNVFMA 304
Cdd:PRK07867 171 RCTHRKVASAGVMLAQRFGLGPDDVCYVSMPLFHSNAVMAGWAVALAAGASIALRRKFSA--------SGFLPDVRRYGA 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 305 VPTIY-SKLIEYYdqhFTQPQVQDfiravckER---IRLMVSGSAALPQpvLERWAEITGHVLLERYGMTEIGMALSnPL 380
Cdd:PRK07867 243 TYANYvGKPLSYV---LATPERPD-------DAdnpLRIVYGNEGAPGD--IARFARRFGCVVVDGFGSTEGGVAIT-RT 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 381 KGSRvPGAVGVPLPGVEVRIMMTNSTNAIiAEGNSKGTrvkagLEGKE--GELL-VRGSSVFQKYWNKPQETADTFtEDG 457
Cdd:PRK07867 310 PDTP-PGALGPLPPGVAIVDPDTGTECPP-AEDADGRL-----LNADEaiGELVnTAGPGGFEGYYNDPEADAERM-RGG 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 458 WFKTGDTAlYRD--GVYWIMGRTSvDIIKSGGYKISALDVERHLLAHPDITDVAVIGAPDPTWGQKVTAVVQLKKGKTLT 535
Cdd:PRK07867 382 VYWSGDLA-YRDadGYAYFAGRLG-DWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVMAALVLAPGAKFD 459
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 2073725801 536 LSQLQAW--AREHMAPYTIPTGLILVEEMPRNQMGKVNKKDL 575
Cdd:PRK07867 460 PDAFAEFlaAQPDLGPKQWPSYVRVCAELPRTATFKVLKRQL 501
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
64-575 |
1.00e-34 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.
Pssm-ID: 341279 [Multi-domain] Cd Length: 477 Bit Score: 137.02 E-value: 1.00e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 64 DNVAITDHSGSHTFCSLYKNSKSLAGLItKALTCQSGDLQGKCISflcaNDASYTVAQWAAWMCGGIAVPLYRKHPPGEL 143
Cdd:cd12114 2 DATAVICGDGTLTYGELAERARRVAGAL-KAAGVRPGDLVAVTLP----KGPEQVVAVLGILAAGAAYVPVDIDQPAARR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 144 EYVISDSQSSLLVagqpfmdTLEPLAQKLGLPclQLPTTSSLDTLQSEDIRMLPEQNISDwaerPAMLIYTSGTTGRPKG 223
Cdd:cd12114 77 EAILADAGARLVL-------TDGPDAQLDVAV--FDVLILDLDALAAPAPPPPVDVAPDD----LAYVIFTSGSTGTPKG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 224 VLHTHSSLQAMVQGLVSEWAWNKDDVILHTLPLHH---VHGIVNklmcPLWVGATCIMLPEFSAQKV--WEQLISSKSpm 298
Cdd:cd12114 144 VMISHRAALNTILDINRRFAVGPDDRVLALSSLSFdlsVYDIFG----ALSAGATLVLPDEARRRDPahWAELIERHG-- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 299 VNVFMAVPTIYSKLIEYYDQhftQPQVQDFIRAVckerirlMVSG---SAALPQPVLERWAEITGHVLlerYGMTEiGMA 375
Cdd:cd12114 218 VTLWNSVPALLEMLLDVLEA---AQALLPSLRLV-------LLSGdwiPLDLPARLRALAPDARLISL---GGATE-ASI 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 376 LSNPLKGSRVPGAV-----GVPLPGVEVRIMmtnstnaiiaegNSKGTRVKaglEGKEGELLVRGSSVFQKYWNKPQETA 450
Cdd:cd12114 284 WSIYHPIDEVPPDWrsipyGRPLANQRYRVL------------DPRGRDCP---DWVPGELWIGGRGVALGYLGDPELTA 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 451 DTFTEDG----WFKTGDTALYR-DGVYWIMGRtsVDI-IKSGGYKISALDVERHLLAHPDITDVAVIGAPDPTWGQKVTA 524
Cdd:cd12114 349 ARFVTHPdgerLYRTGDLGRYRpDGTLEFLGR--RDGqVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDPGGKRLAAF 426
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 2073725801 525 VVQLKKGKTLTLSQLQAWAREHMAPYTIPTGLILVEEMPRNQMGKVNKKDL 575
Cdd:cd12114 427 VVPDNDGTPIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
110-570 |
1.12e-34 |
|
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: 138.14 E-value: 1.12e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 110 LCANDASYTVAQWAAWMCGGIAVPLYRKHPPGE---LEYVISDSQSSLLVAGQPFMDTLEPLAqkLGLPCLQLPTTSSLD 186
Cdd:cd05931 54 LAPPGLDFVAAFLGCLYAGAIAVPLPPPTPGRHaerLAAILADAGPRVVLTTAAALAAVRAFA--ASRPAAGTPRLLVVD 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 187 TLQSEDIRMLPEQNISdwAERPAMLIYTSGTTGRPKGVLHTHSSLQAMVQGLVSEWAWNKDDVILHTLPLHHVHGIVNKL 266
Cdd:cd05931 132 LLPDTSAADWPPPSPD--PDDIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGL 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 267 MCPLWVGATCIMLP--EFSAQKV-WEQLISSKSPmvnVFMAVPTiysklieyydqhFTQPQVQDFIRAVCKE-----RIR 338
Cdd:cd05931 210 LTPLYSGGPSVLMSpaAFLRRPLrWLRLISRYRA---TISAAPN------------FAYDLCVRRVRDEDLEgldlsSWR 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 339 LMVSGSaalpQPV----LERWAE------ITGHVLLERYGMTEIGMALSNP---------------LKGSRVPGA----- 388
Cdd:cd05931 275 VALNGA----EPVrpatLRRFAEafapfgFRPEAFRPSYGLAEATLFVSGGppgtgpvvlrvdrdaLAGRAVAVAaddpa 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 389 ------VGVPLPGVEVRIMmtnstnaiiaegNSKGTRVKAglEGKEGELLVRGSSVFQKYWNKPQETADTF------TED 456
Cdd:cd05931 351 arelvsCGRPLPDQEVRIV------------DPETGRELP--DGEVGEIWVRGPSVASGYWGRPEATAETFgalaatDEG 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 457 GWFKTGDTALYRDGVYWIMGRTSvDIIKSGGYKISALDVERHLLAHPD---ITDVAVIGAPDPTwGQKVTAVVQLKKGKT 533
Cdd:cd05931 417 GWLRTGDLGFLHDGELYITGRLK-DLIIVRGRNHYPQDIEATAEEAHPalrPGCVAAFSVPDDG-EERLVVVAEVERGAD 494
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 2073725801 534 -LTLSQL-----QAWAREH-MAPYTIptglILVE--EMPRNQMGKV 570
Cdd:cd05931 495 pADLAAIaaairAAVAREHgVAPADV----VLVRpgSIPRTSSGKI 536
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
119-575 |
2.86e-34 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 139.71 E-value: 2.86e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 119 VAQWAAWMCGGIAVPLYRKHPPGELEYVISDSQSSLLVAGQPFMDTLePLAQklGLPCLQLPTTSSLDTLQSEDirmlPE 198
Cdd:PRK12316 4616 VGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAALLLTQSHLLQRL-PIPD--GLASLALDRDEDWEGFPAHD----PA 4688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 199 QNISdwAERPAMLIYTSGTTGRPKGVLHTHSSLQAMVQGLVSEWAWNKDDVILHTLPLhHVHGIVNKLMCPLWVGATCIM 278
Cdd:PRK12316 4689 VRLH--PDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSF-SFDGSHEGLYHPLINGASVVI 4765
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 279 ------LPEFSAQKVWEQLISskspmvnVFMAVPTIYsklieyydqhftQPQVQDFIRAVCKERIRLMVSGSAALPQPVL 352
Cdd:PRK12316 4766 rddslwDPERLYAEIHEHRVT-------VLVFPPVYL------------QQLAEHAERDGEPPSLRVYCFGGEAVAQASY 4826
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 353 ERWAEITGHV-LLERYGMTEIGM-ALSNPLKGSRVPGA----VGVPLPGVEVRImMTNSTNAIIAegnskgtrvkagleG 426
Cdd:PRK12316 4827 DLAWRALKPVyLFNGYGPTETTVtVLLWKARDGDACGAaympIGTPLGNRSGYV-LDGQLNPLPV--------------G 4891
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 427 KEGELLVRGSSVFQKYWNKPQETADTFTEDGW-------FKTGDTALYR-DGVYWIMGRtsVD-IIKSGGYKISALDVER 497
Cdd:PRK12316 4892 VAGELYLGGEGVARGYLERPALTAERFVPDPFgapggrlYRTGDLARYRaDGVIDYLGR--VDhQVKIRGFRIELGEIEA 4969
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 498 HLLAHPDITDVAVIGAPDPTWGQKV-------TAVVQLKKGKTLTLSQLQAWAREHMAPYTIPTGLILVEEMPRNQMGKV 570
Cdd:PRK12316 4970 RLREHPAVREAVVIAQEGAVGKQLVgyvvpqdPALADADEAQAELRDELKAALRERLPEYMVPAHLVFLARMPLTPNGKL 5049
|
....*
gi 2073725801 571 NKKDL 575
Cdd:PRK12316 5050 DRKAL 5054
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
174-579 |
3.26e-34 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 136.37 E-value: 3.26e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 174 LPCLQLPTTSSLDTLQSEDIRMlpeqnisDWA---ERPAM-LIYTSGTTGRPKGVLHTHSS--LQAMVQGLVSEWAWNKD 247
Cdd:PRK07008 147 LPAGSTPLLCYETLVGAQDGDY-------DWPrfdENQASsLCYTSGTTGNPKGALYSHRStvLHAYGAALPDAMGLSAR 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 248 DVILHTLPLHHVHGIVNKLMCPLwVGATCIML-PEFSAQKVWEqLISSKSpmVNVFMAVPTIYSKLIeyydQHFTQPQVQ 326
Cdd:PRK07008 220 DAVLPVVPMFHVNAWGLPYSAPL-TGAKLVLPgPDLDGKSLYE-LIEAER--VTFSAGVPTVWLGLL----NHMREAGLR 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 327 dFiravckERIRLMVSGSAALPQPVLERWAEITGHVLLERYGMTEI---GMALSNPLKGSRVPGAV--------GVPLPG 395
Cdd:PRK07008 292 -F------STLRRTVIGGSACPPAMIRTFEDEYGVEVIHAWGMTEMsplGTLCKLKWKHSQLPLDEqrkllekqGRVIYG 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 396 VEVRIMmtnstnaiiaegnskgtrvkaGLEGKE--------GELLVRGSSVFQKYWNKPQETADtfteDGWFKTGDTA-L 466
Cdd:PRK07008 365 VDMKIV---------------------GDDGRElpwdgkafGDLQVRGPWVIDRYFRGDASPLV----DGWFPTGDVAtI 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 467 YRDGVYWIMGRtSVDIIKSGGYKISALDVERHLLAHPDITDVAVIGAPDPTWGQKVTAVVQLKKGKTLTLSQLQAWAREH 546
Cdd:PRK07008 420 DADGFMQITDR-SKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLVVVKRPGAEVTREELLAFYEGK 498
|
410 420 430
....*....|....*....|....*....|...
gi 2073725801 547 MAPYTIPTGLILVEEMPRNQMGKVNKKDLLRKF 579
Cdd:PRK07008 499 VAKWWIPDDVVFVDAIPHTATGKLQKLKLREQF 531
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
164-575 |
4.72e-34 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 136.69 E-value: 4.72e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 164 TLEPLAQKLGLPCL---QLPTTSSLdtlqsedIRMLPEQNISDwaerPAMLIYTSGTTGRPKGVLHTHSSLQAMVQGLVS 240
Cdd:PLN03102 152 PKRPSSEELDYECLiqrGEPTPSLV-------ARMFRIQDEHD----PISLNYTSGTTADPKGVVISHRGAYLSTLSAII 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 241 EWAWNKDDVILHTLPLHHVHGivnklmcplWV--------GATCIMLPEFSAQKVWEQLissksPMVNV--FMAVPTIYS 310
Cdd:PLN03102 221 GWEMGTCPVYLWTLPMFHCNG---------WTftwgtaarGGTSVCMRHVTAPEIYKNI-----EMHNVthMCCVPTVFN 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 311 KLIE--YYDQHFTQPQVQdfiravckerirLMVSGSAalPQPVLERWAEITGHVLLERYGMTEIgmalSNPL-------K 381
Cdd:PLN03102 287 ILLKgnSLDLSPRSGPVH------------VLTGGSP--PPAALVKKVQRLGFQVMHAYGLTEA----TGPVlfcewqdE 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 382 GSRVPGAVGVPLpgvEVRIMMTNSTNAIIAEGNSKgTRVKAGLEGKE-GELLVRGSSVFQKYWNKPQETADTFtEDGWFK 460
Cdd:PLN03102 349 WNRLPENQQMEL---KARQGVSILGLADVDVKNKE-TQESVPRDGKTmGEIVIKGSSIMKGYLKNPKATSEAF-KHGWLN 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 461 TGDTA-LYRDGVYWIMGRtSVDIIKSGGYKISALDVERHLLAHPDITDVAVIGAPDPTWGQKVTAVVQLKKGKTLTLSQ- 538
Cdd:PLN03102 424 TGDVGvIHPDGHVEIKDR-SKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGETTKEDRv 502
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 2073725801 539 ---------LQAWAREHMAPYTIPTGLILVEEMPRNQMGKVNKKDL 575
Cdd:PLN03102 503 dklvtrerdLIEYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKL 548
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
128-575 |
1.67e-33 |
|
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: 133.61 E-value: 1.67e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 128 GGIAVPLYRKHPPGELEYVISDSQSSLLVagqpfmdTLEPLAQKLGLpcLQLPTTSSLDTLQSEDIRML-PEQNISDWAe 206
Cdd:cd17655 71 GGAYLPIDPDYPEERIQYILEDSGADILL-------TQSHLQPPIAF--IGLIDLLDEDTIYHEESENLePVSKSDDLA- 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 207 rpaMLIYTSGTTGRPKGVLHTHSSLQAMVQGLVSEWAWNKDDVILHTLPLhHVHGIVNKLMCPLWVGATCImlpefsaqk 286
Cdd:cd17655 141 ---YVIYTSGSTGKPKGVMIEHRGVVNLVEWANKVIYQGEHLRVALFASI-SFDASVTEIFASLLSGNTLY--------- 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 287 vweqlISSKSPMVNVfmavptiySKLIEYYDQH-----FTQP---QVQDFIRAVCKERIRLMVSGSAALPQPVLERWAEI 358
Cdd:cd17655 208 -----IVRKETVLDG--------QALTQYIRQNritiiDLTPahlKLLDAADDSEGLSLKHLIVGGEALSTELAKKIIEL 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 359 TGH--VLLERYGMTE------IGMALSNPLKGSRVPgaVGVPLpgvevrimmtNSTNAIIAEGNSKGTRVkagleGKEGE 430
Cdd:cd17655 275 FGTnpTITNAYGPTEttvdasIYQYEPETDQQVSVP--IGKPL----------GNTRIYILDQYGRPQPV-----GVAGE 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 431 LLVRGSSVFQKYWNKPQETADTFTEDGW------FKTGDTALYR-DGVYWIMGRTSvDIIKSGGYKISALDVERHLLAHP 503
Cdd:cd17655 338 LYIGGEGVARGYLNRPELTAEKFVDDPFvpgermYRTGDLARWLpDGNIEFLGRID-HQVKIRGYRIELGEIEARLLQHP 416
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2073725801 504 DITDVAVIGAPDPTWGQKVTAVVQLKkgKTLTLSQLQAWAREHMAPYTIPTGLILVEEMPRNQMGKVNKKDL 575
Cdd:cd17655 417 DIKEAVVIARKDEQGQNYLCAYIVSE--KELPVAQLREFLARELPDYMIPSYFIKLDEIPLTPNGKVDRKAL 486
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
205-578 |
1.66e-32 |
|
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called acetyl-CoA synthetase and acetyl-activating enzyme. It catalyzes the reaction ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA and belongs to the family of AMP-binding enzymes described by pfam00501.
