|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
19-464 |
0e+00 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 804.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 19 SDWPWRHWRQVRAKAPALRLNDEALSWSELCARIDHLASGFAAQGVEEGDGVLLRAWNHPRALLAWLALLQCGARVLPVN 98
Cdd:PRK09029 5 SDWPWRHWAQVRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 99 PQLPQSLLDALVPDLTLRFALDLEAAIALPELSPLQMKSLPGDHAAAWLPERLSTMTLTSGSTGLPKAAVHTCQAHLASA 178
Cdd:PRK09029 85 PQLPQPLLEELLPSLTLDFALVLEGENTFSALTSLHLQLVEGAHAVAWQPQRLATMTLTSGSTGLPKAAVHTAQAHLASA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 179 QGVLSLMPFGAEDDWLLSLPLFHVSGQGILWRWLFAGARMTVRDKQPLDQMLAGCTHASLVPTQLWRLLVNN-TPVTLKA 257
Cdd:PRK09029 165 EGVLSLMPFTAQDSWLLSLPLFHVSGQGIVWRWLYAGATLVVRDKQPLEQALAGCTHASLVPTQLWRLLDNRsEPLSLKA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 258 VLLGGAAIPVELTEQAREQGIRCWCGYGLTEFASTVCAKEADGLADVGSALPGREVRIVNDEVWLRAASMAQGYWRNGQL 337
Cdd:PRK09029 245 VLLGGAAIPVELTEQAEQQGIRCWCGYGLTEMASTVCAKRADGLAGVGSPLPGREVKLVDGEIWLRGASLALGYWRQGQL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 338 MPLVNAEGWFATRDRGVLKDGKLTIVGRMDNLFFSGGEGIQPEEVERVIAAHPHVLQAFIVPIEDKEFGHRPVAVVEYDA 417
Cdd:PRK09029 325 VPLVNDEGWFATRDRGEWQNGELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVPVADAEFGQRPVAVVESDS 404
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 489936067 418 NAGETNLAEWVKDKLARFQQPVCWLTLPPELKAGGIKISRRALSDWV 464
Cdd:PRK09029 405 EAAVVNLAEWLQDKLARFQQPVAYYLLPPELKNGGIKISRQALKEWV 451
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
150-464 |
1.50e-136 |
|
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: 395.93 E-value: 1.50e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 150 RLSTMTLTSGSTGLPKAAVHTCQAHLASAQGVLSLMPFGAEDDWLLSLPLFHVSGQGILWRWLFAGARMTVRDK-QPLDQ 228
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLYHVGGLAILVRSLLAGAELVLLERnQALAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 229 MLA--GCTHASLVPTQLWRLLVNN----TPVTLKAVLLGGAAIPVELTEQAREQGIRCWCGYGLTEFASTVCAKEADG-- 300
Cdd:cd17630 81 DLAppGVTHVSLVPTQLQRLLDSGqgpaALKSLRAVLLGGAPIPPELLERAADRGIPLYTTYGMTETASQVATKRPDGfg 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 301 LADVGSALPGREVRIVND-EVWLRAASMAQGYWRnGQLMPLVNAEGWFATRDRGVL-KDGKLTIVGRMDNLFFSGGEGIQ 378
Cdd:cd17630 161 RGGVGVLLPGRELRIVEDgEIWVGGASLAMGYLR-GQLVPEFNEDGWFTTKDLGELhADGRLTVLGRADNMIISGGENIQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 379 PEEVERVIAAHPHVLQAFIVPIEDKEFGHRPVAVVEYDANAGETNLAEWVKDKLARFQQPVCWLTLPPELKAGGIKISRR 458
Cdd:cd17630 240 PEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRGPADPAELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRR 319
|
....*.
gi 489936067 459 ALSDWV 464
Cdd:cd17630 320 ALRAWL 325
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
44-460 |
3.94e-125 |
|
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: 371.01 E-value: 3.94e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 44 SWSELCARIDHLASGFAAQGVEEGDGVLLRAWNHPRALLAWLALLQCGARVLPVNPQLPQSLLDALVPDLTLRFALD--- 120
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTdsl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 121 LEA----AIALPELsplqMKSLPGD--HAAAWLPERLSTMTLTSGSTGLPKAAVHTCQAHLASAQGVLSLMPFGAEDDWL 194
Cdd:TIGR01923 81 LEEkdfqADSLDRI----EAAGRYEtsLSASFNMDQIATLMFTSGTTGKPKAVPHTFRNHYASAVGSKENLGFTEDDNWL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 195 LSLPLFHVSGQGILWRWLFAGARMTVRDKQP-LDQMLAG--CTHASLVPTQLWRLL-VNNTPVTLKAVLLGGAAIPVELT 270
Cdd:TIGR01923 157 LSLPLYHISGLSILFRWLIEGATLRIVDKFNqLLEMIANerVTHISLVPTQLNRLLdEGGHNENLRKILLGGSAIPAPLI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 271 EQAREQGIRCWCGYGLTEFASTVCAKEADGLA---DVGSALPGREVRIVND------EVWLRAASMAQGYWRNGQLMPLV 341
Cdd:TIGR01923 237 EEAQQYGLPIYLSYGMTETCSQVTTATPEMLHarpDVGRPLAGREIKIKVDnkeghgEIMVKGANLMKGYLYQGELTPAF 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 342 NAEGWFATRDRGVLK-DGKLTIVGRMDNLFFSGGEGIQPEEVERVIAAHPHVLQAFIVPIEDKEFGHRPVAVVEYDANAG 420
Cdd:TIGR01923 317 EQQGWFNTGDIGELDgEGFLYVLGRRDDLIISGGENIYPEEIETVLYQHPGIQEAVVVPKPDAEWGQVPVAYIVSESDIS 396
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 489936067 421 ETNLAEWVKDKLARFQQPVCWLTLP--PELKAGgiKISRRAL 460
Cdd:TIGR01923 397 QAKLIAYLTEKLAKYKVPIAFEKLDelPYNASG--KILRNQL 436
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
24-469 |
3.52e-87 |
|
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: 273.99 E-value: 3.52e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 24 RHWRQVRAKAPALRLNDEALSWSELCARIDHLASGFAAQGVEEGDGVLLRAWNHPRALLAWLALLQCGARVLPVNPQLPQ 103
Cdd:COG0318 6 RRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 104 SLLDALvpdltLRfalDLEAAIALpelsplqmkslpgdhaAAWLperlstmTLTSGSTGLPKAAVHTCQAHLASAQGVLS 183
Cdd:COG0318 86 EELAYI-----LE---DSGARALV----------------TALI-------LYTSGTTGRPKGVMLTHRNLLANAAAIAA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 184 LMPFGAEDDWLLSLPLFHVSGQGI-LWRWLFAGARMTVRDKQPLDQMLA-----GCTHASLVPTQLWRLLvnNTPV---- 253
Cdd:COG0318 135 ALGLTPGDVVLVALPLFHVFGLTVgLLAPLLAGATLVLLPRFDPERVLEliereRVTVLFGVPTMLARLL--RHPEfary 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 254 ---TLKAVLLGGAAIPVELTEQAREQ-GIRCWCGYGLTEFASTVCAKEADGLAD----VGSALPGREVRIVND------- 318
Cdd:COG0318 213 dlsSLRLVVSGGAPLPPELLERFEERfGVRIVEGYGLTETSPVVTVNPEDPGERrpgsVGRPLPGVEVRIVDEdgrelpp 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 319 ----EVWLRAASMAQGYWRNGQLMPLVNAEGWFATRDRGVL-KDGKLTIVGRMDNLFFSGGEGIQPEEVERVIAAHPHVL 393
Cdd:COG0318 293 gevgEIVVRGPNVMKGYWNDPEATAEAFRDGWLRTGDLGRLdEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVA 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 394 QAFIVPIEDKEFGHRPVAVVEY--DANAGETNLAEWVKDKLARFQQPVCWL---TLPpeLKAGGiKISRRALSDWVSASS 468
Cdd:COG0318 373 EAAVVGVPDEKWGERVVAFVVLrpGAELDAEELRAFLRERLARYKVPRRVEfvdELP--RTASG-KIDRRALRERYAAGA 449
|
.
gi 489936067 469 L 469
Cdd:COG0318 450 L 450
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
150-455 |
3.21e-81 |
|
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: 254.90 E-value: 3.21e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 150 RLSTMTLTSGSTGLPKAAVHTCQAHLASAQGVLSLMPFGAEDDWLLSLPLFHVSGQGILWRWLFAGARMTVRDKQPLDQM 229
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKFDPEAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 230 LA-----GCTHASLVPTQLWRLLVNNTPV-----TLKAVLLGGAAIPVELTEQAREQ-GIRCWCGYGLTEFASTVCAKEA 298
Cdd:cd04433 81 LEliereKVTILLGVPTLLARLLKAPESAgydlsSLRALVSGGAPLPPELLERFEEApGIKLVNGYGLTETGGTVATGPP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 299 DGLA----DVGSALPGREVRIVND-----------EVWLRAASMAQGYWRNGQLMPLVNAEGWFATRDRGVL-KDGKLTI 362
Cdd:cd04433 161 DDDArkpgSVGRPVPGVEVRIVDPdggelppgeigELVVRGPSVMKGYWNNPEATAAVDEDGWYRTGDLGRLdEDGYLYI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 363 VGRMDNLFFSGGEGIQPEEVERVIAAHPHVLQAFIVPIEDKEFGHRPVAVVEYDANAGETN--LAEWVKDKLARFQQPVC 440
Cdd:cd04433 241 VGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLDAeeLRAHVRERLAPYKVPRR 320
|
330
....*....|....*
gi 489936067 441 WLTLPPELKAGGIKI 455
Cdd:cd04433 321 VVFVDALPRTASGKI 335
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
24-438 |
1.20e-59 |
|
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: 201.68 E-value: 1.20e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 24 RHWRQVRAKAPALRLNDEALSWSELCARIDHLASGFAAQGVEEGDGVLLRAWNHPRAllawlallqcgarvlpvnpqlpq 103
Cdd:cd17631 2 RRRARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEF----------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 104 slldalvpdLTLRFALDLEAAIALP---ELSPLQMKSLPGDHAAAWLPERLSTMTLTSGSTGLPKAAVHTCQAHLASAQG 180
Cdd:cd17631 59 ---------LELLFAAARLGAVFVPlnfRLTPPEVAYILADSGAKVLFDDLALLMYTSGTTGRPKGAMLTHRNLLWNAVN 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 181 VLSLMPFGAEDDWLLSLPLFHVSGQGILW-RWLFAGARMTVRDKQPLDQMLAGC-----THASLVPTQLWRLLvnNTPV- 253
Cdd:cd17631 130 ALAALDLGPDDVLLVVAPLFHIGGLGVFTlPTLLRGGTVVILRKFDPETVLDLIerhrvTSFFLVPTMIQALL--QHPRf 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 254 ------TLKAVLLGGAAIPVELTEQAREQGIRCWCGYGLTEFASTVCAKEADG----LADVGSALPGREVRIVND----- 318
Cdd:cd17631 208 attdlsSLRAVIYGGAPMPERLLRALQARGVKFVQGYGMTETSPGVTFLSPEDhrrkLGSAGRPVFFVEVRIVDPdgrev 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 319 ------EVWLRAASMAQGYWRNgqlmPLVNAE----GWFATRDRGVL-KDGKLTIVGRMDNLFFSGGEGIQPEEVERVIA 387
Cdd:cd17631 288 ppgevgEIVVRGPHVMAGYWNR----PEATAAafrdGWFHTGDLGRLdEDGYLYIVDRKKDMIISGGENVYPAEVEDVLY 363
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 489936067 388 AHPHVLQAFIVPIEDKEFGHRPVAVV--EYDANAGETNLAEWVKDKLARFQQP 438
Cdd:cd17631 364 EHPAVAEVAVIGVPDEKWGEAVVAVVvpRPGAELDEDELIAHCRERLARYKIP 416
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
47-460 |
3.47e-59 |
|
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.
Pssm-ID: 341238 [Multi-domain] Cd Length: 411 Bit Score: 199.88 E-value: 3.47e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 47 ELCARIDHLASGFAAQGVEEGDGVLLRAWNHPRALLAWLALLQCGARVLPVNPQL-PQSLLDALvpdltlrfaldLEAAI 125
Cdd:cd05912 6 ELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLtPNELAFQL-----------KDSDV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 126 ALpelsplqmkslpgdhaaawlpERLSTMTLTSGSTGLPKAAVHTCQAHLASAQGVLSLMPFGAEDDWLLSLPLFHVSGQ 205
Cdd:cd05912 75 KL---------------------DDIATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGLTEDDNWLCALPLFHISGL 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 206 GILWRWLFAGARMTVRDK---QPLDQML--AGCTHASLVPTQLWRLLV---NNTPVTLKAVLLGGAAIPVELTEQAREQG 277
Cdd:cd05912 134 SILMRSVIYGMTVYLVDKfdaEQVLHLInsGKVTIISVVPTMLQRLLEilgEGYPNNLRCILLGGGPAPKPLLEQCKEKG 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 278 IRCWCGYGLTEFASTVCA-KEADGLADVGSA---LPGREVRIVND--------EVWLRAASMAQGYWRNGQLMPLVNAEG 345
Cdd:cd05912 214 IPVYQSYGMTETCSQIVTlSPEDALNKIGSAgkpLFPVELKIEDDgqppyevgEILLKGPNVTKGYLNRPDATEESFENG 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 346 WFATRDRGVL-KDGKLTIVGRMDNLFFSGGEGIQPEEVERVIAAHPHVLQAFIVPIEDKEFGHRPVAVVEYDANAGETNL 424
Cdd:cd05912 294 WFKTGDIGYLdEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSERPISEEEL 373
|
410 420 430
....*....|....*....|....*....|....*...
gi 489936067 425 AEWVKDKLARFQQP--VCWLTLPPELKAGgiKISRRAL 460
Cdd:cd05912 374 IAYCSEKLAKYKVPkkIYFVDELPRTASG--KLLRHEL 409
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
25-438 |
4.27e-58 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 199.03 E-value: 4.27e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 25 HWRQVRA----KAPALRLNDEALSWSELCARIDHLASGFAAQGVEEGDGVLLRAWNHPRALLAWLALLQCGARVLPVNPQ 100
Cdd:PRK03640 6 NWLKQRAfltpDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 101 LP-------------------QSLLDALVPDLTLRFAlDLEAAiALPELSPLQMKSLpgdhaaawlpERLSTMTLTSGST 161
Cdd:PRK03640 86 LSreellwqlddaevkclitdDDFEAKLIPGISVKFA-ELMNG-PKEEAEIQEEFDL----------DEVATIMYTSGTT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 162 GLPKAAVHTCQAHLASAQG-VLSLmpfG--AEDDWLLSLPLFHVSGQGILWRWLFAGARMTVRDK---QPLDQML--AGC 233
Cdd:PRK03640 154 GKPKGVIQTYGNHWWSAVGsALNL---GltEDDCWLAAVPIFHISGLSILMRSVIYGMRVVLVEKfdaEKINKLLqtGGV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 234 THASLVPTQLWRLLV----NNTPVTLKAVLLGGAAIPVELTEQAREQGIRCWCGYGLTEFASTVCA-KEADGLADVGSA- 307
Cdd:PRK03640 231 TIISVVSTMLQRLLErlgeGTYPSSFRCMLLGGGPAPKPLLEQCKEKGIPVYQSYGMTETASQIVTlSPEDALTKLGSAg 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 308 --LPGREVRIVND----------EVWLRAASMAQGYWRNGQLMPLVNAEGWFATRDRGVL-KDGKLTIVGRMDNLFFSGG 374
Cdd:PRK03640 311 kpLFPCELKIEKDgvvvppfeegEIVVKGPNVTKGYLNREDATRETFQDGWFKTGDIGYLdEEGFLYVLDRRSDLIISGG 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489936067 375 EGIQPEEVERVIAAHPHVLQAFIVPIEDKEFGHRPVAVVEYDANAGETNLAEWVKDKLARFQQP 438
Cdd:PRK03640 391 ENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVKSGEVTEEELRHFCEEKLAKYKVP 454
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
24-460 |
6.96e-53 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 185.78 E-value: 6.96e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 24 RHWRQVRAKAPALRLNDEALSWSELCARIDHLASGFAAQGVEEGDGVLLRAWNHPRALLAWLALLQCGARVLPVNPQLPQ 103
Cdd:PRK06187 13 RHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPINIRLKP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 104 ----------------------SLLDALVPDL-TLRFALDLEAAIALPELSPLQ-----MKSLPGDHAAAWLPER-LSTM 154
Cdd:PRK06187 93 eeiayilndaedrvvlvdsefvPLLAAILPQLpTVRTVIVEGDGPAAPLAPEVGeyeelLAAASDTFDFPDIDENdAAAM 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 155 TLTSGSTGLPKAAVHTcqaH---LASAQGVLSLMPFGAEDDWLLSLPLFHVSGQGILWRWLFAGARMTVRDK-QP---LD 227
Cdd:PRK06187 173 LYTSGTTGHPKGVVLS---HrnlFLHSLAVCAWLKLSRDDVYLVIVPMFHVHAWGLPYLALMAGAKQVIPRRfDPenlLD 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 228 QMLA-GCTHASLVPTqLWRLLVNN---TPV---TLKAVLLGGAAIPVELTEQAREQ-GIRCWCGYGLTEFASTV-CAKEA 298
Cdd:PRK06187 250 LIETeRVTFFFAVPT-IWQMLLKApraYFVdfsSLRLVIYGGAALPPALLREFKEKfGIDLVQGYGMTETSPVVsVLPPE 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 299 DGLAD-------VGSALPGREVRIVND-------------EVWLRAASMAQGYWRngqlMPLVNAE----GWFATRDRGV 354
Cdd:PRK06187 329 DQLPGqwtkrrsAGRPLPGVEARIVDDdgdelppdggevgEIIVRGPWLMQGYWN----RPEATAEtidgGWLHTGDVGY 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 355 L-KDGKLTIVGRMDNLFFSGGEGIQPEEVERVIAAHPHVLQAFIVPIEDKEFGHRPVAVVEY--DANAGETNLAEWVKDK 431
Cdd:PRK06187 405 IdEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVLkpGATLDAKELRAFLRGR 484
|
490 500 510
....*....|....*....|....*....|..
gi 489936067 432 LARFQQPVCWL---TLPpeLKAGGiKISRRAL 460
Cdd:PRK06187 485 LAKFKLPKRIAfvdELP--RTSVG-KILKRVL 513
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
30-460 |
1.63e-51 |
|
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: 181.22 E-value: 1.63e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 30 RAKAPALRLNDEALSWSELCARIDHLASGFAAQGVEEGDGVLLRAWNHPRALLAWLALLQCGARVLPVNPQLPQSLLDAL 109
Cdd:cd05936 12 FPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYTPRELEHI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 110 VPDLTLRFaldLEAAIALPEL--SPLQMKSLPGDHaaawlPERLSTMTLTSGSTGLPKAAVHTCQAHLASAQGVLSLMPF 187
Cdd:cd05936 92 LNDSGAKA---LIVAVSFTDLlaAGAPLGERVALT-----PEDVAVLQYTSGTTGVPKGAMLTHRNLVANALQIKAWLED 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 188 G--AEDDWLLSLPLFHVSGQGI-LWRWLFAGARM----TVRDKQPLDQMLA-GCTHASLVPTqLWRLLVNNTPV------ 253
Cdd:cd05936 164 LleGDDVVLAALPLFHVFGLTVaLLLPLALGATIvlipRFRPIGVLKEIRKhRVTIFPGVPT-MYIALLNAPEFkkrdfs 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 254 TLKAVLLGGAAIPVELTEQAREQ-GIRCWCGYGLTEFASTVCAKEADGLADVGS---ALPGREVRIVND----------- 318
Cdd:cd05936 243 SLRLCISGGAPLPVEVAERFEELtGVPIVEGYGLTETSPVVAVNPLDGPRKPGSigiPLPGTEVKIVDDdgeelppgevg 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 319 EVWLRAASMAQGYWRNGQLMPLVNAEGWFATRDRGVL-KDGKLTIVGRMDNLFFSGGEGIQPEEVERVIAAHPHVLQAFI 397
Cdd:cd05936 323 ELWVRGPQVMKGYWNRPEETAEAFVDGWLRTGDIGYMdEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAV 402
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489936067 398 VPIEDKEFGHRPVAVV--EYDANAGETNLAEWVKDKLARFQQPVCwLTLPPELKAGGI-KISRRAL 460
Cdd:cd05936 403 VGVPDPYSGEAVKAFVvlKEGASLTEEEIIAFCREQLAGYKVPRQ-VEFRDELPKSAVgKILRREL 467
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
157-461 |
6.08e-50 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 174.08 E-value: 6.08e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 157 TSGSTGLPKAAVHTCQAHLASAQGVLSLMpfGAEDDWLLSLPLFHVSGQGILWRWLFAGARMTVRD----------KQPL 226
Cdd:PRK07824 43 TSGTTGTPKGAMLTAAALTASADATHDRL--GGPGQWLLALPAHHIAGLQVLVRSVIAGSEPVELDvsagfdptalPRAV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 227 DQMLAGCTHASLVPTQLWRLLVNNTPV----TLKAVLLGGAAIPVELTEQAREQGIRCWCGYGLTEfastvcakEADGLA 302
Cdd:PRK07824 121 AELGGGRRYTSLVPMQLAKALDDPAATaalaELDAVLVGGGPAPAPVLDAAAAAGINVVRTYGMSE--------TSGGCV 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 303 DVGSALPGREVRIVNDEVWLRAASMAQGYwRNGQLMPLVNAEGWFATRDRGVLKDGKLTIVGRMDNLFFSGGEGIQPEEV 382
Cdd:PRK07824 193 YDGVPLDGVRVRVEDGRIALGGPTLAKGY-RNPVDPDPFAEPGWFRTDDLGALDDGVLTVLGRADDAISTGGLTVLPQVV 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 383 ERVIAAHPHVLQAFIVPIEDKEFGHRPVAVVEYDANAGET--NLAEWVKDKLARFQQPVcWLTLPPELKAGGI-KISRRA 459
Cdd:PRK07824 272 EAALATHPAVADCAVFGLPDDRLGQRVVAAVVGDGGPAPTleALRAHVARTLDRTAAPR-ELHVVDELPRRGIgKVDRRA 350
|
..
