|
Name |
Accession |
Description |
Interval |
E-value |
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
4-492 |
2.41e-166 |
|
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: 477.77 E-value: 2.41e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 4 DWIKTRSDFDDDKPAVIDHAKqtSWTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLN 83
Cdd:COG0318 3 DLLRRAAARHPDRPALVFGGR--RLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 84 WRLNPKEIAAIVEDAQLKLLFYAekhlssltdidqnllhmdidvaqydeivnpdyhqpfqatpvepqdlaALIYTSGTTG 163
Cdd:COG0318 81 PRLTAEELAYILEDSGARALVTA-----------------------------------------------LILYTSGTTG 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 164 SPKGVMFSYESFVHNGANLELTYKFNSNYITIVSTPMFHVLGFNDTVLPVLMSGGTLILQRYFNGEELNDMIAQYHPTFI 243
Cdd:COG0318 114 RPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLPRFDPERVLELIERERVTVL 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 244 IMIPTMYYSTLRASNFNPENFRAMDYIIQGGSqPLPS--IQAAFKQYGINIINGYGLTEA-PLVLVNTPENSKRKPMSIG 320
Cdd:COG0318 194 FGVPTMLARLLRHPEFARYDLSSLRLVVSGGA-PLPPelLERFEERFGVRIVEGYGLTETsPVVTVNPEDPGERRPGSVG 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 321 KAVMFVDARILDDNGEEVPTGEIGELAIKAKNVTPGYWNKPAETAKAFHGRYLLTGDLAKMDNDGDIFIIDRKKELIITG 400
Cdd:COG0318 273 RPLPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAFRDGWLRTGDLGRLDEDGYLYIVGRKKDMIISG 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 401 GENVLPSEVENALAEHPLVDRCVVVGYDHPKYGESIAAAIILREDEPHYAEILNQHMRSRLAGYKVPRMYVPVTHMPLNS 480
Cdd:COG0318 353 GENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPGAELDAEELRAFLRERLARYKVPRRVEFVDELPRTA 432
|
490
....*....|..
gi 584959700 481 TQKPDKLAIRQM 492
Cdd:COG0318 433 SGKIDRRALRER 444
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
15-486 |
8.40e-149 |
|
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: 432.42 E-value: 8.40e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 15 DKPAVIDhaKQTSWTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAAI 94
Cdd:cd17631 10 DRTALVF--GGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEVAYI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 95 VEDAQLKLLFyaekhlssltdidqnllhmdidvaqydeivnpdyhqpfqatpvepQDLAALIYTSGTTGSPKGVMFSYES 174
Cdd:cd17631 88 LADSGAKVLF---------------------------------------------DDLALLMYTSGTTGRPKGAMLTHRN 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 175 FVHNGANLELTYKFNSNYITIVSTPMFHVLGFNDTVLPVLMSGGTLILQRYFNGEELNDMIAQYHPTFIIMIPTMYYSTL 254
Cdd:cd17631 123 LLWNAVNALAALDLGPDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVILRKFDPETVLDLIERHRVTSFFLVPTMIQALL 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 255 RASNFNPENFRAMDYIIQGGSQPLPSIQAAFKQYGINIINGYGLTEA-PLVLVNTPENSKRKPMSIGKAVMFVDARILDD 333
Cdd:cd17631 203 QHPRFATTDLSSLRAVIYGGAPMPERLLRALQARGVKFVQGYGMTETsPGVTFLSPEDHRRKLGSAGRPVFFVEVRIVDP 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 334 NGEEVPTGEIGELAIKAKNVTPGYWNKPAETAKAFHGRYLLTGDLAKMDNDGDIFIIDRKKELIITGGENVLPSEVENAL 413
Cdd:cd17631 283 DGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFRDGWFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVL 362
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 584959700 414 AEHPLVDRCVVVGYDHPKYGESIAAAIILREDEPHYAEILNQHMRSRLAGYKVPRMYVPVTHMPLNSTQKPDK 486
Cdd:cd17631 363 YEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPGAELDEDELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
15-496 |
3.84e-137 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 405.72 E-value: 3.84e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 15 DKPAVIDHAKQtsWTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAAI 94
Cdd:PRK06187 21 DKEAVYFDGRR--TTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPINIRLKPEEIAYI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 95 VEDAQLKLLFYAEKHLSSLTDI--------------DQNLLHMDIDVAQYDEIVN---PDYHQPfqatPVEPQDLAALIY 157
Cdd:PRK06187 99 LNDAEDRVVLVDSEFVPLLAAIlpqlptvrtvivegDGPAAPLAPEVGEYEELLAaasDTFDFP----DIDENDAAAMLY 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 158 TSGTTGSPKGVMFSYESFVHNGANLELTYKFNSNYITIVSTPMFHVLGFNDTVLPvLMSGGTLILQRYFNGEELNDMIAQ 237
Cdd:PRK06187 175 TSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVPMFHVHAWGLPYLA-LMAGAKQVIPRRFDPENLLDLIET 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 238 YHPTFIIMIPTMYYSTLRASNFNPENFRAMDYIIQGGSqPLPS--IQAAFKQYGINIINGYGLTE-APLVLVNTPE---- 310
Cdd:PRK06187 254 ERVTFFFAVPTIWQMLLKAPRAYFVDFSSLRLVIYGGA-ALPPalLREFKEKFGIDLVQGYGMTEtSPVVSVLPPEdqlp 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 311 NSKRKPMSIGKAVMFVDARILDDNGEEVP--TGEIGELAIKAKNVTPGYWNKPAETAKAFHGRYLLTGDLAKMDNDGDIF 388
Cdd:PRK06187 333 GQWTKRRSAGRPLPGVEARIVDDDGDELPpdGGEVGEIIVRGPWLMQGYWNRPEATAETIDGGWLHTGDVGYIDEDGYLY 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 389 IIDRKKELIITGGENVLPSEVENALAEHPLVDRCVVVGYDHPKYGESIAAAIILREDEPHYAEILNQHMRSRLAGYKVPR 468
Cdd:PRK06187 413 ITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVLKPGATLDAKELRAFLRGRLAKFKLPK 492
|
490 500
....*....|....*....|....*...
gi 584959700 469 MYVPVTHMPLNSTQKPDKLAIRQMMNDK 496
Cdd:PRK06187 493 RIAFVDELPRTSVGKILKRVLREQYAEG 520
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
15-490 |
1.45e-130 |
|
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: 387.30 E-value: 1.45e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 15 DKPAVIDHAKqtSWTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAAI 94
Cdd:cd05936 14 DKTALIFMGR--KLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYTPRELEHI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 95 VEDAQLKLLFYAEkhlsSLTDIDQNLLHMDIDVAqydeivnpdyhqpfqatpVEPQDLAALIYTSGTTGSPKGVMFSYES 174
Cdd:cd05936 92 LNDSGAKALIVAV----SFTDLLAAGAPLGERVA------------------LTPEDVAVLQYTSGTTGVPKGAMLTHRN 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 175 FVHNGANLELTYKFN--SNYITIVSTPMFHVLGFndTV---LPVLMsGGTLILQRYFNGEELNDMIAQYHPTFIIMIPTM 249
Cdd:cd05936 150 LVANALQIKAWLEDLleGDDVVLAALPLFHVFGL--TVallLPLAL-GATIVLIPRFRPIGVLKEIRKHRVTIFPGVPTM 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 250 YYSTLRASNFNPENFRAMDYIIQGGSqPLP-SIQAAFKQ-YGINIINGYGLTEA-PLVLVNTPENsKRKPMSIGKAVMFV 326
Cdd:cd05936 227 YIALLNAPEFKKRDFSSLRLCISGGA-PLPvEVAERFEElTGVPIVEGYGLTETsPVVAVNPLDG-PRKPGSIGIPLPGT 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 327 DARILDDNGEEVPTGEIGELAIKAKNVTPGYWNKPAETAKAFHGRYLLTGDLAKMDNDGDIFIIDRKKELIITGGENVLP 406
Cdd:cd05936 305 EVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFVDGWLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYP 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 407 SEVENALAEHPLVDRCVVVGYDHPKYGESIAAAIILREDEPHYAEILNQHMRSRLAGYKVPRMYVPVTHMPLNSTQKPDK 486
Cdd:cd05936 385 REVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEGASLTEEEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILR 464
|
....
gi 584959700 487 LAIR 490
Cdd:cd05936 465 RELR 468
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
151-485 |
4.29e-125 |
|
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: 368.15 E-value: 4.29e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 151 DLAALIYTSGTTGSPKGVMFSYESFVHNGANLELTYKFNSNYITIVSTPMFHVLGFNdTVLPVLMSGGTLILQRYFNGEE 230
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLF-GLLGALLAGGTVVLLPKFDPEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 231 LNDMIAQYHPTFIIMIPTMYYSTLRASNFNPENFRAMDYIIQGGSQPLPSIQAAFKQY-GINIINGYGLTEA-PLVLVNT 308
Cdd:cd04433 80 ALELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGAPLPPELLERFEEApGIKLVNGYGLTETgGTVATGP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 309 PENSKRKPMSIGKAVMFVDARILDDNGEEVPTGEIGELAIKAKNVTPGYWNKPAETAKAFHGRYLLTGDLAKMDNDGDIF 388
Cdd:cd04433 160 PDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVDEDGWYRTGDLGRLDEDGYLY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 389 IIDRKKELIITGGENVLPSEVENALAEHPLVDRCVVVGYDHPKYGESIAAAIILREDEPHYAEILNQHMRSRLAGYKVPR 468
Cdd:cd04433 240 IVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLDAEELRAHVRERLAPYKVPR 319
|
330
....*....|....*..
gi 584959700 469 MYVPVTHMPLNSTQKPD 485
Cdd:cd04433 320 RVVFVDALPRTASGKID 336
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
5-496 |
1.46e-106 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 326.43 E-value: 1.46e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 5 WIKTRSDFDDDKPAVIdhAKQTSWTYQQLNARADNMAHYLTSQ-GVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLN 83
Cdd:PRK06839 7 WIEKRAYLHPDRIAII--TEEEEMTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 84 WRLNPKEIAAIVEDAQLKLLFYAEKHLSSLTDIDQ--NLLHMdIDVAQYDEIVNpdyHQPFQATPVEPQDLAALIYTSGT 161
Cdd:PRK06839 85 IRLTENELIFQLKDSGTTVLFVEKTFQNMALSMQKvsYVQRV-ISITSLKEIED---RKIDNFVEKNESASFIICYTSGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 162 TGSPKGVMFSYESFVHNGANLELTYKFNSNYITIVSTPMFHVLGFNDTVLPVLMSGGTLILQRYFNGEELNDMIAQYHPT 241
Cdd:PRK06839 161 TGKPKGAVLTQENMFWNALNNTFAIDLTMHDRSIVLLPLFHIGGIGLFAFPTLFAGGVIIVPRKFEPTKALSMIEKHKVT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 242 FIIMIPTMYYSTLRASNFNPENFRAMDYIIQGGSQ-PLPSIQAaFKQYGINIINGYGLTE-APLVLVNTPENSKRKPMSI 319
Cdd:PRK06839 241 VVMGVPTIHQALINCSKFETTNLQSVRWFYNGGAPcPEELMRE-FIDRGFLFGQGFGMTEtSPTVFMLSEEDARRKVGSI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 320 GKAVMFVDARILDDNGEEVPTGEIGELAIKAKNVTPGYWNKPAETAKAFHGRYLLTGDLAKMDNDGDIFIIDRKKELIIT 399
Cdd:PRK06839 320 GKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEETIQDGWLCTGDLARVDEDGFVYIVGRKKEMIIS 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 400 GGENVLPSEVENALAEHPLVDRCVVVGYDHPKYGESIAAAIILREDEPHYAEILNQHMRSRLAGYKVPRMYVPVTHMPLN 479
Cdd:PRK06839 400 GGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVLIEKDVIEHCRLFLAKYKIPKEIVFLKELPKN 479
|
490
....*....|....*..
gi 584959700 480 STQKPDKLAIRQMMNDK 496
Cdd:PRK06839 480 ATGKIQKAQLVNQLKSR 496
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
14-491 |
3.29e-105 |
|
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: 323.11 E-value: 3.29e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 14 DDKPAVIDHAKQTSWTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAA 93
Cdd:cd05926 1 PDAPALVVPGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 94 IVEDAQLKLLFY----------AEKHLSSLTdidQNLLHMD---IDVAQYDEIVN--PDYHQPFQATPVEPQDLAALIYT 158
Cdd:cd05926 81 YLADLGSKLVLTpkgelgpasrAASKLGLAI---LELALDVgvlIRAPSAESLSNllADKKNAKSEGVPLPDDLALILHT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 159 SGTTGSPKGVMFSYESFVHNGANLELTYKFNSNYITIVSTPMFHVLGFNDTVLPVLMSGGTLILQRYFNGEELNDMIAQY 238
Cdd:cd05926 158 SGTTGRPKGVPLTHRNLAASATNITNTYKLTPDDRTLVVMPLFHVHGLVASLLSTLAAGGSVVLPPRFSASTFWPDVRDY 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 239 HPTFIIMIPTMYYSTLRASNFNPENFRAMDYIIQGGSQPLP-----SIQAAFkqyGINIINGYGLTEA-PLVLVNTPENS 312
Cdd:cd05926 238 NATWYTAVPTIHQILLNRPEPNPESPPPKLRFIRSCSASLPpavleALEATF---GAPVLEAYGMTEAaHQMTSNPLPPG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 313 KRKPMSIGKAVMfVDARILDDNGEEVPTGEIGELAIKAKNVTPGYWNKPAETAK-AFHGRYLLTGDLAKMDNDGDIFIID 391
Cdd:cd05926 315 PRKPGSVGKPVG-VEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEaAFKDGWFRTGDLGYLDADGYLFLTG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 392 RKKELIITGGENVLPSEVENALAEHPLVDRCVVVGYDHPKYGESIAAAIILREDEPHYAEILNQHMRSRLAGYKVPRMYV 471
Cdd:cd05926 394 RIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGASVTEEELRAFCRKHLAAFKVPKKVY 473
|
490 500
....*....|....*....|
gi 584959700 472 PVTHMPLNSTQKPDKLAIRQ 491
Cdd:cd05926 474 FVDELPKTATGKIQRRKVAE 493
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
15-400 |
5.16e-105 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 320.03 E-value: 5.16e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 15 DKPAVIDHAKQTsWTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAAI 94
Cdd:pfam00501 10 DKTALEVGEGRR-LTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 95 VEDAQLKLLFYAEKHLSSLTDIDQNLLHMDIDVAQYD-----------EIVNPDYHQPFQATPVEPQDLAALIYTSGTTG 163
Cdd:pfam00501 89 LEDSGAKVLITDDALKLEELLEALGKLEVVKLVLVLDrdpvlkeeplpEEAKPADVPPPPPPPPDPDDLAYIIYTSGTTG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 164 SPKGVMFSYESFVHNGANLELTY----KFNSNYITIVSTPMFHVLGFNDTVLPVLMSGGTLILQRYFN---GEELNDMIA 236
Cdd:pfam00501 169 KPKGVMLTHRNLVANVLSIKRVRprgfGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVVLPPGFPaldPAALLELIE 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 237 QYHPTFIIMIPTMYYSTLRASNFNPENFRAMDYIIQGGSQPLPSIQAAFKQ-YGINIINGYGLTEA--PLVLVNTPENSK 313
Cdd:pfam00501 249 RYKVTVLYGVPTLLNMLLEAGAPKRALLSSLRLVLSGGAPLPPELARRFRElFGGALVNGYGLTETtgVVTTPLPLDEDL 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 314 RKPMSIGKAVMFVDARILDDN-GEEVPTGEIGELAIKAKNVTPGYWNKPAETAKAF-HGRYLLTGDLAKMDNDGDIFIID 391
Cdd:pfam00501 329 RSLGSVGRPLPGTEVKIVDDEtGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFdEDGWYRTGDLGRRDEDGYLEIVG 408
|
....*....
gi 584959700 392 RKKELIITG 400
Cdd:pfam00501 409 RKKDQIKLG 417
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
15-492 |
8.14e-100 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 309.53 E-value: 8.14e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 15 DKPAVIDHAKQTswTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAAI 94
Cdd:PRK07656 20 DKEAYVFGDQRL--TYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADEAAYI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 95 VEDAQLKLLFYAEKHLSSLTDIDQNLLHMDIDVAQYDEIVNPDY-------------HQPFQATPVEPQDLAALIYTSGT 161
Cdd:PRK07656 98 LARGDAKALFVLGLFLGVDYSATTRLPALEHVVICETEEDDPHTekmktftdflaagDPAERAPEVDPDDVADILFTSGT 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 162 TGSPKGVMFSYESFVHN----GANLELTYkfNSNYITIvsTPMFHVLGFNDTVLPVLMSGGTLILQRYFNGEELNDMIAQ 237
Cdd:PRK07656 178 TGRPKGAMLTHRQLLSNaadwAEYLGLTE--GDRYLAA--NPFFHVFGYKAGVNAPLMRGATILPLPVFDPDEVFRLIET 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 238 YHPTFIIMIPTMYYSTLRASNFNPENFRAMDYIIQGG-SQPLPSIQAAFKQYGINII-NGYGLTEA-PLVLVNTPENS-K 313
Cdd:PRK07656 254 ERITVLPGPPTMYNSLLQHPDRSAEDLSSLRLAVTGAaSMPVALLERFESELGVDIVlTGYGLSEAsGVTTFNRLDDDrK 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 314 RKPMSIGKAVMFVDARILDDNGEEVPTGEIGELAIKAKNVTPGYWNKPAETAKAFHGR-YLLTGDLAKMDNDGDIFIIDR 392
Cdd:PRK07656 334 TVAGTIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDDPEATAAAIDADgWLHTGDLGRLDEEGYLYIVDR 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 393 KKELIITGGENVLPSEVENALAEHPLVDRCVVVGYDHPKYGESIAAAIILREDEPHYAEILNQHMRSRLAGYKVPRMYVP 472
Cdd:PRK07656 414 KKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVLKPGAELTEEELIAYCREHLAKYKVPRSIEF 493
|
490 500
....*....|....*....|
gi 584959700 473 VTHMPLNSTQKPDKLAIRQM 492
Cdd:PRK07656 494 LDELPKNATGKVLKRALREK 513
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
15-491 |
3.13e-99 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 308.40 E-value: 3.13e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 15 DKPAVIDhaKQTSWTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAAI 94
Cdd:PRK08316 26 DKTALVF--GDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 95 VEDAQLKLLF-------YAEKHLSSLTDIDQNLLHMDIDVAQYDEIVNPDYHQPFQATPvEPQ------DLAALIYTSGT 161
Cdd:PRK08316 104 LDHSGARAFLvdpalapTAEAALALLPVDTLILSLVLGGREAPGGWLDFADWAEAGSVA-EPDveladdDLAQILYTSGT 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 162 TGSPKGVMFSYESFVHNGANLELTYKFNSNYITIVSTPMFHVLGFNDTVLPVLMSGGTLILQRYFNGEELNDMIAQYHPT 241
Cdd:PRK08316 183 ESLPKGAMLTHRALIAEYVSCIVAGDMSADDIPLHALPLYHCAQLDVFLGPYLYVGATNVILDAPDPELILRTIEAERIT 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 242 FIIMIPTMYYSTLRASNFNPENFRAMDYIIQGGS----QPLPSIQAAFKqyGINIINGYGLTE-APLVLVNTPENSKRKP 316
Cdd:PRK08316 263 SFFAPPTVWISLLRHPDFDTRDLSSLRKGYYGASimpvEVLKELRERLP--GLRFYNCYGQTEiAPLATVLGPEEHLRRP 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 317 MSIGKAVMFVDARILDDNGEEVPTGEIGELAIKAKNVTPGYWNKPAETAKAFHGRYLLTGDLAKMDNDGDIFIIDRKKEL 396
Cdd:PRK08316 341 GSAGRPVLNVETRVVDDDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEAFRGGWFHSGDLGVMDEEGYITVVDRKKDM 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 397 IITGGENVLPSEVENALAEHPLVDRCVVVGYDHPKYGESIAAAIILREDEPHYAEILNQHMRSRLAGYKVPRMYVPVTHM 476
Cdd:PRK08316 421 IKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAGATVTEDELIAHCRARLAGFKVPKRVIFVDEL 500
|
490
....*....|....*
gi 584959700 477 PLNSTQKPDKLAIRQ 491
Cdd:PRK08316 501 PRNPSGKILKRELRE 515
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
15-490 |
3.88e-99 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 307.12 E-value: 3.88e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 15 DKPAVIDHAKQTSWTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAAI 94
Cdd:PRK09088 10 QRLAAVDLALGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDAL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 95 VEDAQLKLLFyAEKHLSSLTDIDqnllhmdIDVAQYdeIVNPDYHQPFQATPVEPQDLAALIYTSGTTGSPKGVMFSYES 174
Cdd:PRK09088 90 LQDAEPRLLL-GDDAVAAGRTDV-------EDLAAF--IASADALEPADTPSIPPERVSLILFTSGTSGQPKGVMLSERN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 175 FVHNGANLELTYKFNSNYITIVSTPMFHVLGFNDTVLPVLMSGGTLILQRYFNGEELNDMIAQyhPTFIIM----IPTMY 250
Cdd:PRK09088 160 LQQTAHNFGVLGRVDAHSSFLCDAPMFHIIGLITSVRPVLAVGGSILVSNGFEPKRTLGRLGD--PALGIThyfcVPQMA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 251 YSTLRASNFNPENFRAMDYIIQGGS-QPLPSIQAAFKQyGINIINGYGLTEAPLVLvNTPENSKR---KPMSIGKAVMFV 326
Cdd:PRK09088 238 QAFRAQPGFDAAALRHLTALFTGGApHAAEDILGWLDD-GIPMVDGFGMSEAGTVF-GMSVDCDViraKAGAAGIPTPTV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 327 DARILDDNGEEVPTGEIGELAIKAKNVTPGYWNKPAETAKAFHGR-YLLTGDLAKMDNDGDIFIIDRKKELIITGGENVL 405
Cdd:PRK09088 316 QTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFTGDgWFRTGDIARRDADGFFWVVDRKKDMFISGGENVY 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 406 PSEVENALAEHPLVDRCVVVGYDHPKYGESIAAAIILREDEPHYAEILNQHMRSRLAGYKVPRMYVPVTHMPLNSTQKPD 485
Cdd:PRK09088 396 PAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADGAPLDLERIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQ 475
|
....*
gi 584959700 486 KLAIR 490
Cdd:PRK09088 476 KARLR 480
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
5-483 |
3.06e-96 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 299.57 E-value: 3.06e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 5 WIKTRSDFDDDKPAVIDhaKQTSWTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNW 84
Cdd:PRK03640 7 WLKQRAFLTPDRTAIEF--EEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 85 RLNPKEIAAIVEDAQLKLLFYAEKHLSSLTDIDQnllhmdidvAQYDEIVNPDYHQPfqaTPVEPQDL---AALIYTSGT 161
Cdd:PRK03640 85 RLSREELLWQLDDAEVKCLITDDDFEAKLIPGIS---------VKFAELMNGPKEEA---EIQEEFDLdevATIMYTSGT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 162 TGSPKGVMFSYE----SFVHNGANLELTYkfNSNYITIVstPMFHVLGFNdTVLPVLMSGGTLILQRYFNGEELNDMIAQ 237
Cdd:PRK03640 153 TGKPKGVIQTYGnhwwSAVGSALNLGLTE--DDCWLAAV--PIFHISGLS-ILMRSVIYGMRVVLVEKFDAEKINKLLQT 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 238 YHPTFIIMIPTMYYSTL-RASNFN-PENFRAMdyIIQGGSQPLPSIQAAfKQYGINIINGYGLTE-APLVLVNTPENSKR 314
Cdd:PRK03640 228 GGVTIISVVSTMLQRLLeRLGEGTyPSSFRCM--LLGGGPAPKPLLEQC-KEKGIPVYQSYGMTEtASQIVTLSPEDALT 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 315 KPMSIGKAVMFVDARILDDnGEEVPTGEIGELAIKAKNVTPGYWNKPAETAKAFHGRYLLTGDLAKMDNDGDIFIIDRKK 394
Cdd:PRK03640 305 KLGSAGKPLFPCELKIEKD-GVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQDGWFKTGDIGYLDEEGFLYVLDRRS 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 395 ELIITGGENVLPSEVENALAEHPLVDRCVVVGYDHPKYGESIAAAIILreDEPHYAEILNQHMRSRLAGYKVPRMYVPVT 474
Cdd:PRK03640 384 DLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVK--SGEVTEEELRHFCEEKLAKYKVPKRFYFVE 461
|
....*....
gi 584959700 475 HMPLNSTQK 483
Cdd:PRK03640 462 ELPRNASGK 470
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
28-486 |
6.56e-95 |
|
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: 294.20 E-value: 6.56e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 28 WTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAAIVEDAQLKLLFYae 107
Cdd:cd05934 4 WTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 108 khlssltdidqnllhmdidvaqydeivnpdyhqpfqatpvepqDLAALIYTSGTTGSPKGVMFSYESFVHNGANLELTYK 187
Cdd:cd05934 82 -------------------------------------------DPASILYTSGTTGPPKGVVITHANLTFAGYYSARRFG 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 188 FNSNYITIVSTPMFHVLGFNDTVLPVLMSGGTLILQRYFNGEELNDMIAQYHPT---FIIMIPTMYYSTLRASNFNPENF 264
Cdd:cd05934 119 LGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLLPRFSASRFWSDVRRYGATvtnYLGAMLSYLLAQPPSPDDRAHRL 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 265 RAMdyiiqGGSQPLPSIQAAF-KQYGINIINGYGLTEAPLVLVNTPEnSKRKPMSIGKAVMFVDARILDDNGEEVPTGEI 343
Cdd:cd05934 199 RAA-----YGAPNPPELHEEFeERFGVRLLEGYGMTETIVGVIGPRD-EPRRPGSIGRPAPGYEVRIVDDDGQELPAGEP 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 344 GELAIKA---KNVTPGYWNKPAETAKAFHGRYLLTGDLAKMDNDGDIFIIDRKKELIITGGENVLPSEVENALAEHPLVD 420
Cdd:cd05934 273 GELVIRGlrgWGFFKGYYNMPEATAEAMRNGWFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVR 352
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 584959700 421 RCVVVGYDHPKYGESIAAAIILREDEPHYAEILNQHMRSRLAGYKVPRmYVP-VTHMPLNSTQKPDK 486
Cdd:cd05934 353 EAAVVAVPDEVGEDEVKAVVVLRPGETLDPEELFAFCEGQLAYFKVPR-YIRfVDDLPKTPTEKVAK 418
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
15-488 |
4.72e-92 |
|
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: 287.50 E-value: 4.72e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 15 DKPAVIDHakQTSWTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAAI 94
Cdd:cd05930 2 DAVAVVDG--DQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 95 VEDAQLKLLfyaekhlssLTDidqnllhmdidvaqydeivnpdyhqpfqatpvePQDLAALIYTSGTTGSPKGVMFSYES 174
Cdd:cd05930 80 LEDSGAKLV---------LTD---------------------------------PDDLAYVIYTSGSTGKPKGVMVEHRG 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 175 FVHNGANLELTYKFNSNYITIVSTPmfhvLGFNDTV---LPVLMSGGTLIL---QRYFNGEELNDMIAQYHPTFIIMIPT 248
Cdd:cd05930 118 LVNLLLWMQEAYPLTPGDRVLQFTS----FSFDVSVweiFGALLAGATLVVlpeEVRKDPEALADLLAEEGITVLHLTPS 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 249 MYYSTLRASNfnPENFRAMDYIIQGGSQPLPSIQAAFKQY--GINIINGYGLTEA---PLVLVNTPENSKRKPMSIGKAV 323
Cdd:cd05930 194 LLRLLLQELE--LAALPSLRLVLVGGEALPPDLVRRWRELlpGARLVNLYGPTEAtvdATYYRVPPDDEEDGRVPIGRPI 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 324 MFVDARILDDNGEEVPTGEIGELAIKAKNVTPGYWNKPAETAKAF-------HGRYLLTGDLAKMDNDGDIFIIDRKKEL 396
Cdd:cd05930 272 PNTRVYVLDENLRPVPPGVPGELYIGGAGLARGYLNRPELTAERFvpnpfgpGERMYRTGDLVRWLPDGNLEFLGRIDDQ 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 397 IITGGENVLPSEVENALAEHPLVDRCVVVGYDHPKYGESIAAAIILREDEPHYAEILNQHMRSRLAGYKVPRMYVPVTHM 476
Cdd:cd05930 352 VKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEGGELDEEELRAHLAERLPDYMVPSAFVVLDAL 431
|
490
....*....|..
gi 584959700 477 PLNSTQKPDKLA 488
Cdd:cd05930 432 PLTPNGKVDRKA 443
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
15-490 |
4.50e-89 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 282.26 E-value: 4.50e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 15 DKPAVIDhaKQTSWTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAAI 94
Cdd:PRK06188 27 DRPALVL--GDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHPLGSLDDHAYV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 95 VEDAQLKLLF-----YAEKHLSSLTDIDqNLLHM----------DIdVAQYDeivnpdyhqPFQATPVE----PQDLAAL 155
Cdd:PRK06188 105 LEDAGISTLIvdpapFVERALALLARVP-SLKHVltlgpvpdgvDL-LAAAA---------KFGPAPLVaaalPPDIAGL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 156 IYTSGTTGSPKGVMFSYESFVHNGANLELTYKFNSNYITIVSTPMFHVLGFndTVLPVLMSGGTLILQRYFNGEELNDMI 235
Cdd:PRK06188 174 AYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLSHAGGA--FFLPTLLRGGTVIVLAKFDPAEVLRAI 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 236 AQYHPTFIIMIPTMYYSTLRASNFNPENFRAMDYIIQGGSQPLPS-IQAAFKQYGINIINGYGLTEAPLVLV------NT 308
Cdd:PRK06188 252 EEQRITATFLVPTMIYALLDHPDLRTRDLSSLETVYYGASPMSPVrLAEAIERFGPIFAQYYGQTEAPMVITylrkrdHD 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 309 PENSKRKpMSIGKAVMFVDARILDDNGEEVPTGEIGELAIKAKNVTPGYWNKPAETAKAFHGRYLLTGDLAKMDNDGDIF 388
Cdd:PRK06188 332 PDDPKRL-TSCGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAFRDGWLHTGDVAREDEDGFYY 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 389 IIDRKKELIITGGENVLPSEVENALAEHPLVDRCVVVGYDHPKYGESIAAAIILREDEPHYAEILNQHMRSRLAGYKVPR 468
Cdd:PRK06188 411 IVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRPGAAVDAAELQAHVKERKGSVHAPK 490
|
490 500
....*....|....*....|..
gi 584959700 469 MYVPVTHMPLNSTQKPDKLAIR 490
Cdd:PRK06188 491 QVDFVDSLPLTALGKPDKKALR 512
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
29-491 |
1.28e-87 |
|
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: 278.36 E-value: 1.28e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 29 TYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAAIVEDAQLKLLFYAE- 107
Cdd:cd12119 27 TYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAEDRVVFVDRd 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 108 ---------------KHLSSLTDIDQNLLHMDIDVAQYDEIVN---PDYHQPfqatPVEPQDLAALIYTSGTTGSPKGVM 169
Cdd:cd12119 107 flplleaiaprlptvEHVVVMTDDAAMPEPAGVGVLAYEELLAaesPEYDWP----DFDENTAAAICYTSGTTGNPKGVV 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 170 FSYESFVHN--GANLELTYKFNSNYITIVSTPMFHVLGFNdtvLP--VLMSGGTLIL-QRYFNGEELNDMIAQYHPTFII 244
Cdd:cd12119 183 YSHRSLVLHamAALLTDGLGLSESDVVLPVVPMFHVNAWG---LPyaAAMVGAKLVLpGPYLDPASLAELIEREGVTFAA 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 245 MIPTMYYSTLRASNFNPENFRAMDYIIQGGSQPLPSIQAAFKQYGINIINGYGLTEA-PLVLVNTPENSKRKP------- 316
Cdd:cd12119 260 GVPTVWQGLLDHLEANGRDLSSLRRVVIGGSAVPRSLIEAFEERGVRVIHAWGMTETsPLGTVARPPSEHSNLsedeqla 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 317 --MSIGKAVMFVDARILDDNGEEVP-TGE-IGELAIKAKNVTPGYWNKPAETAKAFHGRYLLTGDLAKMDNDGDIFIIDR 392
Cdd:cd12119 340 lrAKQGRPVPGVELRIVDDDGRELPwDGKaVGELQVRGPWVTKSYYKNDEESEALTEDGWLRTGDVATIDEDGYLTITDR 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 393 KKELIITGGENVLPSEVENALAEHPLVDRCVVVGYDHPKYGESIAAAIILREDEPHYAEILNQHMRSRLAGYKVPRMYVP 472
Cdd:cd12119 420 SKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLKEGATVTAEELLEFLADKVAKWWLPDDVVF 499
|
490
....*....|....*....
gi 584959700 473 VTHMPLNSTQKPDKLAIRQ 491
Cdd:cd12119 500 VDEIPKTSTGKIDKKALRE 518
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
15-494 |
3.94e-87 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 276.38 E-value: 3.94e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 15 DKPAVIDHAKQTSwtYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAAI 94
Cdd:PRK06145 17 DRAALVYRDQEIS--YAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 95 VEDAQLKLLFYAEKHlssltDIDQNLLHMDI---DVAQYDEIVNPDYHQPF-QATPVEPQDLAALIYTSGTTGSPKGVMF 170
Cdd:PRK06145 95 LGDAGAKLLLVDEEF-----DAIVALETPKIvidAAAQADSRRLAQGGLEIpPQAAVAPTDLVRLMYTSGTTDRPKGVMH 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 171 SYESFVHNGANLELTYKFNSNYITIVSTPMFHVLGFNDTVLPVLMSGGTLILQRYFNGEELNDMIAQYHPTFIIMIPTMY 250
Cdd:PRK06145 170 SYGNLHWKSIDHVIALGLTASERLLVVGPLYHVGAFDLPGIAVLWVGGTLRIHREFDPEAVLAAIERHRLTCAWMAPVML 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 251 YSTLRASNFNPENFRAMDYIIQGGSQPLPSIQAAFKQY--GINIINGYGLTEAplVLVNTPENSKR---KPMSIGKAVMF 325
Cdd:PRK06145 250 SRVLTVPDRDRFDLDSLAWCIGGGEKTPESRIRDFTRVftRARYIDAYGLTET--CSGDTLMEAGReieKIGSTGRALAH 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 326 VDARILDDNGEEVPTGEIGELAIKAKNVTPGYWNKPAETAKAFHGRYLLTGDLAKMDNDGDIFIIDRKKELIITGGENVL 405
Cdd:PRK06145 328 VEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGDWFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIA 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 406 PSEVENALAEHPLVDRCVVVGYDHPKYGESIAAAIILREDEPHYAEILNQHMRSRLAGYKVPRMYVPVTHMPLNSTQKPD 485
Cdd:PRK06145 408 SSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPGATLTLEALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVL 487
|
....*....
gi 584959700 486 KLAIRQMMN 494
Cdd:PRK06145 488 KRVLRDELN 496
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
13-496 |
5.32e-87 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 278.15 E-value: 5.32e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 13 DDDKPAVI---DHAKQTSWTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPK 89
Cdd:COG0365 22 RGDKVALIwegEDGEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPVFPGFGAE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 90 EIAAIVEDAQLKLLF------YAEKHLSSLTDIDQNL------------------LHMDIDVAqYDEIVnPDYHQPFQAT 145
Cdd:COG0365 102 ALADRIEDAEAKVLItadgglRGGKVIDLKEKVDEALeelpslehvivvgrtgadVPMEGDLD-WDELL-AAASAEFEPE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 146 PVEPQDLAALIYTSGTTGSPKGVmfsyesfVHnganleltykFNSNYITIVSTPMFHVLGFNDT---------------- 209
Cdd:COG0365 180 PTDADDPLFILYTSGTTGKPKGV-------VH----------THGGYLVHAATTAKYVLDLKPGdvfwctadigwatghs 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 210 --VLPVLMSGGTLIL----QRYFNGEELNDMIAQYHPTFIIMIPTMYYSTLRASNFNPE--NFRAMDYIIQGGSqPLP-- 279
Cdd:COG0365 243 yiVYGPLLNGATVVLyegrPDFPDPGRLWELIEKYGVTVFFTAPTAIRALMKAGDEPLKkyDLSSLRLLGSAGE-PLNpe 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 280 SIQAAFKQYGINIINGYGLTEAPLVLVNTPENSKRKPMSIGKAVMFVDARILDDNGEEVPTGEIGELAIKAKN--VTPGY 357
Cdd:COG0365 322 VWEWWYEAVGVPIVDGWGQTETGGIFISNLPGLPVKPGSMGKPVPGYDVAVVDEDGNPVPPGEEGELVIKGPWpgMFRGY 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 358 WNKPAETAKAFHGRYL---LTGDLAKMDNDGDIFIIDRKKELIITGGENVLPSEVENALAEHPLVDRCVVVGYDHPKYGE 434
Cdd:COG0365 402 WNDPERYRETYFGRFPgwyRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVGVPDEIRGQ 481
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 584959700 435 SIAAAIILREDEPHYAEI---LNQHMRSRLAGYKVPRMYVPVTHMPLNSTQKPDKLAIRQMMNDK 496
Cdd:COG0365 482 VVKAFVVLKPGVEPSDELakeLQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLRKIAEGR 546
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
18-465 |
6.76e-87 |
|
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: 275.25 E-value: 6.76e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 18 AVIDHAKQTSWTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAAIVED 97
Cdd:cd05911 1 AQIDADTGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 98 AQLKLLFYAEKHLSSLTDIDQNL------------LHMDIDVAQYDEIVNPDYHQPFQATPVE-PQDLAALIYTSGTTGS 164
Cdd:cd05911 81 SKPKVIFTDPDGLEKVKEAAKELgpkdkiivlddkPDGVLSIEDLLSPTLGEEDEDLPPPLKDgKDDTAAILYSSGTTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 165 PKGVMFSYESFVhngANLELTYKF-----NSNYITIVSTPMFHVLGFNdTVLPVLMSGGTLILQRYFNGEELNDMIAQYH 239
Cdd:cd05911 161 PKGVCLSHRNLI---ANLSQVQTFlygndGSNDVILGFLPLYHIYGLF-TTLASLLNGATVIIMPKFDSELFLDLIEKYK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 240 PTFIIMIPTMYYSTLRASNFNPENFRAMDYIIQGGSQPLPSIQAAFKQYGIN--IINGYGLTEAPLVLVNTPENSKrKPM 317
Cdd:cd05911 237 ITFLYLVPPIAAALAKSPLLDKYDLSSLRVILSGGAPLSKELQELLAKRFPNatIKQGYGMTETGGILTVNPDGDD-KPG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 318 SIGKAVMFVDARILDDNG-EEVPTGEIGELAIKAKNVTPGYWNKPAETAKAF-HGRYLLTGDLAKMDNDGDIFIIDRKKE 395
Cdd:cd05911 316 SVGRLLPNVEAKIVDDDGkDSLGPNEPGEICVRGPQVMKGYYNNPEATKETFdEDGWLHTGDIGYFDEDGYLYIVDRKKE 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 396 LIITGGENVLPSEVENALAEHPLVDRCVVVGYDHPKYGESIAAAIILREDEPHYAEILNQHMRSRLAGYK 465
Cdd:cd05911 396 LIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGEKLTEKEVKDYVAKKVASYK 465
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
27-483 |
1.99e-84 |
|
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: 266.52 E-value: 1.99e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 27 SWTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAAIVEDAQlkllfya 106
Cdd:cd05912 1 SYTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSD------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 107 ekhlssltdidqnllhmdidvAQYDEIvnpdyhqpfqatpvepqdlAALIYTSGTTGSPKGVMFSYE----SFVHNGANL 182
Cdd:cd05912 74 ---------------------VKLDDI-------------------ATIMYTSGTTGKPKGVQQTFGnhwwSAIGSALNL 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 183 ELTYkfNSNYITIVstPMFHVLGFNdTVLPVLMSGGTLILQRYFNGEELNDMIAQYHPTFIIMIPTMYYSTL-RASNFNP 261
Cdd:cd05912 114 GLTE--DDNWLCAL--PLFHISGLS-ILMRSVIYGMTVYLVDKFDAEQVLHLINSGKVTIISVVPTMLQRLLeILGEGYP 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 262 ENFRAMdyIIQGGSQPLPSIQAAfKQYGINIINGYGLTE-APLVLVNTPENSKRKPMSIGKAVMFVDARILDDNGEEvpt 340
Cdd:cd05912 189 NNLRCI--LLGGGPAPKPLLEQC-KEKGIPVYQSYGMTEtCSQIVTLSPEDALNKIGSAGKPLFPVELKIEDDGQPP--- 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 341 GEIGELAIKAKNVTPGYWNKPAETAKAFHGRYLLTGDLAKMDNDGDIFIIDRKKELIITGGENVLPSEVENALAEHPLVD 420
Cdd:cd05912 263 YEVGEILLKGPNVTKGYLNRPDATEESFENGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIK 342
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 584959700 421 RCVVVGYDHPKYGESIAAAIILreDEPHYAEILNQHMRSRLAGYKVPRMYVPVTHMPLNSTQK 483
Cdd:cd05912 343 EAGVVGIPDDKWGQVPVAFVVS--ERPISEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGK 403
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
17-490 |
2.56e-83 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 266.77 E-value: 2.56e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 17 PAVIDHAKQTSWTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAAIVE 96
Cdd:PRK08276 1 PAVIMAPSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 97 DAQLKLLFYAEK------HLSSLTDIDQNLLHMDI----DVAQYDEIVNPdyhQPfqATPVEPQDL-AALIYTSGTTGSP 165
Cdd:PRK08276 81 DSGAKVLIVSAAladtaaELAAELPAGVPLLLVVAgpvpGFRSYEEALAA---QP--DTPIADETAgADMLYSSGTTGRP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 166 KGVMfsyESFVHNG---------ANLELTYKFNSNYITIVSTPMFH--VLGFNDTVLpvlMSGGTLILQRYFNGEELNDM 234
Cdd:PRK08276 156 KGIK---RPLPGLDpdeapgmmlALLGFGMYGGPDSVYLSPAPLYHtaPLRFGMSAL---ALGGTVVVMEKFDAEEALAL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 235 IAQYHPTFIIMIPTMYYSTLRAsnfnPENFRA------MDYIIQGGSQ-PLPSIQAAFKQYGINIINGYGLTEAPLVLVN 307
Cdd:PRK08276 230 IERYRVTHSQLVPTMFVRMLKL----PEEVRArydvssLRVAIHAAAPcPVEVKRAMIDWWGPIIHEYYASSEGGGVTVI 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 308 TPENSKRKPMSIGKAVMFVdARILDDNGEEVPTGEIGELAIKAKNVTPGYWNKPAETAKAFHGRYLLT-GDLAKMDNDGD 386
Cdd:PRK08276 306 TSEDWLAHPGSVGKAVLGE-VRILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARNPHGWVTvGDVGYLDEDGY 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 387 IFIIDRKKELIITGGENVLPSEVENALAEHPLVDRCVVVGYDHPKYGESIAAAIILR---EDEPHYAEILNQHMRSRLAG 463
Cdd:PRK08276 385 LYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKAVVQPAdgaDAGDALAAELIAWLRGRLAH 464
|
490 500
....*....|....*....|....*..
gi 584959700 464 YKVPRMYVPVTHMPLNSTQKPDKLAIR 490
Cdd:PRK08276 465 YKCPRSIDFEDELPRTPTGKLYKRRLR 491
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
15-483 |
7.29e-82 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 264.13 E-value: 7.29e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 15 DKPAVIDHAkqTSWTYQQLNARADNMAHYLTSQ-GVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAA 93
Cdd:PRK08314 25 DKTAIVFYG--RAISYRELLEEAERLAGYLQQEcGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAH 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 94 IVEDAQLKLLF----YAEK--HLSSLTDIDQNLLHMDID-VAQYDEIVNPDYHQ---PFQATP----------------- 146
Cdd:PRK08314 103 YVTDSGARVAIvgseLAPKvaPAVGNLRLRHVIVAQYSDyLPAEPEIAVPAWLRaepPLQALApggvvawkealaaglap 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 147 ----VEPQDLAALIYTSGTTGSPKGVMFSYESFVHNGANLELTYKFNSNYITIVSTPMFHVLGFNDTVLPVLMSGGTLIL 222
Cdd:PRK08314 183 pphtAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVLPLFHVTGMVHSMNAPIYAGATVVL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 223 QRYFNGEELNDMIAQYHPTFIIMIPTMYYSTLRASNFNPENFRAMDYIiQGGSQPLPsiQAA----FKQYGINIINGYGL 298
Cdd:PRK08314 263 MPRWDREAAARLIERYRVTHWTNIPTMVVDFLASPGLAERDLSSLRYI-GGGGAAMP--EAVaerlKELTGLDYVEGYGL 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 299 TE--APLvLVNTPENSKRKPMSIgkAVMFVDARILD-DNGEEVPTGEIGELAIKAKNVTPGYWNKPAETAKAF---HG-R 371
Cdd:PRK08314 340 TEtmAQT-HSNPPDRPKLQCLGI--PTFGVDARVIDpETLEELPPGEVGEIVVHGPQVFKGYWNRPEATAEAFieiDGkR 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 372 YLLTGDLAKMDNDGDIFIIDRKKELIITGGENVLPSEVENALAEHPLVDRCVVVGYDHPKYGESIAAAIILRedePHY-- 449
Cdd:PRK08314 417 FFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPDPRRGETVKAVVVLR---PEArg 493
|
490 500 510
....*....|....*....|....*....|....*..
gi 584959700 450 ---AEILNQHMRSRLAGYKVPRMYVPVTHMPLNSTQK 483
Cdd:PRK08314 494 kttEEEIIAWAREHMAAYKYPRIVEFVDSLPKSGSGK 530
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
4-491 |
4.58e-81 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 262.02 E-value: 4.58e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 4 DWIKTRSDFDDDKPAVIDHAKQTSWtyQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLN 83
Cdd:PRK07786 21 NQLARHALMQPDAPALRFLGNTTTW--RELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 84 WRLNPKEIAAIVEDAQLKLLFyAEKHLSSLT----DIDQNLLHM-------DIDVAQYDEIVNPDYHQPfqaTPVE-PQD 151
Cdd:PRK07786 99 FRLTPPEIAFLVSDCGAHVVV-TEAALAPVAtavrDIVPLLSTVvvaggssDDSVLGYEDLLAEAGPAH---APVDiPND 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 152 LAALI-YTSGTTGSPKGVMFSYESFVHNGANLELTYKFNSNY-ITIVSTPMFHVLGFNdTVLPVLMSGGTLILQ--RYFN 227
Cdd:PRK07786 175 SPALImYTSGTTGRPKGAVLTHANLTGQAMTCLRTNGADINSdVGFVGVPLFHIAGIG-SMLPGLLLGAPTVIYplGAFD 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 228 GEELNDMIAQYHPTFIIMIPTMYYSTLRASNFNPENFRAMdyIIQGGSQP-----LPSIQAAFKqyGINIINGYGLTE-A 301
Cdd:PRK07786 254 PGQLLDVLEAEKVTGIFLVPAQWQAVCAEQQARPRDLALR--VLSWGAAPasdtlLRQMAATFP--EAQILAAFGQTEmS 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 302 PLVLVNTPENSKRKPMSIGKAVMFVDARILDDNGEEVPTGEIGELAIKAKNVTPGYWNKPAETAKAFHGRYLLTGDLAKM 381
Cdd:PRK07786 330 PVTCMLLGEDAIRKLGSVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFAGGWFHSGDLVRQ 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 382 DNDGDIFIIDRKKELIITGGENVLPSEVENALAEHPLVDRCVVVGYDHPKYGESIAAAIILREDEPHYA-EILNQHMRSR 460
Cdd:PRK07786 410 DEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRNDDAALTlEDLAEFLTDR 489
|
490 500 510
....*....|....*....|....*....|.
gi 584959700 461 LAGYKVPRMYVPVTHMPLNSTQKPDKLAIRQ 491
Cdd:PRK07786 490 LARYKHPKALEIVDALPRNPAGKVLKTELRE 520
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
15-490 |
1.68e-80 |
|
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: 258.77 E-value: 1.68e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 15 DKPAVIDHAkqTSWTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAAI 94
Cdd:cd12118 19 DRTSIVYGD--RRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 95 VEDAQLKLLFyaekhlssltdIDQNLlhmdidvaQYDEIV---NPDYH-QPfqatPVEPQDLAALIYTSGTTGSPKGVMF 170
Cdd:cd12118 97 LRHSEAKVLF-----------VDREF--------EYEDLLaegDPDFEwIP----PADEWDPIALNYTSGTTGRPKGVVY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 171 SyesfvHNGANL-------ELTYKFNSNYITIVstPMFHVLGFndtVLP--VLMSGGTLILQRYFNGEELNDMIAQYHPT 241
Cdd:cd12118 154 H-----HRGAYLnalanilEWEMKQHPVYLWTL--PMFHCNGW---CFPwtVAAVGGTNVCLRKVDAKAIYDLIEKHKVT 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 242 FIIMIPTMYySTLraSNFNPENFRAMDYIIQ---GGSQPLPSIQAAFKQYGINIINGYGLTEA-PLVLVN---------- 307
Cdd:cd12118 224 HFCGAPTVL-NML--ANAPPSDARPLPHRVHvmtAGAPPPAAVLAKMEELGFDVTHVYGLTETyGPATVCawkpewdelp 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 308 TPENSKRK-----PMSIGKAVMFVDArildDNGEEVP-TGE-IGELAIKAKNVTPGYWNKPAETAKAFHGRYLLTGDLAK 380
Cdd:cd12118 301 TEERARLKarqgvRYVGLEEVDVLDP----ETMKPVPrDGKtIGEIVFRGNIVMKGYLKNPEATAEAFRGGWFHSGDLAV 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 381 MDNDGDIFIIDRKKELIITGGENVLPSEVENALAEHPLVDRCVVVGYDHPKYGESIAAAIILREDEPHYAEILNQHMRSR 460
Cdd:cd12118 377 IHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVELKEGAKVTEEEIIAFCREH 456
|
490 500 510
....*....|....*....|....*....|
gi 584959700 461 LAGYKVPRMYVpVTHMPLNSTQKPDKLAIR 490
Cdd:cd12118 457 LAGFMVPKTVV-FGELPKTSTGKIQKFVLR 485
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
29-483 |
2.97e-80 |
|
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: 256.61 E-value: 2.97e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 29 TYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAAIVEDAQLKLLFyaek 108
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLL---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 109 hlssltdIDQNLLHMDIDVAQYDEIVNPDYHQPFQATPVEPQDLAALIYTSGTTGSPKGVMFSYESFVHNGANLELTYKF 188
Cdd:TIGR01923 77 -------TDSLLEEKDFQADSLDRIEAAGRYETSLSASFNMDQIATLMFTSGTTGKPKAVPHTFRNHYASAVGSKENLGF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 189 NSNYITIVSTPMFHVLGFNdTVLPVLMSGGTLILQRYFNgeELNDMIAQYHPTFIIMIPTMYYSTLRASNfNPENFRAmd 268
Cdd:TIGR01923 150 TEDDNWLLSLPLYHISGLS-ILFRWLIEGATLRIVDKFN--QLLEMIANERVTHISLVPTQLNRLLDEGG-HNENLRK-- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 269 yIIQGGSQ-PLPSIQAAfKQYGINIINGYGLTE-APLVLVNTPENSKRKPmSIGKAVMFVDARILDDNGEEVptgeiGEL 346
Cdd:TIGR01923 224 -ILLGGSAiPAPLIEEA-QQYGLPIYLSYGMTEtCSQVTTATPEMLHARP-DVGRPLAGREIKIKVDNKEGH-----GEI 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 347 AIKAKNVTPGYW-NKPAETAKAFHGrYLLTGDLAKMDNDGDIFIIDRKKELIITGGENVLPSEVENALAEHPLVDRCVVV 425
Cdd:TIGR01923 296 MVKGANLMKGYLyQGELTPAFEQQG-WFNTGDIGELDGEGFLYVLGRRDDLIISGGENIYPEEIETVLYQHPGIQEAVVV 374
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 584959700 426 GYDHPKYGESIAAAIILREDEPhyAEILNQHMRSRLAGYKVPRMYVPVTHMPLNSTQK 483
Cdd:TIGR01923 375 PKPDAEWGQVPVAYIVSESDIS--QAKLIAYLTEKLAKYKVPIAFEKLDELPYNASGK 430
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
13-483 |
3.47e-79 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 256.99 E-value: 3.47e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 13 DDDKPAVIDHAKqtSWTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIA 92
Cdd:PRK13382 56 CPDRPGLIDELG--TLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPALA 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 93 AIVEDAQLKLLFYAEKHLSSL----------------TDIDQNLLHMDIdvaqydeIVNPDYHQPfqatPVEPQDLAALI 156
Cdd:PRK13382 134 EVVTREGVDTVIYDEEFSATVdraladcpqatrivawTDEDHDLTVEVL-------IAAHAGQRP----EPTGRKGRVIL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 157 YTSGTTGSPKGVMfsyesfvHNGANLELTYK-------FNSNYITIVSTPMFHVLGFNDTVLPVLMSGgTLILQRYFNGE 229
Cdd:PRK13382 203 LTSGTTGTPKGAR-------RSGPGGIGTLKaildrtpWRAEEPTVIVAPMFHAWGFSQLVLAASLAC-TIVTRRRFDPE 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 230 ELNDMIAQYHPTFIIMIPTMYYSTLR--ASNFNPENFRAMDYIIQGGSQPLPSIQAAF-KQYGINIINGYGLTEAPLVLV 306
Cdd:PRK13382 275 ATLDLIDRHRATGLAVVPVMFDRIMDlpAEVRNRYSGRSLRFAAASGSRMRPDVVIAFmDQFGDVIYNNYNATEAGMIAT 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 307 NTPENSKRKPMSIGKAVMFVDARILDDNGEEVPTGEIGELAIKAKNVTPGYwnkPAETAKAFHGRYLLTGDLAKMDNDGD 386
Cdd:PRK13382 355 ATPADLRAAPDTAGRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGY---TSGSTKDFHDGFMASGDVGYLDENGR 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 387 IFIIDRKKELIITGGENVLPSEVENALAEHPLVDRCVVVGYDHPKYGESIAAAIILREDEPHYAEILNQHMRSRLAGYKV 466
Cdd:PRK13382 432 LFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPGASATPETLKQHVRDNLANYKV 511
|
490
....*....|....*..