Pssm-ID: 274022 [Multi-domain] Cd Length: 626 Bit Score: 132.37 E-value: 1.66e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 205 AERPAMLIYTSGTTGRPKGVLHThsSLQAMVQGLVS-EWAWN-KDDVIL-----------HTlplHHVHGivnklmcPLW 271
Cdd:TIGR02188 236 SEDPLFILYTSGSTGKPKGVLHT--TGGYLLYAAMTmKYVFDiKDGDIFwctadvgwitgHS---YIVYG-------PLA 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 272 VGATCIML---PEFSAQKVWEQLISSKSpmVNVFMAVPTIYSKLIEYYDQHftqpqVQDFIRavckERIRLMvsGSAALP 348
Cdd:TIGR02188 304 NGATTVMFegvPTYPDPGRFWEIIEKHK--VTIFYTAPTAIRALMRLGDEW-----VKKHDL----SSLRLL--GSVGEP 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 349 -QPVLERWA-EITGH---VLLERYGMTEIGMALSNPLKG--SRVPGAVGVPLPGVEVRIMmtnstnaiiaegNSKGTRVK 421
Cdd:TIGR02188 371 iNPEAWMWYyKVVGKercPIVDTWWQTETGGIMITPLPGatPTKPGSATLPFFGIEPAVV------------DEEGNPVE 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 422 AglEGKEGELLVRGS--SVFQKYWNKPQETADTFTED--GWFKTGDTALY-RDGVYWIMGRTSvDIIKSGGYKISALDVE 496
Cdd:TIGR02188 439 G--PGEGGYLVIKQPwpGMLRTIYGDHERFVDTYFSPfpGYYFTGDGARRdKDGYIWITGRVD-DVINVSGHRLGTAEIE 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 497 RHLLAHPDITDVAVIGAPDPTWGQKVTAVVQLKKGKT--LTLSQ-LQAWAREHMAPYTIPTGLILVEEMPRNQMGKVNKK 573
Cdd:TIGR02188 516 SALVSHPAVAEAAVVGIPDDIKGQAIYAFVTLKDGYEpdDELRKeLRKHVRKEIGPIAKPDKIRFVPGLPKTRSGKIMRR 595
|
....*
gi 2073725801 574 dLLRK 578
Cdd:TIGR02188 596 -LLRK 599
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
115-575 |
4.65e-32 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 132.77 E-value: 4.65e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 115 ASYTVAQWAAWMCGGIAVPLYRKHPPGELEYVISDSQSSLLVAGQPFMDTLePLAQKLGLPCLQLPTtSSLDTLQSEDir 194
Cdd:PRK12316 572 IEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQSHLGRKL-PLAAGVQVLDLDRPA-AWLEGYSEEN-- 647
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 195 mlPEQNISdwAERPAMLIYTSGTTGRPKGVLHTHSSLQAMVQGLVSEWAWNKDDVILHTLPLHHVHGiVNKLMCPLWVGA 274
Cdd:PRK12316 648 --PGTELN--PENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVS-VWEFFWPLMSGA 722
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 275 TCIMLPE---FSAQKVWEqLISSKSpmVNVFMAVPTIYSKLIEyydqhftQPQVQDFiravckERIRLMVSGSAALPQPV 351
Cdd:PRK12316 723 RLVVAAPgdhRDPAKLVE-LINREG--VDTLHFVPSMLQAFLQ-------DEDVASC------TSLRRIVCSGEALPADA 786
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 352 LER-WAEITGHVLLERYGMTE--IGMALSNPLK--GSRVPgaVGVPLPGVEVRIMmtnstnaiiaegNSKGTRVKAGLeg 426
Cdd:PRK12316 787 QEQvFAKLPQAGLYNLYGPTEaaIDVTHWTCVEegGDSVP--IGRPIANLACYIL------------DANLEPVPVGV-- 850
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 427 kEGELLVRGSSVFQKYWNKPQETADTFTEDGW------FKTGDTALYR-DGVYWIMGRTSvDIIKSGGYKISALDVERHL 499
Cdd:PRK12316 851 -LGELYLAGRGLARGYHGRPGLTAERFVPSPFvagermYRTGDLARYRaDGVIEYAGRID-HQVKLRGLRIELGEIEARL 928
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2073725801 500 LAHPDITDVAVIGAPdptwGQKVTAVVQLKKGKTLTLSQLQAWAREHMAPYTIPTGLILVEEMPRNQMGKVNKKDL 575
Cdd:PRK12316 929 LEHPWVREAAVLAVD----GKQLVGYVVLESEGGDWREALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKAL 1000
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
209-550 |
6.17e-32 |
|
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: 129.26 E-value: 6.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 209 AMLIYTSGTTGRPKGVLHTHSSLQAMVQGL---VSEWAwNKDDVILHTLPLHHVHGIVNKLMCPLWVGATC--------- 276
Cdd:cd17639 91 ACIMYTSGSTGNPKGVMLTHGNLVAGIAGLgdrVPELL-GPDDRYLAYLPLAHIFELAAENVCLYRGGTIGygsprtltd 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 277 -IM------LPEF------SAQKVWEQL---ISSKSPMVNVFMAvpTIYSKLIEY--------YDQHFTQPQVQDFIRAV 332
Cdd:cd17639 170 kSKrgckgdLTEFkptlmvGVPAIWDTIrkgVLAKLNPMGGLKR--TLFWTAYQSklkalkegPGTPLLDELVFKKVRAA 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 333 CKERIRLMVSGSAALpQPVLERWAEITGHVLLERYGMTEI--GMALSNPlkGSRVPGAVGVPLPGVEVRIMMtnstnaiI 410
Cdd:cd17639 248 LGGRLRYMLSGGAPL-SADTQEFLNIVLCPVIQGYGLTETcaGGTVQDP--GDLETGRVGPPLPCCEIKLVD-------W 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 411 AEGN----SKGTRvkaglegkeGELLVRGSSVFQKYWNKPQETADTFTEDGWFKTGDTALYR-DGVYWIMGRTSvDIIKS 485
Cdd:cd17639 318 EEGGystdKPPPR---------GEILIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHpDGTLKIIDRKK-DLVKL 387
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2073725801 486 --GGYkISALDVERHLLAHPDITDVAVIGAPDPTwgqKVTAVVqlkkgkTLTLSQLQAWAREHMAPY 550
Cdd:cd17639 388 qnGEY-IALEKLESIYRSNPLVNNICVYADPDKS---YPVAIV------VPNEKHLTKLAEKHGVIN 444
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
47-577 |
1.03e-31 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 128.59 E-value: 1.03e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 47 PGV-GRVAPvfSRASVYgdnVAITDHSGSHTfcSLYKNSKSLAGLITKAltcqsGDLQGKCISFLCANDASYTVAQWAAW 125
Cdd:PRK13390 3 PGThAQIAP--DRPAVI---VAETGEQVSYR--QLDDDSAALARVLYDA-----GLRTGDVVALLSDNSPEALVVLWAAL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 126 MCGGIAVPLYRKHPPGELEYVISDSQSSLLVAGQpfmdTLEPLAQKLGLPC-LQLPTTSSLDTLQSEDIRMLPEQniSDW 204
Cdd:PRK13390 71 RSGLYITAINHHLTAPEADYIVGDSGARVLVASA----ALDGLAAKVGADLpLRLSFGGEIDGFGSFEAALAGAG--PRL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 205 AERP--AMLIYTSGTTGRPKGV---LHTHSSLQ------AMVQGLvseWAWNKDDVILHTLPLHHVH-----GIVNKLmc 268
Cdd:PRK13390 145 TEQPcgAVMLYSSGTTGFPKGIqpdLPGRDVDApgdpivAIARAF---YDISESDIYYSSAPIYHAAplrwcSMVHAL-- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 269 plwvGATCIMLPEFSAQKVWEQLISSKspmVNVFMAVPTIYSKLIEYYDQHFTQPQVQDfIRAVCKerirlmvsgsAALP 348
Cdd:PRK13390 220 ----GGTVVLAKRFDAQATLGHVERYR---ITVTQMVPTMFVRLLKLDADVRTRYDVSS-LRAVIH----------AAAP 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 349 QPVLERWAEIT--GHVLLERYGMTEI-GMALSNPLKGSRVPGAVGVPLPGvEVRIMmtnstnaiiaegNSKGTRVKAGle 425
Cdd:PRK13390 282 CPVDVKHAMIDwlGPIVYEYYSSTEAhGMTFIDSPDWLAHPGSVGRSVLG-DLHIC------------DDDGNELPAG-- 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 426 gKEGELLVRGSSVFQKYWNKPQETADTF--TEDGWFKTGDTA-LYRDGVYWIMGRTSVDIIkSGGYKISALDVERHLLAH 502
Cdd:PRK13390 347 -RIGTVYFERDRLPFRYLNDPEKTAAAQhpAHPFWTTVGDLGsVDEDGYLYLADRKSFMII-SGGVNIYPQETENALTMH 424
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2073725801 503 PDITDVAVIGAPDPTWGQKVTAVVQLKKG---KTLTLSQLQAWAREHMAPYTIPTGLILVEEMPRNQMGKVnKKDLLR 577
Cdd:PRK13390 425 PAVHDVAVIGVPDPEMGEQVKAVIQLVEGirgSDELARELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKL-VKGLLR 501
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
128-577 |
1.06e-31 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 131.82 E-value: 1.06e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 128 GGIAVPLYRKHPPGELEYVISDSQSSLLVAGQPFMDTLePLAQklGLPCLQL-PTTSSLDTLQSEDirmlPEQNISDwaE 206
Cdd:PRK12467 1648 GGAYVPLDPEYPRERLAYMIEDSGIELLLTQSHLQARL-PLPD--GLRSLVLdQEDDWLEGYSDSN----PAVNLAP--Q 1718
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 207 RPAMLIYTSGTTGRPKGVLHTHSSLQAMVQGLVSEWAWNKDDVILHTLPlHHVHGIVNKLMCPLWVGATCIMLPeFSAQK 286
Cdd:PRK12467 1719 NLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTS-FAFDVSVWELFWPLINGARLVIAP-PGAHR 1796
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 287 VWEQLISS-KSPMVNVFMAVPTIYSKLIEyYDQHFTQPQvqdfiravckeRIRLMVSGSAALPQPVLERWAEITGHV-LL 364
Cdd:PRK12467 1797 DPEQLIQLiERQQVTTLHFVPSMLQQLLQ-MDEQVEHPL-----------SLRRVVCGGEALEVEALRPWLERLPDTgLF 1864
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 365 ERYGMTEIGM-------ALSNPLKGSRVPgaVGVPLPGVEVRImMTNSTNAIIAegnskgtrvkagleGKEGELLVRGSS 437
Cdd:PRK12467 1865 NLYGPTETAVdvthwtcRRKDLEGRDSVP--IGQPIANLSTYI-LDASLNPVPI--------------GVAGELYLGGVG 1927
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 438 VFQKYWNKPQETADTFTEDGW-------FKTGDTALYR-DGVYWIMGRtsVD-IIKSGGYKISALDVERHLLAHPDITDV 508
Cdd:PRK12467 1928 LARGYLNRPALTAERFVADPFgtvgsrlYRTGDLARYRaDGVIEYLGR--IDhQVKIRGFRIELGEIEARLREQGGVREA 2005
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2073725801 509 AVIGAPDPTWGQKVTAVVQLKKG---KTLTLSQLQAWAREHMAP----YTIPTGLILVEEMPRNQMGKVNKKDLLR 577
Cdd:PRK12467 2006 VVIAQDGANGKQLVAYVVPTDPGlvdDDEAQVALRAILKNHLKAslpeYMVPAHLVFLARMPLTPNGKLDRKALPA 2081
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
185-583 |
5.60e-31 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 125.88 E-value: 5.60e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 185 LDTLQSEDIRMLPEQNISDWAERPAMLIYTSGTTGRPKGVLHTHSSLQAMVQGLVSEWAWNKddviLHT---LPLHHVHG 261
Cdd:PRK07445 99 LDQLKLSHPPPLPSQGILPNLETGWIMIPTGGSSGQIRFAIHTWETLTASVQGFQRYFQLQQ----VNSfcvLPLYHVSG 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 262 IVnKLMCPLWVGATCIMLPefsaqkvWEQLISSKSPMVNV---FMA-VPTiysKLieyydQHFTQPQVQ---DFiRAVck 334
Cdd:PRK07445 175 LM-QFMRSFLTGGKLVILP-------YKRLKSGQELPPNPsdfFLSlVPT---QL-----QRLLQLRPQwlaQF-RTI-- 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 335 erirlMVSGSAALPQpVLE--RWAEITghvLLERYGMTEIG--MALSNP---LKGSRvpgAVGVPLPGVEVRIMmtnstn 407
Cdd:PRK07445 236 -----LLGGAPAWPS-LLEqaRQLQLR---LAPTYGMTETAsqIATLKPddfLAGNN---SSGQVLPHAQITIP------ 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 408 aiiaegnskgtrvkaglEGKEGELLVRGSSVFQKYWnkPQetadTFTEDGWFKTGDTA-LYRDGVYWIMGRTSVDIIkSG 486
Cdd:PRK07445 298 -----------------ANQTGNITIQAQSLALGYY--PQ----ILDSQGIFETDDLGyLDAQGYLHILGRNSQKII-TG 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 487 GYKISALDVERHLLAHPDITDVAVIGAPDPTWGQKVTAVVQLKKGkTLTLSQLQAWAREHMAPYTIPTGLILVEEMPRNQ 566
Cdd:PRK07445 354 GENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYVPKDP-SISLEELKTAIKDQLSPFKQPKHWIPVPQLPRNP 432
|
410
....*....|....*..
gi 2073725801 567 MGKVNKKdLLRKFFPTR 583
Cdd:PRK07445 433 QGKINRQ-QLQQIAVQR 448
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
63-570 |
6.58e-31 |
|
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: 127.31 E-value: 6.58e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 63 GDNVAI------TDHSGSHTFCSLYKNSKSLAGLItKALTCQSGDLQGKCISFLcandASYTVAQWAAWMCGGIAVPLYR 136
Cdd:cd17634 67 GDRTAIiyegddTSQSRTISYRELHREVCRFAGTL-LDLGVKKGDRVAIYMPMI----PEAAVAMLACARIGAVHSVIFG 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 137 KHPPGELEYVISDSQSSLLVAGQPFMD-----TLEPLAQKLGLPCLQLPTTSSLDTLQSEDIRMLPEQNIsDW------- 204
Cdd:cd17634 142 GFAPEAVAGRIIDSSSRLLITADGGVRagrsvPLKKNVDDALNPNVTSVEHVIVLKRTGSDIDWQEGRDL-WWrdliaka 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 205 ----------AERPAMLIYTSGTTGRPKGVLHTHSS-LQAMVQGLVSEWAWNKDDVILHTLPLHHVHGIVNKLMCPLWVG 273
Cdd:cd17634 221 spehqpeamnAEDPLFILYTSGTTGKPKGVLHTTGGyLVYAATTMKYVFDYGPGDIYWCTADVGWVTGHSYLLYGPLACG 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 274 ATCIMlpeFSAQKVWeqlisskspmvnvfmavPTIySKLIEYYDQH-----FTQPQVqdfIRAVCKE---------RIRL 339
Cdd:cd17634 301 ATTLL---YEGVPNW-----------------PTP-ARMWQVVDKHgvnilYTAPTA---IRALMAAgddaiegtdRSSL 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 340 MVSGSAALP-QPVLERWAeiTGHVLLER------YGMTEIGMALSNPLKGSR--VPGAVGVPLPGVEVRImmtnstnaII 410
Cdd:cd17634 357 RILGSVGEPiNPEAYEWY--WKKIGKEKcpvvdtWWQTETGGFMITPLPGAIelKAGSATRPVFGVQPAV--------VD 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 411 AEGNSKGTrvkagleGKEGELLVRGS--SVFQKYWNKPQETADTF--TEDGWFKTGDTAlYRD--GVYWIMGRtSVDIIK 484
Cdd:cd17634 427 NEGHPQPG-------GTEGNLVITDPwpGQTRTLFGDHERFEQTYfsTFKGMYFSGDGA-RRDedGYYWITGR-SDDVIN 497
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 485 SGGYKISALDVERHLLAHPDITDVAVIGAPDPTWGQKVTAVVQLKKGKT--LTL-SQLQAWAREHMAPYTIPTGLILVEE 561
Cdd:cd17634 498 VAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLNHGVEpsPELyAELRNWVRKEIGPLATPDVVHWVDS 577
|
....*....
gi 2073725801 562 MPRNQMGKV 570
Cdd:cd17634 578 LPKTRSGKI 586
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
55-578 |
9.53e-31 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 126.25 E-value: 9.53e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 55 VFSRASVYGDNVAITDH--SGSHTFCSLYKNSKSLAglitKALTcQSGDLQGKCISFLCANDASYTVAQWAAWMCGGIav 132
Cdd:PLN02330 34 VLQDAELYADKVAFVEAvtGKAVTYGEVVRDTRRFA----KALR-SLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGV-- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 133 pLYRKHPPG---ELEYVISDSQSSLLVAGqpfmDTLEPLAQKLGLPCLQLPTTS----------------SLDTLQSEDI 193
Cdd:PLN02330 107 -FSGANPTAlesEIKKQAEAAGAKLIVTN----DTNYGKVKGLGLPVIVLGEEKiegavnwkelleaadrAGDTSDNEEI 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 194 RMlpeqniSDWAERPamliYTSGTTGRPKGVLHTHSSLqamVQGLVSEWAWNKDDVI-----LHTLPLHHVHGIVNKLMC 268
Cdd:PLN02330 182 LQ------TDLCALP----FSSGTTGISKGVMLTHRNL---VANLCSSLFSVGPEMIgqvvtLGLIPFFHIYGITGICCA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 269 PLWVGATCIMLPEFSAQKVWEQLISSKspmVNVFMAVPTIYSKLIEyydqhftQPQVQDFirAVCKERIRLMVSGSAALP 348
Cdd:PLN02330 249 TLRNKGKVVVMSRFELRTFLNALITQE---VSFAPIVPPIILNLVK-------NPIVEEF--DLSKLKLQAIMTAAAPLA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 349 QPVLERW-AEITGHVLLERYGMTE---IGMALSNPLKGSRVP--GAVGVPLPGVEVRIMMTNSTNAIIaegnskgtrvka 422
Cdd:PLN02330 317 PELLTAFeAKFPGVQVQEAYGLTEhscITLTHGDPEKGHGIAkkNSVGFILPNLEVKFIDPDTGRSLP------------ 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 423 glEGKEGELLVRGSSVFQKYWNKPQETADTFTEDGWFKTGDTA-LYRDGVYWIMGRTSvDIIKSGGYKISALDVERHLLA 501
Cdd:PLN02330 385 --KNTPGELCVRSQCVMQGYYNNKEETDRTIDEDGWLHTGDIGyIDDDGDIFIVDRIK-ELIKYKGFQVAPAELEAILLT 461
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2073725801 502 HPDITDVAVIGAPDPTWGQKVTAVVQLKKGKTLTLSQLQAWAREHMAPYTIPTGLILVEEMPRNQMGKVNKKDLLRK 578
Cdd:PLN02330 462 HPSVEDAAVVPLPDEEAGEIPAACVVINPKAKESEEDILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLKEK 538
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
128-575 |
1.61e-30 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 127.97 E-value: 1.61e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 128 GGIAVPLYRKHPPGELEYVISDSQSSLLvagqpfmdtlepLAQKLGLPCLQLPTtssldtlqseDIRMLPEQNISDW--- 204
Cdd:PRK12467 586 GGAYVPLDPEYPQDRLAYMLDDSGVRLL------------LTQSHLLAQLPVPA----------GLRSLCLDEPADLlcg 643
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 205 --AERP---------AMLIYTSGTTGRPKGVLHTHSSLQAMVQGLVSEWAWNKDDVILHTLPLhHVHGIVNKLMCPLWVG 273
Cdd:PRK12467 644 ysGHNPevaldpdnlAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVSTF-AFDLGVTELFGALASG 722
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 274 ATCIMLPE---FSAQKVWEQLISSKspmVNVFMAVPTIYSKLIeyydqhftqpqvQDFIRAVCKERIRLMVSGSaALPQP 350
Cdd:PRK12467 723 ATLHLLPPdcaRDAEAFAALMADQG---VTVLKIVPSHLQALL------------QASRVALPRPQRALVCGGE-ALQVD 786
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 351 VLERWAEITGHV-LLERYGMTE--IGMALSNPLKGSRVPGAV--GVPLPGVEVRImMTNSTNAIIAegnskgtrvkagle 425
Cdd:PRK12467 787 LLARVRALGPGArLINHYGPTEttVGVSTYELSDEERDFGNVpiGQPLANLGLYI-LDHYLNPVPV-------------- 851
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 426 GKEGELLVRGSSVFQKYWNKPQETADTFTEDGW-------FKTGDTALYR-DGVYWIMGRTSvDIIKSGGYKISALDVER 497
Cdd:PRK12467 852 GVVGELYIGGAGLARGYHRRPALTAERFVPDPFgadggrlYRTGDLARYRaDGVIEYLGRMD-HQVKIRGFRIELGEIEA 930
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 498 HLLAHPDITDVAVIGAPDPTWGQKVTAVVQLKKG----KTLTLSQLQAWAREHMAPYTIPTGLILVEEMPRNQMGKVNKK 573
Cdd:PRK12467 931 RLLAQPGVREAVVLAQPGDAGLQLVAYLVPAAVAdgaeHQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRK 1010
|
..
gi 2073725801 574 DL 575
Cdd:PRK12467 1011 AL 1012
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
128-463 |
2.07e-30 |
|
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: 125.41 E-value: 2.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 128 GGIAVPLYRKHPPGELEYVISDSQSSLLVAgqpfmdtleplaqklglpclqlptTSSLDTLQSEDIRMLPEQNISDwAER 207
Cdd:cd05927 56 SLVTVPLYDTLGPEAIEYILNHAEISIVFC------------------------DAGVKVYSLEEFEKLGKKNKVP-PPP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 208 P-----AMLIYTSGTTGRPKGVLHTHSSLQAMVQGLVSEW----AWNKDDVILHTLPLHHVHGIVNKLMCpLWVGAtCIM 278
Cdd:cd05927 111 PkpedlATICYTSGTTGNPKGVMLTHGNIVSNVAGVFKILeilnKINPTDVYISYLPLAHIFERVVEALF-LYHGA-KIG 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 279 LPEFSAQKVWEQLISSKsPmvNVFMAVPTIYSKLieyYDQHFTQPQVQDFIR------------------AVCKE----- 335
Cdd:cd05927 189 FYSGDIRLLLDDIKALK-P--TVFPGVPRVLNRI---YDKIFNKVQAKGPLKrklfnfalnyklaelrsgVVRASpfwdk 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 336 ------------RIRLMVSGSAALPQPVLERWAEITGHVLLERYGMTEI--GMALSNPlkGSRVPGAVGVPLPGVEVRIm 401
Cdd:cd05927 263 lvfnkikqalggNVRLMLTGSAPLSPEVLEFLRVALGCPVLEGYGQTECtaGATLTLP--GDTSVGHVGGPLPCAEVKL- 339
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2073725801 402 mtnstnAIIAEGNSKGTRVKAglegkEGELLVRGSSVFQKYWNKPQETADTFTEDGWFKTGD 463
Cdd:cd05927 340 ------VDVPEMNYDAKDPNP-----RGEVCIRGPNVFSGYYKDPEKTAEALDEDGWLHTGD 390
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
76-572 |
1.18e-29 |
|
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: 123.30 E-value: 1.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 76 TFCSLYKNSKSLA-GLitKALTCQSGDLqgkcISFLCANDASYTVAQWAAWMCGGIAVPLYRKHPPGELEYVISDSQSSL 154
Cdd:cd17641 13 TWADYADRVRAFAlGL--LALGVGRGDV----VAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 155 LVAG-QPFMDTLEPLAQKL------------GLPCLQLPTTSSLDTLQSED---IRMLPEQNISDWAERP----AMLIYT 214
Cdd:cd17641 87 VIAEdEEQVDKLLEIADRIpsvryviycdprGMRKYDDPRLISFEDVVALGralDRRDPGLYEREVAAGKgedvAVLCTT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 215 SGTTGRPKGVLHTHSSLQAMVQGLVSEWAWNKDDVILHTLPLHHVHGIVNKLMCPLWVGaTCIMLPE------------- 281
Cdd:cd17641 167 SGTTGKPKLAMLSHGNFLGHCAAYLAADPLGPGDEYVSVLPLPWIGEQMYSVGQALVCG-FIVNFPEepetmmedlreig 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 282 ----FSAQKVWEQLIS------SKSPMVNVFMAvpTIYSKL-IEYYDQHFTQPQVQDFIRAVCK---------------- 334
Cdd:cd17641 246 ptfvLLPPRVWEGIAAdvrarmMDATPFKRFMF--ELGMKLgLRALDRGKRGRPVSLWLRLASWladallfrplrdrlgf 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 335 ERIRLMVSGSAALpQPVLERWAEITGHVLLERYGMTEIGMALSNPLKGSRVPGAVGVPLPGVEVRImmtnstnaiiaegn 414
Cdd:cd17641 324 SRLRSAATGGAAL-GPDTFRFFHAIGVPLKQLYGQTELAGAYTVHRDGDVDPDTVGVPFPGTEVRI-------------- 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 415 skgtrvkagleGKEGELLVRGSSVFQKYWNKPQETADTFTEDGWFKTGDTALYR-DGVYWIMGRTSvDIIK-SGGYKISA 492
Cdd:cd17641 389 -----------DEVGEILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKeNGHLVVIDRAK-DVGTtSDGTRFSP 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 493 LDVERHLLAHPDITDVAVIGAPDPtwgqKVTAVVQLKkgktltLSQLQAWAREHMAPYTIPTGLIL---VEEMPRNQMGK 569
Cdd:cd17641 457 QFIENKLKFSPYIAEAVVLGAGRP----YLTAFICID------YAIVGKWAEQRGIAFTTYTDLASrpeVYELIRKEVEK 526
|
...