gi 489936067 460 LS 461
Cdd:PRK07824 351 LV 352
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
23-370 |
1.38e-47 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 169.42 E-value: 1.38e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 23 WRHWRQVRAKAPALRLND-EALSWSELCARIDHLASGFAAQGVEEGDGVLLRAWNHPRALLAWLALLQCGARVLPVNPQL 101
Cdd:pfam00501 1 LERQAARTPDKTALEVGEgRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 102 P------------------------QSLLDAL--VPDLTLRFALDLEAAIALPELSPLQMKSLPGDHAAAWL-PERLSTM 154
Cdd:pfam00501 81 PaeelayiledsgakvlitddalklEELLEALgkLEVVKLVLVLDRDPVLKEEPLPEEAKPADVPPPPPPPPdPDDLAYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 155 TLTSGSTGLPKAAVHTCQAHLASAQGVLSL----MPFGAEDDWLLSLPLFHVSGQG-ILWRWLFAGARMTVRDKQPLDQM 229
Cdd:pfam00501 161 IYTSGTTGKPKGVMLTHRNLVANVLSIKRVrprgFGLGPDDRVLSTLPLFHDFGLSlGLLGPLLAGATVVLPPGFPALDP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 230 LA--------GCTHASLVPTqLWRLLVNNTPV------TLKAVLLGGAAIPVELTEQAREQ-GIRCWCGYGLTEfASTVC 294
Cdd:pfam00501 241 AAllelieryKVTVLYGVPT-LLNMLLEAGAPkrallsSLRLVLSGGAPLPPELARRFRELfGGALVNGYGLTE-TTGVV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 295 AKEADGLAD------VGSALPGREVRIVND------------EVWLRAASMAQGYWRNGQLmplvNAE-----GWFATRD 351
Cdd:pfam00501 319 TTPLPLDEDlrslgsVGRPLPGTEVKIVDDetgepvppgepgELCVRGPGVMKGYLNDPEL----TAEafdedGWYRTGD 394
|
410 420
....*....|....*....|
gi 489936067 352 RGV-LKDGKLTIVGRMDNLF 370
Cdd:pfam00501 395 LGRrDEDGYLEIVGRKKDQI 414
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
43-448 |
4.26e-43 |
|
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: 158.14 E-value: 4.26e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 43 LSWSELCARIDHLASGFAAQGVEEGDGVLLRAWNHPRALLAWLALLQCGARVLPVNPQLPqslldalvPDLTLRFALDLE 122
Cdd:cd05907 6 ITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSS--------AEQIAYILNDSE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 123 AAIALpelsplqmkslpGDHaaawlPERLSTMTLTSGSTGLPKAAVHTCQAHLASAQGVLSLMPFGAEDDWLLSLPLFHV 202
Cdd:cd05907 78 AKALF------------VED-----PDDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPATEGDRHLSFLPLAHV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 203 SGQgILWRWLFAGARMTVRDKQPLDQMLAGCTHASlvPTQL------WRLLVNNTPVT-----------------LKAVL 259
Cdd:cd05907 141 FER-RAGLYVPLLAGARIYFASSAETLLDDLSEVR--PTVFlavprvWEKVYAAIKVKavpglkrklfdlavggrLRFAA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 260 LGGAAIPVELTEQAREQGIRCWCGYGLTEFASTVCAKEADG--LADVGSALPGREVRIVND-EVWLRAASMAQGYWRN-G 335
Cdd:cd05907 218 SGGAPLPAELLHFFRALGIPVYEGYGLTETSAVVTLNPPGDnrIGTVGKPLPGVEVRIADDgEILVRGPNVMLGYYKNpE 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 336 QLMPLVNAEGWFATRDRGVLK-DGKLTIVGRMDNLFF-SGGEGIQPEEVERVIAAHPHVLQ------------AFIVPIE 401
Cdd:cd05907 298 ATAEALDADGWLHTGDLGEIDeDGFLHITGRKKDLIItSGGKNISPEPIENALKASPLISQavvigdgrpflvALIVPDP 377
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 489936067 402 D------KEFGHRPVAVVEYDANAG-ETNLAEWVKD---KLARFQQPVCWLTLPPEL 448
Cdd:cd05907 378 EaleawaEEHGIAYTDVAELAANPAvRAEIEAAVEAanaRLSRYEQIKKFLLLPEPF 434
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
44-460 |
7.31e-42 |
|
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: 155.87 E-value: 7.31e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 44 SWSELCARIDHLASGFAAQGVEEGDGVLLRAWNHPRALLAWLALLQCGARVLPVNPQLP--------------------- 102
Cdd:cd12119 27 TYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFpeqiayiinhaedrvvfvdrd 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 103 -QSLLDALVPDLTlrfalDLEAAIALPELSPLQMKSLPGDHA-----------AAW--LPERL-STMTLTSGSTGLPKAA 167
Cdd:cd12119 107 fLPLLEAIAPRLP-----TVEHVVVMTDDAAMPEPAGVGVLAyeellaaespeYDWpdFDENTaAAICYTSGTTGNPKGV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 168 V--------HTCQAHLASAqgvlslMPFGAEDDWLLSLPLFHVSGQGILWRWLFAGARMTV--RDKQP--LDQMLA--GC 233
Cdd:cd12119 182 VyshrslvlHAMAALLTDG------LGLSESDVVLPVVPMFHVNAWGLPYAAAMVGAKLVLpgPYLDPasLAELIEreGV 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 234 THASLVPTqLWRLLVN------NTPVTLKAVLLGGAAIPVELTEQAREQGIRCWCGYGLTEF-----ASTVCAKEADGLA 302
Cdd:cd12119 256 TFAAGVPT-VWQGLLDhleangRDLSSLRRVVIGGSAVPRSLIEAFEERGVRVIHAWGMTETsplgtVARPPSEHSNLSE 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 303 DV--------GSALPGREVRIVND-------------EVWLRAASMAQGYWRNGQLMPLVNAEGWFATRDRGVL-KDGKL 360
Cdd:cd12119 335 DEqlalrakqGRPVPGVELRIVDDdgrelpwdgkavgELQVRGPWVTKSYYKNDEESEALTEDGWLRTGDVATIdEDGYL 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 361 TIVGRMDNLFFSGGEGIQPEEVERVIAAHPHVLQAFIVPIEDKEFGHRPVAVVEY--DANAGETNLAEWVKDKLARFQQP 438
Cdd:cd12119 415 TITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLkeGATVTAEELLEFLADKVAKWWLP 494
|
490 500
....*....|....*....|....*
gi 489936067 439 VCWL---TLPpeLKAGGiKISRRAL 460
Cdd:cd12119 495 DDVVfvdEIP--KTSTG-KIDKKAL 516
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
39-437 |
2.53e-41 |
|
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: 153.91 E-value: 2.53e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 39 NDEALSWSELCARIDHLASGFAAQGVEEGDGVLLRAWNHPRALLAWLALLQCGARVLPVNPQLPQSLLDALV-------- 110
Cdd:cd05911 7 TGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLkiskpkvi 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 111 ---PDL--TLR------------FALDLEAAIALPELSPLQMKSLPGDHAAAWLPERLSTMTL----TSGSTGLPKAAV- 168
Cdd:cd05911 87 ftdPDGleKVKeaakelgpkdkiIVLDDKPDGVLSIEDLLSPTLGEEDEDLPPPLKDGKDDTAailySSGTTGLPKGVCl 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 169 --HTCQAHLASAQGVLSLMpFGAEDDWLLSLPLFHVSGQGILWRWLFAGARMTVRDKQPLDQMLAGC-----THASLVPT 241
Cdd:cd05911 167 shRNLIANLSQVQTFLYGN-DGSNDVILGFLPLYHIYGLFTTLASLLNGATVIIMPKFDSELFLDLIekykiTFLYLVPP 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 242 QLwRLLVNNTPVT------LKAVLLGGAAIPVELTEQAREQGIRCWC--GYGLTE--FASTVCAKEADGLADVGSALPGR 311
Cdd:cd05911 246 IA-AALAKSPLLDkydlssLRVILSGGAPLSKELQELLAKRFPNATIkqGYGMTEtgGILTVNPDGDDKPGSVGRLLPNV 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 312 EVRIVND------------EVWLRAASMAQGYWRNgqlmPLVNAE-----GWFATRDRGVL-KDGKLTIVGRMDNLFFSG 373
Cdd:cd05911 325 EAKIVDDdgkdslgpnepgEICVRGPQVMKGYYNN----PEATKEtfdedGWLHTGDIGYFdEDGYLYIVDRKKELIKYK 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489936067 374 GEGIQPEEVERVIAAHPHVLQAFIVPIEDKEFGHRPVAVV--EYDANAGETNLAEWVKDKLARFQQ 437
Cdd:cd05911 401 GFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVvrKPGEKLTEKEVKDYVAKKVASYKQ 466
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
127-464 |
4.19e-40 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 149.76 E-value: 4.19e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 127 LPELSPLQMKSLPGDHAAAWL--PERLSTMTLTSGSTGLPKAAVHTCQAHLASAQGVLSLMPFGAEDDwLLSLPLFHVSG 204
Cdd:PRK07445 96 IWGLDQLKLSHPPPLPSQGILpnLETGWIMIPTGGSSGQIRFAIHTWETLTASVQGFQRYFQLQQVNS-FCVLPLYHVSG 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 205 QGILWRWLFAGARMTVRDKQPLDQ---MLAGCTHA--SLVPTQLWRLLVNNTP--VTLKAVLLGGAAIPVELTEQAREQG 277
Cdd:PRK07445 175 LMQFMRSFLTGGKLVILPYKRLKSgqeLPPNPSDFflSLVPTQLQRLLQLRPQwlAQFRTILLGGAPAWPSLLEQARQLQ 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 278 IRCWCGYGLTEFASTVCA-KEADGLA---DVGSALPGREVRIVND---EVWLRAASMAQGYWRNgqlmpLVNAEGWFATR 350
Cdd:PRK07445 255 LRLAPTYGMTETASQIATlKPDDFLAgnnSSGQVLPHAQITIPANqtgNITIQAQSLALGYYPQ-----ILDSQGIFETD 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 351 DRGVL-KDGKLTIVGRMDNLFFSGGEGIQPEEVERVIAAHPHVLQAFIVPIEDKEFGHRPVAVveYDANAGETNLAE--- 426
Cdd:PRK07445 330 DLGYLdAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAI--YVPKDPSISLEElkt 407
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 489936067 427 WVKDKLARFQQPVCWLTLP--PELKAGgiKISRRALSDWV 464
Cdd:PRK07445 408 AIKDQLSPFKQPKHWIPVPqlPRNPQG--KINRQQLQQIA 445
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
33-438 |
1.36e-37 |
|
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: 142.81 E-value: 1.36e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 33 APALRLNDEALSWSELCARIDHLASGFAAQG-VEEGDGVLLRAWNHPRALLAWLALLQCGARVLPVNPQLPQSLLDALVP 111
Cdd:cd05941 2 RIAIVDDGDSITYADLVARAARLANRLLALGkDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVIT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 112 DltlrfaldleaaialpelsplqmkSLPgdhaAAWLpeRLSTMTLTSGSTGLPKAAVHTCQAHLASAQGVLSLMPFGAED 191
Cdd:cd05941 82 D------------------------SEP----SLVL--DPALILYTSGTTGRPKGVVLTHANLAANVRALVDAWRWTEDD 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 192 DWLLSLPLFHVSGQG-ILWRWLFAGARMTVRDKQPLDQMLAGCTHASL-----VPTQLWRLL----VNNTPVTLKAVLL- 260
Cdd:cd05941 132 VLLHVLPLHHVHGLVnALLCPLFAGASVEFLPKFDPKEVAISRLMPSItvfmgVPTIYTRLLqyyeAHFTDPQFARAAAa 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 261 --------GGAAIPVELTEQARE-QGIRCWCGYGLTEFA-STVCAKEADGLA-DVGSALPGREVRIVND----------- 318
Cdd:cd05941 212 erlrlmvsGSAALPVPTLEEWEAiTGHTLLERYGMTEIGmALSNPLDGERRPgTVGMPLPGVQARIVDEetgeplprgev 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 319 -EVWLRAASMAQGYWRNgqlmPLVNAE-----GWFATRDRGVLK-DGKLTIVGRM-DNLFFSGGEGIQPEEVERVIAAHP 390
Cdd:cd05941 292 gEIQVRGPSVFKEYWNK----PEATKEeftddGWFKTGDLGVVDeDGYYWILGRSsVDIIKSGGYKVSALEIERVLLAHP 367
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 489936067 391 HVLQAFIVPIEDKEFGHRPVAVVEYDANAG---ETNLAEWVKDKLARFQQP 438
Cdd:cd05941 368 GVSECAVIGVPDPDWGERVVAVVVLRAGAAalsLEELKEWAKQRLAPYKRP 418
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
28-438 |
3.09e-37 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 143.53 E-value: 3.09e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 28 QVRAKAPALRLNDEALSWSELCARIDHLASGFAAQGVEEGDGVLLRAWNHPRALLAWLALLQCGARVLPVN-----PQLP 102
Cdd:PRK07788 60 RRAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNtgfsgPQLA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 103 Q-----------------SLLDALVPDLTlrfalDLEAAIALPELSPLQMKSLP--------GDHAAAWLPERLSTMT-L 156
Cdd:PRK07788 140 EvaaregvkalvyddeftDLLSALPPDLG-----RLRAWGGNPDDDEPSGSTDEtlddliagSSTAPLPKPPKPGGIViL 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 157 TSGSTGLPKAAVHTCQAHLASAQGVLSLMPFGAEDDWLLSLPLFHVSGQGILWRWLFAGARMTVRDKQPLDQMLAG---- 232
Cdd:PRK07788 215 TSGTTGTPKGAPRPEPSPLAPLAGLLSRVPFRAGETTLLPAPMFHATGWAHLTLAMALGSTVVLRRRFDPEATLEDiakh 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 233 -CTHASLVPTQLWRLL-----VNNTPVT--LKAVLLGGAAIPVELTEQAREQ-GIRCWCGYGLTEFASTVCAKEADGLAD 303
Cdd:PRK07788 295 kATALVVVPVMLSRILdlgpeVLAKYDTssLKIIFVSGSALSPELATRALEAfGPVLYNLYGSTEVAFATIATPEDLAEA 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 304 ---VGSALPGREVRIVNDE-----------VWLRAASMAQGYwRNGQLMPLVNaeGWFATRDRGVL-KDGKLTIVGRMDN 368
Cdd:PRK07788 375 pgtVGRPPKGVTVKILDENgnevprgvvgrIFVGNGFPFEGY-TDGRDKQIID--GLLSSGDVGYFdEDGLLFVDGRDDD 451
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489936067 369 LFFSGGEGIQPEEVERVIAAHPHVLQAFIVPIEDKEFGHRPVA--VVEYDANAGETNLAEWVKDKLARFQQP 438
Cdd:PRK07788 452 MIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAfvVKAPGAALDEDAIKDYVRDNLARYKVP 523
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
33-460 |
4.59e-37 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 142.35 E-value: 4.59e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 33 APALRLNDEALSWSELCARIDHLASGFAAQGVEEGDGVLLRAWNHPRALLAWLALLQCGARVLPVNPQ------------ 100
Cdd:PRK07656 21 KEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRytadeaayilar 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 101 ------------LPQS-LLDALVPDLTLRFALDLEAAIALPElsplQMKSL--------PGDHAAAWLPERLSTMTLTSG 159
Cdd:PRK07656 101 gdakalfvlglfLGVDySATTRLPALEHVVICETEEDDPHTE----KMKTFtdflaagdPAERAPEVDPDDVADILFTSG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 160 STGLPKAAVHTCQAHLASAQGVLSLMPFGAEDDWLLSLPLFHVSG--QGILwRWLFAGARM-------------TVRDKQ 224
Cdd:PRK07656 177 TTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLAANPFFHVFGykAGVN-APLMRGATIlplpvfdpdevfrLIETER 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 225 PldQMLAGcthaslVPTQLWRLLvnNTP-------VTLKAVLLGGAAIPVELTEQAREQ-GIR-CWCGYGLTEFASTVCA 295
Cdd:PRK07656 256 I--TVLPG------PPTMYNSLL--QHPdrsaedlSSLRLAVTGAASMPVALLERFESElGVDiVLTGYGLSEASGVTTF 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 296 KEADGLAD-----VGSALPGREVRIVND-----------EVWLRAASMAQGYWRngqlMP-----LVNAEGWFATRDRGV 354
Cdd:PRK07656 326 NRLDDDRKtvagtIGTAIAGVENKIVNElgeevpvgevgELLVRGPNVMKGYYD----DPeataaAIDADGWLHTGDLGR 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 355 L-KDGKLTIVGRMDNLFFSGGEGIQPEEVERVIAAHPHVLQAFIVPIEDKEFGH--RPVAVVEYDANAGETNLAEWVKDK 431
Cdd:PRK07656 402 LdEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEvgKAYVVLKPGAELTEEELIAYCREH 481
|
490 500 510
....*....|....*....|....*....|..
gi 489936067 432 LARFQQP--VCWL-TLPpeLKAGGiKISRRAL 460
Cdd:PRK07656 482 LAKYKVPrsIEFLdELP--KNATG-KVLKRAL 510
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
33-460 |
4.60e-37 |
|
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: 141.13 E-value: 4.60e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 33 APALRLNDEALSWSELCARIDHLASGFAAQGVEEGD--GVL--------------LRAwnhprallawlallqcGARVLP 96
Cdd:cd05930 3 AVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDlvAVLlerslemvvailavLKA----------------GAAYVP 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 97 VNPQLPQSLLDALVpdltlrfaLDLEAAIALPElsplqmkslpgdhaaawlPERLSTMTLTSGSTGLPKAAVHTCQAHLA 176
Cdd:cd05930 67 LDPSYPAERLAYIL--------EDSGAKLVLTD------------------PDDLAYVIYTSGSTGKPKGVMVEHRGLVN 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 177 SAQGVLSLMPFGAEDDWL-LSLPLFHVSGQGILWrWLFAGA------RMTVRDKQPLDQMLA--GCTHASLVPTqLWRLL 247
Cdd:cd05930 121 LLLWMQEAYPLTPGDRVLqFTSFSFDVSVWEIFG-ALLAGAtlvvlpEEVRKDPEALADLLAeeGITVLHLTPS-LLRLL 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 248 VN----NTPVTLKAVLLGGAAIPVELTEQAREQGIRC--WCGYGLTE--FAST--VCAKEADGLADV--GSALPGREVRI 315
Cdd:cd05930 199 LQelelAALPSLRLVLVGGEALPPDLVRRWRELLPGArlVNLYGPTEatVDATyyRVPPDDEEDGRVpiGRPIPNTRVYV 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 316 VND-----------EVWLRAASMAQGYWRNGQLM-------PLVNAEGWFATRDRG-VLKDGKLTIVGRMDNLFFSGGEG 376
Cdd:cd05930 279 LDEnlrpvppgvpgELYIGGAGLARGYLNRPELTaerfvpnPFGPGERMYRTGDLVrWLPDGNLEFLGRIDDQVKIRGYR 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 377 IQPEEVERVIAAHPHVLQAFIVPIEDKEFGHRPVA--VVEYDANAGETNLAEWVKDKLARFQQPVCWLTLP--PeLKAGG 452
Cdd:cd05930 359 IELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAyvVPDEGGELDEEELRAHLAERLPDYMVPSAFVVLDalP-LTPNG 437
|
....*...