gi 584959700 467 PRMYVPVTHMPLNSTQK 483
Cdd:PRK13382 512 PRDIVVLDELPRGATGK 528
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
27-483 |
1.25e-78 |
|
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: 252.40 E-value: 1.25e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 27 SWTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAAIVEDAQLKLLfya 106
Cdd:cd05935 1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVA--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 107 ekhlssltdidqnLLHMDIDvaqydeivnpdyhqpfqatpvepqDLAALIYTSGTTGSPKGVMFSYESFVHNGANLELTY 186
Cdd:cd05935 78 -------------VVGSELD------------------------DLALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWT 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 187 KFNSNYITIVSTPMFHVLGFNDTVLPVLMSGGTLILQRYFNGEELNDMIAQYHPTFIIMIPTMYYSTLRASNFNPENFRA 266
Cdd:cd05935 121 GLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMARWDRETALELIEKYKVTFWTNIPTMLVDLLATPEFKTRDLSS 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 267 MdYIIQGGSQPLPS--IQAAFKQYGINIINGYGLTEA-PLVLVNTPENSKRKpmSIGKAVMFVDARILD-DNGEEVPTGE 342
Cdd:cd05935 201 L-KVLTGGGAPMPPavAEKLLKLTGLRFVEGYGLTETmSQTHTNPPLRPKLQ--CLGIP*FGVDARVIDiETGRELPPNE 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 343 IGELAIKAKNVTPGYWNKPAETAKAF----HGRYLLTGDLAKMDNDGDIFIIDRKKELIITGGENVLPSEVENALAEHPL 418
Cdd:cd05935 278 VGEIVVRGPQIFKGYWNRPEETEESFieikGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPA 357
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 419 VDRCVVVGYDHPKYGESIAAAIILRedePHY-----AEILNQHMRSRLAGYKVPRMYVPVTHMPLNSTQK 483
Cdd:cd05935 358 I*EVCVISVPDERVGEEVKAFIVLR---PEYrgkvtEEDIIEWAREQMAAYKYPREVEFVDELPRSASGK 424
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
10-451 |
4.06e-77 |
|
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: 250.61 E-value: 4.06e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 10 SDFDDDKPAVIDHAKQTSWTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPK 89
Cdd:cd05904 15 ASAHPSRPALIDAATGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 90 EIAAIVEDAQLKLLFYAEKHLSSLTDIDQNLLHMDIDVAQYDEIVNPDYHQPFQATPVE---PQDLAALIYTSGTTGSPK 166
Cdd:cd05904 95 EIAKQVKDSGAKLAFTTAELAEKLASLALPVVLLDSAEFDSLSFSDLLFEADEAEPPVVvikQDDVAALLYSSGTTGRSK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 167 GVMFSYESFVhngANLELTYKF---NSNY--ITIVSTPMFHVLGFNDTVLPVLMSGGTLILQRYFNGEELNDMIAQYHPT 241
Cdd:cd05904 175 GVMLTHRNLI---AMVAQFVAGegsNSDSedVFLCVLPMFHIYGLSSFALGLLRLGATVVVMPRFDLEELLAAIERYKVT 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 242 FIIMIPTMYYSTLRASNFNPENFRAMDYIIQGGSqPLPS-IQAAFKQY--GINIINGYGLTE--APLVLVNTPENSKRKP 316
Cdd:cd05904 252 HLPVVPPIVLALVKSPIVDKYDLSSLRQIMSGAA-PLGKeLIEAFRAKfpNVDLGQGYGMTEstGVVAMCFAPEKDRAKY 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 317 MSIGKAVMFVDARILD-DNGEEVPTGEIGELAIKAKNVTPGYWNKPAETAKAFHG-RYLLTGDLAKMDNDGDIFIIDRKK 394
Cdd:cd05904 331 GSVGRLVPNVEAKIVDpETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDKeGWLHTGDLCYIDEDGYLFIVDRLK 410
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 584959700 395 ELIITGGENVLPSEVENALAEHPLVDRCVVVGYDHPKYGEsIAAAIILREDEPHYAE 451
Cdd:cd05904 411 ELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGE-VPMAFVVRKPGSSLTE 466
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
26-451 |
4.05e-76 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 250.40 E-value: 4.05e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 26 TSWTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDI--AILDllFACFKTGAVFLPLNWRLNPKEIAAIVEDAQLKLL 103
Cdd:COG1022 39 QSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPewVIAD--LAILAAGAVTVPIYPTSSAEEVAYILNDSGAKVL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 104 F-----YAEKHLSSLTD---------IDQNLLHMDIDVAQYDEIV-------NPDYHQpFQATPVEPQDLAALIYTSGTT 162
Cdd:COG1022 117 FvedqeQLDKLLEVRDElpslrhivvLDPRGLRDDPRLLSLDELLalgrevaDPAELE-ARRAAVKPDDLATIIYTSGTT 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 163 GSPKGVMFSYESFVHNGANLELTYKFNSNYITIVSTPMFHVLGFNDTVLpVLMSGGTLILQRyfNGEELNDMIAQYHPTF 242
Cdd:COG1022 196 GRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFLPLAHVFERTVSYY-ALAAGATVAFAE--SPDTLAEDLREVKPTF 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 243 IIMIPTMY---YSTLRA----------SNFNpenfRAMD-------YIIQGGSQPL--------------PSIQAAF--- 285
Cdd:COG1022 273 MLAVPRVWekvYAGIQAkaeeagglkrKLFR----WALAvgrryarARLAGKSPSLllrlkhaladklvfSKLREALggr 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 286 KQY-------------------GINIINGYGLTE-APLVLVNTPEnsKRKPMSIGKAVMFVDARILDDngeevptgeiGE 345
Cdd:COG1022 349 LRFavsggaalgpelarffralGIPVLEGYGLTEtSPVITVNRPG--DNRIGTVGPPLPGVEVKIAED----------GE 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 346 LAIKAKNVTPGYWNKPAETAKAFH-GRYLLTGDLAKMDNDGDIFIIDRKKELIIT-GGENVLPSEVENALAEHPLVDRCV 423
Cdd:COG1022 417 ILVRGPNVMKGYYKNPEATAEAFDaDGWLHTGDIGELDEDGFLRITGRKKDLIVTsGGKNVAPQPIENALKASPLIEQAV 496
|
490 500
....*....|....*....|....*....
gi 584959700 424 VVGYDHPkygeSIAAAIILREDE-PHYAE 451
Cdd:COG1022 497 VVGDGRP----FLAALIVPDFEAlGEWAE 521
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
15-491 |
9.50e-76 |
|
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: 244.89 E-value: 9.50e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 15 DKPAVIDhaKQTSWTYQQLNARADNMAHYLTSQG-VKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAA 93
Cdd:cd05941 1 DRIAIVD--DGDSITYADLVARAARLANRLLALGkDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 94 IVEDAQLKLLFyaekhlssltdidqnllhmdidvaqydeivnpdyhqpfqatpvepqDLAALIYTSGTTGSPKGVMFSYE 173
Cdd:cd05941 79 VITDSEPSLVL----------------------------------------------DPALILYTSGTTGRPKGVVLTHA 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 174 SFVHNGANLELTYKFNSNYITIVSTPMFHVLGFNDTVLPVLMSGGTLILQRYFNGEELNDMIAQYHPTFIIMIPTMYyst 253
Cdd:cd05941 113 NLAANVRALVDAWRWTEDDVLLHVLPLHHVHGLVNALLCPLFAGASVEFLPKFDPKEVAISRLMPSITVFMGVPTIY--- 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 254 LRASNFNPENFRAMDYIIQG----------GSQPLP-SIQAAFKQ-YGINIINGYGLTEAPLVLVNtPENSKRKPMSIGK 321
Cdd:cd05941 190 TRLLQYYEAHFTDPQFARAAaaerlrlmvsGSAALPvPTLEEWEAiTGHTLLERYGMTEIGMALSN-PLDGERRPGTVGM 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 322 AVMFVDARILDDN-GEEVPTGEIGELAIKAKNVTPGYWNKPAETAKAFHG-RYLLTGDLAKMDNDGDIFIIDRKKELII- 398
Cdd:cd05941 269 PLPGVQARIVDEEtGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDdGWFKTGDLGVVDEDGYYWILGRSSVDIIk 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 399 TGGENVLPSEVENALAEHPLVDRCVVVGYDHPKYGESIAAAIILRED-EPHYAEILNQHMRSRLAGYKVPRMYVPVTHMP 477
Cdd:cd05941 349 SGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGaAALSLEELKEWAKQRLAPYKRPRRLILVDELP 428
|
490
....*....|....
gi 584959700 478 LNSTQKPDKLAIRQ 491
Cdd:cd05941 429 RNAMGKVNKKELRK 442
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
25-470 |
1.23e-75 |
|
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: 245.20 E-value: 1.23e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 25 QTSWTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDI--AILDllFACFKTGAVFLPLNWRLNPKEIAAIVEDAQLKL 102
Cdd:cd05907 3 WQPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPewTIAD--LAILAIGAVPVPIYPTSSAEQIAYILNDSEAKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 103 LFyaekhlssltdidqnllhmdidvaqydeivnpdyhqpfqatpVE-PQDLAALIYTSGTTGSPKGVMFSYESFVHNGAN 181
Cdd:cd05907 81 LF------------------------------------------VEdPDDLATIIYTSGTTGRPKGVMLSHRNILSNALA 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 182 LELTYKFNSNYITIVSTPMFHVLGFNDTVLPVLMSGGTLilqrYFNG--EELNDMIAQYHPTFIIMIPTMY---YSTLRA 256
Cdd:cd05907 119 LAERLPATEGDRHLSFLPLAHVFERRAGLYVPLLAGARI----YFASsaETLLDDLSEVRPTVFLAVPRVWekvYAAIKV 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 257 SNfNPENFRAM---------DYIIQGGSqPL-PSIQAAFKQYGINIINGYGLTE-APLVLVNTPEnsKRKPMSIGKAVMF 325
Cdd:cd05907 195 KA-VPGLKRKLfdlavggrlRFAASGGA-PLpAELLHFFRALGIPVYEGYGLTEtSAVVTLNPPG--DNRIGTVGKPLPG 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 326 VDARILDDngeevptgeiGELAIKAKNVTPGYWNKPAETAKAF-HGRYLLTGDLAKMDNDGDIFIIDRKKELIIT-GGEN 403
Cdd:cd05907 271 VEVRIADD----------GEILVRGPNVMLGYYKNPEATAEALdADGWLHTGDLGEIDEDGFLHITGRKKDLIITsGGKN 340
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 584959700 404 VLPSEVENALAEHPLVDRCVVVGyDHPKYgesIAAAIILREDE-PHYAEILNQHMRSRLAGYKVPRMY 470
Cdd:cd05907 341 ISPEPIENALKASPLISQAVVIG-DGRPF---LVALIVPDPEAlEAWAEEHGIAYTDVAELAANPAVR 404
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
3-491 |
3.55e-75 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 245.56 E-value: 3.55e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 3 FDWIKTRSDfDDDKPAVIDHAKQTsWTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPL 82
Cdd:PRK07514 6 FDALRAAFA-DRDAPFIETPDGLR-YTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 83 NWRLNPKEIAAIVEDAQLKLLFYAEKHLSSLTDIDQNLlhmdidVAQYDEIVNPD---------YHQP--FQATPVEPQD 151
Cdd:PRK07514 84 NTAYTLAELDYFIGDAEPALVVCDPANFAWLSKIAAAA------GAPHVETLDADgtgslleaaAAAPddFETVPRGADD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 152 LAALIYTSGTTGSPKGVMFSYESFVHNGANLELTYKFNSNYITIVSTPMFHVLGFNDTVLPVLMSGGTLILQRYFNGEEL 231
Cdd:PRK07514 158 LAAILYTSGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPDDVLIHALPIFHTHGLFVATNVALLAGASMIFLPKFDPDAV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 232 NDMIAQyhPTFIIMIPTMYYSTLRASNFNPENFRAMDYIIQGgSQPL-PSIQAAFKQ-YGINIINGYGLTEApLVLVNTP 309
Cdd:PRK07514 238 LALMPR--ATVMMGVPTFYTRLLQEPRLTREAAAHMRLFISG-SAPLlAETHREFQErTGHAILERYGMTET-NMNTSNP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 310 ENSKRKPMSIGKAVMFVDARILD-DNGEEVPTGEIGELAIKAKNVTPGYWNKPAETAKAFHGR-YLLTGDLAKMDNDGDI 387
Cdd:PRK07514 314 YDGERRAGTVGFPLPGVSLRVTDpETGAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADgFFITGDLGKIDERGYV 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 388 FIIDRKKELIITGGENVLPSEVENALAEHPLVDRCVVVGYDHPKYGESIAAAIILRE----DEphyAEILNQhMRSRLAG 463
Cdd:PRK07514 394 HIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKPgaalDE---AAILAA-LKGRLAR 469
|
490 500
....*....|....*....|....*...
gi 584959700 464 YKVPRMYVPVTHMPLNSTQKPDKLAIRQ 491
Cdd:PRK07514 470 FKQPKRVFFVDELPRNTMGKVQKNLLRE 497
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
30-477 |
6.11e-73 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 239.60 E-value: 6.11e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 30 YQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAAIVEDAQLKLLFYAEKH 109
Cdd:PRK12406 14 FDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAHADL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 110 LSSLTDIDQNLLHMdIDVAQYDEI-----VNPDY---------------HQPFQATPVEPQDlAALIYTSGTTGSPKGVM 169
Cdd:PRK12406 94 LHGLASALPAGVTV-LSVPTPPEIaaayrISPALltppagaidwegwlaQQEPYDGPPVPQP-QSMIYTSGTTGHPKGVR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 170 ---FSYESFVHNGANLELTYKFNSNYITIVSTPMFH----VLGFNDTVLpvlmsGGTLILQRYFNGEELNDMIAQYHPTF 242
Cdd:PRK12406 172 raaPTPEQAAAAEQMRALIYGLKPGIRALLTGPLYHsapnAYGLRAGRL-----GGVLVLQPRFDPEELLQLIERHRITH 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 243 IIMIPTMYYSTLRAsnfnPENFRA------MDYIIQGGSQ-PLPSIQAAFKQYGINIINGYGLTEAPLVLVNTPENSKRK 315
Cdd:PRK12406 247 MHMVPTMFIRLLKL----PEEVRAkydvssLRHVIHAAAPcPADVKRAMIEWWGPVIYEYYGSTESGAVTFATSEDALSH 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 316 PMSIGKAVMFVDARILDDNGEEVPTGEIGELAIKAKNVTP-GYWNKPAETAKAFHGRYLLTGDLAKMDNDGDIFIIDRKK 394
Cdd:PRK12406 323 PGTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPDfTYHNKPEKRAEIDRGGFITSGDVGYLDADGYLFLCDRKR 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 395 ELIITGGENVLPSEVENALAEHPLVDRCVVVGYDHPKYGESIAAAIilredEPH-----YAEILNQHMRSRLAGYKVPRM 469
Cdd:PRK12406 403 DMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVV-----EPQpgatlDEADIRAQLKARLAGYKVPKH 477
|
....*...
gi 584959700 470 YVPVTHMP 477
Cdd:PRK12406 478 IEIMAELP 485
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
147-477 |
3.64e-72 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 239.52 E-value: 3.64e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 147 VEPQDLAALIYTSGTTGSPKGVMFSYESFVHNGANLELTYKF--NSNYITIVSTPMFHVLGFNDTVLPVLMSGGTLILQR 224
Cdd:PRK05605 216 PTPDDVALILYTSGTTGKPKGAQLTHRNLFANAAQGKAWVPGlgDGPERVLAALPMFHAYGLTLCLTLAVSIGGELVLLP 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 225 YFNGEELNDMIAQYHPTFIIMIPTMYYSTLRASNFNPENFRAMDYIIQGGSqPLPSIQAAF--KQYGINIINGYGLTE-A 301
Cdd:PRK05605 296 APDIDLILDAMKKHPPTWLPGVPPLYEKIAEAAEERGVDLSGVRNAFSGAM-ALPVSTVELweKLTGGLLVEGYGLTEtS 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 302 PLVLVNtPENSKRKPMSIGkaVMF--VDARILD--DNGEEVPTGEIGELAIKAKNVTPGYWNKPAETAKAFHGRYLLTGD 377
Cdd:PRK05605 375 PIIVGN-PMSDDRRPGYVG--VPFpdTEVRIVDpeDPDETMPDGEEGELLVRGPQVFKGYWNRPEETAKSFLDGWFRTGD 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 378 LAKMDNDGDIFIIDRKKELIITGGENVLPSEVENALAEHPLVDRCVVVGYDHPKYGESIAAAIILREDEPHYAEILNQHM 457
Cdd:PRK05605 452 VVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEPGAALDPEGLRAYC 531
|
330 340
....*....|....*....|
gi 584959700 458 RSRLAGYKVPRMYVPVTHMP 477
Cdd:PRK05605 532 REHLTRYKVPRRFYHVDELP 551
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
15-489 |
3.91e-72 |
|
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: 237.76 E-value: 3.91e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 15 DKPAVIdHAKQTsWTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAAI 94
Cdd:TIGR03098 15 DATALV-HHDRT-LTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLKAEQVAHI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 95 VEDAQLKLLFYAEKHLSSLTDID------QNLLHMDIDVAQYDEIVNPDYHQ---------PFQATPVEPQDLAALIYTS 159
Cdd:TIGR03098 93 LADCNVRLLVTSSERLDLLHPALpgchdlRTLIIVGDPAHASEGHPGEEPASwpkllalgdADPPHPVIDSDMAAILYTS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 160 GTTGSPKGVMFSYESFVhNGANLELTYKFNSNYITIVST-PMFHVLGFNDtVLPVLMSGGTLILQRYFNGEELNDMIAQY 238
Cdd:TIGR03098 173 GSTGRPKGVVLSHRNLV-AGAQSVATYLENRPDDRLLAVlPLSFDYGFNQ-LTTAFYVGATVVLHDYLLPRDVLKALEKH 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 239 HPTFIIMIPTMyYSTLRASNFNPENFRAMDYIIQ-GGSQP---LPSIQAAFKQYGINIIngYGLTEAPLVLVNTPENSKR 314
Cdd:TIGR03098 251 GITGLAAVPPL-WAQLAQLDWPESAAPSLRYLTNsGGAMPratLSRLRSFLPNARLFLM--YGLTEAFRSTYLPPEEVDR 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 315 KPMSIGKAVMFVDARILDDNGEEVPTGEIGELAIKAKNVTPGYWNKPAETAKAF------------HGRYLLTGDLAKMD 382
Cdd:TIGR03098 328 RPDSIGKAIPNAEVLVLREDGSECAPGEEGELVHRGALVAMGYWNDPEKTAERFrplppfpgelhlPELAVWSGDTVRRD 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 383 NDGDIFIIDRKKELIITGGENVLPSEVENALAEHPLVDRCVVVGYDHPKYGESIAAAIILREDEPHYAEILNQHMRSRLA 462
Cdd:TIGR03098 408 EEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAFGVPDPTLGQAIVLVVTPPGGEELDRAALLAECRARLP 487
|
490 500
....*....|....*....|....*..
gi 584959700 463 GYKVPRMYVPVTHMPLNSTQKPDKLAI 489
Cdd:TIGR03098 488 NYMVPALIHVRQALPRNANGKIDRKAL 514
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
15-483 |
1.54e-71 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 237.13 E-value: 1.54e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 15 DKPAVIDHAKQTswTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAAI 94
Cdd:PRK07788 64 DRAALIDERGTL--TYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQLAEV 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 95 VEDAQLKLLFYAEKHLSSLTDIDQnllhmdiDVAQYDEIV-NPDYHQPFQATPVEPQDLAA----------------LIY 157
Cdd:PRK07788 142 AAREGVKALVYDDEFTDLLSALPP-------DLGRLRAWGgNPDDDEPSGSTDETLDDLIAgsstaplpkppkpggiVIL 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 158 TSGTTGSPKGVMFSYESFVHNGANLELTYKFNSNYITIVSTPMFHVLGFNDTVLpVLMSGGTLILQRYFNGEELNDMIAQ 237
Cdd:PRK07788 215 TSGTTGTPKGAPRPEPSPLAPLAGLLSRVPFRAGETTLLPAPMFHATGWAHLTL-AMALGSTVVLRRRFDPEATLEDIAK 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 238 YHPTFIIMIPTMYYSTLRAsnfnPENFRAmDY-------IIQGGSQPLPSI-QAAFKQYGINIINGYGLTEAPLVLVNTP 309
Cdd:PRK07788 294 HKATALVVVPVMLSRILDL----GPEVLA-KYdtsslkiIFVSGSALSPELaTRALEAFGPVLYNLYGSTEVAFATIATP 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 310 ENSKRKPMSIGKAVMFVDARILDDNGEEVPTGEIGElaIKAKNVTP--GYWNKPaeTAKAFHGrYLLTGDLAKMDNDGDI 387
Cdd:PRK07788 369 EDLAEAPGTVGRPPKGVTVKILDENGNEVPRGVVGR--IFVGNGFPfeGYTDGR--DKQIIDG-LLSSGDVGYFDEDGLL 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 388 FIIDRKKELIITGGENVLPSEVENALAEHPLVDRCVVVGYDHPKYGESIAAAIILREDEPHYAEILNQHMRSRLAGYKVP 467
Cdd:PRK07788 444 FVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKAPGAALDEDAIKDYVRDNLARYKVP 523
|
490
....*....|....*.
gi 584959700 468 RMYVPVTHMPLNSTQK 483
Cdd:PRK07788 524 RDVVFLDELPRNPTGK 539
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
15-488 |
2.56e-71 |
|
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: 246.69 E-value: 2.56e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 15 DKPAVIDHakQTSWTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPND----IAILdllfACFKTGAVFLPL--NWrlnP 88
Cdd:COG1020 491 DAVAVVFG--DQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSlemvVALL----AVLKAGAAYVPLdpAY---P 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 89 KE-IAAIVEDAQLKLLFYAEKHLSSLTDIDQNLLHMD-IDVAQYDEIvNPdyhqpfqATPVEPQDLAALIYTSGTTGSPK 166
Cdd:COG1020 562 AErLAYMLEDAGARLVLTQSALAARLPELGVPVLALDaLALAAEPAT-NP-------PVPVTPDDLAYVIYTSGSTGRPK 633
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 167 GVMFSYESFVHNGANLELTYKFNSNyitiVSTPMFHVLGFNDTV---LPVLMSGGTLIL---QRYFNGEELNDMIAQYHP 240
Cdd:COG1020 634 GVMVEHRALVNLLAWMQRRYGLGPG----DRVLQFASLSFDASVweiFGALLSGATLVLappEARRDPAALAELLARHRV 709
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 241 TFIIMIPTMYYSTLRASnfnPENFRAMDYIIQGGSQPLPSIQAAFKQY--GINIINGYGLTEA---PLVLVNTPENSKRK 315
Cdd:COG1020 710 TVLNLTPSLLRALLDAA---PEALPSLRLVLVGGEALPPELVRRWRARlpGARLVNLYGPTETtvdSTYYEVTPPDADGG 786
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 316 PMSIGKAVMFVDARILDDNGEEVPTGEIGELAIKAKNVTPGYWNKPAETAKAF--------HGRYLLTGDLAKMDNDGDI 387
Cdd:COG1020 787 SVPIGRPIANTRVYVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFvadpfgfpGARLYRTGDLARWLPDGNL 866
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 388 FIIDRK----K------ELiitggenvlpSEVENALAEHPLVDRCVVVGYDHPKYGESIAAAIILREDEPHYAEILNQHM 457
Cdd:COG1020 867 EFLGRAddqvKirgfriEL----------GEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAALLRLAL 936
|
490 500 510
....*....|....*....|....*....|.
gi 584959700 458 RSRLAGYKVPRMYVPVTHMPLNSTQKPDKLA 488
Cdd:COG1020 937 ALLLPPYMVPAAVVLLLPLPLTGNGKLDRLA 967
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
15-483 |
2.65e-71 |
|
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: 235.10 E-value: 2.65e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 15 DKPAVIDHAKQTSWTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAAI 94
Cdd:cd05923 16 DACAIADPARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 95 VEDAQLKLLFYAEKHLSSLTDIDQN--LLHMDIDVaqyDEIVNPDYHQPFQATPVEPQDLAALIYTSGTTGSPKGVMFSY 172
Cdd:cd05923 96 IERGEMTAAVIAVDAQVMDAIFQSGvrVLALSDLV---GLGEPESAGPLIEDPPREPEQPAFVFYTSGTTGLPKGAVIPQ 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 173 ---ESFVHNGANlELTYKFNSNYITIVSTPMFHVLGFNDTVLPVLMSGGTLILQRYFNGEELNDMIAQYHPTFIIMIPTM 249
Cdd:cd05923 173 raaESRVLFMST-QAGLRHGRHNVVLGLMPLYHVIGFFAVLVAALALDGTYVVVEEFDPADALKLIEQERVTSLFATPTH 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 250 YYSTLRASNFNPENFRAMDYII-QGGSQPLPSIQAAFKQYGINIINGYGLTEAplvlVNTPENSKRKPMSIGKAVMFVD- 327
Cdd:cd05923 252 LDALAAAAEFAGLKLSSLRHVTfAGATMPDAVLERVNQHLPGEKVNIYGTTEA----MNSLYMRDARTGTEMRPGFFSEv 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 328 --ARILDDNGEEVPTGEIGELAIKAKN--VTPGYWNKPAETAKAFHGRYLLTGDLAKMDNDGDIFIIDRKKELIITGGEN 403
Cdd:cd05923 328 riVRIGGSPDEALANGEEGELIVAAAAdaAFTGYLNQPEATAKKLQDGWYRTGDVGYVDPSGDVRILGRVDDMIISGGEN 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 404 VLPSEVENALAEHPLVDRCVVVGYDHPKYGESIAAAIILREDEPHyAEILNQHMR-SRLAGYKVPRMYVPVTHMPLNSTQ 482
Cdd:cd05923 408 IHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREGTLS-ADELDQFCRaSELADFKRPRRYFFLDELPKNAMN 486
|
.
gi 584959700 483 K 483
Cdd:cd05923 487 K 487
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
15-493 |
2.87e-71 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 236.59 E-value: 2.87e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 15 DKPAVIDHAKQTSWTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAAI 94
Cdd:PRK12583 33 DREALVVRHQALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 95 VEDAQLKLLFYAEKHLSSltDIDQNLLHM--DIDVAQYDEIVNPDYhqPF---------QATP--------------VEP 149
Cdd:PRK12583 113 LGQSGVRWVICADAFKTS--DYHAMLQELlpGLAEGQPGALACERL--PElrgvvslapAPPPgflawhelqargetVSR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 150 QDLAA------------LIYTSGTTGSPKGVMFSYESFVHNGANLELTYKFNSNYITIVSTPMFHVLGFNDTVLPVLMSG 217
Cdd:PRK12583 189 EALAErqasldrddpinIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCVPVPLYHCFGMVLANLGCMTVG 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 218 GTLIL-QRYFNGEELNDMIAQYHPTFIIMIPTMYYSTLRASNFNPENFRAMDYIIQGGSQ-PLPSIQAAFKQYGI-NIIN 294
Cdd:PRK12583 269 ACLVYpNEAFDPLATLQAVEEERCTALYGVPTMFIAELDHPQRGNFDLSSLRTGIMAGAPcPIEVMRRVMDEMHMaEVQI 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 295 GYGLTEA-PLVLVNTPENS-KRKPMSIGKAVMFVDARILDDNGEEVPTGEIGELAIKAKNVTPGYWNKPAETAKAFHGR- 371
Cdd:PRK12583 349 AYGMTETsPVSLQTTAADDlERRVETVGRTQPHLEVKVVDPDGATVPRGEIGELCTRGYSVMKGYWNNPEATAESIDEDg 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 372 YLLTGDLAKMDNDGDIFIIDRKKELIITGGENVLPSEVENALAEHPLVDRCVVVGYDHPKYGESIAAAIILREDEPHYAE 451
Cdd:PRK12583 429 WMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRLHPGHAASEE 508
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 584959700 452 ILNQHMRSRLAGYKVPRMYVPVTHMPLNSTQKPDKLAIRQMM 493
Cdd:PRK12583 509 ELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMREIS 550
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
29-424 |
1.52e-69 |
|
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: 227.92 E-value: 1.52e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 29 TYQQLNARADNMAHYLTSQ-GVKKGDVIGIFAPND----IAILdllfACFKTGAVFLPLNWRLNPKEIAAIVEDAQLKLL 103
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSaelvVAIL----AVLKAGAAYVPLDPAYPAERLAFILEDAGARLL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 104 FYAEKHLSSLTDIDQnllhMDIDVAQYDEIVNPDYHQPFQAT-PVEPQDLAALIYTSGTTGSPKGVMFSYESFVHNGANL 182
Cdd:TIGR01733 77 LTDSALASRLAGLVL----PVILLDPLELAALDDAPAPPPPDaPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 183 ELTYKFNSNyitiVSTPMFHVLGFnDT----VLPVLMSGGTLIL----QRYFNGEELNDMIAQYHPTFIIMIPTMYYSTL 254
Cdd:TIGR01733 153 ARRYGLDPD----DRVLQFASLSF-DAsveeIFGALLAGATLVVppedEERDDAALLAALIAEHPVTVLNLTPSLLALLA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 255 RASNFNPENFRamdYIIQGGSQPLP----SIQAAFKqyGINIINGYGLTEAPLV----LVNTPENSKRKPMSIGKAVMFV 326
Cdd:TIGR01733 228 AALPPALASLR---LVILGGEALTPalvdRWRARGP--GARLINLYGPTETTVWstatLVDPDDAPRESPVPIGRPLANT 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 327 DARILDDNGEEVPTGEIGELAIKAKNVTPGYWNKPAETAKAF---------HGRYLLTGDLAKMDNDGDIFIIDRKKELI 397
Cdd:TIGR01733 303 RLYVLDDDLRPVPVGVVGELYIGGPGVARGYLNRPELTAERFvpdpfaggdGARLYRTGDLVRYLPDGNLEFLGRIDDQV 382
|
410 420
....*....|....*....|....*..
gi 584959700 398 ITGGENVLPSEVENALAEHPLVDRCVV 424
Cdd:TIGR01733 383 KIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
29-491 |
7.85e-68 |
|
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: 224.18 E-value: 7.85e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 29 TYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAAIVEDAQLKLLFYAEK 108
Cdd:cd05903 3 TYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVPER 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 109 HlssltdidqnllhmdidvAQYDeivnpdyHQPfqatpvEPQDLAALIYTSGTTGSPKGVMFSYESFVHNGANLELTYKF 188
Cdd:cd05903 83 F------------------RQFD-------PAA------MPDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 189 NSNYITIVSTPMFHVLGFNDTVLPVLMSGGTLILQRYFNGEELNDMIAQYHPTFIIMIPTMYYSTLRASNFNPENFRAMD 268
Cdd:cd05903 132 GPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQDIWDPDKALALMREHGVTFMMGATPFLTDLLNAVEEAGEPLSRLR 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 269 YIIQGGSQ-PLPSIQAAFKQYGINIINGYGLTEAPLVLVN-TPENSKRKPMSIGKAVMFVDARILDDNGEEVPTGEIGEL 346
Cdd:cd05903 212 TFVCGGATvPRSLARRAAELLGAKVCSAYGSTECPGAVTSiTPAPEDRRLYTDGRPLPGVEIKVVDDTGATLAPGVEGEL 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 347 AIKAKNVTPGYWNKPAETAKAFHGRYLLTGDLAKMDNDGDIFIIDRKKELIITGGENVLPSEVENALAEHPLVDRCVVVG 426
Cdd:cd05903 292 LSRGPSVFLGYLDRPDLTADAAPEGWFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVA 371
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 584959700 427 YDHPKYGESIAAAIILRED-EPHYAEILNQHMRSRLAGYKVPRMYVPVTHMPLNSTQKPDKLAIRQ 491
Cdd:cd05903 372 LPDERLGERACAVVVTKSGaLLTFDELVAYLDRQGVAKQYWPERLVHVDDLPRTPSGKVQKFRLRE 437
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
15-493 |
7.99e-67 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 224.69 E-value: 7.99e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 15 DKPAVIDHAKQTSWTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLN--WRLNpkEIA 92
Cdd:PRK08315 31 DREALVYRDQGLRWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVTINpaYRLS--ELE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 93 AIVEDAQLKLLFYAEK-------------------------------HLSSLTDIDQN----------LLHM--DIDVAQ 129
Cdd:PRK08315 109 YALNQSGCKALIAADGfkdsdyvamlyelapelatcepgqlqsarlpELRRVIFLGDEkhpgmlnfdeLLALgrAVDDAE 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 130 YDEIvnpdyhqpfQATpVEPQDLAALIYTSGTTGSPKGVMFSYESFVHNGANLELTYKFNSNYITIVSTPMFH----VLG 205
Cdd:PRK08315 189 LAAR---------QAT-LDPDDPINIQYTSGTTGFPKGATLTHRNILNNGYFIGEAMKLTEEDRLCIPVPLYHcfgmVLG 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 206 fndtVLPVLMSGGTLIlqryFNGEELN-----DMIAQYHPTFIIMIPTMYYSTLRASNFNPENFRAMDYIIQGGSqPLPS 280
Cdd:PRK08315 259 ----NLACVTHGATMV----YPGEGFDplatlAAVEEERCTALYGVPTMFIAELDHPDFARFDLSSLRTGIMAGS-PCPI 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 281 -----IQAAFKQYGINIinGYGLTEAPLV----LVNTPEnsKRKPMSIGKAVMFVDARILD-DNGEEVPTGEIGELAIKA 350
Cdd:PRK08315 330 evmkrVIDKMHMSEVTI--AYGMTETSPVstqtRTDDPL--EKRVTTVGRALPHLEVKIVDpETGETVPRGEQGELCTRG 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 351 KNVTPGYWNKPAETAKAF-HGRYLLTGDLAKMDNDGDIFIIDRKKELIITGGENVLPSEVENALAEHPLVDRCVVVGYDH 429
Cdd:PRK08315 406 YSVMKGYWNDPEKTAEAIdADGWMHTGDLAVMDEEGYVNIVGRIKDMIIRGGENIYPREIEEFLYTHPKIQDVQVVGVPD 485
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 584959700 430 PKYGESIAAAIILREDEPHYAEILNQHMRSRLAGYKVPRMYVPVTHMPLNSTQKPDKLAIRQMM 493
Cdd:PRK08315 486 EKYGEEVCAWIILRPGATLTEEDVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGKIQKFKMREMM 549
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
157-490 |
1.76e-66 |
|
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: 217.92 E-value: 1.76e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 157 YTSGTTGSPKGVMFSYESFVHNGANLELTYKFNSNYITIVSTPMFHVLGFNDTVLPVLMSGGTLIL-QRYFNGEELNDMI 235
Cdd:cd05917 9 FTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLCIPVPLFHCFGSVLGVLACLTHGATMVFpSPSFDPLAVLEAI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 236 AQYHPTFIIMIPTMYYSTL---RASNFNPENFRAMdyIIQGGSQPLPSIQAAFKQYGI-NIINGYGLTEA-PLVLVNTPE 310
Cdd:cd05917 89 EKEKCTALHGVPTMFIAELehpDFDKFDLSSLRTG--IMAGAPCPPELMKRVIEVMNMkDVTIAYGMTETsPVSTQTRTD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 311 NS-KRKPMSIGKAVMFVDARILD-DNGEEVPTGEIGELAIKAKNVTPGYWNKPAETAKAFHG-RYLLTGDLAKMDNDGDI 387
Cdd:cd05917 167 DSiEKRVNTVGRIMPHTEAKIVDpEGGIVPPVGVPGELCIRGYSVMKGYWNDPEKTAEAIDGdGWLHTGDLAVMDEDGYC 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 388 FIIDRKKELIITGGENVLPSEVENALAEHPLVDRCVVVGYDHPKYGESIAAAIILREDEPHYAEILNQHMRSRLAGYKVP 467
Cdd:cd05917 247 RIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLKEGAELTEEDIKAYCKGKIAHYKVP 326
|
330 340
....*....|....*....|...
gi 584959700 468 RMYVPVTHMPLNSTQKPDKLAIR 490
Cdd:cd05917 327 RYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
15-485 |
3.99e-66 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 222.45 E-value: 3.99e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 15 DKPAVIDHAKQtsWTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAAI 94
Cdd:PRK07798 18 DRVALVCGDRR--LTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 95 VEDAQLKLLFY--------AE--------KHLSSLTDIDQNLLhmDIDVAQYDEIV-NPDYHQPFQATpvEPQDLAaLIY 157
Cdd:PRK07798 96 LDDSDAVALVYerefaprvAEvlprlpklRTLVVVEDGSGNDL--LPGAVDYEDALaAGSPERDFGER--SPDDLY-LLY 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 158 TSGTTGSPKGVMFSYESFVH---NGANL----------ELTYKFNSN--YITIVSTPMFHVLGFNdTVLPVLMSGGTLIL 222
Cdd:PRK07798 171 TGGTTGMPKGVMWRQEDIFRvllGGRDFatgepiedeeELAKRAAAGpgMRRFPAPPLMHGAGQW-AAFAALFSGQTVVL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 223 QRY--FNGEELNDMIAQYHPTFIIMIPTMYYSTLRASNFNPENFR--AMDYIIQGGSQPLPSIQAAFKQY--GINIINGY 296
Cdd:PRK07798 250 LPDvrFDADEVWRTIEREKVNVITIVGDAMARPLLDALEARGPYDlsSLFAIASGGALFSPSVKEALLELlpNVVLTDSI 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 297 GLTEAPLVLVNTpenSKRKPMSIGKAVMFVDAR--ILDDNGEEVPTG--EIGELAIKAkNVTPGYWNKPAETAKAF---H 369
Cdd:PRK07798 330 GSSETGFGGSGT---VAKGAVHTGGPRFTIGPRtvVLDEDGNPVEPGsgEIGWIARRG-HIPLGYYKDPEKTAETFptiD 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 370 G-RYLLTGDLAKMDNDGDIFIIDRKKELIITGGENVLPSEVENALAEHPLVDRCVVVGYDHPKYGESIAAAIILREDEPH 448
Cdd:PRK07798 406 GvRYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVPDERWGQEVVAVVQLREGARP 485
|
490 500 510
....*....|....*....|....*....|....*..
gi 584959700 449 YAEILNQHMRSRLAGYKVPRMYVPVTHMPLNSTQKPD 485
Cdd:PRK07798 486 DLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGKAD 522
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
15-490 |
4.71e-66 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 224.45 E-value: 4.71e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 15 DKPAVI------DHAKQTSWTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFlPLNWRLNP 88
Cdd:PRK07529 40 DAPALSflldadPLDRPETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGEAAGIAN-PINPLLEP 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 89 KEIAAIVEDAQLKLLFY------------AEKHLSSLTDIdQNLLHMD---------------------IDVAQYDEIVN 135
Cdd:PRK07529 119 EQIAELLRAAGAKVLVTlgpfpgtdiwqkVAEVLAALPEL-RTVVEVDlarylpgpkrlavplirrkahARILDFDAELA 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 136 PDYH-QPFQATPVEPQDLAALIYTSGTTGSPKGVMFSYESFVHNGANLELTYKFNSNYITIVSTPMFHVLGFNDTVLPVL 214
Cdd:PRK07529 198 RQPGdRLFSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPGDTVFCGLPLFHVNALLVTGLAPL 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 215 MSGGTLIL---QRYfNGEELND----MIAQYHPTFIIMIPTMYYSTLRAsnfnPENfrAMD-----YIIqGGSQPLP-SI 281
Cdd:PRK07529 278 ARGAHVVLatpQGY-RGPGVIAnfwkIVERYRINFLSGVPTVYAALLQV----PVD--GHDisslrYAL-CGAAPLPvEV 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 282 QAAFKQY-GINIINGYGLTEAP-LVLVNTPENSkRKPMSIGKAVMFVDARI--LDDNG---EEVPTGEIGELAIKAKNVT 354
Cdd:PRK07529 350 FRRFEAAtGVRIVEGYGLTEATcVSSVNPPDGE-RRIGSVGLRLPYQRVRVviLDDAGrylRDCAVDEVGVLCIAGPNVF 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 355 PGYWNkpAETAKA--FHGRYLLTGDLAKMDNDGDIFIIDRKKELIITGGENVLPSEVENALAEHPLVDRCVVVGYDHPKY 432
Cdd:PRK07529 429 SGYLE--AAHNKGlwLEDGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPDAHA 506
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 584959700 433 GESIAAAIILRE----DEPHYAEILNQHMRSRLAgykVPRMYVPVTHMPLNSTQKPDKLAIR 490
Cdd:PRK07529 507 GELPVAYVQLKPgasaTEAELLAFARDHIAERAA---VPKHVRILDALPKTAVGKIFKPALR 565
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
8-468 |
2.00e-65 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 219.95 E-value: 2.00e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 8 TRSDFDDDKPAVIDHAKQTSWTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLN 87
Cdd:PRK13391 5 IHAQTTPDKPAVIMASTGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 88 PKEIAAIVEDAQLKLLFYAEKHL---SSLTDIDQNLLH-----MDIDVAQYDEIVNPDYHQPfqATPVEPQDL-AALIYT 158
Cdd:PRK13391 85 PAEAAYIVDDSGARALITSAAKLdvaRALLKQCPGVRHrlvldGDGELEGFVGYAEAVAGLP--ATPIADESLgTDMLYS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 159 SGTTGSPKGVM-----------FSYESFVHNganlelTYKFNSNYITIVSTPMFHV--LGFNDTVLPVlmsGGTLILQRY 225
Cdd:PRK13391 163 SGTTGRPKGIKrplpeqppdtpLPLTAFLQR------LWGFRSDMVYLSPAPLYHSapQRAVMLVIRL---GGTVIVMEH 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 226 FNGEELNDMIAQYHPTFIIMIPTMYYSTLRAsnfnPENFR------AMDYIIQGGSQPLPSI-QAAFKQYGINIINGYGL 298
Cdd:PRK13391 234 FDAEQYLALIEEYGVTHTQLVPTMFSRMLKL----PEEVRdkydlsSLEVAIHAAAPCPPQVkEQMIDWWGPIIHEYYAA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 299 TEAPLVLVNTPENSKRKPMSIGKAvMFVDARILDDNGEEVPTGEIGElaIKAKNVTP-GYWNKPAETAKAFH--GRYLLT 375
Cdd:PRK13391 310 TEGLGFTACDSEEWLAHPGTVGRA-MFGDLHILDDDGAELPPGEPGT--IWFEGGRPfEYLNDPAKTAEARHpdGTWSTV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 376 GDLAKMDNDGDIFIIDRKKELIITGGENVLPSEVENALAEHPLVDRCVVVGYDHPKYGESIAAAIILR---EDEPHYAEI 452
Cdd:PRK13391 387 GDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPVdgvDPGPALAAE 466
|
490
....*....|....*.
gi 584959700 453 LNQHMRSRLAGYKVPR 468
Cdd:PRK13391 467 LIAFCRQRLSRQKCPR 482
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
29-483 |
4.16e-65 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 220.67 E-value: 4.16e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 29 TYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAAIVEDAQLK------L 102
Cdd:PRK06710 51 TFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKvilcldL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 103 LFYAEKHLSSLTDID--------------QNLLHMDIDVAQYDEIVNPDYHQPFQ-------------ATPVEPQ-DLAA 154
Cdd:PRK06710 131 VFPRVTNVQSATKIEhvivtriadflpfpKNLLYPFVQKKQSNLVVKVSESETIHlwnsvekevntgvEVPCDPEnDLAL 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 155 LIYTSGTTGSPKGVMFSYESFVHNGAnLELTYKFN---SNYITIVSTPMFHVLGFNDTVLPVLMSGGTLILQRYFNGEEL 231
Cdd:PRK06710 211 LQYTGGTTGFPKGVMLTHKNLVSNTL-MGVQWLYNckeGEEVVLGVLPFFHVYGMTAVMNLSIMQGYKMVLIPKFDMKMV 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 232 NDMIAQYHPTFIIMIPTMYYSTLRASNFNPENFRAMDYIIQGgSQPLP-SIQAAFKQY-GINIINGYGLTEAPLVLVNTP 309
Cdd:PRK06710 290 FEAIKKHKVTLFPGAPTIYIALLNSPLLKEYDISSIRACISG-SAPLPvEVQEKFETVtGGKLVEGYGLTESSPVTHSNF 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 310 ENSKRKPMSIGKAVMFVDARILD-DNGEEVPTGEIGELAIKAKNVTPGYWNKPAETAKAFHGRYLLTGDLAKMDNDGDIF 388
Cdd:PRK06710 369 LWEKRVPGSIGVPWPDTEAMIMSlETGEALPPGEIGEIVVKGPQIMKGYWNKPEETAAVLQDGWLHTGDVGYMDEDGFFY 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 389 IIDRKKELIITGGENVLPSEVENALAEHPLVDRCVVVGYDHPKYGESIAAAIILREDEPHYAEILNQHMRSRLAGYKVPR 468
Cdd:PRK06710 449 VKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVLKEGTECSEEELNQFARKYLAAYKVPK 528
|
490
....*....|....*
gi 584959700 469 MYVPVTHMPLNSTQK 483
Cdd:PRK06710 529 VYEFRDELPKTTVGK 543
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
15-489 |
7.57e-65 |
|
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: 216.73 E-value: 7.57e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 15 DKPAVIDhaKQTSWTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAAI 94
Cdd:cd05945 6 DRPAVVE--GGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERIREI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 95 VEDAQLKLLFYAEKhlssltdidqnllhmdidvaqydeivnpdyhqpfqatpvepqDLAALIYTSGTTGSPKGVMFSYES 174
Cdd:cd05945 84 LDAAKPALLIADGD------------------------------------------DNAYIIFTSGSTGRPKGVQISHDN 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 175 FVHNGANLELTYKFNSNYItIVSTPMFHvlgFnD----TVLPVLMSGGTLIL---QRYFNGEELNDMIAQYH-------P 240
Cdd:cd05945 122 LVSFTNWMLSDFPLGPGDV-FLNQAPFS---F-DlsvmDLYPALASGATLVPvprDATADPKQLFRFLAEHGitvwvstP 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 241 TFIIMIptmyystLRASNFNPENFRAMDYIIQGGsQPLP-----SIQAAFKqyGINIINGYGLTEApLVLVN----TPEN 311
Cdd:cd05945 197 SFAAMC-------LLSPTFTPESLPSLRHFLFCG-EVLPhktarALQQRFP--DARIYNTYGPTEA-TVAVTyievTPEV 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 312 SKR-KPMSIGKAVMFVDARILDDNGEEVPTGEIGELAIKAKNVTPGYWNKPAETAKAFH----GRYLLTGDLAKMDNDGD 386
Cdd:cd05945 266 LDGyDRLPIGYAKPGAKLVILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFpdegQRAYRTGDLVRLEADGL 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 387 IFIIDRKKELIITGGENVLPSEVENALAEHPLVDRCVVVGYDHPKYGESIAAAIILRE-DEPHYAEILNQHMRSRLAGYK 465
Cdd:cd05945 346 LFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPgAEAGLTKAIKAELAERLPPYM 425
|
490 500
....*....|....*....|....
gi 584959700 466 VPRMYVPVTHMPLNSTQKPDKLAI 489
Cdd:cd05945 426 IPRRFVYLDELPLNANGKIDRKAL 449
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
28-490 |
1.39e-64 |
|
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.