gi 2073725801 570 VNK 572
Cdd:cd17641 527 VNA 529
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
211-578 |
1.35e-29 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 123.03 E-value: 1.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 211 LIYTSGTTGRPKGVLHTHSSLQAMVQGLVSEWAWNKDDVILHTLPLHHVHGivnklMCPLWVGA----TCIMLPEFSAQK 286
Cdd:PLN02479 200 LGYTSGTTASPKGVVLHHRGAYLMALSNALIWGMNEGAVYLWTLPMFHCNG-----WCFTWTLAalcgTNICLRQVTAKA 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 287 VWEQLISSKspmVNVFMAVPTIYSKLIEY--YDQHFTQPQVqdfiravckerIRLMVSGSAalPQPVLERWAEITGHVLL 364
Cdd:PLN02479 275 IYSAIANYG---VTHFCAAPVVLNTIVNApkSETILPLPRV-----------VHVMTAGAA--PPPSVLFAMSEKGFRVT 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 365 ERYGMTEIgMALSN------------PLKGSRVPGAVGVPLPGVE-VRIMMTNSTNAIIAEGNSKgtrvkaglegkeGEL 431
Cdd:PLN02479 339 HTYGLSET-YGPSTvcawkpewdslpPEEQARLNARQGVRYIGLEgLDVVDTKTMKPVPADGKTM------------GEI 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 432 LVRGSSVFQKYWNKPQETADTFtEDGWFKTGDTAL-YRDGVYWIMGRtSVDIIKSGGYKISALDVERHLLAHPDITDVAV 510
Cdd:PLN02479 406 VMRGNMVMKGYLKNPKANEEAF-ANGWFHSGDLGVkHPDGYIEIKDR-SKDIIISGGENISSLEVENVVYTHPAVLEASV 483
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2073725801 511 IGAPDPTWGQKVTAVVQLKKG-----KTLTLSQLQAWAREHMAPYTIPTGLILvEEMPRNQMGKVNKKDLLRK 578
Cdd:PLN02479 484 VARPDERWGESPCAFVTLKPGvdksdEAALAEDIMKFCRERLPAYWVPKSVVF-GPLPKTATGKIQKHVLRAK 555
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
205-573 |
1.53e-29 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 124.65 E-value: 1.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 205 AERPAMLIYTSGTTGRPKGVLHTHSSLQAMVQGLVSEWAWNKDDVILHTLPLHHVHGIVNKLMCPLWVGATCIMLPEFSA 284
Cdd:PRK08633 781 PDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSSLPFFHSFGLTVTLWLPLLEGIKVVYHPDPTD 860
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 285 QKVWEQLISSKSpmVNVFMAVPT---IYSKlieyydqhftQPQVQ--DFiravckERIRLMVSGSAALPQPVLERWAEIT 359
Cdd:PRK08633 861 ALGIAKLVAKHR--ATILLGTPTflrLYLR----------NKKLHplMF------ASLRLVVAGAEKLKPEVADAFEEKF 922
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 360 GHVLLERYGMTE-----------IGMALSNPLKGSRvPGAVGVPLPGVEVRIMMTNStnaiiaegnskGTRVKaglEGKE 428
Cdd:PRK08633 923 GIRILEGYGATEtspvasvnlpdVLAADFKRQTGSK-EGSVGMPLPGVAVRIVDPET-----------FEELP---PGED 987
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 429 GELLVRGSSVFQKYWNKPQETADTFTE---DGWFKTGDTA-LYRDGVYWIMGRTSvDIIKSGGYKISALDVERHLLA--H 502
Cdd:PRK08633 988 GLILIGGPQVMKGYLGDPEKTAEVIKDidgIGWYVTGDKGhLDEDGFLTITDRYS-RFAKIGGEMVPLGAVEEELAKalG 1066
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2073725801 503 PDITDVAVIGAPDPTWGQKVTAVVQLKKGKTLTLsqLQAWAREHMAPYTIPTGLILVEEMPRNQMGKVNKK 573
Cdd:PRK08633 1067 GEEVVFAVTAVPDEKKGEKLVVLHTCGAEDVEEL--KRAIKESGLPNLWKPSRYFKVEALPLLGSGKLDLK 1135
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
64-577 |
2.32e-29 |
|
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: 120.88 E-value: 2.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 64 DNVAITDHSGSHTFCSLYKNSKSLAGLITkaltcQSGDLQGKCISFLCANDASYTVAQWAAWMCGGIAVPLYRKHPPGEL 143
Cdd:cd17653 12 DAVAVESLGGSLTYGELDAASNALANRLL-----QLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSARI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 144 EYVISDSQSSLLVagqpfmdtleplaqklglpclqlpTTSSLDTLqsedirmlpeqnisdwaerpAMLIYTSGTTGRPKG 223
Cdd:cd17653 87 QAILRTSGATLLL------------------------TTDSPDDL--------------------AYIIFTSGSTGIPKG 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 224 VLHTHSSLQAMVQglvsewaWNKDDviLHTLP---LHHVHGI-----VNKLMCPLWVGATcIMLPEFSAQkvWEQLISSk 295
Cdd:cd17653 123 VMVPHRGVLNYVS-------QPPAR--LDVGPgsrVAQVLSIafdacIGEIFSTLCNGGT-LVLADPSDP--FAHVART- 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 296 spmVNVFMAVPTIYSKLieyydqhftqpQVQDFiravckERIRLMVSGSAALPQPVLERWAEitGHVLLERYGMTE--IG 373
Cdd:cd17653 190 ---VDALMSTPSILSTL-----------SPQDF------PNLKTIFLGGEAVPPSLLDRWSP--GRRLYNAYGPTEctIS 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 374 MALSNPLKGSRVPgaVGVPLPGVEVRIMmtnstnaiiaegNSKGTRVkagLEGKEGELLVRGSSVFQKYWNKPQETADTF 453
Cdd:cd17653 248 STMTELLPGQPVT--IGKPIPNSTCYIL------------DADLQPV---PEGVVGEICISGVQVARGYLGNPALTASKF 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 454 TEDGW------FKTGDTALY-RDGVYWIMGRTSVDIiKSGGYKIS-ALDVERHLLAHPDITDVAVIGAPDptwgqkvtAV 525
Cdd:cd17653 311 VPDPFwpgsrmYRTGDYGRWtEDGGLEFLGREDNQV-KVRGFRINlEEIEEVVLQSQPEVTQAAAIVVNG--------RL 381
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 2073725801 526 VQLKKGKTLTLSQLQAWAREHMAPYTIPTGLILVEEMPRNQMGKVNKKDLLR 577
Cdd:cd17653 382 VAFVTPETVDVDGLRSELAKHLPSYAVPDRIIALDSFPLTANGKVDRKALRE 433
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
149-583 |
3.01e-29 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 122.83 E-value: 3.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 149 DSQSSLLVAGQPFMDTLEPlaqklglpclqlPTTSSLDTLQSEDIRMLPEQNISDWAERPAMLIYTSGTTGRPKGVLHTH 228
Cdd:PRK06060 100 NTEPALVVTSDALRDRFQP------------SRVAEAAELMSEAARVAPGGYEPMGGDALAYATYTSGTTGPPKAAIHRH 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 229 SSLQAMVQGLVSE-WAWNKDDVILHTLPLHHVHGIVNKLMCPLWVGATCIMLPEFSAQKVWEQLISSKSPmvNVFMAVPT 307
Cdd:PRK06060 168 ADPLTFVDAMCRKaLRLTPEDTGLCSARMYFAYGLGNSVWFPLATGGSAVINSAPVTPEAAAILSARFGP--SVLYGVPN 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 308 IYSKLIEYYDQhftqpqvqDFIRAVckeriRLMVSGSAALPQPVLERWAEITGHV-LLERYGMTEIGMA-LSNPLKGSRv 385
Cdd:PRK06060 246 FFARVIDSCSP--------DSFRSL-----RCVVSAGEALELGLAERLMEFFGGIpILDGIGSTEVGQTfVSNRVDEWR- 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 386 PGAVGVPLPGVEVRImmtnstnaIIAEGNSKGTrvkagleGKEGELLVRGSSVFQKYWNKPQEtadTFTEDGWFKTGDTA 465
Cdd:PRK06060 312 LGTLGRVLPPYEIRV--------VAPDGTTAGP-------GVEGDLWVRGPAIAKGYWNRPDS---PVANEGWLDTRDRV 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 466 LYrDGVYWIM-GRTSVDIIKSGGYKISALDVERHLLAHPDITDVAVIGAPDPTWGQKVTAVVQLKKGKTLTLSQLQAWAR 544
Cdd:PRK06060 374 CI-DSDGWVTyRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSGATIDGSVMRDLHR 452
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 2073725801 545 E---HMAPYTIPTGLILVEEMPRNQMGKVnKKDLLRKFFPTR 583
Cdd:PRK06060 453 GllnRLSAFKVPHRFAVVDRLPRTPNGKL-VRGALRKQSPTK 493
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
205-577 |
4.40e-29 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 119.98 E-value: 4.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 205 AERPAMLIYTSGTTGRPKGVLHTHSSLQAmvqGLVSEWAW---NKDDVILH-TLPLHHVHGIVNkLMCPLWVGATCIML- 279
Cdd:cd05974 84 ADDPMLLYFTSGTTSKPKLVEHTHRSYPV---GHLSTMYWiglKPGDVHWNiSSPGWAKHAWSC-FFAPWNAGATVFLFn 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 280 -PEFSAQKVWEQLISSKspmVNVFMAVPTIYSKLIEyydqhftqpqvQDFIRAvcKERIRLMVSGSAALPQPVLERWAEI 358
Cdd:cd05974 160 yARFDAKRVLAALVRYG---VTTLCAPPTVWRMLIQ-----------QDLASF--DVKLREVVGAGEPLNPEVIEQVRRA 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 359 TGHVLLERYGMTEIGMALSNPLKGSRVPGAVGVPLPGVEVRIMMTnstnaiiaegnskgtrvkAGLEGKEGELLV----- 433
Cdd:cd05974 224 WGLTIRDGYGQTETTALVGNSPGQPVKAGSMGRPLPGYRVALLDP------------------DGAPATEGEVALdlgdt 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 434 RGSSVFQKYWNKPQETADTFtEDGWFKTGDTALYR-DGVYWIMGRTSvDIIKSGGYKISALDVERHLLAHPDITDVAVIG 512
Cdd:cd05974 286 RPVGLMKGYAGDPDKTAHAM-RGGYYRTGDIAMRDeDGYLTYVGRAD-DVFKSSDYRISPFELESVLIEHPAVAEAAVVP 363
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2073725801 513 APDPTWGQKVTAVVQLKKG----KTLTLSQLQaWAREHMAPYTIPTGLILVeEMPRNQMGKVNKKDLLR 577
Cdd:cd05974 364 SPDPVRLSVPKAFIVLRAGyepsPETALEIFR-FSRERLAPYKRIRRLEFA-ELPKTISGKIRRVELRR 430
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
205-578 |
8.28e-29 |
|
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.
Pssm-ID: 341270 [Multi-domain] Cd Length: 608 Bit Score: 121.13 E-value: 8.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 205 AERPAMLIYTSGTTGRPKGVLHTHSSLqaMVQ-GLVSEWAWN-KDDVIL-----------HTlplHHVHGivnklmcPLW 271
Cdd:cd05966 230 SEDPLFILYTSGSTGKPKGVVHTTGGY--LLYaATTFKYVFDyHPDDIYwctadigwitgHS---YIVYG-------PLA 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 272 VGATCIML---PEFSAQKVWEQLISSKSpmVNVFMAVPTIYSKLIEYYDQHftqPQVQDfiravckeRIRLMVSGSAALP 348
Cdd:cd05966 298 NGATTVMFegtPTYPDPGRYWDIVEKHK--VTIFYTAPTAIRALMKFGDEW---VKKHD--------LSSLRVLGSVGEP 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 349 -QPvlERWAEITGHVLLER------YGMTEIGMALSNPLKGSR--VPGAVGVPLPGVEVRIMmtnstnaiiaegNSKGTR 419
Cdd:cd05966 365 iNP--EAWMWYYEVIGKERcpivdtWWQTETGGIMITPLPGATplKPGSATRPFFGIEPAIL------------DEEGNE 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 420 VKAGLEGKegeLLVRGS--SVFQKYWNKPQETADTFTED--GWFKTGDTALY-RDGVYWIMGRTSvDIIKSGGYKISALD 494
Cdd:cd05966 431 VEGEVEGY---LVIKRPwpGMARTIYGDHERYEDTYFSKfpGYYFTGDGARRdEDGYYWITGRVD-DVINVSGHRLGTAE 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 495 VERHLLAHPDITDVAVIGAPDPTWGQKVTAVVQLKKGKTLT--LSQ-LQAWAREHMAPYTIPTGLILVEEMPRNQMGKVN 571
Cdd:cd05966 507 VESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGEEPSdeLRKeLRKHVRKEIGPIATPDKIQFVPGLPKTRSGKIM 586
|
....*..
gi 2073725801 572 KKdLLRK 578
Cdd:cd05966 587 RR-ILRK 592
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
119-577 |
1.60e-28 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 121.99 E-value: 1.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 119 VAQWAAWMCGGIAVPLYRKHPPGELEYVISDSQSSLLvagqpfmdtleplaqkLGLPCLQLPTTSSLDTLQSE-DIRMLP 197
Cdd:PRK12316 3122 VGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLL----------------LSQSHLRLPLAQGVQVLDLDrGDENYA 3185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 198 EQN--ISDWAERPAMLIYTSGTTGRPKGVLHTHSSLQAMVQGLVSEWAWNKDDVILHTLPLhHVHGIVNKLMCPLWVGAT 275
Cdd:PRK12316 3186 EANpaIRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTF-SFDVFVEELFWPLMSGAR 3264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 276 CIMLPEFSAQKVWEQLISSKSPMVNVFMAVPTIYSKLIEyydqhftQPQVQDFIravckeRIRLMVSGSAALPQPVLERW 355
Cdd:PRK12316 3265 VVLAGPEDWRDPALLVELINSEGVDVLHAYPSMLQAFLE-------EEDAHRCT------SLKRIVCGGEALPADLQQQV 3331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 356 aeITGHVLLERYGMTEIGMALSNPLKGSRVPGA--VGVPLPGVEVRIMMTNSTNAIIaegnskgtrvkagleGKEGELLV 433
Cdd:PRK12316 3332 --FAGLPLYNLYGPTEATITVTHWQCVEEGKDAvpIGRPIANRACYILDGSLEPVPV---------------GALGELYL 3394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 434 RGSSVFQKYWNKPQETADTFTEDGW------FKTGDTALYR-DGVYWIMGRTSVDiIKSGGYKISALDVERHLLAHPDIT 506
Cdd:PRK12316 3395 GGEGLARGYHNRPGLTAERFVPDPFvpgerlYRTGDLARYRaDGVIEYIGRVDHQ-VKIRGFRIELGEIEARLLEHPWVR 3473
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2073725801 507 DVAVIGAPdptwGQKVTAVVQLKKGKTLTLSQLQAWAREHMAPYTIPTGLILVEEMPRNQMGKVNKKDLLR 577
Cdd:PRK12316 3474 EAVVLAVD----GRQLVAYVVPEDEAGDLREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPR 3540
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
128-575 |
2.94e-28 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 121.04 E-value: 2.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 128 GGIAVPLYRKHPPGELEYVISDSQSSLLVAGQPFMDTLEPLAQKLGLPCLQlpttSSLDTLQSEDIRMLPEQNISDwaeR 207
Cdd:PRK05691 2262 GGAYVPLDPEYPLERLHYMIEDSGIGLLLSDRALFEALGELPAGVARWCLE----DDAAALAAYSDAPLPFLSLPQ---H 2334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 208 PAMLIYTSGTTGRPKGVLHTHSSLQAMVQGLVSEWAWNKDDVILHTLPLhHVHGIVNKLMCPLWVGATCIMlpefSAQKV 287
Cdd:PRK05691 2335 QAYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIERFGMRADDCELHFYSI-NFDAASERLLVPLLCGARVVL----RAQGQ 2409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 288 WE-----QLISSKSpmVNVFMAVPTIYSKLIEYY-DQHFTQPqvqdfiravckerIRLMVSGSAALPQPVLERW-AEITG 360
Cdd:PRK05691 2410 WGaeeicQLIREQQ--VSILGFTPSYGSQLAQWLaGQGEQLP-------------VRMCITGGEALTGEHLQRIrQAFAP 2474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 361 HVLLERYGMTE-IGMALSNPLKGSRVPGAVGVPLpgvevrimmtnstnaiiaeGNSKGTRVKAGL--------EGKEGEL 431
Cdd:PRK05691 2475 QLFFNAYGPTEtVVMPLACLAPEQLEEGAASVPI-------------------GRVVGARVAYILdadlalvpQGATGEL 2535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 432 LVRGSSVFQKYWNKPQETADTFTEDGW-------FKTGDTALYR-DGVYWIMGRTSVDiIKSGGYKISALDVERHLLAHP 503
Cdd:PRK05691 2536 YVGGAGLAQGYHDRPGLTAERFVADPFaadggrlYRTGDLVRLRaDGLVEYVGRIDHQ-VKIRGFRIELGEIESRLLEHP 2614
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2073725801 504 DITDVAVIGAPDPTWGQ----KVTAVVQLKKGKTLTLSQ-LQAWAREHMAPYTIPTGLILVEEMPRNQMGKVNKKDL 575
Cdd:PRK05691 2615 AVREAVVLALDTPSGKQlagyLVSAVAGQDDEAQAALREaLKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRAL 2691
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
64-575 |
6.89e-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: 116.65 E-value: 6.89e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 64 DNVAITDHSGSHTFCSLYKNSKSLAGLITKAltcqsGDLQGKCISFLCANDASYTVAQWAAWMCGGIAVPLYRKHPPGEL 143
Cdd:cd12115 14 DAIALVCGDESLTYAELNRRANRLAARLRAA-----GVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPERL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 144 EYVISDSQSSLLVAGqpfmdtleplaqklglpclqlpttssldtlqsedirmlpeqnisdwAERPAMLIYTSGTTGRPKG 223
Cdd:cd12115 89 RFILEDAQARLVLTD----------------------------------------------PDDLAYVIYTSGSTGRPKG 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 224 VLHTHSSLQAMVQglvseWAwnkddviLHTLPLHHVHGI-----------VNKLMCPLWVGATCIMlpefsAQKVWEQLI 292
Cdd:cd12115 123 VAIEHRNAAAFLQ-----WA-------AAAFSAEELAGVlastsicfdlsVFELFGPLATGGKVVL-----ADNVLALPD 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 293 SSKSPMVNVFMAVPTIYSKLIEyydqHFTQPQVqdfIRAVCkerirlmVSGSAALPQPVLERWAEITGHVLLERYGMTE- 371
Cdd:cd12115 186 LPAAAEVTLINTVPSAAAELLR----HDALPAS---VRVVN-------LAGEPLPRDLVQRLYARLQVERVVNLYGPSEd 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 372 --IGMALSNPLKGSRVPGaVGVPLPGVEVRIMmtnstnaiiaegNSKGTRVKAGLEGkegELLVRGSSVFQKYWNKPQET 449
Cdd:cd12115 252 ttYSTVAPVPPGASGEVS-IGRPLANTQAYVL------------DRALQPVPLGVPG---ELYIGGAGVARGYLGRPGLT 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 450 ADTFTEDGW------FKTGDTALYR-DGVYWIMGRTSvDIIKSGGYKISALDVERHLLAHPDITDVAVIGAPDPTWGQKV 522
Cdd:cd12115 316 AERFLPDPFgpgarlYRTGDLVRWRpDGLLEFLGRAD-NQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRL 394
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 2073725801 523 TAVVQLKKGKTLTLSQLQAWAREHMAPYTIPTGLILVEEMPRNQMGKVNKKDL 575
Cdd:cd12115 395 VAYIVAEPGAAGLVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
205-579 |
8.12e-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: 118.19 E-value: 8.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 205 AERPAMLIYTSGTTGRPKGVL-----------HTHSSLQAMVQGLV----SEWAWnkddVILHTLPlhhVHGivnklmcP 269
Cdd:cd05967 229 ATDPLYILYTSGTTGKPKGVVrdngghavalnWSMRNIYGIKPGDVwwaaSDVGW----VVGHSYI---VYG-------P 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 270 LWVGATCIML-------PEFSAqkvWEQLISSKSpmVNVFMAVPTIYsKLIEYYDQHftqpqvQDFIRAVCKERIRLMVS 342
Cdd:cd05967 295 LLHGATTVLYegkpvgtPDPGA---FWRVIEKYQ--VNALFTAPTAI-RAIRKEDPD------GKYIKKYDLSSLRTLFL 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 343 GSAALPQPVLErWAE-ITGHVLLERYGMTEIGMALSNPLKG----SRVPGAVGVPLPGVEVRIMmtnstnaiiaegNSKG 417
Cdd:cd05967 363 AGERLDPPTLE-WAEnTLGVPVIDHWWQTETGWPITANPVGleplPIKAGSPGKPVPGYQVQVL------------DEDG 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 418 TRVKAgleGKEGELLVRG---SSVFQKYWNKPQETADTFTED--GWFKTGDTALY-RDGVYWIMGRTSvDIIKSGGYKIS 491
Cdd:cd05967 430 EPVGP---NELGNIVIKLplpPGCLLTLWKNDERFKKLYLSKfpGYYDTGDAGYKdEDGYLFIMGRTD-DVINVAGHRLS 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 492 ALDVERHLLAHPDITDVAVIGAPDPTWGQKVTAVVQLKKGKTLTLSQLQ----AWAREHMAPYTIPTGLILVEEMPRNQM 567
Cdd:cd05967 506 TGEMEESVLSHPAVAECAVVGVRDELKGQVPLGLVVLKEGVKITAEELEkelvALVREQIGPVAAFRLVIFVKRLPKTRS 585
|
410
....*....|..