gi 489936067 453 iKISRRAL 460
Cdd:cd05930 438 -KVDRKAL 444
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
44-438 |
8.53e-36 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 137.42 E-value: 8.53e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 44 SWSELCARIDHLASGFAAQGVEEGDGVLLRAWNHPRALLAWLALLQCGARVLPVNPQLPQSLLDALVpdltlrfaldlea 123
Cdd:cd05934 5 TYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYII------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 124 aialpelsplqmkslpgDHA-AAWLPERLSTMTLTSGSTGLPKAAVHTCQAHLASAQGVLSLMPFGAEDDWLLSLPLFHV 202
Cdd:cd05934 72 -----------------DHSgAQLVVVDPASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGEDDVYLTVLPLFHI 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 203 SGQgiLWRWLFA---GARMTVRDK----QPLDQML-AGCTHASLVPTQLWRLLVnnTPV-------TLKAVllGGAAIPV 267
Cdd:cd05934 135 NAQ--AVSVLAAlsvGATLVLLPRfsasRFWSDVRrYGATVTNYLGAMLSYLLA--QPPspddrahRLRAA--YGAPNPP 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 268 ELTEQAREQ-GIRCWCGYGLTE----FASTVCAKEADGLAdvGSALPGREVRIVND-----------EVWLRAA---SMA 328
Cdd:cd05934 209 ELHEEFEERfGVRLLEGYGMTEtivgVIGPRDEPRRPGSI--GRPAPGYEVRIVDDdgqelpagepgELVIRGLrgwGFF 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 329 QGYWRngqlMPLVNAE----GWFATRDRGVL-KDGKLTIVGRMDNLFFSGGEGIQPEEVERVIAAHPHVLQAFIVPIEDk 403
Cdd:cd05934 287 KGYYN----MPEATAEamrnGWFHTGDLGYRdADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPD- 361
|
410 420 430
....*....|....*....|....*....|....*...
gi 489936067 404 EFGHRPVA---VVEYDANAGETNLAEWVKDKLARFQQP 438
Cdd:cd05934 362 EVGEDEVKavvVLRPGETLDPEELFAFCEGQLAYFKVP 399
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
42-413 |
3.48e-35 |
|
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: 135.97 E-value: 3.48e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 42 ALSWSELCARIDHLASGFAAQGVEEGDGVLLRAWNHPRALLAWLALLQCGARVLPVNPQLPQSlldalvpdlTLRFALDL 121
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREH---------ELAFILRR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 122 EAAIALpeLSPLQMKSLpgDHAAawLPERLSTMTLTSGSTGLPKAAVHTCQAHLASAQGVLSLMPFGAEDDWLLSLPLFH 201
Cdd:cd05903 72 AKAKVF--VVPERFRQF--DPAA--MPDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPGDVFLVASPMAH 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 202 VSGQ-GILWRWLFAGARMTVRDKQPLDQMLA-----GCTHASLVPTQLWRLL-----VNNTPVTLKAVLLGGAAIPVELT 270
Cdd:cd05903 146 QTGFvYGFTLPLLLGAPVVLQDIWDPDKALAlmrehGVTFMMGATPFLTDLLnaveeAGEPLSRLRTFVCGGATVPRSLA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 271 EQAREQGIRCWCG-YGLTEFASTVCAKEaDGLADV-----GSALPGREVRIVND-----------EVWLRAASMAQGYWR 333
Cdd:cd05903 226 RRAAELLGAKVCSaYGSTECPGAVTSIT-PAPEDRrlytdGRPLPGVEIKVVDDtgatlapgvegELLSRGPSVFLGYLD 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 334 NGQLMPLVNAEGWFATRDRGVL-KDGKLTIVGRMDNLFFSGGEGIQPEEVERVIAAHPHVLQAFIVPIEDKEFGHRPVAV 412
Cdd:cd05903 305 RPDLTADAAPEGWFRTGDLARLdEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAV 384
|
.
gi 489936067 413 V 413
Cdd:cd05903 385 V 385
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
31-462 |
9.15e-35 |
|
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: 135.52 E-value: 9.15e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 31 AKAPAL--RLNDEALSWSELCARIDHLASGFAAQGVEEGDGVLLRAWNHPRALLAWLALLQCGARVLPVNPQLPQSLLDA 108
Cdd:cd05926 1 PDAPALvvPGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 109 LVPDLTLRFAL--------DLEAA----IALPEL--------SPLQMKSLPG---DHAAAW-----LPERLSTMTLTSGS 160
Cdd:cd05926 81 YLADLGSKLVLtpkgelgpASRAAsklgLAILELaldvgvliRAPSAESLSNllaDKKNAKsegvpLPDDLALILHTSGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 161 TGLPKAAVHTCQAHLASAQGVLSLMPFGAEDDWLLSLPLFHVSGQ-GILWRWLFAGARMTVRDK-QPL---DQMLA-GCT 234
Cdd:cd05926 161 TGRPKGVPLTHRNLAASATNITNTYKLTPDDRTLVVMPLFHVHGLvASLLSTLAAGGSVVLPPRfSAStfwPDVRDyNAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 235 HASLVPTQLWRLLVN------NTPVTLKAVLLGGAAIPVELTEQAREQ-GIRCWCGYGLTEFASTVCAKEADGLAD---- 303
Cdd:cd05926 241 WYTAVPTIHQILLNRpepnpeSPPPKLRFIRSCSASLPPAVLEALEATfGAPVLEAYGMTEAAHQMTSNPLPPGPRkpgs 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 304 VGSALpGREVRIVND-----------EVWLRAASMAQGYWRNgqlmPLVNAE-----GWFATRDRGVLK-DGKLTIVGRM 366
Cdd:cd05926 321 VGKPV-GVEVRILDEdgeilppgvvgEICLRGPNVTRGYLNN----PEANAEaafkdGWFRTGDLGYLDaDGYLFLTGRI 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 367 DNLFFSGGEGIQPEEVERVIAAHPHVLQAFIVPIEDKEFGHRPVAVV--EYDANAGETNLAEWVKDKLARFQQPV-CWLT 443
Cdd:cd05926 396 KELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVvlREGASVTEEELRAFCRKHLAAFKVPKkVYFV 475
|
490 500
....*....|....*....|.
gi 489936067 444 --LPPelKAGGiKISRRALSD 462
Cdd:cd05926 476 deLPK--TATG-KIQRRKVAE 493
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
43-438 |
2.92e-34 |
|
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: 133.37 E-value: 2.92e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 43 LSWSELCARIDHLASGFAAQGVEEGDGVLLRAWNHPRALLAWLALLQCGARVLPVNPQLPQSLLDALVPDltlrfaLDLE 122
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILND------SGAK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 123 AAIALPELsplqmkslpgdhaaawlpERLSTMTLTSGSTGLPKAAVHTCQAHLASAQGVLSLMPFGAEDDWLLSLPLFHV 202
Cdd:cd05935 76 VAVVGSEL------------------DDLALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPSDVILACLPLFHV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 203 SG-QGILWRWLFAGAR---MTVRDKQPLDQMLA--GCTHASLVPTQLWRLLvnNTP-------VTLKAVLLGGAAIPVEL 269
Cdd:cd05935 138 TGfVGSLNTAVYVGGTyvlMARWDRETALELIEkyKVTFWTNIPTMLVDLL--ATPefktrdlSSLKVLTGGGAPMPPAV 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 270 TEQAREQ-GIRCWCGYGLTEFAS--TVCAKEADGLADVGSALPGREVRIVN------------DEVWLRAASMAQGYWRN 334
Cdd:cd05935 216 AEKLLKLtGLRFVEGYGLTETMSqtHTNPPLRPKLQCLGIP*FGVDARVIDietgrelppnevGEIVVRGPQIFKGYWNR 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 335 gqlmPLVNAEGW--------FATRDRGVL-KDGKLTIVGRMDNLFFSGGEGIQPEEVERVIAAHPHVLQAFIVPIEDKEF 405
Cdd:cd05935 296 ----PEETEESFieikgrrfFRTGDLGYMdEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERV 371
|
410 420 430
....*....|....*....|....*....|....*..
gi 489936067 406 GHRPVAVV----EYDANAGETNLAEWVKDKLARFQQP 438
Cdd:cd05935 372 GEEVKAFIvlrpEYRGKVTEEDIIEWAREQMAAYKYP 408
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
24-438 |
5.72e-33 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 131.44 E-value: 5.72e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 24 RHwRQVRAKAPALRLNDEALSWSELCARIDHLASGFAAQGVEEGDGVLLRAWNHPRALLAWLALLQCGARVLPVNPQLPQ 103
Cdd:PRK07786 25 RH-ALMQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 104 SLLDALVPDLTLRfALDLEA-----AIALPELSPL--------------------QMKSLPGDHAAAWLPERLSTMTL-T 157
Cdd:PRK07786 104 PEIAFLVSDCGAH-VVVTEAalapvATAVRDIVPLlstvvvaggssddsvlgyedLLAEAGPAHAPVDIPNDSPALIMyT 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 158 SGSTGLPKAAVHTcqaHL-ASAQGVLSLMPFGA---EDDWLLSLPLFHVSGQGILWRWLFAGARMTVRDKQPLD--QML- 230
Cdd:PRK07786 183 SGTTGRPKGAVLT---HAnLTGQAMTCLRTNGAdinSDVGFVGVPLFHIAGIGSMLPGLLLGAPTVIYPLGAFDpgQLLd 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 231 ----AGCTHASLVPTQLWRLLVNNTP----VTLKAVLLGGAAIPVELTEQAREQ--GIRCWCGYGLTEFASTVCAKEADG 300
Cdd:PRK07786 260 vleaEKVTGIFLVPAQWQAVCAEQQArprdLALRVLSWGAAPASDTLLRQMAATfpEAQILAAFGQTEMSPVTCMLLGED 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 301 ----LADVGSALPGREVRIVND-----------EVWLRAASMAQGYWRNGQLMPLVNAEGWFATRD--RgVLKDGKLTIV 363
Cdd:PRK07786 340 airkLGSVGKVIPTVAARVVDEnmndvpvgevgEIVYRAPTLMSGYWNNPEATAEAFAGGWFHSGDlvR-QDEEGYVWVV 418
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489936067 364 GRMDNLFFSGGEGIQPEEVERVIAAHPHVLQAFIVPIEDKEFGHRPVAVVEYDANAGE---TNLAEWVKDKLARFQQP 438
Cdd:PRK07786 419 DRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRNDDAAltlEDLAEFLTDRLARYKHP 496
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
44-466 |
6.14e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 130.31 E-value: 6.14e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 44 SWSELCARIDHLASGFAAQGVEEGDGVLLRAWNHPRALLAWLALLQCGARVLPVNPQLPQSLLDALVPDLTLRFAL-DLE 122
Cdd:PRK09088 24 TYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLLLgDDA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 123 AAIALPELSPL-----QMKSLPGDHAAAWLPERLSTMTLTSGSTGLPKAAVHTCQAHLASAQGVLSLMPFGAEDDWLLSL 197
Cdd:PRK09088 104 VAAGRTDVEDLaafiaSADALEPADTPSIPPERVSLILFTSGTSGQPKGVMLSERNLQQTAHNFGVLGRVDAHSSFLCDA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 198 PLFHVSGQGILWR-WLFAGARMTVRD----KQPL----DQMLaGCTHASLVPtQLWRLLVNNTPV------TLKAVLLGG 262
Cdd:PRK09088 184 PMFHIIGLITSVRpVLAVGGSILVSNgfepKRTLgrlgDPAL-GITHYFCVP-QMAQAFRAQPGFdaaalrHLTALFTGG 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 263 AAIPVELTEQAREQGIRCWCGYGLTEfASTV------CAKEADGLADVGSALPGREVRIVND-----------EVWLRAA 325
Cdd:PRK09088 262 APHAAEDILGWLDDGIPMVDGFGMSE-AGTVfgmsvdCDVIRAKAGAAGIPTPTVQTRVVDDqgndcpagvpgELLLRGP 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 326 SMAQGYWRNGQLMPLV-NAEGWFATRDRGVLK-DGKLTIVGRMDNLFFSGGEGIQPEEVERVIAAHPHVLQAFIVPIEDK 403
Cdd:PRK09088 341 NLSPGYWRRPQATARAfTGDGWFRTGDIARRDaDGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADA 420
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489936067 404 EFGHRPVAVVEYdANAGETNLAE---WVKDKLARFQQPVCWLTLPPELKAGGIKISRRALSDWVSA 466
Cdd:PRK09088 421 QWGEVGYLAIVP-ADGAPLDLERirsHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARLRDALAA 485
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
23-398 |
2.49e-32 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 129.84 E-value: 2.49e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 23 WRHWRQVRAKAPALRLND----EALSWSELCARIDHLASGFAAQGVEEGDGVLLRAWNHPRALLAWLALLQCGARVLPVN 98
Cdd:COG1022 17 LRRRAARFPDRVALREKEdgiwQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVPIY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 99 PQLP--------------------QSLLDAL------VPDLTLRFALDLEAAIALPELSPL-QMKSLPGDHA-------- 143
Cdd:COG1022 97 PTSSaeevayilndsgakvlfvedQEQLDKLlevrdeLPSLRHIVVLDPRGLRDDPRLLSLdELLALGREVAdpaelear 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 144 -AAWLPERLSTMTLTSGSTGLPKAAVHTCQAHLASAQGVLSLMPFGAEDDWLLSLPLFHVSGQGI--------------- 207
Cdd:COG1022 177 rAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFLPLAHVFERTVsyyalaagatvafae 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 208 ----------------------LWRWLFAGARMTVRDKQPLDQML----------------AGCTHASL--VPTQLWRLL 247
Cdd:COG1022 257 spdtlaedlrevkptfmlavprVWEKVYAGIQAKAEEAGGLKRKLfrwalavgrryararlAGKSPSLLlrLKHALADKL 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 248 V---------NNtpvtLKAVLLGGAAIPVELTEQAREQGIRCWCGYGLTEFASTVCAKEADG--LADVGSALPGREVRIV 316
Cdd:COG1022 337 VfsklrealgGR----LRFAVSGGAALGPELARFFRALGIPVLEGYGLTETSPVITVNRPGDnrIGTVGPPLPGVEVKIA 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 317 ND-EVWLRAASMAQGYWRNgqlmP-----LVNAEGWFATRDRGVL-KDGKLTIVGRMDNLFF-SGGEGIQPEEVERVIAA 388
Cdd:COG1022 413 EDgEILVRGPNVMKGYYKN----PeataeAFDADGWLHTGDIGELdEDGFLRITGRKKDLIVtSGGKNVAPQPIENALKA 488
|
490
....*....|
gi 489936067 389 HPHVLQAFIV 398
Cdd:COG1022 489 SPLIEQAVVV 498
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
35-457 |
7.94e-32 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 127.28 E-value: 7.94e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 35 ALRLNDEALSWSELCARIDHLASGFAAQ-GVEEGDGVLLRAWNHPRALLAWLALLQCGARVLPVNPQLPQSLLDALVPDL 113
Cdd:PRK06839 20 AIITEEEEMTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 114 -TLRFALDLEAAIALPELS-------PLQMKSLPG--DHAAAWLPERLSTMTL----TSGSTGLPKAAVHTCQAHLASAQ 179
Cdd:PRK06839 100 gTTVLFVEKTFQNMALSMQkvsyvqrVISITSLKEieDRKIDNFVEKNESASFiicyTSGTTGKPKGAVLTQENMFWNAL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 180 GVLSLMPFGAEDDWLLSLPLFHVSGQGIL-WRWLFAGARMTVRDKQPLDQMLA-----GCTHASLVPTQLWRLLvnNTPV 253
Cdd:PRK06839 180 NNTFAIDLTMHDRSIVLLPLFHIGGIGLFaFPTLFAGGVIIVPRKFEPTKALSmiekhKVTVVMGVPTIHQALI--NCSK 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 254 TLKAVLL-------GGAAIPVELTEQAREQGIRCWCGYGLTEFASTV--CAKE--ADGLADVGSALPGREVRIVND---- 318
Cdd:PRK06839 258 FETTNLQsvrwfynGGAPCPEELMREFIDRGFLFGQGFGMTETSPTVfmLSEEdaRRKVGSIGKPVLFCDYELIDEnknk 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 319 -------EVWLRAASMAQGYWRNGQLMPLVNAEGWFATRDRG-VLKDGKLTIVGRMDNLFFSGGEGIQPEEVERVIAAHP 390
Cdd:PRK06839 338 vevgevgELLIRGPNVMKEYWNRPDATEETIQDGWLCTGDLArVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLS 417
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489936067 391 HVLQAFIVPIEDKEFGHRPVA--VVEYDANAGETNLAEWVKDKLARFQQP--VCWLTLPPELKAGGIKISR 457
Cdd:PRK06839 418 DVYEVAVVGRQHVKWGEIPIAfiVKKSSSVLIEKDVIEHCRLFLAKYKIPkeIVFLKELPKNATGKIQKAQ 488
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
24-460 |
1.35e-31 |
|
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: 126.71 E-value: 1.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 24 RHWRQVRAKAPALRLNDEALSWSELCARIDHLASGFAAQGVEEGDGVLL----------------RAWNHPRALLAWLAL 87
Cdd:cd05959 11 LNLNEGRGDKTAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLimldtvdfptaflgaiRAGIVPVPVNTLLTP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 88 LQ-------CGARVLPVNPQLPQSLLDALVPDLTLRFALDLEAAiALPELSPLQMKSLPGDHA-----AAWLPERLSTMT 155
Cdd:cd05959 91 DDyayyledSRARVVVVSGELAPVLAAALTKSEHTLVVLIVSGG-AGPEAGALLLAELVAAEAeqlkpAATHADDPAFWL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 156 LTSGSTGLPKAAVHTcQAHLAS-----AQGVLSLmpfgAEDDWLLSLP-LFHVSGQG-ILWRWLFAGARMTVRDKQP--- 225
Cdd:cd05959 170 YSSGSTGRPKGVVHL-HADIYWtaelyARNVLGI----REDDVCFSAAkLFFAYGLGnSLTFPLSVGATTVLMPERPtpa 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 226 --LDQMLAGctHASL---VPTQLWRLLVNNTP-----VTLKAVLLGGAAIPVELTEQAREQ-GIRCWCGYGLTEFASTVC 294
Cdd:cd05959 245 avFKRIRRY--RPTVffgVPTLYAAMLAAPNLpsrdlSSLRLCVSAGEALPAEVGERWKARfGLDILDGIGSTEMLHIFL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 295 AKEADGL--ADVGSALPGREVRIVND-----------EVWLRAASMAQGYWRNGQLMPLVNAEGWFATRDRGV-LKDGKL 360
Cdd:cd05959 323 SNRPGRVryGTTGKPVPGYEVELRDEdggdvadgepgELYVRGPSSATMYWNNRDKTRDTFQGEWTRTGDKYVrDDDGFY 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 361 TIVGRMDNLFFSGGEGIQPEEVERVIAAHPHVLQAFIVPIEDKEFGHRPVAVV----EYDANAG-ETNLAEWVKDKLARF 435
Cdd:cd05959 403 TYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVvlrpGYEDSEAlEEELKEFVKDRLAPY 482
|
490 500
....*....|....*....|....*.