Pssm-ID: 341276 [Multi-domain] Cd Length: 428 Bit Score: 215.28 E-value: 1.39e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 28 WTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPND----IAILdllfACFKTGAVFLPLNWRLNPKEIAAIVEDAQLKLL 103
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVpelwAVIL----AVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 104 FYAEkhlssltdidqnllhmdidvaqydeivnpdyhqpfqatpvepQDLAALIYTSGTTGSPKGVmfsyesfVHnGANLE 183
Cdd:cd05972 77 VTDA------------------------------------------EDPALIYFTSGTTGLPKGV-------LH-THSYP 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 184 LTYKFNSNYITIVSTPMFH--------VLGFNDTVLPVLMSGGTLILQRY--FNGEELNDMIAQYHPTFIIMIPTMYYST 253
Cdd:cd05972 107 LGHIPTAAYWLGLRPDDIHwniadpgwAKGAWSSFFGPWLLGATVFVYEGprFDAERILELLERYGVTSFCGPPTAYRML 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 254 LRA--SNFNPENFRamdyIIQGGSQPL-PSIQAAFK-QYGINIINGYGLTEAPLVLVNTPeNSKRKPMSIGKAVMFVDAR 329
Cdd:cd05972 187 IKQdlSSYKFSHLR----LVVSAGEPLnPEVIEWWRaATGLPIRDGYGQTETGLTVGNFP-DMPVKPGSMGRPTPGYDVA 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 330 ILDDNGEEVPTGEIGELAIKAKNVTP--GYWNKPAETAKAFHGRYLLTGDLAKMDNDGDIFIIDRKKELIITGGENVLPS 407
Cdd:cd05972 262 IIDDDGRELPPGEEGDIAIKLPPPGLflGYVGDPEKTEASIRGDYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPF 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 408 EVENALAEHPLVDRCVVVGYDHPKYGESIAAAIILREDEP---HYAEILNQHMRSRLAGYKVPRMYVPVTHMPLNSTQKP 484
Cdd:cd05972 342 EVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYEpseELAEELQGHVKKVLAPYKYPREIEFVEELPKTISGKI 421
|
....*.
gi 584959700 485 DKLAIR 490
Cdd:cd05972 422 RRVELR 427
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
14-490 |
5.11e-64 |
|
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: 216.08 E-value: 5.11e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 14 DDKPAVIDhaKQTSWTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAA 93
Cdd:cd05959 18 GDKTAFID--DAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 94 IVEDAQLKLLF----YAEKHLSSLTDIDQNLLHMDI--------DVAQYDEIVnPDYHQPFQATPVEPQDLAALIYTSGT 161
Cdd:cd05959 96 YLEDSRARVVVvsgeLAPVLAAALTKSEHTLVVLIVsggagpeaGALLLAELV-AAEAEQLKPAATHADDPAFWLYSSGS 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 162 TGSPKGVmfsyesfVHNGANL---ELTYKFNSNYIT----IVSTP-MFHVLGFNDTVLPVLMSGGTLIL-------QRYF 226
Cdd:cd05959 175 TGRPKGV-------VHLHADIywtAELYARNVLGIReddvCFSAAkLFFAYGLGNSLTFPLSVGATTVLmperptpAAVF 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 227 ngeelnDMIAQYHPTFIIMIPTMYYSTLRASNFNPENFRAMDYIIQGGsQPLP-SIQAAFK-QYGINIINGYGLTEA-PL 303
Cdd:cd05959 248 ------KRIRRYRPTVFFGVPTLYAAMLAAPNLPSRDLSSLRLCVSAG-EALPaEVGERWKaRFGLDILDGIGSTEMlHI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 304 VLVNTPENSKrkPMSIGKAVMFVDARILDDNGEEVPTGEIGELAIKAKNVTPGYWNKPAETAKAFHGRYLLTGDLAKMDN 383
Cdd:cd05959 321 FLSNRPGRVR--YGTTGKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQGEWTRTGDKYVRDD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 384 DGDIFIIDRKKELIITGGENVLPSEVENALAEHPLVDRCVVVGYDHPKYGESIAAAIILR---EDEPHYAEILNQHMRSR 460
Cdd:cd05959 399 DGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRpgyEDSEALEEELKEFVKDR 478
|
490 500 510
....*....|....*....|....*....|
gi 584959700 461 LAGYKVPRMYVPVTHMPLNSTQKPDKLAIR 490
Cdd:cd05959 479 LAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
15-490 |
6.41e-64 |
|
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: 215.29 E-value: 6.41e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 15 DKPAVIDhaKQTSWTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAAI 94
Cdd:cd17651 10 DAPALVA--EGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERLAFM 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 95 VEDAQLKLLFYAEKHLSSLTDIDQNLLHMDIDVAQYDEIVNPDyhqpfqaTPVEPQDLAALIYTSGTTGSPKGVMFSYES 174
Cdd:cd17651 88 LADAGPVLVLTHPALAGELAVELVAVTLLDQPGAAAGADAEPD-------PALDADDLAYVIYTSGSTGRPKGVVMPHRS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 175 FvhngANLELTYKFNSNYITIVSTPMFHVLGFNDTV---LPVLMSGGTLILQRyfnGEELNDMIA-----QYHPTFIIMI 246
Cdd:cd17651 161 L----ANLVAWQARASSLGPGARTLQFAGLGFDVSVqeiFSTLCAGATLVLPP---EEVRTDPPAlaawlDEQRISRVFL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 247 PTMYYSTL-----RASNFNPenfrAMDYIIQGGSQ--PLPSIQAAFK-QYGINIINGYGLTEAPLV---LVNTPENSKRK 315
Cdd:cd17651 234 PTVALRALaehgrPLGVRLA----ALRYLLTGGEQlvLTEDLREFCAgLPGLRLHNHYGPTETHVVtalSLPGDPAAWPA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 316 PMSIGKAVMFVDARILDDNGEEVPTGEIGELAIKAKNVTPGYWNKPAETAKAFH-------GRYLLTGDLAKMDNDGDIF 388
Cdd:cd17651 310 PPPIGRPIDNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVpdpfvpgARMYRTGDLARWLPDGELE 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 389 IIDRKKELIITGGENVLPSEVENALAEHPLVDRCVVVGYDHPKYGESIAAAIILREDEPHYAEILNQHMRSRLAGYKVPR 468
Cdd:cd17651 390 FLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPEAPVDAAELRAALATHLPEYMVPS 469
|
490 500
....*....|....*....|..
gi 584959700 469 MYVPVTHMPLNSTQKPDKLAIR 490
Cdd:cd17651 470 AFVLLDALPLTPNGKLDRRALP 491
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
15-491 |
1.80e-62 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 213.08 E-value: 1.80e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 15 DKPAVIdhAKQTSWTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAAI 94
Cdd:PRK06155 36 DRPLLV--FGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 95 VEDAQLKLLFYAEKHLSSLTDIDQNLLHMD----IDVAQ-------YDEIVNPDYHQPFQATPVEPQDLAALIYTSGTTG 163
Cdd:PRK06155 114 LRNSGARLLVVEAALLAALEAADPGDLPLPavwlLDAPAsvsvpagWSTAPLPPLDAPAPAAAVQPGDTAAILYTSGTTG 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 164 SPKGVMFSYESF----VHNGANLELTykfnSNYITIVSTPMFHVLGFNdTVLPVLMSGGTLILQRYFNGEELNDMIAQYH 239
Cdd:PRK06155 194 PSKGVCCPHAQFywwgRNSAEDLEIG----ADDVLYTTLPLFHTNALN-AFFQALLAGATYVLEPRFSASGFWPAVRRHG 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 240 PTFIIMIPTMYySTLRASNFNPENFRAMDYIIQGGSQPlPSIQAAFKQ-YGINIINGYGLTEAPLVLVNTPenSKRKPMS 318
Cdd:PRK06155 269 ATVTYLLGAMV-SILLSQPARESDRAHRVRVALGPGVP-AALHAAFRErFGVDLLDGYGSTETNFVIAVTH--GSQRPGS 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 319 IGKAVMFVDARILDDNGEEVPTGEIGELAIKAKN---VTPGYWNKPAETAKAFHGRYLLTGDLAKMDNDGDIFIIDRKKE 395
Cdd:PRK06155 345 MGRLAPGFEARVVDEHDQELPDGEPGELLLRADEpfaFATGYFGMPEKTVEAWRNLWFHTGDRVVRDADGWFRFVDRIKD 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 396 LIITGGENVLPSEVENALAEHPLVDRCVVVGYDHPKYGESIAAAIILREDEPHYAEILNQHMRSRLAGYKVPRmYVPVTH 475
Cdd:PRK06155 425 AIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDGTALEPVALVRHCEPRLAYFAVPR-YVEFVA 503
|
490
....*....|....*..
gi 584959700 476 -MPLNSTQKPDKLAIRQ 491
Cdd:PRK06155 504 aLPKTENGKVQKFVLRE 520
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
15-491 |
1.91e-62 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 213.07 E-value: 1.91e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 15 DKPAVIDHaKQTSWTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPN--DIAILDLlfACFKTGAVFLPLNWRLNPKEIA 92
Cdd:PRK06087 38 DKIAVVDN-HGASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGwcEFTIIYL--ACLKVGAVSVPLLPSWREAELV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 93 AIVEDAQLKLLF----YAE--------------KHLSSLTDIDQNL-LHMDIDVAQydeiVNPDYHQPFQATPVEPQDLA 153
Cdd:PRK06087 115 WVLNKCQAKMFFaptlFKQtrpvdlilplqnqlPQLQQIVGVDKLApATSSLSLSQ----IIADYEPLTTAITTHGDELA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 154 ALIYTSGTTGSPKGVM-------FSYESFVhngANLELTykfnSNYITIVSTPMFHVLGFNDTVLPVLMSGGTLILQRYF 226
Cdd:PRK06087 191 AVLFTSGTEGLPKGVMlthnnilASERAYC---ARLNLT----WQDVFMMPAPLGHATGFLHGVTAPFLIGARSVLLDIF 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 227 NGEELNDMIAQYHPTFIIMIPTMYYSTLRASNFNPENFRAMDYIIQGGSqPLPS--IQAAfKQYGINIINGYGLTEA-PL 303
Cdd:PRK06087 264 TPDACLALLEQQRCTCMLGATPFIYDLLNLLEKQPADLSALRFFLCGGT-TIPKkvAREC-QQRGIKLLSVYGSTESsPH 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 304 VLVNTPENSKRKPMSIGKAVMFVDARILDDNGEEVPTGEIGELAIKAKNVTPGYWNKPAETAKAF--HGRYLlTGDLAKM 381
Cdd:PRK06087 342 AVVNLDDPLSRFMHTDGYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYLDEPELTARALdeEGWYY-SGDLCRM 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 382 DNDGDIFIIDRKKELIITGGENVLPSEVENALAEHPLVDRCVVVGYDHPKYGESIAAAIILREDE--PHYAEILNQHMRS 459
Cdd:PRK06087 421 DEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVVLKAPHhsLTLEEVVAFFSRK 500
|
490 500 510
....*....|....*....|....*....|..
gi 584959700 460 RLAGYKVPRMYVPVTHMPLNSTQKPDKLAIRQ 491
Cdd:PRK06087 501 RVAKYKYPEHIVVIDKLPRTASGKIQKFLLRK 532
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
15-491 |
1.75e-61 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 209.90 E-value: 1.75e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 15 DKPAVIDhaKQTSWTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAAI 94
Cdd:PRK07470 22 DRIALVW--GDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPDEVAYL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 95 VEDAQLKLLFYAE---KHLSSLTDIDQNLLH-MDIDVAQ----YDEIVNPDYHQPFQATPVEPQDLAALIYTSGTTGSPK 166
Cdd:PRK07470 100 AEASGARAMICHAdfpEHAAAVRAASPDLTHvVAIGGARagldYEALVARHLGARVANAAVDHDDPCWFFFTSGTTGRPK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 167 GVMFSYE--SFVHNGANLELTYKFNSNYITIVSTPMFHVLGFNDtvLPVLMSGGTLIL--QRYFNGEELNDMIAQYHPTF 242
Cdd:PRK07470 180 AAVLTHGqmAFVITNHLADLMPGTTEQDASLVVAPLSHGAGIHQ--LCQVARGAATVLlpSERFDPAEVWALVERHRVTN 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 243 IIMIPT---MYYSTLRASNFNPENFRamdYIIQGGSqPL--PSIQAAFKQYGINIINGYGLTEAP---LVLVNTPENSKR 314
Cdd:PRK07470 258 LFTVPTilkMLVEHPAVDRYDHSSLR---YVIYAGA-PMyrADQKRALAKLGKVLVQYFGLGEVTgniTVLPPALHDAED 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 315 KPM----SIGKAVMFVDARILDDNGEEVPTGEIGELAIKAKNVTPGYWNKPAETAKAFHGRYLLTGDLAKMDNDGDIFII 390
Cdd:PRK07470 334 GPDarigTCGFERTGMEVQIQDDEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAFRDGWFRTGDLGHLDARGFLYIT 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 391 DRKKELIITGGENVLPSEVENALAEHPLVDRCVVVGYDHPKYGESIAAAIILREDEPHYAEILNQHMRSRLAGYKVPRMY 470
Cdd:PRK07470 414 GRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVARDGAPVDEAELLAWLDGKVARYKLPKRF 493
|
490 500
....*....|....*....|.
gi 584959700 471 VPVTHMPLNSTQKPDKLAIRQ 491
Cdd:PRK07470 494 FFWDALPKSGYGKITKKMVRE 514
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
15-495 |
2.05e-61 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 210.19 E-value: 2.05e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 15 DKPAVIDHAKQTSWtyQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAAI 94
Cdd:PRK08162 33 DRPAVIHGDRRRTW--AETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAASIAFM 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 95 VEDAQLKLLF----YAEKHLSSLTDID-QNLLHMDIDVAQY---DEIVNPDYHQ-------PFQATPvePQD---LAALI 156
Cdd:PRK08162 111 LRHGEAKVLIvdteFAEVAREALALLPgPKPLVIDVDDPEYpggRFIGALDYEAflasgdpDFAWTL--PADewdAIALN 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 157 YTSGTTGSPKGVMFSyesfvHNGANLELTykfnSNYIT---------IVSTPMFHVLG--FNDTVLpvlMSGGTLILQRY 225
Cdd:PRK08162 189 YTSGTTGNPKGVVYH-----HRGAYLNAL----SNILAwgmpkhpvyLWTLPMFHCNGwcFPWTVA---ARAGTNVCLRK 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 226 FNGEELNDMIAQYHPTFIIMIPTMYySTLraSNFNPENFRAMDYIIQG---GSQPLPSIQAAFKQYGINIINGYGLTE-- 300
Cdd:PRK08162 257 VDPKLIFDLIREHGVTHYCGAPIVL-SAL--INAPAEWRAGIDHPVHAmvaGAAPPAAVIAKMEEIGFDLTHVYGLTEty 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 301 APLVL---------VNTPENSKRKPMSIGKAVMFVDARILD-DNGEEVPT-GE-IGELAIKAKNVTPGYWNKPAETAKAF 368
Cdd:PRK08162 334 GPATVcawqpewdaLPLDERAQLKARQGVRYPLQEGVTVLDpDTMQPVPAdGEtIGEIMFRGNIVMKGYLKNPKATEEAF 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 369 HGRYLLTGDLAKMDNDGDIFIIDRKKELIITGGENVLPSEVENALAEHPLVDRCVVVGYDHPKYGESIAAAIILREDEPH 448
Cdd:PRK08162 414 AGGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDPKWGEVPCAFVELKDGASA 493
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 584959700 449 YAEILNQHMRSRLAGYKVPRMYVpVTHMPLNSTQKPDKLAIRQMMND 495
Cdd:PRK08162 494 TEEEIIAHCREHLAGFKVPKAVV-FGELPKTSTGKIQKFVLREQAKS 539
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
26-491 |
3.10e-61 |
|
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: 206.90 E-value: 3.10e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 26 TSWTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAAIVEDAQLKLLfy 105
Cdd:cd05971 5 EKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASAL-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 106 aekhlssLTDidqnllhmdidvaqydeivnpdyhqpfqatpvEPQDLAALIYTSGTTGSPKGVMFSYESFVHNGANLELT 185
Cdd:cd05971 83 -------VTD--------------------------------GSDDPALIIYTSGTTGPPKGALHAHRVLLGHLPGVQFP 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 186 YKFNSNYITIVSTPM--FHVLGFNDTVLPVLMSGGTLILQRY--FNGEELNDMIAQYHPTFIIMIPTmyysTLRASNFNP 261
Cdd:cd05971 124 FNLFPRDGDLYWTPAdwAWIGGLLDVLLPSLYFGVPVLAHRMtkFDPKAALDLMSRYGVTTAFLPPT----ALKMMRQQG 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 262 ENF----RAMDYIIQGGsQPL--PSIQAAFKQYGINIINGYGLTEAPLVLVNTPENSKRKPMSIGKAVMFVDARILDDNG 335
Cdd:cd05971 200 EQLkhaqVKLRAIATGG-ESLgeELLGWAREQFGVEVNEFYGQTECNLVIGNCSALFPIKPGSMGKPIPGHRVAIVDDNG 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 336 EEVPTGEIGELAIKAKNVTP--GYWNKPAETAKAFHGRYLLTGDLAKMDNDGDIFIIDRKKELIITGGENVLPSEVENAL 413
Cdd:cd05971 279 TPLPPGEVGEIAVELPDPVAflGYWNNPSATEKKMAGDWLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECL 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 414 AEHPLVDRCVVVGYDHPKYGESIAAAIILREDEPHYAEI---LNQHMRSRLAGYKVPRMYVPVTHMPLNSTQKPDKLAIR 490
Cdd:cd05971 359 LKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGETPSDALareIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRRELR 438
|
.
gi 584959700 491 Q 491
Cdd:cd05971 439 A 439
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
15-492 |
3.93e-61 |
|
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: 207.78 E-value: 3.93e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 15 DKPAVidHAKQTSWTYQQLNARADNMAHYLTSQGVKKGDVIGI------FAPndIAILdllfACFKTGAVFLPLNWRLNP 88
Cdd:cd05918 14 DAPAV--CAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLcfekskWAV--VAML----AVLKAGGAFVPLDPSHPL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 89 KEIAAIVEDAQLKLLfyaekhLSSltdidqnllhmdidvaqydeivnpdyhqpfqatpvEPQDLAALIYTSGTTGSPKGV 168
Cdd:cd05918 86 QRLQEILQDTGAKVV------LTS-----------------------------------SPSDAAYVIFTSGSTGKPKGV 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 169 MFSYESFV----HNGANLELT-----YKFnSNYITIVStpMFHVLGfndtvlpVLMSGGTLIL----QRYFNgeeLNDMI 235
Cdd:cd05918 125 VIEHRALStsalAHGRALGLTsesrvLQF-ASYTFDVS--ILEIFT-------TLAAGGCLCIpseeDRLND---LAGFI 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 236 AQYHPTFIIMIPTMyystlrASNFNPENFRAMDYIIQGGSQPLPSIQAAFKQyGINIINGYGLTEAPLVLVNTPENSKRK 315
Cdd:cd05918 192 NRLRVTWAFLTPSV------ARLLDPEDVPSLRTLVLGGEALTQSDVDTWAD-RVRLINAYGPAECTIAATVSPVVPSTD 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 316 PMSIGKAVMFVdARILD--DNGEEVPTGEIGELAIKAKNVTPGYWNKPAETAKAF--------------HGRYLLTGDLA 379
Cdd:cd05918 265 PRNIGRPLGAT-CWVVDpdNHDRLVPIGAVGELLIEGPILARGYLNDPEKTAAAFiedpawlkqegsgrGRRLYRTGDLV 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 380 KMDNDGDIFIIDRKKELIITGGENVLPSEVENALAEHPLVDRCVVVGYDHPKYGES---IAAAIILREDEPH-------- 448
Cdd:cd05918 344 RYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSLPGAKEVVVEVVKPKDGSSspqLVAFVVLDGSSSGsgdgdslf 423
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 584959700 449 ---------YAEILNQHMRSRLAGYKVPRMYVPVTHMPLNSTQKPDKLAIRQM 492
Cdd:cd05918 424 lepsdefraLVAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRALREL 476
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
15-468 |
6.17e-61 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 209.14 E-value: 6.17e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 15 DKPAVIDHAKqtSWTYQQLNARADNMAHYLTSQ-GVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEI-- 91
Cdd:PRK08974 38 DQPAFINMGE--VMTFRKLEERSRAFAAYLQNGlGLKKGDRVALMMPNLLQYPIALFGILRAGMIVVNVNPLYTPRELeh 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 92 -------AAIVEDAQL-----KLLFYAE-KH--LSSLTDI----DQNLLHMdidVAQYDEIVNPDYHQP----FQAT--- 145
Cdd:PRK08974 116 qlndsgaKAIVIVSNFahtleKVVFKTPvKHviLTRMGDQlstaKGTLVNF---VVKYIKRLVPKYHLPdaisFRSAlhk 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 146 --------P-VEPQDLAALIYTSGTTGSPKGVMFSYESFVhngANLEltyKFNSNY---------ITIVSTPMFHVLGFN 207
Cdd:PRK08974 193 grrmqyvkPeLVPEDLAFLQYTGGTTGVAKGAMLTHRNML---ANLE---QAKAAYgpllhpgkeLVVTALPLYHIFALT 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 208 DTVLPVLMSGGTLILqrYFNGEELNDMIA--QYHP-TFIIMIPTMYYSTLRASNFNPENFRAMDYIIQGGSqplpSIQAA 284
Cdd:PRK08974 267 VNCLLFIELGGQNLL--ITNPRDIPGFVKelKKYPfTAITGVNTLFNALLNNEEFQELDFSSLKLSVGGGM----AVQQA 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 285 F-----KQYGINIINGYGLTE-APLVLVNtPENSKRKPMSIGKAVMFVDARILDDNGEEVPTGEIGELAIKAKNVTPGYW 358
Cdd:PRK08974 341 VaerwvKLTGQYLLEGYGLTEcSPLVSVN-PYDLDYYSGSIGLPVPSTEIKLVDDDGNEVPPGEPGELWVKGPQVMLGYW 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 359 NKPAETAKAFHGRYLLTGDLAKMDNDGDIFIIDRKKELIITGGENVLPSEVENALAEHPLVDRCVVVGYDHPKYGESIAA 438
Cdd:PRK08974 420 QRPEATDEVIKDGWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAVKI 499
|
490 500 510
....*....|....*....|....*....|
gi 584959700 439 AIIlREDEPHYAEILNQHMRSRLAGYKVPR 468
Cdd:PRK08974 500 FVV-KKDPSLTEEELITHCRRHLTGYKVPK 528
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
15-489 |
6.84e-61 |
|
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: 206.39 E-value: 6.84e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 15 DKPAVIDHAKQTswTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAAI 94
Cdd:cd17643 2 EAVAVVDEDRRL--TYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 95 VEDAQLKLLFyaekhlssltdidqnllhmdidvaqydeivnpdyhqpfqatpVEPQDLAALIYTSGTTGSPKGVMFSYES 174
Cdd:cd17643 80 LADSGPSLLL------------------------------------------TDPDDLAYVIYTSGSTGRPKGVVVSHAN 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 175 FVHNGANLELTYKFNSNYITIvstpMFHVLGFNDTVLP---VLMSGGTLILQRYF---NGEELNDMIAQYHPTFIIMIPT 248
Cdd:cd17643 118 VLALFAATQRWFGFNEDDVWT----LFHSYAFDFSVWEiwgALLHGGRLVVVPYEvarSPEDFARLLRDEGVTVLNQTPS 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 249 MYYSTLRASNFNPENFRAMDYIIQGG-SQPLPSIQAAFKQYGIN---IINGYGLTEAPlVLVN----TPENSKRKPMS-I 319
Cdd:cd17643 194 AFYQLVEAADRDGRDPLALRYVIFGGeALEAAMLRPWAGRFGLDrpqLVNMYGITETT-VHVTfrplDAADLPAAAASpI 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 320 GKAVMFVDARILDDNGEEVPTGEIGELAIKAKNVTPGYWNKPAETAKAF--------HGRYLLTGDLAKMDNDGDIFIID 391
Cdd:cd17643 273 GRPLPGLRVYVLDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFvanpfggpGSRMYRTGDLARRLPDGELEYLG 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 392 RKKELIITGGENVLPSEVENALAEHPLVDRCVVVGYDHPKYGESIAAAIILREDEPHYAEILNQHMRSRLAGYKVPRMYV 471
Cdd:cd17643 353 RADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVADDGAAADIAELRALLKELLPDYMVPARYV 432
|
490
....*....|....*...
gi 584959700 472 PVTHMPLNSTQKPDKLAI 489
Cdd:cd17643 433 PLDALPLTVNGKLDRAAL 450
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
15-488 |
9.80e-61 |
|
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: 206.67 E-value: 9.80e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 15 DKPAVIDhaKQTSWTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAAI 94
Cdd:cd12117 12 DAVAVVY--GDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAERLAFM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 95 VEDAQLKLLFYAEKHLSSLTDIDQNLLHMDIDVAQydEIVNPdyhqpfqATPVEPQDLAALIYTSGTTGSPKGVMFSYES 174
Cdd:cd12117 90 LADAGAKVLLTDRSLAGRAGGLEVAVVIDEALDAG--PAGNP-------AVPVSPDDLAYVMYTSGSTGRPKGVAVTHRG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 175 ---FVHNGANLELT----YKFNSNYITIVSTpmFHVLGfndtvlpVLMSGGTLIL---QRYFNGEELNDMIAQYHPTfii 244
Cdd:cd12117 161 vvrLVKNTNYVTLGpddrVLQTSPLAFDAST--FEIWG-------ALLNGARLVLapkGTLLDPDALGALIAEEGVT--- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 245 mipTMYystLRASNFN------PENFRAMDYIIQGGSQ-PLPSIQAAFKQY-GINIINGYGLTEaplvlvNT-------- 308
Cdd:cd12117 229 ---VLW---LTAALFNqladedPECFAGLRELLTGGEVvSPPHVRRVLAACpGLRLVNGYGPTE------NTtfttshvv 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 309 -PENSKRKPMSIGKAVMFVDARILDDNGEEVPTGEIGELAIKAKNVTPGYWNKPAETAKAF-------HGRYLLTGDLAK 380
Cdd:cd12117 297 tELDEVAGSIPIGRPIANTRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFvadpfgpGERLYRTGDLAR 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 381 MDNDGDI-FI--IDRKKELiitGGENVLPSEVENALAEHPLVDRCVVVGYDHPKYGESIAAAIILREDEPhyAEILNQHM 457
Cdd:cd12117 377 WLPDGRLeFLgrIDDQVKI---RGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVVAEGALD--AAELRAFL 451
|
490 500 510
....*....|....*....|....*....|.
gi 584959700 458 RSRLAGYKVPRMYVPVTHMPLNSTQKPDKLA 488
Cdd:cd12117 452 RERLPAYMVPAAFVVLDELPLTANGKVDRRA 482
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
15-488 |
9.86e-61 |
|
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: 206.37 E-value: 9.86e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 15 DKPAVIDhaKQTSWTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAAI 94
Cdd:cd12116 2 DATAVRD--DDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 95 VEDAQLKLLfyaekhlssLTDID-QNLLHMDIDVAqydEIVNPDYHQPF--QATPVEPQDLAALIYTSGTTGSPKGVMFS 171
Cdd:cd12116 80 LEDAEPALV---------LTDDAlPDRLPAGLPVL---LLALAAAAAAPaaPRTPVSPDDLAYVIYTSGSTGRPKGVVVS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 172 YESFVHNGANLELTYKFN-SNYITIVSTPMFHVLGFnDTVLPvLMSGGTLIL-----QRyfNGEELNDMIAQYHPTFIIM 245
Cdd:cd12116 148 HRNLVNFLHSMRERLGLGpGDRLLAVTTYAFDISLL-ELLLP-LLAGARVVIapretQR--DPEALARLIEAHSITVMQA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 246 IPTMYYSTLRASNFNPENFRAMdyiiqGGSQPLPSIQAA-FKQYGINIINGYGLTEAPLVLVNTPENSKRKPMSIGKAVM 324
Cdd:cd12116 224 TPATWRMLLDAGWQGRAGLTAL-----CGGEALPPDLAArLLSRVGSLWNLYGPTETTIWSTAARVTAAAGPIPIGRPLA 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 325 FVDARILDDNGEEVPTGEIGELAIKAKNVTPGYWNKPAETAKAF--------HGRYLLTGDLAKMDNDGDIFIIDRKKEL 396
Cdd:cd12116 299 NTQVYVLDAALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFvpdpfagpGSRLYRTGDLVRRRADGRLEYLGRADGQ 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 397 IITGGENVLPSEVENALAEHPLVDRCVVVGyDHPKYGESIAAAIILREDEPHYAEILNQHMRSRLAGYKVPRMYVPVTHM 476
Cdd:cd12116 379 VKIRGHRIELGEIEAALAAHPGVAQAAVVV-REDGGDRRLVAYVVLKAGAAPDAAALRAHLRATLPAYMVPSAFVRLDAL 457
|
490
....*....|..
gi 584959700 477 PLNSTQKPDKLA 488
Cdd:cd12116 458 PLTANGKLDRKA 469
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
26-492 |
1.21e-60 |
|
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: 206.80 E-value: 1.21e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 26 TSWTYQQLNARADNMAHYLtSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAAIVEDAQLKLLFY 105
Cdd:cd05909 6 TSLTYRKLLTGAIALARKL-AKMTKEGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVLT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 106 AEKHLSSLT-------DIDQNLLHMD-----------IDVAQYDEIVNPDYHQPFQATPVEPQDLAALIYTSGTTGSPKG 167
Cdd:cd05909 85 SKQFIEKLKlhhlfdvEYDARIVYLEdlrakiskadkCKAFLAGKFPPKWLLRIFGVAPVQPDDPAVILFTSGSEGLPKG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 168 VMFSYESFVHNGANLELTYKFNSNYITIVSTPMFHVLGFNDTVLPVLMSGGTLILqrYFN---GEELNDMIAQYHPTFII 244
Cdd:cd05909 165 VVLSHKNLLANVEQITAIFDPNPEDVVFGALPFFHSFGLTGCLWLPLLSGIKVVF--HPNpldYKKIPELIYDKKATILL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 245 MIPTMYYSTLRASNfnPENFRAMDYIIQGGSQPLPSIQAAF-KQYGINIINGYGLTE-APLVLVNTPeNSKRKPMSIGKA 322
Cdd:cd05909 243 GTPTFLRGYARAAH--PEDFSSLRLVVAGAEKLKDTLRQEFqEKFGIRILEGYGTTEcSPVISVNTP-QSPNKEGTVGRP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 323 VMFVDARILD-DNGEEVPTGEIGELAIKAKNVTPGYWNKPAETAKAFHGRYLLTGDLAKMDNDGDIFIIDRKKELIITGG 401
Cdd:cd05909 320 LPGMEVKIVSvETHEEVPIGEGGLLLVRGPNVMLGYLNEPELTSFAFGDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 402 ENVLPSEVENALAEH-PLVDRCVVVGYDHPKYGESIAAAIILREDEPHYaeiLNQHMR-SRLAGYKVPRMYVPVTHMPLN 479
Cdd:cd05909 400 EMVSLEAIEDILSEIlPEDNEVAVVSVPDGRKGEKIVLLTTTTDTDPSS---LNDILKnAGISNLAKPSYIHQVEEIPLL 476
|
490
....*....|...
gi 584959700 480 STQKPDKLAIRQM 492
Cdd:cd05909 477 GTGKPDYVTLKAL 489
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
11-493 |
2.01e-60 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 207.60 E-value: 2.01e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 11 DFDD------DKPAVID----HAKQTSWTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFL 80
Cdd:PRK13295 29 DLDAcvascpDKTAVTAvrlgTGAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 81 PLNWRLNPKEIAAIVEDAQLKLL-----FYAEKHLSSLTDID------QNLLHMDIDVAQYDEIV--------NPDYHQP 141
Cdd:PRK13295 109 PLMPIFRERELSFMLKHAESKVLvvpktFRGFDHAAMARRLRpelpalRHVVVVGGDGADSFEALlitpaweqEPDAPAI 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 142 FQATPVEPQDLAALIYTSGTTGSPKGVMFSYESFVHNGANLELTYKFNSNYITIVSTPMFHVLGFNDTVLPVLMSGGTLI 221
Cdd:PRK13295 189 LARLRPGPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILMASPMAHQTGFMYGLMMPVMLGATAV 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 222 LQRYFNGEELNDMIAQYHPTFIiMIPTMYYSTL-RASNFNPENFRAMD-YIIQGGSQPLPSIQAAFKQYGINIINGYGLT 299
Cdd:PRK13295 269 LQDIWDPARAAELIRTEGVTFT-MASTPFLTDLtRAVKESGRPVSSLRtFLCAGAPIPGALVERARAALGAKIVSAWGMT 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 300 EAPLVLVNTPENS-KRKPMSIGKAVMFVDARILDDNGEEVPTGEIGELAIKAKNVTPGYWNKPAETAKAFHGrYLLTGDL 378
Cdd:PRK13295 348 ENGAVTLTKLDDPdERASTTDGCPLPGVEVRVVDADGAPLPAGQIGRLQVRGCSNFGGYLKRPQLNGTDADG-WFDTGDL 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 379 AKMDNDGDIFIIDRKKELIITGGENVLPSEVENALAEHPLVDRCVVVGYDHPKYGESIAAAIILRE----DEPHYAEILN 454
Cdd:PRK13295 427 ARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPRPgqslDFEEMVEFLK 506
|
490 500 510
....*....|....*....|....*....|....*....
gi 584959700 455 QHmrsRLAGYKVPRMYVPVTHMPLNSTQKPDKLAIRQMM 493
Cdd:PRK13295 507 AQ---KVAKQYIPERLVVRDALPRTPSGKIQKFRLREML 542
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
48-490 |
3.69e-60 |
|
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: 204.60 E-value: 3.69e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 48 GVKKGDVIGIFAPNDIAILDLLFACFKTGA----VFLPLNWRLNPKEIAAIVEDAQLKLLFyAEKHLSSLTDIDQNLLHM 123
Cdd:cd05922 14 GGVRGERVVLILPNRFTYIELSFAVAYAGGrlglVFVPLNPTLKESVLRYLVADAGGRIVL-ADAGAADRLRDALPASPD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 124 DIDVAQYDEIVnpDYHQPFQATPVEPQDLAALIYTSGTTGSPKGVMFSYESFVHNGANLELTYKFNSNYITIVSTPMFHV 203
Cdd:cd05922 93 PGTVLDADGIR--AARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADDRALTVLPLSYD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 204 LGFNdTVLPVLMSGGTLIL-QRYFNGEELNDMIAQYHPTFIIMIPTMYySTLRASNFNPENFRAMDYIIQGGSQPLPSIQ 282
Cdd:cd05922 171 YGLS-VLNTHLLRGATLVLtNDGVLDDAFWEDLREHGATGLAGVPSTY-AMLTRLGFDPAKLPSLRYLTQAGGRLPQETI 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 283 AAFKQY--GINIINGYGLTEA-PLVLVNTPENSKRKPMSIGKAVMFVDARILDDNGEEVPTGEIGELAIKAKNVTPGYWN 359
Cdd:cd05922 249 ARLRELlpGAQVYVMYGQTEAtRRMTYLPPERILEKPGSIGLAIPGGEFEILDDDGTPTPPGEPGEIVHRGPNVMKGYWN 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 360 KPAETAKAFHGRYLL-TGDLAKMDNDGDIFIIDRKKELIITGGENVLPSEVENALAEHPLVDRCVVVGYDHPKyGESIAA 438
Cdd:cd05922 329 DPPYRRKEGRGGGVLhTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDPL-GEKLAL 407
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 584959700 439 AIILR-EDEPHYAeilNQHMRSRLAGYKVPRMYVPVTHMPLNSTQKPDKLAIR 490
Cdd:cd05922 408 FVTAPdKIDPKDV---LRSLAERLPPYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
16-490 |
1.75e-59 |
|
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: 202.31 E-value: 1.75e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 16 KPAVIdHAKQTSwTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAAIV 95
Cdd:cd05919 1 KTAFY-AADRSV-TYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 96 EDAQLKLLFyaekhlssltdidqnllhmdidvaqydeivnpdyhqpfqatpVEPQDLAALIYTSGTTGSPKGVMfsyesf 175
Cdd:cd05919 79 RDCEARLVV------------------------------------------TSADDIAYLLYSSGTTGPPKGVM------ 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 176 vHNGANLELTYK-FNSNYI------TIVSTP-MFHVLGFNDTVLPVLMSGGTLILqryFNG----EELNDMIAQYHPTFI 243
Cdd:cd05919 111 -HAHRDPLLFADaMAREALgltpgdRVFSSAkMFFGYGLGNSLWFPLAVGASAVL---NPGwptaERVLATLARFRPTVL 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 244 IMIPTMYYSTLRASNFNPENFRAMDYIIQGGSqPLP-SIQAAFKQ-YGINIINGYGLTEA-PLVLVNTPENSKrkPMSIG 320
Cdd:cd05919 187 YGVPTFYANLLDSCAGSPDALRSLRLCVSAGE-ALPrGLGERWMEhFGGPILDGIGATEVgHIFLSNRPGAWR--LGSTG 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 321 KAVMFVDARILDDNGEEVPTGEIGELAIKAKNVTPGYWNKPAETAKAFHGRYLLTGDLAKMDNDGDIFIIDRKKELIITG 400
Cdd:cd05919 264 RPVPGYEIRLVDEEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKVG 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 401 GENVLPSEVENALAEHPLVDRCVVVGYDHPKYGESIAAAIIL-REDEPH--YAEILNQHMRSRLAGYKVPRMYVPVTHMP 477
Cdd:cd05919 344 GQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLkSPAAPQesLARDIHRHLLERLSAHKVPRRIAFVDELP 423
|
490
....*....|...
gi 584959700 478 LNSTQKPDKLAIR 490
Cdd:cd05919 424 RTATGKLQRFKLR 436
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
151-486 |
2.03e-58 |
|
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341292 [Multi-domain] Cd Length: 333 Bit Score: 196.34 E-value: 2.03e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 151 DLAALIYTSGTTGSPKGVMFSYESFVHNGANLELTYKFNSNYITIVSTPMFHVLGFNdTVLPVLMSGGTLILQRYFNGEE 230
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPLFHIAGLN-LALATFHAGGANVVMEKFDPAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 231 LNDMIAQYHPTFIIMIPTMYYSTLRASNFNPENFRAMDYIiqGGSQPLPSIQAAFKQYGINIINGYGLTEAPLVLVNTPe 310
Cdd:cd17637 80 ALELIEEEKVTLMGSFPPILSNLLDAAEKSGVDLSSLRHV--LGLDAPETIQRFEETTGATFWSLYGQTETSGLVTLSP- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 311 nSKRKPMSIGKAVMFVDARILDDNGEEVPTGEIGELAIKAKNVTPGYWNKPAETAKAFHGRYLLTGDLAKMDNDGDIFII 390
Cdd:cd17637 157 -YRERPGSAGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTFRNGWHHTGDLGRFDEDGYLWYA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 391 DRK--KELIITGGENVLPSEVENALAEHPLVDRCVVVGYDHPKYGESIAAAIILREDEPHYAEILNQHMRSRLAGYKVPR 468
Cdd:cd17637 236 GRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKPGATLTADELIEFVGSRIARYKKPR 315
|
330
....*....|....*...
gi 584959700 469 MYVPVTHMPLNSTQKPDK 486
Cdd:cd17637 316 YVVFVEALPKTADGSIDR 333
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
15-488 |
1.01e-57 |
|
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: 199.04 E-value: 1.01e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 15 DKPAVIDHAKQTswTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAAI 94
Cdd:cd17646 13 DAPAVVDEGRTL--TYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRLAYM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 95 VEDAQLKLLFYAEKHLSSLTDIDQNLLHMDIDVAQYDeivnPDYHQPfqatPVEPQDLAALIYTSGTTGSPKGVMFSYES 174
Cdd:cd17646 91 LADAGPAVVLTTADLAARLPAGGDVALLGDEALAAPP----ATPPLV----PPRPDNLAYVIYTSGSTGRPKGVMVTHAG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 175 FVHNGANLELTYKFNSNYITIVSTPmfhvLGFNDTV----LPvLMSGGTLILQRYFNGEE---LNDMIAQYHPTFIIMIP 247
Cdd:cd17646 163 IVNRLLWMQDEYPLGPGDRVLQKTP----LSFDVSVwelfWP-LVAGARLVVARPGGHRDpayLAALIREHGVTTCHFVP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 248 TMYYSTLRASnfNPENFRAMDYIIQGGsQPLPSIQAA--FKQYGINIINGYGLTEAPL--VLVNTPENSKRKPMSIGKAV 323
Cdd:cd17646 238 SMLRVFLAEP--AAGSCASLRRVFCSG-EALPPELAArfLALPGAELHNLYGPTEAAIdvTHWPVRGPAETPSVPIGRPV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 324 MFVDARILDDNGEEVPTGEIGELAIKAKNVTPGYWNKPAETAKAF-------HGRYLLTGDLAKMDNDGDIFIIDRKKEL 396
Cdd:cd17646 315 PNTRLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFvpdpfgpGSRMYRTGDLARWRPDGALEFLGRSDDQ 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 397 IITGGENVLPSEVENALAEHPLVDRCVVVGYDHPKYGESIAAAIILREDEPHY-AEILNQHMRSRLAGYKVPRMYVPVTH 475
Cdd:cd17646 395 VKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAAGAAGPdTAALRAHLAERLPEYMVPAAFVVLDA 474
|
490
....*....|...
gi 584959700 476 MPLNSTQKPDKLA 488
Cdd:cd17646 475 LPLTANGKLDRAA 487
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
15-488 |
4.76e-57 |
|
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: 195.93 E-value: 4.76e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 15 DKPAVIDHAKQTswTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAAI 94
Cdd:cd17652 2 DAPAVVFGDETL--TYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 95 VEDAQLKLLfyaekhlssLTdidqnllhmdidvaqydeivnpdyhqpfqatpvEPQDLAALIYTSGTTGSPKGVMFSyes 174
Cdd:cd17652 80 LADARPALL---------LT---------------------------------TPDNLAYVIYTSGSTGRPKGVVVT--- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 175 fvHNG-ANL--ELTYKFNSnyitivsTP-----MFHVLGFNDTVLPVLM---SGGTLIL---QRYFNGEELNDMIAQYHP 240
Cdd:cd17652 115 --HRGlANLaaAQIAAFDV-------GPgsrvlQFASPSFDASVWELLMallAGATLVLapaEELLPGEPLADLLREHRI 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 241 TFIIMIPtmyySTLRAsnFNPENFRAMDYIIQGGSQPLPSIQAAFKQyGINIINGYGLTEAPLVLVNTPENSKRKPMSIG 320
Cdd:cd17652 186 THVTLPP----AALAA--LPPDDLPDLRTLVVAGEACPAELVDRWAP-GRRMINAYGPTETTVCATMAGPLPGGGVPPIG 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 321 KAVMFVDARILDDNGEEVPTGEIGELAIKAKNVTPGYWNKPAETAKAF--------HGRYLLTGDLAKMDNDGDIFIIDR 392
Cdd:cd17652 259 RPVPGTRVYVLDARLRPVPPGVPGELYIAGAGLARGYLNRPGLTAERFvadpfgapGSRMYRTGDLARWRADGQLEFLGR 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 393 KKELIITGGENVLPSEVENALAEHPLVDRCVVVGYDHPKYGESIAAAIILREDEPHYAEILNQHMRSRLAGYKVPRMYVP 472
Cdd:cd17652 339 ADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAPGAAPTAAELRAHLAERLPGYMVPAAFVV 418
|
490
....*....|....*.
gi 584959700 473 VTHMPLNSTQKPDKLA 488
Cdd:cd17652 419 LDALPLTPNGKLDRRA 434
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
15-468 |
6.67e-57 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 198.45 E-value: 6.67e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 15 DKPAVIDHAKqtSWTYQQLNARADNMAHYLTSQ-GVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAA 93
Cdd:PRK05677 39 DKPAFSNLGK--TLTYGELYKLSGAFAAWLQQHtDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVNTNPLYTAREMEH 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 94 IVEDAQLKLLF-------YAEKHL----------SSLTDIDQNLLHMDID-VAQYDEIVNPDYH---------------- 139
Cdd:PRK05677 117 QFNDSGAKALVclanmahLAEKVLpktgvkhvivTEVADMLPPLKRLLINaVVKHVKKMVPAYHlpqavkfndalakgag 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 140 QPFQATPVEPQDLAALIYTSGTTGSPKGVMFSYESFVHN--------GANLEltykfNSNYITIVSTPMFHVLGFNDTVL 211
Cdd:PRK05677 197 QPVTEANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANmlqcralmGSNLN-----EGCEILIAPLPLYHIYAFTFHCM 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 212 PVLMSGGTLILQRyfNGEELNDMI---AQYHPTFIIMIPTMYYSTLRASNFNPENFRAMDYIIQGGSQPLPSIQAAFKQY 288
Cdd:PRK05677 272 AMMLIGNHNILIS--NPRDLPAMVkelGKWKFSGFVGLNTLFVALCNNEAFRKLDFSALKLTLSGGMALQLATAERWKEV 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 289 -GINIINGYGLTE-APLVLVNTPENSKrkPMSIGKAVMFVDARILDDNGEEVPTGEIGELAIKAKNVTPGYWNKPAETAK 366
Cdd:PRK05677 350 tGCAICEGYGMTEtSPVVSVNPSQAIQ--VGTIGIPVPSTLCKVIDDDGNELPLGEVGELCVKGPQVMKGYWQRPEATDE 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 367 AFHGR-YLLTGDLAKMDNDGDIFIIDRKKELIITGGENVLPSEVENALAEHPLVDRCVVVGYDHPKYGESIAAAIILRED 445
Cdd:PRK05677 428 ILDSDgWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIKVFVVVKPG 507
|
490 500
....*....|....*....|...
gi 584959700 446 EPHYAEILNQHMRSRLAGYKVPR 468
Cdd:PRK05677 508 ETLTKEQVMEHMRANLTGYKVPK 530
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
25-492 |
9.65e-57 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 198.32 E-value: 9.65e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 25 QTSWTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAAIVEDAQLKLLF 104
Cdd:PLN03102 37 KTRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILF 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 105 -------YAEKHLSSLTDIDQNLLHMDIDVAQYDEIVNP-----DYH---QPFQATPV---------EPQDLAALIYTSG 160
Cdd:PLN03102 117 vdrsfepLAREVLHLLSSEDSNLNLPVIFIHEIDFPKRPsseelDYEcliQRGEPTPSlvarmfriqDEHDPISLNYTSG 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 161 TTGSPKGVMFSyesfvHNGANLE-----LTYKFNSNYITIVSTPMFHVLGFNDTvLPVLMSGGTLILQRYFNGEELNDMI 235
Cdd:PLN03102 197 TTADPKGVVIS-----HRGAYLStlsaiIGWEMGTCPVYLWTLPMFHCNGWTFT-WGTAARGGTSVCMRHVTAPEIYKNI 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 236 AQYHPTFIIMIPTMYYSTLRASNFNPENFRAMDYIIQGGSQPLPSIQAAFKQYGINIINGYGLTEA--PLVLVN------ 307
Cdd:PLN03102 271 EMHNVTHMCCVPTVFNILLKGNSLDLSPRSGPVHVLTGGSPPPAALVKKVQRLGFQVMHAYGLTEAtgPVLFCEwqdewn 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 308 -TPENSK-----RKPMSIgKAVMFVDARIlDDNGEEVPTG--EIGELAIKAKNVTPGYWNKPAETAKAFHGRYLLTGDLA 379
Cdd:PLN03102 351 rLPENQQmelkaRQGVSI-LGLADVDVKN-KETQESVPRDgkTMGEIVIKGSSIMKGYLKNPKATSEAFKHGWLNTGDVG 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 380 KMDNDGDIFIIDRKKELIITGGENVLPSEVENALAEHPLVDRCVVVGYDHPKYGESIAAAIILREDEPHYAEI------- 452
Cdd:PLN03102 429 VIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGETTKEDRvdklvtr 508
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 584959700 453 ---LNQHMRSRLAGYKVPRMYVPVTHMPLNSTQKPDKLAIRQM 492
Cdd:PLN03102 509 erdLIEYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKLRDI 551
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
15-495 |
1.56e-56 |
|
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: 196.91 E-value: 1.56e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 15 DKPAVIDHAKQtsWTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGA--VF-LPLNWRLnpkEI 91
Cdd:COG1021 40 DRIAVVDGERR--LSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAipVFaLPAHRRA---EI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 92 AAIVEDAQLKLLFYAEKHL--------SSLTDIDQNLLHMDI-----DVAQYDEIVNPDYHQPFQATPvePQDLAALIYT 158
Cdd:COG1021 115 SHFAEQSEAVAYIIPDRHRgfdyralaRELQAEVPSLRHVLVvgdagEFTSLDALLAAPADLSEPRPD--PDDVAFFQLS 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 159 SGTTGSPKGVMFSYESFVHNG-ANLELTyKFNSNYITIVSTPMFH--------VLGfndtvlpVLMSGGTLILQRYFNGE 229
Cdd:COG1021 193 GGTTGLPKLIPRTHDDYLYSVrASAEIC-GLDADTVYLAALPAAHnfplsspgVLG-------VLYAGGTVVLAPDPSPD 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 230 ELNDMIAQYHPTFIIMIPTMYYSTLRASNFNPENFRAMDyIIQGGSQPLPS-----IQAAFkqyGINIINGYGLTEAplv 304
Cdd:COG1021 265 TAFPLIERERVTVTALVPPLALLWLDAAERSRYDLSSLR-VLQVGGAKLSPelarrVRPAL---GCTLQQVFGMAEG--- 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 305 LVNT-----PE----NSKRKPMSIGKAVmfvdaRILDDNGEEVPTGEIGELAIKAKNVTPGYWNKPAETAKAF--HGRYL 373
Cdd:COG1021 338 LVNYtrlddPEevilTTQGRPISPDDEV-----RIVDEDGNPVPPGEVGELLTRGPYTIRGYYRAPEHNARAFtpDGFYR 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 374 lTGDLAKMDNDGDIFIIDRKKELIITGGENVLPSEVENALAEHPLVDRCVVVGYDHPKYGESIAAAIILREDEPHYAEiL 453
Cdd:COG1021 413 -TGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGERSCAFVVPRGEPLTLAE-L 490
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 584959700 454 NQHMRSR-LAGYKVPRMYVPVTHMPLNSTQKPDKLAIRQMMND 495
Cdd:COG1021 491 RRFLRERgLAAFKLPDRLEFVDALPLTAVGKIDKKALRAALAA 533
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
14-486 |
2.53e-55 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 193.36 E-value: 2.53e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 14 DDKPAVI--DHAKQTS-WTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKE 90
Cdd:PRK08008 21 GHKTALIfeSSGGVVRrYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 91 IAAIVEDAQLKLLFYAEKHLSSLTDIDQ-------NLLHMDIDVAQYDEIVNPDY---HQPFQ---ATPVEPQDLAALIY 157
Cdd:PRK08008 101 SAWILQNSQASLLVTSAQFYPMYRQIQQedatplrHICLTRVALPADDGVSSFTQlkaQQPATlcyAPPLSTDDTAEILF 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 158 TSGTTGSPKGVMFSYESFVHNG--ANLELTYKFNSNYITIVstPMFHVlGFNDTV-LPVLMSGGTLILQRYFNGEELNDM 234
Cdd:PRK08008 181 TSGTTSRPKGVVITHYNLRFAGyySAWQCALRDDDVYLTVM--PAFHI-DCQCTAaMAAFSAGATFVLLEKYSARAFWGQ 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 235 IAQYHPTFIIMIPtMYYSTLRASNFNPEN----FRAMDYIIQGGSQPlpsiQAAFKQ-YGINIINGYGLTEAPLVLVNTP 309
Cdd:PRK08008 258 VCKYRATITECIP-MMIRTLMVQPPSANDrqhcLREVMFYLNLSDQE----KDAFEErFGVRLLTSYGMTETIVGIIGDR 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 310 ENSKRKPMSIGKAVMFVDARILDDNGEEVPTGEIGELAIKA---KNVTPGYWNKPAETAKAFHGR-YLLTGDLAKMDNDG 385
Cdd:PRK08008 333 PGDKRRWPSIGRPGFCYEAEIRDDHNRPLPAGEIGEICIKGvpgKTIFKEYYLDPKATAKVLEADgWLHTGDTGYVDEEG 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 386 DIFIIDRKKELIITGGENVLPSEVENALAEHPLVDRCVVVGYDHPKYGESIAAAIILREDEPHYAEILNQHMRSRLAGYK 465
Cdd:PRK08008 413 FFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEEEFFAFCEQNMAKFK 492
|
490 500
....*....|....*....|.
gi 584959700 466 VPRMYVPVTHMPLNSTQKPDK 486
Cdd:PRK08008 493 VPSYLEIRKDLPRNCSGKIIK 513
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
15-490 |
8.77e-55 |
|
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: 190.27 E-value: 8.77e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 15 DKPAVIdHAKQtSWTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAAI 94
Cdd:cd17649 2 DAVALV-FGDQ-SLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 95 VEDAQLKLLfyaekhlssltdidqnLLHmdidvaqydeivnpdyhqpfqatpvEPQDLAALIYTSGTTGSPKGVMFSYES 174
Cdd:cd17649 80 LEDSGAGLL----------------LTH-------------------------HPRQLAYVIYTSGSTGTPKGVAVSHGP 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 175 FVHNGANLELTYKFNSNYITIVSTPmFHVLGFNDTVLPVLMSGGTLIL---QRYFNGEELNDMIAQYHPTfIIMIPTMYY 251
Cdd:cd17649 119 LAAHCQATAERYGLTPGDRELQFAS-FNFDGAHEQLLPPLICGACVVLrpdELWASADELAEMVRELGVT-VLDLPPAYL 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 252 STL--RASNFNPENFRAMDYIIQGGSQPLPSIQAAFKQYGINIINGYGLTEA---PLVLVNTPENSKRKP-MSIGKAVMF 325
Cdd:cd17649 197 QQLaeEADRTGDGRPPSLRLYIFGGEALSPELLRRWLKAPVRLFNAYGPTEAtvtPLVWKCEAGAARAGAsMPIGRPLGG 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 326 VDARILDDNGEEVPTGEIGELAIKAKNVTPGYWNKPAETAKAF--------HGRYLLTGDLAKMDNDGDIFIIDRKKELI 397
Cdd:cd17649 277 RSAYILDADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFvpdpfgapGSRLYRTGDLARWRDDGVIEYLGRVDHQV 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 398 ITGGENVLPSEVENALAEHPLVDRCVVVGYDHPKyGESIAAAIILREDE--PHYAEILNQHMRSRLAGYKVPRMYVPVTH 475
Cdd:cd17649 357 KIRGFRIELGEIEAALLEHPGVREAAVVALDGAG-GKQLVAYVVLRAAAaqPELRAQLRTALRASLPDYMVPAHLVFLAR 435
|
490
....*....|....*
gi 584959700 476 MPLNSTQKPDKLAIR 490
Cdd:cd17649 436 LPLTPNGKLDRKALP 450
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
15-489 |
8.51e-54 |
|
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: 188.07 E-value: 8.51e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 15 DKPAVIDHAKQtsWTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAAI 94
Cdd:cd17656 3 DAVAVVFENQK--LTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 95 VEDAQLKLLFYAEKHLSSLTDIDQNLLHMDIDVAQYDEiVNPDYHqpfqatpVEPQDLAALIYTSGTTGSPKGVMFSYES 174
Cdd:cd17656 81 MLDSGVRVVLTQRHLKSKLSFNKSTILLEDPSISQEDT-SNIDYI-------NNSDDLLYIIYTSGTTGKPKGVQLEHKN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 175 FV--------HNGANLE------LTYKFNSNYITIVSTpmfhvlgfndtvlpvLMSGGTLILQR---YFNGEELNDMIAQ 237
Cdd:cd17656 153 MVnllhfereKTNINFSdkvlqfATCSFDVCYQEIFST---------------LLSGGTLYIIReetKRDVEQLFDLVKR 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 238 yHPTFIIMIPTMYYSTL-RASNFNPENFRAMDYIIQGGSQPLPS--IQAAFKQYGINIINGYGLTEAPLVLVNT--PENS 312
Cdd:cd17656 218 -HNIEVVFLPVAFLKFIfSEREFINRFPTCVKHIITAGEQLVITneFKEMLHEHNVHLHNHYGPSETHVVTTYTinPEAE 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 313 KRKPMSIGKAVMFVDARILDDNGEEVPTGEIGELAIKAKNVTPGYWNKPAETAKAF-------HGRYLLTGDLAKMDNDG 385
Cdd:cd17656 297 IPELPPIGKPISNTWIYILDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFfpdpfdpNERMYRTGDLARYLPDG 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 386 DIFIIDRKKELIITGGENVLPSEVENALAEHPLVDRCVVVGYDHPKyGESIAAAIILREDEPHYAEiLNQHMRSRLAGYK 465
Cdd:cd17656 377 NIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDK-GEKYLCAYFVMEQELNISQ-LREYLAKQLPEYM 454
|
490 500
....*....|....*....|....