gi 2073725801 568 GKVNKKdLLRKF 579
Cdd:cd05967 586 GKILRR-TLRKI 596
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
107-575 |
2.11e-27 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 116.28 E-value: 2.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 107 ISFLCANDASYTVAQWAAWMCGGIAVPLYRKHPPGELEYVISDSQSSLLVAGQPFMdtlePLAQKLGLPCLQLPTTSSLD 186
Cdd:PRK13388 55 VGVLLGNTPEMLFWLAAAALGGYVLVGLNTTRRGAALAADIRRADCQLLVTDAEHR----PLLDGLDLPGVRVLDVDTPA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 187 TLQ--SEDIRMLPEQNISdwAERPAMLIYTSGTTGRPKGVLHTHSSLQAMVQGLVSEWAWNKDDVILHTLPLHHVHGIVN 264
Cdd:PRK13388 131 YAElvAAAGALTPHREVD--AMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLTRDDVCYVSMPLFHSNAVMA 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 265 KLMCPLWVGATCIMLPEFSAqkvweqliSSKSPMVNVFMAVPTIY-SKLIEYYdqhFTQPQVQDFIRAvckeriRLMVS- 342
Cdd:PRK13388 209 GWAPAVASGAAVALPAKFSA--------SGFLDDVRRYGATYFNYvGKPLAYI---LATPERPDDADN------PLRVAf 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 343 GSAALPQPVlERWAEITGHVLLERYGMTEIGMALSNPlkGSRVPGAVGVPLPGVEVRIMMTNSTNAIiAEGNSKGTRVKA 422
Cdd:PRK13388 272 GNEASPRDI-AEFSRRFGCQVEDGYGSSEGAVIVVRE--PGTPPGSIGRGAPGVAIYNPETLTECAV-ARFDAHGALLNA 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 423 glEGKEGELLVR-GSSVFQKYWNKPQETADTFtEDGWFKTGDTAlYRDGVYWI--MGRTSvDIIKSGGYKISALDVERHL 499
Cdd:PRK13388 348 --DEAIGELVNTaGAGFFEGYYNNPEATAERM-RHGMYWSGDLA-YRDADGWIyfAGRTA-DWMRVDGENLSAAPIERIL 422
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2073725801 500 LAHPDITDVAVIGAPDPTWGQKVTAVVQLKKGKTLTLSQLQAW--AREHMAPYTIPTGLILVEEMPRNQMGKVNKKDL 575
Cdd:PRK13388 423 LRHPAINRVAVYAVPDERVGDQVMAALVLRDGATFDPDAFAAFlaAQPDLGTKAWPRYVRIAADLPSTATNKVLKREL 500
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
117-497 |
2.25e-27 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 118.35 E-value: 2.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 117 YTVAQWAAWMCGGIAVPLY-----RKHPPGELEYVISDSQSSLLVAGQpfmDTLEPLAQKLGLPCLQLPTTSSLDTLQSE 191
Cdd:PRK05691 77 YVAAFFGCLYAGVIAVPAYppesaRRHHQERLLSIIADAEPRLLLTVA---DLRDSLLQMEELAAANAPELLCVDTLDPA 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 192 DIRMLPEQNISdwAERPAMLIYTSGTTGRPKGVLHTHSSLQAmvqglvSEW--------AWNKDDVILHTLPLHHVHGIV 263
Cdd:PRK05691 154 LAEAWQEPALQ--PDDIAFLQYTSGSTALPKGVQVSHGNLVA------NEQlirhgfgiDLNPDDVIVSWLPLYHDMGLI 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 264 NKLMCPLWVGATCIMLpefsaqkvweqlisskSPmvNVFMAVPTIYSKLIEYYDQhfTQPQVQDFIRAVCKERI------ 337
Cdd:PRK05691 226 GGLLQPIFSGVPCVLM----------------SP--AYFLERPLRWLEAISEYGG--TISGGPDFAYRLCSERVsesale 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 338 -------RLMVSGSAALPQPVLERWAE------ITGHVLLERYGMTEIGMALSNPLKGSRVP------------------ 386
Cdd:PRK05691 286 rldlsrwRVAYSGSEPIRQDSLERFAEkfaacgFDPDSFFASYGLAEATLFVSGGRRGQGIPaleldaealarnraepgt 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 387 GAV----GVPLPGVEVRIMMTNSTNAIIaegnskgtrvkaglEGKEGELLVRGSSVFQKYWNKPQETADTFTE-DG--WF 459
Cdd:PRK05691 366 GSVlmscGRSQPGHAVLIVDPQSLEVLG--------------DNRVGEIWASGPSIAHGYWRNPEASAKTFVEhDGrtWL 431
|
410 420 430
....*....|....*....|....*....|....*...
gi 2073725801 460 KTGDTALYRDGVYWIMGRTSvDIIKSGGYKISALDVER 497
Cdd:PRK05691 432 RTGDLGFLRDGELFVTGRLK-DMLIVRGHNLYPQDIEK 468
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
128-575 |
1.67e-26 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 115.65 E-value: 1.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 128 GGIAVPLYRKHPPGELEYVISDSQSSLLVAGQPFMDtleplaqklGLPCLQLPTTSSLDTLQSEDirmlpeqnisdWAER 207
Cdd:PRK05691 1205 GGAYVPLDPDYPAERLAYMLADSGVELLLTQSHLLE---------RLPQAEGVSAIALDSLHLDS-----------WPSQ 1264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 208 P----------AMLIYTSGTTGRPKGVLHTHSSLQAMVQGLVSEWAWNKDDVILHTLPLHHvhgIVNKLMC--PLWVGAT 275
Cdd:PRK05691 1265 ApglhlhgdnlAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKAPISF---DVSVWECfwPLITGCR 1341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 276 CIML-------PEFSAQKVWEQlisskspmvnvfmAVPTIysklieyydqHFTQPQVQDFIR----AVCKeRIRLMVSGS 344
Cdd:PRK05691 1342 LVLAgpgehrdPQRIAELVQQY-------------GVTTL----------HFVPPLLQLFIDeplaAACT-SLRRLFSGG 1397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 345 AALPQP----VLERWAEITGHvllERYGMTEIGMALSN----PLKGSRVPgaVGVPLPGVEVRIMmtnstnaiiaegNSK 416
Cdd:PRK05691 1398 EALPAElrnrVLQRLPQVQLH---NRYGPTETAINVTHwqcqAEDGERSP--IGRPLGNVLCRVL------------DAE 1460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 417 GTRVKAGLEGkegELLVRGSSVFQKYWNKPQETADTFT-----EDG--WFKTGDTALYR-DGVYWIMGRTSVDIiKSGGY 488
Cdd:PRK05691 1461 LNLLPPGVAG---ELCIGGAGLARGYLGRPALTAERFVpdplgEDGarLYRTGDRARWNaDGALEYLGRLDQQV-KLRGF 1536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 489 KISALDVERHLLAHPDITDVAVIgAPDPTWGQKVTAVVQLKKGKTLTLSQLQAWAREHMAPYTIPTGLILVEEMPRNQMG 568
Cdd:PRK05691 1537 RVEPEEIQARLLAQPGVAQAAVL-VREGAAGAQLVGYYTGEAGQEAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSG 1615
|
....*..
gi 2073725801 569 KVNKKDL 575
Cdd:PRK05691 1616 KLDRRAL 1622
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
64-575 |
3.71e-26 |
|
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: 111.41 E-value: 3.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 64 DNVAITDHSGSHTFCSLYKNSKSLAGLItKALTCQSGDLQGkcisfLCANDASYT-VAQWAAWMCGGIAVPLYRKHPPGE 142
Cdd:cd17650 2 DAIAVSDATRQLTYRELNERANQLARTL-RGLGVAPGSVVG-----VCADRSLDAiVGLLAVLKAGGAYVPIDPDYPAER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 143 LEYVISDSQSSLLVagqpfmdtLEPlaqklglpclqlpttssldtlqsedirmlpeqnisdwaERPAMLIYTSGTTGRPK 222
Cdd:cd17650 76 LQYMLEDSGAKLLL--------TQP--------------------------------------EDLAYVIYTSGTTGKPK 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 223 GVLHTHSSLQAMVQGLVSEWAWNKDDVILHTLPLHHVHGIVNKLMCPLWVGATCIMLPE---FSAQKVWEQLISSKspmV 299
Cdd:cd17650 110 GVMVEHRNVAHAAHAWRREYELDSFPVRLLQMASFSFDVFAGDFARSLLNGGTLVICPDevkLDPAALYDLILKSR---I 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 300 NVFMAVPTIYSKLIEYYDQHFTQPqvqdfiravckERIRLMVSGSAALP-QPVLERWAEITGH-VLLERYGMTEIGMALS 377
Cdd:cd17650 187 TLMESTPALIRPVMAYVYRNGLDL-----------SAMRLLIVGSDGCKaQDFKTLAARFGQGmRIINSYGVTEATIDST 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 378 ------NPLKGSR-VPgaVGVPLPgvevrimmtNSTNAIIAEgnskgtRVKAGLEGKEGELLVRGSSVFQKYWNKPQETA 450
Cdd:cd17650 256 yyeegrDPLGDSAnVP--IGRPLP---------NTAMYVLDE------RLQPQPVGVAGELYIGGAGVARGYLNRPELTA 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 451 DTFTEDGW------FKTGDTALYR-DGVYWIMGRTSvDIIKSGGYKISALDVERHLLAHPDITDVAVIGAPDPtwGQKVT 523
Cdd:cd17650 319 ERFVENPFapgermYRTGDLARWRaDGNVELLGRVD-HQVKIRGFRIELGEIESQLARHPAIDEAVVAVREDK--GGEAR 395
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 2073725801 524 AVVQLKKGKTLTLSQLQAWAREHMAPYTIPTGLILVEEMPRNQMGKVNKKDL 575
Cdd:cd17650 396 LCAYVVAAATLNTAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
119-575 |
1.24e-25 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 112.95 E-value: 1.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 119 VAQWAAWMCGGIAVPLYRKHPPGELEYVISDSQSSLLVagqpfmdTLEPLAQKLGLPCLQLPTTSSLDTLQSEdirmlPE 198
Cdd:PRK12467 3160 VALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLL-------TQAHLLEQLPAPAGDTALTLDRLDLNGY-----SE 3227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 199 QN--ISDWAERPAMLIYTSGTTGRPKGVLHTHSSLQAMVQGLVSEWAWNKDDVILHTLPLhHVHGIVNKLMCPLWVGATC 276
Cdd:PRK12467 3228 NNpsTRVMGENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDRVLLFMSF-SFDGAQERFLWTLICGGCL 3306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 277 IMlpefSAQKVWEqlisskspmvnvfmavPTIYSKLIEYYD---QHFTQPQVQDFI----RAVCKERIRLMVSGSAALPQ 349
Cdd:PRK12467 3307 VV----RDNDLWD----------------PEELWQAIHAHRisiACFPPAYLQQFAedagGADCASLDIYVFGGEAVPPA 3366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 350 PVLERWAEITGHVLLERYGMTEigmALSNPL----KGSRVPGA----VGVPLPGVEVRIMmtnstnaiiaEGNSKGTRVk 421
Cdd:PRK12467 3367 AFEQVKRKLKPRGLTNGYGPTE---AVVTVTlwkcGGDAVCEApyapIGRPVAGRSIYVL----------DGQLNPVPV- 3432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 422 agleGKEGELLVRGSSVFQKYWNKPQETADTFTEDGW-------FKTGDTALYR-DGVYWIMGRtsVD-IIKSGGYKISA 492
Cdd:PRK12467 3433 ----GVAGELYIGGVGLARGYHQRPSLTAERFVADPFsgsggrlYRTGDLARYRaDGVIEYLGR--IDhQVKIRGFRIEL 3506
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 493 LDVERHLLAHPDITDVAVIgAPDPTWGQKVTAVVQLKKGKTLTLSQLQAWAREHMAPYTIPTGLILVEEMPRNQMGKVNK 572
Cdd:PRK12467 3507 GEIEARLLQHPSVREAVVL-ARDGAGGKQLVAYVVPADPQGDWRETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDR 3585
|
...
gi 2073725801 573 KDL 575
Cdd:PRK12467 3586 KAL 3588
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
206-575 |
2.11e-25 |
|
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: 109.44 E-value: 2.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 206 ERPAMLIYTSGTTGRPKGVLHTHSSLQAMVQgLVSEWAWNKD-DVILHTLPLHHVHGIVNKLMCPLWVGATCIMLPEFSA 284
Cdd:cd05937 87 DDPAILIYTSGTTGLPKAAAISWRRTLVTSN-LLSHDLNLKNgDRTYTCMPLYHGTAAFLGACNCLMSGGTLALSRKFSA 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 285 QKVWEQLISSKSPMV-------NVFMAVPtiysklIEYYDQhftqpqvqdfiravcKERIRlMVSGSAALPQpVLERWAE 357
Cdd:cd05937 166 SQFWKDVRDSGATIIqyvgelcRYLLSTP------PSPYDR---------------DHKVR-VAWGNGLRPD-IWERFRE 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 358 ITG-HVLLERYGMTEIGMALSNPLKGSRVPGAVG-------VPLPGVEVRIMMTNSTNAIIAEgNSKGTRVKAGLeGKEG 429
Cdd:cd05937 223 RFNvPEIGEFYAATEGVFALTNHNVGDFGAGAIGhhglirrWKFENQVVLVKMDPETDDPIRD-PKTGFCVRAPV-GEPG 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 430 ELLVR----GSSVFQKYWNKPQETA-----DTFTE-DGWFKTGDtALYRD--GVYWIMGRTSvDIIKSGGYKISALDVER 497
Cdd:cd05937 301 EMLGRvpfkNREAFQGYLHNEDATEsklvrDVFRKgDIYFRTGD-LLRQDadGRWYFLDRLG-DTFRWKSENVSTTEVAD 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 498 HLLAHPDITDVAVIGAPDPTW-GQKVTAVVQLKKGKT----LTLSQLQAWAREHMAPYTIPTGLILVEEMPRNQMGKVNK 572
Cdd:cd05937 379 VLGAHPDIAEANVYGVKVPGHdGRAGCAAITLEESSAvpteFTKSLLASLARKNLPSYAVPLFLRLTEEVATTDNHKQQK 458
|
...
gi 2073725801 573 KDL 575
Cdd:cd05937 459 GVL 461
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
123-575 |
3.11e-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: 3.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 123 AAWMCGGIAVPLYRKHPPGELEYVISDSQSSLLVAgQPfmdtleplaqklglpclqlpttssldtlqsedirmlpeqnis 202
Cdd:cd17644 69 AILKAGGAYVPLDPNYPQERLTYILEDAQISVLLT-QP------------------------------------------ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 203 dwaERPAMLIYTSGTTGRPKGVLHTHSSLQAMVQGLVSEWAWNKDDVILHTLPLHhVHGIVNKLMCPLWVGATCIMLPEf 282
Cdd:cd17644 106 ---ENLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEYGITSSDRVLQFASIA-FDVAAEEIYVTLLSGATLVLRPE- 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 283 saqkvweQLISSKSPMVNVfmavptIYSKLIEYYDqhFTQPQVQDFIRAVCKERI------RLMVSGSAALPQPVLERWA 356
Cdd:cd17644 181 -------EMRSSLEDFVQY------IQQWQLTVLS--LPPAYWHLLVLELLLSTIdlpsslRLVIVGGEAVQPELVRQWQ 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 357 EITGHV--LLERYGMTEIGMA-----LSNPLKGSRVPGAVGVPLPGVEVRIMMTNSTNAIIaegnskgtrvkagleGKEG 429
Cdd:cd17644 246 KNVGNFiqLINVYGPTEATIAatvcrLTQLTERNITSVPIGRPIANTQVYILDENLQPVPV---------------GVPG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 430 ELLVRGSSVFQKYWNKPQETADTFTEDGW--------FKTGDTALY-RDGVYWIMGRTSvDIIKSGGYKISALDVERHLL 500
Cdd:cd17644 311 ELHIGGVGLARGYLNRPELTAEKFISHPFnsseserlYKTGDLARYlPDGNIEYLGRID-NQVKIRGFRIELGEIEAVLS 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2073725801 501 AHPDITDVAVIGAPDPTWGQKVTAVVQLKKGKTLTLSQLQAWAREHMAPYTIPTGLILVEEMPRNQMGKVNKKDL 575
Cdd:cd17644 390 QHNDVKTAVVIVREDQPGNKRLVAYIVPHYEESPSTVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
166-548 |
4.07e-25 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 108.42 E-value: 4.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 166 EPLAQKLgLPCLQL---------PTTSSLDTLQsedIRMLPEQNISDW-AERPAMLIYTSGTTGRPKGVLHTHSSLQAMV 235
Cdd:PRK09029 89 QPLLEEL-LPSLTLdfalvlegeNTFSALTSLH---LQLVEGAHAVAWqPQRLATMTLTSGSTGLPKAAVHTAQAHLASA 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 236 QGLVSEWAWNKDDVILHTLPLHHV--HGIVnklmcplW----VGATcIMLPEfsAQKVWEQLIsskspmvNVFMA--VPT 307
Cdd:PRK09029 165 EGVLSLMPFTAQDSWLLSLPLFHVsgQGIV-------WrwlyAGAT-LVVRD--KQPLEQALA-------GCTHAslVPT 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 308 IYSKLIEYYDQHFTqpqvqdfIRAVckerirLMvsGSAALPQPVLERwAEITGHVLLERYGMTEigMAlsnplkgSRV-- 385
Cdd:PRK09029 228 QLWRLLDNRSEPLS-------LKAV------LL--GGAAIPVELTEQ-AEQQGIRCWCGYGLTE--MA-------STVca 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 386 ------PGaVGVPLPGVEVRImmtnstnaiiaegnskgtrvkaglegKEGELLVRGSSVFQKYW--NKPQETADtftEDG 457
Cdd:PRK09029 283 kradglAG-VGSPLPGREVKL--------------------------VDGEIWLRGASLALGYWrqGQLVPLVN---DEG 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 458 WFKTGDTALYRDGVYWIMGRTSVDIIkSGGYKISALDVERHLLAHPDITDVAVIGAPDPTWGQKVTAVVQLKKGKTLTls 537
Cdd:PRK09029 333 WFATRDRGEWQNGELTILGRLDNLFF-SGGEGIQPEEIERVINQHPLVQQVFVVPVADAEFGQRPVAVVESDSEAAVV-- 409
|
410
....*....|.
gi 2073725801 538 QLQAWAREHMA 548
Cdd:PRK09029 410 NLAEWLQDKLA 420
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
208-563 |
4.71e-25 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 109.22 E-value: 4.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 208 PAMLIYTSGTTGRPKGVLHTHSSLQAMVQGLVSEWAWNKDDVILHTLPLHHVHGIVnklmcplwVGATCImLPEFSA--- 284
Cdd:PRK09274 176 MAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEIDLPTFPLFALFGPA--------LGMTSV-IPDMDPtrp 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 285 -----QKVWEQL----ISskspmvNVFMAvPTIYSKLIEYYDQH-FTQPQVqdfiravckeriRLMVSGSAALPQPVLER 354
Cdd:PRK09274 247 atvdpAKLFAAIerygVT------NLFGS-PALLERLGRYGEANgIKLPSL------------RRVISAGAPVPIAVIER 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 355 WAEITGHV--LLERYGMTE------IGMalSNPLKGSRV---PGA---VGVPLPGVEVRIMmtNSTNAIIAEgnSKGTRV 420
Cdd:PRK09274 308 FRAMLPPDaeILTPYGATEalpissIES--REILFATRAatdNGAgicVGRPVDGVEVRII--AISDAPIPE--WDDALR 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 421 KAglEGKEGELLVRGSSVFQKYWNKPQETADTFTEDG----WFKTGDTAlYRD--GVYWIMGRTSVDIIKSGG--YKIsa 492
Cdd:PRK09274 382 LA--TGEIGEIVVAGPMVTRSYYNRPEATRLAKIPDGqgdvWHRMGDLG-YLDaqGRLWFCGRKAHRVETAGGtlYTI-- 456
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2073725801 493 lDVERHLLAHPDITDVAVIGAPDPTwGQKVTAVVQLKKGKTLTLSQLQAWAREHMA--PYTIPTGLILV-EEMP 563
Cdd:PRK09274 457 -PCERIFNTHPGVKRSALVGVGVPG-AQRPVLCVELEPGVACSKSALYQELRALAAahPHTAGIERFLIhPSFP 528
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
64-575 |
5.57e-25 |
|
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341311 [Multi-domain] Cd Length: 479 Bit Score: 108.33 E-value: 5.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 64 DNVAITDHSGSHTFCSLYKNSKSLAglitKALTCQsGDLQGKCISFLCANDASYTVAQWAAWMCGGIAVPLYRKHPPGEL 143
Cdd:cd17656 3 DAVAVVFENQKLTYRELNERSNQLA----RFLREK-GVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 144 EYVISDSQSSLLVAGQPFMDtlePLAQKLGLPCLQLPTTSSLDTlqsEDIrmlpeqNISDWAERPAMLIYTSGTTGRPKG 223
Cdd:cd17656 78 IYIMLDSGVRVVLTQRHLKS---KLSFNKSTILLEDPSISQEDT---SNI------DYINNSDDLLYIIYTSGTTGKPKG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 224 VLHTHSSLQAMVQGLVSEWAWNK-DDVILHTLPLHHV--HGIVNKLMcplwVGATCIMLPEfSAQKVWEQLIS--SKSPM 298
Cdd:cd17656 146 VQLEHKNMVNLLHFEREKTNINFsDKVLQFATCSFDVcyQEIFSTLL----SGGTLYIIRE-ETKRDVEQLFDlvKRHNI 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 299 VNVFMavPTIYSKLIEYYDQHFtqpqvQDFIRAVcKERI----RLMVSgsaalpQPVLERWAEITGHvLLERYGMTE--- 371
Cdd:cd17656 221 EVVFL--PVAFLKFIFSEREFI-----NRFPTCV-KHIItageQLVIT------NEFKEMLHEHNVH-LHNHYGPSEthv 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 372 IGMALSNPlkGSRVP--GAVGVPLPGVEVRIMmtnstnaiiaegNSKGTRVKAGLEGkegELLVRGSSVFQKYWNKPQET 449
Cdd:cd17656 286 VTTYTINP--EAEIPelPPIGKPISNTWIYIL------------DQEQQLQPQGIVG---ELYISGASVARGYLNRQELT 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 450 ADTFTEDGW------FKTGDTALY-RDGVYWIMGRTSvDIIKSGGYKISALDVERHLLAHPDITDVAVIGAPDPTWGQKV 522
Cdd:cd17656 349 AEKFFPDPFdpnermYRTGDLARYlPDGNIEFLGRAD-HQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYL 427
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 2073725801 523 TA-VVQLKkgkTLTLSQLQAWAREHMAPYTIPTGLILVEEMPRNQMGKVNKKDL 575
Cdd:cd17656 428 CAyFVMEQ---ELNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
209-469 |
6.44e-25 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 109.37 E-value: 6.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 209 AMLIYTSGTTGRPKGVLHTHSSL---QAMVQGLVSEWAWNKDDVILHTLPLHHVHG---IVNKLmcpLWVGATCIM---- 278
Cdd:PRK12582 223 AKYLFTSGSTGMPKAVINTQRMMcanIAMQEQLRPREPDPPPPVSLDWMPWNHTMGgnaNFNGL---LWGGGTLYIddgk 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 279 -LPEFSAQKVweQLISSKSPMVnvFMAVPTIYSKLIEYYDQhftqpqvQDFIRAVCKERIRLMVSGSAALPQPVLERWAE 357
Cdd:PRK12582 300 pLPGMFEETI--RNLREISPTV--YGNVPAGYAMLAEAMEK-------DDALRRSFFKNLRLMAYGGATLSDDLYERMQA 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 358 ----ITGH--VLLERYGMTEIGMALSNPLKGSRVPGAVGVPLPGVEVRIMMTnstnaiiaegnskgtrvkagleGKEGEL 431
Cdd:PRK12582 369 lavrTTGHriPFYTGYGATETAPTTTGTHWDTERVGLIGLPLPGVELKLAPV----------------------GDKYEV 426
|
250 260 270
....*....|....*....|....*....|....*...