gi 489936067 436 QQPVcWLTLPPEL-KAGGIKISRRAL 460
Cdd:cd05959 483 KYPR-WIVFVDELpKTATGKIQRFKL 507
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
27-460 |
2.32e-30 |
|
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: 123.08 E-value: 2.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 27 RQVRAK--APALRLNDEALSWSELCARIDHLASGFAAQGVEEGDGVLLRAWNHPRALLAWLALLQCGARVLPVNPQLPQS 104
Cdd:cd12117 5 EQAARTpdAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 105 LLDALVPDLTLRFALD---LEAAIALPELSPLQMKSLPGDHAAAWL----PERLSTMTLTSGSTGLPKAAvhtcqahLAS 177
Cdd:cd12117 85 RLAFMLADAGAKVLLTdrsLAGRAGGLEVAVVIDEALDAGPAGNPAvpvsPDDLAYVMYTSGSTGRPKGV-------AVT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 178 AQGVLSL------MPFGAEDDWLLSLPL-FHVSGQGIlWRWLFAGARMTVRDKQPLDQMLA--------GCThASLVPTQ 242
Cdd:cd12117 158 HRGVVRLvkntnyVTLGPDDRVLQTSPLaFDASTFEI-WGALLNGARLVLAPKGTLLDPDAlgaliaeeGVT-VLWLTAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 243 LWRLLVNNTP---VTLKAVLLGGAAIPVELTEQAREQ--GIRCWCGYGLTE---FASTVCAKEADGLAD---VGSALPGR 311
Cdd:cd12117 236 LFNQLADEDPecfAGLRELLTGGEVVSPPHVRRVLAAcpGLRLVNGYGPTEnttFTTSHVVTELDEVAGsipIGRPIANT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 312 EVRIVND-----------EVWLRAASMAQGYWRNGQL-------MPLVNAEGWFATRDR-GVLKDGKLTIVGRMDNLFFS 372
Cdd:cd12117 316 RVYVLDEdgrpvppgvpgELYVGGDGLALGYLNRPALtaerfvaDPFGPGERLYRTGDLaRWLPDGRLEFLGRIDDQVKI 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 373 GGEGIQPEEVERVIAAHPHVLQAFIVPIEDKEFGHRPVAVVEYDANAGETNLAEWVKDKLARFQQPVCWL---TLPpeLK 449
Cdd:cd12117 396 RGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVVAEGALDAAELRAFLRERLPAYMVPAAFVvldELP--LT 473
|
490
....*....|.
gi 489936067 450 AGGiKISRRAL 460
Cdd:cd12117 474 ANG-KVDRRAL 483
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
43-438 |
3.87e-30 |
|
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: 122.41 E-value: 3.87e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 43 LSWSELCARIDHLASGFAAQGVEEGDGVLLRAWNHPRALLAWLALLQCGARVLPVNPQLpqsllDALvpdlTLRFALDLE 122
Cdd:cd12118 30 YTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRL-----DAE----EIAFILRHS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 123 AAIALPELSPLQMKSL--PGDHAAAWLP--ERLSTMTL--TSGSTGLPKAAVHTCQ-AHLASAQGVLSlmpFGAEDD--W 193
Cdd:cd12118 101 EAKVLFVDREFEYEDLlaEGDPDFEWIPpaDEWDPIALnyTSGTTGRPKGVVYHHRgAYLNALANILE---WEMKQHpvY 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 194 LLSLPLFHVSGQGILWRWLFAGA-----RmTVRDKQPLDQM-LAGCTHASLVPTQLwRLLVNNTPVTLKA------VLLG 261
Cdd:cd12118 178 LWTLPMFHCNGWCFPWTVAAVGGtnvclR-KVDAKAIYDLIeKHKVTHFCGAPTVL-NMLANAPPSDARPlphrvhVMTA 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 262 GAAIPVELTEQAREQGIRCWCGYGLTEFA--STVCAK--EADGL-ADVGSALPGR---------EVRIVND--------- 318
Cdd:cd12118 256 GAPPPAAVLAKMEELGFDVTHVYGLTETYgpATVCAWkpEWDELpTEERARLKARqgvryvgleEVDVLDPetmkpvprd 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 319 -----EVWLRAASMAQGYWRNgqlmPLVNAE----GWFATRDRGVLK-DGKLTIVGRMDNLFFSGGEGIQPEEVERVIAA 388
Cdd:cd12118 336 gktigEIVFRGNIVMKGYLKN----PEATAEafrgGWFHSGDLAVIHpDGYIEIKDRSKDIIISGGENISSVEVEGVLYK 411
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 489936067 389 HPHVLQAFIVPIEDKEFGHRPVAVVEY--DANAGETNLAEWVKDKLARFQQP 438
Cdd:cd12118 412 HPAVLEAAVVARPDEKWGEVPCAFVELkeGAKVTEEEIIAFCREHLAGFMVP 463
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
27-460 |
8.84e-30 |
|
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: 121.23 E-value: 8.84e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 27 RQVRAK--APALRLNDEALSWSELCARIDHLASGFAAQGVEEGDGVLLRAWNHPRALLAWLALLQCGARVLPVNPQLPQS 104
Cdd:cd17646 6 EQAARTpdAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPAD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 105 LLDALVPDLTLRFALD-------LEAAIALPELSPLQMKSLPG-DHAAAWLPERLSTMTLTSGSTGLPKAAVHTcqaHLA 176
Cdd:cd17646 86 RLAYMLADAGPAVVLTtadlaarLPAGGDVALLGDEALAAPPAtPPLVPPRPDNLAYVIYTSGSTGRPKGVMVT---HAG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 177 SAQGVLSL---MPFGAEDDWLLSLPL-FHVSGQGILWRwLFAGARMTV------RDKQPLDQMLA--GCTHASLVPTQLW 244
Cdd:cd17646 163 IVNRLLWMqdeYPLGPGDRVLQKTPLsFDVSVWELFWP-LVAGARLVVarpgghRDPAYLAALIRehGVTTCHFVPSMLR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 245 RLLVNNTP---VTLKAVLLGGAAIPVELTEQAREQ-GIRCWCGYGLTEFASTVCAKEADGLAD-----VGSALPGREVRI 315
Cdd:cd17646 242 VFLAEPAAgscASLRRVFCSGEALPPELAARFLALpGAELHNLYGPTEAAIDVTHWPVRGPAEtpsvpIGRPVPNTRLYV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 316 VND-----------EVWLRAASMAQGYWRNGQLM-------PLVNAEGWFATRDRG-VLKDGKLTIVGRMDNLFFSGGEG 376
Cdd:cd17646 322 LDDalrpvpvgvpgELYLGGVQLARGYLGRPALTaerfvpdPFGPGSRMYRTGDLArWRPDGALEFLGRSDDQVKIRGFR 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 377 IQPEEVERVIAAHPHVLQAFIVPIEDKEFGHRPVA--VVEYDANAGETN-LAEWVKDKLARFQQPVCWLTLP--PeLKAG 451
Cdd:cd17646 402 VEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGyvVPAAGAAGPDTAaLRAHLAERLPEYMVPAAFVVLDalP-LTAN 480
|
....*....
gi 489936067 452 GiKISRRAL 460
Cdd:cd17646 481 G-KLDRAAL 488
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
40-462 |
1.13e-29 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 121.79 E-value: 1.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 40 DEA--LSWSELCARIDHLASGFAAQGVEEGDGVLLRAWNHPRALLAWLALLQCGARVLPVN-----PQLPQSL----LDA 108
Cdd:PRK13382 64 DELgtLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNtsfagPALAEVVtregVDT 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 109 LVPD----LTLRFALD-------LEAAIALP-ELSPLQMKSLPGDHAAAWLPERLSTMTLTSGSTGLPKAAVHTCQAHLA 176
Cdd:PRK13382 144 VIYDeefsATVDRALAdcpqatrIVAWTDEDhDLTVEVLIAAHAGQRPEPTGRKGRVILLTSGTTGTPKGARRSGPGGIG 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 177 SAQGVLSLMPFGAEDDWLLSLPLFHVSGQGILwrwLFAGA---RMTVRDK-------QPLDQMLAgcTHASLVPTQLWRL 246
Cdd:PRK13382 224 TLKAILDRTPWRAEEPTVIVAPMFHAWGFSQL---VLAASlacTIVTRRRfdpeatlDLIDRHRA--TGLAVVPVMFDRI 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 247 L-----VNN--TPVTLKAVLLGGAAIPVELTEQAREQ-GIRCWCGYGLTEFASTVCAKEADGLA---DVGSALPGREVRI 315
Cdd:PRK13382 299 MdlpaeVRNrySGRSLRFAAASGSRMRPDVVIAFMDQfGDVIYNNYNATEAGMIATATPADLRAapdTAGRPAEGTEIRI 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 316 VNDE-----------VWLRAASMAQGYwRNGQLMPLVnaEGWFATRDRGVLKD-GKLTIVGRMDNLFFSGGEGIQPEEVE 383
Cdd:PRK13382 379 LDQDfrevptgevgtIFVRNDTQFDGY-TSGSTKDFH--DGFMASGDVGYLDEnGRLFVVGRDDEMIVSGGENVYPIEVE 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 384 RVIAAHPHVLQAFIVPIEDKEFGHRPVA--VVEYDANAGETNLAEWVKDKLARFQQPVcWLTLPPELKAGGI-KISRRAL 460
Cdd:PRK13382 456 KTLATHPDVAEAAVIGVDDEQYGQRLAAfvVLKPGASATPETLKQHVRDNLANYKVPR-DIVVLDELPRGATgKILRREL 534
|
..
gi 489936067 461 SD 462
Cdd:PRK13382 535 QA 536
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
33-460 |
5.80e-29 |
|
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: 118.93 E-value: 5.80e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 33 APALRLNDEALSWSELCARIDHLASGFAAQGVEEGDGVLLRAWNHPRALLAWLALLQCGARVLPVNPQLP----QSLLDA 108
Cdd:cd12116 3 ATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPadrlRYILED 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 109 LVPDLTLRFALDLEAAIALPELSPLQMKSLPGDHAAAW---LPERLSTMTLTSGSTGLPKaAVHTCQAHLAS-AQGVLSL 184
Cdd:cd12116 83 AEPALVLTDDALPDRLPAGLPVLLLALAAAAAAPAAPRtpvSPDDLAYVIYTSGSTGRPK-GVVVSHRNLVNfLHSMRER 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 185 MPFGAEDDWL-LSLPLFHVSGQGILWRwLFAGARM------TVRDKQPLDQMLA--GCTHASLVPTqLWRLLV-----NN 250
Cdd:cd12116 162 LGLGPGDRLLaVTTYAFDISLLELLLP-LLAGARVviapreTQRDPEALARLIEahSITVMQATPA-TWRMLLdagwqGR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 251 TPVTLkavLLGGAAIPVELTEQAREQGIRCWCGYGLTEFA--STVCA-KEADGLADVGSALPGREVRIVND--------- 318
Cdd:cd12116 240 AGLTA---LCGGEALPPDLAARLLSRVGSLWNLYGPTETTiwSTAARvTAAAGPIPIGRPLANTQVYVLDAalrpvppgv 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 319 --EVWLRAASMAQGYWRNGQL-----MPLVNAEG---WFATRDRGVLK-DGKLTIVGRMDNLFFSGGEGIQPEEVERVIA 387
Cdd:cd12116 317 pgELYIGGDGVAQGYLGRPALtaerfVPDPFAGPgsrLYRTGDLVRRRaDGRLEYLGRADGQVKIRGHRIELGEIEAALA 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489936067 388 AHPHVLQAFIVPIEDkEFGHRPVAVVEYDANAG--ETNLAEWVKDKLARFQQPVCWLTLP--PeLKAGGiKISRRAL 460
Cdd:cd12116 397 AHPGVAQAAVVVRED-GGDRRLVAYVVLKAGAApdAAALRAHLRATLPAYMVPSAFVRLDalP-LTANG-KLDRKAL 470
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
154-457 |
6.04e-29 |
|
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: 115.97 E-value: 6.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 154 MTLTSGSTGLPKAAVHTCQAHLASAQGVLSLMPFGAEDDWLLSLPLFHvsgQGILWRWLFA----GARMTVRDKQPLDQM 229
Cdd:cd17633 5 IGFTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSH---SLFLYGAISAlylgGTFIGQRKFNPKSWI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 230 LAGCTHAS----LVPTQLWRLLVNNTPVT-LKAVLLGGAAIPVELTEQAREQ--GIRCWCGYGLTE--FASTVCAKEADG 300
Cdd:cd17633 82 RKINQYNAtviyLVPTMLQALARTLEPESkIKSIFSSGQKLFESTKKKLKNIfpKANLIEFYGTSElsFITYNFNQESRP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 301 LADVGSALPGREVRIVNDE------VWLRAASMAQGYWRNGQlmplVNAEGWFATRDRGVLK-DGKLTIVGRMDNLFFSG 373
Cdd:cd17633 162 PNSVGRPFPNVEIEIRNADggeigkIFVKSEMVFSGYVRGGF----SNPDGWMSVGDIGYVDeEGYLYLVGRESDMIIIG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 374 GEGIQPEEVERVIAAHPHVLQAFIVPIEDKEFGHRPVAVVEYDaNAGETNLAEWVKDKLARFQQPVCWLTLP--PELKAG 451
Cdd:cd17633 238 GINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYSGD-KLTYKQLKRFLKQKLSRYEIPKKIIFVDslPYTSSG 316
|
....*.
gi 489936067 452 giKISR 457
Cdd:cd17633 317 --KIAR 320
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
153-438 |
1.88e-28 |
|
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: 115.45 E-value: 1.88e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 153 TMTLTSGSTGLPKAAVHTCQAHLASAQGVLSLMPFGAEDDWLLSLPLFHVSGQ--GILwRWLFAGARMTVRDKQ--PLDQ 228
Cdd:cd05917 6 NIQFTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLCIPVPLFHCFGSvlGVL-ACLTHGATMVFPSPSfdPLAV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 229 MLA----GCTHASLVPTQLWRLL-----VNNTPVTLKAVLLGGAAIPVELTEQAREQ-GIR-CWCGYGLTEfASTVC-AK 296
Cdd:cd05917 85 LEAiekeKCTALHGVPTMFIAELehpdfDKFDLSSLRTGIMAGAPCPPELMKRVIEVmNMKdVTIAYGMTE-TSPVStQT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 297 EADGLAD-----VGSALPGREVRIVND------------EVWLRAASMAQGYWRNGQLMPLV-NAEGWFATRDRGVL-KD 357
Cdd:cd05917 164 RTDDSIEkrvntVGRIMPHTEAKIVDPeggivppvgvpgELCIRGYSVMKGYWNDPEKTAEAiDGDGWLHTGDLAVMdED 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 358 GKLTIVGRMDNLFFSGGEGIQPEEVERVIAAHPHVLQAFIVPIEDKEFGHRPVAVV--EYDANAGETNLAEWVKDKLARF 435
Cdd:cd05917 244 GYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIrlKEGAELTEEDIKAYCKGKIAHY 323
|
...
gi 489936067 436 QQP 438
Cdd:cd05917 324 KVP 326
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
41-430 |
2.86e-28 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 118.13 E-value: 2.86e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 41 EALSWSELCARIDHLASGFAAQGVEEGDGVLLRAWNHPRALLAWLALLQCGArVLPVNPQL--PQ--SLLDA-------- 108
Cdd:PRK07529 57 ETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGEAAGI-ANPINPLLepEQiaELLRAagakvlvt 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 109 LVPDLTLRFALDLEAAIA-LPELSPL---------------------------------QMKSLPGDH---AAAWLPERL 151
Cdd:PRK07529 136 LGPFPGTDIWQKVAEVLAaLPELRTVvevdlarylpgpkrlavplirrkaharildfdaELARQPGDRlfsGRPIGPDDV 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 152 STMTLTSGSTGLPKAAVHTCQAHLASAQGVLSLMPFGAEDDWLLSLPLFHVSGQ-GILWRWLFAGARMTV------RDKQ 224
Cdd:PRK07529 216 AAYFHTGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPGDTVFCGLPLFHVNALlVTGLAPLARGAHVVLatpqgyRGPG 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 225 PLDQMLA-----GCTHASLVPTQLWRLLvnNTPV------TLKAVLLGGAAIPVELTEQAREQ-GIRCWCGYGLTEFAST 292
Cdd:PRK07529 296 VIANFWKiveryRINFLSGVPTVYAALL--QVPVdghdisSLRYALCGAAPLPVEVFRRFEAAtGVRIVEGYGLTEATCV 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 293 VCAKEADGLADVGSA---LPGREVRIVN-------------DEV---WLRAASMAQGYWRNGQLMPLVNAEGWFATRDRG 353
Cdd:PRK07529 374 SSVNPPDGERRIGSVglrLPYQRVRVVIlddagrylrdcavDEVgvlCIAGPNVFSGYLEAAHNKGLWLEDGWLNTGDLG 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 354 -VLKDGKLTIVGRMDNLFFSGGEGIQPEEVERVIAAHPHVLQAFIVPIEDKEFGHRPVAVVEY--DANAGETNLAEWVKD 430
Cdd:PRK07529 454 rIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGELPVAYVQLkpGASATEAELLAFARD 533
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
26-438 |
3.06e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 116.91 E-value: 3.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 26 WRQVRAKAPALRLNDEALSWSELCARIDHLASGFAAQGVEEGDGVLLRAWNHPRALLAWLALLQCGARVLPVNPQLPQSL 105
Cdd:PRK06145 11 HARRTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 106 LDALVPDLTLRFAL---DLEAAIAL------------PELSPLQMKSLPGDHAAAWLPERLSTMTLTSGSTGLPKAAVHT 170
Cdd:PRK06145 91 VAYILGDAGAKLLLvdeEFDAIVALetpkividaaaqADSRRLAQGGLEIPPQAAVAPTDLVRLMYTSGTTDRPKGVMHS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 171 C-QAHLASAQGVLSLmPFGAEDDWLLSLPLFHVS-----GQGILWRwlfAGARMTVRDKQPlDQMLAGC-----THASLV 239
Cdd:PRK06145 171 YgNLHWKSIDHVIAL-GLTASERLLVVGPLYHVGafdlpGIAVLWV---GGTLRIHREFDP-EAVLAAIerhrlTCAWMA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 240 PTQLWRLLVNNTPV-----TLKAVLLGGAAIPVELTEQARE--QGIRCWCGYGLTEFAS----TVCAKEADGLADVGSAL 308
Cdd:PRK06145 246 PVMLSRVLTVPDRDrfdldSLAWCIGGGEKTPESRIRDFTRvfTRARYIDAYGLTETCSgdtlMEAGREIEKIGSTGRAL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 309 PGREVRI-----------VNDEVWLRAASMAQGYWRNGQLMPLVNAEGWFATRDRGVLKD-GKLTIVGRMDNLFFSGGEG 376
Cdd:PRK06145 326 AHVEIRIadgagrwlppnMKGEICMRGPKVTKGYWKDPEKTAEAFYGDWFRSGDVGYLDEeGFLYLTDRKKDMIISGGEN 405
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489936067 377 IQPEEVERVIAAHPHVLQAFIVPIEDKEFGHRPVAVVEYDANAGET--NLAEWVKDKLARFQQP 438
Cdd:PRK06145 406 IASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPGATLTleALDRHCRQRLASFKVP 469
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
33-413 |
4.03e-28 |
|
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: 116.95 E-value: 4.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 33 APAL--RLNDEALSWSELCARIDHLASGFAAQGVEEGDGVLLRAWNHPRALLAWLALLQCGARVLPVNPqlpqslldALV 110
Cdd:cd05904 21 RPALidAATGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANP--------LST 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 111 PDLTLRFALDLEAAIAL------PELSPLQ-----MKSLPGDHAAAWLPERLSTMTLT----------------SGSTGL 163
Cdd:cd05904 93 PAEIAKQVKDSGAKLAFttaelaEKLASLAlpvvlLDSAEFDSLSFSDLLFEADEAEPpvvvikqddvaallysSGTTGR 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 164 PKAAVHTCQAHLASAQGVLSLMP--FGAEDDWLLSLPLFHVSG-QGILWRWLFAGARMTVRDKQPLDQMLA-----GCTH 235
Cdd:cd05904 173 SKGVMLTHRNLIAMVAQFVAGEGsnSDSEDVFLCVLPMFHIYGlSSFALGLLRLGATVVVMPRFDLEELLAaieryKVTH 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 236 ASLVPTQLWRL----LVNNTPV-TLKAVLLGGAAIPVELTEQAREQ--GIRCWCGYGLTEF--ASTVCAKEADGLADVGS 306
Cdd:cd05904 253 LPVVPPIVLALvkspIVDKYDLsSLRQIMSGAAPLGKELIEAFRAKfpNVDLGQGYGMTEStgVVAMCFAPEKDRAKYGS 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 307 A---LPGREVRIVN------------DEVWLRAASMAQGYWRNGQ-LMPLVNAEGWFATRDRGVL-KDGKLTIVGRMDNL 369
Cdd:cd05904 333 VgrlVPNVEAKIVDpetgeslppnqtGELWIRGPSIMKGYLNNPEaTAATIDKEGWLHTGDLCYIdEDGYLFIVDRLKEL 412