gi 584959700 466 VPRMYVPVTHMPLNSTQKPDKLAI 489
Cdd:cd17656 455 IPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
16-490 |
9.55e-54 |
|
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: 186.92 E-value: 9.55e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 16 KPAVIdhAKQTSWTYQQLNARADNMAHYLTSQGV-KKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAAI 94
Cdd:cd05958 1 RTCLR--SPEREWTYRDLLALANRIANVLVGELGiVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 95 VEDAQLKLLFYAEKhlssLTDIDqnllhmdidvaqydeivnpdyhqpfqatpvepqDLAALIYTSGTTGSPKGVMFSYES 174
Cdd:cd05958 79 LDKARITVALCAHA----LTASD---------------------------------DICILAFTSGTTGAPKATMHFHRD 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 175 FvhnganLELTYKFNSNYI-------TIVSTPMFHVLGFNDTVLPVLMSGGTLILQRYFNGEELNDMIAQYHPTFIIMIP 247
Cdd:cd05958 122 P------LASADRYAVNVLrlreddrFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEEATPDLLLSAIARYKPTVLFTAP 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 248 TMYYSTLRASNFNPENFRAMDYIIQGGSQ-PLPSIQAAFKQYGINIINGYGLTEAPLVLVNTPENSKRkPMSIGKAVMFV 326
Cdd:cd05958 196 TAYRAMLAHPDAAGPDLSSLRKCVSAGEAlPAALHRAWKEATGIPIIDGIGSTEMFHIFISARPGDAR-PGATGKPVPGY 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 327 DARILDDNGEEVPTGEIGELAIKAKNvtpGYW-NKPAETAKAFHGRYLLTGDLAKMDNDGDIFIIDRKKELIITGGENVL 405
Cdd:cd05958 275 EAKVVDDEGNPVPDGTIGRLAVRGPT---GCRyLADKRQRTYVQGGWNITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIA 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 406 PSEVENALAEHPLVDRCVVVGYDHPKYGESIAAAIILREDE---PHYAEILNQHMRSRLAGYKVPRMYVPVTHMPLNSTQ 482
Cdd:cd05958 352 PPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVipgPVLARELQDHAKAHIAPYKYPRAIEFVTELPRTATG 431
|
....*...
gi 584959700 483 KPDKLAIR 490
Cdd:cd05958 432 KLQRFALR 439
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
15-468 |
1.44e-53 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 189.46 E-value: 1.44e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 15 DKPAVIDHAKqtSWTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAAI 94
Cdd:PRK07059 38 DRPAFICMGK--AITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVNPLYTPRELEHQ 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 95 VEDAQLKLLFYAEKHLSSLTDIDQNLLHMDIDVAQYDE-------IVN---------------PDYH-----------QP 141
Cdd:PRK07059 116 LKDSGAEAIVVLENFATTVQQVLAKTAVKHVVVASMGDllgfkghIVNfvvrrvkkmvpawslPGHVrfndalaegarQT 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 142 FQATPVEPQDLAALIYTSGTTGSPKGVMFSYESFVHNGANLEL-------TYKFNSNYITIVSTPMFHVLGFNDTVLPVL 214
Cdd:PRK07059 196 FKPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVLQMEAwlqpafeKKPRPDQLNFVCALPLYHIFALTVCGLLGM 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 215 MSGGTLILqrYFNGEELNDMIAQYHPTFIIMIPTMyySTLRASNFNPENFRAMDY----IIQGGSQplpSIQAA-----F 285
Cdd:PRK07059 276 RTGGRNIL--IPNPRDIPGFIKELKKYQVHIFPAV--NTLYNALLNNPDFDKLDFskliVANGGGM---AVQRPvaerwL 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 286 KQYGINIINGYGLTEAPLVLVNTPENSKRKPMSIGKAVMFVDARILDDNGEEVPTGEIGELAIKAKNVTPGYWNKPAETA 365
Cdd:PRK07059 349 EMTGCPITEGYGLSETSPVATCNPVDATEFSGTIGLPLPSTEVSIRDDDGNDLPLGEPGEICIRGPQVMAGYWNRPDETA 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 366 KA-FHGRYLLTGDLAKMDNDGDIFIIDRKKELIITGGENVLPSEVENALAEHPLVDRCVVVGYDHPKYGESIAAAIILRE 444
Cdd:PRK07059 429 KVmTADGFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGEAVKLFVVKKD 508
|
490 500
....*....|....*....|....
gi 584959700 445 DEPHYAEILnQHMRSRLAGYKVPR 468
Cdd:PRK07059 509 PALTEEDVK-AFCKERLTNYKRPK 531
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
15-489 |
5.74e-53 |
|
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: 185.21 E-value: 5.74e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 15 DKPAVidHAKQTSWTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAAI 94
Cdd:cd12115 14 DAIAL--VCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPERLRFI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 95 VEDAQLKLLfyaekhlssLTDidqnllhmdidvaqydeivnpdyhqpfqatpvePQDLAALIYTSGTTGSPKGVMFSYes 174
Cdd:cd12115 92 LEDAQARLV---------LTD---------------------------------PDDLAYVIYTSGSTGRPKGVAIEH-- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 175 fvHNGANLELTYK--FNSNYITIV--STPMFHVLGFNDTVLPvLMSGGTLILQRyfNGEELNDMIAQYHPTFIIMIPTMY 250
Cdd:cd12115 128 --RNAAAFLQWAAaaFSAEELAGVlaSTSICFDLSVFELFGP-LATGGKVVLAD--NVLALPDLPAAAEVTLINTVPSAA 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 251 YSTLRASNFnPENFRAMDYiiqgGSQPLP-----SIQAafKQYGINIINGYGLTEA---PLVLVNTPENSKrkPMSIGKA 322
Cdd:cd12115 203 AELLRHDAL-PASVRVVNL----AGEPLPrdlvqRLYA--RLQVERVVNLYGPSEDttySTVAPVPPGASG--EVSIGRP 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 323 VMFVDARILDDNGEEVPTGEIGELAIKAKNVTPGYWNKPAETAKAF-------HGRYLLTGDLAKMDNDGDIFIIDRKKE 395
Cdd:cd12115 274 LANTQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFlpdpfgpGARLYRTGDLVRWRPDGLLEFLGRADN 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 396 LIITGGENVLPSEVENALAEHPLVDRCVVVGYDHPKYGESIAAAIILREDEPHYAEILNQHMRSRLAGYKVPRMYVPVTH 475
Cdd:cd12115 354 QVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEPGAAGLVEDLRRHLGTRLPAYMVPSRFVRLDA 433
|
490
....*....|....
gi 584959700 476 MPLNSTQKPDKLAI 489
Cdd:cd12115 434 LPLTPNGKIDRSAL 447
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
28-497 |
5.88e-53 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 187.22 E-value: 5.88e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 28 WTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAAIVEDAQLKLLFY-- 105
Cdd:PRK07008 40 YTYRDCERRAKQLAQALAALGVEPGDRVGTLAWNGYRHLEAYYGVSGSGAVCHTINPRLFPEQIAYIVNHAEDRYVLFdl 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 106 --------------AEKHLSSLTDIDQnLLHMDIDVAQYDEIV---NPDYHQPfqatPVEPQDLAALIYTSGTTGSPKGV 168
Cdd:PRK07008 120 tflplvdalapqcpNVKGWVAMTDAAH-LPAGSTPLLCYETLVgaqDGDYDWP----RFDENQASSLCYTSGTTGNPKGA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 169 MFSYESFV-HN-GANLELTYKFNSNYITIVSTPMFHVlgfNDTVLP--VLMSGGTLILQ-RYFNGEELNDMIAQYHPTFI 243
Cdd:PRK07008 195 LYSHRSTVlHAyGAALPDAMGLSARDAVLPVVPMFHV---NAWGLPysAPLTGAKLVLPgPDLDGKSLYELIEAERVTFS 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 244 IMIPTMYYSTLRASNFNPENFRAMDYIIQGGSQPLPSIQAAFKQ-YGINIINGYGLTE-APLVLVNT--------PENSK 313
Cdd:PRK07008 272 AGVPTVWLGLLNHMREAGLRFSTLRRTVIGGSACPPAMIRTFEDeYGVEVIHAWGMTEmSPLGTLCKlkwkhsqlPLDEQ 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 314 RK-PMSIGKAVMFVDARILDDNGEEVP-TGE-IGELAIKAKNVTPGYWNKpaeTAKAFHGRYLLTGDLAKMDNDGDIFII 390
Cdd:PRK07008 352 RKlLEKQGRVIYGVDMKIVGDDGRELPwDGKaFGDLQVRGPWVIDRYFRG---DASPLVDGWFPTGDVATIDADGFMQIT 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 391 DRKKELIITGGENVLPSEVENALAEHPLVDRCVVVGYDHPKYGESIAAAIILREDEPHYAEILNQHMRSRLAGYKVPRMY 470
Cdd:PRK07008 429 DRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLVVVKRPGAEVTREELLAFYEGKVAKWWIPDDV 508
|
490 500
....*....|....*....|....*..
gi 584959700 471 VPVTHMPLNSTQKPDKLAIRQMMNDKV 497
Cdd:PRK07008 509 VFVDAIPHTATGKLQKLKLREQFRDYV 535
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
4-489 |
8.41e-53 |
|
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: 185.61 E-value: 8.41e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 4 DWIKTRSDFDDDKPAVIDhaKQTSWTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAV---FL 80
Cdd:cd05920 19 DLLARSAARHPDRIAVVD--GDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAVpvlAL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 81 PLNWRLnpkEIAAIVEDAQLKLLFYAEKHlssltdidqnllhmdidvAQYDEivNPDYHQPFQATPvepqDLAALIYTSG 160
Cdd:cd05920 97 PSHRRS---ELSAFCAHAEAVAYIVPDRH------------------AGFDH--RALARELAESIP----EVALFLLSGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 161 TTGSPKGVMFSYESFVHN-GANLELTyKFNSNYITIVSTPMFHvlGFNDT---VLPVLMSGGTLILQRYFNGEELNDMIA 236
Cdd:cd05920 150 TTGTPKLIPRTHNDYAYNvRASAEVC-GLDQDTVYLAVLPAAH--NFPLAcpgVLGTLLAGGRVVLAPDPSPDAAFPLIE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 237 QYHPTFIIMIPTMYYSTLRASNFNPENFRAMDyIIQGGSQPLPSIQAAF--KQYGINIINGYGLTEAplvLVN-----TP 309
Cdd:cd05920 227 REGVTVTALVPALVSLWLDAAASRRADLSSLR-LLQVGGARLSPALARRvpPVLGCTLQQVFGMAEG---LLNytrldDP 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 310 E----NSKRKPMSIGKAVmfvdaRILDDNGEEVPTGEIGELAIKAKNVTPGYWNKPAETAKAF--HGRYLlTGDLAKMDN 383
Cdd:cd05920 303 DeviiHTQGRPMSPDDEI-----RVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFtpDGFYR-TGDLVRRTP 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 384 DGDIFIIDRKKELIITGGENVLPSEVENALAEHPLVDRCVVVGYDHPKYGESIAAAIILREDEPHYAEiLNQHMRSR-LA 462
Cdd:cd05920 377 DGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVLRDPPPSAAQ-LRRFLRERgLA 455
|
490 500
....*....|....*....|....*..
gi 584959700 463 GYKVPRMYVPVTHMPLNSTQKPDKLAI 489
Cdd:cd05920 456 AYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
15-469 |
1.05e-52 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 187.01 E-value: 1.05e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 15 DKPAVidHAKQTSWTYQQLNARADNMAHYLTSQ-GVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAA 93
Cdd:PRK08751 40 DRPAY--HSFGKTITYREADQLVEQFAAYLLGElQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKH 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 94 IVEDAQLKLLFYAEKHLSSLTDI--DQNLLHMDID----------------VAQYDEIVNPDYHQP-------------- 141
Cdd:PRK08751 118 QLIDSGASVLVVIDNFGTTVQQViaDTPVKQVITTglgdmlgfpkaalvnfVVKYVKKLVPEYRINgairfrealalgrk 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 142 --FQATPVEPQDLAALIYTSGTTGSPKGVMFSYESFVHN----GANLELTYKFNS-NYITIVSTPMFHVLGFNDTVLPVL 214
Cdd:PRK08751 198 hsMPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANmqqaHQWLAGTGKLEEgCEVVITALPLYHIFALTANGLVFM 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 215 MSGGT--LILqryfNGEELNDMIAQYHP---TFIIMIPTMYYSTLRASNFNPENFRAMDYIIQGGSQPLPSIQAAFKQY- 288
Cdd:PRK08751 278 KIGGCnhLIS----NPRDMPGFVKELKKtrfTAFTGVNTLFNGLLNTPGFDQIDFSSLKMTLGGGMAVQRSVAERWKQVt 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 289 GINIINGYGLTEA-PLVLVNtPENSKRKPMSIGKAVMFVDARILDDNGEEVPTGEIGELAIKAKNVTPGYWNKPAETAKA 367
Cdd:PRK08751 354 GLTLVEAYGLTETsPAACIN-PLTLKEYNGSIGLPIPSTDACIKDDAGTVLAIGEIGELCIKGPQVMKGYWKRPEETAKV 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 368 FHGR-YLLTGDLAKMDNDGDIFIIDRKKELIITGGENVLPSEVENALAEHPLVDRCVVVGYDHPKYGEsIAAAIILREDE 446
Cdd:PRK08751 433 MDADgWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGE-IVKVVIVKKDP 511
|
490 500
....*....|....*....|...
gi 584959700 447 PHYAEILNQHMRSRLAGYKVPRM 469
Cdd:PRK08751 512 ALTAEDVKAHARANLTGYKQPRI 534
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
15-489 |
1.82e-52 |
|
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: 184.84 E-value: 1.82e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 15 DKPAVIDHAKQTswTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLnPKE-IAA 93
Cdd:cd17655 12 DHTAVVFEDQTL--TYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDY-PEErIQY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 94 IVEDAQLKLLFyAEKHLSSLTDIDQNLLHMDIDVAQYDEIVNpdyhqpfQATPVEPQDLAALIYTSGTTGSPKGVMFSYE 173
Cdd:cd17655 89 ILEDSGADILL-TQSHLQPPIAFIGLIDLLDEDTIYHEESEN-------LEPVSKSDDLAYVIYTSGSTGKPKGVMIEHR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 174 SFVHnganleLTYKFNSNYI--TIVSTPMFHVLGFNDTV---LPVLMSGGTLILQRY---FNGEELNDMIAQYHPTFIIM 245
Cdd:cd17655 161 GVVN------LVEWANKVIYqgEHLRVALFASISFDASVteiFASLLSGNTLYIVRKetvLDGQALTQYIRQNRITIIDL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 246 IPTmYYSTLRASNFNPEnFRAMDYIIQGGSQPLPSIQAAFKQYG--INIINGYGLTEAPL---VLVNTPENSKRKPMSIG 320
Cdd:cd17655 235 TPA-HLKLLDAADDSEG-LSLKHLIVGGEALSTELAKKIIELFGtnPTITNAYGPTETTVdasIYQYEPETDQQVSVPIG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 321 KAVMFVDARILDDNGEEVPTGEIGELAIKAKNVTPGYWNKPAETAKAF-------HGRYLLTGDLAKMDNDGDIFIIDRK 393
Cdd:cd17655 313 KPLGNTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFvddpfvpGERMYRTGDLARWLPDGNIEFLGRI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 394 KELIITGGENVLPSEVENALAEHPLVDRCVVV---GYDHPKYgesIAAAIILREDEPhyAEILNQHMRSRLAGYKVPRMY 470
Cdd:cd17655 393 DHQVKIRGYRIELGEIEARLLQHPDIKEAVVIarkDEQGQNY---LCAYIVSEKELP--VAQLREFLARELPDYMIPSYF 467
|
490
....*....|....*....
gi 584959700 471 VPVTHMPLNSTQKPDKLAI 489
Cdd:cd17655 468 IKLDEIPLTPNGKVDRKAL 486
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
15-489 |
3.97e-52 |
|
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: 183.05 E-value: 3.97e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 15 DKPAVIDHAKQTswTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLnPKE-IAA 93
Cdd:cd17650 2 DAIAVSDATRQL--TYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDY-PAErLQY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 94 IVEDAQLKLLFyaekhlssltdidqnllhmdidvaqydeivnpdyhqpfqatpVEPQDLAALIYTSGTTGSPKGVMFSYE 173
Cdd:cd17650 79 MLEDSGAKLLL------------------------------------------TQPEDLAYVIYTSGTTGKPKGVMVEHR 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 174 SFVHNGANLELTYKFNSNYITIVSTPMFHVLGFNDTVLPVLMSGGTLIL---QRYFNGEELNDMIAQYHPTFIIMIPTMY 250
Cdd:cd17650 117 NVAHAAHAWRREYELDSFPVRLLQMASFSFDVFAGDFARSLLNGGTLVIcpdEVKLDPAALYDLILKSRITLMESTPALI 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 251 YSTLRASNFNPENFRAMDYIIQGG----SQPLPSIQAAFKQyGINIINGYGLTEAPLVLVNTPENSKRKPMS----IGKA 322
Cdd:cd17650 197 RPVMAYVYRNGLDLSAMRLLIVGSdgckAQDFKTLAARFGQ-GMRIINSYGVTEATIDSTYYEEGRDPLGDSanvpIGRP 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 323 VMFVDARILDDNGEEVPTGEIGELAIKAKNVTPGYWNKPAETAKAF-------HGRYLLTGDLAKMDNDGDIFIIDRKKE 395
Cdd:cd17650 276 LPNTAMYVLDERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFvenpfapGERMYRTGDLARWRADGNVELLGRVDH 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 396 LIITGGENVLPSEVENALAEHPLVDRCVVVgYDHPKYGESIAAAIILREDEPHYAEiLNQHMRSRLAGYKVPRMYVPVTH 475
Cdd:cd17650 356 QVKIRGFRIELGEIESQLARHPAIDEAVVA-VREDKGGEARLCAYVVAAATLNTAE-LRAFLAKELPSYMIPSYYVQLDA 433
|
490
....*....|....
gi 584959700 476 MPLNSTQKPDKLAI 489
Cdd:cd17650 434 LPLTPNGKVDRRAL 447
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
151-491 |
5.02e-52 |
|
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: 179.06 E-value: 5.02e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 151 DLAALIYTSGTTGSPKGVMFSYESFVHNGANLELTYKFNSNYITIVSTPMFHVLGFNdTVLPVLMSGGTLILQRYFNGEE 230
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLYHVGGLA-ILVRSLLAGAELVLLERNQALA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 231 LNdmIAQYHPTFIIMIPTMYYSTLRASnFNPENFRAMDYIIQGGSqPLPS-IQAAFKQYGINIINGYGLTE-APLVLVNT 308
Cdd:cd17630 80 ED--LAPPGVTHVSLVPTQLQRLLDSG-QGPAALKSLRAVLLGGA-PIPPeLLERAADRGIPLYTTYGMTEtASQVATKR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 309 PENSKRKpmSIGKAVMFVDARILDDngeevptgeiGELAIKAKNVTPGYWNKPAETAKA----FHgryllTGDLAKMDND 384
Cdd:cd17630 156 PDGFGRG--GVGVLLPGRELRIVED----------GEIWVGGASLAMGYLRGQLVPEFNedgwFT-----TKDLGELHAD 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 385 GDIFIIDRKKELIITGGENVLPSEVENALAEHPLVDRCVVVGYDHPKYGESIAAAIILREDEPHyaEILNQHMRSRLAGY 464
Cdd:cd17630 219 GRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRGPADP--AELRAWLKDKLARF 296
|
330 340
....*....|....*....|....*..
gi 584959700 465 KVPRMYVPVTHMPLNSTQKPDKLAIRQ 491
Cdd:cd17630 297 KLPKRIYPVPELPRTGGGKVDRRALRA 323
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
29-491 |
2.08e-51 |
|
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: 180.58 E-value: 2.08e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 29 TYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAAIVEDAQLKLLFYAEK 108
Cdd:cd17653 24 TYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSARIQAILRTSGATLLLTTDS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 109 hlssltdidqnllhmdidvaqydeivnpdyhqpfqatpvePQDLAALIYTSGTTGSPKGVMFSYESFVH----NGANLEL 184
Cdd:cd17653 104 ----------------------------------------PDDLAYIIFTSGSTGIPKGVMVPHRGVLNyvsqPPARLDV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 185 TykfnsnyitiVSTPMFHVL--GFNDTVLPV---LMSGGTLILQRyfNGEELNDMIAQYHptFIIMIPTMYySTLRasnf 259
Cdd:cd17653 144 G----------PGSRVAQVLsiAFDACIGEIfstLCNGGTLVLAD--PSDPFAHVARTVD--ALMSTPSIL-STLS---- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 260 nPENFRAMDYIIQGGSQPLPSIQAAFKQyGINIINGYGLTEAPlVLVNTPENSKRKPMSIGKAVMFVDARILDDNGEEVP 339
Cdd:cd17653 205 -PQDFPNLKTIFLGGEAVPPSLLDRWSP-GRRLYNAYGPTECT-ISSTMTELLPGQPVTIGKPIPNSTCYILDADLQPVP 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 340 TGEIGELAIKAKNVTPGYWNKPAETAKAF------HG-RYLLTGDLAKMDNDGDIFIIDRKKELIITGGENV-LPSEVEN 411
Cdd:cd17653 282 EGVVGEICISGVQVARGYLGNPALTASKFvpdpfwPGsRMYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRInLEEIEEV 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 412 ALAEHPLVDRcvvvgydhpkygesiaAAIILREDE------PHYAEI--LNQHMRSRLAGYKVPRMYVPVTHMPLNSTQK 483
Cdd:cd17653 362 VLQSQPEVTQ----------------AAAIVVNGRlvafvtPETVDVdgLRSELAKHLPSYAVPDRIIALDSFPLTANGK 425
|
....*...
gi 584959700 484 PDKLAIRQ 491
Cdd:cd17653 426 VDRKALRE 433
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
149-490 |
6.40e-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: 341266 [Multi-domain] Cd Length: 359 Bit Score: 177.29 E-value: 6.40e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 149 PQDLAALIYTSGTTGSPKGVMFSYESFVHNGANLELTYKFNSNYITIVSTPMFHVLGFNDTVLPVLMSGGTLIL---QRY 225
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVVLagpAGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 226 FNG---EELNDMIAQYHPTFIIMIPTMYYSTL-RASNFNPENFR-AMdyiiqGGSQPLP-SIQAAF-KQYGINIINGYGL 298
Cdd:cd05944 81 RNPglfDNFWKLVERYRITSLSTVPTVYAALLqVPVNADISSLRfAM-----SGAAPLPvELRARFeDATGLPVVEGYGL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 299 TEAPLVLVNTPENSKRKPMSIGKAVMFVDARILDDNGE-----EVPTGEIGELAIKAKNVTPGYWNKPAETAKAFHGRYL 373
Cdd:cd05944 156 TEATCLVAVNPPDGPKRPGSVGLRLPYARVRIKVLDGVgrllrDCAPDEVGEICVAGPGVFGGYLYTEGNKNAFVADGWL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 374 LTGDLAKMDNDGDIFIIDRKKELIITGGENVLPSEVENALAEHPLVDRCVVVGYDHPKYGESIAAAIILREDEPHYAEIL 453
Cdd:cd05944 236 NTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPGAVVEEEEL 315
|
330 340 350
....*....|....*....|....*....|....*...
gi 584959700 454 NQHMRSRLAGY-KVPRMYVPVTHMPLNSTQKPDKLAIR 490
Cdd:cd05944 316 LAWARDHVPERaAVPKHIEVLEELPVTAVGKVFKPALR 353
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
4-462 |
7.21e-51 |
|
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: 181.67 E-value: 7.21e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 4 DWIKTRSD-----FDDDKPAVIDHakqtsWTYQQLNARADNMAHYLTSQGvKKGDVIGIFAPNDIAILDLLFACFKTGAV 78
Cdd:cd05931 1 RRAAARPDrpaytFLDDEGGREET-----LTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 79 FLPLNWRLNPKE---IAAIVEDAQLKLLFYAEKHLSSLTDIDQNLLHMDIDVAQYDEIVNPDYHQPFQATPVEPQDLAAL 155
Cdd:cd05931 75 AVPLPPPTPGRHaerLAAILADAGPRVVLTTAAALAAVRAFAASRPAAGTPRLLVVDLLPDTSAADWPPPSPDPDDIAYL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 156 IYTSGTTGSPKGVMFSYESFVHNGANLELTYKFNSNyITIVS-TPMFHVLGFNDTVLPVLMSGGTLILQ--RYFngeeLN 232
Cdd:cd05931 155 QYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPG-DVVVSwLPLYHDMGLIGGLLTPLYSGGPSVLMspAAF----LR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 233 D------MIAQYHPTFIIMiPTMYYStLRASNFNPENFRAMDY----IIQGGSQP-----LPSIQAAFKQYGIN---IIN 294
Cdd:cd05931 230 RplrwlrLISRYRATISAA-PNFAYD-LCVRRVRDEDLEGLDLsswrVALNGAEPvrpatLRRFAEAFAPFGFRpeaFRP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 295 GYGLTEAPL-------------------------VLVNTPENSKRKPMSIGKAVMFVDARILDDNG-EEVPTGEIGELAI 348
Cdd:cd05931 308 SYGLAEATLfvsggppgtgpvvlrvdrdalagraVAVAADDPAARELVSCGRPLPDQEVRIVDPETgRELPDGEVGEIWV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 349 KAKNVTPGYWNKPAETAKAF-------HGRYLLTGDLAKMdNDGDIFIIDRKKELIITGGENVLPSEVENALAEHPLVDR 421
Cdd:cd05931 388 RGPSVASGYWGRPEATAETFgalaatdEGGWLRTGDLGFL-HDGELYITGRLKDLIIVRGRNHYPQDIEATAEEAHPALR 466
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 584959700 422 ---CVVVGYDHPKYGESIAAAIILREDEPHYAEILNQHMRSRLA 462
Cdd:cd05931 467 pgcVAAFSVPDDGEERLVVVAEVERGADPADLAAIAAAIRAAVA 510
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
15-490 |
9.45e-51 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 180.59 E-value: 9.45e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 15 DKPAVIDHAKQTSWTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAAI 94
Cdd:PRK13390 12 DRPAVIVAETGEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 95 VEDAQLKLLFyAEKHLSSLtdIDQNLLHMDIDVAQYDEIvnpDYHQPFQAT------PVEPQDLAA-LIYTSGTTGSPKG 167
Cdd:PRK13390 92 VGDSGARVLV-ASAALDGL--AAKVGADLPLRLSFGGEI---DGFGSFEAAlagagpRLTEQPCGAvMLYSSGTTGFPKG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 168 VM--FSYESFVHNG----ANLELTYKFNSNYITIVSTPMFHVLGFNDTVLpVLMSGGTLILQRYFNGEELNDMIAQYHPT 241
Cdd:PRK13390 166 IQpdLPGRDVDAPGdpivAIARAFYDISESDIYYSSAPIYHAAPLRWCSM-VHALGGTVVLAKRFDAQATLGHVERYRIT 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 242 FIIMIPTMYYSTLR-----ASNFNPENFRAMdyIIQGGSQPLPSIQAAFKQYGINIINGYGLTEA-PLVLVNTPENSKRk 315
Cdd:PRK13390 245 VTQMVPTMFVRLLKldadvRTRYDVSSLRAV--IHAAAPCPVDVKHAMIDWLGPIVYEYYSSTEAhGMTFIDSPDWLAH- 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 316 PMSIGKAVMFvDARILDDNGEEVPTGEIGELAIKAKNVTPGYWNKPAETAKAFHGR---YLLTGDLAKMDNDGDIFIIDR 392
Cdd:PRK13390 322 PGSVGRSVLG-DLHICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAAAQHPAhpfWTTVGDLGSVDEDGYLYLADR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 393 KKELIITGGENVLPSEVENALAEHPLVDRCVVVGYDHPKYGESIAAAIILRED---EPHYAEILNQHMRSRLAGYKVPRM 469
Cdd:PRK13390 401 KSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLVEGirgSDELARELIDYTRSRIAHYKAPRS 480
|
490 500
....*....|....*....|.
gi 584959700 470 YVPVTHMPLNSTQKPDKLAIR 490
Cdd:PRK13390 481 VEFVDELPRTPTGKLVKGLLR 501
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
15-498 |
1.25e-50 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 179.98 E-value: 1.25e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 15 DKPAVIDHAKQTswTYQQLNARADNMAHYLTSQGvKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAAI 94
Cdd:PRK07638 16 NKIAIKENDRVL--TYKDWFESVCKVANWLNEKE-SKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKER 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 95 VEDAQLKLLFYAEKHLSSLTD-------IDQNLLHMDIDVAQYDEIVNPDyHQPFQatpvepqdlaaLIYTSGTTGSPKG 167
Cdd:PRK07638 93 LAISNADMIVTERYKLNDLPDeegrvieIDEWKRMIEKYLPTYAPIENVQ-NAPFY-----------MGFTSGSTGKPKA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 168 VMFSYESFVHNGANLELTYKFNSNYITIVSTPMFHVLgFNDTVLPVLMSGGTLILQRYFNGEELNDMIAQYHPTFIIMIP 247
Cdd:PRK07638 161 FLRAQQSWLHSFDCNVHDFHMKREDSVLIAGTLVHSL-FLYGAISTLYVGQTVHLMRKFIPNQVLDKLETENISVMYTVP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 248 TMYYSTLRASNFnPENfrAMDYIIQGGSQPLPSIQAAFKQY-GINIINGYGLTEAPLVLVNTPENSKRKPMSIGKAVMFV 326
Cdd:PRK07638 240 TMLESLYKENRV-IEN--KMKIISSGAKWEAEAKEKIKNIFpYAKLYEFYGASELSFVTALVDEESERRPNSVGRPFHNV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 327 DARILDDNGEEVPTGEIGELAIKAKNVTPGYWNKPAETAKAFHGRYLLTGDLAKMDNDGDIFIIDRKKELIITGGENVLP 406
Cdd:PRK07638 317 QVRICNEAGEEVQKGEIGTVYVKSPQFFMGYIIGGVLARELNADGWMTVRDVGYEDEEGFIYIVGREKNMILFGGINIFP 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 407 SEVENALAEHPLVDRCVVVGYDHPKYGEsIAAAIIL-REDephyAEILNQHMRSRLAGYKVPRMYVPVTHMPLNSTQKPD 485
Cdd:PRK07638 397 EEIESVLHEHPAVDEIVVIGVPDSYWGE-KPVAIIKgSAT----KQQLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIA 471
|
490
....*....|...
gi 584959700 486 KLAIRQMMNDKVS 498
Cdd:PRK07638 472 RMEAKSWIENQEK 484
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
15-489 |
1.24e-49 |
|
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: 176.21 E-value: 1.24e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 15 DKPAVIDHAKqtSWTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAAI 94
Cdd:cd17645 13 DHVAVVDRGQ--SLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGERIAYM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 95 VEDAQLKLLfyaekhlssLTDidqnllhmdidvaqydeivnpdyhqpfqatpvePQDLAALIYTSGTTGSPKGVMFSYES 174
Cdd:cd17645 91 LADSSAKIL---------LTN---------------------------------PDDLAYVIYTSGSTGLPKGVMIEHHN 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 175 FVhngaNLELTYKFNSNYITIVSTPMFHVLGFNDTVL---PVLMSGGTLIL---QRYFNGEELNDMIAQYHPTfIIMIPT 248
Cdd:cd17645 129 LV----NLCEWHRPYFGVTPADKSLVYASFSFDASAWeifPHLTAGAALHVvpsERRLDLDALNDYFNQEGIT-ISFLPT 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 249 MYystlrasnfnPENFRAMD-----YIIQGGSQplpsiQAAFKQYGINIINGYGLTEAPLVLVNTPENSKRKPMSIGKAV 323
Cdd:cd17645 204 GA----------AEQFMQLDnqslrVLLTGGDK-----LKKIERKGYKLVNNYGPTENTVVATSFEIDKPYANIPIGKPI 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 324 MFVDARILDDNGEEVPTGEIGELAIKAKNVTPGYWNKPAETAKAFHG-------RYLLTGDLAKMDNDGDIFIIDRKKEL 396
Cdd:cd17645 269 DNTRVYILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVhpfvpgeRMYRTGDLAKFLPDGNIEFLGRLDQQ 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 397 IITGGENVLPSEVENALAEHPLVDRCVVVGYDHPKYGESIAAAIILREDEPHyaEILNQHMRSRLAGYKVPRMYVPVTHM 476
Cdd:cd17645 349 VKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTAPEEIPH--EELREWLKNDLPDYMIPTYFVHLKAL 426
|
490
....*....|...
gi 584959700 477 PLNSTQKPDKLAI 489
Cdd:cd17645 427 PLTANGKVDRKAL 439
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
29-442 |
2.06e-49 |
|
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: 176.01 E-value: 2.06e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 29 TYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAAIVEDAQLKLLFyaek 108
Cdd:cd17640 7 TYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALV---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 109 hlssltdidqnllhmdidvaqydeivnpdyhqpfqatpVE--PQDLAALIYTSGTTGSPKGVMFSYESFVHNGANLELTY 186
Cdd:cd17640 83 --------------------------------------VEndSDDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIV 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 187 KFNSNYITIVSTPMFHVlgFNDTVLPVLMSGGtlILQRYFNGEELNDMIAQYHPTFIIMIPTMY-------YSTLRASNF 259
Cdd:cd17640 125 PPQPGDRFLSILPIWHS--YERSAEYFIFACG--CSQAYTSIRTLKDDLKRVKPHYIVSVPRLWeslysgiQKQVSKSSP 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 260 NPE----------NFRAMdyIIQGGSQPlPSIQAAFKQYGINIINGYGLTE-APLVLVNTPENSKRKpmSIGKAVMFVDA 328
Cdd:cd17640 201 IKQflflfflsggIFKFG--ISGGGALP-PHVDTFFEAIGIEVLNGYGLTEtSPVVSARRLKCNVRG--SVGRPLPGTEI 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 329 RILDDNGEEV-PTGEIGELAIKAKNVTPGYWNKPAETAKAFHGR-YLLTGDLAKMDNDGDIFIIDRKKELII-TGGENVL 405
Cdd:cd17640 276 KIVDPEGNVVlPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDgWFNTGDLGWLTCGGELVLTGRAKDTIVlSNGENVE 355
|
410 420 430
....*....|....*....|....*....|....*..
gi 584959700 406 PSEVENALAEHPLVDRCVVVGYDHPKYGesiaaAIIL 442
Cdd:cd17640 356 PQPIEEALMRSPFIEQIMVVGQDQKRLG-----ALIV 387
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
15-483 |
3.31e-49 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 177.71 E-value: 3.31e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 15 DKPAVIDHAKqtSWTYQQLNARADNMAHYLTSQ-GVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAA 93
Cdd:PRK12492 39 DRPAFSNLGV--TLSYAELERHSAAFAAYLQQHtDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVNTNPLYTAREMRH 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 94 IVEDAQLKLLFYAE---KHLSSL---TDIdQNLLHM---DIDVAQYDEIVN----------PDYHQP------------- 141
Cdd:PRK12492 117 QFKDSGARALVYLNmfgKLVQEVlpdTGI-EYLIEAkmgDLLPAAKGWLVNtvvdkvkkmvPAYHLPqavpfkqalrqgr 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 142 ---FQATPVEPQDLAALIYTSGTTGSPKGVMFSYESFVhngANLELTYKFNSNY-------------ITIVSTPMFHVLG 205
Cdd:PRK12492 196 glsLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLV---ANMLQVRACLSQLgpdgqplmkegqeVMIAPLPLYHIYA 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 206 FNDTVLPVLMSGGTLILqrYFNGEELNDMIAQ---YHPTFIIMIPTMYYSTLRASNFNPENFRAMDYIIQGGSQPLPSIQ 282
Cdd:PRK12492 273 FTANCMCMMVSGNHNVL--ITNPRDIPGFIKElgkWRFSALLGLNTLFVALMDHPGFKDLDFSALKLTNSGGTALVKATA 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 283 AAFKQY-GINIINGYGLTEAPLVLVNTPENSKRKPMSIGKAVMFVDARILDDNGEEVPTGEIGELAIKAKNVTPGYWNKP 361
Cdd:PRK12492 351 ERWEQLtGCTIVEGYGLTETSPVASTNPYGELARLGTVGIPVPGTALKVIDDDGNELPLGERGELCIKGPQVMKGYWQQP 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 362 AETAKAFHGR-YLLTGDLAKMDNDGDIFIIDRKKELIITGGENVLPSEVENALAEHPLVDRCVVVGYDHPKYGESIAAAI 440
Cdd:PRK12492 431 EATAEALDAEgWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVKLFV 510
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 584959700 441 ILREDEPHYAEiLNQHMRSRLAGYKVPRMYVPVTHMPLNSTQK 483
Cdd:PRK12492 511 VARDPGLSVEE-LKAYCKENFTGYKVPKHIVLRDSLPMTPVGK 552
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
151-486 |
6.21e-49 |
|
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.
Pssm-ID: 341293 [Multi-domain] Cd Length: 330 Bit Score: 171.14 E-value: 6.21e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 151 DLAALIYTSGTTGSPKGVMFSY----ESFVHNGANLELTYkfNSNYITIvsTPMFHVLGFNDTVLPVLMSGGTLILQRYF 226
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHrqtlRAAAAWADCADLTE--DDRYLII--NPFFHTFGYKAGIVACLLTGATVVPVAVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 227 NGEELNDMIAQYHPTFIIMIPTMYYSTLRASNFNPENFRAMDYIIQGGSQ-PLPSIQAAFKQYGI-NIINGYGLTEAPLV 304
Cdd:cd17638 77 DVDAILEAIERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVTGAATvPVELVRRMRSELGFeTVLTAYGLTEAGVA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 305 LVNTPENSKRK-PMSIGKAVMFVDARILDDngeevptgeiGELAIKAKNVTPGYWNKPAETAKAFHGR-YLLTGDLAKMD 382
Cdd:cd17638 157 TMCRPGDDAETvATTCGRACPGFEVRIADD----------GEVLVRGYNVMQGYLDDPEATAEAIDADgWLHTGDVGELD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 383 NDGDIFIIDRKKELIITGGENVLPSEVENALAEHPLVDRCVVVGYDHPKYGESIAAAIILREDEPHYAEILNQHMRSRLA 462
Cdd:cd17638 227 ERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGVTLTEEDVIAWCRERLA 306
|
330 340
....*....|....*....|....
gi 584959700 463 GYKVPRMYVPVTHMPLNSTQKPDK 486
Cdd:cd17638 307 NYKVPRFVRFLDELPRNASGKVMK 330
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
15-485 |
9.02e-49 |
|
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: 174.13 E-value: 9.02e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 15 DKPAVIDHAKqtSWTYQQLNARADNMAHYLTSQGVKKGD-VIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAA 93
Cdd:cd17648 2 DRVAVVYGDK--RLTYRELNERANRLAHYLLSVAEIRPDdLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 94 IVEDAQLKLLfyaekhlssLTDidqnllhmdidvaqydeivnpdyhqpfqatpvePQDLAALIYTSGTTGSPKGVMFSYE 173
Cdd:cd17648 80 ILEDTGARVV---------ITN---------------------------------STDLAYAIYTSGTTGKPKGVLVEHG 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 174 SFVHNGANLELTYK----------FNSNYITivstpMFHVlgfnDTVLPVLMSGGTLILqryfngeeLNDMIAQYHPTFI 243
Cdd:cd17648 118 SVVNLRTSLSERYFgrdngdeavlFFSNYVF-----DFFV----EQMTLALLNGQKLVV--------PPDEMRFDPDRFY 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 244 IMIPTMYYSTLRASnfnPENFRAMDY--------IIQGGSQPLPSIQAAFKQ-YGINIINGYGLTEAPLVLVNTP-ENSK 313
Cdd:cd17648 181 AYINREKVTYLSGT---PSVLQQYDLarlphlkrVDAAGEEFTAPVFEKLRSrFAGLIINAYGPTETTVTNHKRFfPGDQ 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 314 RKPMSIGKAVMFVDARILDDNGEEVPTGEIGELAIKAKNVTPGYWNKPAETAKAF---------------HGRYLLTGDL 378
Cdd:cd17648 258 RFDKSLGRPVRNTKCYVLNDAMKRVPVGAVGELYLGGDGVARGYLNRPELTAERFlpnpfqteqerargrNARLYKTGDL 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 379 AKMDNDGDIFIIDRKKELIITGGENVLPSEVENALAEHPLVDRCVVV-GYDHPKYGESIAAAII---LREDEPHYAEILN 454
Cdd:cd17648 338 VRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVaKEDASQAQSRIQKYLVgyyLPEPGHVPESDLL 417
|
490 500 510
....*....|....*....|....*....|.
gi 584959700 455 QHMRSRLAGYKVPRMYVPVTHMPLNSTQKPD 485
Cdd:cd17648 418 SFLRAKLPRYMVPARLVRLEGIPVTINGKLD 448
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
5-486 |
9.77e-49 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 176.38 E-value: 9.77e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 5 WIKTRSDfdddKPAVIDHAKQTswTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPN----DIAILDLLfacfKTGAVFL 80
Cdd:PRK06178 42 WARERPQ----RPAIIFYGHVI--TYAELDELSDRFAALLRQRGVGAGDRVAVFLPNcpqfHIVFFGIL----KLGAVHV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 81 PLNWRLNPKEIAAIVEDAQLK-------LLFYAEKHLS----------SLTDidqnLLHMDIDVAQYDEIVNP------- 136
Cdd:PRK06178 112 PVSPLFREHELSYELNDAGAEvllaldqLAPVVEQVRAetslrhvivtSLAD----VLPAEPTLPLPDSLRAPrlaaaga 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 137 --------DYHQPFQATPVEPQDLAALIYTSGTTGSPKGVMFSYESFVHNGA-NLELTYKFNSNYITIVSTPMFHVLGFN 207
Cdd:PRK06178 188 idllpalrACTAPVPLPPPALDALAALNYTGGTTGMPKGCEHTQRDMVYTAAaAYAVAVVGGEDSVFLSFLPEFWIAGEN 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 208 DTVLPVLMSGGTLILQRYFNGEELNDMIAQYHPTFIIM-----IPTMYYSTLRASNFNP-ENFRAMDYIIQggsqpL-PS 280
Cdd:PRK06178 268 FGLLFPLFSGATLVLLARWDAVAFMAAVERYRVTRTVMlvdnaVELMDHPRFAEYDLSSlRQVRVVSFVKK-----LnPD 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 281 IQAAFKQY-GINIING-YGLTEAplvlvNT-----------PENSKRKPMSIGKAVMFVDARILD-DNGEEVPTGEIGEL 346
Cdd:PRK06178 343 YRQRWRALtGSVLAEAaWGMTET-----HTcdtftagfqddDFDLLSQPVFVGLPVPGTEFKICDfETGELLPLGAEGEI 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 347 AIKAKNVTPGYWNKPAETAKAFHGRYLLTGDLAKMDNDGDIFIIDRKKELIITGGENVLPSEVENALAEHPLVDRCVVVG 426
Cdd:PRK06178 418 VVRTPSLLKGYWNKPEATAEALRDGWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVG 497
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 427 YDHPKYGESIAAAIILREDEPHYAEILNQHMRSRLAGYKVPRMYVpVTHMPLNSTQKPDK 486
Cdd:PRK06178 498 RPDPDKGQVPVAFVQLKPGADLTAAALQAWCRENMAVYKVPEIRI-VDALPMTATGKVRK 556
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
15-491 |
1.54e-48 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 175.07 E-value: 1.54e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 15 DKPAVIDHAKQTSWTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAAI 94
Cdd:PRK05852 31 EAPALVVTADRIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 95 VEDAQLKLLFY---------AEKH--------LSSLTDIDQNLLHMDIDVAqydeiVNPdyhQPFQATP--VEPQDlAAL 155
Cdd:PRK05852 111 SQAAGARVVLIdadgphdraEPTTrwwpltvnVGGDSGPSGGTLSVHLDAA-----TEP---TPATSTPegLRPDD-AMI 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 156 IYTSGTTGSPKGVMFSYESFVHNGANLELTYKFNSNYITIVSTPMFHVLGFNDTVLPVLMSGGTLIL--QRYFNGEELND 233
Cdd:PRK05852 182 MFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHGHGLIAALLATLASGGAVLLpaRGRFSAHTFWD 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 234 MIAQYHPTFIIMIPTMYYSTL-RASNFNPENFRAMDYIIQGGSQPL--PSIQAAFKQYGINIINGYGLTEAPLVLVNT-- 308
Cdd:PRK05852 262 DIKAVGATWYTAVPTIHQILLeRAATEPSGRKPAALRFIRSCSAPLtaETAQALQTEFAAPVVCAFGMTEATHQVTTTqi 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 309 -----PENSKRKPMSIGKAVMfVDARILDDNGEEVPTGEIGELAIKAKNVTPGYWNKPAETAKAFHGRYLLTGDLAKMDN 383
Cdd:PRK05852 342 egigqTENPVVSTGLVGRSTG-AQIRIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDPTITAANFTDGWLRTGDLGSLSA 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 384 DGDIFIIDRKKELIITGGENVLPSEVENALAEHPLVDRCVVVGYDHPKYGESIAAAIILREDEPHYAEILNQHMRSRLAG 463
Cdd:PRK05852 421 AGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIVPRESAPPTAEELVQFCRERLAA 500
|
490 500
....*....|....*....|....*...
gi 584959700 464 YKVPRMYVPVTHMPLNSTQKPDKLAIRQ 491
Cdd:PRK05852 501 FEIPASFQEASGLPHTAKGSLDRRAVAE 528
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
40-492 |
6.46e-48 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 174.22 E-value: 6.46e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 40 MAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAAIVEDAQLKLL-------FYAEKHLSS 112
Cdd:PLN02860 45 LAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWSFEEAKSAMLLVRPVMLvtdetcsSWYEELQND 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 113 ----------LTDIDQNLLHMDIDVAQYDEIVNPDYHQPfQATPVEPQDLAALI-YTSGTTGSPKGVMFSYESF-VHNGA 180
Cdd:PLN02860 125 rlpslmwqvfLESPSSSVFIFLNSFLTTEMLKQRALGTT-ELDYAWAPDDAVLIcFTSGTTGRPKGVTISHSALiVQSLA 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 181 NLELTyKFNSNYITIVSTPMFHVLGFNdTVLPVLMSGGTLILQRYFNGEELNDMIAQYHPTFIIMIPTMYYSTLR--ASN 258
Cdd:PLN02860 204 KIAIV-GYGEDDVYLHTAPLCHIGGLS-SALAMLMVGACHVLLPKFDAKAALQAIKQHNVTSMITVPAMMADLISltRKS 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 259 FNPENFRAMDYIIQG-GSQPLPSIQAAFKQY-GINIINGYGLTEA----------------PLVLVNTPENSKRKPMS-- 318
Cdd:PLN02860 282 MTWKVFPSVRKILNGgGSLSSRLLPDAKKLFpNAKLFSAYGMTEAcssltfmtlhdptlesPKQTLQTVNQTKSSSVHqp 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 319 ----IGKAVMFVDARILDDngEEVPTGEIgelAIKAKNVTPGYWNKPAETAKAFHGR-YLLTGDLAKMDNDGDIFIIDRK 393
Cdd:PLN02860 362 qgvcVGKPAPHVELKIGLD--ESSRVGRI---LTRGPHVMLGYWGQNSETASVLSNDgWLDTGDIGWIDKAGNLWLIGRS 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 394 KELIITGGENVLPSEVENALAEHPLVDRCVVVGYDHPKYGESIAAAIILRE-------DEPHY-------AEILNQHMRS 459
Cdd:PLN02860 437 NDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEMVVACVRLRDgwiwsdnEKENAkknltlsSETLRHHCRE 516
|
490 500 510
....*....|....*....|....*....|....*...
gi 584959700 460 R-LAGYKVPRMYV----PvthMPLNSTQKPDKLAIRQM 492
Cdd:PLN02860 517 KnLSRFKIPKLFVqwrkP---FPLTTTGKIRRDEVRRE 551
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
15-483 |
6.71e-48 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 173.26 E-value: 6.71e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 15 DKPAVIDhaKQTSWTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAAI 94
Cdd:PRK13383 50 GRTAIID--DDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 95 VEDAQLKLLFYAEKHLSSLTDIDQNLLHMDIDVAQYDEIVNpdyhQPFQATPVEpqdlaALIYTSGTTGSPKGVMFSYEs 174
Cdd:PRK13383 128 LRAHHISTVVADNEFAERIAGADDAVAVIDPATAGAEESGG----RPAVAAPGR-----IVLLTSGTTGKPKGVPRAPQ- 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 175 fVHNGANLELTY----KFNSNYITIVSTPMFHVLGFNDTVLPVLMsGGTLILQRYFNGEELNDMIAQYHPTFIIMIPTMY 250
Cdd:PRK13383 198 -LRSAVGVWVTIldrtRLRTGSRISVAMPMFHGLGLGMLMLTIAL-GGTVLTHRHFDAEAALAQASLHRADAFTAVPVVL 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 251 YSTL------RASNFNPEnfraMDYIIQGGSQPLPSIQAAFKQ-YGINIINGYGLTEAPLVLVNTPENSKRKPMSIGKAV 323
Cdd:PRK13383 276 ARILelpprvRARNPLPQ----LRVVMSSGDRLDPTLGQRFMDtYGDILYNGYGSTEVGIGALATPADLRDAPETVGKPV 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 324 MFVDARILDDNGEEVPTGEIGELAIKAKNVTPGYWNKpaeTAKAFHGRYLLTGDLAKMDNDGDIFIIDRKKELIITGGEN 403
Cdd:PRK13383 352 AGCPVRILDRNNRPVGPRVTGRIFVGGELAGTRYTDG---GGKAVVDGMTSTGDMGYLDNAGRLFIVGREDDMIISGGEN 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 404 VLPSEVENALAEHPLVDRCVVVGYDHPKYGESIAAAIILREDEPHYAEILNQHMRSRLAGYKVPRMYVPVTHMPLNSTQK 483
Cdd:PRK13383 429 VYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPGSGVDAAQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGK 508
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
15-491 |
6.93e-48 |
|
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: 173.45 E-value: 6.93e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 15 DKPAVI---DHAKQTSWTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEI 91
Cdd:cd05970 32 DKLALVwcdDAGEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQLTAKDI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 92 AAIVEDAQLKLLF-YAEKHL--------------SSLTDIDQNLLHMDIDVAQYDEIVNPDYHQPFQATPVEPQDLAALI 156
Cdd:cd05970 112 VYRIESADIKMIVaIAEDNIpeeiekaapecpskPKLVWVGDPVPEGWIDFRKLIKNASPDFERPTANSYPCGEDILLVY 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 157 YTSGTTGSPKGV--MFSYE-------SFVHNganleltYKFNSNYITIVSTpmfhvlGFNDTVLPVL----MSGGTLILQ 223
Cdd:cd05970 192 FSSGTTGMPKMVehDFTYPlghivtaKYWQN-------VREGGLHLTVADT------GWGKAVWGKIygqwIAGAAVFVY 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 224 RY--FNGEELNDMIAQYHPTFIIMIPTMYYSTLRAsNFNPENFRAMDYIIQGGSQPLPSIQAAFKQY-GINIINGYGLTE 300
Cdd:cd05970 259 DYdkFDPKALLEKLSKYGVTTFCAPPTIYRFLIRE-DLSRYDLSSLRYCTTAGEALNPEVFNTFKEKtGIKLMEGFGQTE 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 301 APLVLVNTPeNSKRKPMSIGKAVMFVDARILDDNGEEVPTGEIGELAIKAKNVTP-----GYWNKPAETAKAFHGRYLLT 375
Cdd:cd05970 338 TTLTIATFP-WMEPKPGSMGKPAPGYEIDLIDREGRSCEAGEEGEIVIRTSKGKPvglfgGYYKDAEKTAEVWHDGYYHT 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 376 GDLAKMDNDGDIFIIDRKKELIITGGENVLPSEVENALAEHPLVDRCVVVGYDHPKYGESIAAAIILRED-EPHYAEI-- 452
Cdd:cd05970 417 GDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIVLAKGyEPSEELKke 496
|
490 500 510
....*....|....*....|....*....|....*....