gi 2073725801 432 LVRGSSVFQKYWNKPQETADTFTEDGWFKTGDTALYRD 469
Cdd:PRK12582 427 RVKGPNVTPGYHKDPELTAAAFDEEGFYRLGDAARFVD 464
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
103-470 |
8.95e-25 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 109.03 E-value: 8.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 103 QGKCISFLCANDASYTVAQWAAWMCGGIAVPLYRKHPPGELEYVISDSQ-SSLLVAGQPFMDTLEPLAQklgLPCLQL-- 179
Cdd:PLN02736 102 KGACVGLYFINRPEWLIVDHACSAYSYVSVPLYDTLGPDAVKFIVNHAEvAAIFCVPQTLNTLLSCLSE---IPSVRLiv 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 180 ------------PTTSSLDTLQSEdiRMLPEQNISDWAERP------AMLIYTSGTTGRPKGVLHTHSSLQAMVQGLVSE 241
Cdd:PLN02736 179 vvggadeplpslPSGTGVEIVTYS--KLLAQGRSSPQPFRPpkpedvATICYTSGTTGTPKGVVLTHGNLIANVAGSSLS 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 242 WAWNKDDVILHTLPLHHVHGIVNKLMCpLWVGATcIMLPEFSAQKVWEQLISSKSpmvNVFMAVPTIYSKLieyYDQHFT 321
Cdd:PLN02736 257 TKFYPSDVHISYLPLAHIYERVNQIVM-LHYGVA-VGFYQGDNLKLMDDLAALRP---TIFCSVPRLYNRI---YDGITN 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 322 QPQ----------------------------------VQDFIRAVCKERIRLMVSGSAALPQPVLERWAEITGHVLLERY 367
Cdd:PLN02736 329 AVKesgglkerlfnaaynakkqalengknpspmwdrlVFNKIKAKLGGRVRFMSSGASPLSPDVMEFLRICFGGRVLEGY 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 368 GMTEIGMALSNPLKGSRVPGAVGVPLPGVEVRIM----MtNSTNAiiaegNSKGTRvkaglegkeGELLVRGSSVFQKYW 443
Cdd:PLN02736 409 GMTETSCVISGMDEGDNLSGHVGSPNPACEVKLVdvpeM-NYTSE-----DQPYPR---------GEICVRGPIIFKGYY 473
|
410 420
....*....|....*....|....*..
gi 2073725801 444 NKPQETADTFTEDGWFKTGDTALYRDG 470
Cdd:PLN02736 474 KDEVQTREVIDEDGWLHTGDIGLWLPG 500
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
205-575 |
1.18e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 106.66 E-value: 1.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 205 AERPAMLIYTSGTTGRPKGVLHTHSSLQAMVQGLVSEWAWNKDDVILHTLPLHHVHGIVNKLMCPLWVGATCIML----P 280
Cdd:PRK08308 100 AEEPSLLQYSSGTTGEPKLIRRSWTEIDREIEAYNEALNCEQDETPIVACPVTHSYGLICGVLAALTRGSKPVIItnknP 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 281 EFSAQKVweqlissKSPMVNVFMAVPTIYSKLIEyydqhFTQPQVQDFiravckeriRLMVSGsAALPQPVLERWAEITG 360
Cdd:PRK08308 180 KFALNIL-------RNTPQHILYAVPLMLHILGR-----LLPGTFQFH---------AVMTSG-TPLPEAWFYKLRERTT 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 361 HvLLERYGMTEIG-MALSNPLkgsRVPGAVGVPLPGVevrimmtnstnaiiaegnskgtRVKAGL-EGKEGELLVrgssv 438
Cdd:PRK08308 238 Y-MMQQYGCSEAGcVSICPDM---KSHLDLGNPLPHV----------------------SVSAGSdENAPEEIVV----- 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 439 fqkyWNKPQETadtFTEDGWFKTGDTALYrdgvywIMGRTSvDIIKSGGYKISALDVERHLLAHPDITDVAVIGAPDPTW 518
Cdd:PRK08308 287 ----KMGDKEI---FTKDLGYKSERGTLH------FMGRMD-DVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVA 352
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 2073725801 519 GQKVTAVVQLKKgkTLTLSQLQAWAREHMAPYTIPTGLILVEEMPRNQMGKVNKKDL 575
Cdd:PRK08308 353 GERVKAKVISHE--EIDPVQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLL 407
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
208-469 |
2.18e-24 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 107.66 E-value: 2.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 208 PAMLIYTSGTTGRPKGVLHTHSSLQAMVQGLVSEWAWNKDD--VILHTLPLHHVHGIVNKLMCPLWVGATCIM-----LP 280
Cdd:PRK08180 211 IAKFLFTSGSTGLPKAVINTHRMLCANQQMLAQTFPFLAEEppVLVDWLPWNHTFGGNHNLGIVLYNGGTLYIddgkpTP 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 281 EFSAQKVweQLISSKSPmvNVFMAVPTIYSKLIEYYDQhftqpqvQDFIRAVCKERIRLMVSGSAALPQPVLERWAEITG 360
Cdd:PRK08180 291 GGFDETL--RNLREISP--TVYFNVPKGWEMLVPALER-------DAALRRRFFSRLKLLFYAGAALSQDVWDRLDRVAE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 361 HVLLER------YGMTEIG-MALSNPLKGSRvPGAVGVPLPGVEVRImmtnstnaiiaegnskgtrVKAGleGKEgELLV 433
Cdd:PRK08180 360 ATCGERirmmtgLGMTETApSATFTTGPLSR-AGNIGLPAPGCEVKL-------------------VPVG--GKL-EVRV 416
|
250 260 270
....*....|....*....|....*....|....*.
gi 2073725801 434 RGSSVFQKYWNKPQETADTFTEDGWFKTGDTALYRD 469
Cdd:PRK08180 417 KGPNVTPGYWRAPELTAEAFDEEGYYRSGDAVRFVD 452
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
205-578 |
2.94e-24 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 107.15 E-value: 2.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 205 AERPAMLIYTSGTTGRPKGVLHThsSLQAMVQGLVS-EWAWN-KDDVIL-----------HTlplHHVHGivnklmcPLW 271
Cdd:PRK00174 244 AEDPLFILYTSGSTGKPKGVLHT--TGGYLVYAAMTmKYVFDyKDGDVYwctadvgwvtgHS---YIVYG-------PLA 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 272 VGATCIML---PEFSAQKVWEQLISSKSpmVNVFMAVPTIYSKLIEYYDQHftqpqVQDFIRAvckeRIRLMvsGSAALP 348
Cdd:PRK00174 312 NGATTLMFegvPNYPDPGRFWEVIDKHK--VTIFYTAPTAIRALMKEGDEH-----PKKYDLS----SLRLL--GSVGEP 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 349 -QPVLERWA-EITGHvllER------YGMTEIGMALSNPLKGSR--VPGAVGVPLPGVEVRIMmtnstnaiiaegNSKGT 418
Cdd:PRK00174 379 iNPEAWEWYyKVVGG---ERcpivdtWWQTETGGIMITPLPGATplKPGSATRPLPGIQPAVV------------DEEGN 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 419 RVKAGlegKEGELLVRGS--SVFQKYWNKPQETADTF--TEDGWFKTGDTALY-RDGVYWIMGRTSvDIIKSGGYKISAL 493
Cdd:PRK00174 444 PLEGG---EGGNLVIKDPwpGMMRTIYGDHERFVKTYfsTFKGMYFTGDGARRdEDGYYWITGRVD-DVLNVSGHRLGTA 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 494 DVERHLLAHPDITDVAVIGAPDPTWGQKVTAVVQLKKGKTLT---LSQLQAWAREHMAPYTIPTGLILVEEMPRNQMGKV 570
Cdd:PRK00174 520 EIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLKGGEEPSdelRKELRNWVRKEIGPIAKPDVIQFAPGLPKTRSGKI 599
|
....*...
gi 2073725801 571 NKKdLLRK 578
Cdd:PRK00174 600 MRR-ILRK 606
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
58-580 |
3.75e-23 |
|
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341242 [Multi-domain] Cd Length: 481 Bit Score: 103.01 E-value: 3.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 58 RASVYGDNVAITDHSGSHTFCSLYKNSKSLAGLItkaltCQSGDLQGKCISfLCANDASYT-VAQWAAWMCGGIAVPLYR 136
Cdd:cd05918 8 RARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHL-----RSLGVGPGVFVP-LCFEKSKWAvVAMLAVLKAGGAFVPLDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 137 KHPPGELEYVISDSQSSLLVAGQPfmdtleplaqklglpclqlpttssldtlqsedirmlpeqnisdwaERPAMLIYTSG 216
Cdd:cd05918 82 SHPLQRLQEILQDTGAKVVLTSSP---------------------------------------------SDAAYVIFTSG 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 217 TTGRPKGVLHTHSSLQAMVQGLVSEWAWNKDDVIL----HTLPLHhvhgiVNKLMCPLWVGAT-CIM--------LPEFs 283
Cdd:cd05918 117 STGKPKGVVIEHRALSTSALAHGRALGLTSESRVLqfasYTFDVS-----ILEIFTTLAAGGClCIPseedrlndLAGF- 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 284 aqkvweqlISSKspMVNVFMAVPTIySKLIeyydqhftQPQVqdfiravcKERIRLMVSGSAALPQPVLERWAEitgHV- 362
Cdd:cd05918 191 --------INRL--RVTWAFLTPSV-ARLL--------DPED--------VPSLRTLVLGGEALTQSDVDTWAD---RVr 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 363 LLERYGMTE--IGMALSNPLKGSRvPGAVGVPLPGVevrimmtnstnAIIAEGNSKGTRVKAGLEGkegELLVRGSSVFQ 440
Cdd:cd05918 241 LINAYGPAEctIAATVSPVVPSTD-PRNIGRPLGAT-----------CWVVDPDNHDRLVPIGAVG---ELLIEGPILAR 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 441 KYWNKPQETADTFTED-GW------------FKTGDTALYR-DGVYWIMGRTSvDIIKSGGYKISALDVERHLLAH-PDI 505
Cdd:cd05918 306 GYLNDPEKTAAAFIEDpAWlkqegsgrgrrlYRTGDLVRYNpDGSLEYVGRKD-TQVKIRGQRVELGEIEHHLRQSlPGA 384
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 506 TDVAV--IGAPDPTWGQKVTAVVQLKKGKT-----------------LTLSQLQAWAREHMAPYTIPTGLILVEEMPRNQ 566
Cdd:cd05918 385 KEVVVevVKPKDGSSSPQLVAFVVLDGSSSgsgdgdslflepsdefrALVAELRSKLRQRLPSYMVPSVFLPLSHLPLTA 464
|
570
....*....|....
gi 2073725801 567 MGKVNKKdLLRKFF 580
Cdd:cd05918 465 SGKIDRR-ALRELA 477
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
205-557 |
1.05e-22 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 101.38 E-value: 1.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 205 AERPAMLIYTSGTTGRPKGVLHTHSSLQAMVQGLVSEWAWNKDDVILHTLPLhhvHGIVNKLMcplwvGATCI---MLPE 281
Cdd:cd05910 84 ADEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGEVDLATFPL---FALFGPAL-----GLTSVipdMDPT 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 282 FSAQKVWEQLISS-KSPMVNVFMAVPTIYSKLIEYYDQH-FTQPQVQDFIRAVCKERIRLMVSGSAALPQPvlerwAEIt 359
Cdd:cd05910 156 RPARADPQKLVGAiRQYGVSIVFGSPALLERVARYCAQHgITLPSLRRVLSAGAPVPIALAARLRKMLSDE-----AEI- 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 360 ghvlLERYGMTE---IGMALSNPLKGSRVPGA-------VGVPLPGVEVRIMmtnstnAIIAEGNSKGTRVKAGLEGKEG 429
Cdd:cd05910 230 ----LTPYGATEalpVSSIGSRELLATTTAATsggagtcVGRPIPGVRVRII------EIDDEPIAEWDDTLELPRGEIG 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 430 ELLVRGSSVFQKYWNKPQETADTFTEDG----WFKTGDTALYRD-GVYWIMGRTSVDIIKSGGyKISALDVERHLLAHPD 504
Cdd:cd05910 300 EITVTGPTVTPTYVNRPVATALAKIDDNsegfWHRMGDLGYLDDeGRLWFCGRKAHRVITTGG-TLYTEPVERVFNTHPG 378
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 2073725801 505 ITDVAVIGAPDPTwGQKVTAVVQLKKGKTLTLSQ----LQAWAREHMAPYTIPTGLI 557
Cdd:cd05910 379 VRRSALVGVGKPG-CQLPVLCVEPLPGTITPRARleqeLRALAKDYPHTQRIGRFLI 434
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
128-570 |
1.44e-22 |
|
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: 101.80 E-value: 1.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 128 GGIAVPLYRKHPPGELEYVISDSQSSLLVAGQPFM--DTLEPLAQKLGLPCLQLPTTSSL---------DTLQSEDIRML 196
Cdd:cd05968 140 GGIVVPIFSGFGKEAAATRLQDAEAKALITADGFTrrGREVNLKEEADKACAQCPTVEKVvvvrhlgndFTPAKGRDLSY 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 197 PEQNIS--DWAER-----PAMLIYTSGTTGRPKGVLHTHSS--LQA---------MVQGLVSEW----AWnkddvilhtl 254
Cdd:cd05968 220 DEEKETagDGAERtesedPLMIIYTSGTTGKPKGTVHVHAGfpLKAaqdmyfqfdLKPGDLLTWftdlGW---------- 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 255 plhhvhgivnkLMCP------LWVGATCIM---LPEF-SAQKVWEQLISSKSPMVNVfmaVPTIYSKLIeyydqhftqPQ 324
Cdd:cd05968 290 -----------MMGPwlifggLILGATMVLydgAPDHpKADRLWRMVEDHEITHLGL---SPTLIRALK---------PR 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 325 VQDFIRAVCKERIRLMVS-GSAALPQPvlerWAEITGHVLLER-----Y-GMTEI-----GMALSNPLKgsrvPGAVGVP 392
Cdd:cd05968 347 GDAPVNAHDLSSLRVLGStGEPWNPEP----WNWLFETVGKGRnpiinYsGGTEIsggilGNVLIKPIK----PSSFNGP 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 393 LPGVEVRIMmtnstnaiiaegNSKGTRVKagleGKEGELLVRGS--SVFQKYWNKPQETADTFTE--DGWFKTGDTALY- 467
Cdd:cd05968 419 VPGMKADVL------------DESGKPAR----PEVGELVLLAPwpGMTRGFWRDEDRYLETYWSrfDNVWVHGDFAYYd 482
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 468 RDGVYWIMGRtSVDIIKSGGYKISALDVERHLLAHPDITDVAVIGAPDPTWGQKVTAVVQLKKGKTLT---LSQLQAWAR 544
Cdd:cd05968 483 EEGYFYILGR-SDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVLKPGVTPTealAEELMERVA 561
|
490 500
....*....|....*....|....*.