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 489936067 370 FFSGGEGIQPEEVERVIAAHPHVLQAFIVPIEDKEFGHRPVAVV 413
Cdd:cd05904 413 IKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFV 456
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
34-438 |
7.08e-28 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 116.60 E-value: 7.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 34 PALRLNDEALSWSELCARIDHLAsGFAAQ--GVEEGDGVLLRAWNHPRALLAWLALLQCGARVLPVNPQL---------- 101
Cdd:PRK08314 27 TAIVFYGRAISYRELLEEAERLA-GYLQQecGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNreeelahyvt 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 102 ---------PQSLLDALVP---DLTLRF--------ALDLEAAIALPEL----SPLQMKSLPGDHA-----AAWL----- 147
Cdd:PRK08314 106 dsgarvaivGSELAPKVAPavgNLRLRHvivaqysdYLPAEPEIAVPAWlraePPLQALAPGGVVAwkealAAGLappph 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 148 ---PERLSTMTLTSGSTGLPKAAVHTCQAHLASAQGVLSLMPFGAEDDWLLSLPLFHVSG-QGILWRWLFAGAR---MTV 220
Cdd:PRK08314 186 tagPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVLPLFHVTGmVHSMNAPIYAGATvvlMPR 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 221 RDKQPLDQMLA--GCTHASLVPTQLWRLLVNntP-------VTLKAVLLGGAAIPVELTEQAREQ-GIRCWCGYGLTEFA 290
Cdd:PRK08314 266 WDREAAARLIEryRVTHWTNIPTMVVDFLAS--PglaerdlSSLRYIGGGGAAMPEAVAERLKELtGLDYVEGYGLTETM 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 291 STVCAKEAD--GLADVGSALPGREVRIVN------------DEVWLRAASMAQGYWRN-------------------GQL 337
Cdd:PRK08314 344 AQTHSNPPDrpKLQCLGIPTFGVDARVIDpetleelppgevGEIVVHGPQVFKGYWNRpeataeafieidgkrffrtGDL 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 338 mPLVNAEGWFATRDRgvLKdgkltivgRMDNlffSGGEGIQPEEVERVIAAHPHVLQAFIVPIEDKEFGHRPVAVV---- 413
Cdd:PRK08314 424 -GRMDEEGYFFITDR--LK--------RMIN---ASGFKVWPAEVENLLYKHPAIQEACVIATPDPRRGETVKAVVvlrp 489
|
490 500
....*....|....*....|....*
gi 489936067 414 EYDANAGETNLAEWVKDKLARFQQP 438
Cdd:PRK08314 490 EARGKTTEEEIIAWAREHMAAYKYP 514
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
34-460 |
1.41e-27 |
|
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: 114.48 E-value: 1.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 34 PALRLNDEALSWSELCARIDHLASGFAAQGVEEGDGVLLrawnhprallawlallqcgarVLPVNPQLPQSLLDALvpdl 113
Cdd:cd05919 2 TAFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLL---------------------LMLDSPELVQLFLGCL---- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 114 tlrfALDLEAAIALPELSPLQMKSLPGDHAAAWL---PERLSTMTLTSGSTGLPKAAVHTCQAHLASAQG----VLSLmp 186
Cdd:cd05919 57 ----ARGAIAVVINPLLHPDDYAYIARDCEARLVvtsADDIAYLLYSSGTTGPPKGVMHAHRDPLLFADAmareALGL-- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 187 fgAEDDWLLSLP-LFHVSGQG-ILWRWLFAGARMTVRDKQPL-DQMLAgcTHASLVPTQLW-------RLLV--NNTPVT 254
Cdd:cd05919 131 --TPGDRVFSSAkMFFGYGLGnSLWFPLAVGASAVLNPGWPTaERVLA--TLARFRPTVLYgvptfyaNLLDscAGSPDA 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 255 LKAVLL---GGAAIPVELTEQAREQ-GIRCWCGYGLTEFASTVCAKEADG--LADVGSALPGREVRIVNDE--------- 319
Cdd:cd05919 207 LRSLRLcvsAGEALPRGLGERWMEHfGGPILDGIGATEVGHIFLSNRPGAwrLGSTGRPVPGYEIRLVDEEghtippgee 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 320 --VWLRAASMAQGYWRNGQLMPLVNAEGWFATRDR-GVLKDGKLTIVGRMDNLFFSGGEGIQPEEVERVIAAHPHVLQAF 396
Cdd:cd05919 287 gdLLVRGPSAAVGYWNNPEKSRATFNGGWYRTGDKfCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAA 366
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 397 IVPIEDKEFGHRPVA-VVEYDANAGETNLAE----WVKDKLARFQQPVcWLTLPPEL-KAGGIKISRRAL 460
Cdd:cd05919 367 VVAVPESTGLSRLTAfVVLKSPAAPQESLARdihrHLLERLSAHKVPR-RIAFVDELpRTATGKLQRFKL 435
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
27-460 |
1.29e-26 |
|
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: 112.22 E-value: 1.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 27 RQVRAKAPALRLNDEALSWSELCARIDHLASGFAAQGVEEGDGVLLRAWNHPRALLAWLALLQCGARVLPVNPQLPQSLL 106
Cdd:cd05923 13 RAPDACAIADPARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAEL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 107 DALVPDLTLRFALDLEAA-----IALPELSPLQMKSLPGDHAA----------AWLPERLSTMTLTSGSTGLPKAAV--H 169
Cdd:cd05923 93 AELIERGEMTAAVIAVDAqvmdaIFQSGVRVLALSDLVGLGEPesagpliedpPREPEQPAFVFYTSGTTGLPKGAVipQ 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 170 TCQAHLASAQGVLSLMPFGAEDDWLLSLPLFHVSG-QGILWRWL-FAGARMTVRDKQPLDQML----AGCTHASLVPTQL 243
Cdd:cd05923 173 RAAESRVLFMSTQAGLRHGRHNVVLGLMPLYHVIGfFAVLVAALaLDGTYVVVEEFDPADALKlieqERVTSLFATPTHL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 244 WRLL--VNNTPVTLKA---VLLGGAAIPVELTEQAREqgirCWCG-----YGLTEFASTVCAKEADgladVGSAL-PG-- 310
Cdd:cd05923 253 DALAaaAEFAGLKLSSlrhVTFAGATMPDAVLERVNQ----HLPGekvniYGTTEAMNSLYMRDAR----TGTEMrPGff 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 311 REVRIVN------------DE----VWLRAASMAQGYWRNGQLMPLVNAEGWFATRDRGVLK-DGKLTIVGRMDNLFFSG 373
Cdd:cd05923 325 SEVRIVRiggspdealangEEgeliVAAAADAAFTGYLNQPEATAKKLQDGWYRTGDVGYVDpSGDVRILGRVDDMIISG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 374 GEGIQPEEVERVIAAHPHVLQAFIVPIEDKEFGHRPVA-VVEYDANAGETNLAEWVKD-KLARFQQPVCWLTLPPELKAG 451
Cdd:cd05923 405 GENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTAcVVPREGTLSADELDQFCRAsELADFKRPRRYFFLDELPKNA 484
|
....*....
gi 489936067 452 GIKISRRAL 460
Cdd:cd05923 485 MNKVLRRQL 493
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
33-460 |
1.67e-26 |
|
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: 111.19 E-value: 1.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 33 APALRLNDEALSWSELCARIDHLASGFAAQGV--EEGDGVLLrawnhPRALLAWLAL---LQCGARVLPVNPQLPQSLLD 107
Cdd:cd17652 3 APAVVFGDETLTYAELNARANRLARLLAARGVgpERLVALAL-----PRSAELVVAIlavLKAGAAYLPLDPAYPAERIA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 108 ALVPDltlrfaldleaaiALPELSPLQmkslpgdhaaawlPERLSTMTLTSGSTGLPKAAV--HTCQAHLASAQGvlSLM 185
Cdd:cd17652 78 YMLAD-------------ARPALLLTT-------------PDNLAYVIYTSGSTGRPKGVVvtHRGLANLAAAQI--AAF 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 186 PFGAEDDWL-LSLPLFHVSgqgiLWRW---LFAGARMTVRDK------QPLDQMLA--GCTHASLVPTQLWRLLVNNTPV 253
Cdd:cd17652 130 DVGPGSRVLqFASPSFDAS----VWELlmaLLAGATLVLAPAeellpgEPLADLLRehRITHVTLPPAALAALPPDDLPD 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 254 tLKAVLLGGAAIPVELTEQArEQGIRCWCGYGLTEfaSTVCAKEADGLAD-----VGSALPGREVRIVND---------- 318
Cdd:cd17652 206 -LRTLVVAGEACPAELVDRW-APGRRMINAYGPTE--TTVCATMAGPLPGggvppIGRPVPGTRVYVLDArlrpvppgvp 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 319 -EVWLRAASMAQGYWRNgqlmPLVNAEGWFA------------TRDRGVLK-DGKLTIVGRMDNLFFSGGEGIQPEEVER 384
Cdd:cd17652 282 gELYIAGAGLARGYLNR----PGLTAERFVAdpfgapgsrmyrTGDLARWRaDGQLEFLGRADDQVKIRGFRIELGEVEA 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 385 VIAAHPHVLQAFIVPIEDKEFGHRPVA--VVEYDANAGETNLAEWVKDKLARFQQPVCWLTLP--PeLKAGGiKISRRAL 460
Cdd:cd17652 358 ALTEHPGVAEAVVVVRDDRPGDKRLVAyvVPAPGAAPTAAELRAHLAERLPGYMVPAAFVVLDalP-LTPNG-KLDRRAL 435
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
30-431 |
1.86e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 112.00 E-value: 1.86e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 30 RAKAPALRLNDEALSWSELCARIDHLASGFAAQGVEEGDGVLLRAWNHPRALLAWLALLQCGARVLPVNP---------Q 100
Cdd:PRK06188 25 YPDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHPlgslddhayV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 101 LPQSLLDALVPD--------LTLR----------------FALDLEAAIALPELSPLQMKSLPGDhaaawlperLSTMTL 156
Cdd:PRK06188 105 LEDAGISTLIVDpapfveraLALLarvpslkhvltlgpvpDGVDLLAAAAKFGPAPLVAAALPPD---------IAGLAY 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 157 TSGSTGLPKAAVHTCQAHLASAQGVLSLMPFGAEDDWLLSLPLFHVSGQGILwRWLFAGARMTVRDKQPLDQMLA----- 231
Cdd:PRK06188 176 TGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLSHAGGAFFL-PTLLRGGTVIVLAKFDPAEVLRaieeq 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 232 GCTHASLVPTQLWRLLVNNTPVT-----LKAVLLGGAAI-PVELTEQAREQGIRCWCGYGLTEFASTVC--------AKE 297
Cdd:PRK06188 255 RITATFLVPTMIYALLDHPDLRTrdlssLETVYYGASPMsPVRLAEAIERFGPIFAQYYGQTEAPMVITylrkrdhdPDD 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 298 ADGLADVGSALPGREVRIVND-----------EVWLRAASMAQGYWRngqlMPLVNAE----GWF-----ATRDrgvlKD 357
Cdd:PRK06188 335 PKRLTSCGRPTPGLRVALLDEdgrevaqgevgEICVRGPLVMDGYWN----RPEETAEafrdGWLhtgdvARED----ED 406
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489936067 358 GKLTIVGRMDNLFFSGGEGIQPEEVERVIAAHPHVLQAFIVPIEDKEFGHRPVAVV--EYDANAGETNLAEWVKDK 431
Cdd:PRK06188 407 GFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVvlRPGAAVDAAELQAHVKER 482
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
28-438 |
3.05e-26 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 111.52 E-value: 3.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 28 QVRAKAPALRLNDE--ALSWSELCARIDHLASGFAAQGVEEGDGVLLRAWNHPRALLAWLALLQCGARVLPVNPQLPQS- 104
Cdd:PRK05852 27 TRLPEAPALVVTADriAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAe 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 105 -------------LLDALVP-----------DLTLRFALDLEAAIALPELSpLQMKSLPgdHAAAWLPERL----STMTL 156
Cdd:PRK05852 107 qrvrsqaagarvvLIDADGPhdraepttrwwPLTVNVGGDSGPSGGTLSVH-LDAATEP--TPATSTPEGLrpddAMIMF 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 157 TSGSTGLPKAAVHTCQAHLASAQGVLSLMPFGAEDDWLLSLPLFH------------VSGQGILwrwLFAGARMTVRDKQ 224
Cdd:PRK05852 184 TGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHghgliaallatlASGGAVL---LPARGRFSAHTFW 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 225 PlDQMLAGCTHASLVPTQLWRLL-------VNNTPVTLKAVLLGGAAIPVELTEQAREQ-GIRCWCGYGLTEFASTVCAK 296
Cdd:PRK05852 261 D-DIKAVGATWYTAVPTIHQILLeraatepSGRKPAALRFIRSCSAPLTAETAQALQTEfAAPVVCAFGMTEATHQVTTT 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 297 EADGLAD-----VGSALPGR----EVRIVND-----------EVWLRAASMAQGYWRNGQLMPLVNAEGWFATRDRGVLK 356
Cdd:PRK05852 340 QIEGIGQtenpvVSTGLVGRstgaQIRIVGSdglplpagavgEVWLRGTTVVRGYLGDPTITAANFTDGWLRTGDLGSLS 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 357 -DGKLTIVGRMDNLFFSGGEGIQPEEVERVIAAHPHVLQAFIVPIEDKEFGHRPVAVVEYDANAGET--NLAEWVKDKLA 433
Cdd:PRK05852 420 aAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIVPRESAPPTaeELVQFCRERLA 499
|
....*
gi 489936067 434 RFQQP 438
Cdd:PRK05852 500 AFEIP 504
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
151-438 |
3.18e-26 |
|
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: 108.74 E-value: 3.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 151 LSTMTLTSGSTGLPKAAVHTCQAHLASAQGVLSLMPFGAEDDWLLSLPLFHVSG--QGILwRWLFAGArmTVRDKQPLD- 227
Cdd:cd17638 2 VSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIINPFFHTFGykAGIV-ACLLTGA--TVVPVAVFDv 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 228 ------------QMLAGcthaslVPTQLWRLLV-----NNTPVTLKAVLLGGAAIPVELTEQAREQ-GIR-CWCGYGLTE 288
Cdd:cd17638 79 daileaiereriTVLPG------PPTLFQSLLDhpgrkKFDLSSLRAAVTGAATVPVELVRRMRSElGFEtVLTAYGLTE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 289 FASTVCAKEADGLADV----GSALPGREVRIVND-EVWLRAASMAQGYWRNGQLMP-LVNAEGWFATRDRGVLKD-GKLT 361
Cdd:cd17638 153 AGVATMCRPGDDAETVattcGRACPGFEVRIADDgEVLVRGYNVMQGYLDDPEATAeAIDADGWLHTGDVGELDErGYLR 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489936067 362 IVGRMDNLFFSGGEGIQPEEVERVIAAHPHVLQAFIVPIEDKEFGH--RPVAVVEYDANAGETNLAEWVKDKLARFQQP 438
Cdd:cd17638 233 ITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEvgKAFVVARPGVTLTEEDVIAWCRERLANYKVP 311
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
1-438 |
2.56e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 108.87 E-value: 2.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 1 MTQQERPDSVSLSGLIQpsdwpwRHWRQVRAKaPALRLNDEALSWSELCARIDHLASGFAAQGVEEGDGVLLRAWNHPRA 80
Cdd:PRK08316 2 MERSTRARRQTIGDILR------RSARRYPDK-TALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 81 LLAWLALLQCGARVLPVNPQLP---------QSLLDALVPDLTLRFALDLEAAIALPELSPLQMKSLPGDHAAAWLP--- 148
Cdd:PRK08316 75 ALLWLACARAGAVHVPVNFMLTgeelayildHSGARAFLVDPALAPTAEAALALLPVDTLILSLVLGGREAPGGWLDfad 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 149 ----------------ERLSTMTLTSGSTGLPKAAVHTCQAHLASAQGVLSLMPFGAEDDWLLSLPLFHvSGQ--GILWR 210
Cdd:PRK08316 155 waeagsvaepdveladDDLAQILYTSGTESLPKGAMLTHRALIAEYVSCIVAGDMSADDIPLHALPLYH-CAQldVFLGP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 211 WLFAGARMTVRDKQPLDQMLA-----GCTHASLVPTqLWRLLVNNtPV-------TLKAVLLGGAAIPVELTEQAREQ-- 276
Cdd:PRK08316 234 YLYVGATNVILDAPDPELILRtieaeRITSFFAPPT-VWISLLRH-PDfdtrdlsSLRKGYYGASIMPVEVLKELRERlp 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 277 GIRCWCGYGLTEFA--STVCAKEaDGLADVGSAlpGR-----EVRIVND-----------EVWLRAASMAQGYWRNGQLM 338
Cdd:PRK08316 312 GLRFYNCYGQTEIAplATVLGPE-EHLRRPGSA--GRpvlnvETRVVDDdgndvapgevgEIVHRSPQLMLGYWDDPEKT 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 339 PLVNAEGWFATRDRGVL-KDGKLTIVGRMDNLFFSGGEGIQPEEVERVIAAHPHVLQAFIVPIEDKEFGHRPVAVV--EY 415
Cdd:PRK08316 389 AEAFRGGWFHSGDLGVMdEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVvpKA 468
|
490 500
....*....|....*....|...
gi 489936067 416 DANAGETNLAEWVKDKLARFQQP 438
Cdd:PRK08316 469 GATVTEDELIAHCRARLAGFKVP 491
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
148-413 |
3.14e-25 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 108.60 E-value: 3.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 148 PERLSTMTLTSGSTGLPKAAVHTCQAHLASAQGVLSLMPFGAEDDWLLSLPLFHVSGQGILWRW-LFAGARMTVRDKQPL 226
Cdd:PRK13295 196 PDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILMASPMAHQTGFMYGLMMpVMLGATAVLQDIWDP 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 227 DQMLA-----GCTHaSLVPTQLWRLLVNN-----TPV-TLKAVLLGGAAIPVELTEQAREQ-GIRCWCGYGLTE--FAST 292
Cdd:PRK13295 276 ARAAElirteGVTF-TMASTPFLTDLTRAvkesgRPVsSLRTFLCAGAPIPGALVERARAAlGAKIVSAWGMTEngAVTL 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 293 VCAKEADGLADV--GSALPGREVRIVNDE-----------VWLRAASMAQGYWRNGQlMPLVNAEGWFATRDRG-VLKDG 358
Cdd:PRK13295 355 TKLDDPDERASTtdGCPLPGVEVRVVDADgaplpagqigrLQVRGCSNFGGYLKRPQ-LNGTDADGWFDTGDLArIDADG 433
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 489936067 359 KLTIVGRMDNLFFSGGEGIQPEEVERVIAAHPHVLQAFIVPIEDKEFGHRPVAVV 413
Cdd:PRK13295 434 YIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFV 488
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
154-464 |
4.69e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 107.56 E-value: 4.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 154 MTLTSGSTGLPKAAVHTCQAHLASAQGVLSLMPFGAEDDWLLSLPLFH-------VSGqgilwrwLFAGARMTVRDKQPL 226
Cdd:PRK07638 148 MGFTSGSTGKPKAFLRAQQSWLHSFDCNVHDFHMKREDSVLIAGTLVHslflygaIST-------LYVGQTVHLMRKFIP 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 227 DQMLAGCTHASL-----VPTQLWRLL-VNNTPVTLKAVLLGGAAIPVELTEQAREQ--GIRCWCGYGLTEFaSTVCAkea 298
Cdd:PRK07638 221 NQVLDKLETENIsvmytVPTMLESLYkENRVIENKMKIISSGAKWEAEAKEKIKNIfpYAKLYEFYGASEL-SFVTA--- 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 299 dgLADVGSALP----GR-----EVRIVN--------DE---VWLRAASMAQGYWRNGQLMPLVNAEGWFATRDRGVL-KD 357
Cdd:PRK07638 297 --LVDEESERRpnsvGRpfhnvQVRICNeageevqkGEigtVYVKSPQFFMGYIIGGVLARELNADGWMTVRDVGYEdEE 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 358 GKLTIVGRMDNLFFSGGEGIQPEEVERVIAAHPHVLQAFIVPIEDKEFGHRPVAVVEYDANAGEtnLAEWVKDKLARFQQ 437
Cdd:PRK07638 375 GFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAIIKGSATKQQ--LKSFCLQRLSSFKI 452
|
330 340
....*....|....*....|....*....