gi 584959700 453 LNQHMRSRLAGYKVPRMYVPVTHMPLNSTQKPDKLAIRQ 491
Cdd:cd05970 497 LQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEIRE 535
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
29-491 |
8.82e-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: 341277 [Multi-domain] Cd Length: 437 Bit Score: 171.16 E-value: 8.82e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 29 TYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAAIVEDAQLKLLfyaek 108
Cdd:cd05973 2 TFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLV----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 109 hlssLTDIDQNllhmdidvAQYDEivnpdyhqpfqatpvepqDLAALIYTSGTTGSPKGVMFSYESFVHNGANLE--LTY 186
Cdd:cd05973 77 ----VTDAANR--------HKLDS------------------DPFVMMFTSGTTGLPKGVPVPLRALAAFGAYLRdaVDL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 187 KFNSNYITIVSTPMFHVLgFNDTVLPVLMSGGTLILQRYFNGEELNDMIAQYHPTFIIMIPTMYYSTLRASNFNPENFRA 266
Cdd:cd05973 127 RPEDSFWNAADPGWAYGL-YYAITGPLALGHPTILLEGGFSVESTWRVIERLGVTNLAGSPTAYRLLMAAGAEVPARPKG 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 267 MDYIIQGGSQPL-PSIQAAFK-QYGINIINGYGLTEAPLVLVN--TPENSKRKPmSIGKAVMFVDARILDDNGEEVPTGE 342
Cdd:cd05973 206 RLRRVSSAGEPLtPEVIRWFDaALGVPIHDHYGQTELGMVLANhhALEHPVHAG-SAGRAMPGWRVAVLDDDGDELGPGE 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 343 IGELAIKAKNVT----PGYWNKPAetaKAFHGRYLLTGDLAKMDNDGDIFIIDRKKELIITGGENVLPSEVENALAEHPL 418
Cdd:cd05973 285 PGRLAIDIANSPlmwfRGYQLPDT---PAIDGGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPA 361
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 584959700 419 VDRCVVVGYDHPKYGESIAAAIILR---EDEPHYAEILNQHMRSRLAGYKVPRMYVPVTHMPLNSTQKPDKLAIRQ 491
Cdd:cd05973 362 VAEAAVIGVPDPERTEVVKAFVVLRgghEGTPALADELQLHVKKRLSAHAYPRTIHFVDELPKTPSGKIQRFLLRR 437
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
13-490 |
8.96e-48 |
|
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: 171.79 E-value: 8.96e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 13 DDDKPAVidHAKQTSWTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLnPKEIA 92
Cdd:cd05929 5 DLDRAQV--FHQRRLLLLDVYSIALNRNARAAAAEGVWIADGVYIYLINSILTVFAAAAAWKCGACPAYKSSRA-PRAEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 93 AIVEDAQ---LKLLFYAEKHLSSltdidqnllhmdidvaqydeiVNPDYHQPFQATPVEP-QDLAA---LIYTSGTTGSP 165
Cdd:cd05929 82 CAIIEIKaaaLVCGLFTGGGALD---------------------GLEDYEAAEGGSPETPiEDEAAgwkMLYSGGTTGRP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 166 KGVM--FSYESF-VHNGANLELTYKFNSNYITIVSTPMFHVLGFNdTVLPVLMSGGTLILQRYFNGEELNDMIAQYHPTF 242
Cdd:cd05929 141 KGIKrgLPGGPPdNDTLMAAALGFGPGADSVYLSPAPLYHAAPFR-WSMTALFMGGTLVLMEKFDPEEFLRLIERYRVTF 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 243 IIMIPTMYYSTLRAsnfnPENFRamdyiiqgGSQPLPSIQAAF----------KQYGIN-----IINGYGLTEAPLVLVN 307
Cdd:cd05929 220 AQFVPTMFVRLLKL----PEAVR--------NAYDLSSLKRVIhaaapcppwvKEQWIDwggpiIWEYYGGTEGQGLTII 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 308 TPENSKRKPMSIGKAVMfVDARILDDNGEEVPTGEIGELAIKAkNVTPGYWNKPAETAKAFHGRYLLT-GDLAKMDNDGD 386
Cdd:cd05929 288 NGEEWLTHPGSVGRAVL-GKVHILDEDGNEVPPGEIGEVYFAN-GPGFEYTNDPEKTAAARNEGGWSTlGDVGYLDEDGY 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 387 IFIIDRKKELIITGGENVLPSEVENALAEHPLVDRCVVVGYDHPKYGESIAAAI---ILREDEPHYAEILNQHMRSRLAG 463
Cdd:cd05929 366 LYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVqpaPGADAGTALAEELIAFLRDRLSR 445
|
490 500
....*....|....*....|....*..
gi 584959700 464 YKVPRMYVPVTHMPLNSTQKPDKLAIR 490
Cdd:cd05929 446 YKCPRSIEFVAELPRDDTGKLYRRLLR 472
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
15-489 |
1.09e-47 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 178.05 E-value: 1.09e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 15 DKPAVIDHAKQTSwtYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAAI 94
Cdd:PRK12467 3110 EAPALVFGDQQLS--YAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYM 3187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 95 VEDAQLKLLFyAEKHLSSLTDIDQNLLHMDIDvaQYDEIVNPDyHQPfqATPVEPQDLAALIYTSGTTGSPKGVMFSYES 174
Cdd:PRK12467 3188 IEDSGVKLLL-TQAHLLEQLPAPAGDTALTLD--RLDLNGYSE-NNP--STRVMGENLAYVIYTSGSTGKPKGVGVRHGA 3261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 175 FVHNGANLELTYKFNSNYITIVSTPmFHVLGFNDTVLPVLMSGGTLILQ--RYFNGEELNDMIAQYHPTFIIMIPTMYYS 252
Cdd:PRK12467 3262 LANHLCWIAEAYELDANDRVLLFMS-FSFDGAQERFLWTLICGGCLVVRdnDLWDPEELWQAIHAHRISIACFPPAYLQQ 3340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 253 TLRASnfNPENFRAMDYIIQGGSQPLPSIQAAFKQYGIN--IINGYGLTEAPLV--LVNTPENSKRKPMS--IGKAVMFV 326
Cdd:PRK12467 3341 FAEDA--GGADCASLDIYVFGGEAVPPAAFEQVKRKLKPrgLTNGYGPTEAVVTvtLWKCGGDAVCEAPYapIGRPVAGR 3418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 327 DARILDDNGEEVPTGEIGELAIKAKNVTPGYWNKPAETAKAF--------HGRYLLTGDLAKMDNDGDIFIIDRKKELII 398
Cdd:PRK12467 3419 SIYVLDGQLNPVPVGVAGELYIGGVGLARGYHQRPSLTAERFvadpfsgsGGRLYRTGDLARYRADGVIEYLGRIDHQVK 3498
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 399 TGGENVLPSEVENALAEHPLVDRCVVVGYDHPKyGESIAAAIILREDEPHYAEILNQHMRSRLAGYKVPRMYVPVTHMPL 478
Cdd:PRK12467 3499 IRGFRIELGEIEARLLQHPSVREAVVLARDGAG-GKQLVAYVVPADPQGDWRETLRDHLAASLPDYMVPAQLLVLAAMPL 3577
|
490
....*....|.
gi 584959700 479 NSTQKPDKLAI 489
Cdd:PRK12467 3578 GPNGKVDRKAL 3588
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
29-419 |
1.30e-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: 1.30e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 29 TYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAAIVEDAQLKLLFYAEk 108
Cdd:cd05914 9 TYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFVSD- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 109 hlssltdidqnllhmdidvaqydeivnpdyhqpfqatpvePQDLAALIYTSGTTGSPKGVMFSYESFVHNGANLELTYKF 188
Cdd:cd05914 88 ----------------------------------------EDDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLL 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 189 NSNYITIVSTPMFHVLGF-NDTVLPVLMSGGTLILQRYfnGEELNDMIAQYHPTFIIMIPTMY----------------- 250
Cdd:cd05914 128 GKGDKILSILPLHHIYPLtFTLLLPLLNGAHVVFLDKI--PSAKIIALAFAQVTPTLGVPVPLviekifkmdiipkltlk 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 251 ------YSTLRASNFNPENFRAM--------DYIIQGGSQPLPSIQAAFKQYGINIINGYGLTE-APLVLVNTPENSKRK 315
Cdd:cd05914 206 kfkfklAKKINNRKIRKLAFKKVheafggniKEFVIGGAKINPDVEEFLRTIGFPYTIGYGMTEtAPIISYSPPNRIRLG 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 316 pmSIGKAVMFVDARILDDNgeevPTGEIGELAIKAKNVTPGYWNKPAETAKAFHGR-YLLTGDLAKMDNDGDIFIIDRKK 394
Cdd:cd05914 286 --SAGKVIDGVEVRIDSPD----PATGEGEIIVRGPNVMKGYYKNPEATAEAFDKDgWFHTGDLGKIDAEGYLYIRGRKK 359
|
410 420
....*....|....*....|....*.
gi 584959700 395 ELIITG-GENVLPSEVENALAEHPLV 419
Cdd:cd05914 360 EMIVLSsGKNIYPEEIEAKINNMPFV 385
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
155-477 |
1.85e-47 |
|
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: 167.09 E-value: 1.85e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 155 LIYTSGTTGSPKGVMFSYESFVHNGANLELTYKFNSNYITIVSTPMFHVlGFNDTVLPVLMSGGTLILQRYFNGEELNDM 234
Cdd:cd17636 5 AIYTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTVFLNSGPLFHI-GTLMFTLATFHAGGTNVFVRRVDAEEVLEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 235 IAQYHPTF-IIMIPTMY------------YSTLRASNFNPEnFRAMdyiiqggSQPLPSiqAAFKQYGiniinGYGLTEA 301
Cdd:cd17636 84 IEAERCTHaFLLPPTIDqivelnadglydLSSLRSSPAAPE-WNDM-------ATVDTS--PWGRKPG-----GYGQTEV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 302 pLVLVNTPENSKRKPMSIGKAVMFVDARILDDNGEEVPTGEIGELAIKAKNVTPGYWNKPAETAKAFHGRYLLTGDLAKM 381
Cdd:cd17636 149 -MGLATFAALGGGAIGGAGRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRTRGGWHHTNDLGRR 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 382 DNDGDIFIIDRKKELIITGGENVLPSEVENALAEHPLVDRCVVVGYDHPKYGESIAAAIILREDEPHYAEILNQHMRSRL 461
Cdd:cd17636 228 EPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPGASVTEAELIEHCRARI 307
|
330
....*....|....*.
gi 584959700 462 AGYKVPRMYVPVTHMP 477
Cdd:cd17636 308 ASYKKPKSVEFADALP 323
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
28-483 |
2.13e-47 |
|
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: 169.99 E-value: 2.13e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 28 WTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAAIVEDAQLKLLfyae 107
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVL---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 108 khlssltdidqnllhmdidvaqydeIVNPDYHQPfqatpVEPQDLAALIYTSGTTGSPKGVMFSYESFVhnganlelTYK 187
Cdd:cd05969 77 -------------------------ITTEELYER-----TDPEDPTLLHYTSGTTGTPKGVLHVHDAMI--------FYY 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 188 FNSNYI-TIVSTPMFHVLG--------FNDTVLPVLMSGGTLILQRYFNGEELNDMIAQYHPTFIIMIPT-----MYYST 253
Cdd:cd05969 119 FTGKYVlDLHPDDIYWCTAdpgwvtgtVYGIWAPWLNGVTNVVYEGRFDAESWYGIIERVKVTVWYTAPTairmlMKEGD 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 254 LRASNFNPENFRamdyIIQGGSQPL--PSIQAAFKQYGINIINGYGLTE-APLVLVNTPeNSKRKPMSIGKAVMFVDARI 330
Cdd:cd05969 199 ELARKYDLSSLR----FIHSVGEPLnpEAIRWGMEVFGVPIHDTWWQTEtGSIMIANYP-CMPIKPGSMGKPLPGVKAAV 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 331 LDDNGEEVPTGEIGELAIKA--KNVTPGYWNKPAETAKAFHGRYLLTGDLAKMDNDGDIFIIDRKKELIITGGENVLPSE 408
Cdd:cd05969 274 VDENGNELPPGTKGILALKPgwPSMFRGIWNDEERYKNSFIDGWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFE 353
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 584959700 409 VENALAEHPLVDRCVVVGYDHPKYGESIAAAIILRED-EPHYA---EILNqHMRSRLAGYKVPRMYVPVTHMPLNSTQK 483
Cdd:cd05969 354 VESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGfEPSDElkeEIIN-FVRQKLGAHVAPREIEFVDNLPKTRSGK 431
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
5-485 |
3.16e-47 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 176.27 E-value: 3.16e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 5 WIKT-RSDFDddKPAVIDHAKqTSWTYQQLNARADNMAHYLtSQGVKKGDVIGIFAPNDI--AILDLlfACFKTGAVFLP 81
Cdd:PRK08633 621 WIDTaKRNWS--RLAVADSTG-GELSYGKALTGALALARLL-KRELKDEENVGILLPPSVagALANL--ALLLAGKVPVN 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 82 LNWRLNPKEIAAIVEDAQLKLLFYAEKHLSSLTDIDQNL-LHMDIDVAQYDEIV-NPDYHQPFQA--------------- 144
Cdd:PRK08633 695 LNYTASEAALKSAIEQAQIKTVITSRKFLEKLKNKGFDLeLPENVKVIYLEDLKaKISKVDKLTAllaarllparllkrl 774
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 145 --TPVEPQDLAALIYTSGTTGSPKGVMFSYESFVHNGANLELTYKFNSNYITIVSTPMFHVLGFNDTVLPVLMSGgtlIL 222
Cdd:PRK08633 775 ygPTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSSLPFFHSFGLTVTLWLPLLEG---IK 851
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 223 QRYF----NGEELNDMIAQYHPTFIIMIPTMYYSTLRASNFNPENFRAMDYIIQGGSQPLPSIQAAFKQ-YGINIINGYG 297
Cdd:PRK08633 852 VVYHpdptDALGIAKLVAKHRATILLGTPTFLRLYLRNKKLHPLMFASLRLVVAGAEKLKPEVADAFEEkFGIRILEGYG 931
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 298 LTE-APLVLVNTP--------ENSKRKPMSIGKAVMFVDARILD-DNGEEVPTGEIGELAIKAKNVTPGYWNKPAETAKA 367
Cdd:PRK08633 932 ATEtSPVASVNLPdvlaadfkRQTGSKEGSVGMPLPGVAVRIVDpETFEELPPGEDGLILIGGPQVMKGYLGDPEKTAEV 1011
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 368 FH----GRYLLTGDLAKMDNDGDIFIIDRKKELIITGGENVLPSEVENALAE--HPLVDRCVVVGYDHPKYGESIAAAII 441
Cdd:PRK08633 1012 IKdidgIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAKalGGEEVVFAVTAVPDEKKGEKLVVLHT 1091
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 584959700 442 LREDEPhyAEILNQHMRSRLAGYKVPRMYVPVTHMPLNSTQKPD 485
Cdd:PRK08633 1092 CGAEDV--EELKRAIKESGLPNLWKPSRYFKVEALPLLGSGKLD 1133
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
18-489 |
7.28e-47 |
|
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: 169.15 E-value: 7.28e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 18 AVIDHAKQTswTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAAIVED 97
Cdd:cd17644 18 AVVFEDQQL--TYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLDPNYPQERLTYILED 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 98 AQLKLLfyaekhlssLTdidqnllhmdidvaqydeivnpdyhqpfqatpvEPQDLAALIYTSGTTGSPKGVMFSYESFVH 177
Cdd:cd17644 96 AQISVL---------LT---------------------------------QPENLAYVIYTSGSTGKPKGVMIEHQSLVN 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 178 NGANLELTYKFNSNyitiVSTPMFHVLGFN---DTVLPVLMSGGTLIL---QRYFNGEELNDMIAQYHPTfIIMIPTMYY 251
Cdd:cd17644 134 LSHGLIKEYGITSS----DRVLQFASIAFDvaaEEIYVTLLSGATLVLrpeEMRSSLEDFVQYIQQWQLT-VLSLPPAYW 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 252 STLrASNFNPENF---RAMDYIIQGGSQPLPS-IQAAFKQYG--INIINGYGLTEAP----LVLVNTPENSKRKPMSIGK 321
Cdd:cd17644 209 HLL-VLELLLSTIdlpSSLRLVIVGGEAVQPElVRQWQKNVGnfIQLINVYGPTEATiaatVCRLTQLTERNITSVPIGR 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 322 AVMFVDARILDDNGEEVPTGEIGELAIKAKNVTPGYWNKPAETAK-----AFHG----RYLLTGDLAKMDNDGDIFIIDR 392
Cdd:cd17644 288 PIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEkfishPFNSseseRLYKTGDLARYLPDGNIEYLGR 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 393 KKELIITGGENVLPSEVENALAEHPLVDRCVVVGYDHPKYGESIAAAIIlredePHYAEI-----LNQHMRSRLAGYKVP 467
Cdd:cd17644 368 IDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIV-----PHYEESpstveLRQFLKAKLPDYMIP 442
|
490 500
....*....|....*....|..
gi 584959700 468 RMYVPVTHMPLNSTQKPDKLAI 489
Cdd:cd17644 443 SAFVVLEELPLTPNGKIDRRAL 464
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
17-489 |
1.20e-46 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 174.76 E-value: 1.20e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 17 PAVIdHAKQTsWTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAAIVE 96
Cdd:PRK12316 528 PALA-FGEET-LDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLE 605
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 97 DAQLKLLFyAEKHLSSLTDIDQNLLHMDIDV------AQYDEivNPDYHqpfqatpVEPQDLAALIYTSGTTGSPKGVMF 170
Cdd:PRK12316 606 DSGVQLLL-SQSHLGRKLPLAAGVQVLDLDRpaawleGYSEE--NPGTE-------LNPENLAYVIYTSGSTGKPKGAGN 675
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 171 SYESFVHNGANLELTYKFNSNYITIVSTPMFHVLGFNDTVLPvLMSGGTLIL---QRYFNGEELNDMIAQYHPTFIIMIP 247
Cdd:PRK12316 676 RHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWP-LMSGARLVVaapGDHRDPAKLVELINREGVDTLHFVP 754
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 248 TMYYSTLRASnfNPENFRAMDYIIQGGsQPLP--SIQAAF-KQYGINIINGYGLTEAPLVLVN-TPENSKRKPMSIGKAV 323
Cdd:PRK12316 755 SMLQAFLQDE--DVASCTSLRRIVCSG-EALPadAQEQVFaKLPQAGLYNLYGPTEAAIDVTHwTCVEEGGDSVPIGRPI 831
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 324 MFVDARILDDNGEEVPTGEIGELAIKAKNVTPGYWNKPAETAKAF-------HGRYLLTGDLAKMDNDGDIFIIDRKKEL 396
Cdd:PRK12316 832 ANLACYILDANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFvpspfvaGERMYRTGDLARYRADGVIEYAGRIDHQ 911
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 397 IITGGENVLPSEVENALAEHPLVDRCVVVGYDhpkyGESIAAAIILREDEPHYAEILNQHMRSRLAGYKVPRMYVPVTHM 476
Cdd:PRK12316 912 VKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GKQLVGYVVLESEGGDWREALKAHLAASLPEYMVPAQWLALERL 987
|
490
....*....|...
gi 584959700 477 PLNSTQKPDKLAI 489
Cdd:PRK12316 988 PLTPNGKLDRKAL 1000
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
157-486 |
3.03e-46 |
|
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: 163.73 E-value: 3.03e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 157 YTSGTTGSPKGVMFSYESFVHNGANLELTYKFNSNYITIVSTPMFHVLGFNdTVLPVLMSGGTLILQRYFNGEELNDMIA 236
Cdd:cd17633 7 FTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSHSLFLY-GAISALYLGGTFIGQRKFNPKSWIRKIN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 237 QYHPTFIIMIPTMYYSTLRASNfnPENfrAMDYIIQGGSQPLPSIQAAFKQY--GINIINGYGLTEAPLVLVNTPENSkR 314
Cdd:cd17633 86 QYNATVIYLVPTMLQALARTLE--PES--KIKSIFSSGQKLFESTKKKLKNIfpKANLIEFYGTSELSFITYNFNQES-R 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 315 KPMSIGKAVMFVDARILDDNGeevptGEIGELAIKAKNVTPGYWNKPAETAkafhGRYLLTGDLAKMDNDGDIFIIDRKK 394
Cdd:cd17633 161 PPNSVGRPFPNVEIEIRNADG-----GEIGKIFVKSEMVFSGYVRGGFSNP----DGWMSVGDIGYVDEEGYLYLVGRES 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 395 ELIITGGENVLPSEVENALAEHPLVDRCVVVGYDHPKYGEsIAAAIILREDEPHYAeiLNQHMRSRLAGYKVPRMYVPVT 474
Cdd:cd17633 232 DMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGE-IAVALYSGDKLTYKQ--LKRFLKQKLSRYEIPKKIIFVD 308
|
330
....*....|..
gi 584959700 475 HMPLNSTQKPDK 486
Cdd:cd17633 309 SLPYTSSGKIAR 320
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
29-489 |
3.26e-46 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 173.42 E-value: 3.26e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 29 TYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAAIVEDAQLKLLFyAEK 108
Cdd:PRK12467 539 SYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLL-TQS 617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 109 HLSSLTDIDQNLLHMDID-----VAQYDEiVNPDyhqpfqaTPVEPQDLAALIYTSGTTGSPKGVMFSYESFVHNGANLE 183
Cdd:PRK12467 618 HLLAQLPVPAGLRSLCLDepadlLCGYSG-HNPE-------VALDPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIA 689
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 184 LTYKFNS-NYITIVSTPMFHVlgFNDTVLPVLMSGGTLIL---QRYFNGEELNDMIAQYHPTFIIMIPTMYYSTLRASnf 259
Cdd:PRK12467 690 ERLQLAAdDSMLMVSTFAFDL--GVTELFGALASGATLHLlppDCARDAEAFAALMADQGVTVLKIVPSHLQALLQAS-- 765
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 260 NPENFRAMDYIIQGGSQPLPSIQAAFKQYGIN--IINGYGLTEAPLVLVNTP---ENSKRKPMSIGKAVMFVDARILDDN 334
Cdd:PRK12467 766 RVALPRPQRALVCGGEALQVDLLARVRALGPGarLINHYGPTETTVGVSTYElsdEERDFGNVPIGQPLANLGLYILDHY 845
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 335 GEEVPTGEIGELAIKAKNVTPGYWNKPAETAKAF--------HGRYLLTGDLAKMDNDGDIFIIDRKKELIITGGENVLP 406
Cdd:PRK12467 846 LNPVPVGVVGELYIGGAGLARGYHRRPALTAERFvpdpfgadGGRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIEL 925
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 407 SEVENALAEHPLVDRCVV-----------VGYDHPKYGESIAAAIILREDephyaeiLNQHMRSRLAGYKVPRMYVPVTH 475
Cdd:PRK12467 926 GEIEARLLAQPGVREAVVlaqpgdaglqlVAYLVPAAVADGAEHQATRDE-------LKAQLRQVLPDYMVPAHLLLLDS 998
|
490
....*....|....
gi 584959700 476 MPLNSTQKPDKLAI 489
Cdd:PRK12467 999 LPLTPNGKLDRKAL 1012
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
15-491 |
6.36e-46 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 172.83 E-value: 6.36e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 15 DKPAVIDHAKQTswTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAAI 94
Cdd:PRK12316 4566 DAVAVVFDEEKL--TYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYM 4643
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 95 VEDAQLKLLFyAEKHLSSLTDIDQNLLHMDIDvaQYDEIVNPDYHQPfqATPVEPQDLAALIYTSGTTGSPKGVMFSYES 174
Cdd:PRK12316 4644 MEDSGAALLL-TQSHLLQRLPIPDGLASLALD--RDEDWEGFPAHDP--AVRLHPDNLAYVIYTSGSTGRPKGVAVSHGS 4718
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 175 FVHNGANLELTYKFNSNYITIVSTPmFHVLGFNDTVLPVLMSGGTLILQ--RYFNGEELNDMIAQYHPTFIIMIPTMYYS 252
Cdd:PRK12316 4719 LVNHLHATGERYELTPDDRVLQFMS-FSFDGSHEGLYHPLINGASVVIRddSLWDPERLYAEIHEHRVTVLVFPPVYLQQ 4797
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 253 TLRASNFNPENFRAMDYIIQGGSQPLPSIQAAFKQ-YGINIINGYGLTEAPLV--LVNTPENSKRKP--MSIGKAVMFVD 327
Cdd:PRK12316 4798 LAEHAERDGEPPSLRVYCFGGEAVAQASYDLAWRAlKPVYLFNGYGPTETTVTvlLWKARDGDACGAayMPIGTPLGNRS 4877
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 328 ARILDDNGEEVPTGEIGELAIKAKNVTPGYWNKPAETAKAF--------HGRYLLTGDLAKMDNDGDIFIIDRKKELIIT 399
Cdd:PRK12316 4878 GYVLDGQLNPLPVGVAGELYLGGEGVARGYLERPALTAERFvpdpfgapGGRLYRTGDLARYRADGVIDYLGRVDHQVKI 4957
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 400 GGENVLPSEVENALAEHPLVDRCVVVGYDHPkYGESIAAAIIlrEDEPHYAEI----------LNQHMRSRLAGYKVPRM 469
Cdd:PRK12316 4958 RGFRIELGEIEARLREHPAVREAVVIAQEGA-VGKQLVGYVV--PQDPALADAdeaqaelrdeLKAALRERLPEYMVPAH 5034
|
490 500
....*....|....*....|..
gi 584959700 470 YVPVTHMPLNSTQKPDKLAIRQ 491
Cdd:PRK12316 5035 LVFLARMPLTPNGKLDRKALPQ 5056
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
29-489 |
9.43e-46 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 172.45 E-value: 9.43e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 29 TYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAAIVEDAQLKLLFYAEK 108
Cdd:PRK12316 3084 SYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLSQSH 3163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 109 HLSSLTDIDQNLLhMDIDVAQYDEiVNPDYHqpfqatpVEPQDLAALIYTSGTTGSPKGVMFSYESFVHNGANLELTYKF 188
Cdd:PRK12316 3164 LRLPLAQGVQVLD-LDRGDENYAE-ANPAIR-------TMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGL 3234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 189 NSNYITIVSTPmFHVLGFNDTVLPVLMSGGTLILQRYFNGEELNDMIAQYHPTfIIMIPTMYYSTLRASNFNPENFRAMD 268
Cdd:PRK12316 3235 GVGDRVLQFTT-FSFDVFVEELFWPLMSGARVVLAGPEDWRDPALLVELINSE-GVDVLHAYPSMLQAFLEEEDAHRCTS 3312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 269 Y-IIQGGSQPLPSIQAAFKQYGINIINGYGLTEAPL-VLVNTPENSKRKPMSIGKAVMFVDARILDDNGEEVPTGEIGEL 346
Cdd:PRK12316 3313 LkRIVCGGEALPADLQQQVFAGLPLYNLYGPTEATItVTHWQCVEEGKDAVPIGRPIANRACYILDGSLEPVPVGALGEL 3392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 347 AIKAKNVTPGYWNKPAETAKAF-------HGRYLLTGDLAKMDNDGDIFIIDRKKELIITGGENVLPSEVENALAEHPLV 419
Cdd:PRK12316 3393 YLGGEGLARGYHNRPGLTAERFvpdpfvpGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWV 3472
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 420 DRCVVVGYDhpkyGESIAAAIILREDEPHYAEILNQHMRSRLAGYKVPRMYVPVTHMPLNSTQKPDKLAI 489
Cdd:PRK12316 3473 REAVVLAVD----GRQLVAYVVPEDEAGDLREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKAL 3538
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
15-492 |
4.50e-45 |
|
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: 165.01 E-value: 4.50e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 15 DKPAVIDhaKQTSWTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAAI 94
Cdd:TIGR02262 20 GKTAFID--DISSLSYGELEAQVRRLAAALRRLGVKREERVLLLMLDGVDFPIAFLGAIRAGIVPVALNTLLTADDYAYM 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 95 VEDAQLKLLFYAEKHLSSLTDIDQNLLHMDIDVA---------QYDEIVNPDYHQpFQATPVEPQDLAALIYTSGTTGSP 165
Cdd:TIGR02262 98 LEDSRARVVFVSGALLPVIKAALGKSPHLEHRVVvgrpeagevQLAELLATESEQ-FKPAATQADDPAFWLYSSGSTGMP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 166 KGVMFSYESFVHNGANL-ELTYKFNSNYITIVSTPMFHVLGFNDTVLPVLMSGGTLILqryfNGEE-----LNDMIAQYH 239
Cdd:TIGR02262 177 KGVVHTHSNPYWTAELYaRNTLGIREDDVCFSAAKLFFAYGLGNALTFPMSVGATTVL----MGERptpdaVFDRLRRHQ 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 240 PTFIIMIPTMYYSTLRASNFNPENFRAMDYIIQGGsQPLP-SIQAAFK-QYGINIINGYGLTE-APLVLVNTPENSKRKp 316
Cdd:TIGR02262 253 PTIFYGVPTLYAAMLADPNLPSEDQVRLRLCTSAG-EALPaEVGQRWQaRFGVDIVDGIGSTEmLHIFLSNLPGDVRYG- 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 317 mSIGKAVMFVDARILDDNGEEVPTGEIGELAIKAKNVTPGYWNKPAETAKAFHGRYLLTGDLAKMDNDGDIFIIDRKKEL 396
Cdd:TIGR02262 331 -TSGKPVPGYRLRLVGDGGQDVADGEPGELLISGPSSATMYWNNRAKSRDTFQGEWTRSGDKYVRNDDGSYTYAGRTDDM 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 397 IITGGENVLPSEVENALAEHPLVDRCVVVGYDHPKYGESIAAAIILREDEPHYAEILNQHMRSRLAGYKVPRMYVPVTHM 476
Cdd:TIGR02262 410 LKVSGIYVSPFEIESALIQHPAVLEAAVVGVADEDGLIKPKAFVVLRPGQTALETELKEHVKDRLAPYKYPRWIVFVDDL 489
|
490
....*....|....*.
gi 584959700 477 PLNSTQKPDKLAIRQM 492
Cdd:TIGR02262 490 PKTATGKIQRFKLREG 505
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
15-490 |
8.22e-45 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 165.40 E-value: 8.22e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 15 DKPAVIDHAKQTSW--TYQqlnaRADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIA 92
Cdd:PLN02479 35 TRKSVVHGSVRYTWaqTYQ----RCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRLNAPTIA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 93 AIVEDAQLKLL-----FY--AEKHLSSLTDIDQNLLHMDIDVAQYDEIVNP------------DYHQpFQAT-------- 145
Cdd:PLN02479 111 FLLEHSKSEVVmvdqeFFtlAEEALKILAEKKKSSFKPPLLIVIGDPTCDPkslqyalgkgaiEYEK-FLETgdpefawk 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 146 -PVEPQDLAALIYTSGTTGSPKGVMFSyesfvHNGANL-----ELTYKFNSNYITIVSTPMFHVLGFNDT-VLPVLMsgG 218
Cdd:PLN02479 190 pPADEWQSIALGYTSGTTASPKGVVLH-----HRGAYLmalsnALIWGMNEGAVYLWTLPMFHCNGWCFTwTLAALC--G 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 219 TLILQRYFNGEELNDMIAQYHPTFIIMIPTMYYSTLRASNfnPENFRAMDYIIQ---GGSQPLPSIQAAFKQYGINIING 295
Cdd:PLN02479 263 TNICLRQVTAKAIYSAIANYGVTHFCAAPVVLNTIVNAPK--SETILPLPRVVHvmtAGAAPPPSVLFAMSEKGFRVTHT 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 296 YGLTEA---PLVLVNTPE-----NSKRKPMSIGKAVMFVDARILD----DNGEEVPT--GEIGELAIKAKNVTPGYWNKP 361
Cdd:PLN02479 341 YGLSETygpSTVCAWKPEwdslpPEEQARLNARQGVRYIGLEGLDvvdtKTMKPVPAdgKTMGEIVMRGNMVMKGYLKNP 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 362 AETAKAFHGRYLLTGDLAKMDNDGDIFIIDRKKELIITGGENVLPSEVENALAEHPLVDRCVVVGYDHPKYGESIAAAII 441
Cdd:PLN02479 421 KANEEAFANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERWGESPCAFVT 500
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 584959700 442 LRE-----DEPHYAEILNQHMRSRLAGYKVPRMYV--PvthMPLNSTQKPDKLAIR 490
Cdd:PLN02479 501 LKPgvdksDEAALAEDIMKFCRERLPAYWVPKSVVfgP---LPKTATGKIQKHVLR 553
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
15-486 |
1.11e-44 |
|
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: 163.60 E-value: 1.11e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 15 DKPAVIDHAKQtsWTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAAI 94
Cdd:cd12114 2 DATAVICGDGT--LTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 95 VEDAQLKLLfyaekhlssLTDIDQNLLHMDIDVAQYDEIVNPDYHQPFQATPVEPQDLAALIYTSGTTGSPKGVMFSyes 174
Cdd:cd12114 80 LADAGARLV---------LTDGPDAQLDVAVFDVLILDLDALAAPAPPPPVDVAPDDLAYVIFTSGSTGTPKGVMIS--- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 175 fvHNGAnleltykfnSNyiTIVSTPMFHVLGFNDTVLPV---------------LMSGGTLIL---QRYFNGEELNDMIA 236
Cdd:cd12114 148 --HRAA---------LN--TILDINRRFAVGPDDRVLALsslsfdlsvydifgaLSAGATLVLpdeARRRDPAHWAELIE 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 237 QYHPTFIIMIPT---MYYSTLRASNFNPENFRAM----DYIiqGGSQPlPSIQAAFKqyGINIINGYGLTEAPL---VLV 306
Cdd:cd12114 215 RHGVTLWNSVPAlleMLLDVLEAAQALLPSLRLVllsgDWI--PLDLP-ARLRALAP--DARLISLGGATEASIwsiYHP 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 307 NTPENSKRKPMSIGKAVMFVDARILDDNGEEVPTGEIGELAIKAKNVTPGYWNKPAETAKAF----HGRYLL-TGDLAKM 381
Cdd:cd12114 290 IDEVPPDWRSIPYGRPLANQRYRVLDPRGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFvthpDGERLYrTGDLGRY 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 382 DNDGDIFIIDRKKELIITGGENVLPSEVENALAEHPLVDRCVVVGYDHPkYGESIAAAIILRED-EPHYAEILNQHMRSR 460
Cdd:cd12114 370 RPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDP-GGKRLAAFVVPDNDgTPIAPDALRAFLAQT 448
|
490 500
....*....|....*....|....*.
gi 584959700 461 LAGYKVPRMYVPVTHMPLNSTQKPDK 486
Cdd:cd12114 449 LPAYMIPSRVIALEALPLTANGKVDR 474
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
13-492 |
9.21e-44 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 162.22 E-value: 9.21e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 13 DDDKPAVIDHAKQTSwtYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIA 92
Cdd:PRK06164 23 RPDAVALIDEDRPLS--RAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 93 AIVEDAQLKLLFYAEKH-----LSSLTDIDQNLLHMDIDVAQYD----EIVNP---DYHQPFQ----------ATPVEPQ 150
Cdd:PRK06164 101 HILGRGRARWLVVWPGFkgidfAAILAAVPPDALPPLRAIAVVDdaadATPAPapgARVQLFAlpdpappaaaGERAADP 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 151 DLAALIY-TSGTTGSPKGVMFSYESFVHNGANLELTYKFNSNYITIVSTPMFHVLGFNdTVLPVLMSGGTLILQRYFNGE 229
Cdd:PRK06164 181 DAGALLFtTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFGFS-TLLGALAGGAPLVCEPVFDAA 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 230 ELNDMIAQYHPTFIImiptmyystlrASNfnpENFRAMdYIIQGGSQPLPSIQ----AAF-----------KQYGINIIN 294
Cdd:PRK06164 260 RTARALRRHRVTHTF-----------GND---EMLRRI-LDTAGERADFPSARlfgfASFapalgelaalaRARGVPLTG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 295 GYGLTEA-PLVL---VNTPENSKR----KPMSIGKAVmfvdaRILD-DNGEEVPTGEIGELAIKAKNVTPGYWNKPAETA 365
Cdd:PRK06164 325 LYGSSEVqALVAlqpATDPVSVRIegggRPASPEARV-----RARDpQDGALLPDGESGEIEIRAPSLMRGYLDNPDATA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 366 KAFHGR-YLLTGDLAKMDNDGDIFIIDRKKELIITGGENVLPSEVENALAEHPLVDRCVVVGYDHPKYGESiAAAIILRE 444
Cdd:PRK06164 400 RALTDDgYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGATRDGKTVP-VAFVIPTD 478
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 584959700 445 DEPHYAEILNQHMRSRLAGYKVP-RMYVpVTHMPL----NSTqKPDKLAIRQM 492
Cdd:PRK06164 479 GASPDEAGLMAACREALAGFKVPaRVQV-VEAFPVtesaNGA-KIQKHRLREM 529
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
2-468 |
1.52e-43 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 161.99 E-value: 1.52e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 2 NFDWIKTRSDFDD----------------------DKPAV--IDHAKQTSWTYQQLNARADNMAHYLTSQGVKKGDVIGI 57
Cdd:PRK04319 24 TFSWEEVEKEFSWletgkvniayeaidrhadggrkDKVALryLDASRKEKYTYKELKELSNKFANVLKELGVEKGDRVFI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 58 FAPNdiaILDLLFACF---KTGAVFLPLNWRLNPKEIAAIVEDAQLKLL-----FYAEKHLSSLTDIDQNLLhMDIDVAQ 129
Cdd:PRK04319 104 FMPR---IPELYFALLgalKNGAIVGPLFEAFMEEAVRDRLEDSEAKVLittpaLLERKPADDLPSLKHVLL-VGEDVEE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 130 YDEIVnpDYHQPFQA-------TPVEPQDLAALIYTSGTTGSPKGVMFsyesfVHNGAnleLTYkfnsnYITivstpMFH 202
Cdd:PRK04319 180 GPGTL--DFNALMEQasdefdiEWTDREDGAILHYTSGSTGKPKGVLH-----VHNAM---LQH-----YQT-----GKY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 203 VLGFNDT-------------------VLPVLMSGGTLILQRYFNGEELNDMIAQYH-------PTFIIMIptMYYSTLRA 256
Cdd:PRK04319 240 VLDLHEDdvywctadpgwvtgtsygiFAPWLNGATNVIDGGRFSPERWYRILEDYKvtvwytaPTAIRML--MGAGDDLV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 257 SNFNpenFRAMDYIIQGGsQPL-P-SIQAAFKQYGINIINGYGLTE-APLVLVNTPeNSKRKPMSIGKAVMFVDARILDD 333
Cdd:PRK04319 318 KKYD---LSSLRHILSVG-EPLnPeVVRWGMKVFGLPIHDNWWMTEtGGIMIANYP-AMDIKPGSMGKPLPGIEAAIVDD 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 334 NGEEVPTGEIGELAIKaknvtPG-------YWNKPAETAKAFHGRYLLTGDLAKMDNDGDIFIIDRKKELIITGGENVLP 406
Cdd:PRK04319 393 QGNELPPNRMGNLAIK-----KGwpsmmrgIWNNPEKYESYFAGDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGP 467
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 584959700 407 SEVENALAEHPLVDRCVVVGYDHPKYGESIAAAIILRED-EPHYA---EILnQHMRSRLAGYKVPR 468
Cdd:PRK04319 468 FEVESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVALRPGyEPSEElkeEIR-GFVKKGLGAHAAPR 532
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
17-490 |
1.46e-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: 158.78 E-value: 1.46e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 17 PA---VIDHAKQTSWTYQQLNARADNMAHYLTSQ-GVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIA 92
Cdd:cd05928 28 PAlwwVNGKGDEVKWSFRELGSLSRKAANVLSGAcGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDIL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 93 AIVEDAQLKLLFYAEKHLSSLTDIDQNL--LHMDIDVAQ--------YDEIVN--PDYHQPFQATPVEPQdlaALIYTSG 160
Cdd:cd05928 108 YRLQASKAKCIVTSDELAPEVDSVASECpsLKTKLLVSEksrdgwlnFKELLNeaSTEHHCVETGSQEPM---AIYFTSG 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 161 TTGSPKGVMFSYESFVHNganleltYKFNSNYITIVsTPMFHVLGFNDT---------VLPVLMSGGTLILQRY--FNGE 229
Cdd:cd05928 185 TTGSPKMAEHSHSSLGLG-------LKVNGRYWLDL-TASDIMWNTSDTgwiksawssLFEPWIQGACVFVHHLprFDPL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 230 ELNDMIAQYHPTFIIMIPTMYySTLRASNFNPENFRAMDYIIQGGSQPLPSIQAAFK-QYGINIINGYGLTEAPLVLVNt 308
Cdd:cd05928 257 VILKTLSSYPITTFCGAPTVY-RMLVQQDLSSYKFPSLQHCVTGGEPLNPEVLEKWKaQTGLDIYEGYGQTETGLICAN- 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 309 PENSKRKPMSIGKAVMFVDARILDDNGEEVPTGEIGELAIKAKNVTP-----GYWNKPAETAKAFHGRYLLTGDLAKMDN 383
Cdd:cd05928 335 FKGMKIKPGSMGKASPPYDVQIIDDNGNVLPPGTEGDIGIRVKPIRPfglfsGYVDNPEKTAATIRGDFYLTGDRGIMDE 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 384 DGDIFIIDRKKELIITGGENVLPSEVENALAEHPLVDRCVVVGYDHPKYGESIAAAIIL------REDEPHYAEiLNQHM 457
Cdd:cd05928 415 DGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLapqflsHDPEQLTKE-LQQHV 493
|
490 500 510
....*....|....*....|....*....|...
gi 584959700 458 RSRLAGYKVPRMYVPVTHMPLNSTQKPDKLAIR 490
Cdd:cd05928 494 KSVTAPYKYPRKVEFVQELPKTVTGKIQRNELR 526
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
29-495 |
2.25e-42 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 158.79 E-value: 2.25e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 29 TYQQLNARADNMAHYLTSQ-GVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAAIVEDAQLKLLF--- 104
Cdd:PRK05620 40 TFAAIGARAAALAHALHDElGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIVadp 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 105 -YAEKHLSSLT--------------DIDQNLLHM--DIDVAQYDEIVN---PDYHQPfqatPVEPQDLAALIYTSGTTGS 164
Cdd:PRK05620 120 rLAEQLGEILKecpcvravvfigpsDADSAAAHMpeGIKVYSYEALLDgrsTVYDWP----ELDETTAAAICYSTGTTGA 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 165 PKGVMFSYESFVHNGANLELTYKFNSNYIT--IVSTPMFHVLGFNdTVLPVLMSGGTLILQ-RYFNGEELNDMIAQYHPT 241
Cdd:PRK05620 196 PKGVVYSHRSLYLQSLSLRTTDSLAVTHGEsfLCCVPIYHVLSWG-VPLAAFMSGTPLVFPgPDLSAPTLAKIIATAMPR 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 242 FIIMIPTMYYSTLRASNFNPENFRAMDYIIQGGSQPLPS-IQAAFKQYGINIINGYGLTE-APLVLVNTP------ENSK 313
Cdd:PRK05620 275 VAHGVPTLWIQLMVHYLKNPPERMSLQEIYVGGSAVPPIlIKAWEERYGVDVVHVWGMTEtSPVGTVARPpsgvsgEARW 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 314 RKPMSIGKAVMFVDARILDDnGEEVPTGE--IGELAIKAKNVTPGYWNKPAET----AKAFHGR-------------YLL 374
Cdd:PRK05620 355 AYRVSQGRFPASLEYRIVND-GQVMESTDrnEGEIQVRGNWVTASYYHSPTEEgggaASTFRGEdvedandrftadgWLR 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 375 TGDLAKMDNDGDIFIIDRKKELIITGGENVLPSEVENALAEHPLVDRCVVVGYDHPKYGESIAAAIILREDEP---HYAE 451
Cdd:PRK05620 434 TGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLAVTVLAPGIEptrETAE 513
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 584959700 452 ILNQHMRSRLAGYKVPRMYVPVTHMPLNSTQKPDKLAIRQMMND 495
Cdd:PRK05620 514 RLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDLRQHLAD 557
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
15-446 |
3.22e-42 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 157.83 E-value: 3.22e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 15 DKPAVIDHAKQTSWTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAAI 94
Cdd:PLN02246 38 DRPCLIDGATGRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQ 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 95 VEDAQLKLLF----YAEKhLSSLtDIDQNLLHMDID-----VAQYDEIVNPDyHQPFQATPVEPQDLAALIYTSGTTGSP 165
Cdd:PLN02246 118 AKASGAKLIItqscYVDK-LKGL-AEDDGVTVVTIDdppegCLHFSELTQAD-ENELPEVEISPDDVVALPYSSGTTGLP 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 166 KGVMFSYESFVHN------GANLELTykFNSNYITIVSTPMFHVLGFNDTVLPVLMSGGTLILQRYFNGEELNDMIAQYH 239
Cdd:PLN02246 195 KGVMLTHKGLVTSvaqqvdGENPNLY--FHSDDVILCVLPMFHIYSLNSVLLCGLRVGAAILIMPKFEIGALLELIQRHK 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 240 PTFIIMIPTMyystLRASNFNPEnfrAMDY------IIQGGSQPL-PSIQAAFKQYGINII--NGYGLTEAPLVLVNTPE 310
Cdd:PLN02246 273 VTIAPFVPPI----VLAIAKSPV---VEKYdlssirMVLSGAAPLgKELEDAFRAKLPNAVlgQGYGMTEAGPVLAMCLA 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 311 NSKR----KPMSIGKAVMFVDARILD-DNGEEVPTGEIGELAIKAKNVTPGYWNKPAETAKAF-HGRYLLTGDLAKMDND 384
Cdd:PLN02246 346 FAKEpfpvKSGSCGTVVRNAELKIVDpETGASLPRNQPGEICIRGPQIMKGYLNDPEATANTIdKDGWLHTGDIGYIDDD 425
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 584959700 385 GDIFIIDRKKELIITGGENVLPSEVENALAEHPLVDRCVVVGYDHPKYGEsIAAAIILR-------EDE 446
Cdd:PLN02246 426 DELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGE-VPVAFVVRsngseitEDE 493
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
29-489 |
7.59e-42 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 160.71 E-value: 7.59e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 29 TYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAAIVEDAQLKLLFyAEK 108
Cdd:PRK12467 1601 TYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLL-TQS 1679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 109 HLSSLTDIDQNLLHMDIDVAQ-----YDEiVNPdyhqpfqATPVEPQDLAALIYTSGTTGSPKGVMFSYESFVHNGANLE 183
Cdd:PRK12467 1680 HLQARLPLPDGLRSLVLDQEDdwlegYSD-SNP-------AVNLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQ 1751
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 184 LTYKFNSNYITIvstpMFHVLGFNDTVLPV---LMSGGTLILQRYF---NGEELNDMIAQYHPTFIIMIPTMYYSTLR-- 255
Cdd:PRK12467 1752 EAYQLSAADVVL----QFTSFAFDVSVWELfwpLINGARLVIAPPGahrDPEQLIQLIERQQVTTLHFVPSMLQQLLQmd 1827
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 256 ASNFNPENFRAmdYIIQGGSQPLPSIQAAFKQYGIN-IINGYGLTEAPL-VLVNT-----PENSKRKPmsIGKAVMFVDA 328
Cdd:PRK12467 1828 EQVEHPLSLRR--VVCGGEALEVEALRPWLERLPDTgLFNLYGPTETAVdVTHWTcrrkdLEGRDSVP--IGQPIANLST 1903
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 329 RILDDNGEEVPTGEIGELAIKAKNVTPGYWNKPAETAKAF--------HGRYLLTGDLAKMDNDGDIFIIDRKKELIITG 400
Cdd:PRK12467 1904 YILDASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFvadpfgtvGSRLYRTGDLARYRADGVIEYLGRIDHQVKIR 1983
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 401 GENVLPSEVENALAEHPLVDRCVVVGYDHPKYGESIA-----AAIILREDEPH--YAEILNQHMRSRLAGYKVPRMYVPV 473
Cdd:PRK12467 1984 GFRIELGEIEARLREQGGVREAVVIAQDGANGKQLVAyvvptDPGLVDDDEAQvaLRAILKNHLKASLPEYMVPAHLVFL 2063
|
490
....*....|....*.
gi 584959700 474 THMPLNSTQKPDKLAI 489
Cdd:PRK12467 2064 ARMPLTPNGKLDRKAL 2079
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
15-483 |
8.45e-42 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 156.93 E-value: 8.45e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 15 DKPAVIDHAKQTSWTYQQLNARADNMAHYLTSQ-GVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAA 93
Cdd:PLN02574 54 GDTALIDSSTGFSISYSELQPLVKSMAAGLYHVmGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKK 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 94 IVEDAQLKLLFYAEKHLSSLTD-------IDQNLLHMD--IDVAQYDEIVNPDYhQPFQATPVEPQDLAALIYTSGTTGS 164
Cdd:PLN02574 134 RVVDCSVGLAFTSPENVEKLSPlgvpvigVPENYDFDSkrIEFPKFYELIKEDF-DFVPKPVIKQDDVAAIMYSSGTTGA 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 165 PKGVMFSYESFVhngANLELTYKFN-SNY-------ITIVSTPMFHVLGFNDTVLPVLMSGGTLILQRYFNGEELNDMIA 236
Cdd:PLN02574 213 SKGVVLTHRNLI---AMVELFVRFEaSQYeypgsdnVYLAALPMFHIYGLSLFVVGLLSLGSTIVVMRRFDASDMVKVID 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 237 QYHPT-FIIMIPTMYYSTLRASNFNPENFRAMDyIIQGGSQPL--PSIQAAFKQYG-INIINGYGLTEAPLVLVNTPENS 312
Cdd:PLN02574 290 RFKVThFPVVPPILMALTKKAKGVCGEVLKSLK-QVSCGAAPLsgKFIQDFVQTLPhVDFIQGYGMTESTAVGTRGFNTE 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 313 K-RKPMSIGKAVMFVDARILD-DNGEEVPTGEIGELAIKAKNVTPGYWNKPAETA-KAFHGRYLLTGDLAKMDNDGDIFI 389
Cdd:PLN02574 369 KlSKYSSVGLLAPNMQAKVVDwSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQsTIDKDGWLRTGDIAYFDEDGYLYI 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 390 IDRKKELIITGGENVLPSEVENALAEHPLVDRCVVVGYDHPKYGESIAAAIILREDEPHYAEILNQHMRSRLAGYKVPRM 469
Cdd:PLN02574 449 VDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQGSTLSQEAVINYVAKQVAPYKKVRK 528
|
490
....*....|....
gi 584959700 470 YVPVTHMPLNSTQK 483
Cdd:PLN02574 529 VVFVQSIPKSPAGK 542
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
15-489 |
1.19e-41 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 160.12 E-value: 1.19e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 15 DKPAVIDHAKQTSwtYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAAI 94
Cdd:PRK12316 2018 EAIAVVFGDQHLS--YAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYM 2095
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 95 VEDAQLKLLFyAEKHLSSLTDIDQNLLHMDIDVAqyDEIvnPDYHQPFQATPVEPQDLAALIYTSGTTGSPKGVMFSYES 174
Cdd:PRK12316 2096 LEDSGAALLL-TQRHLLERLPLPAGVARLPLDRD--AEW--ADYPDTAPAVQLAGENLAYVIYTSGSTGLPKGVAVSHGA 2170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 175 FVHNGANLELTYKFNSNYITIVSTPmFHVLGFNDTVLPVLMSGGTLILQ--RYFNGEELNDMIAQYHPTFIIMIPTMYYS 252
Cdd:PRK12316 2171 LVAHCQAAGERYELSPADCELQFMS-FSFDGAHEQWFHPLLNGARVLIRddELWDPEQLYDEMERHGVTILDFPPVYLQQ 2249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 253 TLR--ASNFNPENFRAmdYIIQGGSQPLPSIQAAFKQY-GINIINGYGLTEA---PLVLVNTPEN-SKRKPMSIGKAVMF 325
Cdd:PRK12316 2250 LAEhaERDGRPPAVRV--YCFGGEAVPAASLRLAWEALrPVYLFNGYGPTEAvvtPLLWKCRPQDpCGAAYVPIGRALGN 2327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 326 VDARILDDNGEEVPTGEIGELAIKAKNVTPGYWNKPAETAKAF--------HGRYLLTGDLAKMDNDGDIFIIDRKKELI 397
Cdd:PRK12316 2328 RRAYILDADLNLLAPGMAGELYLGGEGLARGYLNRPGLTAERFvpdpfsasGERLYRTGDLARYRADGVVEYLGRIDHQV 2407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 398 ITGGENVLPSEVENALAEHPLVDRCVVVGYDHPKyGESIAAAIILREDEPHYAEILNQHMRSRLAGYKVPRMYVPVTHMP 477
Cdd:PRK12316 2408 KIRGFRIELGEIEARLQAHPAVREAVVVAQDGAS-GKQLVAYVVPDDAAEDLLAELRAWLAARLPAYMVPAHWVVLERLP 2486
|
490
....*....|..
gi 584959700 478 LNSTQKPDKLAI 489
Cdd:PRK12316 2487 LNPNGKLDRKAL 2498
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
15-467 |
2.07e-41 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 156.57 E-value: 2.07e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 15 DKPAVIDhaKQTSWTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRL-------- 86
Cdd:PRK08279 52 DRPALLF--EDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLNTQQrgavlahs 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 87 ----NPKeiAAIVEDAQLKLLFYAEKHLS------SLTDIDQNLLHMDIDVAQydEIVNPDYHQPFQATPVEPQDLAALI 156
Cdd:PRK08279 130 lnlvDAK--HLIVGEELVEAFEEARADLArpprlwVAGGDTLDDPEGYEDLAA--AAAGAPTTNPASRSGVTAKDTAFYI 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 157 YTSGTTGSPKGVMFSYESFVHNGANLELTYKFNSN---YITIvstPMFHVLGFNDTVLPVLMSGGTLILQRYFNGEELND 233
Cdd:PRK08279 206 YTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLTPDdvlYCCL---PLYHNTGGTVAWSSVLAAGATLALRRKFSASRFWD 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 234 MIAQYHPTFIIMIPTMYYSTLRAsnfnPEnfRAMD------YIIQGGSQplPSIQAAFKQ-YGI-NIINGYGLTEAPLVL 305
Cdd:PRK08279 283 DVRRYRATAFQYIGELCRYLLNQ----PP--KPTDrdhrlrLMIGNGLR--PDIWDEFQQrFGIpRILEFYAASEGNVGF 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 306 VN---TPENSKRKPMSIGKAVMFV------DARILDDNG--EEVPTGEIGEL--AIKAKNVTPGYwNKPAETAK-----A 367
Cdd:PRK08279 355 INvfnFDGTVGRVPLWLAHPYAIVkydvdtGEPVRDADGrcIKVKPGEVGLLigRITDRGPFDGY-TDPEASEKkilrdV 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 368 FH-G-RYLLTGDLAKMDNDGDIFIIDR-------KkeliitgGENVLPSEVENALAEHPLVDRCVVvgydhpkYGESIA- 437
Cdd:PRK08279 434 FKkGdAWFNTGDLMRDDGFGHAQFVDRlgdtfrwK-------GENVATTEVENALSGFPGVEEAVV-------YGVEVPg 499
|
490 500 510
....*....|....*....|....*....|....*..