gi 2073725801 545 EHMAPYTIPTGLILVEEMPRNQMGKV 570
Cdd:cd05968 562 DELGKPLSPERILFVKDLPKTRNAKV 587
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
123-575 |
2.36e-22 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 102.04 E-value: 2.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 123 AAWMcggiavPLYRKHPPGELEYVISDSQSSLLVAGQPFMDTLePLAQKLGLPCLQLPTTSSldtlqseDIRMLPEQNIS 202
Cdd:PRK10252 533 AAWL------PLDTGYPDDRLKMMLEDARPSLLITTADQLPRF-ADVPDLTSLCYNAPLAPQ-------GAAPLQLSQPH 598
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 203 DwaerPAMLIYTSGTTGRPKGVLHTHsslQAMVQGLVseWAWNK-----DDVILHTLPL-HHVHgiVNKLMCPLWVGATC 276
Cdd:PRK10252 599 H----TAYIIFTSGSTGRPKGVMVGQ---TAIVNRLL--WMQNHypltaDDVVLQKTPCsFDVS--VWEFFWPFIAGAKL 667
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 277 IML-PEFSAQKVW-EQLISSKSPMVNVFmaVPTIYSKLIeyydqhfTQPQVQDFIRAVCKERiRLMVSGSaALPQPVLER 354
Cdd:PRK10252 668 VMAePEAHRDPLAmQQFFAEYGVTTTHF--VPSMLAAFV-------ASLTPEGARQSCASLR-QVFCSGE-ALPADLCRE 736
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 355 WAEITGHVLLERYGMTEI----------GMALSNpLKGSRVPgaVGVPLPGVEVRIMmtnstnaiiaegNSKGTRVKAGL 424
Cdd:PRK10252 737 WQQLTGAPLHNLYGPTEAavdvswypafGEELAA-VRGSSVP--IGYPVWNTGLRIL------------DARMRPVPPGV 801
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 425 egkEGELLVRGSSVFQKYWNKPQETADTFTEDGW------FKTGDTALYR-DGVYWIMGRtSVDIIKSGGYKISALDVER 497
Cdd:PRK10252 802 ---AGDLYLTGIQLAQGYLGRPDLTASRFIADPFapgermYRTGDVARWLdDGAVEYLGR-SDDQLKIRGQRIELGEIDR 877
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 498 HLLAHPDITDVA----VIGAPDPTWG---QKVTAVVQlKKGKTLTLSQLQAWAREHMAPYTIPTGLILVEEMPRNQMGKV 570
Cdd:PRK10252 878 AMQALPDVEQAVthacVINQAAATGGdarQLVGYLVS-QSGLPLDTSALQAQLRERLPPHMVPVVLLQLDQLPLSANGKL 956
|
....*
gi 2073725801 571 NKKDL 575
Cdd:PRK10252 957 DRKAL 961
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
195-563 |
3.71e-22 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 100.94 E-value: 3.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 195 MLPEQnisdwAERPAMLIYTSGTTGRPKGVLHTHSSLQAMVQGLVSEWAWNKDDVILHTLPLHHVHGIVNKLMCPLWVGA 274
Cdd:PRK08043 359 QVKQQ-----PEDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPNDRFMSALPLFHSFGLTVGLFTPLLTGA 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 275 TCIMLPEFSAQKVWEQLISSKSPMVnVFMAvptiySKLIEYYDQhFTQPqvQDFiravckERIRLMVSGSAALPQPVLER 354
Cdd:PRK08043 434 EVFLYPSPLHYRIVPELVYDRNCTV-LFGT-----STFLGNYAR-FANP--YDF------ARLRYVVAGAEKLQESTKQL 498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 355 WAEITGHVLLERYGMTEIGMALSNPLKGSRVPGAVGVPLPGVEVRIMMTNStnaiIAEGnskgtrvkaglegkeGELLVR 434
Cdd:PRK08043 499 WQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLSVPG----IEQG---------------GRLQLK 559
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 435 GSSVFQKY--------WNKPQ-ETADTFTEDGWFKTGD-TALYRDGVYWIMGRTSvDIIKSGGYKISALDVER-HLLAHP 503
Cdd:PRK08043 560 GPNIMNGYlrvekpgvLEVPTaENARGEMERGWYDTGDiVRFDEQGFVQIQGRAK-RFAKIAGEMVSLEMVEQlALGVSP 638
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2073725801 504 DITDVAVIgAPDPTWGQkvtAVVQLKKGKTLTLSQLQAWAREHMAP-YTIPTGLILVEEMP 563
Cdd:PRK08043 639 DKQHATAI-KSDASKGE---ALVLFTTDSELTREKLQQYAREHGVPeLAVPRDIRYLKQLP 695
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
113-512 |
4.61e-22 |
|
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341256 [Multi-domain] Cd Length: 596 Bit Score: 100.12 E-value: 4.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 113 NDASYTVAQWAAWMCGGIAVPLYRKHPPGELEYVISDSQSSLLVagqpfMDTLEPLaQKLGLPCLQLPTTSSLDTLQsED 192
Cdd:cd05933 42 NSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSEANILV-----VENQKQL-QKILQIQDKLPHLKAIIQYK-EP 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 193 IRMLpEQNISDWAE--------------------RP---AMLIYTSGTTGRPKGVLHTHSSL----QAMVQGLVSEWAWN 245
Cdd:cd05933 115 LKEK-EPNLYSWDEfmelgrsipdeqldaiissqKPnqcCTLIYTSGTTGMPKGVMLSHDNItwtaKAASQHMDLRPATV 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 246 KDDVILHTLPLHHVHGIVNKLMCPLWVGAtCIMLPEFSAQKvWEQLISSKSPMVNVFMAVPTIYSKLIEYYDQHFTQPQv 325
Cdd:cd05933 194 GQESVVSYLPLSHIAAQILDIWLPIKVGG-QVYFAQPDALK-GTLVKTLREVRPTAFMGVPRVWEKIQEKMKAVGAKSG- 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 326 qdFIR---------AVCKERIRLMVSGSaalPQPVLERWAE-------------------ITGHV--------------- 362
Cdd:cd05933 271 --TLKrkiaswakgVGLETNLKLMGGES---PSPLFYRLAKklvfkkvrkalgldrcqkfFTGAApisretlefflslni 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 363 -LLERYGMTEIGMA--LSNPlkGSRVPGAVGVPLPGVEVRIMMTNstnaiiAEGNskgtrvkaglegkeGELLVRGSSVF 439
Cdd:cd05933 346 pIMELYGMSETSGPhtISNP--QAYRLLSCGKALPGCKTKIHNPD------ADGI--------------GEICFWGRHVF 403
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2073725801 440 QKYWNKPQETADTFTEDGWFKTGDTA-LYRDGVYWIMGRTSVDIIKSGGYKISALDVERHLLAH-PDITDVAVIG 512
Cdd:cd05933 404 MGYLNMEDKTEEAIDEDGWLHSGDLGkLDEDGFLYITGRIKELIITAGGENVPPVPIEDAVKKElPIISNAMLIG 478
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
209-469 |
6.04e-22 |
|
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: 99.81 E-value: 6.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 209 AMLIYTSGTTGRPKGVLHTHSSLQAMVQGLVSEWAWNKDD--VILHTLPLHHVHGIVNKLMCPLWVGATC-IMLPEFSAQ 285
Cdd:cd05921 168 AKFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFFGEEppVLVDWLPWNHTFGGNHNFNLVLYNGGTLyIDDGKPMPG 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 286 KVWEQLISSKSPMVNVFMAVPTIYSKLIEYYDQhftqpqvQDFIRAVCKERIRLMVSGSAALPQPVLERWAEI----TGH 361
Cdd:cd05921 248 GFEETLRNLREISPTVYFNVPAGWEMLVAALEK-------DEALRRRFFKRLKLMFYAGAGLSQDVWDRLQALavatVGE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 362 --VLLERYGMTEIGMALSNPLKGSRVPGAVGVPLPGVEVRImmtnstnaiiaegnskgtrVKAGleGKEgELLVRGSSVF 439
Cdd:cd05921 321 riPMMAGLGATETAPTATFTHWPTERSGLIGLPAPGTELKL-------------------VPSG--GKY-EVRVKGPNVT 378
|
250 260 270
....*....|....*....|....*....|
gi 2073725801 440 QKYWNKPQETADTFTEDGWFKTGDTALYRD 469
Cdd:cd05921 379 PGYWRQPELTAQAFDEEGFYCLGDAAKLAD 408
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
124-512 |
1.40e-21 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 99.15 E-value: 1.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 124 AWMCGGIA-VPLYRKHPPGELEYVISDSQSSL----------LVAGQP--------------FMDTLEPLAQKLGLPCLQ 178
Cdd:PLN02861 121 ACNSQGITyVPLYDTLGANAVEFIINHAEVSIafvqeskissILSCLPkcssnlktivsfgdVSSEQKEEAEELGVSCFS 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 179 LPTTSSLDTLQSEdirmLPEQNISDWAerpaMLIYTSGTTGRPKGVLHTHSSLQAMVQG-----LVSEWAWNKDDVILHT 253
Cdd:PLN02861 201 WEEFSLMGSLDCE----LPPKQKTDIC----TIMYTSGTTGEPKGVILTNRAIIAEVLStdhllKVTDRVATEEDSYFSY 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 254 LPLHHVHGIVNKLMC-------PLWVGATCIMLPEFSAQKvweqlissksPmvNVFMAVPTIY----------------- 309
Cdd:PLN02861 273 LPLAHVYDQVIETYCiskgasiGFWQGDIRYLMEDVQALK----------P--TIFCGVPRVYdriytgimqkissggml 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 310 -SKLIEY------------YDQHFTQPQVQDFIRAVCKE----RIRLMVSGSAALPQPVLERWAEITGHVLLERYGMTE- 371
Cdd:PLN02861 341 rKKLFDFaynyklgnlrkgLKQEEASPRLDRLVFDKIKEglggRVRLLLSGAAPLPRHVEEFLRVTSCSVLSQGYGLTEs 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 372 IGMALSNPLKGSRVPGAVGVPLPGVEVRImmtNSTNAIIAEGNSKGTRvkaglegkeGELLVRGSSVFQKYWNKPQETAD 451
Cdd:PLN02861 421 CGGCFTSIANVFSMVGTVGVPMTTIEARL---ESVPEMGYDALSDVPR---------GEICLRGNTLFSGYHKRQDLTEE 488
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2073725801 452 TFTeDGWFKTGDTALYR-DGVYWIMGRTSvDIIK-SGGYKISALDVERHLLAHPDITDVAVIG 512
Cdd:PLN02861 489 VLI-DGWFHTGDIGEWQpNGAMKIIDRKK-NIFKlSQGEYVAVENLENTYSRCPLIASIWVYG 549
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
208-580 |
4.99e-20 |
|
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: 93.19 E-value: 4.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 208 PAMLIYTSGTTGRPKGVLHTHSSLQAMVqGLVSEWAWNKD-DVILHTLPLHHVHGIVNKLMCPLWVGATCIMLPEFSAQK 286
Cdd:cd05940 83 AALYIYTSGTTGLPKAAIISHRRAWRGG-AFFAGSGGALPsDVLYTCLPLYHSTALIVGWSACLASGATLVIRKKFSASN 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 287 VWEQLISSKSPMvnvfmaVPTIySKLIEYYdqhFTQPQVQDfiraVCKERIRlMVSGSAALPqpvlERWAEIT-----GH 361
Cdd:cd05940 162 FWDDIRKYQATI------FQYI-GELCRYL---LNQPPKPT----ERKHKVR-MIFGNGLRP----DIWEEFKerfgvPR 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 362 VlLERYGMTEIGMALSNPlkgSRVPGAVgvplpGVEVRIMMTNSTNAIIAEGNSKGT--RVKAGL-----EGKEGELLVR 434
Cdd:cd05940 223 I-AEFYAATEGNSGFINF---FGKPGAI-----GRNPSLLRKVAPLALVKYDLESGEpiRDAEGRcikvpRGEPGLLISR 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 435 GSSV--FQKYWNKPQETA----DTFTE-DGWFKTGD-TALYRDGVYWIMGRTSvDIIKSGGYKISALDVERHLLAHPDIT 506
Cdd:cd05940 294 INPLepFDGYTDPAATEKkilrDVFKKgDAWFNTGDlMRLDGEGFWYFVDRLG-DTFRWKGENVSTTEVAAVLGAFPGVE 372
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2073725801 507 DVAVIGAPDP-TWGQKVTAVVQLKKGKTLTLSQLQAWAREHMAPYTIPTGLILVEEMPRNQMGKVNKKDLLRKFF 580
Cdd:cd05940 373 EANVYGVQVPgTDGRAGMAAIVLQPNEEFDLSALAAHLEKNLPGYARPLFLRLQPEMEITGTFKQQKVDLRNEGF 447
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
64-575 |
6.28e-20 |
|
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: 92.62 E-value: 6.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 64 DNVAITDHSGSHTFCSLYKNSKSLAGLitkaltcqsgdLQGKCIS------FLCANDASYTVAQWAAWMCGGIAVPLYRK 137
Cdd:cd17645 13 DHVAVVDRGQSLTYKQLNEKANQLARH-----------LRGKGVKpddqvgIMLDKSLDMIAAILGVLKAGGAYVPIDPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 138 HPPGELEYVISDSQSSLLVAgqpfmdtleplaqklglpclqlpttssldtlQSEDIrmlpeqnisdwaerpAMLIYTSGT 217
Cdd:cd17645 82 YPGERIAYMLADSSAKILLT-------------------------------NPDDL---------------AYVIYTSGS 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 218 TGRPKGVLHTHsslqamvQGLVSEWAWNKDDVILHTLPLHHVH------GIVNKLMCPLWVGATCIMLPEFSAQKVweql 291
Cdd:cd17645 116 TGLPKGVMIEH-------HNLVNLCEWHRPYFGVTPADKSLVYasfsfdASAWEIFPHLTAGAALHVVPSERRLDL---- 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 292 isskspmvnvfmavptiySKLIEYYDQH-----FTQPQVQDFIRAVCKERIRLMVSGSAALPQpvlerwAEITGHVLLER 366
Cdd:cd17645 185 ------------------DALNDYFNQEgitisFLPTGAAEQFMQLDNQSLRVLLTGGDKLKK------IERKGYKLVNN 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 367 YGMTEIG-MALSNPLKGSRVPGAVGVPLPgvEVRIMMTNSTNAIIAEGNSkgtrvkaglegkeGELLVRGSSVFQKYWNK 445
Cdd:cd17645 241 YGPTENTvVATSFEIDKPYANIPIGKPID--NTRVYILDEALQLQPIGVA-------------GELCIAGEGLARGYLNR 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 446 PQETADTFTEDGW------FKTGDTALY-RDGVYWIMGRTSvDIIKSGGYKISALDVERHLLAHPDITDVAVIGAPDPTW 518
Cdd:cd17645 306 PELTAEKFIVHPFvpgermYRTGDLAKFlPDGNIEFLGRLD-QQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADG 384
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 2073725801 519 GQKVTAVVQLKKgkTLTLSQLQAWAREHMAPYTIPTGLILVEEMPRNQMGKVNKKDL 575
Cdd:cd17645 385 RKYLVAYVTAPE--EIPHEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
205-571 |
7.46e-20 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 94.26 E-value: 7.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 205 AERPAMLIYTSGTTGRPKGVLHTHSSLQAMVQGLVSEWAWNKDDVILHTLPLHHVHGIVNKLMCPLWVGATCIMLPefsa 284
Cdd:PRK06814 792 PDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARIDFSPEDKVFNALPVFHSFGLTGGLVLPLLSGVKVFLYP---- 867
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 285 qkvweqlisskSPMVnvFMAVP--------TI----------YSKLIEYYDQHftqpqvqdfiravckeRIRLMVSGSAA 346
Cdd:PRK06814 868 -----------SPLH--YRIIPeliydtnaTIlfgtdtflngYARYAHPYDFR----------------SLRYVFAGAEK 918
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 347 LPQPVLERWAEITGHVLLERYGMTEIG--MALSNPLKGSrvPGAVGVPLPGVEVRIMMTnstnaiiaEGNSKGtrvkagl 424
Cdd:PRK06814 919 VKEETRQTWMEKFGIRILEGYGVTETApvIALNTPMHNK--AGTVGRLLPGIEYRLEPV--------PGIDEG------- 981
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 425 egkeGELLVRGSSVFQKYW--NKP---QEtadtfTEDGWFKTGD-TALYRDGVYWIMGRTSvDIIKSGGYKISALDVERh 498
Cdd:PRK06814 982 ----GRLFVRGPNVMLGYLraENPgvlEP-----PADGWYDTGDiVTIDEEGFITIKGRAK-RFAKIAGEMISLAAVEE- 1050
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2073725801 499 lLAH---PDiTDVAVIGAPDPTWGQKvtaVVQLKKGKTLTLSQLQAWAREHMAP-YTIPTGLILVEEMPRNQMGKVN 571
Cdd:PRK06814 1051 -LAAelwPD-ALHAAVSIPDARKGER---IILLTTASDATRAAFLAHAKAAGASeLMVPAEIITIDEIPLLGTGKID 1122
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
425-584 |
9.33e-20 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 92.75 E-value: 9.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 425 EGKEGELLVRGSSVFQKYWNKPQETADTFTEDGWFKTGDTALYR-DGVYWIMGRTSvDIIKSGGYKISALDVERHLLAHP 503
Cdd:PRK10946 377 QGEVGRLMTRGPYTFRGYYKSPQHNASAFDANGFYCSGDLVSIDpDGYITVVGREK-DQINRGGEKIAAEEIENLLLRHP 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 504 DITDVAVIGAPDPTWGQKVTAVVQLKKGktLTLSQLQAWAREH-MAPYTIPTGLILVEEMPRNQMGKVNKKdLLRKFFPT 582
Cdd:PRK10946 456 AVIHAALVSMEDELMGEKSCAFLVVKEP--LKAVQLRRFLREQgIAEFKLPDRVECVDSLPLTAVGKVDKK-QLRQWLAS 532
|
..
gi 2073725801 583 RS 584
Cdd:PRK10946 533 RA 534
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
205-497 |
1.00e-19 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 92.55 E-value: 1.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 205 AERPAMLIYTSGTTGRPKGVLHTHSSLQAMVQGLVSEWAWNKDDVILHTLPLHHVHGIVNKLMCPLWVGATCIMLPefsa 284
Cdd:cd05908 105 ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGMNQYLMP---- 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 285 qkvweqlisskspmVNVFMAVPTIYSKLIEYYD------QHFTQPQVQDFIRAVCKE-----RIRLMVSGSaalpQPVL- 352
Cdd:cd05908 181 --------------TRLFIRRPILWLKKASEHKativssPNFGYKYFLKTLKPEKANdwdlsSIRMILNGA----EPIDy 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 353 ERWAEITGHV---------LLERYGMTEIGMALSNP----------------LKGSRVPG------------AVGVPLPG 395
Cdd:cd05908 243 ELCHEFLDHMskyglkrnaILPVYGLAEASVGASLPkaqspfktitlgrrhvTHGEPEPEvdkkdsecltfvEVGKPIDE 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 396 VEVRImmTNSTNAIIAEGNSkgtrvkaglegkeGELLVRGSSVFQKYWNKPQETADTFTEDGWFKTGDTALYRDGVYWIM 475
Cdd:cd05908 323 TDIRI--CDEDNKILPDGYI-------------GHIQIRGKNVTPGYYNNPEATAKVFTDDGWLKTGDLGFIRNGRLVIT 387
|
330 340
....*....|....*....|..
gi 2073725801 476 GRTSvDIIKSGGYKISALDVER 497
Cdd:cd05908 388 GREK-DIIFVNGQNVYPHDIER 408
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
200-477 |
1.86e-19 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 92.35 E-value: 1.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 200 NISDWAERPAMLIYTSGTTGRPKGVLHTHSSLQAMVQGLvSEW------AWNKDDVILHTLPLHHV--HGIVNKLM---C 268
Cdd:PTZ00216 258 NIPENNDDLALIMYTSGTTGDPKGVMHTHGSLTAGILAL-EDRlndligPPEEDETYCSYLPLAHImeFGVTNIFLargA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 269 PLWVGATCIMLPEFSaqKVWEQLISSKsPMvnVFMAVPTIY--------SKL----------------------IEYYDQ 318
Cdd:PTZ00216 337 LIGFGSPRTLTDTFA--RPHGDLTEFR-PV--FLIGVPRIFdtikkaveAKLppvgslkrrvfdhayqsrlralKEGKDT 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 319 HFTQPQVQDFIRAVCKERIRLMVSGSAALPQPVLErWAEITGHVLLERYGMTEIGMALSNPLKGSRVPGAVGVPLPGVEV 398
Cdd:PTZ00216 412 PYWNEKVFSAPRAVLGGRVRAMLSGGGPLSAATQE-FVNVVFGMVIQGWGLTETVCCGGIQRTGDLEPNAVGQLLKGVEM 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 399 RIMMTNstnaiiaegnskgtrvkaglEGK-------EGELLVRGSSVFQKYWNKPQETADTFTEDGWFKTGDTA-LYRDG 470
Cdd:PTZ00216 491 KLLDTE--------------------EYKhtdtpepRGEILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGsIAANG 550
|
....*..
gi 2073725801 471 VYWIMGR 477
Cdd:PTZ00216 551 TLRIIGR 557
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
208-578 |
4.73e-19 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.
Pssm-ID: 213283 [Multi-domain] Cd Length: 509 Bit Score: 90.57 E-value: 4.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 208 PAMLIYTSGTTGRPKGVLHTH--SSLQAMVQGLVSEWAWNKDDVILHTLPLHHVHGivnklMCPLWV----GATCIMLPE 281
Cdd:cd05915 155 ACGMAYTTGTTGLPKGVVYSHraLVLHSLAASLVDGTALSEKDVVLPVVPMFHVNA-----WCLPYAatlvGAKQVLPGP 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 282 FSAQKV-WEQLISSKspmVNVFMAVPTIYSKLieyydqhftqPQVQDFIRAVCKERIRLMVSGSAalPQPVLERWAEITG 360
Cdd:cd05915 230 RLDPASlVELFDGEG---VTFTAGVPTVWLAL----------ADYLESTGHRLKTLRRLVVGGSA--APRSLIARFERMG 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 361 HVLLERYGMTEI---GMALSNPLKGSRVPGAVGVPLPG-------VEVRIMMTNSTNAIIAEGnsKGTRVKAglegkege 430
Cdd:cd05915 295 VEVRQGYGLTETspvVVQNFVKSHLESLSEEEKLTLKAktglpipLVRLRVADEEGRPVPKDG--KALGEVQ-------- 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 431 llVRGSSVFQKYWNKPQETADTFTEDGWFKTGDTALYRDGVYWIMGRTSVDIIKSGGYKISALDVERHLLAHPDITDVAV 510
Cdd:cd05915 365 --LKGPWITGGYYGNEEATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAV 442
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2073725801 511 IGAPDPTWGQKVTAVVQLKKGKTLTLSQLQAWAREHMAPYTIPTGLILVEEMPRNQMGKVnKKDLLRK 578
Cdd:cd05915 443 VAIPHPKWQERPLAVVVPRGEKPTPEELNEHLLKAGFAKWQLPDAYVFAEEIPRTSAGKF-LKRALRE 509
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
205-578 |
5.00e-19 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 91.11 E-value: 5.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 205 AERPAMLIYTSGTTGRPKGVLHTHSSLqaMVQGLVS---EWAWNKDDVILHTLPLHHVHGIVNKLMCPLWVGATCIML-- 279
Cdd:PLN02654 274 AEDPLFLLYTSGSTGKPKGVLHTTGGY--MVYTATTfkyAFDYKPTDVYWCTADCGWITGHSYVTYGPMLNGATVLVFeg 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 280 -PEF-SAQKVWEQLISSKspmVNVFMAVPTIYSKLIEYYDQHFTQpqvqdfiravcKERIRLMVSGSAALP-QPVLERW- 355
Cdd:PLN02654 352 aPNYpDSGRCWDIVDKYK---VTIFYTAPTLVRSLMRDGDEYVTR-----------HSRKSLRVLGSVGEPiNPSAWRWf 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 356 AEITGHV---LLERYGMTEIGMALSNPLKGS--RVPGAVGVPLPGVEVRIMmtnstnaiiaegNSKGTRvkagLEGK-EG 429
Cdd:PLN02654 418 FNVVGDSrcpISDTWWQTETGGFMITPLPGAwpQKPGSATFPFFGVQPVIV------------DEKGKE----IEGEcSG 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 430 ELLVRGS--SVFQKYWNKPQETADTFTE--DGWFKTGD-TALYRDGVYWIMGRTSvDIIKSGGYKISALDVERHLLAHPD 504
Cdd:PLN02654 482 YLCVKKSwpGAFRTLYGDHERYETTYFKpfAGYYFSGDgCSRDKDGYYWLTGRVD-DVINVSGHRIGTAEVESALVSHPQ 560
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 505 ITDVAVIGAPDPTWGQKVTAVVQLKKG--------KTLTL---SQLQAWA---REHMAPytiptGLilveemPRNQMGKV 570
Cdd:PLN02654 561 CAEAAVVGIEHEVKGQGIYAFVTLVEGvpyseelrKSLILtvrNQIGAFAapdKIHWAP-----GL------PKTRSGKI 629
|
....*...