gi 489936067 438 PVCWLTLP--PELKAGgiKISRRALSDWV 464
Cdd:PRK07638 453 PKEWHFVDeiPYTNSG--KIARMEAKSWI 479
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
44-468 |
7.83e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 107.34 E-value: 7.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 44 SWSELCARIDHLASGFAAQGVEEGDGVLLRAWNHPRALLAWLALLQCGA-----------------------RVLPVNPQ 100
Cdd:PRK08162 45 TWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAvlntlntrldaasiafmlrhgeaKVLIVDTE 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 101 LPQSLLDAL----VPDLTL------------RF-ALDLEAAIAlpelsplqmkslPGDHAAAW-LPE---RLSTMTLTSG 159
Cdd:PRK08162 125 FAEVAREALallpGPKPLVidvddpeypggrFIgALDYEAFLA------------SGDPDFAWtLPAdewDAIALNYTSG 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 160 STGLPKAAV-HTCQAHLASAQGVLSL-MPFGAEddWLLSLPLFHVSGqgilwrWLF-------AGARMTVRDKQP---LD 227
Cdd:PRK08162 193 TTGNPKGVVyHHRGAYLNALSNILAWgMPKHPV--YLWTLPMFHCNG------WCFpwtvaarAGTNVCLRKVDPkliFD 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 228 QMLA-GCTHASLVPTQLWRLLvnNTPVTLKA-------VLLGGAAIPVELTEQAREQGIRCWCGYGLTEF--ASTVCAKE 297
Cdd:PRK08162 265 LIREhGVTHYCGAPIVLSALI--NAPAEWRAgidhpvhAMVAGAAPPAAVIAKMEEIGFDLTHVYGLTETygPATVCAWQ 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 298 A--DGLADVGSA-LPGRE-VR-------IVND---------------EVWLRAASMAQGYWRNGQLMPLVNAEGWFATRD 351
Cdd:PRK08162 343 PewDALPLDERAqLKARQgVRyplqegvTVLDpdtmqpvpadgetigEIMFRGNIVMKGYLKNPKATEEAFAGGWFHTGD 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 352 RGVL-KDGKLTIVGRMDNLFFSGGEGIQPEEVERVIAAHPHVLQAFIVPIEDKEFGHRPVAVVEY--DANAGETNLAEWV 428
Cdd:PRK08162 423 LAVLhPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDPKWGEVPCAFVELkdGASATEEEIIAHC 502
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 489936067 429 KDKLARFQQP--VCWLTLPpelKAGGIKISRRALSDWVSASS 468
Cdd:PRK08162 503 REHLAGFKVPkaVVFGELP---KTSTGKIQKFVLREQAKSLK 541
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
157-438 |
7.90e-25 |
|
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: 105.04 E-value: 7.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 157 TSGSTGLPKAAVHTCQAHLASAQGVLS-LMPFGAEDDWLLSLPLFHVSGqgiLWRWL----FAGARMTVRDKQPLDQMLA 231
Cdd:cd17635 9 TSGTTGEPKAVLLANKTFFAVPDILQKeGLNWVVGDVTYLPLPATHIGG---LWWILtcliHGGLCVTGGENTTYKSLFK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 232 -----GCTHASLVPTqLWRLLVNNTPVTLKAV-----LLGGAAIPVELTEQARE--QGIRCWCGYGLTEFASTVCAKEAD 299
Cdd:cd17635 86 ilttnAVTTTCLVPT-LLSKLVSELKSANATVpslrlIGYGGSRAIAADVRFIEatGLTNTAQVYGLSETGTALCLPTDD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 300 GLAD---VGSALPGREVRIVND-----------EVWLRAASMAQGYWRNGQLMPLVNAEGWFATRDRG-VLKDGKLTIVG 364
Cdd:cd17635 165 DSIEinaVGRPYPGVDVYLAATdgiagpsasfgTIWIKSPANMLGYWNNPERTAEVLIDGWVNTGDLGeRREDGFLFITG 244
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489936067 365 RMDNLFFSGGEGIQPEEVERVIAAHPHVLQAFIVPIEDKEFGHRPVAVV---EYDANAGETNLAEWVKDKLARFQQP 438
Cdd:cd17635 245 RSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVvasAELDENAIRALKHTIRRELEPYARP 321
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
43-438 |
8.55e-25 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 107.55 E-value: 8.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 43 LSWSELCARIDHLASGFAAQGVEEGDGVLLRAWNHPRALLAWLALLQCGARVLPVNPQ---------LPQS--------- 104
Cdd:PRK12583 46 YTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAyraseleyaLGQSgvrwvicad 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 105 ---------LLDALVPDLTLRFALDLEAAiALPELSPL-QMKSLPGDHAAAW----------LPERLST----------- 153
Cdd:PRK12583 126 afktsdyhaMLQELLPGLAEGQPGALACE-RLPELRGVvSLAPAPPPGFLAWhelqargetvSREALAErqasldrddpi 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 154 -MTLTSGSTGLPKAAVHTCQAHLASAQGVLSLMPFGAEDDWLLSLPLFHVSGQgILWRW--LFAGARMTVRDK--QPLDQ 228
Cdd:PRK12583 205 nIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCVPVPLYHCFGM-VLANLgcMTVGACLVYPNEafDPLAT 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 229 MLA----GCTHASLVPTQLWRLL-----VNNTPVTLKAVLLGGAAIPVELTEQAREQgIRC---WCGYGLTEfASTVCAK 296
Cdd:PRK12583 284 LQAveeeRCTALYGVPTMFIAELdhpqrGNFDLSSLRTGIMAGAPCPIEVMRRVMDE-MHMaevQIAYGMTE-TSPVSLQ 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 297 E--ADGL----ADVGSALPGREVRIVND-----------EVWLRAASMAQGYWRNGQLMPL-VNAEGWFATRDRGVL-KD 357
Cdd:PRK12583 362 TtaADDLerrvETVGRTQPHLEVKVVDPdgatvprgeigELCTRGYSVMKGYWNNPEATAEsIDEDGWMHTGDLATMdEQ 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 358 GKLTIVGRMDNLFFSGGEGIQPEEVERVIAAHPHVLQAFIVPIEDKEFGHRPVAVV--EYDANAGETNLAEWVKDKLARF 435
Cdd:PRK12583 442 GYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVrlHPGHAASEEELREFCKARIAHF 521
|
...
gi 489936067 436 QQP 438
Cdd:PRK12583 522 KVP 524
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
34-462 |
1.32e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 106.66 E-value: 1.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 34 PALRLNDEALSWSELCARIDHLASGFAAQGVEEGDGVLLRAWNHPRALLAWLALLQCGARVLPVN-PQLPQ--------- 103
Cdd:PRK07470 24 IALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNfRQTPDevaylaeas 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 104 ---------------SLLDALVPDLTL-------RFALDLEAAIALPELSPLQMKSLPGDHAAaWLperlstmTLTSGST 161
Cdd:PRK07470 104 garamichadfpehaAAVRAASPDLTHvvaiggaRAGLDYEALVARHLGARVANAAVDHDDPC-WF-------FFTSGTT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 162 GLPKAAVHT-------CQAHLASaqgvlsLMPFGAEDDW-LLSLPLFHvsGQGIlwRWLFAGAR-----MTVRDKQPLDQ 228
Cdd:PRK07470 176 GRPKAAVLThgqmafvITNHLAD------LMPGTTEQDAsLVVAPLSH--GAGI--HQLCQVARgaatvLLPSERFDPAE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 229 MLA-----GCTHASLVPTQLwRLLVNNTPV------TLKAVLLGGAAIPVELTEQAREQ-GIRCWCGYGLTEFASTV--- 293
Cdd:PRK07470 246 VWAlverhRVTNLFTVPTIL-KMLVEHPAVdrydhsSLRYVIYAGAPMYRADQKRALAKlGKVLVQYFGLGEVTGNItvl 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 294 --CAKEADGLADV-----GSALPGREVRIVND-----------EVWLRAASMAQGYWRNgqlmPLVNAE----GWFATRD 351
Cdd:PRK07470 325 ppALHDAEDGPDArigtcGFERTGMEVQIQDDegrelppgetgEICVIGPAVFAGYYNN----PEANAKafrdGWFRTGD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 352 RGVL-KDGKLTIVGRMDNLFFSGGEGIQPEEVERVIAAHPHVLQAFIVPIEDKEFGHRPVAVV--EYDANAGETNLAEWV 428
Cdd:PRK07470 401 LGHLdARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCvaRDGAPVDEAELLAWL 480
|
490 500 510
....*....|....*....|....*....|....*..
gi 489936067 429 KDKLARFQQP---VCWLTLPpelKAGGIKISRRALSD 462
Cdd:PRK07470 481 DGKVARYKLPkrfFFWDALP---KSGYGKITKKMVRE 514
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
59-462 |
1.36e-24 |
|
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: 105.92 E-value: 1.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 59 FAAQGVEEGDGVLLRAWNH---PRALLAWLALLQCGARVLPVNPQ-----LPQSLLDALVPDL-TLRFALD-LEAAIALP 128
Cdd:cd05929 34 AAAEGVWIADGVYIYLINSiltVFAAAAAWKCGACPAYKSSRAPRaeacaIIEIKAAALVCGLfTGGGALDgLEDYEAAE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 129 ELSPlqmKSLPGDHAAAWLperlstMTLTSGSTGLPKA------AVHTCQAHLASAQGvlsLMPFGAEDDWLLSLPLFHV 202
Cdd:cd05929 114 GGSP---ETPIEDEAAGWK------MLYSGGTTGRPKGikrglpGGPPDNDTLMAAAL---GFGPGADSVYLSPAPLYHA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 203 SGQGILWRWLFAGARMTVRDKQPLDQMLA-----GCTHASLVPTQLWRLLVNNTPV-------TLKAVLLGGAAIPVELT 270
Cdd:cd05929 182 APFRWSMTALFMGGTLVLMEKFDPEEFLRlieryRVTFAQFVPTMFVRLLKLPEAVrnaydlsSLKRVIHAAAPCPPWVK 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 271 EQARE-QGIRCWCGYGLTE-FASTVCAKEaDGLA---DVGSALPGrEVRIVND-----------EVWLRAASMAQGYWRN 334
Cdd:cd05929 262 EQWIDwGGPIIWEYYGGTEgQGLTIINGE-EWLThpgSVGRAVLG-KVHILDEdgnevppgeigEVYFANGPGFEYTNDP 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 335 GQLMPLVNAEGWFATRDRGVL-KDGKLTIVGRMDNLFFSGGEGIQPEEVERVIAAHPHVLQAFIVPIEDKEFGHRPVAVV 413
Cdd:cd05929 340 EKTAAARNEGGWSTLGDVGYLdEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVV 419
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 489936067 414 E-------YDANAGEtnLAEWVKDKLARFQQP--VCWLTLPPELKAGgiKISRRALSD 462
Cdd:cd05929 420 QpapgadaGTALAEE--LIAFLRDRLSRYKCPrsIEFVAELPRDDTG--KLYRRLLRD 473
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
30-438 |
1.63e-24 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 106.11 E-value: 1.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 30 RAKAPALRLND-EALSWSELCARIDHLASGFAAQGVEEGDGVLLRAWNHPRALLAWLALLQCGARVLPVNPQLPQSLLDa 108
Cdd:PRK07514 15 DRDAPFIETPDgLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELD- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 109 lvpdltlRFALDLEAAI------ALPELSPL-------QMKSLPGD------HAAAWLPER----------LSTMTLTSG 159
Cdd:PRK07514 94 -------YFIGDAEPALvvcdpaNFAWLSKIaaaagapHVETLDADgtgsllEAAAAAPDDfetvprgaddLAAILYTSG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 160 STGLPKAAVHTcQAHLAS-AQGVLSLMPFGAEDDWLLSLPLFHVSG-----QGILwrwlFAGARMTVRDKQPLDQMLAGC 233
Cdd:PRK07514 167 TTGRSKGAMLS-HGNLLSnALTLVDYWRFTPDDVLIHALPIFHTHGlfvatNVAL----LAGASMIFLPKFDPDAVLALM 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 234 THASL---VPTQLWRLLVNN--TPVTLKAVLL---GGAAIPVELTEQAREQ-GIRCWCGYGLTE---FASTVCAKEADGl 301
Cdd:PRK07514 242 PRATVmmgVPTFYTRLLQEPrlTREAAAHMRLfisGSAPLLAETHREFQERtGHAILERYGMTEtnmNTSNPYDGERRA- 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 302 ADVGSALPGREVRIVNDE------------VWLRAASMAQGYWRngqlMPLVNAE-----GWFATRDRGVL-KDGKLTIV 363
Cdd:PRK07514 321 GTVGFPLPGVSLRVTDPEtgaelppgeigmIEVKGPNVFKGYWR----MPEKTAEefradGFFITGDLGKIdERGYVHIV 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489936067 364 GRMDNLFFSGGEGIQPEEVERVIAAHPHVLQAFIVPIEDKEFGHRPVAVVEYDANAG--ETNLAEWVKDKLARFQQP 438
Cdd:PRK07514 397 GRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKPGAAldEAAILAALKGRLARFKQP 473
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
36-404 |
2.38e-24 |
|
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: 105.22 E-value: 2.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 36 LRLNDEALSWSELCARIDHLASGFAAQGVEEGDGVLLRAWNHPRALLAWLALLQCGARVLPVnpqLPQSLLDALvpdltl 115
Cdd:cd05914 1 LYYGGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPI---LAEFTADEV------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 116 RFALDLEAAIALpelsplqmksLPGDhaaawlPERLSTMTLTSGSTGLPKAAVHTCQAHLASAQGVLSLMPFGAEDDWLL 195
Cdd:cd05914 72 HHILNHSEAKAI----------FVSD------EDDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLLGKGDKILS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 196 SLPLFHVSG-QGILWRWLFAGARMTVRDKQPLDQMLA------GCTHASLVPTQL------------------WRLL--V 248
Cdd:cd05914 136 ILPLHHIYPlTFTLLLPLLNGAHVVFLDKIPSAKIIAlafaqvTPTLGVPVPLVIekifkmdiipkltlkkfkFKLAkkI 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 249 NNTPVT--------------LKAVLLGGAAIPVELTEQAREQGIRCWCGYGLTEFASTVC--AKEADGLADVGSALPGRE 312
Cdd:cd05914 216 NNRKIRklafkkvheafggnIKEFVIGGAKINPDVEEFLRTIGFPYTIGYGMTETAPIISysPPNRIRLGSAGKVIDGVE 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 313 VRIVND-------EVWLRAASMAQGYWRNGQL-MPLVNAEGWFATRDRGVL-KDGKLTIVGRMDNLFFSG-GEGIQPEEV 382
Cdd:cd05914 296 VRIDSPdpatgegEIIVRGPNVMKGYYKNPEAtAEAFDKDGWFHTGDLGKIdAEGYLYIRGRKKEMIVLSsGKNIYPEEI 375
|
410 420
....*....|....*....|..
gi 489936067 383 ERVIAAHPHVLQAFIVPIEDKE 404
Cdd:cd05914 376 EAKINNMPFVLESLVVVQEKKL 397
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
157-453 |
2.47e-24 |
|
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: 103.50 E-value: 2.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 157 TSGSTGLPKAAVHTCQAHLASAQGVLSLMPFGAEDDWLLSLPLFHVSGQGILWRWLFAGARMTVRDK----QPLDQMLAg 232
Cdd:cd17637 8 TAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPLFHIAGLNLALATFHAGGANVVMEKfdpaEALELIEE- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 233 cTHASLV---PTQLWRLL--VNNTPV---TLKAVLlgGAAIPVELTEQAREQGIRCWCGYGLTE---FASTVCAKEADGL 301
Cdd:cd17637 87 -EKVTLMgsfPPILSNLLdaAEKSGVdlsSLRHVL--GLDAPETIQRFEETTGATFWSLYGQTEtsgLVTLSPYRERPGS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 302 AdvGSALPGREVRIVND-----------EVWLRAASMAQGYWRNGQLMPLVNAEGWFATRDRGVL-KDGKLTIVGRM--D 367
Cdd:cd17637 164 A--GRPGPLVRVRIVDDndrpvpagetgEIVVRGPLVFQGYWNLPELTAYTFRNGWHHTGDLGRFdEDGYLWYAGRKpeK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 368 NLFFSGGEGIQPEEVERVIAAHPHVLQAFIVPIEDKEFGHRPVAVVEydANAGET----NLAEWVKDKLARFQQP--VCW 441
Cdd:cd17637 242 ELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCV--LKPGATltadELIEFVGSRIARYKKPryVVF 319
|
330
....*....|..
gi 489936067 442 LTLPPELKAGGI 453
Cdd:cd17637 320 VEALPKTADGSI 331
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
33-460 |
2.57e-24 |
|
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: 105.14 E-value: 2.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 33 APALRLNDEALSWSELCARIDHLASGFAAQGVEEGDGVLLRAWNHPRALLAWLALLQCGARVLPVNPQLPQSLLDALVPD 112
Cdd:cd17649 3 AVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYMLED 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 113 ltlrfaldleAAIALpelsplqmksLPGDHaaawlPERLSTMTLTSGSTGLPKAAVHTCQAHLASAQGVLSLMPFGAEDD 192
Cdd:cd17649 83 ----------SGAGL----------LLTHH-----PRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAERYGLTPGDR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 193 WLLSLPL-FHVSGQGILWRWLfAGARMTVRDKQPLD--QMLA------GCTHASLVPT---QLWRLLVNNT---PVTLKA 257
Cdd:cd17649 138 ELQFASFnFDGAHEQLLPPLI-CGACVVLRPDELWAsaDELAemvrelGVTVLDLPPAylqQLAEEADRTGdgrPPSLRL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 258 VLLGGAAIPVELTEQAREQGIRCWCGYGLTE--FASTVCAKEAD-----GLADVGSALPGREVRI-----------VNDE 319
Cdd:cd17649 217 YIFGGEALSPELLRRWLKAPVRLFNAYGPTEatVTPLVWKCEAGaaragASMPIGRPLGGRSAYIldadlnpvpvgVTGE 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 320 VWLRAASMAQGYWRNGQLM-------PLvNAEG--WFATRD--RGvLKDGKLTIVGRMDNLFFSGGEGIQPEEVERVIAA 388
Cdd:cd17649 297 LYIGGEGLARGYLGRPELTaerfvpdPF-GAPGsrLYRTGDlaRW-RDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLE 374
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489936067 389 HPHVLQAFIVpIEDKEFGHRPVAVVEYDANAGETNLAE----WVKDKLARFQQPVCWLTLP--PeLKAGGiKISRRAL 460
Cdd:cd17649 375 HPGVREAAVV-ALDGAGGKQLVAYVVLRAAAAQPELRAqlrtALRASLPDYMVPAHLVFLArlP-LTPNG-KLDRKAL 449
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
26-464 |
2.64e-24 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 105.96 E-value: 2.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 26 WRQVRAKAPALRLNDEA-----LSWSELCARIDHLASGFAAQGVEEGDGVLLRAWNHP----------RAllawlallqc 90
Cdd:COG0365 18 HAEGRGDKVALIWEGEDgeertLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPeaviamlacaRI---------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 91 GARVLPVNPQL-PQSLLD---------------------------------ALVPDLT-------LRFALDLEAAIALPE 129
Cdd:COG0365 88 GAVHSPVFPGFgAEALADriedaeakvlitadgglrggkvidlkekvdealEELPSLEhvivvgrTGADVPMEGDLDWDE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 130 LsplqMKSLPGDHAAAWLPerlSTMTL----TSGSTGLPKAAVHTCQAHLASAQGVLSLMpFGAEDD---WLLSlPLFHV 202
Cdd:COG0365 168 L----LAAASAEFEPEPTD---ADDPLfilyTSGTTGKPKGVVHTHGGYLVHAATTAKYV-LDLKPGdvfWCTA-DIGWA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 203 SGqgiLWRWLFA----GARMTVRDKQPL----DQMLA-----GCTHASLVPTqLWRLLVNNTPV--------TLKAVLLG 261
Cdd:COG0365 239 TG---HSYIVYGpllnGATVVLYEGRPDfpdpGRLWEliekyGVTVFFTAPT-AIRALMKAGDEplkkydlsSLRLLGSA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 262 GAAIPVELTEQAREQ-GIRCWCGYGLTEFASTVCAkeADGLADV--GSA---LPGREVRIVND-----------EVWLRA 324
Cdd:COG0365 315 GEPLNPEVWEWWYEAvGVPIVDGWGQTETGGIFIS--NLPGLPVkpGSMgkpVPGYDVAVVDEdgnpvppgeegELVIKG 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 325 A--SMAQGYWRNGQLMplVNA-----EGWFATRDRGVL-KDGKLTIVGRMDNLFFSGGEGIQPEEVERVIAAHPHVLQAF 396
Cdd:COG0365 393 PwpGMFRGYWNDPERY--RETyfgrfPGWYRTGDGARRdEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAA 470
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489936067 397 IVPIEDKEFGHRPVAVV----EYDANAG-ETNLAEWVKDKLARFQQP--VCWLtlpPEL---KAGgiKISRRALSDWV 464
Cdd:COG0365 471 VVGVPDEIRGQVVKAFVvlkpGVEPSDElAKELQAHVREELGPYAYPreIEFV---DELpktRSG--KIMRRLLRKIA 543
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
148-460 |
2.79e-24 |
|
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: 103.71 E-value: 2.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 148 PERLSTMTLTSGSTGLPKAAVHTCQAHLASAQGVLSLMPFGAEDDWLLSLPLFHVSGQ-GILWRWLFAGARMTV------ 220
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSvVTLLTPLASGAHVVLagpagy 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 221 RDKQPLDQMLA-----GCTHASLVPTQLWRLL---VNNTPVTLKAVLLGGAAIPVELTEQAREQ-GIRCWCGYGLTEFAS 291
Cdd:cd05944 81 RNPGLFDNFWKlveryRITSLSTVPTVYAALLqvpVNADISSLRFAMSGAAPLPVELRARFEDAtGLPVVEGYGLTEATC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 292 TVCAKEADG---LADVGSALPGREVRIVND----------------EVWLRAASMAQGYWRNGQLMPLVNAEGWFATRDR 352
Cdd:cd05944 161 LVAVNPPDGpkrPGSVGLRLPYARVRIKVLdgvgrllrdcapdevgEICVAGPGVFGGYLYTEGNKNAFVADGWLNTGDL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 353 GVL-KDGKLTIVGRMDNLFFSGGEGIQPEEVERVIAAHPHVLQAFIVPIEDKEFGHRPVAVVEY--DANAGETNLAEWVK 429
Cdd:cd05944 241 GRLdADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLkpGAVVEEEELLAWAR 320
|
330 340 350
....*....|....*....|....*....|..