gi 584959700 438 -------AAIILREDEPHYAEILNQHMRSRLAGYKVP 467
Cdd:PRK08279 500 tdgragmAAIVLADGAEFDLAALAAHLYERLPAYAVP 536
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
15-500 |
6.45e-41 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 154.37 E-value: 6.45e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 15 DKPAVIDHAKQTSWTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPN----DIAILDLLFAcfktGAVFLPLNWRLNPKE 90
Cdd:PLN02330 43 DKVAFVEAVTGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNvaeyGIVALGIMAA----GGVFSGANPTALESE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 91 IAAIVEDAQLKLLFYAEKHLSSL----------------TDIDQNLLHMDIDVAQyDEIVNPDYHQpfqatpvepQDLAA 154
Cdd:PLN02330 119 IKKQAEAAGAKLIVTNDTNYGKVkglglpvivlgeekieGAVNWKELLEAADRAG-DTSDNEEILQ---------TDLCA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 155 LIYTSGTTGSPKGVMFSYESFVhngANLELT-YKFNSNYITIVST----PMFHVLGFNDTVLPVLMSGGTLI-LQRYFNG 228
Cdd:PLN02330 189 LPFSSGTTGISKGVMLTHRNLV---ANLCSSlFSVGPEMIGQVVTlgliPFFHIYGITGICCATLRNKGKVVvMSRFELR 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 229 EELNDMIAQyHPTFIIMIPTMYYSTLRasnfNP--ENFRAMDYIIQG---GSQPL-PSIQAAFKQY--GINIINGYGLTE 300
Cdd:PLN02330 266 TFLNALITQ-EVSFAPIVPPIILNLVK----NPivEEFDLSKLKLQAimtAAAPLaPELLTAFEAKfpGVQVQEAYGLTE 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 301 APLVLVNTPENSKRKPMSIGKAVMFV----DARILD-DNGEEVPTGEIGELAIKAKNVTPGYWNKPAETAKAFHGR-YLL 374
Cdd:PLN02330 341 HSCITLTHGDPEKGHGIAKKNSVGFIlpnlEVKFIDpDTGRSLPKNTPGELCVRSQCVMQGYYNNKEETDRTIDEDgWLH 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 375 TGDLAKMDNDGDIFIIDRKKELIITGGENVLPSEVENALAEHPLVDRCVVVGYDHPKYGESIAAAIILREDEPHYAEILN 454
Cdd:PLN02330 421 TGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVVINPKAKESEEDIL 500
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 584959700 455 QHMRSRLAGYKVPRMYVPVTHMPLNSTQKpdklAIRQMMNDKVSQT 500
Cdd:PLN02330 501 NFVAANVAHYKKVRVVQFVDSIPKSLSGK----IMRRLLKEKMLSI 542
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
13-491 |
8.97e-41 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 152.45 E-value: 8.97e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 13 DDDKPAV-IDhakQTSWTYQQLNARADNMAHyltsqGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEI 91
Cdd:PRK07787 13 ADIADAVrIG---GRVLSRSDLAGAATAVAE-----RVAGARRVAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 92 AAIVEDAQLKLLfyaekhLSSLTDIDQNLLHMDIDVaqydeivnpdYHQPFQATPVEPQDLAALI-YTSGTTGSPKGVMF 170
Cdd:PRK07787 85 RHILADSGAQAW------LGPAPDDPAGLPHVPVRL----------HARSWHRYPEPDPDAPALIvYTSGTTGPPKGVVL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 171 SYESFVHNGANLELTYKFNSNYITIVSTPMFHVLGFNDTVLPVLMSGGTLI------LQRYfnGEELNDmiaqyHPTFII 244
Cdd:PRK07787 149 SRRAIAADLDALAEAWQWTADDVLVHGLPLFHVHGLVLGVLGPLRIGNRFVhtgrptPEAY--AQALSE-----GGTLYF 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 245 MIPTMYYSTLRasnfNPENFRAMD--YIIQGGSQPLP-----SIQAAfkqYGINIINGYGLTEApLVLVNTPENSKRKPM 317
Cdd:PRK07787 222 GVPTVWSRIAA----DPEAARALRgaRLLVSGSAALPvpvfdRLAAL---TGHRPVERYGMTET-LITLSTRADGERRPG 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 318 SIGKAVMFVDARILDDNGEEVPT-GE-IGELAIKAKNVTPGYWNKPAETAKAFHGR-YLLTGDLAKMDNDGDIFIIDRKK 394
Cdd:PRK07787 294 WVGLPLAGVETRLVDEDGGPVPHdGEtVGELQVRGPTLFDGYLNRPDATAAAFTADgWFRTGDVAVVDPDGMHRIVGRES 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 395 -ELIITGGENVLPSEVENALAEHPLVDRCVVVGYDHPKYGESIAAAIILREDEPhyAEILNQHMRSRLAGYKVPRMYVPV 473
Cdd:PRK07787 374 tDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVGADDVA--ADELIDFVAQQLSVHKRPREVRFV 451
|
490
....*....|....*...
gi 584959700 474 THMPLNSTQKPDKLAIRQ 491
Cdd:PRK07787 452 DALPRNAMGKVLKKQLLS 469
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
29-495 |
9.64e-41 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 153.75 E-value: 9.64e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 29 TYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAAIVEDAQLKLLFYAEK 108
Cdd:PRK06018 41 TYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVITDLT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 109 HLSSLTDIDQNLLHMDIDVAQYDEIVNPDYHQP---------------FQATPVEPQDLAALIYTSGTTGSPKGVMFSYE 173
Cdd:PRK06018 121 FVPILEKIADKLPSVERYVVLTDAAHMPQTTLKnavayeewiaeadgdFAWKTFDENTAAGMCYTSGTTGDPKGVLYSHR 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 174 SfvhnganleltykfnsNYITIVSTPMFHVLGFN--DTVLPVL---------------MSGGTLILQ-RYFNGEELNDMI 235
Cdd:PRK06018 201 S----------------NVLHALMANNGDALGTSaaDTMLPVVplfhanswgiafsapSMGTKLVMPgAKLDGASVYELL 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 236 AQYHPTFIIMIPTMYYSTLRASNFNPENFRAMDYIIQGGSQPLPSIQAAFKQYGINIINGYGLTE-APLVLVNT--PENS 312
Cdd:PRK06018 265 DTEKVTFTAGVPTVWLMLLQYMEKEGLKLPHLKMVVCGGSAMPRSMIKAFEDMGVEVRHAWGMTEmSPLGTLAAlkPPFS 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 313 KRKP---MSI----GKAVMFVDARILDDNGEEVP-TGE-IGELAIKAKNVTPGYWNKPAETAKAfhGRYLLTGDLAKMDN 383
Cdd:PRK06018 345 KLPGdarLDVlqkqGYPPFGVEMKITDDAGKELPwDGKtFGRLKVRGPAVAAAYYRVDGEILDD--DGFFDTGDVATIDA 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 384 DGDIFIIDRKKELIITGGENVLPSEVENALAEHPLVDRCVVVGYDHPKYGESIAAAIILREDE-PHYAEILnQHMRSRLA 462
Cdd:PRK06018 423 YGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQLKPGEtATREEIL-KYMDGKIA 501
|
490 500 510
....*....|....*....|....*....|...
gi 584959700 463 GYKVPRMYVPVTHMPLNSTQKPDKLAIRQMMND 495
Cdd:PRK06018 502 KWWMPDDVAFVDAIPHTATGKILKTALREQFKD 534
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
150-483 |
2.15e-39 |
|
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.
Pssm-ID: 341290 [Multi-domain] Cd Length: 340 Bit Score: 145.87 E-value: 2.15e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 150 QDLAALIYTSGTTGSPKGVMFSYESFVHNGANLELTYK-FNSNYITIVSTPMFHVLGFNDTVLPVLMSGGTLILQRYFNG 228
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLnWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGENTTY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 229 EELNDMIAQYHPTFIIMIPT-MYYSTLRASNFNPENfRAMDYIIQGGSQPLPSIQAAFKQYG-INIINGYGLTEAPLVLV 306
Cdd:cd17635 81 KSLFKILTTNAVTTTCLVPTlLSKLVSELKSANATV-PSLRLIGYGGSRAIAADVRFIEATGlTNTAQVYGLSETGTALC 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 307 NTPENSKRKPMSIGKAVMFVDARILDDNGEEVPTGEIGELAIKAKNVTPGYWNKPAETAKAFHGRYLLTGDLAKMDNDGD 386
Cdd:cd17635 160 LPTDDDSIEINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLIDGWVNTGDLGERREDGF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 387 IFIIDRKKELIITGGENVLPSEVENALAEHPLVDRCVVVGYDHPKYGESIAAAIILRE-DEPHYAEILNQHMRSRLAGYK 465
Cdd:cd17635 240 LFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVASAeLDENAIRALKHTIRRELEPYA 319
|
330
....*....|....*...
gi 584959700 466 VPRMYVPVTHMPLNSTQK 483
Cdd:cd17635 320 RPSTIVIVTDIPRTQSGK 337
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
15-492 |
2.29e-39 |
|
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: 149.98 E-value: 2.29e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 15 DKPAVIDHAKQTSWTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAAI 94
Cdd:cd17642 32 GTIAFTDAHTGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHS 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 95 VEDAQLKLLFYAEKHLSSLTDIDQNL--------LHMDIDVAQYDEIVN------PDYHQPFQATPVE---PQDLAALIY 157
Cdd:cd17642 112 LNISKPTIVFCSKKGLQKVLNVQKKLkiiktiiiLDSKEDYKGYQCLYTfitqnlPPGFNEYDFKPPSfdrDEQVALIMN 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 158 TSGTTGSPKGVMFSYESFVHNGAN-LELTYKFNSNYITIVST--PMFHVLGFNdTVLPVLMSGGTLILQRYFNGEELNDM 234
Cdd:cd17642 192 SSGSTGLPKGVQLTHKNIVARFSHaRDPIFGNQIIPDTAILTviPFHHGFGMF-TTLGYLICGFRVVLMYKFEEELFLRS 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 235 IAQYHPTFIIMIPTMYYSTLRASNFNPENFRAMDYIIQGGSqPLPSI--QAAFKQYGINII-NGYGLTEAPLVLVNTPEN 311
Cdd:cd17642 271 LQDYKVQSALLVPTLFAFFAKSTLVDKYDLSNLHEIASGGA-PLSKEvgEAVAKRFKLPGIrQGYGLTETTSAILITPEG 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 312 SKrKPMSIGKAVMFVDARILD-DNGEEVPTGEIGELAIKAKNVTPGYWNKPAETAKAFHGR-YLLTGDLAKMDNDGDIFI 389
Cdd:cd17642 350 DD-KPGAVGKVVPFFYAKVVDlDTGKTLGPNERGELCVKGPMIMKGYVNNPEATKALIDKDgWLHSGDIAYYDEDGHFFI 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 390 IDRKKELIITGGENVLPSEVENALAEHPLVDRCVVVGYDHPKYGESIAAAIILREDEPHYAEILNQHMRSRLAGYKVPRM 469
Cdd:cd17642 429 VDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVVLEAGKTMTEKEVMDYVASQVSTAKRLRG 508
|
490 500
....*....|....*....|....
gi 584959700 470 YVP-VTHMPLNSTQKPDKLAIRQM 492
Cdd:cd17642 509 GVKfVDEVPKGLTGKIDRRKIREI 532
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
28-491 |
8.73e-38 |
|
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: 144.88 E-value: 8.73e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 28 WTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAAIVEDAQLKLLFY-- 105
Cdd:cd05915 25 TTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVLLFdp 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 106 -----AEKHLSSLTDIDQNLLHMDiDVAQYDEIV---NPDYhQPFQatPVEPQDLAALIYTSGTTGSPKGVMFSYESFVH 177
Cdd:cd05915 105 nllplVEAIRGELKTVQHFVVMDE-KAPEGYLAYeeaLGEE-ADPV--RVPERAACGMAYTTGTTGLPKGVVYSHRALVL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 178 N----GANLELTYKFNSNYITIVstPMFHVLGFNdTVLPVLMSGGTLI-LQRYFNGEELNDMIAQYHPTFIIMIPTMYYS 252
Cdd:cd05915 181 HslaaSLVDGTALSEKDVVLPVV--PMFHVNAWC-LPYAATLVGAKQVlPGPRLDPASLVELFDGEGVTFTAGVPTVWLA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 253 TLRASNFNPENFRAMDYIIQGGSQPlPSIQAAFKQYG-INIINGYGLTE------APLVLV---NTPENSKRKPMSIGKA 322
Cdd:cd05915 258 LADYLESTGHRLKTLRRLVVGGSAA-PRSLIARFERMgVEVRQGYGLTEtspvvvQNFVKShleSLSEEEKLTLKAKTGL 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 323 VMFVDA-RILDDNGEEVPTG--EIGELAIKAKNVTPGYW-NKPAETAKAFHGRYLLTGDLAKMDNDGDIFIIDRKKELII 398
Cdd:cd05915 337 PIPLVRlRVADEEGRPVPKDgkALGEVQLKGPWITGGYYgNEEATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIK 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 399 TGGENVLPSEVENALAEHPLVDRCVVVGYDHPKYGESIAAAIILREDEPHYAEILnQHMRSRLAGYK-VPRMYVPVTHMP 477
Cdd:cd05915 417 SGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVVVPRGEKPTPEELN-EHLLKAGFAKWqLPDAYVFAEEIP 495
|
490
....*....|....
gi 584959700 478 LNSTQKPDKLAIRQ 491
Cdd:cd05915 496 RTSAGKFLKRALRE 509
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
28-468 |
1.23e-37 |
|
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: 143.65 E-value: 1.23e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 28 WTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAAIVEDAQLKLLFYae 107
Cdd:cd05940 4 LTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLVV-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 108 khlssltdidqnllhmdidvaqydeivnpdyhqpfqatpvepqDLAALIYTSGTTGSPKGVMFSYESFVHNG---ANLEL 184
Cdd:cd05940 82 -------------------------------------------DAALYIYTSGTTGLPKAAIISHRRAWRGGaffAGSGG 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 185 TYKFNSNYITIvstPMFHVLGFNDTVLPVLMSGGTLILQRYFNGEELNDMIAQYHPTFIIMIPTMYYSTLRASNFNPENF 264
Cdd:cd05940 119 ALPSDVLYTCL---PLYHSTALIVGWSACLASGATLVIRKKFSASNFWDDIRKYQATIFQYIGELCRYLLNQPPKPTERK 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 265 RAMDYIIQGGSQPlpSIQAAFK-QYGI-NIINGYGLTEAPLVLVNTPEN-----------SKRKPMSIGKAVMFVDARIL 331
Cdd:cd05940 196 HKVRMIFGNGLRP--DIWEEFKeRFGVpRIAEFYAATEGNSGFINFFGKpgaigrnpsllRKVAPLALVKYDLESGEPIR 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 332 DDNG--EEVPTGEIGELAIKAKNVTP--GYWNKPAETAKAFHG------RYLLTGDLAKMDNDGDIFIIDRKKELIITGG 401
Cdd:cd05940 274 DAEGrcIKVPRGEPGLLISRINPLEPfdGYTDPAATEKKILRDvfkkgdAWFNTGDLMRLDGEGFWYFVDRLGDTFRWKG 353
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 584959700 402 ENVLPSEVENALAEHPLVDRCVVVGYDHPKY-GESIAAAIILREDEPHYAEILNQHMRSRLAGYKVPR 468
Cdd:cd05940 354 ENVSTTEVAAVLGAFPGVEEANVYGVQVPGTdGRAGMAAIVLQPNEEFDLSALAAHLEKNLPGYARPL 421
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
15-477 |
1.24e-37 |
|
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: 145.80 E-value: 1.24e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 15 DKPAVIDHAKQTS----WTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKE 90
Cdd:cd17634 68 DRTAIIYEGDDTSqsrtISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 91 IAAIVEDAQLKLLFYAEKHLSSLTDIdqNLLHMDIDVA--------------------QYDEIVNPDYH-----QP--FQ 143
Cdd:cd17634 148 VAGRIIDSSSRLLITADGGVRAGRSV--PLKKNVDDALnpnvtsvehvivlkrtgsdiDWQEGRDLWWRdliakASpeHQ 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 144 ATPVEPQDLAALIYTSGTTGSPKGVMFsyesfVHNGANLELTYKFNSNY------ITIVSTPMFHVLGFNDTVLPVLMSG 217
Cdd:cd17634 226 PEAMNAEDPLFILYTSGTTGKPKGVLH-----TTGGYLVYAATTMKYVFdygpgdIYWCTADVGWVTGHSYLLYGPLACG 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 218 GTLILqryFNG-------EELNDMIAQYHPTFIIMIPTMY---------------YSTLR-----ASNFNPENFRAMDYI 270
Cdd:cd17634 301 ATTLL---YEGvpnwptpARMWQVVDKHGVNILYTAPTAIralmaagddaiegtdRSSLRilgsvGEPINPEAYEWYWKK 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 271 IQGGSQPlpsiqaafkqyginIINGYGLTEAPLVLV-NTPENSKRKPMSIGKAVMFVDARILDDNGEEVPTGEIGELAIK 349
Cdd:cd17634 378 IGKEKCP--------------VVDTWWQTETGGFMItPLPGAIELKAGSATRPVFGVQPAVVDNEGHPQPGGTEGNLVIT 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 350 AK--NVTPGYWNKPAETAKAFHGR---YLLTGDLAKMDNDGDIFIIDRKKELIITGGENVLPSEVENALAEHPLVDRCVV 424
Cdd:cd17634 444 DPwpGQTRTLFGDHERFEQTYFSTfkgMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAV 523
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 584959700 425 VGYDHPKYGESIAAAIILR---EDEPHYAEILNQHMRSRLAGYKVPRMYVPVTHMP 477
Cdd:cd17634 524 VGIPHAIKGQAPYAYVVLNhgvEPSPELYAELRNWVRKEIGPLATPDVVHWVDSLP 579
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
155-485 |
1.82e-37 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 140.98 E-value: 1.82e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 155 LIYTSGTTGSPKGVMFSYESF---VHNGANLElTYKFNSNYITIVST------------PMFHVLGFNdTVLPVLMSGGT 219
Cdd:cd05924 8 ILYTGGTTGMPKGVMWRQEDIfrmLMGGADFG-TGEFTPSEDAHKAAaaaagtvmfpapPLMHGTGSW-TAFGGLLGGQT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 220 LILQRY-FNGEELNDMIAQYHPTFIIMI-PTMYYSTLRA-SNFNPENFRAMDYIIQGGSQPLPSIQAAFKQYGINI--IN 294
Cdd:cd05924 86 VVLPDDrFDPEEVWRTIEKHKVTSMTIVgDAMARPLIDAlRDAGPYDLSSLFAISSGGALLSPEVKQGLLELVPNItlVD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 295 GYGLTEAPLVLVNTpenSKRKPMSIGKAVMFV-DARILDDNGEEVPTGEIGELAIKAKNVTP-GYWNKPAETAKAFHG-- 370
Cdd:cd05924 166 AFGSSETGFTGSGH---SAGSGPETGPFTRANpDTVVLDDDGRVVPPGSGGVGWIARRGHIPlGYYGDEAKTAETFPEvd 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 371 --RYLLTGDLAKMDNDGDIFIIDRKKELIITGGENVLPSEVENALAEHPLVDRCVVVGYDHPKYGESIAAAIILREDEPH 448
Cdd:cd05924 243 gvRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQEVVAVVQLREGAGV 322
|
330 340 350
....*....|....*....|....*....|....*..
gi 584959700 449 YAEILNQHMRSRLAGYKVPRMYVPVTHMPLNSTQKPD 485
Cdd:cd05924 323 DLEELREHCRTRIARYKLPKQVVFVDEIERSPAGKAD 359
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
15-489 |
3.78e-37 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 146.34 E-value: 3.78e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 15 DKPAVIDhaKQTSWTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAAI 94
Cdd:PRK10252 473 DAPALAD--ARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMM 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 95 VEDAQLKLLFYAEKHLSSLTDIDqnllhmDIDVAQYDEIVNPDYHQPFQatPVEPQDLAALIYTSGTTGSPKGVMFSYES 174
Cdd:PRK10252 551 LEDARPSLLITTADQLPRFADVP------DLTSLCYNAPLAPQGAAPLQ--LSQPHHTAYIIFTSGSTGRPKGVMVGQTA 622
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 175 FVHNGANLELTYKFNSNYITIVSTPMfhvlGFNDTV----LPvLMSGGTLIL---QRYFNGEELNDMIAQYHPTFIIMIP 247
Cdd:PRK10252 623 IVNRLLWMQNHYPLTADDVVLQKTPC----SFDVSVweffWP-FIAGAKLVMaepEAHRDPLAMQQFFAEYGVTTTHFVP 697
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 248 TMyystLRASNFNPENframdyiiQGGSQPLPSIQAAF---------------KQYGINIINGYGLTEA----------P 302
Cdd:PRK10252 698 SM----LAAFVASLTP--------EGARQSCASLRQVFcsgealpadlcrewqQLTGAPLHNLYGPTEAavdvswypafG 765
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 303 LVLVNTPENskrkPMSIGKAVMFVDARILDDNGEEVPTGEIGELAIKAKNVTPGYWNKPAETAKAF-------HGRYLLT 375
Cdd:PRK10252 766 EELAAVRGS----SVPIGYPVWNTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFiadpfapGERMYRT 841
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 376 GDLAKMDNDGDIFIIDRKKELIITGGENVLPSEVENALAEHPLVDRCVV---VGYDHPKYG---ESIAAAIILREDEPHY 449
Cdd:PRK10252 842 GDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAVThacVINQAAATGgdaRQLVGYLVSQSGLPLD 921
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 584959700 450 AEILNQHMRSRLAGYKVPRMYVPVTHMPLNSTQKPDKLAI 489
Cdd:PRK10252 922 TSALQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKAL 961
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
15-462 |
3.97e-37 |
|
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: 144.56 E-value: 3.97e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 15 DKPAVI---DHAKQTSWTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEI 91
Cdd:cd05968 76 TRPALRwegEDGTSRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAA 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 92 AAIVEDAQLKLLFYAE------KHLSSLTDIDQNLLHM--------------DIDVAQYDEIVNPDY--HQPFQATPVEP 149
Cdd:cd05968 156 ATRLQDAEAKALITADgftrrgREVNLKEEADKACAQCptvekvvvvrhlgnDFTPAKGRDLSYDEEkeTAGDGAERTES 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 150 QDLAALIYTSGTTGSPKGVMFSYESFVHNGAnLELTYKFNSNyitivstPMFHVLGFND--------TVLPVLMSGGTLI 221
Cdd:cd05968 236 EDPLMIIYTSGTTGKPKGTVHVHAGFPLKAA-QDMYFQFDLK-------PGDLLTWFTDlgwmmgpwLIFGGLILGATMV 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 222 LqryFNG-------EELNDMIAQYHPTFIIMIPTMY---------------YSTLRA-----SNFNPENFRAMDYIIQGG 274
Cdd:cd05968 308 L---YDGapdhpkaDRLWRMVEDHEITHLGLSPTLIralkprgdapvnahdLSSLRVlgstgEPWNPEPWNWLFETVGKG 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 275 SQPlpsiqaafkqyginIINGYGLTE-APLVLVNTPENSKrKPMSIGKAVMFVDARILDDNGEEVPtGEIGELAIKAK-- 351
Cdd:cd05968 385 RNP--------------IINYSGGTEiSGGILGNVLIKPI-KPSSFNGPVPGMKADVLDESGKPAR-PEVGELVLLAPwp 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 352 NVTPGYWNKPAETAKAFHGRY---LLTGDLAKMDNDGDIFIIDRKKELIITGGENVLPSEVENALAEHPLVDRCVVVGYD 428
Cdd:cd05968 449 GMTRGFWRDEDRYLETYWSRFdnvWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVP 528
|
490 500 510
....*....|....*....|....*....|....
gi 584959700 429 HPKYGESIAAAIILREDEPhYAEILNQHMRSRLA 462
Cdd:cd05968 529 HPVKGEAIVCFVVLKPGVT-PTEALAEELMERVA 561
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
28-426 |
8.09e-36 |
|
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: 139.53 E-value: 8.09e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 28 WTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPN--DIAILDLlfACFKTGAVFLPLNWRLNPKEIAAIVEDAQLKLLFY 105
Cdd:cd05932 7 FTWGEVADKARRLAAALRALGLEPGSKIALISKNcaEWFITDL--AIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 106 -------AEKHLSSLTDIDQNLLHMDIDVAQY--DEIVNpdYHQPFQATPV-EPQDLAALIYTSGTTGSPKGVMFSYESF 175
Cdd:cd05932 85 gklddwkAMAPGVPEGLISISLPPPSAANCQYqwDDLIA--QHPPLEERPTrFPEQLATLIYTSGTTGQPKGVMLTFGSF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 176 VHNGANLELTYKFNSNYITIVSTPMFHVlgfndtVLPVLMSGGTLI--LQRYFnGEELNDMIA--QYH-PTFIIMIPTMY 250
Cdd:cd05932 163 AWAAQAGIEHIGTEENDRMLSYLPLAHV------TERVFVEGGSLYggVLVAF-AESLDTFVEdvQRArPTLFFSVPRLW 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 251 -------YSTLRASNFN-----PENFR----------AMDY--IIQGGSQPLP-SIQAAFKQYGINIINGYGLTEAPLV- 304
Cdd:cd05932 236 tkfqqgvQDKIPQQKLNlllkiPVVNSlvkrkvlkglGLDQcrLAGCGSAPVPpALLEWYRSLGLNILEAYGMTENFAYs 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 305 LVNTPenSKRKPMSIGKAVMFVDARILDDngeevptgeiGELAIKAKNVTPGYWNKPAETAKAFHGR-YLLTGDLAKMDN 383
Cdd:cd05932 316 HLNYP--GRDKIGTVGNAGPGVEVRISED----------GEILVRSPALMMGYYKDPEATAEAFTADgFLRTGDKGELDA 383
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 584959700 384 DGDIFIIDRKKELIITG-GENVLPSEVENALAEHPLVDRCVVVG 426
Cdd:cd05932 384 DGNLTITGRVKDIFKTSkGKYVAPAPIENKLAEHDRVEMVCVIG 427
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
55-483 |
1.86e-35 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 138.66 E-value: 1.86e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 55 IGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAAIVEDAQLKLLFYAEKHLSSLTDIDQNLLHMDIDVAQYDEIV 134
Cdd:PRK07867 57 VGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARDIAHADCQLVLTESAHAELLDGLDPGVRVINVDSPAWADEL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 135 NPDYHQPFQATPVEPQDLAALIYTSGTTGSPKGVMFSYESFVHNGANLELTYKFNSNYITIVSTPMFHvlgfNDTVL--- 211
Cdd:PRK07867 137 AAHRDAEPPFRVADPDDLFMLIFTSGTSGDPKAVRCTHRKVASAGVMLAQRFGLGPDDVCYVSMPLFH----SNAVMagw 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 212 -PVLMSGGTLILQRYFNGEELNDMIAQYHPTFiimiptMYY-----STLRASNFNPEN----FRAMdYiiqgGSQPLPSI 281
Cdd:PRK07867 213 aVALAAGASIALRRKFSASGFLPDVRRYGATY------ANYvgkplSYVLATPERPDDadnpLRIV-Y----GNEGAPGD 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 282 QAAF-KQYGINIINGYGLTEAPLVLVNTPENskrKPMSIGKAvmFVDARILD-DNGEEVPTGE------------IGELA 347
Cdd:PRK07867 282 IARFaRRFGCVVVDGFGSTEGGVAITRTPDT---PPGALGPL--PPGVAIVDpDTGTECPPAEdadgrllnadeaIGELV 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 348 ikakNVT-----PGYWNKP-AETAKAFHGRYLlTGDLAKMDNDGDIFIIDRKKELIITGGENVLPSEVENALAEHPLVDR 421
Cdd:PRK07867 357 ----NTAgpggfEGYYNDPeADAERMRGGVYW-SGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATE 431
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 584959700 422 CVVVGYDHPKYGESIAAAIILRE----DEPHYAEILnqHMRSRLAGYKVPRMYVPVTHMPLNSTQK 483
Cdd:PRK07867 432 VAVYAVPDPVVGDQVMAALVLAPgakfDPDAFAEFL--AAQPDLGPKQWPSYVRVCAELPRTATFK 495
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
15-499 |
3.30e-35 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 136.93 E-value: 3.30e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 15 DKPAVIDHakQTSWTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAAI 94
Cdd:PRK09029 18 QAIALRLN--DEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLLEEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 95 VEDAQLKLLFYAE--KHLSSLTDIDQNLLHMDIDVAqydeivnpdyhqpFQatpvePQDLAALIYTSGTTGSPKGVMFSY 172
Cdd:PRK09029 96 LPSLTLDFALVLEgeNTFSALTSLHLQLVEGAHAVA-------------WQ-----PQRLATMTLTSGSTGLPKAAVHTA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 173 ESFVHNGAN-LELTyKFNSNYITIVSTPMFHVLGfNDTVLPVLMSGGTLILQryfNGEELNDMIAQYhpTFIIMIPTMYY 251
Cdd:PRK09029 158 QAHLASAEGvLSLM-PFTAQDSWLLSLPLFHVSG-QGIVWRWLYAGATLVVR---DKQPLEQALAGC--THASLVPTQLW 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 252 STLrASNFNPENFRAmdyIIQGGSQ-PLPSIQAAfKQYGINIINGYGLTEAplvlvntpenskrkpmsiGKAVMFVDARI 330
Cdd:PRK09029 231 RLL-DNRSEPLSLKA---VLLGGAAiPVELTEQA-EQQGIRCWCGYGLTEM------------------ASTVCAKRADG 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 331 LDDNGEEVPTGEI----GELAIKAKNVTPGYWNK----PAETAKA-FHgryllTGDLAKMdNDGDIFIIDRKKELIITGG 401
Cdd:PRK09029 288 LAGVGSPLPGREVklvdGEIWLRGASLALGYWRQgqlvPLVNDEGwFA-----TRDRGEW-QNGELTILGRLDNLFFSGG 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 402 ENVLPSEVENALAEHPLVDRCVVVGYDHPKYGESIAAAIILREDEPhyAEILNQHMRSRLAGYKVPRMYVPVTHMPLNST 481
Cdd:PRK09029 362 EGIQPEEIERVINQHPLVQQVFVVPVADAEFGQRPVAVVESDSEAA--VVNLAEWLQDKLARFQQPVAYYLLPPELKNGG 439
|
490
....*....|....*...
gi 584959700 482 QKPDKLAIRQMMNDKVSQ 499
Cdd:PRK09029 440 IKISRQALKEWVAQQLGN 457
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
27-491 |
1.11e-34 |
|
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: 135.64 E-value: 1.11e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 27 SWTYQQLNARADNMAHYLTSQ-GVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAAIVEDAQLKLLFY 105
Cdd:cd05937 5 TWTYSETYDLVLRYAHWLHDDlGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLSGSRFVIV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 106 aekhlssltdidqnllhmdidvaqydeivnpdyhqpfqatpvEPQDLAALIYTSGTTGSPKGVMFSY------ESFVHNG 179
Cdd:cd05937 85 ------------------------------------------DPDDPAILIYTSGTTGLPKAAAISWrrtlvtSNLLSHD 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 180 ANLeltyKFNSNYITIVstPMFHVLGFNDTVLPVLMSGGTLILQRYFNGEELNDMIAQYHPTFIIMI-PTMYYstLRASN 258
Cdd:cd05937 123 LNL----KNGDRTYTCM--PLYHGTAAFLGACNCLMSGGTLALSRKFSASQFWKDVRDSGATIIQYVgELCRY--LLSTP 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 259 FNPENfRAMDYIIQGGSQPLPSIQAAFKQ-YGINIING-YGLTEAPLVLVNTPENS------------KRKPMSIGKAVM 324
Cdd:cd05937 195 PSPYD-RDHKVRVAWGNGLRPDIWERFRErFNVPEIGEfYAATEGVFALTNHNVGDfgagaighhgliRRWKFENQVVLV 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 325 FVDAR----ILDD-NG--EEVPTGEIGEL--AIKAKNVT--PGYWNKPAETAKAF------HGR-YLLTGDLAKMDNDGD 386
Cdd:cd05937 274 KMDPEtddpIRDPkTGfcVRAPVGEPGEMlgRVPFKNREafQGYLHNEDATESKLvrdvfrKGDiYFRTGDLLRQDADGR 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 387 IFIIDRKKELIITGGENVLPSEVENALAEHPLVDRCVVVGYDHPKY-GESIAAAIILREDEPHYAEI----LNQHMRSRL 461
Cdd:cd05937 354 WYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGVKVPGHdGRAGCAAITLEESSAVPTEFtkslLASLARKNL 433
|
490 500 510
....*....|....*....|....*....|
gi 584959700 462 AGYKVPRMYVPVTHMPLNSTQKPDKLAIRQ 491
Cdd:cd05937 434 PSYAVPLFLRLTEEVATTDNHKQQKGVLRD 463
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
15-489 |
1.30e-34 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 135.79 E-value: 1.30e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 15 DKPAViDHAKQTSwTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAAI 94
Cdd:PRK04813 17 DFPAY-DYLGEKL-TYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPVDVSSPAERIEMI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 95 VEDAQLKLLFyaekhlsSLTDIDQNLLHMD-IDVAQYDEIVNPDYHQPFQAtPVEPQDLAALIYTSGTTGSPKGVMFSYE 173
Cdd:PRK04813 95 IEVAKPSLII-------ATEELPLEILGIPvITLDELKDIFATGNPYDFDH-AVKGDDNYYIIFTSGTTGKPKGVQISHD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 174 ---SFVHNGANLeltykFN-SNYITIVSTPMFhvlGFNDTVL---PVLMSGGTL------ILQRYfngEELNDMIAQYH- 239
Cdd:PRK04813 167 nlvSFTNWMLED-----FAlPEGPQFLNQAPY---SFDLSVMdlyPTLASGGTLvalpkdMTANF---KQLFETLPQLPi 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 240 ------PTFIIMiptmyysTLRASNFNPENFRAMDYIIQGGSQ-PLPSIQAAFKQY-GINIINGYGLTEAPlVLVN---- 307
Cdd:PRK04813 236 nvwvstPSFADM-------CLLDPSFNEEHLPNLTHFLFCGEElPHKTAKKLLERFpSATIYNTYGPTEAT-VAVTsiei 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 308 TPEN-SKRKPMSIGKAVMFVDARILDDNGEEVPTGEIGELAIKAKNVTPGYWNKPAETAKAF-----HGRYlLTGDLAKM 381
Cdd:PRK04813 308 TDEMlDQYKRLPIGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFftfdgQPAY-HTGDAGYL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 382 DnDGDIFIIDRKKELIITGGENVLPSEVENALAEHPLVDRCVVVGY--DHpKYgESIAAAIIL----REDEPHYAEILNQ 455
Cdd:PRK04813 387 E-DGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVVPYnkDH-KV-QYLIAYVVPkeedFEREFELTKAIKK 463
|
490 500 510
....*....|....*....|....*....|....
gi 584959700 456 HMRSRLAGYKVPRMYVPVTHMPLNSTQKPDKLAI 489
Cdd:PRK04813 464 ELKERLMEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
25-419 |
2.17e-34 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 135.87 E-value: 2.17e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 25 QTSWTYQQLNARADNMAHYLTSQGVKKGDVIgIFAPND-IAILDLLFACFKTGAVFLPLNwrlnPKEIAAIVEDAQLKLl 103
Cdd:cd05906 37 EEFQSYQDLLEDARRLAAGLRQLGLRPGDSV-ILQFDDnEDFIPAFWACVLAGFVPAPLT----VPPTYDEPNARLRKL- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 104 fyaeKHLSS-------LTD---------IDQNLLHMDIDVAQYDEIvnPDYHQPFQATPVEPQDLAALIYTSGTTGSPKG 167
Cdd:cd05906 111 ----RHIWQllgspvvLTDaelvaefagLETLSGLPGIRVLSIEEL--LDTAADHDLPQSRPDDLALLMLTSGSTGFPKA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 168 VMFSYESFVHNGANLELTYKFNSNYITIVSTPMFHVLGFNDTVLPVLMSGG-------TLILQRYFNgeeLNDMIAQYHP 240
Cdd:cd05906 185 VPLTHRNILARSAGKIQHNGLTPQDVFLNWVPLDHVGGLVELHLRAVYLGCqqvhvptEEILADPLR---WLDLIDRYRV 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 241 TFIIMiPTMYYSTLRASNFNPE----NFRAMDYIIQGGSQPLPSIQAAF----KQYGIN---IINGYGLTE-APLVLVNT 308
Cdd:cd05906 262 TITWA-PNFAFALLNDLLEEIEdgtwDLSSLRYLVNAGEAVVAKTIRRLlrllEPYGLPpdaIRPAFGMTEtCSGVIYSR 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 309 PENSKRKP-----MSIGKAVMFVDARILDDNGEEVPTGEIGELAIKAKNVTPGYWNKPAETAKAF-HGRYLLTGDLAKMD 382
Cdd:cd05906 341 SFPTYDHSqalefVSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFtEDGWFRTGDLGFLD 420
|
410 420 430
....*....|....*....|....*....|....*..
gi 584959700 383 NdGDIFIIDRKKELIITGGENVLPSEVENALAEHPLV 419
Cdd:cd05906 421 N-GNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGV 456
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
13-498 |
3.90e-34 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 135.12 E-value: 3.90e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 13 DDDKPAVIDHAKQtsWTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVflPLNWRLNPK--E 90
Cdd:PRK10946 36 ASDAIAVICGERQ--FSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLGVA--PVNALFSHQrsE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 91 IAAIVEDAQLKL--------LFYAEKHLSSLTDIDQNLLHMDIDVAQYDEIVNPDYHQP---FQATPVEPQDLAALIYTS 159
Cdd:PRK10946 112 LNAYASQIEPALliadrqhaLFSDDDFLNTLVAEHSSLRVVLLLNDDGEHSLDDAINHPaedFTATPSPADEVAFFQLSG 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 160 GTTGSPKGVmfsyeSFVHNG------ANLELTyKFNSNYITIVSTPMFH--------VLGfndtvlpVLMSGGTLILQRy 225
Cdd:PRK10946 192 GSTGTPKLI-----PRTHNDyyysvrRSVEIC-GFTPQTRYLCALPAAHnypmsspgALG-------VFLAGGTVVLAP- 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 226 fNGEELN--DMIAQYHPTFIIMIP---TMYYSTLRASNFNpENFRAMDyIIQGGSQPLPSIQAAF--KQYGINIINGYGL 298
Cdd:PRK10946 258 -DPSATLcfPLIEKHQVNVTALVPpavSLWLQAIAEGGSR-AQLASLK-LLQVGGARLSETLARRipAELGCQLQQVFGM 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 299 TEAplvLVN------TPE---NSKRKPMSIGKAVmfvdaRILDDNGEEVPTGEIGELAIKAKNVTPGYWNKPAETAKAF- 368
Cdd:PRK10946 335 AEG---LVNytrlddSDErifTTQGRPMSPDDEV-----WVADADGNPLPQGEVGRLMTRGPYTFRGYYKSPQHNASAFd 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 369 -HGRYLlTGDLAKMDNDGDIFIIDRKKELIITGGENVLPSEVENALAEHPLVDRCVVVGYDHPKYGESIAAAIILRedEP 447
Cdd:PRK10946 407 aNGFYC-SGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAFLVVK--EP 483
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 584959700 448 HYAEILNQHMRSR-LAGYKVPRMYVPVTHMPLNSTQKPDKLAIRQMMNDKVS 498
Cdd:PRK10946 484 LKAVQLRRFLREQgIAEFKLPDRVECVDSLPLTAVGKVDKKQLRQWLASRAS 535
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
29-441 |
1.88e-33 |
|
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: 133.11 E-value: 1.88e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 29 TYQQLNARADNMAHYLTSQGVK--KGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAAIVEDAQLKLLFYA 106
Cdd:cd05927 7 SYKEVAERADNIGSALRSLGGKpaPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVFCD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 107 EkhlssltdidqnllhmDIDVAQYDEIVNPDYHQPFQATPVEPQDLAALIYTSGTTGSPKGVMFSYESFVHNGANLELT- 185
Cdd:cd05927 87 A----------------GVKVYSLEEFEKLGKKNKVPPPPPKPEDLATICYTSGTTGNPKGVMLTHGNIVSNVAGVFKIl 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 186 ---YKFNSNYITIVSTPMFHVlgFNDTVLPVLMSGGTLIlqRYFNGE--ELNDMIAQYHPTFIIMIPTMY---------- 250
Cdd:cd05927 151 eilNKINPTDVYISYLPLAHI--FERVVEALFLYHGAKI--GFYSGDirLLLDDIKALKPTVFPGVPRVLnriydkifnk 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 251 -------------------YSTLRASNFNPENF--RAMDYIIQ-----------GGSQPLPS-----IQAAFkqyGINII 293
Cdd:cd05927 227 vqakgplkrklfnfalnykLAELRSGVVRASPFwdKLVFNKIKqalggnvrlmlTGSAPLSPevlefLRVAL---GCPVL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 294 NGYGLTE-------------------APLV-----LVNTPEnskrkpmsigkavMFVDARilDDNGEevptgeiGELAIK 349
Cdd:cd05927 304 EGYGQTEctagatltlpgdtsvghvgGPLPcaevkLVDVPE-------------MNYDAK--DPNPR-------GEVCIR 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 350 AKNVTPGYWNKPAETAKAFH--GrYLLTGDLAKMDNDGDIFIIDRKKELI-ITGGENVLPSEVENALAEHPLVDRCVVvg 426
Cdd:cd05927 362 GPNVFSGYYKDPEKTAEALDedG-WLHTGDIGEWLPNGTLKIIDRKKNIFkLSQGEYVAPEKIENIYARSPFVAQIFV-- 438
|
490
....*....|....*
gi 584959700 427 ydhpkYGESIAAAII 441
Cdd:cd05927 439 -----YGDSLKSFLV 448
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
13-492 |
7.23e-33 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 131.30 E-value: 7.23e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 13 DDDKPAVIDHAKQtsWTYQQLNARADNMAHYLTSQGVKKGDV-IGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEI 91
Cdd:PRK13388 14 GDDTIAVRYGDRT--WTWREVLAEAAARAAALIALADPDRPLhVGVLLGNTPEMLFWLAAAALGGYVLVGLNTTRRGAAL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 92 AAIVEDAQLKLLFYAEKHLSSLTDIDQNLLH-MDIDVAQYDEIVNPDyHQPFQATPVEPQDLAALIYTSGTTGSPKGVMF 170
Cdd:PRK13388 92 AADIRRADCQLLVTDAEHRPLLDGLDLPGVRvLDVDTPAYAELVAAA-GALTPHREVDAMDPFMLIFTSGTTGAPKAVRC 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 171 SYESFVHNGANLELTYKFNSNYITIVSTPMFHvlgfNDTVL----PVLMSGGTLILQRYFNGEELNDMIAQYHPTFiimi 246
Cdd:PRK13388 171 SHGRLAFAGRALTERFGLTRDDVCYVSMPLFH----SNAVMagwaPAVASGAAVALPAKFSASGFLDDVRRYGATY---- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 247 ptMYYSTlrasnfnpenfRAMDYIIQGGSQP---------------LPSIQAAFKQ-YGINIINGYGLTEAPLVLV---N 307
Cdd:PRK13388 243 --FNYVG-----------KPLAYILATPERPddadnplrvafgneaSPRDIAEFSRrFGCQVEDGYGSSEGAVIVVrepG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 308 TPenskrkPMSIGKAvmFVDARILD-DNGEEVPTGE-------------IGELAIK--AKNVTpGYWNKPAETAKAF-HG 370
Cdd:PRK13388 310 TP------PGSIGRG--APGVAIYNpETLTECAVARfdahgallnadeaIGELVNTagAGFFE-GYYNNPEATAERMrHG 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 371 RYlLTGDLAKMDNDGDIFIIDRKKELIITGGENVLPSEVENALAEHPLVDRCVVVGYDHPKYGESIAAAIILRE----DE 446
Cdd:PRK13388 381 MY-WSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVGDQVMAALVLRDgatfDP 459
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 584959700 447 PHYAEILnqHMRSRLAGYKVPRmYVPV-THMPLNSTQKPDKLAIRQM 492
Cdd:PRK13388 460 DAFAAFL--AAQPDLGTKAWPR-YVRIaADLPSTATNKVLKRELIAQ 503
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
29-491 |
3.12e-32 |
|
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: 129.15 E-value: 3.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 29 TYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNpkeiaaivEDAQLKLLfyaek 108
Cdd:cd05908 17 SYRHLREEALGYLGALQELGIKPGQEVVFQITHNNKFLYLFWACLLGGMIAVPVSIGSN--------EEHKLKLN----- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 109 hlssltdidqnllhmdidvaqydEIVNpDYHQPFQATPVEPQD-----LAALIYTSGTTGSPKGVMFSYESFVHN--GAN 181
Cdd:cd05908 84 -----------------------KVWN-TLKNPYLITEEEVLCeladeLAFIQFSSGSTGDPKGVMLTHENLVHNmfAIL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 182 LELTYKFNSNYITIVstPMFHVLGFNDTVLPVLMSGGT--LILQRYFNGEELNDMI-AQYHPTFIIMIPTMYYSTLrASN 258
Cdd:cd05908 140 NSTEWKTKDRILSWM--PLTHDMGLIAFHLAPLIAGMNqyLMPTRLFIRRPILWLKkASEHKATIVSSPNFGYKYF-LKT 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 259 FNPENFRAMDY----IIQGGSQPLPS-----IQAAFKQYGIN---IINGYGLTEA--------------PLVLVN----- 307
Cdd:cd05908 217 LKPEKANDWDLssirMILNGAEPIDYelcheFLDHMSKYGLKrnaILPVYGLAEAsvgaslpkaqspfkTITLGRrhvth 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 308 ---TPENSKRKP-----MSIGKAVMFVDARILDDNGEEVPTGEIGELAIKAKNVTPGYWNKPAETAKAFHGR-YLLTGDL 378
Cdd:cd05908 297 gepEPEVDKKDSecltfVEVGKPIDETDIRICDEDNKILPDGYIGHIQIRGKNVTPGYYNNPEATAKVFTDDgWLKTGDL 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 379 AKMDNdGDIFIIDRKKELIITGGENVLPSEVENALAEHPLVD--RCVVVG-YDHPKYGESIAAAIILREDEPH---YAEI 452
Cdd:cd05908 377 GFIRN-GRLVITGREKDIIFVNGQNVYPHDIERIAEELEGVElgRVVACGvNNSNTRNEEIFCFIEHRKSEDDfypLGKK 455
|
490 500 510
....*....|....*....|....*....|....*....
gi 584959700 453 LNQHMRSRlAGYKVPRMYvPVTHMPLNSTQKPDKLAIRQ 491
Cdd:cd05908 456 IKKHLNKR-GGWQINEVL-PIRRIPKTTSGKVKRYELAQ 492
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
15-489 |
2.05e-31 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 129.52 E-value: 2.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 15 DKPAVIdHAKQTsWTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAAI 94
Cdd:PRK05691 2203 QAPALT-FAGQT-LSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHYM 2280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 95 VEDAQLKLLFYAEKHLSSLTDIDQNLLH--MDIDVAQYDEIvnPDYHQPFQATPvepQDLAALIYTSGTTGSPKGVMFSY 172
Cdd:PRK05691 2281 IEDSGIGLLLSDRALFEALGELPAGVARwcLEDDAAALAAY--SDAPLPFLSLP---QHQAYLIYTSGSTGKPKGVVVSH 2355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 173 -ESFVHNGANLElTYKFNSNYITIvstpMFHVLGFN---DTVLPVLMSGGTLIL--QRYFNGEELNDMIAQYHPTFIIMI 246
Cdd:PRK05691 2356 gEIAMHCQAVIE-RFGMRADDCEL----HFYSINFDaasERLLVPLLCGARVVLraQGQWGAEEICQLIREQQVSILGFT 2430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 247 PTmYYSTLRASNFNPENFRAMDYIIQGGS----QPLPSIQAAFK-QYginIINGYGLTE------APLVLVNTPENSKRK 315
Cdd:PRK05691 2431 PS-YGSQLAQWLAGQGEQLPVRMCITGGEaltgEHLQRIRQAFApQL---FFNAYGPTEtvvmplACLAPEQLEEGAASV 2506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 316 PmsIGKAVMFVDARILDDNGEEVPTGEIGELAIKAKNVTPGYWNKPAETAKAF--------HGRYLLTGDLAKMDNDGDI 387
Cdd:PRK05691 2507 P--IGRVVGARVAYILDADLALVPQGATGELYVGGAGLAQGYHDRPGLTAERFvadpfaadGGRLYRTGDLVRLRADGLV 2584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 388 FIIDRKKELIITGGENVLPSEVENALAEHPLVDRCVVVGYDHPKyGESIAA----AIILREDEPHYA--EILNQHMRSRL 461
Cdd:PRK05691 2585 EYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLALDTPS-GKQLAGylvsAVAGQDDEAQAAlrEALKAHLKQQL 2663
|
490 500
....*....|....*....|....*...
gi 584959700 462 AGYKVPRMYVPVTHMPLNSTQKPDKLAI 489
Cdd:PRK05691 2664 PDYMVPAHLILLDSLPLTANGKLDRRAL 2691
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
29-462 |
3.90e-31 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 126.55 E-value: 3.90e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 29 TYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAAIVEDAQ--------- 99
Cdd:PRK09274 43 SFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGAVPVLVDPGMGIKNLKQCLAEAQpdafigipk 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 100 ---LKLLF-YAEKHLSSLTDIDQNLLhmdIDVAQYDEIVNPDYHQPFQATPVEPQDLAALIYTSGTTGSPKGVMFSYESF 175
Cdd:PRK09274 123 ahlARRLFgWGKPSVRRLVTVGGRLL---WGGTTLATLLRDGAAAPFPMADLAPDDMAAILFTSGSTGTPKGVVYTHGMF 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 176 VHNGANLELTYKFNSNYITIVSTPMFhVLgFNdtvlPVLmsGGTLILQRY-------FNGEELNDMIAQYHPTFIIMIPT 248
Cdd:PRK09274 200 EAQIEALREDYGIEPGEIDLPTFPLF-AL-FG----PAL--GMTSVIPDMdptrpatVDPAKLFAAIERYGVTNLFGSPA 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 249 MYYSTLRASNFNPENFRAMDYIIQGGSQPLPSIQAAFKQY---GINIINGYGLTEA-PL-------VLVNTPENSKRKP- 316
Cdd:PRK09274 272 LLERLGRYGEANGIKLPSLRRVISAGAPVPIAVIERFRAMlppDAEILTPYGATEAlPIssiesreILFATRAATDNGAg 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 317 MSIGKAVMFVDARILD---------DNGEEVPTGEIGELAIKAKNVTPGYWNKPAETAKA---------FHgRyllTGDL 378
Cdd:PRK09274 352 ICVGRPVDGVEVRIIAisdapipewDDALRLATGEIGEIVVAGPMVTRSYYNRPEATRLAkipdgqgdvWH-R---MGDL 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 379 AKMDNDGDIFIIDRKKELIITGGENVLPSEVENALAEHPLVDRCVVVGydHPKYGESIAAAII-LREDEPHYAEILNQHM 457
Cdd:PRK09274 428 GYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGVKRSALVG--VGVPGAQRPVLCVeLEPGVACSKSALYQEL 505
|
....*
gi 584959700 458 RSRLA 462
Cdd:PRK09274 506 RALAA 510
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
15-468 |
1.91e-30 |
|
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: 124.98 E-value: 1.91e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 15 DKPAVI---DHAKQT-SWTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPN----DIAILdllfACFKTGAV-------F 79
Cdd:cd05966 68 DKVAIIwegDEPDQSrTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMipelVIAML----ACARIGAVhsvvfagF 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 80 lplnwrlNPKEIAAIVEDAQLKLL-----FY-----------AEKHLSSLTDIDQNLL--HMDIDVAQ-------YDEIV 134
Cdd:cd05966 144 -------SAESLADRINDAQCKLVitadgGYrggkviplkeiVDEALEKCPSVEKVLVvkRTGGEVPMtegrdlwWHDLM 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 135 N--PDYHQPfqaTPVEPQDLAALIYTSGTTGSPKGVMFS---YESFVHnganleLTYKFNSNY--------------IT- 194
Cdd:cd05966 217 AkqSPECEP---EWMDSEDPLFILYTSGSTGKPKGVVHTtggYLLYAA------TTFKYVFDYhpddiywctadigwITg 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 195 ---IVSTPmfhvlgfndtvlpvLMSGGTLIL----------QRYFngeelnDMIAQYH-------PTFIIM-------IP 247
Cdd:cd05966 288 hsyIVYGP--------------LANGATTVMfegtptypdpGRYW------DIVEKHKvtifytaPTAIRAlmkfgdeWV 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 248 TMYY-STLR-----ASNFNPENFRAMDYIIQGGSQPlpsiqaafkqyginIINGYGLTE------APLVLVnTPenskRK 315
Cdd:cd05966 348 KKHDlSSLRvlgsvGEPINPEAWMWYYEVIGKERCP--------------IVDTWWQTEtggimiTPLPGA-TP----LK 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 316 PMSIGKAVMFVDARILDDNGEEVPTGEIGELAIKakNVTPG---------------YWnkpaetaKAFHGRYLlTGDLAK 380
Cdd:cd05966 409 PGSATRPFFGIEPAILDEEGNEVEGEVEGYLVIK--RPWPGmartiygdheryedtYF-------SKFPGYYF-TGDGAR 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 381 MDNDGDIFIIDRKKELIITGGENVLPSEVENALAEHPLVDRCVVVGYDHPKYGESIAAAIILREDEPHYAEI---LNQHM 457
Cdd:cd05966 479 RDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGEEPSDELrkeLRKHV 558
|
570
....*....|.