gi 2073725801 571 NKKdLLRK 578
Cdd:PLN02654 630 MRR-ILRK 636
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
205-562 |
7.17e-19 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 90.32 E-value: 7.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 205 AERPAMLIYTSGTTGRPKGVLHTHSSLQAMVQGLVSEWAWNKDDVILHTLPLHHVHGIVNKLMCPLWVGATCIMLPEFSA 284
Cdd:PRK08279 198 AKDTAFYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLTPDDVLYCCLPLYHNTGGTVAWSSVLAAGATLALRRKFSA 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 285 QKVWEQLISSKspmVNVFMAVPTIYSKLIEyydqhftQPqVQDFIRAvckERIRLMVsGSAALPQpVLERWAEITG--HV 362
Cdd:PRK08279 278 SRFWDDVRRYR---ATAFQYIGELCRYLLN-------QP-PKPTDRD---HRLRLMI-GNGLRPD-IWDEFQQRFGipRI 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 363 lLERYGMTEIGMALSNPLKgsrVPGAVG-VPLPGVE-VRIM-MTNSTNAIIAEGNSKGTRVKAGlegkE-GELL--VRGS 436
Cdd:PRK08279 342 -LEFYAASEGNVGFINVFN---FDGTVGrVPLWLAHpYAIVkYDVDTGEPVRDADGRCIKVKPG----EvGLLIgrITDR 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 437 SVFQKYwNKPQETA-----DTFTE-DGWFKTGDtaLYRD---GVYWImgrtsVDII------KsgGYKISALDVERHLLA 501
Cdd:PRK08279 414 GPFDGY-TDPEASEkkilrDVFKKgDAWFNTGD--LMRDdgfGHAQF-----VDRLgdtfrwK--GENVATTEVENALSG 483
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2073725801 502 HPDITDVAVIGAPDP-TWGQKVTAVVQLKKGKTLTLSQLQAWAREHMAPYTIPTGLILVEEM 562
Cdd:PRK08279 484 FPGVEEAVVYGVEVPgTDGRAGMAAIVLADGAEFDLAALAAHLYERLPAYAVPLFVRLVPEL 545
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
113-563 |
8.71e-19 |
|
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: 89.82 E-value: 8.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 113 NDASYTVAQWAAWMCGGIAVPLYRKHPPGELEYVISDSQSSLLVAGqpfMDTLePLAQKLGLPCLQLP------------ 180
Cdd:cd17632 102 TSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLAVS---AEHL-DLAVEAVLEGGTPPrlvvfdhrpevd 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 181 --------------------TTSSLDTLQSEDIRMLPEQNISDWAERPAMLIYTSGTTGRPKGVLHTHSSLQAMVQGLVS 240
Cdd:cd17632 178 ahraalesarerlaavgipvTTLTLIAVRGRDLPPAPLFRPEPDDDPLALLIYTSGSTGTPKGAMYTERLVATFWLKVSS 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 241 EWAWNKDDVI-LHTLPLHHVHGiVNKLMCPLWVGATCIMLPEFSAQKVWEQLiSSKSPmVNVFMaVPTIYSKLIEYY--- 316
Cdd:cd17632 258 IQDIRPPASItLNFMPMSHIAG-RISLYGTLARGGTAYFAAASDMSTLFDDL-ALVRP-TELFL-VPRVCDMLFQRYqae 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 317 ---------DQHFTQPQVQDFIRA-VCKERIRLMVSGSAALpQPVLERWAEITGHV-LLERYGMTEIGMALsnpLKG--S 383
Cdd:cd17632 334 ldrrsvagaDAETLAERVKAELRErVLGGRLLAAVCGSAPL-SAEMKAFMESLLDLdLHDGYGSTEAGAVI---LDGviV 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 384 RVP----GAVGVPlpgvEVRIMMTNSTNAiiaegnskgtrvkaglegkEGELLVRGSSVFQKYWNKPQETADTFTEDGWF 459
Cdd:cd17632 410 RPPvldyKLVDVP----ELGYFRTDRPHP-------------------RGELLVKTDTLFPGYYKRPEVTAEVFDEDGFY 466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 460 KTGDtalyrdgvywIMGRTSVD----------IIK-SGGYKISALDVERHLLAHPDITDVAVIGAPD---------PTwg 519
Cdd:cd17632 467 RTGD----------VMAELGPDrlvyvdrrnnVLKlSQGEFVTVARLEAVFAASPLVRQIFVYGNSErayllavvvPT-- 534
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 2073725801 520 QKVTAVVQLKKGKTLTLSQLQAWAREH-MAPYTIPTGLIlVEEMP 563
Cdd:cd17632 535 QDALAGEDTARLRAALAESLQRIAREAgLQSYEIPRDFL-IETEP 578
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
118-497 |
1.98e-18 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 88.51 E-value: 1.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 118 TVAQwAAWMCGGIAVPLYRKHPPGEL-------EYVISDSQSSLLVAGQPFMDTLEPLAQKlGLPCLQLPttsslDTLQS 190
Cdd:PRK07768 69 PTAQ-GLWMRGASLTMLHQPTPRTDLavwaedtLRVIGMIGAKAVVVGEPFLAAAPVLEEK-GIRVLTVA-----DLLAA 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 191 EDIRMlPEQNISDwaerPAMLIYTSGTTGRPKGVLHTHSSLQAMVQGLVSEWAWNKD-DVILHTLPLHHVHGIVNKLMCP 269
Cdd:PRK07768 142 DPIDP-VETGEDD----LALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEFDVEtDVMVSWLPLFHDMGMVGFLTVP 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 270 LWVGATCImlpefsaqKVweqlisskSPMvnVFMAVPTIYSKLIEYYdqHFTQPQVQDFIRAVCKER------------- 336
Cdd:PRK07768 217 MYFGAELV--------KV--------TPM--DFLRDPLLWAELISKY--RGTMTAAPNFAYALLARRlrrqakpgafdls 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 337 -IRLMVSGSAALPQPVLERWAEITG------HVLLERYGMTEIGMALS-----NPLK------------GSRVPGAVGV- 391
Cdd:PRK07768 277 sLRFALNGAEPIDPADVEDLLDAGArfglrpEAILPAYGMAEATLAVSfspcgAGLVvdevdadllaalRRAVPATKGNt 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 392 --------PLPGVEVRImmtnstnaIIAEGNSKGTRvkaglegKEGELLVRGSSVFQKYwnkpqETADTFT----EDGWF 459
Cdd:PRK07768 357 rrlatlgpPLPGLEVRV--------VDEDGQVLPPR-------GVGVIELRGESVTPGY-----LTMDGFIpaqdADGWL 416
|
410 420 430
....*....|....*....|....*....|....*....
gi 2073725801 460 KTGDTA-LYRDGVYWIMGRTSvDIIKSGGYKISALDVER 497
Cdd:PRK07768 417 DTGDLGyLTEEGEVVVCGRVK-DVIIMAGRNIYPTDIER 454
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
121-579 |
5.65e-18 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 87.56 E-value: 5.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 121 QWAAWM--CGG---IAVPLYRKHPPGELEYVISDSQSSLL-VAGQPFMDTLEP---LAQKL-GLPCLQLPTTSSLDtlQS 190
Cdd:PLN02430 113 QWIVAMeaCAAhslICVPLYDTLGPGAVDYIVDHAEIDFVfVQDKKIKELLEPdckSAKRLkAIVSFTSVTEEESD--KA 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 191 EDIRMLP---EQNISDWAERPA-----------MLIYTSGTTGRPKGVLHTHSSLQAMVQG--LVSEWAWNK---DDVIL 251
Cdd:PLN02430 191 SQIGVKTyswIDFLHMGKENPSetnppkpldicTIMYTSGTSGDPKGVVLTHEAVATFVRGvdLFMEQFEDKmthDDVYL 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 252 HTLPLHHV-------------------HGIVNKLMCPLW-VGATCIMLPEFSAQKVWEQL---ISSKSPMVNVfmavptI 308
Cdd:PLN02430 271 SFLPLAHIldrmieeyffrkgasvgyyHGDLNALRDDLMeLKPTLLAGVPRVFERIHEGIqkaLQELNPRRRL------I 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 309 YSKLIEY--------YDQHFTQPqVQDF-----IRAVCKERIRLMVSGSAALPQPVLERWAEITGHVLLERYGMTEI--G 373
Cdd:PLN02430 345 FNALYKYklawmnrgYSHKKASP-MADFlafrkVKAKLGGRLRLLISGGAPLSTEIEEFLRVTSCAFVVQGYGLTETlgP 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 374 MALSNPLKGSRVpGAVGVPLPGVEVRIMMTNSTnaiiaEGNSKGtrvkaglEGKEGELLVRGSSVFQKYWNKPQETADTF 453
Cdd:PLN02430 424 TTLGFPDEMCML-GTVGAPAVYNELRLEEVPEM-----GYDPLG-------EPPRGEICVRGKCLFSGYYKNPELTEEVM 490
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 454 tEDGWFKTGDTA-LYRDGVYWIMGRTSvDIIK-SGGYKISALDVERHLLAHPDITDVAVIGapdPTWGQKVTAVVQLKKG 531
Cdd:PLN02430 491 -KDGWFHTGDIGeILPNGVLKIIDRKK-NLIKlSQGEYVALEYLENVYGQNPIVEDIWVYG---DSFKSMLVAVVVPNEE 565
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 2073725801 532 KTltlsqlQAWARE--HMAPYTIPTGLILVEEMPRNQMGKVNKKDLLRKF 579
Cdd:PLN02430 566 NT------NKWAKDngFTGSFEELCSLPELKEHILSELKSTAEKNKLRGF 609
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
212-576 |
1.11e-17 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 86.10 E-value: 1.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 212 IYTSGTTGRPKGVLHTHSSLQAMVQGLVSEWAWNKDDVILHTLP-------------------LHHV-HGIVNKL----- 266
Cdd:PRK04813 149 IFTSGTTGKPKGVQISHDNLVSFTNWMLEDFALPEGPQFLNQAPysfdlsvmdlyptlasggtLVALpKDMTANFkqlfe 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 267 MCP-----LWVgAT------CIMLPEFSAQKVweqlissksPMVNVFMavptiysklieyydqhftqpqvqdFiravCKE 335
Cdd:PRK04813 229 TLPqlpinVWV-STpsfadmCLLDPSFNEEHL---------PNLTHFL------------------------F----CGE 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 336 rirlmvsgsaALPQPVLERwaeitghvLLER---------YGMTEIGMALSNPL-------KGSRVPgaVGVPLPGVEVR 399
Cdd:PRK04813 271 ----------ELPHKTAKK--------LLERfpsatiyntYGPTEATVAVTSIEitdemldQYKRLP--IGYAKPDSPLL 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 400 IMMtnstnaiiaegnSKGTRVKaglEGKEGELLVRGSSVFQKYWNKPQETADTF-TEDGW--FKTGDTALYRDGVYWIMG 476
Cdd:PRK04813 331 IID------------EEGTKLP---DGEQGEIVISGPSVSKGYLNNPEKTAEAFfTFDGQpaYHTGDAGYLEDGLLFYQG 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 477 RtsVDI-IKSGGYKISALDVERHLLAHPDITDVAVIgapdPTWGQ-KVT---AVVQLKKGK-----TLTlSQLQAWAREH 546
Cdd:PRK04813 396 R--IDFqIKLNGYRIELEEIEQNLRQSSYVESAVVV----PYNKDhKVQyliAYVVPKEEDferefELT-KAIKKELKER 468
|
410 420 430
....*....|....*....|....*....|
gi 2073725801 547 MAPYTIPTGLILVEEMPRNQMGKVNKKDLL 576
Cdd:PRK04813 469 LMEYMIPRKFIYRDSLPLTPNGKIDRKALI 498
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
494-569 |
1.51e-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: 77.20 E-value: 1.51e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2073725801 494 DVERHLLAHPDITDVAVIGAPDPTWGQKVTAVVQLKKGKTLTLSQLQAWAREHMAPYTIPTGLILVEEMPRNQMGK 569
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
64-575 |
1.33e-16 |
|
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: 82.45 E-value: 1.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 64 DNVAITDHSGSHTFCSLYKNSKSLAGLITKALTCQSGDLQGkciSFLcanDAS--YTVAQWAAWMCGGIAVPLYRKHPPG 141
Cdd:cd17648 2 DRVAVVYGDKRLTYRELNERANRLAHYLLSVAEIRPDDLVG---LVL---DKSelMIIAILAVWKAGAAYVPIDPSYPDE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 142 ELEYVISDSQSSLLVAgqpfmdtleplaqklglpclqlpttssldtlqsedirmlpeqNISDWAerpaMLIYTSGTTGRP 221
Cdd:cd17648 76 RIQFILEDTGARVVIT------------------------------------------NSTDLA----YAIYTSGTTGKP 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 222 KGVLHTHSSLQAMVQGLVSEW--AWNKDDVIL---HTLPLHHVHGIVNKLMCplwvGATCIMLPEfSAQKVWEQLIssks 296
Cdd:cd17648 110 KGVLVEHGSVVNLRTSLSERYfgRDNGDEAVLffsNYVFDFFVEQMTLALLN----GQKLVVPPD-EMRFDPDRFY---- 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 297 pmvnvfmavPTIYSKLIEYYdqHFTQPQVQDFIRAVCKERIRLMVSGSAaLPQPVLERWAEITGHVLLERYGMTEIGM-A 375
Cdd:cd17648 181 ---------AYINREKVTYL--SGTPSVLQQYDLARLPHLKRVDAAGEE-FTAPVFEKLRSRFAGLIINAYGPTETTVtN 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 376 LSNPLKG-SRVPGAVGVPLPGVEVRIMmtnstnaiiaegNSKGTRVKAGlegKEGELLVRGSSVFQKYWNKPQETADTFT 454
Cdd:cd17648 249 HKRFFPGdQRFDKSLGRPVRNTKCYVL------------NDAMKRVPVG---AVGELYLGGDGVARGYLNRPELTAERFL 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 455 EDGW--------------FKTGDTALYR-DGVYWIMGRTSVDiIKSGGYKISALDVERHLLAHPDITDVAVIGAPDPTW- 518
Cdd:cd17648 314 PNPFqteqerargrnarlYKTGDLVRWLpSGELEYLGRNDFQ-VKIRGQRIEPGEVEAALASYPGVRECAVVAKEDASQa 392
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 519 ---GQKVTAVVQLKKGKTLTLSQLQAWAREHMAPYTIPTGLILVEEMPRNQMGKVNKKDL 575
Cdd:cd17648 393 qsrIQKYLVGYYLPEPGHVPESDLLSFLRAKLPRYMVPARLVRLEGIPVTINGKLDVRAL 452
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
81-562 |
2.58e-16 |
|
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: 81.95 E-value: 2.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 81 YKNSKSLAGLITKALTCQSGDLQGKCISFLCANDASYtVAQWAAWMCGGIAVPLYRKH-PPGELEYVISDSQSSLLVAGQ 159
Cdd:cd05938 8 YRDVDRRSNQAARALLAHAGLRPGDTVALLLGNEPAF-LWIWLGLAKLGCPVAFLNTNiRSKSLLHCFRCCGAKVLVVAP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 160 PFMDTLE---PLAQKLGLPCLQLPTTSS-------LDTLQSEDIRMLP-----EQNISDwaerPAMLIYTSGTTGRPKGV 224
Cdd:cd05938 87 ELQEAVEevlPALRADGVSVWYLSHTSNtegvislLDKVDAASDEPVPaslraHVTIKS----PALYIYTSGTTGLPKAA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 225 LHTHSSLQAMvQGLVSEWAWNKDDVILHTLPLHHVHGIVNKLMCPLWVGATCIMLPEFSAQKVWEQlisSKSPMVNVFMA 304
Cdd:cd05938 163 RISHLRVLQC-SGFLSLCGVTADDVIYITLPLYHSSGFLLGIGGCIELGATCVLKPKFSASQFWDD---CRKHNVTVIQY 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 305 VPTIYSKLIEyydqhfTQPQVQDfiravCKERIRLMVsGSAALPQpVLERWAEITGHV-LLERYGMTEIGMALSNPlkgS 383
Cdd:cd05938 239 IGELLRYLCN------QPQSPND-----RDHKVRLAI-GNGLRAD-VWREFLRRFGPIrIREFYGSTEGNIGFFNY---T 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 384 RVPGAVG---------VPLPGVEVRIMmtnsTNAIIAEGNSKGTRVKAGLEGkegeLLV---RGSSVFQKYWNKPQET-- 449
Cdd:cd05938 303 GKIGAVGrvsylykllFPFELIKFDVE----KEEPVRDAQGFCIPVAKGEPG----LLVakiTQQSPFLGYAGDKEQTek 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 450 ---ADTF-TEDGWFKTGDT-ALYRDGVYWIMGRTSvDIIKSGGYKISALDVERHLLAHPDITDVAVIGAPDPTWGQKV-T 523
Cdd:cd05938 375 kllRDVFkKGDVYFNTGDLlVQDQQNFLYFHDRVG-DTFRWKGENVATTEVADVLGLLDFLQEVNVYGVTVPGHEGRIgM 453
|
490 500 510
....*....|....*....|....*....|....*....
gi 2073725801 524 AVVQLKKGKTLTLSQLQAWAREHMAPYTIPTGLILVEEM 562
Cdd:cd05938 454 AAVKLKPGHEFDGKKLYQHVREYLPAYARPRFLRIQDSL 492
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
113-527 |
4.28e-15 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 78.12 E-value: 4.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 113 NDASYTVAQWAAWMCGGIAVPLYRKHPPGELE-YV------ISDSQSSLLVAGQPFMDTLEPLAQKLGLPCLQLPTtsSL 185
Cdd:PRK09192 83 TDGDFVEAFFACQYAGLVPVPLPLPMGFGGREsYIaqlrgmLASAQPAAIITPDELLPWVNEATHGNPLLHVLSHA--WF 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 186 DTLQSEDIRmLPEQNISDwaerPAMLIYTSGTTGRPKGVLHTHSSLQAMVQGLVSEWAWNKD-DVILHTLPLHHVHGIVN 264
Cdd:PRK09192 161 KALPEADVA-LPRPTPDD----IAYLQYSSGSTRFPRGVIITHRALMANLRAISHDGLKVRPgDRCVSWLPFYHDMGLVG 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 265 KLMCPLWVGATCIMLP--EFSAQK-VWEQLIS------SKSPMVNVFMAVPTIYSKLIEYYDQhftqpqvqdfiravckE 335
Cdd:PRK09192 236 FLLTPVATQLSVDYLPtrDFARRPlQWLDLISrnrgtiSYSPPFGYELCARRVNSKDLAELDL----------------S 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 336 RIRLMVSGSAALPQPVLERWAEITGHV------LLERYGMTEIGMALS-NPL-KGSRV--------------------PG 387
Cdd:PRK09192 300 CWRVAGIGADMIRPDVLHQFAEAFAPAgfddkaFMPSYGLAEATLAVSfSPLgSGIVVeevdrdrleyqgkavapgaeTR 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 388 AV------GVPLPGVEVRIMmtNSTNAIIAEgnskgTRVkaglegkeGELLVRGSSVFQKYWNKpQETADTFTEDGWFKT 461
Cdd:PRK09192 380 RVrtfvncGKALPGHEIEIR--NEAGMPLPE-----RVV--------GHICVRGPSLMSGYFRD-EESQDVLAADGWLDT 443
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2073725801 462 GDTALYRDGVYWIMGRTSvDIIKSGGYKISALDVERHLLAHPDIT--DVAVIGAPDPTwGQKVTAVVQ 527
Cdd:PRK09192 444 GDLGYLLDGYLYITGRAK-DLIIINGRNIWPQDIEWIAEQEPELRsgDAAAFSIAQEN-GEKIVLLVQ 509
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
200-522 |
7.40e-15 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 77.55 E-value: 7.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 200 NISDW-AERPAMLIYTSGTTGRPKGVLHTHSSLQAMVQGLVSEWAWNKDDVILHTLPLHHVHGIvnklmcplwvgATCIM 278
Cdd:PRK06334 176 GVSDKdPEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSFLPPFHAYGF-----------NSCTL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 279 LPEFSAQKVweqlisskspmvnVFMAVPTIYSKLIEYYDQ-HFT----QPQVQDFIRAVCK------ERIRLMVSGSAAL 347
Cdd:PRK06334 245 FPLLSGVPV-------------VFAYNPLYPKKIVEMIDEaKVTflgsTPVFFDYILKTAKkqesclPSLRFVVIGGDAF 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 348 PQPVLERWAEITGHVLLER-YGMTEIGMALS-NPLKGSRVPGAVGVPLPGVEVRIMmtnstnaiiaegnSKGTRVKAGlE 425
Cdd:PRK06334 312 KDSLYQEALKTFPHIQLRQgYGTTECSPVITiNTVNSPKHESCVGMPIRGMDVLIV-------------SEETKVPVS-S 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 426 GKEGELLVRGSSVFQKYW-NKPQETADTFTEDGWFKTGDTA-LYRDGVYWIMGRTSvDIIKSGGYKISALDVERHLLAH- 502
Cdd:PRK06334 378 GETGLVLTRGTSLFSGYLgEDFGQGFVELGGETWYVTGDLGyVDRHGELFLKGRLS-RFVKIGAEMVSLEALESILMEGf 456
|
330 340
....*....|....*....|....*
gi 2073725801 503 -----PDITDVAVIGAPdptwGQKV 522
Cdd:PRK06334 457 gqnaaDHAGPLVVCGLP----GEKV 477
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
128-575 |
2.31e-13 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 73.66 E-value: 2.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 128 GGIAVPLYRKHPPGELEYVISDSQSSLLVAGQPFMDtlepLAQKL--GLPCLQLPTTSSLDTLQSEDIrmlPEQN--ISD 203
Cdd:PRK05691 3794 GAGYLPLDPGLPAQRLQRIIELSRTPVLVCSAACRE----QARALldELGCANRPRLLVWEEVQAGEV---ASHNpgIYS 3866
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 204 WAERPAMLIYTSGTTGRPKGVLHTHSSLQAMVQGLVSEWAWNKDDVILHTLPLHHVHGIVNKLMCPLWvGATCIMLPEFS 283
Cdd:PRK05691 3867 GPDNLAYVIYTSGSTGLPKGVMVEQRGMLNNQLSKVPYLALSEADVIAQTASQSFDISVWQFLAAPLF-GARVEIVPNAI 3945
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 284 AQKVWEQLISSKSPMVNVFMAVPTIYSKLIEYYDQHFtqpqvqdfiravckERIRLMVSGSAALPQPVLERWaeitghvl 363
Cdd:PRK05691 3946 AHDPQGLLAHVQAQGITVLESVPSLIQGMLAEDRQAL--------------DGLRWMLPTGEAMPPELARQW-------- 4003
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 364 LERYgmTEIGmaLSNPLKGSRVPGAVGVplpgveVRIMMTNSTNAIIAEG----NSKGTRVKAGLE----GKEGELLVRG 435
Cdd:PRK05691 4004 LQRY--PQIG--LVNAYGPAECSDDVAF------FRVDLASTRGSYLPIGsptdNNRLYLLDEALElvplGAVGELCVAG 4073
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 436 SSVFQKYWNKPQETADTFTEDGW-------FKTGDTALYR-DGVYWIMGRtsVD-IIKSGGYKISALDVERHLLAHPDIT 506
Cdd:PRK05691 4074 TGVGRGYVGDPLRTALAFVPHPFgapgerlYRTGDLARRRsDGVLEYVGR--IDhQVKIRGYRIELGEIEARLHEQAEVR 4151
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2073725801 507 DVAVIGAPDPTWGQKVTAVV--QLKKGKTLTLSQLQAWAREHMAPYTIPTGLILVEEMPRNQMGKVNKKDL 575
Cdd:PRK05691 4152 EAAVAVQEGVNGKHLVGYLVphQTVLAQGALLERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKAL 4222
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
209-575 |
4.63e-13 |
|
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: 71.35 E-value: 4.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 209 AMLIYTSGTTGRPKGVLHTHSSLQAMVQGLVSEWAWNKDDVILHTLPLHHVHGIVNKLMCpLWVGATCIMLPefSAQKVW 288
Cdd:cd17654 121 AYVIHTSGTTGTPKIVAVPHKCILPNIQHFRSLFNITSEDILFLTSPLTFDPSVVEIFLS-LSSGATLLIVP--TSVKVL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 289 EQLISS---KSPMVNVFMAVPTIYSKlieyydqhFTQPQVQDFIRAVCKErIRLMVSGSAALPQPV-LERWA-EITGHVL 363
Cdd:cd17654 198 PSKLADilfKRHRITVLQATPTLFRR--------FGSQSIKSTVLSATSS-LRVLALGGEPFPSLViLSSWRgKGNRTRI 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 364 LERYGMTEIGM-ALSNPLKGSRVPGAVGVPLPGVEVRIMMTNstnaiiaegnskgtrvkaGLEGkEGELLVRGSS---VF 439
Cdd:cd17654 269 FNIYGITEVSCwALAYKVPEEDSPVQLGSPLLGTVIEVRDQN------------------GSEG-TGQVFLGGLNrvcIL 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 440 QKYWNKPQETadtftedgWFKTGDTALYRDGVYWIMGRTSvDIIKSGGYKISALDVERHLLAHPDITDVAVigapdpTW- 518
Cdd:cd17654 330 DDEVTVPKGT--------MRATGDFVTVKDGELFFLGRKD-SQIKRRGKRINLDLIQQVIESCLGVESCAV------TLs 394
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 2073725801 519 -GQKVTAVVQLKKGKTLTLSQLQawaREHMAPYTIPTGLILVEEMPRNQMGKVNKKDL 575
Cdd:cd17654 395 dQQRLIAFIVGESSSSRIHKELQ---LTLLSSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
182-580 |
1.12e-12 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 70.15 E-value: 1.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 182 TSSLDTLQSEDIRMLPEQNISDWAERpAMLIYTSGTTGRPKGVLHTHSSLQAMVQGLVSEWAWNKDDVILHTLPLHH-VH 260
Cdd:cd05939 81 FNLLDPLLTQSSTEPPSQDDVNFRDK-LFYIYTSGTTGLPKAAVIVHSRYYRIAAGAYYAFGMRPEDVVYDCLPLYHsAG 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 261 GIVNKLMCPLWvGATCIMLPEFSAQKVWEQLISSKSpmvnvfmavpTIYSKLIEYYDQHFTQPQVQDfiraVCKERIRLM 340
Cdd:cd05939 160 GIMGVGQALLH-GSTVVIRKKFSASNFWDDCVKYNC----------TIVQYIGEICRYLLAQPPSEE----EQKHNVRLA 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 341 VsGSAALPQPvlerWAEITGHV----LLERYGMTEIGMALSNplKGSRVpGAVG---VPLPGV-EVRIMMTN-STNAIIA 411
Cdd:cd05939 225 V-GNGLRPQI----WEQFVRRFgipqIGEFYGATEGNSSLVN--IDNHV-GACGfnsRILPSVyPIRLIKVDeDTGELIR 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 412 egNSKGTRVKAGlEGKEGELLVR-----GSSVFQKYWNKpQETA-----DTFTE-DGWFKTGDTaLYRD--GVYWIMGRT 478
Cdd:cd05939 297 --DSDGLCIPCQ-PGEPGLLVGKiiqndPLRRFDGYVNE-GATNkkiarDVFKKgDSAFLSGDV-LVMDelGYLYFKDRT 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 479 SvDIIKSGGYKISALDVERHLLAHPDITDVAVIGAPDP-TWGQKVTAVVQLKKGKTlTLSQLQAWAREHMAPYTIPTGLI 557
Cdd:cd05939 372 G-DTFRWKGENVSTTEVEGILSNVLGLEDVVVYGVEVPgVEGRAGMAAIVDPERKV-DLDRFSAVLAKSLPPYARPQFIR 449
|
410 420
....*....|....*....|...