gi 489936067 430 DKLA-RFQQPVCWLTLPPELKAGGIKISRRAL 460
Cdd:cd05944 321 DHVPeRAAVPKHIEVLEELPVTAVGKVFKPAL 352
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
24-413 |
3.73e-24 |
|
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: 104.72 E-value: 3.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 24 RHWRQVRAKAPALRLNDEALSWSELCARIDHLASGFAAQGVEEGDGVLLRAWNHPRALLAWLALLQCGARVLPVNPQLPQ 103
Cdd:cd05920 22 ARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPVLALPSHRR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 104 SLLDAL----------VPDLTLRF---ALDLEAAIALPELSPLQmkslpgdhaaawlperlstmtLTSGSTGLPKAAVHT 170
Cdd:cd05920 102 SELSAFcahaeavayiVPDRHAGFdhrALARELAESIPEVALFL---------------------LSGGTTGTPKLIPRT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 171 CQAHLASAQGVLSLMPFGAEDDWLLSLPLFH---VSGQGILWRWLFAGARMTVRDKQPLDQMLA----GCTHASLVPT-- 241
Cdd:cd05920 161 HNDYAYNVRASAEVCGLDQDTVYLAVLPAAHnfpLACPGVLGTLLAGGRVVLAPDPSPDAAFPLiereGVTVTALVPAlv 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 242 QLW---RLLVNNTPVTLKAVLLGGAAIPVELTEQAREQ-GIRCWCGYGLTEfaSTVCAKEADGLADVGSALPGR------ 311
Cdd:cd05920 241 SLWldaAASRRADLSSLRLLQVGGARLSPALARRVPPVlGCTLQQVFGMAE--GLLNYTRLDDPDEVIIHTQGRpmspdd 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 312 EVRIVND-----------EVWLRAASMAQGYWR----NGQLMplvNAEGWFATRDRGVL-KDGKLTIVGRMDNLFFSGGE 375
Cdd:cd05920 319 EIRVVDEegnpvppgeegELLTRGPYTIRGYYRapehNARAF---TPDGFYRTGDLVRRtPDGYLVVEGRIKDQINRGGE 395
|
410 420 430
....*....|....*....|....*....|....*...
gi 489936067 376 GIQPEEVERVIAAHPHVLQAFIVPIEDKEFGHRPVAVV 413
Cdd:cd05920 396 KIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFV 433
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
33-460 |
8.66e-24 |
|
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: 103.54 E-value: 8.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 33 APALRLNDEALSWSELCARIDHLASGFAAQGVEEGDGVLLRAWNHPRALLAWLALLQCGARVLPVNPQLPQSLLDALVPD 112
Cdd:cd17643 3 AVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFILAD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 113 LTLRFALDLeaaialpelsplqmkslpgdhaaawlPERLSTMTLTSGSTGLPKAAV--HTCQAHLASAQGvlSLMPFGAE 190
Cdd:cd17643 83 SGPSLLLTD--------------------------PDDLAYVIYTSGSTGRPKGVVvsHANVLALFAATQ--RWFGFNED 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 191 DDWLlslpLFHVSGQGI----LWRWLFAGARMTVRDKqpldqmlagctHASLVPTQLWRLL-------VNNTPVT----- 254
Cdd:cd17643 135 DVWT----LFHSYAFDFsvweIWGALLHGGRLVVVPY-----------EVARSPEDFARLLrdegvtvLNQTPSAfyqlv 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 255 ------------LKAVLLGGAAIPVELTEQARE----QGIRCWCGYGLTEfaSTV-------CAKEADGLAD--VGSALP 309
Cdd:cd17643 200 eaadrdgrdplaLRYVIFGGEALEAAMLRPWAGrfglDRPQLVNMYGITE--TTVhvtfrplDAADLPAAAAspIGRPLP 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 310 GREVRIVND-----------EVWLRAASMAQGYWRNgqlmPLVNAE-----------------GWFATRdrgvLKDGKLT 361
Cdd:cd17643 278 GLRVYVLDAdgrpvppgvvgELYVSGAGVARGYLGR----PELTAErfvanpfggpgsrmyrtGDLARR----LPDGELE 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 362 IVGRMDNLFFSGGEGIQPEEVERVIAAHPHVLQAFIVPIEDKEFGHRPVAVVEYDANAGET--NLAEWVKDKLARFQQPV 439
Cdd:cd17643 350 YLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVADDGAAADiaELRALLKELLPDYMVPA 429
|
490 500
....*....|....*....|...
gi 489936067 440 CWLTLP--PeLKAGGiKISRRAL 460
Cdd:cd17643 430 RYVPLDalP-LTVNG-KLDRAAL 450
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
90-395 |
1.81e-23 |
|
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: 101.96 E-value: 1.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 90 CGARVLPVNPQLPQSLLDALVPDLTLRfALDLEAAIALPELSPLQMKSLPGDHAAAwlperlstmTLTSGSTGLPKAAVH 169
Cdd:TIGR01733 71 AGARLLLTDSALASRLAGLVLPVILLD-PLELAALDDAPAPPPPDAPSGPDDLAYV---------IYTSGSTGRPKGVVV 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 170 TCQAHLASAQGVLSLMPFGAEDDWLLSLPL-FHVSGQGILWRWLFAGARMTVRDKQPLD------QMLA--GCTHASLVP 240
Cdd:TIGR01733 141 THRSLVNLLAWLARRYGLDPDDRVLQFASLsFDASVEEIFGALLAGATLVVPPEDEERDdaallaALIAehPVTVLNLTP 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 241 T--QLWRLLVNNTPVTLKAVLLGGAAIPVELTEQAREQ--GIRCWCGYGLTEFASTVCAKEADG-------LADVGSALP 309
Cdd:TIGR01733 221 SllALLAAALPPALASLRLVILGGEALTPALVDRWRARgpGARLINLYGPTETTVWSTATLVDPddapresPVPIGRPLA 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 310 GREVRIVND-----------EVWLRAASMAQGYWRngqlMPLVNAE-------------GWFATRDRG-VLKDGKLTIVG 364
Cdd:TIGR01733 301 NTRLYVLDDdlrpvpvgvvgELYIGGPGVARGYLN----RPELTAErfvpdpfaggdgaRLYRTGDLVrYLPDGNLEFLG 376
|
330 340 350
....*....|....*....|....*....|.
gi 489936067 365 RMDNLFFSGGEGIQPEEVERVIAAHPHVLQA 395
Cdd:TIGR01733 377 RIDDQVKIRGYRIELGEIEAALLRHPGVREA 407
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
26-413 |
2.68e-23 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 102.90 E-value: 2.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 26 WRQvRAKAPALR---LNDEALSWSElcARIDHLASGFA----AQGVEEGDGV--------------------------LL 72
Cdd:PRK06087 29 WQQ-TARAMPDKiavVDNHGASYTY--SALDHAASRLAnwllAKGIEPGDRVafqlpgwceftiiylaclkvgavsvpLL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 73 RAWNHpraLLAWLALLQCGARV----------------LPVNPQLPQ----SLLDALVPDLTlrfALDLEAAIALPElsP 132
Cdd:PRK06087 106 PSWRE---AELVWVLNKCQAKMffaptlfkqtrpvdliLPLQNQLPQlqqiVGVDKLAPATS---SLSLSQIIADYE--P 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 133 LQMK-SLPGDHAAAWLperlstmtLTSGSTGLPKAAVHTCQAHLASAQGVLSLMPFGAEDDWLLSLPLFHVSG--QGILW 209
Cdd:PRK06087 178 LTTAiTTHGDELAAVL--------FTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGflHGVTA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 210 RWLfAGARMTVRDKQPLDQMLA-----GCTHASLVPTQLWRLL--VNNTPV---TLKAVLLGGAAIPVELTEQAREQGIR 279
Cdd:PRK06087 250 PFL-IGARSVLLDIFTPDACLAlleqqRCTCMLGATPFIYDLLnlLEKQPAdlsALRFFLCGGTTIPKKVARECQQRGIK 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 280 CWCGYGLTEFASTVCAKEADGL----ADVGSALPGREVRIVND-----------EVWLRAASMAQGYWRNGQLMPLV-NA 343
Cdd:PRK06087 329 LLSVYGSTESSPHAVVNLDDPLsrfmHTDGYAAAGVEIKVVDEarktlppgcegEEASRGPNVFMGYLDEPELTARAlDE 408
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489936067 344 EGWFATRDRGVL-KDGKLTIVGRMDNLFFSGGEGIQPEEVERVIAAHPHVLQAFIVPIEDKEFGHRPVAVV 413
Cdd:PRK06087 409 EGWYYSGDLCRMdEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYV 479
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
16-438 |
6.66e-23 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 101.61 E-value: 6.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 16 IQPSDWPWRhwrqvrakaPALRLNDEALSWSELCARIDHLASGFAAQGVEEGDGVLLRAWNHPRALLAWLALLQCGARVL 95
Cdd:PRK13383 43 VTAARWPGR---------TAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 96 PVNPQLPQSLLDALVPDLTLR-------FALDLEA---AIALPELSPLQMKSLPGDHAAAwLPERLstMTLTSGSTGLPK 165
Cdd:PRK13383 114 PISTEFRSDALAAALRAHHIStvvadneFAERIAGaddAVAVIDPATAGAEESGGRPAVA-APGRI--VLLTSGTTGKPK 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 166 AAVHTCQahLASAQGV----LSLMPFGAEDDWLLSLPLFHVSGQGILWRWLFAGARMTVRDKQPLDQMLAGCT-HA---- 236
Cdd:PRK13383 191 GVPRAPQ--LRSAVGVwvtiLDRTRLRTGSRISVAMPMFHGLGLGMLMLTIALGGTVLTHRHFDAEAALAQASlHRadaf 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 237 SLVPTQLWRLL-------VNNTPVTLKAVLLGGAAIPVELTEQAREQ-GIRCWCGYGLTEFASTVCAKEADgLAD----V 304
Cdd:PRK13383 269 TAVPVVLARILelpprvrARNPLPQLRVVMSSGDRLDPTLGQRFMDTyGDILYNGYGSTEVGIGALATPAD-LRDapetV 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 305 GSALPGREVRI-----------VNDEVWLRAASMAQGYWRNGQLMPLvnaEGWFATRDRGVLKD-GKLTIVGRMDNLFFS 372
Cdd:PRK13383 348 GKPVAGCPVRIldrnnrpvgprVTGRIFVGGELAGTRYTDGGGKAVV---DGMTSTGDMGYLDNaGRLFIVGREDDMIIS 424
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489936067 373 GGEGIQPEEVERVIAAHPHVLQAFIVPIEDKEFGHRPVAVV------EYDANAgetnLAEWVKDKLARFQQP 438
Cdd:PRK13383 425 GGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVvlhpgsGVDAAQ----LRDYLKDRVSRFEQP 492
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
40-438 |
1.07e-22 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 100.75 E-value: 1.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 40 DEALSWSELCARIDHLASGFAAQGVEEGDGVLLRAWNHPRALLAWLALLQ-----------------------CGARVLP 96
Cdd:PRK08276 9 GEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRsglyytpinwhltaaeiayivddSGAKVLI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 97 VNPQL---PQSLLDALVPDLTLRFAL--DLEAAIALPELSPLQMKSLPGDHAAAWLperlstMTLTSGSTGLPKA----- 166
Cdd:PRK08276 89 VSAALadtAAELAAELPAGVPLLLVVagPVPGFRSYEEALAAQPDTPIADETAGAD------MLYSSGTTGRPKGikrpl 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 167 -AVHTCQAHLASAQGVLSLMPFGAEDDWLLSLPLFH--VSgqgilwRW----LFAGARMTVRDKQPLDQMLAG-----CT 234
Cdd:PRK08276 163 pGLDPDEAPGMMLALLGFGMYGGPDSVYLSPAPLYHtaPL------RFgmsaLALGGTVVVMEKFDAEEALALieryrVT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 235 HASLVPTQLWRLLVNNTPV-------TLKAVLLGGAAIPVELTEQAREqgircWCG------YGLTEFASTVCAKEADGL 301
Cdd:PRK08276 237 HSQLVPTMFVRMLKLPEEVrarydvsSLRVAIHAAAPCPVEVKRAMID-----WWGpiiheyYASSEGGGVTVITSEDWL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 302 A---DVGSALPGrEVRIVNDEvwlrAASMAQG-----YWRNGQLmPL------------VNAEGWFATRDRGVL-KDGKL 360
Cdd:PRK08276 312 AhpgSVGKAVLG-EVRILDED----GNELPPGeigtvYFEMDGY-PFeyhndpektaaaRNPHGWVTVGDVGYLdEDGYL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 361 TIVGRMDNLFFSGGEGIQPEEVERVIAAHPHVLQAFIVPIEDKEFGHRPVAVVE-------YDANAGEtnLAEWVKDKLA 433
Cdd:PRK08276 386 YLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKAVVQpadgadaGDALAAE--LIAWLRGRLA 463
|
....*
gi 489936067 434 RFQQP 438
Cdd:PRK08276 464 HYKCP 468
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
132-392 |
1.08e-22 |
|
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: 100.62 E-value: 1.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 132 PLQMKSLPGdhaaawlPERLSTMTLTSGSTGLPKAAVHTCQAHLASAQGVLSLMPFGaEDDWLLS-LPLFHVSGQ-GILW 209
Cdd:cd05932 127 PLEERPTRF-------PEQLATLIYTSGTTGQPKGVMLTFGSFAWAAQAGIEHIGTE-ENDRMLSyLPLAHVTERvFVEG 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 210 RWLFAGarMTVRDKQPLDQMLAGCTHASlvPT------QLW-----------------RLL---VNNTPVTLKA------ 257
Cdd:cd05932 199 GSLYGG--VLVAFAESLDTFVEDVQRAR--PTlffsvpRLWtkfqqgvqdkipqqklnLLLkipVVNSLVKRKVlkglgl 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 258 ----VLLGGAA-IPVELTEQAREQGIRCWCGYGLTE-FA-STVCAKEADGLADVGSALPGREVRIVND-EVWLRAASMAQ 329
Cdd:cd05932 275 dqcrLAGCGSApVPPALLEWYRSLGLNILEAYGMTEnFAySHLNYPGRDKIGTVGNAGPGVEVRISEDgEILVRSPALMM 354
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489936067 330 GYWRNG-QLMPLVNAEGWFATRDRGVL-KDGKLTIVGRMDNLF-FSGGEGIQPEEVERVIAAHPHV 392
Cdd:cd05932 355 GYYKDPeATAEAFTADGFLRTGDKGELdADGNLTITGRVKDIFkTSKGKYVAPAPIENKLAEHDRV 420
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
18-438 |
1.69e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 99.68 E-value: 1.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 18 PSDWPWRHwRQVRAKAPALRLNDEALSWSELCAridhlASGFAAQGVEEGDGVLLRAWNHPRALLAWLALLQCGARVLPV 97
Cdd:PRK07787 2 ASLNPAAV-AAAADIADAVRIGGRVLSRSDLAG-----AATAVAERVAGARRVAVLATPTLATVLAVVGALIAGVPVVPV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 98 NPQLPQSLLDALVPDLtlrfalDLEAAIALPELSPLQMKSLPGD-HAAAWL------PERLSTMTLTSGSTGLPKAAVHT 170
Cdd:PRK07787 76 PPDSGVAERRHILADS------GAQAWLGPAPDDPAGLPHVPVRlHARSWHrypepdPDAPALIVYTSGTTGPPKGVVLS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 171 CQAHLASAQGVLSLMPFGAEDDWLLSLPLFHVSGQ--GILWRWLFAGA-RMTVRDKqPLDQMLAGCTHASL---VPTqLW 244
Cdd:PRK07787 150 RRAIAADLDALAEAWQWTADDVLVHGLPLFHVHGLvlGVLGPLRIGNRfVHTGRPT-PEAYAQALSEGGTLyfgVPT-VW 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 245 RLLVNNtPVTLKAV----LL--GGAAIPVELTEQ-AREQGIRCWCGYGLTEFASTVCAKeADG---LADVGSALPGREVR 314
Cdd:PRK07787 228 SRIAAD-PEAARALrgarLLvsGSAALPVPVFDRlAALTGHRPVERYGMTETLITLSTR-ADGerrPGWVGLPLAGVETR 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 315 IVND-------------EVWLRAASMAQGYWRNgqlmPLVNAE-----GWFATRDRGVLK-DGKLTIVGRMD-NLFFSGG 374
Cdd:PRK07787 306 LVDEdggpvphdgetvgELQVRGPTLFDGYLNR----PDATAAaftadGWFRTGDVAVVDpDGMHRIVGREStDLIKSGG 381
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489936067 375 EGIQPEEVERVIAAHPHVLQAFIVPIEDKEFGHRPVAVVEYDANAGETNLAEWVKDKLARFQQP 438
Cdd:PRK07787 382 YRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVGADDVAADELIDFVAQQLSVHKRP 445
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
23-466 |
2.48e-22 |
|
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: 99.83 E-value: 2.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 23 WRHWRQVRAKAPALRLNDEALSWSELCARIDHLASGFAAQGVEEGDGVLLRAWNHPRALLAWLALLQCGArvLPVN--PQ 100
Cdd:COG1021 31 LRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGA--IPVFalPA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 101 LPQSLLDAL----------VPDLTLRFALDLEAAIALPELSPLQMKSLPGDHA-----AAWLPERLST------------ 153
Cdd:COG1021 109 HRRAEISHFaeqseavayiIPDRHRGFDYRALARELQAEVPSLRHVLVVGDAGeftslDALLAAPADLseprpdpddvaf 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 154 MTLTSGSTGLPKAAVHT-----CQAhLASAQgvlsLMPFGAEDDWLLSLPLFH---VSGQGILWRwLFAGARMTV-RDKQ 224
Cdd:COG1021 189 FQLSGGTTGLPKLIPRThddylYSV-RASAE----ICGLDADTVYLAALPAAHnfpLSSPGVLGV-LYAGGTVVLaPDPS 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 225 PlDQMLA-----GCTHASLVPTQLWRLL-----VNNTPVTLKAVLLGGAAIPVELTEQAREQgIRCWCG--YGLtefast 292
Cdd:COG1021 263 P-DTAFPliereRVTVTALVPPLALLWLdaaerSRYDLSSLRVLQVGGAKLSPELARRVRPA-LGCTLQqvFGM------ 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 293 vcakeADGL---------ADV-----GSAL-PGREVRIVND-----------EVWLRAASMAQGYWRNgqlmPLVNA--- 343
Cdd:COG1021 335 -----AEGLvnytrlddpEEVilttqGRPIsPDDEVRIVDEdgnpvppgevgELLTRGPYTIRGYYRA----PEHNAraf 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 344 --EGWFATRDRGVL-KDGKLTIVGRMDNLFFSGGEGIQPEEVERVIAAHPHVLQAFIVPIEDKEFGHRPVAVVEydANAG 420
Cdd:COG1021 406 tpDGFYRTGDLVRRtPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGERSCAFVV--PRGE 483
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 489936067 421 ETNLAE---WVKDK-LARFQQP--VCWLTLPPELKAGgiKISRRALSDWVSA 466
Cdd:COG1021 484 PLTLAElrrFLRERgLAAFKLPdrLEFVDALPLTAVG--KIDKKALRAALAA 533
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
7-438 |
2.57e-22 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 99.83 E-value: 2.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 7 PDSVSLSGLIQpsdwpwrhwRQVR--AKAPALRLNDEALSWSELCARIDHLASGFAAQGVEEGDGVLLRAWNHPRALLAW 84
Cdd:PRK06155 18 PSERTLPAMLA---------RQAEryPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 85 LALLQCGARVLPVN-----PQLPQSL----LDALVPDLTLRFALD--LEAAIALPEL----------SPLQMKSLP---- 139
Cdd:PRK06155 89 LGCAWLGAIAVPINtalrgPQLEHILrnsgARLLVVEAALLAALEaaDPGDLPLPAVwlldapasvsVPAGWSTAPlppl 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 140 --GDHAAAWLPERLSTMTLTSGSTGLPKAAVhtcqahLASAQ----GVLS--LMPFGAEDDWLLSLPLFHVSGQGILWRW 211
Cdd:PRK06155 169 daPAPAAAVQPGDTAAILYTSGTTGPSKGVC------CPHAQfywwGRNSaeDLEIGADDVLYTTLPLFHTNALNAFFQA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 212 LFAGARMTVRDKQPLDQMLA-----GCTHASLVPTQLWRLLVNNTPVTLKA----VLLGGAaIPVELTEQAREQ-GIRCW 281
Cdd:PRK06155 243 LLAGATYVLEPRFSASGFWPavrrhGATVTYLLGAMVSILLSQPARESDRAhrvrVALGPG-VPAALHAAFRERfGVDLL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 282 CGYGLTEfASTVCA--KEADGLADVGSALPGREVRIVND-----------EVWLRAA---SMAQGYWRngqlMPLVNAEG 345
Cdd:PRK06155 322 DGYGSTE-TNFVIAvtHGSQRPGSMGRLAPGFEARVVDEhdqelpdgepgELLLRADepfAFATGYFG----MPEKTVEA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 346 W----FATRDRGVLK-DGKLTIVGRMDNLFFSGGEGIQPEEVERVIAAHPHVLQAFIVPIEdKEFGHRPV--AVVEYDAN 418
Cdd:PRK06155 397 WrnlwFHTGDRVVRDaDGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVP-SELGEDEVmaAVVLRDGT 475
|
490 500
....*....|....*....|.