gi 584959700 458 RSRLAGYKVPR 468
Cdd:cd05966 559 RKEIGPIATPD 569
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
6-498 |
4.76e-30 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 124.69 E-value: 4.76e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 6 IKTRSDFDDDKPAVIDhAKQTSWTYQQLNARADNMAHYLTsQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWR 85
Cdd:PRK06814 638 IEAAKIHGFKKLAVED-PVNGPLTYRKLLTGAFVLGRKLK-KNTPPGENVGVMLPNANGAAVTFFALQSAGRVPAMINFS 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 86 LNPKEIAAIVEDAQLKLLFYA----EK-HLSSL-TDIDQ--NLLHMDiDVAQ----YDEI--VNPDYHQPFQATPVEPQD 151
Cdd:PRK06814 716 AGIANILSACKAAQVKTVLTSrafiEKaRLGPLiEALEFgiRIIYLE-DVRAqiglADKIkgLLAGRFPLVYFCNRDPDD 794
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 152 LAALIYTSGTTGSPKGVMFSYESFVHNGANLELTYKFNSNYITIVSTPMFHVLGFN-DTVLPVLmSGgtliLQRYFNGEE 230
Cdd:PRK06814 795 PAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARIDFSPEDKVFNALPVFHSFGLTgGLVLPLL-SG----VKVFLYPSP 869
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 231 LN-----DMIAQYHPTfiIMIPTMYYSTLRASNFNPENFRAMDYIIqGGSQPL--PSIQAAFKQYGINIINGYGLTE-AP 302
Cdd:PRK06814 870 LHyriipELIYDTNAT--ILFGTDTFLNGYARYAHPYDFRSLRYVF-AGAEKVkeETRQTWMEKFGIRILEGYGVTEtAP 946
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 303 LVLVNTPENSkrKPMSIGKAVMFVDARIlddngEEVP-TGEIGELAIKAKNVTPGYW--NKPA---ETAKAFHGryllTG 376
Cdd:PRK06814 947 VIALNTPMHN--KAGTVGRLLPGIEYRL-----EPVPgIDEGGRLFVRGPNVMLGYLraENPGvlePPADGWYD----TG 1015
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 377 DLAKMDNDGDIFIIDRKKELIITGGENVLPSEVENALAE------HplvdrcVVVGYDHPKYGESIaaaIILREDEPHYA 450
Cdd:PRK06814 1016 DIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAElwpdalH------AAVSIPDARKGERI---ILLTTASDATR 1086
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 584959700 451 EILNQHMRSRLAG-YKVPRMYVPVTHMPLNSTQKPDKLAIRQMMNDKVS 498
Cdd:PRK06814 1087 AAFLAHAKAAGASeLMVPAEIITIDEIPLLGTGKIDYVAVTKLAEEAAA 1135
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
199-492 |
6.12e-30 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 121.64 E-value: 6.12e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 199 PMFHVLGFNdTVLPVLMSGGTLILQRYF---NGEELNDMIAQYhptFIIMIPTMYYSTLRAsnfNPE---NFRAmdyIIQ 272
Cdd:PRK07445 168 PLYHVSGLM-QFMRSFLTGGKLVILPYKrlkSGQELPPNPSDF---FLSLVPTQLQRLLQL---RPQwlaQFRT---ILL 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 273 GGSQPLPSIQAAFKQYGINIINGYGLTE-APLVLVNTPENSKRKPMSIGKAVmfVDARIlddngeEVPTGEIGELAIKAK 351
Cdd:PRK07445 238 GGAPAWPSLLEQARQLQLRLAPTYGMTEtASQIATLKPDDFLAGNNSSGQVL--PHAQI------TIPANQTGNITIQAQ 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 352 NVTPGYWnkPAETAKAfhgRYLLTGDLAKMDNDGDIFIIDRKKELIITGGENVLPSEVENALAEHPLVDRCVVVGYDHPK 431
Cdd:PRK07445 310 SLALGYY--PQILDSQ---GIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPH 384
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 584959700 432 YGESIAAAIILREDEPHyAEILNQHMRSRLAGYKVPRMYVPVTHMPLNSTQKPDKLAIRQM 492
Cdd:PRK07445 385 WGEVVTAIYVPKDPSIS-LEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQQI 444
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
15-490 |
4.09e-29 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 121.29 E-value: 4.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 15 DKPAvidHAKQTSWTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAAI 94
Cdd:PRK06060 21 DRPA---FYAADVVTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 95 VEDAQLKLLFYAekhlSSLTDIDQNllhmdIDVAQYDEIVNpdyhqpfQATPVEPQDLAAL--------IYTSGTTGSPK 166
Cdd:PRK06060 98 ARNTEPALVVTS----DALRDRFQP-----SRVAEAAELMS-------EAARVAPGGYEPMggdalayaTYTSGTTGPPK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 167 GVMFSY-ESFVHNGANLELTYKFNSNYITIVSTPMFHVLGFNDTVLPVLMSGGTLILQRYFNGEELNDMI-AQYHPTFII 244
Cdd:PRK06060 162 AAIHRHaDPLTFVDAMCRKALRLTPEDTGLCSARMYFAYGLGNSVWFPLATGGSAVINSAPVTPEAAAILsARFGPSVLY 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 245 MIPTMYYSTLRASnfNPENFRAMDYIIQGGSQPLPSIQAAFKQY--GINIINGYGLTEAPLVLVNTPENSKRkPMSIGKA 322
Cdd:PRK06060 242 GVPNFFARVIDSC--SPDSFRSLRCVVSAGEALELGLAERLMEFfgGIPILDGIGSTEVGQTFVSNRVDEWR-LGTLGRV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 323 VMFVDARILDDNGEEVPTGEIGELAIKAKNVTPGYWNKPAETAKafHGRYLLTGDLAKMDNDGDIFIIDRKKELIITGGE 402
Cdd:PRK06060 319 LPPYEIRVVAPDGTTAGPGVEGDLWVRGPAIAKGYWNRPDSPVA--NEGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGV 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 403 NVLPSEVENALAEHPLVDRCVVVGYDHPKYGESIAAAIIlredePHYAEILNQ------HMR--SRLAGYKVPRMYVPVT 474
Cdd:PRK06060 397 NVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLV-----ATSGATIDGsvmrdlHRGllNRLSAFKVPHRFAVVD 471
|
490
....*....|....*.
gi 584959700 475 HMPLNSTQKPDKLAIR 490
Cdd:PRK06060 472 RLPRTPNGKLVRGALR 487
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
29-468 |
4.09e-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: 119.21 E-value: 4.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 29 TYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAAIVEDAqlkllfyaeK 108
Cdd:cd05974 2 SFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRDRVDRG---------G 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 109 HLssltdidqnllhmdidVAQYDEIVNPDyhqpfqatpvepqDLAALIYTSGTTGSPKGVMFSYESFvhNGANLELTYkf 188
Cdd:cd05974 73 AV----------------YAAVDENTHAD-------------DPMLLYFTSGTTSKPKLVEHTHRSY--PVGHLSTMY-- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 189 nsnYITI--------VSTPMFHVLGFNDTVLPvLMSGGTLILQRY--FNGEELNDMIAQYHPTFIIMIPTMYYSTLRAsn 258
Cdd:cd05974 120 ---WIGLkpgdvhwnISSPGWAKHAWSCFFAP-WNAGATVFLFNYarFDAKRVLAALVRYGVTTLCAPPTVWRMLIQQ-- 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 259 fNPENFRAMDYIIQGGSQPL-PS-IQAAFKQYGINIINGYGLTEAPLVLVNTPeNSKRKPMSIGKAVMFVDARILDDNGE 336
Cdd:cd05974 194 -DLASFDVKLREVVGAGEPLnPEvIEQVRRAWGLTIRDGYGQTETTALVGNSP-GQPVKAGSMGRPLPGYRVALLDPDGA 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 337 EVPTGEIGeLAIKAKN---VTPGYWNKPAETAKAFHGRYLLTGDLAKMDNDGDIFIIDRKKELIITGGENVLPSEVENAL 413
Cdd:cd05974 272 PATEGEVA-LDLGDTRpvgLMKGYAGDPDKTAHAMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVL 350
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 584959700 414 AEHPLVDRCVVVGYDHPKYGESIAAAIILR---EDEPHYAEILNQHMRSRLAGYKVPR 468
Cdd:cd05974 351 IEHPAVAEAAVVPSPDPVRLSVPKAFIVLRagyEPSPETALEIFRFSRERLAPYKRIR 408
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
27-489 |
2.34e-27 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 116.81 E-value: 2.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 27 SWTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAAIVEDAQLKLLFYA 106
Cdd:PRK05691 1156 SLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELLLTQ 1235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 107 EKHLSSL------TDIDQNLLHMDidvaqydeivnpdyHQPFQATPVEPQD--LAALIYTSGTTGSPKGVMFSYESFVHN 178
Cdd:PRK05691 1236 SHLLERLpqaegvSAIALDSLHLD--------------SWPSQAPGLHLHGdnLAYVIYTSGSTGQPKGVGNTHAALAER 1301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 179 GANLELTYKFNSNYITIVSTPmfhvLGFNDTV----LPvLMSGGTLIL-----QRyfNGEELNDMIAQYHPTFIIMIPTM 249
Cdd:PRK05691 1302 LQWMQATYALDDSDVLMQKAP----ISFDVSVwecfWP-LITGCRLVLagpgeHR--DPQRIAELVQQYGVTTLHFVPPL 1374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 250 YystlraSNFNPE----NFRAMDYIIQGGS-----------QPLPSIQaafkqyginIINGYGLTEAPLVLVN---TPEN 311
Cdd:PRK05691 1375 L------QLFIDEplaaACTSLRRLFSGGEalpaelrnrvlQRLPQVQ---------LHNRYGPTETAINVTHwqcQAED 1439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 312 SKRKPmsIGKAVMFVDARILDDNGEEVPTGEIGELAIKAKNVTPGYWNKPAETAKAF--------HGRYLLTGDLAKMDN 383
Cdd:PRK05691 1440 GERSP--IGRPLGNVLCRVLDAELNLLPPGVAGELCIGGAGLARGYLGRPALTAERFvpdplgedGARLYRTGDRARWNA 1517
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 384 DGDIFIIDRKKELIITGGENVLPSEVENALAEHPLVDRCVVVGYDHPKYGESIAAAIILREDEPHyAEILNQHMRSRLAG 463
Cdd:PRK05691 1518 DGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLVREGAAGAQLVGYYTGEAGQEAE-AERLKAALAAELPE 1596
|
490 500
....*....|....*....|....*.
gi 584959700 464 YKVPRMYVPVTHMPLNSTQKPDKLAI 489
Cdd:PRK05691 1597 YMVPAQLIRLDQMPLGPSGKLDRRAL 1622
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
145-460 |
2.58e-27 |
|
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: 115.00 E-value: 2.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 145 TPVEPQDLAALIYTSGTTGSPKGVMFSYESFVH--NGANLELTYKFNSNYITIVSTPMFHVLGFNDTVLpVLMSGGTLil 222
Cdd:cd17639 83 TDGKPDDLACIMYTSGSTGNPKGVMLTHGNLVAgiAGLGDRVPELLGPDDRYLAYLPLAHIFELAAENV-CLYRGGTI-- 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 223 qRYFNGEELNDMI--------AQYHPTFIIMIP--------------------------TMYYSTLRASNFNPENF---- 264
Cdd:cd17639 160 -GYGSPRTLTDKSkrgckgdlTEFKPTLMVGVPaiwdtirkgvlaklnpmgglkrtlfwTAYQSKLKALKEGPGTPllde 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 265 ------RAM-----DYIIQGGSqPL-PSIQAAFKQYGINIINGYGLTE----APLVLVNTPENSkrkpmSIGKAVMFVDA 328
Cdd:cd17639 239 lvfkkvRAAlggrlRYMLSGGA-PLsADTQEFLNIVLCPVIQGYGLTEtcagGTVQDPGDLETG-----RVGPPLPCCEI 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 329 RILD--------DNGEevPTGEIgelAIKAKNVTPGYWNKPAETAKAFHG-RYLLTGDLAKMDNDGDIFIIDRKKELIIT 399
Cdd:cd17639 313 KLVDweeggystDKPP--PRGEI---LIRGPNVFKGYYKNPEKTKEAFDGdGWFHTGDIGEFHPDGTLKIIDRKKDLVKL 387
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 584959700 400 -GGENVLPSEVENALAEHPLVDR-CVVVGYDHPKygesiAAAIILrEDEPHYAEILNQHMRSR 460
Cdd:cd17639 388 qNGEYIALEKLESIYRSNPLVNNiCVYADPDKSY-----PVAIVV-PNEKHLTKLAEKHGVIN 444
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
15-496 |
1.13e-26 |
|
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: 113.56 E-value: 1.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 15 DKPAVI-DHA---KQTSWTYQQLNARADNMAHYLTSQGVKKGDVIGIFAP----NDIAILdllfACFKTGAVFLPLNWRL 86
Cdd:cd05967 66 DQIALIyDSPvtgTERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPmipeAAIAML----ACARIGAIHSVVFGGF 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 87 NPKEIAAIVEDAQLKLLFYA----------------EKHLS-SLTDIDQNLL-----------HMDIDVAQYDEIVNPDY 138
Cdd:cd05967 142 AAKELASRIDDAKPKLIVTAscgiepgkvvpykpllDKALElSGHKPHHVLVlnrpqvpadltKPGRDLDWSELLAKAEP 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 139 HQPfqaTPVEPQDLAALIYTSGTTGSPKGVMfsyesfvhnganleltyKFNSNYITIVSTPMFHVLGFND---------- 208
Cdd:cd05967 222 VDC---VPVAATDPLYILYTSGTTGKPKGVV-----------------RDNGGHAVALNWSMRNIYGIKPgdvwwaasdv 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 209 --------TVLPVLMSGGTLILqryFNGEELN--------DMIAQYHPTFIIMIPTmyysTLRA-SNFNPENFRAMDYII 271
Cdd:cd05967 282 gwvvghsyIVYGPLLHGATTVL---YEGKPVGtpdpgafwRVIEKYQVNALFTAPT----AIRAiRKEDPDGKYIKKYDL 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 272 QG------GSQPL--PSIQAAFKQYGINIINGYGLTEAPLVLVNTP---ENSKRKPMSIGKAVMFVDARILDDNGEEVPT 340
Cdd:cd05967 355 SSlrtlflAGERLdpPTLEWAENTLGVPVIDHWWQTETGWPITANPvglEPLPIKAGSPGKPVPGYQVQVLDEDGEPVGP 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 341 GEIGELAIK---AKNVTPGYWNKPAETAKAFHGR---YLLTGDLAKMDNDGDIFIIDRKKELIITGGENVLPSEVENALA 414
Cdd:cd05967 435 NELGNIVIKlplPPGCLLTLWKNDERFKKLYLSKfpgYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVL 514
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 415 EHPLVDRCVVVGYDHPKYGESIAAAIILREDEPHYAEILN----QHMRSRLAGYKVPRMYVPVTHMPLNSTQKPDKLAIR 490
Cdd:cd05967 515 SHPAVAECAVVGVRDELKGQVPLGLVVLKEGVKITAEELEkelvALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTLR 594
|
....*.
gi 584959700 491 QMMNDK 496
Cdd:cd05967 595 KIADGE 600
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
5-477 |
1.83e-26 |
|
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: 113.11 E-value: 1.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 5 WIKTRSDfdddKPAVI----DHAKQTSWTYQQLNARADNMAHYLTSQGVKKGDVIGIFAP----NDIAILdllfACFKTG 76
Cdd:TIGR02188 66 HLEARPD----KVAIIwegdEPGEVRKITYRELHREVCRFANVLKSLGVKKGDRVAIYMPmipeAAIAML----ACARIG 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 77 AVFLPLNWRLNPKEIAAIVEDAQLKLLFYAEKHL-----SSLTDI-DQNLLHMDIDVAQ--------------------- 129
Cdd:TIGR02188 138 AIHSVVFGGFSAEALADRINDAGAKLVITADEGLrggkvIPLKAIvDEALEKCPVSVEHvlvvrrtgnpvvpwvegrdvw 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 130 YDEIVN--PDYHQPfqaTPVEPQDLAALIYTSGTTGSPKGVMFS---YESFVHNGANLELTYKFNSNY--------IT-- 194
Cdd:TIGR02188 218 WHDLMAkaSAYCEP---EPMDSEDPLFILYTSGSTGKPKGVLHTtggYLLYAAMTMKYVFDIKDGDIFwctadvgwITgh 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 195 --IVSTPmfhvlgfndtvlpvLMSGGTLIL----QRYFNGEELNDMIAQYH-------PTFIIM-------IPTMY-YST 253
Cdd:TIGR02188 295 syIVYGP--------------LANGATTVMfegvPTYPDPGRFWEIIEKHKvtifytaPTAIRAlmrlgdeWVKKHdLSS 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 254 LR-----ASNFNPENFRAMDYIIQGGSQPlpsiqaafkqyginIINGYGLTE------APLvlvntPENSKRKPMSIGKA 322
Cdd:TIGR02188 361 LRllgsvGEPINPEAWMWYYKVVGKERCP--------------IVDTWWQTEtggimiTPL-----PGATPTKPGSATLP 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 323 VMFVDARILDDNGEEVP-TGEIGELAIkaKNVTPGY----WNKPAETAKAFHGR---YLLTGDLAKMDNDGDIFIIDRKK 394
Cdd:TIGR02188 422 FFGIEPAVVDEEGNPVEgPGEGGYLVI--KQPWPGMlrtiYGDHERFVDTYFSPfpgYYFTGDGARRDKDGYIWITGRVD 499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 395 ELIITGGENVLPSEVENALAEHPLVDRCVVVGYDHPKYGESIAAAIILREDEPHYAEI---LNQHMRSRLAGYKVPRMYV 471
Cdd:TIGR02188 500 DVINVSGHRLGTAEIESALVSHPAVAEAAVVGIPDDIKGQAIYAFVTLKDGYEPDDELrkeLRKHVRKEIGPIAKPDKIR 579
|
....*.
gi 584959700 472 PVTHMP 477
Cdd:TIGR02188 580 FVPGLP 585
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
29-426 |
3.88e-25 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 107.93 E-value: 3.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 29 TYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAAIVEDAqlkllfyaek 108
Cdd:cd05910 4 SFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEA---------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 109 hlssltdidqnllhmdidvaqydeivNPDyhqPFQATPvEPQDLAALIYTSGTTGSPKGVMFSYESFVHNGANLELTYKF 188
Cdd:cd05910 74 --------------------------EPD---AFIGIP-KADEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGI 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 189 NSNYITIVSTPMFHVLGfndtvlPVLmsGGTLILQRY-------FNGEELNDMIAQYHPTFIIMIPTMYYSTLRASNFNP 261
Cdd:cd05910 124 RPGEVDLATFPLFALFG------PAL--GLTSVIPDMdptrparADPQKLVGAIRQYGVSIVFGSPALLERVARYCAQHG 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 262 ENFRAMDYIIQGGSQPLPSIQAAFKQY---GINIINGYGLTEA-PLVLV--------NTPENSKRKPMSIGKAVMFVDAR 329
Cdd:cd05910 196 ITLPSLRRVLSAGAPVPIALAARLRKMlsdEAEILTPYGATEAlPVSSIgsrellatTTAATSGGAGTCVGRPIPGVRVR 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 330 ILD---------DNGEEVPTGEIGELAIKAKNVTPGYWNKPAETAKA-----FHGRYLLTGDLAKMDNDGDIFIIDRKKE 395
Cdd:cd05910 276 IIEiddepiaewDDTLELPRGEIGEITVTGPTVTPTYVNRPVATALAkiddnSEGFWHRMGDLGYLDDEGRLWFCGRKAH 355
|
410 420 430
....*....|....*....|....*....|.
gi 584959700 396 LIITGGENVLPSEVENALAEHPLVDRCVVVG 426
Cdd:cd05910 356 RVITTGGTLYTEPVERVFNTHPGVRRSALVG 386
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
15-489 |
2.37e-24 |
|
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: 105.63 E-value: 2.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 15 DKPAVIDH--AKQTSWTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIA 92
Cdd:cd17654 2 DRPALIIDqtTSDTTVSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 93 AIVEDAQLKLLFYAEKHLSSLTDIDQNLLHMDIDVaqydeivnpdyhqpfqatpvePQDLAALIYTSGTTGSPKGVMFSY 172
Cdd:cd17654 82 TVMKKCHVSYLLQNKELDNAPLSFTPEHRHFNIRT---------------------DECLAYVIHTSGTTGTPKIVAVPH 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 173 ESFVHNGANLELTYKFNSNyITIVSTPMFHvlgFNDTVLPVLM---SGGTLILQRYFNGEE---LNDMIAQYH-PTFIIM 245
Cdd:cd17654 141 KCILPNIQHFRSLFNITSE-DILFLTSPLT---FDPSVVEIFLslsSGATLLIVPTSVKVLpskLADILFKRHrITVLQA 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 246 IPTMYYSTLRAS--NFNPENFRAMDYIIQGGSqPLPSI----QAAFKQYGINIINGYGLTEAPLVLVNTPENSKRKPMSI 319
Cdd:cd17654 217 TPTLFRRFGSQSikSTVLSATSSLRVLALGGE-PFPSLvilsSWRGKGNRTRIFNIYGITEVSCWALAYKVPEEDSPVQL 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 320 GKAVMFVDARILDDNGEEVPtgeiGELAIKAKN---VTPGYWNKPAETAKAfhgryllTGDLAKMdNDGDIFIIDRKKEL 396
Cdd:cd17654 296 GSPLLGTVIEVRDQNGSEGT----GQVFLGGLNrvcILDDEVTVPKGTMRA-------TGDFVTV-KDGELFFLGRKDSQ 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 397 IITGGENVLPSEVENALAEHPLVDRCVVVGYDHpkygESIAAAIIlreDEPHYAEILNQHMRSRLAGYKVPRMYVPVTHM 476
Cdd:cd17654 364 IKRRGKRINLDLIQQVIESCLGVESCAVTLSDQ----QRLIAFIV---GESSSSRIHKELQLTLLSSHAIPDTFVQIDKL 436
|
490
....*....|...
gi 584959700 477 PLNSTQKPDKLAI 489
Cdd:cd17654 437 PLTSHGKVDKSEL 449
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
15-458 |
2.92e-24 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 106.38 E-value: 2.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 15 DKPAVI----DHAKQTSWTYQQLNARADNMAHYLTSQGVKKGDVIGIFAP----NDIAILdllfACFKTGAV-------F 79
Cdd:PRK00174 82 DKVAIIwegdDPGDSRKITYRELHREVCRFANALKSLGVKKGDRVAIYMPmipeAAVAML----ACARIGAVhsvvfggF 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 80 lplnwrlNPKEIAAIVEDAQLKLLFYA----------------EKHLSSLTDIDQNLL--HMDIDVAQ-------YDEIV 134
Cdd:PRK00174 158 -------SAEALADRIIDAGAKLVITAdegvrggkpiplkanvDEALANCPSVEKVIVvrRTGGDVDWvegrdlwWHELV 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 135 N--PDYHQPfqaTPVEPQDLAALIYTSGTTGSPKGVmfsyesfVHNGANleltykfnsnYITIVSTPMFHVLGFNDT--- 209
Cdd:PRK00174 231 AgaSDECEP---EPMDAEDPLFILYTSGSTGKPKGV-------LHTTGG----------YLVYAAMTMKYVFDYKDGdvy 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 210 ---------------VLPVLMSGGTLIL----QRYFNGEELNDMIAQYH-------PTFIIM-------IPTMY-YSTLR 255
Cdd:PRK00174 291 wctadvgwvtghsyiVYGPLANGATTLMfegvPNYPDPGRFWEVIDKHKvtifytaPTAIRAlmkegdeHPKKYdLSSLR 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 256 ASN-----FNPENFRAMDYIIQGGSQPlpsiqaafkqyginIINGYGLTE------APLvlvntPENSKRKPMSIGKAVM 324
Cdd:PRK00174 371 LLGsvgepINPEAWEWYYKVVGGERCP--------------IVDTWWQTEtggimiTPL-----PGATPLKPGSATRPLP 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 325 FVDARILDDNGEEVPTGEIGELAIKAKnvTPG---------------YWNKpaetakaFHGRYLlTGDLAKMDNDGDIFI 389
Cdd:PRK00174 432 GIQPAVVDEEGNPLEGGEGGNLVIKDP--WPGmmrtiygdherfvktYFST-------FKGMYF-TGDGARRDEDGYYWI 501
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 584959700 390 IDRKKELIITGGENVLPSEVENALAEHPLVDRCVVVGYDHPKYGESIAAAIILREDEPHYAEI---LNQHMR 458
Cdd:PRK00174 502 TGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLKGGEEPSDELrkeLRNWVR 573
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
52-416 |
3.04e-24 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 106.05 E-value: 3.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 52 GDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAAIVEDAQLKLLFYAEKHLSSLTDIDQN-------LLHMD 124
Cdd:PRK06334 67 DQHIGIMMPASAGAYIAYFATLLSGKIPVMINWSQGLREVTACANLVGVTHVLTSKQLMQHLAQTHGEdaeypfsLIYME 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 125 -----------IDVAQYDEIVNPDYHQPFQATPVEPQDLAALIYTSGTTGSPKGVMFSYESFVhngANLELTYKF---NS 190
Cdd:PRK06334 147 evrkelsfwekCRIGIYMSIPFEWLMRWFGVSDKDPEDVAVILFTSGTEKLPKGVPLTHANLL---ANQRACLKFfspKE 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 191 NYITIVSTPMFHVLGFND-TVLPVLMSGGTLILQRYFNGEELNDMIAQYHPTFIIMIPTMYYSTLRASNFNPENFRAMDY 269
Cdd:PRK06334 224 DDVMMSFLPPFHAYGFNScTLFPLLSGVPVVFAYNPLYPKKIVEMIDEAKVTFLGSTPVFFDYILKTAKKQESCLPSLRF 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 270 IIQGGSQPLPSIQAAFKQY--GINIINGYGLTE-APLVLVNTpENSKRKPMSIGKAVMFVDARILDDNGE-EVPTGEIGE 345
Cdd:PRK06334 304 VVIGGDAFKDSLYQEALKTfpHIQLRQGYGTTEcSPVITINT-VNSPKHESCVGMPIRGMDVLIVSEETKvPVSSGETGL 382
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 584959700 346 LAIKAKNVTPGYW-NKPAETAKAFHG-RYLLTGDLAKMDNDGDIFIIDRKKELIITGGENVLPSEVENALAEH 416
Cdd:PRK06334 383 VLTRGTSLFSGYLgEDFGQGFVELGGeTWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEG 455
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
29-468 |
3.19e-24 |
|
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: 106.00 E-value: 3.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 29 TYQQLNARADNMAHYL-TSQGVKKGD---VIGiFAPNDIAILDLlfACFKTGAVFLPLNWRLNPKEIAAIVEDAQLKLLF 104
Cdd:cd17632 69 TYAELWERVGAVAAAHdPEQPVRPGDfvaVLG-FTSPDYATVDL--ALTRLGAVSVPLQAGASAAQLAPILAETEPRLLA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 105 YAEKHLSSLTDI------DQNLL----HMDID-------------------VAQYDEIVNPDYHQPFQATPVEPQD---L 152
Cdd:cd17632 146 VSAEHLDLAVEAvleggtPPRLVvfdhRPEVDahraalesarerlaavgipVTTLTLIAVRGRDLPPAPLFRPEPDddpL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 153 AALIYTSGTTGSPKGVMFS-------YESFVHNGANLELTyKFNSNYItivstPMFHVLGFNdTVLPVLMSGGTlilqRY 225
Cdd:cd17632 226 ALLIYTSGSTGTPKGAMYTerlvatfWLKVSSIQDIRPPA-SITLNFM-----PMSHIAGRI-SLYGTLARGGT----AY 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 226 FNGEE----LNDMIAQYHPTFIIMIPTM-------YYSTLRASNFNP-------ENFRA--MDYIIQG-------GSQPL 278
Cdd:cd17632 295 FAAASdmstLFDDLALVRPTELFLVPRVcdmlfqrYQAELDRRSVAGadaetlaERVKAelRERVLGGrllaavcGSAPL 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 279 PSIQAAFKQ--YGINIINGYGLTEAPLVLVNtpeNSKRKPMSIgkavmfvDARILDdngeeVPtgEI-----------GE 345
Cdd:cd17632 375 SAEMKAFMEslLDLDLHDGYGSTEAGAVILD---GVIVRPPVL-------DYKLVD-----VP--ELgyfrtdrphprGE 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 346 LAIKAKNVTPGYWNKPAETAKAF--HGRYlLTGD-LAKMDNDGDIFIIDRKKELIITGGENVLPSEVENALAEHPLVDRC 422
Cdd:cd17632 438 LLVKTDTLFPGYYKRPEVTAEVFdeDGFY-RTGDvMAELGPDRLVYVDRRNNVLKLSQGEFVTVARLEAVFAASPLVRQI 516
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 584959700 423 VVvgydhpkYGESIAA---AIILREDEPHYAEIlNQHMRSR-------------LAGYKVPR 468
Cdd:cd17632 517 FV-------YGNSERAyllAVVVPTQDALAGED-TARLRAAlaeslqriareagLQSYEIPR 570
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
26-467 |
1.96e-23 |
|
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: 102.89 E-value: 1.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 26 TSWTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAAIVEDAQLKLLFY 105
Cdd:cd05939 2 RHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALIF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 106 aeKHLSSLtdidqnllhmdiDVAQYDEivnpdyhqPFQATPVEPQDLAALIYTSGTTGSPKGVMFSYESFVHNGANLELT 185
Cdd:cd05939 82 --NLLDPL------------LTQSSTE--------PPSQDDVNFRDKLFYIYTSGTTGLPKAAVIVHSRYYRIAAGAYYA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 186 YKFNSNYITIVSTPMFHVLGFNDTVLPVLMSGGTLILQRYFNGEELNDMIAQYHPTFIIMIPTMYYSTLRASNFNPENFR 265
Cdd:cd05939 140 FGMRPEDVVYDCLPLYHSAGGIMGVGQALLHGSTVVIRKKFSASNFWDDCVKYNCTIVQYIGEICRYLLAQPPSEEEQKH 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 266 AMDYIIQGGSQplPSIQAAF-KQYGINIING-YGLTEAPLVLVNTPEN-----------SKRKPMSIGKAVMFVDARILD 332
Cdd:cd05939 220 NVRLAVGNGLR--PQIWEQFvRRFGIPQIGEfYGATEGNSSLVNIDNHvgacgfnsrilPSVYPIRLIKVDEDTGELIRD 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 333 DNGEEVPT--GEIGELA--IKAKNVT---PGYWNKPAETAKAF-----HG-RYLLTGDLAKMDNDGDIFIIDRKKELIIT 399
Cdd:cd05939 298 SDGLCIPCqpGEPGLLVgkIIQNDPLrrfDGYVNEGATNKKIArdvfkKGdSAFLSGDVLVMDELGYLYFKDRTGDTFRW 377
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 584959700 400 GGENVLPSEVENALaeHPLVDR--CVVVGYDHPKY-GESIAAAIILREDEpHYAEILNQHMRSRLAGYKVP 467
Cdd:cd05939 378 KGENVSTTEVEGIL--SNVLGLedVVVYGVEVPGVeGRAGMAAIVDPERK-VDLDRFSAVLAKSLPPYARP 445
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
30-441 |
2.15e-23 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 103.55 E-value: 2.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 30 YQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAAIVEDAQLKLLFYAEK- 108
Cdd:PRK05857 44 YRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLPIAAIERFCQITDPAAALVAPGs 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 109 --HLSSLTDIDQNL--LHMDIDVAQYDEIVNPDYHQPFQATPVEPQDLAALIYTSGTTGSPKGVMFSYESFVhngANLEL 184
Cdd:PRK05857 124 kmASSAVPEALHSIpvIAVDIAAVTRESEHSLDAASLAGNADQGSEDPLAMIFTSGTTGEPKAVLLANRTFF---AVPDI 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 185 TYKFNSNYITIVST-------PMFHVLGFNdTVLPVLMSGGTLILQRYfNGEELNDMIAQYHPTFIIMIPTMYYSTLRAS 257
Cdd:PRK05857 201 LQKEGLNWVTWVVGettysplPATHIGGLW-WILTCLMHGGLCVTGGE-NTTSLLEILTTNAVATTCLVPTLLSKLVSEL 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 258 NFNPENFRAMDYIIQGGSQPLPS----IQAAfkqyGINIINGYGLTEAPLVLVNTPEN----SKRKPMSIGKAVMFVDAR 329
Cdd:PRK05857 279 KSANATVPSLRLVGYGGSRAIAAdvrfIEAT----GVRTAQVYGLSETGCTALCLPTDdgsiVKIEAGAVGRPYPGVDVY 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 330 ILDDNG------EEVPTGEIGELAIKAKNVTPGYWNKPAETAKAFHGRYLLTGDLAKMDNDGDIFIIDRKKELIITGGEN 403
Cdd:PRK05857 355 LAATDGigptapGAGPSASFGTLWIKSPANMLGYWNNPERTAEVLIDGWVNTGDLLERREDGFFYIKGRSSEMIICGGVN 434
|
410 420 430
....*....|....*....|....*....|....*...
gi 584959700 404 VLPSEVENALAEHPLVDRCVVVGYDHPKYGESIAAAII 441
Cdd:PRK05857 435 IAPDEVDRIAEGVSGVREAACYEIPDEEFGALVGLAVV 472
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
144-440 |
3.45e-23 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 102.77 E-value: 3.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 144 ATPVE--PQDLAALIYTSGTTGSPKGVMFSYESFVHNGANLELTYKFNSNYITIVS-TPMFHVLGfndtvlpvlMSGGtL 220
Cdd:PRK07768 144 IDPVEtgEDDLALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEFDVETDVMVSwLPLFHDMG---------MVGF-L 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 221 ILQRYFNGEE--------LND------MIAQYHPTfIIMIPTMYYSTL-----RASNFNPENFRAMDYIIQGGSQPLPSI 281
Cdd:PRK07768 214 TVPMYFGAELvkvtpmdfLRDpllwaeLISKYRGT-MTAAPNFAYALLarrlrRQAKPGAFDLSSLRFALNGAEPIDPAD 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 282 QAAF----KQYGIN---IINGYGLTEA-----------PLVL--------------VNTPENSKRKPMSIGKAVMFVDAR 329
Cdd:PRK07768 293 VEDLldagARFGLRpeaILPAYGMAEAtlavsfspcgaGLVVdevdadllaalrraVPATKGNTRRLATLGPPLPGLEVR 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 330 ILDDNGEEVPTGEIGELAIKAKNVTPGYWN----KPAETAkafHGrYLLTGDLAKMDNDGDIFIIDRKKELIITGGENVL 405
Cdd:PRK07768 373 VVDEDGQVLPPRGVGVIELRGESVTPGYLTmdgfIPAQDA---DG-WLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIY 448
|
330 340 350
....*....|....*....|....*....|....*..
gi 584959700 406 PSEVENALAEHPLVDR-CVV-VGYDHPKYGESIAAAI 440
Cdd:PRK07768 449 PTDIERAAARVEGVRPgNAVaVRLDAGHSREGFAVAV 485
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
11-444 |
5.17e-23 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 102.51 E-value: 5.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 11 DFDDDKPAvidHAKQTSWTyqQLNARADNMAHYLtSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLnwrLNPK- 89
Cdd:PRK12476 57 DHSHSAAG---CAVELTWT--QLGVRLRAVGARL-QQVAGPGDRVAILAPQGIDYVAGFFAAIKAGTIAVPL---FAPEl 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 90 -----EIAAIVEDAQLKLLFYAEKHLSSLTDIDQNLLHMDID-VAQYDEIvnPD-YHQPFQATPVEPQDLAALIYTSGTT 162
Cdd:PRK12476 128 pghaeRLDTALRDAEPTVVLTTTAAAEAVEGFLRNLPRLRRPrVIAIDAI--PDsAGESFVPVELDTDDVSHLQYTSGST 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 163 GSPKGVMFSYESFVHNGANLELTYKFNSNYITIVS-TPMFHVLGFNDTVLPVLmSGGTLIL----------QRYFngEEL 231
Cdd:PRK12476 206 RPPVGVEITHRAVGTNLVQMILSIDLLDRNTHGVSwLPLYHDMGLSMIGFPAV-YGGHSTLmsptafvrrpQRWI--KAL 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 232 NDMiAQYHPTFIIMiPTMYYStLRASNFNPENFRAMD-----YIIqgGSQPLpSIQA------AFKQYGI---NIINGYG 297
Cdd:PRK12476 283 SEG-SRTGRVVTAA-PNFAYE-WAAQRGLPAEGDDIDlsnvvLII--GSEPV-SIDAvttfnkAFAPYGLprtAFKPSYG 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 298 LTEAPLVLVNTPENSK-------RKPMSIGKAVMfVD--------------------ARILDDN-GEEVPTGEIGELAIK 349
Cdd:PRK12476 357 IAEATLFVATIAPDAEpsvvyldREQLGAGRAVR-VAadapnavahvscgqvarsqwAVIVDPDtGAELPDGEVGEIWLH 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 350 AKNVTPGYWNKPAETAKAFH-------------------GRYLLTGDLAkMDNDGDIFIIDRKKELIITGGENVLPSEVE 410
Cdd:PRK12476 436 GDNIGRGYWGRPEETERTFGaklqsrlaegshadgaaddGTWLRTGDLG-VYLDGELYITGRIADLIVIDGRNHYPQDIE 514
|
490 500 510
....*....|....*....|....*....|....*
gi 584959700 411 NALAE-HPLVDRCVVVGYDHPkyGESIAAAIILRE 444
Cdd:PRK12476 515 ATVAEaSPMVRRGYVTAFTVP--AEDNERLVIVAE 547
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
146-492 |
9.60e-22 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 96.65 E-value: 9.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 146 PVEPqDLAALIYTSGTTGSPKGVMFSYESFVhngANLELTYKFNSNYIT-IVSTPMFHVLGFNDTVLPVLmsGGT----L 220
Cdd:PRK07824 32 PIDD-DVALVVATSGTTGTPKGAMLTAAALT---ASADATHDRLGGPGQwLLALPAHHIAGLQVLVRSVI--AGSepveL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 221 ILQRYFNGEELNDMIAQYHP--TFIIMIPTMYYSTLRASNfNPENFRAMDYI-IQGGSQPLPSIQAAfKQYGINIINGYG 297
Cdd:PRK07824 106 DVSAGFDPTALPRAVAELGGgrRYTSLVPMQLAKALDDPA-ATAALAELDAVlVGGGPAPAPVLDAA-AAAGINVVRTYG 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 298 LTEaplvlvntpenskrkpmSIGKAVMfvDARILDdnGEEVPTGEiGELAIKAKNVTPGYWNKPAETAKAFHGrYLLTGD 377
Cdd:PRK07824 184 MSE-----------------TSGGCVY--DGVPLD--GVRVRVED-GRIALGGPTLAKGYRNPVDPDPFAEPG-WFRTDD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 378 LAKMDnDGDIFIIDRKKELIITGGENVLPSEVENALAEHPLVDRCVVVGYDHPKYGESIAAAIilrEDEPHYAEILNQ-- 455
Cdd:PRK07824 241 LGALD-DGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAV---VGDGGPAPTLEAlr 316
|
330 340 350
....*....|....*....|....*....|....*...
gi 584959700 456 -HMRSRLAGYKVPRMYVPVTHMPLNSTQKPDKLAIRQM 492
Cdd:PRK07824 317 aHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALVRR 354
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
27-489 |
2.03e-21 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 98.70 E-value: 2.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 27 SWTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAAIVEDAQLKLLF-- 104
Cdd:PRK05691 3745 QWSYAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGLPAQRLQRIIELSRTPVLVcs 3824
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 105 -----YAEKHLSSLTDIDQNLLHMDIDVaQYDEIV--NPDYHQpfqatpvEPQDLAALIYTSGTTGSPKGVMFSYESFVH 177
Cdd:PRK05691 3825 aacreQARALLDELGCANRPRLLVWEEV-QAGEVAshNPGIYS-------GPDNLAYVIYTSGSTGLPKGVMVEQRGMLN 3896
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 178 NGAN----LEL----------TYKFNSNYITIVSTPMF--------------------HVLGFNDTVL---PVLMSGgtl 220
Cdd:PRK05691 3897 NQLSkvpyLALseadviaqtaSQSFDISVWQFLAAPLFgarveivpnaiahdpqgllaHVQAQGITVLesvPSLIQG--- 3973
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 221 ilqryfngeelndMIAQYHPT---FIIMIPTmyystlrasnfnpenframdyiiqGGSQPlPSIQAAFKQ-Y-GINIING 295
Cdd:PRK05691 3974 -------------MLAEDRQAldgLRWMLPT------------------------GEAMP-PELARQWLQrYpQIGLVNA 4015
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 296 YGLTEAP--LVLVNTPENSKRKP-MSIGKAVMFVDARILDDNGEEVPTGEIGELAIKAKNVTPGYWNKPAETAKAF---- 368
Cdd:PRK05691 4016 YGPAECSddVAFFRVDLASTRGSyLPIGSPTDNNRLYLLDEALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFvphp 4095
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 369 HG----RYLLTGDLAKMDNDGDIFIIDRKKELIITGGENVLPSEVENALAEHPLVdRCVVVGYDHPKYGESIAAAIILRE 444
Cdd:PRK05691 4096 FGapgeRLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEV-REAAVAVQEGVNGKHLVGYLVPHQ 4174
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 584959700 445 DEPHYAEILN---QHMRSRLAGYKVPRMYVPVTHMPLNSTQKPDKLAI 489
Cdd:PRK05691 4175 TVLAQGALLErikQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKAL 4222
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
30-492 |
2.04e-21 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 97.38 E-value: 2.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 30 YQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTG--AVFLPLNWRLNPKE-----IAAIVEDAQLKL 102
Cdd:PRK09192 52 YQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGlvPVPLPLPMGFGGREsyiaqLRGMLASAQPAA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 103 LFYAEKHLSSLTDIDQNL-LHMDIDVAQYDEIVNPDYHQPfqatPVEPQDLAALIYTSGTTGSPKGV-------MFSYES 174
Cdd:PRK09192 132 IITPDELLPWVNEATHGNpLLHVLSHAWFKALPEADVALP----RPTPDDIAYLQYSSGSTRFPRGViithralMANLRA 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 175 FVHNGANLELTYKfnsnyitIVS-TPMFHVLGFNDTVLPVLMSGGT--LILQRYFNGEELN--DMIAQ------YHPTFI 243
Cdd:PRK09192 208 ISHDGLKVRPGDR-------CVSwLPFYHDMGLVGFLLTPVATQLSvdYLPTRDFARRPLQwlDLISRnrgtisYSPPFG 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 244 IMIPTMYYSTLRASNFNPENFRAM----DYIiqgGSQPLPSIQAAFKQYGIN---IINGYGLTEAPLVLVNTPENS---- 312
Cdd:PRK09192 281 YELCARRVNSKDLAELDLSCWRVAgigaDMI---RPDVLHQFAEAFAPAGFDdkaFMPSYGLAEATLAVSFSPLGSgivv 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 313 ---KRKPMSIGKAVMFVDAR--------------------ILDDNGEEVPTGEIGELAIKAKNVTPGYWNKPaETAKAFH 369
Cdd:PRK09192 358 eevDRDRLEYQGKAVAPGAEtrrvrtfvncgkalpgheieIRNEAGMPLPERVVGHICVRGPSLMSGYFRDE-ESQDVLA 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 370 -GRYLLTGDLAKMdNDGDIFIIDRKKELIITGGENVLPSEVENALAEHPLV---DRCVVVGYDHPkyGESIAAAIILRED 445
Cdd:PRK09192 437 aDGWLDTGDLGYL-LDGYLYITGRAKDLIIINGRNIWPQDIEWIAEQEPELrsgDAAAFSIAQEN--GEKIVLLVQCRIS 513
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 584959700 446 EPHYAEILNQHMRSRL---AGYKVPRMYVPVTHMPLNSTQKPDKLAIRQM 492
Cdd:PRK09192 514 DEERRGQLIHALAALVrseFGVEAAVELVPPHSLPRTSSGKLSRAKAKKR 563
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
29-425 |
5.10e-21 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 97.55 E-value: 5.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 29 TYQQLNARADNMAHYLTSQGVKkGDVIGIFAPNDIAILDLLFACFKTGAVFLPL-----NWRLNPKEIAAIVEDAQLKLL 103
Cdd:PRK05691 42 SYRDLDLRARTIAAALQARASF-GDRAVLLFPSGPDYVAAFFGCLYAGVIAVPAyppesARRHHQERLLSIIADAEPRLL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 104 FYAEKHLSSLTDIDQ-------NLLHMD-IDVAQYDEivnpdyhqpFQATPVEPQDLAALIYTSGTTGSPKGVMFSYESF 175
Cdd:PRK05691 121 LTVADLRDSLLQMEElaaanapELLCVDtLDPALAEA---------WQEPALQPDDIAFLQYTSGSTALPKGVQVSHGNL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 176 VHNGANLELTYKFNSNYI-TIVS-TPMFHVLGFNDTVLPVLMSGGTLILQ--RYFNGEELN--DMIAQYH------PTFI 243
Cdd:PRK05691 192 VANEQLIRHGFGIDLNPDdVIVSwLPLYHDMGLIGGLLQPIFSGVPCVLMspAYFLERPLRwlEAISEYGgtisggPDFA 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 244 IMIPTMYYSTLRASNFNPENFRamdyIIQGGSQP-----LPSIQAAFKQYGI---NIINGYGLTEAPLVLV--------- 306
Cdd:PRK05691 272 YRLCSERVSESALERLDLSRWR----VAYSGSEPirqdsLERFAEKFAACGFdpdSFFASYGLAEATLFVSggrrgqgip 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 307 -----------NTPENSKRKP-MSIGK-----AVMFVDARilddNGEEVPTGEIGELAIKAKNVTPGYWNKPAETAKAF- 368
Cdd:PRK05691 348 aleldaealarNRAEPGTGSVlMSCGRsqpghAVLIVDPQ----SLEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTFv 423
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 369 --HGR-YLLTGDLAKMdNDGDIFIIDRKKELIITGGENVLPSEVENalaehpLVDRCVVV 425
Cdd:PRK05691 424 ehDGRtWLRTGDLGFL-RDGELFVTGRLKDMLIVRGHNLYPQDIEK------TVEREVEV 476
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
27-441 |
6.17e-21 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 96.32 E-value: 6.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 27 SW-TYQQLNARADNMAHYLTSQGVKKGDVIGIFAPN--DIAILDLlfACFKTGAVFLPLNWRLNPKEIAAIVEDAQLKLL 103
Cdd:PLN02736 77 KWmTYGEAGTARTAIGSGLVQHGIPKGACVGLYFINrpEWLIVDH--ACSAYSYVSVPLYDTLGPDAVKFIVNHAEVAAI 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 104 FYAEKHLSS----LTDI------------DQNL----LHMDIDVAQYDEIVNPDYHQPFQATPVEPQDLAALIYTSGTTG 163
Cdd:PLN02736 155 FCVPQTLNTllscLSEIpsvrlivvvggaDEPLpslpSGTGVEIVTYSKLLAQGRSSPQPFRPPKPEDVATICYTSGTTG 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 164 SPKGVMFSYESFVHNGANLELTYKFNSNYITIVSTPMFHVlgFNDTVLPVLMSGGTLIlqRYFNGE--ELNDMIAQYHPT 241
Cdd:PLN02736 235 TPKGVVLTHGNLIANVAGSSLSTKFYPSDVHISYLPLAHI--YERVNQIVMLHYGVAV--GFYQGDnlKLMDDLAALRPT 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 242 FIIMIPTMY-------YSTLRASNFNPENFRAMDY----------------------------------IIQGGSQPLPS 280
Cdd:PLN02736 311 IFCSVPRLYnriydgiTNAVKESGGLKERLFNAAYnakkqalengknpspmwdrlvfnkikaklggrvrFMSSGASPLSP 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 281 IQAAFKQ--YGINIINGYGLTEAPLVLVNTPEnSKRKPMSIGKAVMFVDARILD-------DNGEEVPTGEIgelAIKAK 351
Cdd:PLN02736 391 DVMEFLRicFGGRVLEGYGMTETSCVISGMDE-GDNLSGHVGSPNPACEVKLVDvpemnytSEDQPYPRGEI---CVRGP 466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 352 NVTPGYWNKPAETAKAFHGR-YLLTGDLAKMDNDGDIFIIDRKKELI-ITGGENVLPSEVENALAEHPLVDRCVVvgydh 429
Cdd:PLN02736 467 IIFKGYYKDEVQTREVIDEDgWLHTGDIGLWLPGGRLKIIDRKKNIFkLAQGEYIAPEKIENVYAKCKFVAQCFV----- 541
|
490
....*....|..
gi 584959700 430 pkYGESIAAAII 441
Cdd:PLN02736 542 --YGDSLNSSLV 551
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
146-492 |
6.78e-21 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 96.32 E-value: 6.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 146 PVEPQDLAALIYTSGTTGSPKGVMFSYESFVHNGANLELTYKFNSNYITIVSTPMFHVLGFNDTVLPVLMSGGTLILqry 225
Cdd:PRK08043 361 KQQPEDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFL--- 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 226 fngeelndmiaqY-HPTFIIMIPTMYY----------STL---RASNFNPENFRAMDYIIQGGSQPLPSI-QAAFKQYGI 290
Cdd:PRK08043 438 ------------YpSPLHYRIVPELVYdrnctvlfgtSTFlgnYARFANPYDFARLRYVVAGAEKLQESTkQLWQDKFGL 505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 291 NIINGYGLTE-APLVLVNTPENSkrKPMSIGKAVMFVDARILDDNGEEvptgEIGELAIKAKNVTPGYW--NKPAE---- 363
Cdd:PRK08043 506 RILEGYGVTEcAPVVSINVPMAA--KPGTVGRILPGMDARLLSVPGIE----QGGRLQLKGPNIMNGYLrvEKPGVlevp 579
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 364 TAKAFHGR----YLLTGDLAKMDNDGDIFIIDRKKELIITGGENVLPSEVEN-ALAEHPLVDRCVVVGYDHPKyGEsiaA 438
Cdd:PRK08043 580 TAENARGEmergWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQlALGVSPDKQHATAIKSDASK-GE---A 655
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 584959700 439 AIILREDEPHYAEILNQHMRSrlagYKVPRMYVP-----VTHMPLNSTQKPDKLAIRQM 492
Cdd:PRK08043 656 LVLFTTDSELTREKLQQYARE----HGVPELAVPrdiryLKQLPLLGSGKPDFVTLKSM 710
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
29-386 |
1.64e-20 |
|
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: 94.81 E-value: 1.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 29 TYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLN--WRLNPKEIAA---IVEDAQLKLL 103
Cdd:cd05921 27 TYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSpaYSLMSQDLAKlkhLFELLKPGLV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 104 FYA-----EKHLSSLTDIDQNLLHMDIDVAQYDEIVNPDyhqpFQATP-----------VEPQDLAALIYTSGTTGSPKG 167
Cdd:cd05921 107 FAQdaapfARALAAIFPLGTPLVVSRNAVAGRGAISFAE----LAATPptaavdaafaaVGPDTVAKFLFTSGSTGLPKA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 168 VMFSYESFVHNGANLELTYKFNSNYITIV--STPMFHVLGFNDTVLPVLMSGGTLILQRyfnGEELNDMIAQ-------Y 238
Cdd:cd05921 183 VINTQRMLCANQAMLEQTYPFFGEEPPVLvdWLPWNHTFGGNHNFNLVLYNGGTLYIDD---GKPMPGGFEEtlrnlreI 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 239 HPTFIIMIPTMYYS---------TLRASNFnpENFRAMDYIIQGGSQPL-PSIQA-AFKQYG--INIINGYGLTE-APLV 304
Cdd:cd05921 260 SPTVYFNVPAGWEMlvaalekdeALRRRFF--KRLKLMFYAGAGLSQDVwDRLQAlAVATVGerIPMMAGLGATEtAPTA 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 305 LVNTPENSKrkPMSIGKAVMFVDARIlddngeeVPTGEIGELAIKAKNVTPGYWNKPAETAKAF--HGRYLLtGDLAKMD 382
Cdd:cd05921 338 TFTHWPTER--SGLIGLPAPGTELKL-------VPSGGKYEVRVKGPNVTPGYWRQPELTAQAFdeEGFYCL-GDAAKLA 407
|
....