gi 2073725801 558 LVEEMPRNQMGKVNKKDLLRKFF 580
Cdd:cd05939 450 LLPEVDKTGTFKLQKTDLQKEGY 472
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
112-477 |
2.13e-12 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 70.05 E-value: 2.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 112 ANDASYTVAQWAAWMCGGIAVPLYRKHPPGELEYVISDSQSSLLVAGQP--------------FMDTLEPL--------- 168
Cdd:PLN02614 112 ANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIVFVEEKkiselfktcpnsteYMKTVVSFggvsreqke 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 169 -AQKLGLPCLQLPTTSSLDTLQSEDirmLPEQNISDWAerpaMLIYTSGTTGRPKGVLHTHSSLQAMVQGLV-----SEW 242
Cdd:PLN02614 192 eAETFGLVIYAWDEFLKLGEGKQYD---LPIKKKSDIC----TIMYTSGTTGDPKGVMISNESIVTLIAGVIrllksANA 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 243 AWNKDDVILHTLPLHHVHGIVNKlMCPLWVGATcIMLPEFSAQKVWEQLISSKSpmvNVFMAVPTI----YSKLIE---- 314
Cdd:PLN02614 265 ALTVKDVYLSYLPLAHIFDRVIE-ECFIQHGAA-IGFWRGDVKLLIEDLGELKP---TIFCAVPRVldrvYSGLQKklsd 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 315 -------YYDQHFT---------------QPQVQDFIRAVCKE----RIRLMVSGSAALPQPVlERWAEITG--HVLlER 366
Cdd:PLN02614 340 ggflkkfVFDSAFSykfgnmkkgqshveaSPLCDKLVFNKVKQglggNVRIILSGAAPLASHV-ESFLRVVAccHVL-QG 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 367 YGMTE--IGMALSNPLKGSRVpGAVGVPLPGVEVRIMMTNSTNAiiaegNSKGTRVKaglegkeGELLVRGSSVFQKYWN 444
Cdd:PLN02614 418 YGLTEscAGTFVSLPDELDML-GTVGPPVPNVDIRLESVPEMEY-----DALASTPR-------GEICIRGKTLFSGYYK 484
|
410 420 430
....*....|....*....|....*....|....
gi 2073725801 445 KPQETADTFTeDGWFKTGDTALYR-DGVYWIMGR 477
Cdd:PLN02614 485 REDLTKEVLI-DGWLHTGDVGEWQpNGSMKIIDR 517
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
45-486 |
4.54e-11 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 65.53 E-value: 4.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 45 ISPGVGRVAPVFSRASVYGDNVA--ITDHSGSHTFCSLYKNSKSLaGLITKALTCQsgdLQ-----GKCISFLCANDASY 117
Cdd:PRK12476 30 LPPGTTLISLIERNIANVGDTVAyrYLDHSHSAAGCAVELTWTQL-GVRLRAVGAR---LQqvagpGDRVAILAPQGIDY 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 118 TVAQWAAWMCGGIAVPLYRKHPPGE---LEYVISDSQSSLL----VAGQP---FMDTLEPLAQKLGLPCLQLPTTSSLD- 186
Cdd:PRK12476 106 VAGFFAAIKAGTIAVPLFAPELPGHaerLDTALRDAEPTVVltttAAAEAvegFLRNLPRLRRPRVIAIDAIPDSAGESf 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 187 ---TLQSEDIrmlpeqnisdwaerpAMLIYTSGTTGRPKGVLHTHSSLQA-MVQGLVSEWAWNKDDVILHTLPLHHVHGI 262
Cdd:PRK12476 186 vpvELDTDDV---------------SHLQYTSGSTRPPVGVEITHRAVGTnLVQMILSIDLLDRNTHGVSWLPLYHDMGL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 263 VnKLMCP-LWVGATCIMLPEFSAQKV--WEQLISSKSPMVNVFMAVPTIyskLIEYYDQHFTQPQVQDF-IRAVckerir 338
Cdd:PRK12476 251 S-MIGFPaVYGGHSTLMSPTAFVRRPqrWIKALSEGSRTGRVVTAAPNF---AYEWAAQRGLPAEGDDIdLSNV------ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 339 LMVSGSAALPQPVLERWAEITGHVLLER------YGMTEIGMALSNPLKGSRvPGAV-----------GVPLPGVEVRIM 401
Cdd:PRK12476 321 VLIIGSEPVSIDAVTTFNKAFAPYGLPRtafkpsYGIAEATLFVATIAPDAE-PSVVyldreqlgagrAVRVAADAPNAV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 402 -------MTNSTNAIIAEGNSkGTRVKaglEGKEGELLVRGSSVFQKYWNKPQETADTF----------------TEDG- 457
Cdd:PRK12476 400 ahvscgqVARSQWAVIVDPDT-GAELP---DGEVGEIWLHGDNIGRGYWGRPEETERTFgaklqsrlaegshadgAADDg 475
|
490 500 510
....*....|....*....|....*....|
gi 2073725801 458 -WFKTGDTALYRDGVYWIMGRTSVDIIKSG 486
Cdd:PRK12476 476 tWLRTGDLGVYLDGELYITGRIADLIVIDG 505
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
117-530 |
1.11e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 64.19 E-value: 1.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 117 YTVAQWAAWMCGGIAVPLYRKHPPGELEYVIS---DSQSSLLVAGQPFMDTLeplAQKLGLPCLQL-PTTSSLDTL--QS 190
Cdd:PRK05850 72 YIVAFLGALQAGLIAVPLSVPQGGAHDERVSAvlrDTSPSVVLTTSAVVDDV---TEYVAPQPGQSaPPVIEVDLLdlDS 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 191 EDIRMLPEQNISDwaerPAMLIYTSGTTGRPKGVLHTHSSLQAMVQGLVSEWAWNKDDV------ILHTLPLHHVHGIVN 264
Cdd:PRK05850 149 PRGSDARPRDLPS----TAYLQYTSGSTRTPAGVMVSHRNVIANFEQLMSDYFGDTGGVpppdttVVSWLPFYHDMGLVL 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 265 KLMCPLWVGATCI-MLPEFSAQKV--WEQLISSKSPmvnVFMAVPTIYSKLieyydqhftqpqvqdfirAVCKER----- 336
Cdd:PRK05850 225 GVCAPILGGCPAVlTSPVAFLQRParWMQLLASNPH---AFSAAPNFAFEL------------------AVRKTSdddma 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 337 ------IRLMVSGSAALPQPVLERWAE------ITGHVLLERYGMTE--IGMALSNPlkgSRVPGAV------------- 389
Cdd:PRK05850 284 gldlggVLGIISGSERVHPATLKRFADrfapfnLRETAIRPSYGLAEatVYVATREP---GQPPESVrfdyeklsaghak 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 390 ------GVPLpgveVRIMMTNSTNAIIAEGNskgTRVKAGlEGKEGELLVRGSSVFQKYWNKPQETADTF---------- 453
Cdd:PRK05850 361 rcetggGTPL----VSYGSPRSPTVRIVDPD---TCIECP-AGTVGEIWVHGDNVAAGYWQKPEETERTFgatlvdpspg 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 454 TEDG-WFKTGDTALYRDGVYWIMGRTSVDIIKSGgykisaldvERHllaHPD--------ITD--VAVIGAPDPTwGQKV 522
Cdd:PRK05850 433 TPEGpWLRTGDLGFISEGELFIVGRIKDLLIVDG---------RNH---YPDdieatiqeITGgrVAAISVPDDG-TEKL 499
|
....*...
gi 2073725801 523 TAVVQLKK 530
Cdd:PRK05850 500 VAIIELKK 507
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
208-497 |
1.47e-10 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 63.63 E-value: 1.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 208 PAMLIYTSGTTGRPKGVLHTHSSLQAMVQGLVSEWAWNKD-DVILHTLPLHHVHGIVNkLMCPLWVGATCIMLPE--FSA 284
Cdd:PRK05851 154 PAVLQGTAGSTGTPRTAILSPGAVLSNLRGLNARVGLDAAtDVGCSWLPLYHDMGLAF-LLTAALAGAPLWLAPTtaFSA 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 285 QKV-WEQLIS-SKSPMVnvfmAVPTIYSKLIEYYdqhftqpqvQDFIRAVCKERIRLMVSGSaalpQPV----LERWAEI 358
Cdd:PRK05851 233 SPFrWLSWLSdSRATLT----AAPNFAYNLIGKY---------ARRVSDVDLGALRVALNGG----EPVdcdgFERFATA 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 359 TGHV------LLERYGMTEIGMALSNPLKGS---------------RVPGAVGVPLPGVEVRIMMTNSTnaiiaegnskg 417
Cdd:PRK05851 296 MAPFgfdagaAAPSYGLAESTCAVTVPVPGIglrvdevttddgsgaRRHAVLGNPIPGMEVRISPGDGA----------- 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 418 trvkAGLEGKE-GELLVRGSSVFQKYWNkpqetADTFTEDGWFKTGDTALYRDGVYWIMGRTSvDIIKSGGYKISALDVE 496
Cdd:PRK05851 365 ----AGVAGREiGEIEIRGASMMSGYLG-----QAPIDPDDWFPTGDLGYLVDGGLVVCGRAK-ELITVAGRNIFPTEIE 434
|
.
gi 2073725801 497 R 497
Cdd:PRK05851 435 R 435
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
204-578 |
2.43e-10 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 63.43 E-value: 2.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 204 WAE--RPAMLIYTSGTTGRPKGVL-----HT---HSSLQAMVQGLVSEWAWNKDD---VILHTlplHHVHGivnklmcPL 270
Cdd:PRK10524 229 WLEsnEPSYILYTSGTTGKPKGVQrdtggYAvalATSMDTIFGGKAGETFFCASDigwVVGHS---YIVYA-------PL 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 271 WVGATCIM---LPEFSAQKVWEQLISSKSpmVNVFMAVPTIYSKLieyydqhftQPQVQDFIRAVCKERIRLMVSGSAAL 347
Cdd:PRK10524 299 LAGMATIMyegLPTRPDAGIWWRIVEKYK--VNRMFSAPTAIRVL---------KKQDPALLRKHDLSSLRALFLAGEPL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 348 PQPVlERW-AEITGHVLLERYGMTEIG---MALSNPL--KGSRvPGAVGVPLPGVEVRIMMTNStnaiiaegnskGTRVK 421
Cdd:PRK10524 368 DEPT-ASWiSEALGVPVIDNYWQTETGwpiLAIARGVedRPTR-LGSPGVPMYGYNVKLLNEVT-----------GEPCG 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 422 AGlegKEGELLVRGS---SVFQKYWNKPQETADTFtedgwFKTGDTALY---------RDGVYWIMGRTSvDIIKSGGYK 489
Cdd:PRK10524 435 PN---EKGVLVIEGPlppGCMQTVWGDDDRFVKTY-----WSLFGRQVYstfdwgirdADGYYFILGRTD-DVINVAGHR 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 490 ISALDVERHLLAHPDITDVAVIGAPDPTWGQKVTAVVQLKKGKTLTL----------------SQLQAWARehmapytiP 553
Cdd:PRK10524 506 LGTREIEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPKDSDSLADrearlalekeimalvdSQLGAVAR--------P 577
|
410 420
....*....|....*....|....*
gi 2073725801 554 TGLILVEEMPRNQMGKvnkkdLLRK 578
Cdd:PRK10524 578 ARVWFVSALPKTRSGK-----LLRR 597
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
104-477 |
4.05e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 62.44 E-value: 4.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 104 GKCISFLCANDASYTVAQWAAWMCGGIAVPLYRKHPPG---ELEYVISDSQSSLLVAGQpfmDTLEPLAQKL-GLPCLQL 179
Cdd:PRK07769 79 GDRVAILAPQNLDYLIAFFGALYAGRIAVPLFDPAEPGhvgRLHAVLDDCTPSAILTTT---DSAEGVRKFFrARPAKER 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 180 PTTSSLDTLqsedirmlPEQNISDWAERP------AMLIYTSGTTGRPKGVLHTHSSLQAMVQGLVSEWAWNKDDVILHT 253
Cdd:PRK07769 156 PRVIAVDAV--------PDEVGATWVPPEanedtiAYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALEGQEGDRGVSW 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 254 LPLHHVHGIVNKLMCPLWVGATCIMLPEFSAQKV--WEQLISSKSP-MVNVFMAVPTiysklieYYDQHFTQpqvqdfiR 330
Cdd:PRK07769 228 LPFFHDMGLITVLLPALLGHYITFMSPAAFVRRPgrWIRELARKPGgTGGTFSAAPN-------FAFEHAAA-------R 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 331 AVCKE--------RIRLMVSGSAALPQPVLERWAEITGHVLLER------YGMTEIGMALSNP---------------LK 381
Cdd:PRK07769 294 GLPKDgeppldlsNVKGLLNGSEPVSPASMRKFNEAFAPYGLPPtaikpsYGMAEATLFVSTTpmdeeptviyvdrdeLN 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 382 GSRV-------PGAVGVPLPGVEVRimmtnSTNAIIAEGNSkGTRVKaglEGKEGELLVRGSSVFQKYWNKPQETADTF- 453
Cdd:PRK07769 374 AGRFvevpadaPNAVAQVSAGKVGV-----SEWAVIVDPET-ASELP---DGQIGEIWLHGNNIGTGYWGKPEETAATFq 444
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 2073725801 454 ---------------TEDG-WFKTGDTALYRDGVYWIMGR 477
Cdd:PRK07769 445 nilksrlseshaegaPDDAlWVRTGDYGVYFDGELYITGR 484
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
179-579 |
1.08e-09 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 61.30 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 179 LPTTSSLDtlqsEDIRMLPEQNISDWAE-------RPAMLIYTSGTTGRPKGVLHTHSSlqAMVqGLVSEWAW---NKDD 248
Cdd:PTZ00237 224 IPNTLSWY----DEIKKIKENNQSPFYEyvpvessHPLYILYTSGTTGNSKAVVRSNGP--HLV-GLKYYWRSiieKDIP 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 249 VILHTlplHHVHGIV---NKLMCPLWVGATCIML------PEFSAQKVWEQLISSKspmVNVFMAVPTIYSKLIEyydqh 319
Cdd:PTZ00237 297 TVVFS---HSSIGWVsfhGFLYGSLSLGNTFVMFeggiikNKHIEDDLWNTIEKHK---VTHTLTLPKTIRYLIK----- 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 320 fTQPQVQDFIRAVCKERIRLMVSGSAALPQPVLERWAEITGHVLLERYGMTEIGMALSNPLKGSRVP-GAVGVPLPGVEV 398
Cdd:PTZ00237 366 -TDPEATIIRSKYDLSNLKEIWCGGEVIEESIPEYIENKLKIKSSRGYGQTEIGITYLYCYGHINIPyNATGVPSIFIKP 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 399 RIMmtnSTNAIIAEGNSKGTRV-KAGLEGKEGELLVRGSSVFQKYWNK-PqetadtftedGWFKTGDTAlYRD--GVYWI 474
Cdd:PTZ00237 445 SIL---SEDGKELNVNEIGEVAfKLPMPPSFATTFYKNDEKFKQLFSKfP----------GYYNSGDLG-FKDenGYYTI 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 475 MGRtSVDIIKSGGYKISALDVERHLLAHPDITDVAVIGAPDPTWGQKVTAVVQLKKGKT---LTLSQLQAWARE----HM 547
Cdd:PTZ00237 511 VSR-SDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPIGLLVLKQDQSnqsIDLNKLKNEINNiitqDI 589
|
410 420 430
....*....|....*....|....*....|..
gi 2073725801 548 APYTIPTGLILVEEMPRNQMGKVnKKDLLRKF 579
Cdd:PTZ00237 590 ESLAVLRKIIIVNQLPKTKTGKI-PRQIISKF 620
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
209-514 |
1.19e-09 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 61.29 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 209 AMLIYTSGTTGRPKGVLHTHSSLQAMVQGLVSEW-AWNKDDVILHTLPLHHVhgivnklmcpLWVGATCIMLPEFSAqkv 287
Cdd:PLN02387 253 AVIMYTSGSTGLPKGVMMTHGNIVATVAGVMTVVpKLGKNDVYLAYLPLAHI----------LELAAESVMAAVGAA--- 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 288 weqlISSKSPMV---------------------NVFMAVPTIYSKL--------------------IEYY---------- 316
Cdd:PLN02387 320 ----IGYGSPLTltdtsnkikkgtkgdasalkpTLMTAVPAILDRVrdgvrkkvdakgglakklfdIAYKrrlaaiegsw 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 317 ------DQHFTQPQVQDFIRAVCKERIRLMVSGSAALpQPVLERWAEIT-GHVLLERYGMTEI--GMALSNPLKGSrvPG 387
Cdd:PLN02387 396 fgawglEKLLWDALVFKKIRAVLGGRIRFMLSGGAPL-SGDTQRFINIClGAPIGQGYGLTETcaGATFSEWDDTS--VG 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 388 AVGVPLPGVEVRIMMTNSTNAIIAEgnSKGTRvkaglegkeGELLVRGSSVFQKYWNKPQETADTFTEDG----WFKTGD 463
Cdd:PLN02387 473 RVGPPLPCCYVKLVSWEEGGYLISD--KPMPR---------GEIVIGGPSVTLGYFKNQEKTDEVYKVDErgmrWFYTGD 541
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 2073725801 464 TALYR-DGVYWIMGRTSvDIIK--SGGYkISALDVERHLLAHPDITDVAVIGAP 514
Cdd:PLN02387 542 IGQFHpDGCLEIIDRKK-DIVKlqHGEY-VSLGKVEAALSVSPYVDNIMVHADP 593
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
211-463 |
1.09e-06 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 51.64 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 211 LIYTSGTTGRPKGVLHTHSSLQAMVQGLvSEWAWNKD---DVILHTLPLHHVHGIVNKLMCPLWVGATCIM---LPEFSa 284
Cdd:PTZ00342 309 IVYTSGTSGKPKGVMLSNKNLYNTVVPL-CKHSIFKKynpKTHLSYLPISHIYERVIAYLSFMLGGTINIWskdINYFS- 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 285 qkvwEQLISSKSpmvNVFMAVPTIYSKL---------------------IEYYDQHFTQPQVQDFIRAVCK--ERIR--- 338
Cdd:PTZ00342 387 ----KDIYNSKG---NILAGVPKVFNRIytnimteinnlpplkrflvkkILSLRKSNNNGGFSKFLEGITHisSKIKdkv 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073725801 339 -----LMVSGSAALPQPVLERWAeitghVLL-----ERYGMTEIGMALSNPLKGSRVPGAVGVPL-PGVEVRIMMTNSTN 407
Cdd:PTZ00342 460 npnleVILNGGGKLSPKIAEELS-----VLLnvnyyQGYGLTETTGPIFVQHADDNNTESIGGPIsPNTKYKVRTWETYK 534
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2073725801 408 AiiaegnsKGTRVKaglegkeGELLVRGSSVFQKYWNKPQETADTFTEDGWFKTGD 463
Cdd:PTZ00342 535 A-------TDTLPK-------GELLIKSDSIFSGYFLEKEQTKNAFTEDGYFKTGD 576
|
|
| |