gi 584959700 383 NDGD 386
Cdd:cd05921 408 DPDD 411
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
9-437 |
1.68e-20 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 95.09 E-value: 1.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 9 RSDFDDDKPAvidhaKQTSWTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNP 88
Cdd:PLN02614 66 RREIVDGKPG-----KYVWQTYQEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGA 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 89 KEIAAIVEDAQLKLLFYAEKHLSSLTDIDQNLL-HMDIDVA--------------------QYDEIVNPDYHQPFQATPV 147
Cdd:PLN02614 141 GAVEFIISHSEVSIVFVEEKKISELFKTCPNSTeYMKTVVSfggvsreqkeeaetfglviyAWDEFLKLGEGKQYDLPIK 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 148 EPQDLAALIYTSGTTGSPKGVMFSYESFVH---------NGANLELTYKfnSNYITIVstPMFHV--------------- 203
Cdd:PLN02614 221 KKSDICTIMYTSGTTGDPKGVMISNESIVTliagvirllKSANAALTVK--DVYLSYL--PLAHIfdrvieecfiqhgaa 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 204 LGF--NDTVL---------PVLMSGGTLILQRYFNG--EELNDmiAQYHPTFIIMIPTMY--------YSTLRASNFNPE 262
Cdd:PLN02614 297 IGFwrGDVKLliedlgelkPTIFCAVPRVLDRVYSGlqKKLSD--GGFLKKFVFDSAFSYkfgnmkkgQSHVEASPLCDK 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 263 ------------NFRamdyIIQGGSQPLPSIQAAFKQY--GINIINGYGLTEAPLVLVNTPENSKRKPMSIGKAVMFVDA 328
Cdd:PLN02614 375 lvfnkvkqglggNVR----IILSGAAPLASHVESFLRVvaCCHVLQGYGLTESCAGTFVSLPDELDMLGTVGPPVPNVDI 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 329 RIlddngEEVPTGEI--------GELAIKAKNVTPGYWNKPAETAKAFHGRYLLTGDLAKMDNDGDIFIIDRKKELI-IT 399
Cdd:PLN02614 451 RL-----ESVPEMEYdalastprGEICIRGKTLFSGYYKREDLTKEVLIDGWLHTGDVGEWQPNGSMKIIDRKKNIFkLS 525
|
490 500 510
....*....|....*....|....*....|....*...
gi 584959700 400 GGENVLPSEVENALAEHPLVDRCVVVGYDHPKYGESIA 437
Cdd:PLN02614 526 QGEYVAVENIENIYGEVQAVDSVWVYGNSFESFLVAIA 563
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
29-410 |
1.95e-20 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 94.80 E-value: 1.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 29 TYQQLNARADNMAHYLtSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLnwrLNPKE------IAAIVEDAQLKL 102
Cdd:PRK07769 57 TWSQFGARNRAVGARL-QQVTKPGDRVAILAPQNLDYLIAFFGALYAGRIAVPL---FDPAEpghvgrLHAVLDDCTPSA 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 103 LFYAEKHLSSLTDIDQNLLHMD----IDVAQYDEIVNPDYHQPfqatPVEPQDLAALIYTSGTTGSPKGVMFSYESFVHN 178
Cdd:PRK07769 133 ILTTTDSAEGVRKFFRARPAKErprvIAVDAVPDEVGATWVPP----EANEDTIAYLQYTSGSTRIPAGVQITHLNLPTN 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 179 GANLELTYKFNSNYITIVSTPMFHVLGFNDTVLPVLMSGG-TLILQRYF---NGEELNDMIAQYHPTF--IIMIPTMYYS 252
Cdd:PRK07769 209 VLQVIDALEGQEGDRGVSWLPFFHDMGLITVLLPALLGHYiTFMSPAAFvrrPGRWIRELARKPGGTGgtFSAAPNFAFE 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 253 TLRASNFNPENFRAMDYI----IQGGSQPLpSIQA------AFKQYGIN---IINGYGLTEAPLVLVNTPENSK------ 313
Cdd:PRK07769 289 HAAARGLPKDGEPPLDLSnvkgLLNGSEPV-SPASmrkfneAFAPYGLPptaIKPSYGMAEATLFVSTTPMDEEptviyv 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 314 -RKPMSIGKAVMfVD--------------------ARILD-DNGEEVPTGEIGELAIKAKNVTPGYWNKPAETAKAFH-- 369
Cdd:PRK07769 368 dRDELNAGRFVE-VPadapnavaqvsagkvgvsewAVIVDpETASELPDGQIGEIWLHGNNIGTGYWGKPEETAATFQni 446
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 584959700 370 ----------------GRYLLTGDLAKMdNDGDIFIIDRKKELIITGGENVLPSEVE 410
Cdd:PRK07769 447 lksrlseshaegapddALWVRTGDYGVY-FDGELYITGRVKDLVIIDGRNHYPQDLE 502
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
147-432 |
3.27e-20 |
|
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: 93.96 E-value: 3.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 147 VEPQDLAALIYTSGTTGSPKGVMFSYESFVHNGANLELTYKFNSNYI---TIVS-TPMFHVLG-FNDTVLPVLMSGGTLI 221
Cdd:cd05933 147 QKPNQCCTLIYTSGTTGMPKGVMLSHDNITWTAKAASQHMDLRPATVgqeSVVSyLPLSHIAAqILDIWLPIKVGGQVYF 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 222 LQRYFNGEELNDMIAQYHPTFIIMIPTMY--------------------------------YSTLRASNFN-PENFRAMD 268
Cdd:cd05933 227 AQPDALKGTLVKTLREVRPTAFMGVPRVWekiqekmkavgaksgtlkrkiaswakgvgletNLKLMGGESPsPLFYRLAK 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 269 YII----------------QGGSQPLPS-IQAAFKQYGINIINGYGLTE-APLVLVNTPENSKRkpMSIGKAVMFVDARI 330
Cdd:cd05933 307 KLVfkkvrkalgldrcqkfFTGAAPISReTLEFFLSLNIPIMELYGMSEtSGPHTISNPQAYRL--LSCGKALPGCKTKI 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 331 L--DDNGeevptgeIGELAIKAKNVTPGYWNKPAETAKAF--HGrYLLTGDLAKMDNDGDIFIIDRKKELIIT-GGENVL 405
Cdd:cd05933 385 HnpDADG-------IGEICFWGRHVFMGYLNMEDKTEEAIdeDG-WLHSGDLGKLDEDGFLYITGRIKELIITaGGENVP 456
|
330 340
....*....|....*....|....*...
gi 584959700 406 PSEVENAL-AEHPLVDRCVVVGyDHPKY 432
Cdd:cd05933 457 PVPIEDAVkKELPIISNAMLIG-DKRKF 483
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
27-467 |
6.04e-20 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 93.04 E-value: 6.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 27 SWTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAAIVEDAQ------- 99
Cdd:PLN02654 120 SLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQRIVDCKpkvvitc 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 100 ------LKLLFYAEKHLSSLTDIDQNLLHMDI---------------------DVAQYDeiVNPDYHQPFQATPVEPQDL 152
Cdd:PLN02654 200 navkrgPKTINLKDIVDAALDESAKNGVSVGIcltyenqlamkredtkwqegrDVWWQD--VVPNYPTKCEVEWVDAEDP 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 153 AALIYTSGTTGSPKGVMFSYESF-VHNGANLELTYKFNSNYITIVSTPMFHVLGFNDTVLPVLMSGGTLIL----QRYFN 227
Cdd:PLN02654 278 LFLLYTSGSTGKPKGVLHTTGGYmVYTATTFKYAFDYKPTDVYWCTADCGWITGHSYVTYGPMLNGATVLVfegaPNYPD 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 228 GEELNDMIAQYHPTFIIMIPTMYYSTLR-----ASNFNPENFRAMdyiiqgGSQPLPSIQAAFKQYgINIIngyGLTEAP 302
Cdd:PLN02654 358 SGRCWDIVDKYKVTIFYTAPTLVRSLMRdgdeyVTRHSRKSLRVL------GSVGEPINPSAWRWF-FNVV---GDSRCP 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 303 L------------VLVNTPENSKRKPMSIGKAVMFVDARILDDNGEEVPTGEIGELAIKAKnvTPGYW------NKPAET 364
Cdd:PLN02654 428 IsdtwwqtetggfMITPLPGAWPQKPGSATFPFFGVQPVIVDEKGKEIEGECSGYLCVKKS--WPGAFrtlygdHERYET 505
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 365 A--KAFHGrYLLTGDLAKMDNDGDIFIIDRKKELIITGGENVLPSEVENALAEHPLVDRCVVVGYDHPKYGESIAAAIIL 442
Cdd:PLN02654 506 TyfKPFAG-YYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEVKGQGIYAFVTL 584
|
490 500
....*....|....*....|....*...
gi 584959700 443 REDEPHYAEI---LNQHMRSRLAGYKVP 467
Cdd:PLN02654 585 VEGVPYSEELrksLILTVRNQIGAFAAP 612
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
27-468 |
4.18e-19 |
|
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: 90.04 E-value: 4.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 27 SWTYQQLNARADNMAHYLTSQ-GVKKGDVIGIFAPNDIAILDLLFACFKTGAV--FLPLNWRLNP--------------- 88
Cdd:cd05938 5 TYTYRDVDRRSNQAARALLAHaGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPvaFLNTNIRSKSllhcfrccgakvlvv 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 89 -KEIAAIVEDAQLKL------LFYAEKHlSSLTDIDQNLLHMDidvAQYDEIVNPDYHQPfqatpVEPQDLAALIYTSGT 161
Cdd:cd05938 85 aPELQEAVEEVLPALradgvsVWYLSHT-SNTEGVISLLDKVD---AASDEPVPASLRAH-----VTIKSPALYIYTSGT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 162 TGSPKGVMFSYESFVHNGANLELTyKFNSNYITIVSTPMFHVLGFNDTVLPVLMSGGTLILQRYFNGEELNDMIAQYHPT 241
Cdd:cd05938 156 TGLPKAARISHLRVLQCSGFLSLC-GVTADDVIYITLPLYHSSGFLLGIGGCIELGATCVLKPKFSASQFWDDCRKHNVT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 242 FIIMI-PTMYYSTlrasNFNP-ENFRAMDYIIQGGSQPLPSIQAAF-KQYG-INIINGYGLTEAPLVLVNTPenskRKPM 317
Cdd:cd05938 235 VIQYIgELLRYLC----NQPQsPNDRDHKVRLAIGNGLRADVWREFlRRFGpIRIREFYGSTEGNIGFFNYT----GKIG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 318 SIGKAVMF---------------VDARILDDNGE--EVPTGEIGELAIKAKNVTP--GYWNKPAETAK-----AFH--GR 371
Cdd:cd05938 307 AVGRVSYLykllfpfelikfdveKEEPVRDAQGFciPVAKGEPGLLVAKITQQSPflGYAGDKEQTEKkllrdVFKkgDV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 372 YLLTGDLAKMDNDGDIFIIDRKKELIITGGENVLPSEVENALAEHPLVDRCVVVGYDHPKY-GESIAAAIILREDEPHYA 450
Cdd:cd05938 387 YFNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVYGVTVPGHeGRIGMAAVKLKPGHEFDG 466
|
490
....*....|....*...
gi 584959700 451 EILNQHMRSRLAGYKVPR 468
Cdd:cd05938 467 KKLYQHVREYLPAYARPR 484
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
28-430 |
4.94e-19 |
|
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: 90.17 E-value: 4.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 28 WTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAAIVEDAQLKLLFYA- 106
Cdd:cd17641 12 FTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIAEd 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 107 EKHLSSLTDIDQNLLHMDiDVAQYDEIVNPDYHQP---FQATPVE---------------------PQDLAALIYTSGTT 162
Cdd:cd17641 92 EEQVDKLLEIADRIPSVR-YVIYCDPRGMRKYDDPrliSFEDVVAlgraldrrdpglyerevaagkGEDVAVLCTTSGTT 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 163 GSPKGVMFSYESFVHNGANLeLTYKFNS---NYITIVstPMFHVLGFNDTVLPVLMSGGTLilqrYFNGEE---LNDMiA 236
Cdd:cd17641 171 GKPKLAMLSHGNFLGHCAAY-LAADPLGpgdEYVSVL--PLPWIGEQMYSVGQALVCGFIV----NFPEEPetmMEDL-R 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 237 QYHPTFIIMIPTMYYSTLR--------ASNFNPENF--------RAMDYIIQGGSQPL---------------------- 278
Cdd:cd17641 243 EIGPTFVLLPPRVWEGIAAdvrarmmdATPFKRFMFelgmklglRALDRGKRGRPVSLwlrlaswladallfrplrdrlg 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 279 ---------------PSIQAAFKQYGINIINGYGLTEAPLVLVNTPENsKRKPMSIGKAVMFVDARIlddngeevptGEI 343
Cdd:cd17641 323 fsrlrsaatggaalgPDTFRFFHAIGVPLKQLYGQTELAGAYTVHRDG-DVDPDTVGVPFPGTEVRI----------DEV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 344 GELAIKAKNVTPGYWNKPAETAKAFHGR-YLLTGDLAKMDNDGDIFIIDRKKELIITG-GENVLPSEVENALAEHPLVDR 421
Cdd:cd17641 392 GEILVRSPGVFVGYYKNPEATAEDFDEDgWLHTGDAGYFKENGHLVVIDRAKDVGTTSdGTRFSPQFIENKLKFSPYIAE 471
|
....*....
gi 584959700 422 CVVVGYDHP 430
Cdd:cd17641 472 AVVLGAGRP 480
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
11-415 |
1.53e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 88.46 E-value: 1.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 11 DFDDDKPAVIDhakqtSWTYQQLNARADNMAHYLTSQGVKkGDVIGIFAPND----IAILDLLFACFKtgAVFLPL-NWR 85
Cdd:PRK05850 24 DYEQDPAGVAE-----TLTWSQLYRRTLNVAEELRRHGST-GDRAVILAPQGleyiVAFLGALQAGLI--AVPLSVpQGG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 86 LNPKEIAAIVEDAQLKLLFYAekhlSSLTDidqnllhmdiDVAQYDE---------IV-----NPDYHQPFQATPVEPQD 151
Cdd:PRK05850 96 AHDERVSAVLRDTSPSVVLTT----SAVVD----------DVTEYVApqpgqsappVIevdllDLDSPRGSDARPRDLPS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 152 LAALIYTSGTTGSPKGVMFSYESFVhngANLEltyKFNSNYI-----------TIVS-TPMFHVLGFndtVLPVLMSggt 219
Cdd:PRK05850 162 TAYLQYTSGSTRTPAGVMVSHRNVI---ANFE---QLMSDYFgdtggvpppdtTVVSwLPFYHDMGL---VLGVCAP--- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 220 lilqryfngeelndMIAQYH-----PTFIIMIPTMYYSTLrASNFNP----ENF-------RAMD------------YII 271
Cdd:PRK05850 230 --------------ILGGCPavltsPVAFLQRPARWMQLL-ASNPHAfsaaPNFafelavrKTSDddmagldlggvlGII 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 272 QGGSQplpsIQAA--------FKQYGIN---IINGYGLTEApLVLVNTPE----------------NSKRKPMSIGKAVM 324
Cdd:PRK05850 295 SGSER----VHPAtlkrfadrFAPFNLRetaIRPSYGLAEA-TVYVATREpgqppesvrfdyeklsAGHAKRCETGGGTP 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 325 FVD--------ARILD-DNGEEVPTGEIGELAIKAKNVTPGYWNKPAETAKAFHGR------------YLLTGDLAKMDn 383
Cdd:PRK05850 370 LVSygsprsptVRIVDpDTCIECPAGTVGEIWVHGDNVAAGYWQKPEETERTFGATlvdpspgtpegpWLRTGDLGFIS- 448
|
490 500 510
....*....|....*....|....*....|..
gi 584959700 384 DGDIFIIDRKKELIITGGENVLPSEVENALAE 415
Cdd:PRK05850 449 EGELFIVGRIKDLLIVDGRNHYPDDIEATIQE 480
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
28-459 |
9.69e-18 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 86.41 E-value: 9.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 28 W-TYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAAIVEDAQLKLLFYA 106
Cdd:PLN02430 76 WkTYKEVYEEVLQIGSALRASGAEPGSRVGIYGSNCPQWIVAMEACAAHSLICVPLYDTLGPGAVDYIVDHAEIDFVFVQ 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 107 EKHLSSLTDID---------------------QNLLHMDIDVAQYDEIVNPDYHQPFQATPVEPQDLAALIYTSGTTGSP 165
Cdd:PLN02430 156 DKKIKELLEPDcksakrlkaivsftsvteeesDKASQIGVKTYSWIDFLHMGKENPSETNPPKPLDICTIMYTSGTSGDP 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 166 KGVMFSYES---FVhNGANL---ELTYKFNSNYITIVSTPMFHVLgfNDTVLPVLMSGGTLIlqRYFNGE--ELNDMIAQ 237
Cdd:PLN02430 236 KGVVLTHEAvatFV-RGVDLfmeQFEDKMTHDDVYLSFLPLAHIL--DRMIEEYFFRKGASV--GYYHGDlnALRDDLME 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 238 YHPTFIIMIPTMY------------------------------------YSTLRASNF-NPENFRAMD--------YIIQ 272
Cdd:PLN02430 311 LKPTLLAGVPRVFerihegiqkalqelnprrrlifnalykyklawmnrgYSHKKASPMaDFLAFRKVKaklggrlrLLIS 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 273 GGSQPLPSIQ-------AAFkqyginIINGYGLTEA-PLVLVNTPENskrkpMS----IGKAVMFVDARIlddngEEVP- 339
Cdd:PLN02430 391 GGAPLSTEIEeflrvtsCAF------VVQGYGLTETlGPTTLGFPDE-----MCmlgtVGAPAVYNELRL-----EEVPe 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 340 -------TGEIGELAIKAKNVTPGYWNKPAETAKAFHGRYLLTGDLAKMDNDGDIFIIDRKKELI-ITGGENVLPSEVEN 411
Cdd:PLN02430 455 mgydplgEPPRGEICVRGKCLFSGYYKNPELTEEVMKDGWFHTGDIGEILPNGVLKIIDRKKNLIkLSQGEYVALEYLEN 534
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 584959700 412 ALAEHPLVDRCVVvgydhpkYGES----IAAAIILREDEPHYAEILNQHMRS 459
Cdd:PLN02430 535 VYGQNPIVEDIWV-------YGDSfksmLVAVVVPNEENTNKWAKDNGFTGS 579
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
29-380 |
8.11e-17 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 83.17 E-value: 8.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 29 TYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPL--NWRLNP------KEIAAIVED--- 97
Cdd:PRK12582 82 TYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAGVPAAPVspAYSLMShdhaklKHLFDLVKPrvv 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 98 -AQLKLLFyaEKHLSSLTDIDQNLLHMD-----IDVAQYDEIVnpdyhqpfqATPVE-----------PQDLAALIYTSG 160
Cdd:PRK12582 162 fAQSGAPF--ARALAALDLLDVTVVHVTgpgegIASIAFADLA---------ATPPTaavaaaiaaitPDTVAKYLFTSG 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 161 TTGSPKGVMFSYESFVHNGANLELTYKFNSNYITIVST---PMFHVLGFNDTVLPVLMSGGTLILQryfNGEELNDMIAQ 237
Cdd:PRK12582 231 STGMPKAVINTQRMMCANIAMQEQLRPREPDPPPPVSLdwmPWNHTMGGNANFNGLLWGGGTLYID---DGKPLPGMFEE 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 238 YHPTFIIMIPTMYYST----------------LRASNFnpENFRAMDYiiqGGSQpLPS-----IQA-AFKQYG--INII 293
Cdd:PRK12582 308 TIRNLREISPTVYGNVpagyamlaeamekddaLRRSFF--KNLRLMAY---GGAT-LSDdlyerMQAlAVRTTGhrIPFY 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 294 NGYGLTEAPLVLVNTPENSKRkPMSIGKAVMFVDARIlddngeeVPTGEIGELAIKAKNVTPGYWNKPAETAKAF--HGR 371
Cdd:PRK12582 382 TGYGATETAPTTTGTHWDTER-VGLIGLPLPGVELKL-------APVGDKYEVRVKGPNVTPGYHKDPELTAAAFdeEGF 453
|
....*....
gi 584959700 372 YLLtGDLAK 380
Cdd:PRK12582 454 YRL-GDAAR 461
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
408-483 |
1.20e-16 |
|
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.
Pssm-ID: 463804 [Multi-domain] Cd Length: 76 Bit Score: 74.50 E-value: 1.20e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 584959700 408 EVENALAEHPLVDRCVVVGYDHPKYGESIAAAIILREDEPHYAEILNQHMRSRLAGYKVPRMYVPVTHMPLNSTQK 483
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
22-420 |
2.41e-16 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 82.09 E-value: 2.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 22 HAKQTSW-TYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFL---------PLNWRLNPKEI 91
Cdd:PLN02387 100 HLGEYEWiTYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVtiyaslgeeALCHSLNETEV 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 92 AAIVEDA-QLKLLFYAEKHLSSL----------TDIDQNLLHM-DIDVAQYDEIVNPDYHQPFQATPVEPQDLAALIYTS 159
Cdd:PLN02387 180 TTVICDSkQLKKLIDISSQLETVkrviymddegVDSDSSLSGSsNWTVSSFSEVEKLGKENPVDPDLPSPNDIAVIMYTS 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 160 GTTGSPKGVMFSYESFVHNGAN-LELTYKFNSNYITIVSTPMFHVL---------------GF------NDT-------- 209
Cdd:PLN02387 260 GSTGLPKGVMMTHGNIVATVAGvMTVVPKLGKNDVYLAYLPLAHILelaaesvmaavgaaiGYgspltlTDTsnkikkgt 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 210 -----VL-PVLMSGGTLILQRYFNG-----EELNDMIAQyhptfiiMIPTMYYSTLRASN-------------FNPENFR 265
Cdd:PLN02387 340 kgdasALkPTLMTAVPAILDRVRDGvrkkvDAKGGLAKK-------LFDIAYKRRLAAIEgswfgawglekllWDALVFK 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 266 AMDYIIQG-------GSQPLPSIQAAFKQ--YGINIINGYGLTE-------------------APLV-----LVNTPENS 312
Cdd:PLN02387 413 KIRAVLGGrirfmlsGGAPLSGDTQRFINicLGAPIGQGYGLTEtcagatfsewddtsvgrvgPPLPccyvkLVSWEEGG 492
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 313 KR---KPMsigkavmfvdarilddngeevPTGEIgelAIKAKNVTPGYWNKPAETAKAFH-----GRYLLTGDLAKMDND 384
Cdd:PLN02387 493 YLisdKPM---------------------PRGEI---VIGGPSVTLGYFKNQEKTDEVYKvdergMRWFYTGDIGQFHPD 548
|
490 500 510
....*....|....*....|....*....|....*..
gi 584959700 385 GDIFIIDRKKELI-ITGGENVLPSEVENALAEHPLVD 420
Cdd:PLN02387 549 GCLEIIDRKKDIVkLQHGEYVSLGKVEAALSVSPYVD 585
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
19-486 |
3.43e-16 |
|
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Pssm-ID: 341302 [Multi-domain] Cd Length: 520 Bit Score: 81.02 E-value: 3.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 19 VIDHAKQTSWTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAAIVEDA 98
Cdd:cd17647 12 SLNSSKTRSFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQNIYLGVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 99 QLKLLfyaekhlssltdidqnllhmdIDVAQYDEIVNPDyhqpfqATPvepqdlaALIYTSGTTGSPKGVMfsyesfvhn 178
Cdd:cd17647 92 KPRGL---------------------IVIRAAGVVVGPD------SNP-------TLSFTSGSEGIPKGVL--------- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 179 GANLELTYKFN----------SNYITIVSTpMFHVLGFNDTVLPVLMSGGTLILQRYFNG--EELNDMIAQYHPTFIIMI 246
Cdd:cd17647 129 GRHFSLAYYFPwmakrfnlseNDKFTMLSG-IAHDPIQRDMFTPLFLGAQLLVPTQDDIGtpGRLAEWMAKYGATVTHLT 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 247 PtmyystlrasnfnpenfrAMDYIIQGG-SQPLPSIQAAFKQYGI----------------NIINGYGLTEA-------- 301
Cdd:cd17647 208 P------------------AMGQLLTAQaTTPFPKLHHAFFVGDIltkrdclrlqtlaenvRIVNMYGTTETqravsyfe 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 302 -------PLVLvntpeNSKRKPMSIGKAVMFVDARILD--DNGEEVPTGEIGELAIKAKNVTPGYWNKPAETAKAF---- 368
Cdd:cd17647 270 vpsrssdPTFL-----KNLKDVMPAGRGMLNVQLLVVNrnDRTQICGIGEVGEIYVRAGGLAEGYRGLPELNKEKFvnnw 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 369 -------------------------HGRYLLTGDLAKMDNDGDIFIIDRKKELIITGGENVLPSEVENALAEHPLV---- 419
Cdd:cd17647 345 fvepdhwnyldkdnnepwrqfwlgpRDRLYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVreni 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 420 --------DRCVVVGYDHPKyGESIAAAIILREDEPH-------------YAEILN---QHMRSRLAGYKVPRMYVPVTH 475
Cdd:cd17647 425 tlvrrdkdEEPTLVSYIVPR-FDKPDDESFAQEDVPKevstdpivkgligYRKLIKdirEFLKKRLASYAIPSLIVVLDK 503
|
570
....*....|.
gi 584959700 476 MPLNSTQKPDK 486
Cdd:cd17647 504 LPLNPNGKVDK 514
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
151-430 |
1.15e-15 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 80.02 E-value: 1.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 151 DLAALIYTSGTTGSPKGVMFSYESFVhNGAN------LELTYKFNSNYITIVSTPMFHVLGFndTVLPVLMSGGTLILqr 224
Cdd:PTZ00216 265 DLALIMYTSGTTGDPKGVMHTHGSLT-AGILaledrlNDLIGPPEEDETYCSYLPLAHIMEF--GVTNIFLARGALIG-- 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 225 YFNGEELNDMIA-------QYHPTFIIMIP----TM----------------------YYSTLRASN------------F 259
Cdd:PTZ00216 340 FGSPRTLTDTFArphgdltEFRPVFLIGVPrifdTIkkaveaklppvgslkrrvfdhaYQSRLRALKegkdtpywnekvF 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 260 NPenFRAM----DYIIQGGSQPLPSIQAAFkqygIN-----IINGYGLTEAplVLVNTPENS-KRKPMSIGKAVMFVDAR 329
Cdd:PTZ00216 420 SA--PRAVlggrVRAMLSGGGPLSAATQEF----VNvvfgmVIQGWGLTET--VCCGGIQRTgDLEPNAVGQLLKGVEMK 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 330 ILD-------DNGEevPTGEI---GELAIKaknvtpGYWNKPAETAKA------FHgryllTGDLAKMDNDGDIFIIDRK 393
Cdd:PTZ00216 492 LLDteeykhtDTPE--PRGEIllrGPFLFK------GYYKQEELTREVldedgwFH-----TGDVGSIAANGTLRIIGRV 558
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 584959700 394 KELIitggENVL----PSEVENAL-AEHPLVDR---CVVVgydHP 430
Cdd:PTZ00216 559 KALA----KNCLgeyiALEALEALyGQNELVVPngvCVLV---HP 596
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
29-426 |
2.68e-15 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 78.73 E-value: 2.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 29 TYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAAIVEDAQLKLLFYAEK 108
Cdd:PLN02861 79 TYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVSIAFVQES 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 109 HLSS-LTDIDQNLLHM-------DIDVAQYDE----------------IVNPDYHQPfqatPVEPQDLAALIYTSGTTGS 164
Cdd:PLN02861 159 KISSiLSCLPKCSSNLktivsfgDVSSEQKEEaeelgvscfsweefslMGSLDCELP----PKQKTDICTIMYTSGTTGE 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 165 PKGVMFSYESFVHNGAN----LELTYKFNSNYITIVS-TPMFHVlgFNDTVLPVLMSGGTLIlqRYFNGE--ELNDMIAQ 237
Cdd:PLN02861 235 PKGVILTNRAIIAEVLStdhlLKVTDRVATEEDSYFSyLPLAHV--YDQVIETYCISKGASI--GFWQGDirYLMEDVQA 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 238 YHPTFIIMIPTMY---YS----------TLR------ASNFNPENFR---------------AMDYIIQG---------- 273
Cdd:PLN02861 311 LKPTIFCGVPRVYdriYTgimqkissggMLRkklfdfAYNYKLGNLRkglkqeeasprldrlVFDKIKEGlggrvrllls 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 274 GSQPLPSIQAAFKQY--GINIINGYGLTEAPLVLVNTPENSKRKPMSIGKAVMFVDARILD------DNGEEVPTGEIge 345
Cdd:PLN02861 391 GAAPLPRHVEEFLRVtsCSVLSQGYGLTESCGGCFTSIANVFSMVGTVGVPMTTIEARLESvpemgyDALSDVPRGEI-- 468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 346 lAIKAKNVTPGYWNKPAETAKAFHGRYLLTGDLAKMDNDGDIFIIDRKKELI-ITGGENVLPSEVENALAEHPLVDRCVV 424
Cdd:PLN02861 469 -CLRGNTLFSGYHKRQDLTEEVLIDGWFHTGDIGEWQPNGAMKIIDRKKNIFkLSQGEYVAVENLENTYSRCPLIASIWV 547
|
..
gi 584959700 425 VG 426
Cdd:PLN02861 548 YG 549
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
130-495 |
1.01e-14 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 76.70 E-value: 1.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 130 YDEI--VNPDYHQPF-QATPVEPQDLAALIYTSGTTGSPKGVMFSyesfvhNGANLeLTYKFNSNYITIVSTPM------ 200
Cdd:PTZ00237 231 YDEIkkIKENNQSPFyEYVPVESSHPLYILYTSGTTGNSKAVVRS------NGPHL-VGLKYYWRSIIEKDIPTvvfshs 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 201 ------FH-----VLGFNDTVLpvlMSGGTLILQRYFNGEELNDMIAQYHPTFIIMIPTMYY-------STLRASNFNPE 262
Cdd:PTZ00237 304 sigwvsFHgflygSLSLGNTFV---MFEGGIIKNKHIEDDLWNTIEKHKVTHTLTLPKTIRYliktdpeATIIRSKYDLS 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 263 NFRAmdyIIQGGSQPLPSIQAAFKQ-YGINIINGYGLTEAPLVLVNTPENSKRKPMSIGKAVMFVDARILDDNGEEVPTG 341
Cdd:PTZ00237 381 NLKE---IWCGGEVIEESIPEYIENkLKIKSSRGYGQTEIGITYLYCYGHINIPYNATGVPSIFIKPSILSEDGKELNVN 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 342 EIGELAIKAKnVTPGY---WNKPAETAKAFHGR---YLLTGDLAKMDNDGDIFIIDRKKELIITGGENVLPSEVENALAE 415
Cdd:PTZ00237 458 EIGEVAFKLP-MPPSFattFYKNDEKFKQLFSKfpgYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILK 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 416 HPLVDRCVVVGYDHPKYGESIAAAIILREDEPHYA-----------EILNQHMRSrlagYKVPRMYVPVTHMPLNSTQKP 484
Cdd:PTZ00237 537 HPLVLECCSIGIYDPDCYNVPIGLLVLKQDQSNQSidlnklkneinNIITQDIES----LAVLRKIIIVNQLPKTKTGKI 612
|
410
....*....|.
gi 584959700 485 DKLAIRQMMND 495
Cdd:PTZ00237 613 PRQIISKFLND 623
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
16-489 |
2.54e-14 |
|
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.
Pssm-ID: 274582 [Multi-domain] Cd Length: 1389 Bit Score: 75.87 E-value: 2.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 16 KPAVIDHAKQTSWTYQQLNaRADN-MAHYLTSQGVKKGDVIGIFAPNDIailDLLFAC---FKTGAVFLPLN-----WRL 86
Cdd:TIGR03443 259 PSFLDPSSKTRSFTYKQIN-EASNiLAHYLLKTGIKRGDVVMIYAYRGV---DLVVAVmgvLKAGATFSVIDpayppARQ 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 87 N-------PKEIAAIVEDAQLKLLF--YAEKHLSSLTDIDQNLLHMDIDV------AQYDEIVNPDyhQPFQATP----V 147
Cdd:TIGR03443 335 TiylsvakPRALIVIEKAGTLDQLVrdYIDKELELRTEIPALALQDDGSLvggsleGGETDVLAPY--QALKDTPtgvvV 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 148 EPQDLAALIYTSGTTGSPKGVMfsyesfvhnGANLELTYKFN----------SNYITIVS------------TPMFhvLG 205
Cdd:TIGR03443 413 GPDSNPTLSFTSGSEGIPKGVL---------GRHFSLAYYFPwmakrfglseNDKFTMLSgiahdpiqrdmfTPLF--LG 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 206 FNDTVlPVLMSGGTlilqryfnGEELNDMIAQYHPTFIIMIPtmyystlrasnfnpenfrAMDYIIQGG-SQPLPSIQAA 284
Cdd:TIGR03443 482 AQLLV-PTADDIGT--------PGRLAEWMAKYGATVTHLTP------------------AMGQLLSAQaTTPIPSLHHA 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 285 F-------KQ---------YGINIINGYGLTE---APLVLVNTPENSKRKPMSIGKAVM-----FVDARIL----DDNGE 336
Cdd:TIGR03443 535 FfvgdiltKRdclrlqtlaENVCIVNMYGTTEtqrAVSYFEIPSRSSDSTFLKNLKDVMpagkgMKNVQLLvvnrNDRTQ 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 337 EVPTGEIGELAIKAKNVTPGYWNKPAETAKAF---------HGRYLL--------------------TGDLAKMDNDGDI 387
Cdd:TIGR03443 615 TCGVGEVGEIYVRAGGLAEGYLGLPELNAEKFvnnwfvdpsHWIDLDkennkperefwlgprdrlyrTGDLGRYLPDGNV 694
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 388 FIIDRKKELIITGGENVLPSEVENALAEHPLVDRCV-----------------VVGYDHPKYGESIAAAIILREDEP--- 447
Cdd:TIGR03443 695 ECCGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVtlvrrdkdeeptlvsyiVPQDKSDELEEFKSEVDDEESSDPvvk 774
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 584959700 448 ------HYAEILNQHMRSRLAGYKVPRMYVPVTHMPLNSTQKPDKLAI 489
Cdd:TIGR03443 775 glikyrKLIKDIREYLKKKLPSYAIPTVIVPLKKLPLNPNGKVDKPAL 822
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
157-483 |
5.11e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 73.92 E-value: 5.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 157 YTSGTTGSPKGVMFSYESFVHNGANLELTYKFNSNYITIVSTPMFHVLGFNDTVLPVLMSGGTLILQRYFNGEELNDMIA 236
Cdd:PRK08308 108 YSSGTTGEPKLIRRSWTEIDREIEAYNEALNCEQDETPIVACPVTHSYGLICGVLAALTRGSKPVIITNKNPKFALNILR 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 237 QYHPTFIIMIPTMYYsTLraSNFNPENFRaMDYIIQGGSqPLP-----SIQAAFKQyginIINGYGLTEAPLVLVNTPen 311
Cdd:PRK08308 188 NTPQHILYAVPLMLH-IL--GRLLPGTFQ-FHAVMTSGT-PLPeawfyKLRERTTY----MMQQYGCSEAGCVSICPD-- 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 312 sKRKPMSIGKAVMFVDARIldDNGEEVPtgeiGELAIKAKnvtpgywnkpaetakafhGRYLLTGDLAKMDNDGDIFIID 391
Cdd:PRK08308 257 -MKSHLDLGNPLPHVSVSA--GSDENAP----EEIVVKMG------------------DKEIFTKDLGYKSERGTLHFMG 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 392 RKKELIITGGENVLPSEVENALAEHPLVDRCVVVGYDHPKYGESIAAAIIlrEDEPHYAEILNQHMRSRLAGYKVPRMYV 471
Cdd:PRK08308 312 RMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVI--SHEEIDPVQLREWCIQHLAPYQVPHEIE 389
|
330
....*....|..
gi 584959700 472 PVTHMPLNSTQK 483
Cdd:PRK08308 390 SVTEIPKNANGK 401
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
25-456 |
1.06e-13 |
|
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.
Pssm-ID: 341231 [Multi-domain] Cd Length: 571 Bit Score: 73.54 E-value: 1.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 25 QTSWTYQQLNARADNMAHYL-TSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPLNWRLNPKEIAAIVEDAQLKLL 103
Cdd:cd05905 12 ATTLTWGKLLSRAEKIAAVLqKKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLGFLLGTCKVRVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 104 FYAE---KHLSSLTD-------IDQNLLHMDIDVAQYDEIVNPDYHQPFQATP-VEPQDLAALIYTSGTTGSPKGVMFSY 172
Cdd:cd05905 92 LTVEaclKGLPKKLLksktaaeIAKKKGWPKILDFVKIPKSKRSKLKKWGPHPpTRDGDTAYIEYSFSSDGSLSGVAVSH 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 173 ESFVHNGANLELTYKFNSNYITIVSTPMFHVLGFNDTVLPVLMSGGTLILQRYF----NGEELNDMIAQYHpTFIIMIP- 247
Cdd:cd05905 172 SSLLAHCRALKEACELYESRPLVTVLDFKSGLGLWHGCLLSVYSGHHTILIPPElmktNPLLWLQTLSQYK-VRDAYVKl 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 248 -TMYYSTLRASNFN--------------------PENFRAmdYIIQGGSQPL----PSIQAAFKQYGINII-----NGYG 297
Cdd:cd05905 251 rTLHWCLKDLSSTLaslknrdvnlsslrmcmvpcENRPRI--SSCDSFLKLFqtlgLSPRAVSTEFGTRVNpficwQGTS 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 298 LTEAPLVLVN--------TPENSKRKPMSIGK---AVMFVDARILDDNGEEVP---TGEIGELAIKAKNVTPGYWNKPAE 363
Cdd:cd05905 329 GPEPSRVYLDmralrhgvVRLDERDKPNSLPLqdsGKVLPGAQVAIVNPETKGlckDGEIGEIWVNSPANASGYFLLDGE 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 364 TAKAFHG-------------RYLLTGDL----------AKMDNDGDIFIIDRKKELIITGGENVLPSEVEN-ALAEHPLV 419
Cdd:cd05905 409 TNDTFKVfpstrlstgitnnSYARTGLLgflrptkctdLNVEEHDLLFVVGSIDETLEVRGLRHHPSDIEAtVMRVHPYR 488
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 584959700 420 DRC--------VVVGYDHPKYGESIAAAIILREdephYAEILNQH 456
Cdd:cd05905 489 GRCavfsitglVVVVAEQPPGSEEEALDLVPLV----LNAILEEH 529
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
5-444 |
2.52e-12 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 69.21 E-value: 2.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 5 WIKTRSDfdddKPAVIDHAKQT----SWTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNdiaILDLLF---ACFKTGA 77
Cdd:PRK10524 62 HLAKRPE----QLALIAVSTETdeerTYTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPM---IAEAAFamlACARIGA 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 78 V-------FLPLNwrlnpkeIAAIVEDAQLKLLFYAE-----------KHL------------SSLTDIDQNLLHMDiDV 127
Cdd:PRK10524 135 IhsvvfggFASHS-------LAARIDDAKPVLIVSADagsrggkvvpyKPLldeaialaqhkpRHVLLVDRGLAPMA-RV 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 128 AQYDEIVNPDYHQPFQA-TPV---EPQDLAALIYTSGTTGSPKGVMFSYESF-VHNGANLELTYKFNSNYITIVSTPMFH 202
Cdd:PRK10524 207 AGRDVDYATLRAQHLGArVPVewlESNEPSYILYTSGTTGKPKGVQRDTGGYaVALATSMDTIFGGKAGETFFCASDIGW 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 203 VLGFNDTVLPVLMSGGTLILqryFNGEELN-------DMIAQYHPTFIIMIPTmyysTLRA-SNFNPENFRAMD-----Y 269
Cdd:PRK10524 287 VVGHSYIVYAPLLAGMATIM---YEGLPTRpdagiwwRIVEKYKVNRMFSAPT----AIRVlKKQDPALLRKHDlsslrA 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 270 IIQGGsQPL--PSIQAAFKQYGINIINGYGLTEA--P-LVLVNTPENSKRKPMSIGKAVMFVDARILDDN-GEEVPTGEI 343
Cdd:PRK10524 360 LFLAG-EPLdePTASWISEALGVPVIDNYWQTETgwPiLAIARGVEDRPTRLGSPGVPMYGYNVKLLNEVtGEPCGPNEK 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 344 GELAIKAKnVTPG---------------YWnkpaetaKAFHGRYLLTGDLAKMDNDGDIFIIDRKKELIITGGENVLPSE 408
Cdd:PRK10524 439 GVLVIEGP-LPPGcmqtvwgdddrfvktYW-------SLFGRQVYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTRE 510
|
490 500 510
....*....|....*....|....*....|....*.
gi 584959700 409 VENALAEHPLVDRCVVVGYDHPKYGESIAAAIILRE 444
Cdd:PRK10524 511 IEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPKD 546
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
89-428 |
4.85e-12 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 68.59 E-value: 4.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 89 KEIAAIVEDAQLKLLFYAEKHLSSLTDIDQNLLHMDIDVAQYDEIVNpDYHQPFQATPVEPQDLAALIYTSGTTGSPKGV 168
Cdd:PTZ00342 244 NDLSNELEDISLGPLEYDKEKLEKIKDLKEKAKKLGISIILFDDMTK-NKTTNYKIQNEDPDFITSIVYTSGTSGKPKGV 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 169 MFSYESFvHNGA------NLELTYKFNSN---------------YITIVSTPMFHVLGFNDTVLP--VLMSGGTLIL--Q 223
Cdd:PTZ00342 323 MLSNKNL-YNTVvplckhSIFKKYNPKTHlsylpishiyerviaYLSFMLGGTINIWSKDINYFSkdIYNSKGNILAgvP 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 224 RYFNGEELNDM--IAQYHPTFIIMIPTMYysTLRASNFNP--ENF----------------RAMDYIIQGGSQPLPSIQA 283
Cdd:PTZ00342 402 KVFNRIYTNIMteINNLPPLKRFLVKKIL--SLRKSNNNGgfSKFlegithisskikdkvnPNLEVILNGGGKLSPKIAE 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 284 AFKQY-GINIINGYGLTEA--PLVLVNTPENSkrkPMSIGKAvmfvdarILDDNGEEVPTGEI---------GELAIKAK 351
Cdd:PTZ00342 480 ELSVLlNVNYYQGYGLTETtgPIFVQHADDNN---TESIGGP-------ISPNTKYKVRTWETykatdtlpkGELLIKSD 549
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 584959700 352 NVTPGYWNKPAETAKAF-HGRYLLTGDLAKMDNDGDIFIIDRKKELI-ITGGENVLPSEVENALAEHPLVDRCVVVGYD 428
Cdd:PTZ00342 550 SIFSGYFLEKEQTKNAFtEDGYFKTGDIVQINKNGSLTFLDRSKGLVkLSQGEYIETDMLNNLYSQISFINFCVVYGDD 628
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
29-381 |
5.84e-11 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 64.90 E-value: 5.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 29 TYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVFLPL---------NW--------RLNPKEI 91
Cdd:PRK08180 71 TYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALAAMYAGVPYAPVspayslvsqDFgklrhvleLLTPGLV 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 92 aaIVEDAQLkllfYAEKHLSSLTDidqnllhmDIDVAQYDEIVNPDYHQPFQ---ATP-----------VEPQDLAALIY 157
Cdd:PRK08180 151 --FADDGAA----FARALAAVVPA--------DVEVVAVRGAVPGRAATPFAallATPptaavdaahaaVGPDTIAKFLF 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 158 TSGTTGSPKGVMFSYESFVHNGANLELTYKF-NSNYITIVS-TPMFHVLGFNDTVLPVLMSGGTLILQryfNGEELNDMI 235
Cdd:PRK08180 217 TSGSTGLPKAVINTHRMLCANQQMLAQTFPFlAEEPPVLVDwLPWNHTFGGNHNLGIVLYNGGTLYID---DGKPTPGGF 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 236 AQ-------YHPTFIIMIPTMYYS---------TLRAsNFnpenFRAMDYIIQGG---SQPL-PSIQAAFKQY-G--INI 292
Cdd:PRK08180 294 DEtlrnlreISPTVYFNVPKGWEMlvpalerdaALRR-RF----FSRLKLLFYAGaalSQDVwDRLDRVAEATcGerIRM 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 293 INGYGLTE-APLVLVNTPENSKrkPMSIGKAVMFVDARIlddngeeVPTGEIGELAIKAKNVTPGYWNKPAETAKAF--H 369
Cdd:PRK08180 369 MTGLGMTEtAPSATFTTGPLSR--AGNIGLPAPGCEVKL-------VPVGGKLEVRVKGPNVTPGYWRAPELTAEAFdeE 439
|
410
....*....|..
gi 584959700 370 GrYLLTGDLAKM 381
Cdd:PRK08180 440 G-YYRSGDAVRF 450
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
139-417 |
2.63e-08 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 55.93 E-value: 2.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 139 HQPFQATPVEPQDLAALIYTSGTTGSPKGVMFSYE-----------SF----------VHNGANLELTykfnsnyitiVS 197
Cdd:COG1541 72 NYPFGLFAVPLEEIVRIHASSGTTGKPTVVGYTRKdldrwaelfarSLraagvrpgdrVQNAFGYGLF----------TG 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 198 TPMFH----VLGFndTVLPvlMSGGtlilqryfNGEELNDMIAQYHPTFIIMIPTMYYS---TLRASNFNPENFRaMDYI 270
Cdd:COG1541 142 GLGLHygaeRLGA--TVIP--AGGG--------NTERQLRLMQDFGPTVLVGTPSYLLYlaeVAEEEGIDPRDLS-LKKG 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 271 IQGGsQPLP-SIQAAFKQ-YGINIINGYGLTEA-PLVLVNTPEnskRKPMSIGKAVMFVDarILD-DNGEEVPTGEIGEL 346
Cdd:COG1541 209 IFGG-EPWSeEMRKEIEErWGIKAYDIYGLTEVgPGVAYECEA---QDGLHIWEDHFLVE--IIDpETGEPVPEGEEGEL 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 347 AIkaknvtpgywnkpaeTAKAFHG----RYlLTGDLAKMDNDGDI---------FIIDRKKELIITGGENVLPSEVENAL 413
Cdd:COG1541 283 VV---------------TTLTKEAmpliRY-RTGDLTRLLPEPCPcgrthprigRILGRADDMLIIRGVNVFPSQIEEVL 346
|
....
gi 584959700 414 AEHP 417
Cdd:COG1541 347 LRIP 350
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
145-428 |
2.75e-08 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 56.31 E-value: 2.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 145 TPVEPQDLAALIYTSGTTGSPKGVMFSYESFVHNGANLELTYKFNSNYITIVS-TPMFHVLGFNdTVLPVLMSGGTLIL- 222
Cdd:PRK05851 147 TPPDSGGPAVLQGTAGSTGTPRTAILSPGAVLSNLRGLNARVGLDAATDVGCSwLPLYHDMGLA-FLLTAALAGAPLWLa 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 223 -QRYFNGEELN--DMIAQYHPTFIiMIPTMYYSTL-----RASNFNPENFRamdYIIQGGS----QPLPSIQAAFKQYGI 290
Cdd:PRK05851 226 pTTAFSASPFRwlSWLSDSRATLT-AAPNFAYNLIgkyarRVSDVDLGALR---VALNGGEpvdcDGFERFATAMAPFGF 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 291 N---IINGYGLTEAPLVlVNTPE---------------NSKRKPMSIGKAVMFVDARIL-DDNGEEVPTGEIGELAIKAK 351
Cdd:PRK05851 302 DagaAAPSYGLAESTCA-VTVPVpgiglrvdevttddgSGARRHAVLGNPIPGMEVRISpGDGAAGVAGREIGEIEIRGA 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 352 NVTPGYWNK-PAEtakafHGRYLLTGDLAKMdNDGDIFIIDRKKELIITGGENVLPSEVENALAEHPLV--DRCVVVGYD 428
Cdd:PRK05851 381 SMMSGYLGQaPID-----PDDWFPTGDLGYL-VDGGLVVCGRAKELITVAGRNIFPTEIERVAAQVRGVreGAVVAVGTG 454
|
|
| PRK07868 |
PRK07868 |
acyl-CoA synthetase; Validated |
29-490 |
6.19e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236121 [Multi-domain] Cd Length: 994 Bit Score: 52.41 E-value: 6.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 29 TYQQLNARADNMAHYLTSQGVKKGDVIGIF------APNDIAILDLLFACfktgAVFLPLNwrlnpKEIAAIVEDAQLKL 102
Cdd:PRK07868 474 TYEAVNRRINNVVRGLIAVGVRQGDRVGVLmetrpsALVAIAALSRLGAV----AVLMPPD-----TDLAAAVRLGGVTE 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 103 LFYAEKHLSSLTDIDQNLLHM------DIDVAQYDEIVN-----------PDYHQPfqaTPVEPQDLAAliytsgttgsp 165
Cdd:PRK07868 545 IITDPTNLEAARQLPGRVLVLgggesrDLDLPDDADVIDmekidpdavelPGWYRP---NPGLARDLAF----------- 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 166 kgVMFSyesfvhnGANLELTYKFNSNYITIVS---TPMFHVLGFNDTV--LPVL-------------MSGGTLI-LQRYF 226
Cdd:PRK07868 611 --IAFS-------TAGGELVAKQITNYRWALSafgTASAAALDRRDTVycLTPLhhesgllvslggaVVGGSRIaLSRGL 681
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 227 NGEELNDMIAQYHPTFIIMIPTMYYSTLRAsnfnpENFRAmdyiiqGGSQP--------LPS-----IQAAFKQygINII 293
Cdd:PRK07868 682 DPDRFVQEVRQYGVTVVSYTWAMLREVVDD-----PAFVL------HGNHPvrlfigsgMPTglwerVVEAFAP--AHVV 748
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 294 NGYGLTEAPLVLVN---TPENSKRKPMSIGKAVMFV-----DARIL-DDNG--EEVPTGEIGELAIKAKNVTpgywnKPA 362
Cdd:PRK07868 749 EFFATTDGQAVLANvsgAKIGSKGRPLPGAGRVELAaydpeHDLILeDDRGfvRRAEVNEVGVLLARARGPI-----DPT 823
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 363 ETAK----AFHGRYLLTGDLAKMDNDGDIFIIDRKKELIITGGENVLPSEVENALAEHPLVDRCVVVGYDHPkyGESIA- 437
Cdd:PRK07868 824 ASVKrgvfAPADTWISTEYLFRRDDDGDYWLVDRRGSVIRTARGPVYTEPVTDALGRIGGVDLAVTYGVEVG--GRQLAv 901
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 584959700 438 AAIILREDEPHYAEILNQHMRSRLAGYKVPRMYVpVTHMPLNSTQKPDKLAIR 490
Cdd:PRK07868 902 AAVTLRPGAAITAADLTEALASLPVGLGPDIVHV-VPEIPLSATYRPTVSALR 953
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
13-177 |
6.46e-07 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 52.10 E-value: 6.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 13 DDDKPAVI----DHAKQTsWTYQQLNARADNMAHYLTSQGVKKGDVIGIFAPNDIAILDLLFACFKTGAVflplnW---- 84
Cdd:PRK03584 97 RDDRPAIIfrgeDGPRRE-LSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLATASLGAI-----Wsscs 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959700 85 -------------RLNPK-------------------EIAAIVEdaqlkllfyaekHLSSLTDI-------DQNLLHMDI 125
Cdd:PRK03584 171 pdfgvqgvldrfgQIEPKvliavdgyryggkafdrraKVAELRA------------ALPSLEHVvvvpylgPAAAAAALP 238
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 584959700 126 DVAQYDEIVNPDYHQPFQATPVEPQDLAALIYTSGTTGSPKGvmfsyesFVH 177
Cdd:PRK03584 239 GALLWEDFLAPAEAAELEFEPVPFDHPLWILYSSGTTGLPKC-------IVH 283
|
|
| |