gi 489936067 419 AGE-TNLAEWVKDKLARFQQP 438
Cdd:PRK06155 476 ALEpVALVRHCEPRLAYFAVP 496
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
24-439 |
3.01e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 99.73 E-value: 3.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 24 RHWRQVRAKAPALRLNDEALSWSELCARIDHLASGFAAQGVEEGDGVLLRAWNHPRALLAWLALLQCGARVLPVNP---- 99
Cdd:PRK06178 40 RAWARERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPlfre 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 100 -QLPQSL----------LDALVP-------DLTLR------FALDLEAAIALPELSPLQ------------MKSLPGDHA 143
Cdd:PRK06178 120 hELSYELndagaevllaLDQLAPvveqvraETSLRhvivtsLADVLPAEPTLPLPDSLRaprlaaagaidlLPALRACTA 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 144 AAWLP----ERLSTMTLTSGSTGLPKAAVHTcQAHL---ASAQGVLSLMpfGAEDDWLLS-LPLFHVSGQ--GILWRwLF 213
Cdd:PRK06178 200 PVPLPppalDALAALNYTGGTTGMPKGCEHT-QRDMvytAAAAYAVAVV--GGEDSVFLSfLPEFWIAGEnfGLLFP-LF 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 214 AGARMTVRDK-QPLDQMLA----GCTHASLVPTQLWRLLvnNTP-------VTLKAVllGGAAIPVELTEQAREQgircW 281
Cdd:PRK06178 276 SGATLVLLARwDAVAFMAAveryRVTRTVMLVDNAVELM--DHPrfaeydlSSLRQV--RVVSFVKKLNPDYRQR----W 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 282 C----------GYGLTEF--ASTVCAKEADGLAD-------VGSALPGREVRIVN------------DEVWLRAASMAQG 330
Cdd:PRK06178 348 RaltgsvlaeaAWGMTEThtCDTFTAGFQDDDFDllsqpvfVGLPVPGTEFKICDfetgellplgaeGEIVVRTPSLLKG 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 331 YWRNGQLMPLVNAEGWFATRDRGVL-KDGKLTIVGRMDNLFFSGGEGIQPEEVERVIAAHPHVLQAFIVPIEDKEFGHRP 409
Cdd:PRK06178 428 YWNKPEATAEALRDGWLHTGDIGKIdEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVP 507
|
490 500 510
....*....|....*....|....*....|..
gi 489936067 410 VAVVEYDANAGET--NLAEWVKDKLARFQQPV 439
Cdd:PRK06178 508 VAFVQLKPGADLTaaALQAWCRENMAVYKVPE 539
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
50-460 |
4.18e-22 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 98.67 E-value: 4.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 50 ARIDHLASGFAAQGVEEGDGVLLRAWNHPRALLAWLALLQCGARV----LPVNPQLPQSLLDALVPDLTLRFALDLEAA- 124
Cdd:cd05922 1 LGVSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRLglvfVPLNPTLKESVLRYLVADAGGRIVLADAGAa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 125 ----IALPELSPLQMkSLPGDHAAAW---------LPERLSTMTLTSGSTGLPKAAVHTCQAHLASAQGVLSLMPFGAED 191
Cdd:cd05922 81 drlrDALPASPDPGT-VLDADGIRAArasapahevSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 192 DWLLSLPLFHVSGQGILWRWLFAGARMTVRDKQPLDQML------AGCTHASLVPT---QLWRLLVNNTPV-TLKAVLLG 261
Cdd:cd05922 160 RALTVLPLSYDYGLSVLNTHLLRGATLVLTNDGVLDDAFwedlreHGATGLAGVPStyaMLTRLGFDPAKLpSLRYLTQA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 262 GAAIPVELTEQARE--QGIRCWCGYGLTE-FA--STVCA-KEADGLADVGSALPGREVRIVNDEVWL-----------RA 324
Cdd:cd05922 240 GGRLPQETIARLREllPGAQVYVMYGQTEaTRrmTYLPPeRILEKPGSIGLAIPGGEFEILDDDGTPtppgepgeivhRG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 325 ASMAQGYWRNGQLMP-LVNAEGWFATRDRGVL-KDGKLTIVGRMDNLFFSGGEGIQPEEVERVIAAHPHVLQAFIVPIED 402
Cdd:cd05922 320 PNVMKGYWNDPPYRRkEGRGGGVLHTGDLARRdEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPD 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489936067 403 kEFGHRPVAVVEYDANAGETNLAEWVKDKLARFQQPV-CWL--TLPpeLKAGGiKISRRAL 460
Cdd:cd05922 400 -PLGEKLALFVTAPDKIDPKDVLRSLAERLPPYKVPAtVRVvdELP--LTASG-KVDYAAL 456
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
2-460 |
6.82e-22 |
|
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: 99.55 E-value: 6.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 2 TQQERPDSVSLSGLIQpsdwpwrhwRQVRA--KAPALRLNDEALSWSELCARIDHLASGFAAQGVEEGD----------- 68
Cdd:COG1020 468 TAAPYPADATLHELFE---------AQAARtpDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDlvgvclersle 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 69 ---GVL--LRAwnhprallawlallqcGARVLPVNPQLPQSLLDALVPDLTLRFALDLEAAiaLPELSPLQMKSLP---- 139
Cdd:COG1020 539 mvvALLavLKA----------------GAAYVPLDPAYPAERLAYMLEDAGARLVLTQSAL--AARLPELGVPVLAldal 600
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 140 --GDHAAAWLPERLSTMTL-----TSGSTGLPK-------AAVHTCQAHLAsaqgvlsLMPFGAEDDWLLSLPL-FHVSG 204
Cdd:COG1020 601 alAAEPATNPPVPVTPDDLayviyTSGSTGRPKgvmvehrALVNLLAWMQR-------RYGLGPGDRVLQFASLsFDASV 673
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 205 QGILWrWLFAGARM------TVRDKQPLDQMLA--GCTHASLVPTqLWRLLVNNTPVT---LKAVLLGGAAIPVELTEQA 273
Cdd:COG1020 674 WEIFG-ALLSGATLvlappeARRDPAALAELLArhRVTVLNLTPS-LLRALLDAAPEAlpsLRLVLVGGEALPPELVRRW 751
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 274 REQ--GIRCWCGYGLTEFASTVCAKEADGLAD------VGSALPGREVRIVND-----------EVWLRAASMAQGYWRN 334
Cdd:COG1020 752 RARlpGARLVNLYGPTETTVDSTYYEVTPPDAdggsvpIGRPIANTRVYVLDAhlqpvpvgvpgELYIGGAGLARGYLNR 831
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 335 GQL-------MPLVNAEG-WFATRDRGV-LKDGKLTIVGRMDNLFFSGGEGIQPEEVERVIAAHPHVLQAFIVPIEDKEF 405
Cdd:COG1020 832 PELtaerfvaDPFGFPGArLYRTGDLARwLPDGNLEFLGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDAPG 911
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 489936067 406 GHRPVAVVEYDANAGETNLAEWVKDKLARFQQPV--CWLTLPPELKAGGIKISRRAL 460
Cdd:COG1020 912 DKRLVAYVVPEAGAAAAAALLRLALALLLPPYMVpaAVVLLLPLPLTGNGKLDRLAL 968
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
41-460 |
1.58e-21 |
|
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: 96.73 E-value: 1.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 41 EALSWSELCARIDHLASGFAAQGVEEGDGVLLRAWNHPRALLAWLALLQCGARVLPvnpqlpqslLDALVPDLTLRFAL- 119
Cdd:cd05971 5 EKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVP---------LFALFGPEALEYRLs 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 120 DLEAAIALPELSplqmkslpgdhaaawlpERLSTMTLTSGSTGLPKAAVHTCQ---AHLASAQGVLSLMP-----FGAED 191
Cdd:cd05971 76 NSGASALVTDGS-----------------DDPALIIYTSGTTGPPKGALHAHRvllGHLPGVQFPFNLFPrdgdlYWTPA 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 192 DWLLSLPLFhvsgqGILWRWLFAGA-----RMTVRDKQPLDQMLA--GCTHASLVPTQLwRLL------VNNTPVTLKAV 258
Cdd:cd05971 139 DWAWIGGLL-----DVLLPSLYFGVpvlahRMTKFDPKAALDLMSryGVTTAFLPPTAL-KMMrqqgeqLKHAQVKLRAI 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 259 LLGGAAIPVELTEQAREQ-GIRCWCGYGLTE--FASTVCAKEADGL-ADVGSALPGREVRIVNDE-------------VW 321
Cdd:cd05971 213 ATGGESLGEELLGWAREQfGVEVNEFYGQTEcnLVIGNCSALFPIKpGSMGKPIPGHRVAIVDDNgtplppgevgeiaVE 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 322 LRAASMAQGYWRNGQLMPLVNAEGWFATRDRGVL-KDGKLTIVGRMDNLFFSGGEGIQPEEVERVIAAHPHVLQAFIVPI 400
Cdd:cd05971 293 LPDPVAFLGYWNNPSATEKKMAGDWLLTGDLGRKdSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGI 372
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489936067 401 EDKEFGHRPVAVVEYdaNAGET-------NLAEWVKDKLARFQQPVcWLTLPPEL--KAGGiKISRRAL 460
Cdd:cd05971 373 PDPIRGEIVKAFVVL--NPGETpsdalarEIQELVKTRLAAHEYPR-EIEFVNELprTATG-KIRRREL 437
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
23-460 |
1.72e-21 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 98.49 E-value: 1.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 23 WRHWRQVRAKAPALRLNDEALSWSELCARIDHLASGFAAQGVEEGDGVLLRAWNHPRALLAWLALLQCGARVLPVNPQLP 102
Cdd:PRK12316 517 FEEQVERTPEAPALAFGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYP 596
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 103 QSLLDALVPDltLRFALDLEAAIALPELS-PLQMKSLPGDHAAAWL-------------PERLSTMTLTSGSTGLPKAAV 168
Cdd:PRK12316 597 AERLAYMLED--SGVQLLLSQSHLGRKLPlAAGVQVLDLDRPAAWLegyseenpgtelnPENLAYVIYTSGSTGKPKGAG 674
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 169 HT---CQAHLASAQGVLSLmpfGAEDDWLLSLPL-FHVSGQGILWRwLFAGARMTV------RDKQPLDQMLA--GCTHA 236
Cdd:PRK12316 675 NRhraLSNRLCWMQQAYGL---GVGDTVLQKTPFsFDVSVWEFFWP-LMSGARLVVaapgdhRDPAKLVELINreGVDTL 750
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 237 SLVPTQLWRLLVNNTP---VTLKAVLLGGAAIPVELTEQ--AREQGIRCWCGYGLTEFASTV----CAKEADGLADVGSA 307
Cdd:PRK12316 751 HFVPSMLQAFLQDEDVascTSLRRIVCSGEALPADAQEQvfAKLPQAGLYNLYGPTEAAIDVthwtCVEEGGDSVPIGRP 830
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 308 LPGREVRI-----------VNDEVWLRAASMAQGYWRNGQLM-------PLVNAEGWFATRDRGVLK-DGKLTIVGRMDN 368
Cdd:PRK12316 831 IANLACYIldanlepvpvgVLGELYLAGRGLARGYHGRPGLTaerfvpsPFVAGERMYRTGDLARYRaDGVIEYAGRIDH 910
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 369 LFFSGGEGIQPEEVERVIAAHPHVLQAFIVPIEDKEFghrpVAVVEYDANAGET--NLAEWVKDKLARFQQPVCWLTLPP 446
Cdd:PRK12316 911 QVKLRGLRIELGEIEARLLEHPWVREAAVLAVDGKQL----VGYVVLESEGGDWreALKAHLAASLPEYMVPAQWLALER 986
|
490
....*....|....*
gi 489936067 447 -ELKAGGiKISRRAL 460
Cdd:PRK12316 987 lPLTPNG-KLDRKAL 1000
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
35-466 |
3.51e-21 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 96.31 E-value: 3.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 35 ALRLNDEALSWSELCARIDHLASGFAAQGVEEGDGV--LLRA----------------------WnHPRALLAWLALLQC 90
Cdd:PRK12406 4 TIISGDRRRSFDELAQRAARAAGGLAALGVRPGDCValLMRNdfaffeaayaamrlgayavpvnW-HFKPEEIAYILEDS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 91 GARVLPVNPQLPQSLLDALVPDLTLrfaldLEAAIAlPELspLQMKSLPGDHAAA---------WLP----------ERL 151
Cdd:PRK12406 83 GARVLIAHADLLHGLASALPAGVTV-----LSVPTP-PEI--AAAYRISPALLTPpagaidwegWLAqqepydgppvPQP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 152 STMTLTSGSTGLPKAAVHTC-QAHLASAQGVLSLMPFGAEDDW--LLSLPLFHVSGQGILWRWLFAGARMTVRDKQPLDQ 228
Cdd:PRK12406 155 QSMIYTSGTTGHPKGVRRAApTPEQAAAAEQMRALIYGLKPGIraLLTGPLYHSAPNAYGLRAGRLGGVLVLQPRFDPEE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 229 MLA-----GCTHASLVPTQLWRLLVNNTPV-------TLKAVLLGGAAIPVELTEQAREqgircWCG------YGLTEFA 290
Cdd:PRK12406 235 LLQlierhRITHMHMVPTMFIRLLKLPEEVrakydvsSLRHVIHAAAPCPADVKRAMIE-----WWGpviyeyYGSTESG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 291 STVCAKEADGLA---DVGSALPGREVRIVND-----------EVWLRAASMAQ-GYWRNGQLMPLVNAEGWFATRDRGVL 355
Cdd:PRK12406 310 AVTFATSEDALShpgTVGKAAPGAELRFVDEdgrplpqgeigEIYSRIAGNPDfTYHNKPEKRAEIDRGGFITSGDVGYL 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 356 -KDGKLTIVGRMDNLFFSGGEGIQPEEVERVIAAHPHVLQAFIVPIEDKEFGHRPVAVVEYDANAG--ETNLAEWVKDKL 432
Cdd:PRK12406 390 dADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPGATldEADIRAQLKARL 469
|
490 500 510
....*....|....*....|....*....|....*...
gi 489936067 433 ARFQQP--VCWLTLPPELKAGgiKISRRALSD--WVSA 466
Cdd:PRK12406 470 AGYKVPkhIEIMAELPREDSG--KIFKRRLRDpyWANA 505
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
140-442 |
4.94e-21 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 96.07 E-value: 4.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 140 GDHAAAWLP--ERLSTMTL--TSGSTGLPKAAV-HTCQAHLASAQGVLSL-MPFGAEddWLLSLPLFHVSGQGILWRW-L 212
Cdd:PLN02479 182 GDPEFAWKPpaDEWQSIALgyTSGTTASPKGVVlHHRGAYLMALSNALIWgMNEGAV--YLWTLPMFHCNGWCFTWTLaA 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 213 FAGARMTVRD--KQPLDQMLA--GCTHASLVPTQLWRLLvnNTPVTLKA--------VLLGGAAIPVELTEQAREQGIRC 280
Cdd:PLN02479 260 LCGTNICLRQvtAKAIYSAIAnyGVTHFCAAPVVLNTIV--NAPKSETIlplprvvhVMTAGAAPPPSVLFAMSEKGFRV 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 281 WCGYGLTEF--ASTVCA--KEADGL-ADVGSALPGRE-VRIVN----------------------DEVWLRAASMAQGYW 332
Cdd:PLN02479 338 THTYGLSETygPSTVCAwkPEWDSLpPEEQARLNARQgVRYIGlegldvvdtktmkpvpadgktmGEIVMRGNMVMKGYL 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 333 RNgqlmPLVNAE----GWFATRDRGVLK-DGKLTIVGRMDNLFFSGGEGIQPEEVERVIAAHPHVLQAFIVPIEDKEFGH 407
Cdd:PLN02479 418 KN----PKANEEafanGWFHSGDLGVKHpDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERWGE 493
|
330 340 350
....*....|....*....|....*....|....*..
gi 489936067 408 RPVAVVEYDANAGETNLAEWVKD--KLARFQQPVCWL 442
Cdd:PLN02479 494 SPCAFVTLKPGVDKSDEAALAEDimKFCRERLPAYWV 530
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
28-460 |
6.80e-21 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 96.56 E-value: 6.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 28 QVRA--KAPALRLNDEALSWSELCARIDHLASGFAAQGVEEGDGVLLRAWNHPRALLAWLALLQCGARVLPVNPQLPQSL 105
Cdd:PRK12316 2012 QAARapEAIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAER 2091
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 106 LDALVPDLTLRFAL---DLEAAIALPElsplQMKSLPGDHAAAW------------LPERLSTMTLTSGSTGLPK----- 165
Cdd:PRK12316 2092 LAYMLEDSGAALLLtqrHLLERLPLPA----GVARLPLDRDAEWadypdtapavqlAGENLAYVIYTSGSTGLPKgvavs 2167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 166 --AAVHTCQA-----HLASAQGVLSLMPFGaeddwllslplFHVSGQGILWRwLFAGARMTVRD------KQPLDQMLA- 231
Cdd:PRK12316 2168 hgALVAHCQAageryELSPADCELQFMSFS-----------FDGAHEQWFHP-LLNGARVLIRDdelwdpEQLYDEMERh 2235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 232 GCTHASLVPTQLWRLL----VNNTPVTLKAVLLGGAAIPVELTEQARE--QGIRCWCGYGLTEFASTV-----CAKEADG 300
Cdd:PRK12316 2236 GVTILDFPPVYLQQLAehaeRDGRPPAVRVYCFGGEAVPAASLRLAWEalRPVYLFNGYGPTEAVVTPllwkcRPQDPCG 2315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 301 LADV--GSALPGREVRIVND-----------EVWLRAASMAQGYWRNgqlmPLVNAEGWFA----------------TRD 351
Cdd:PRK12316 2316 AAYVpiGRALGNRRAYILDAdlnllapgmagELYLGGEGLARGYLNR----PGLTAERFVPdpfsasgerlyrtgdlARY 2391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 352 RGvlkDGKLTIVGRMDNLFFSGGEGIQPEEVERVIAAHPHVLQAFIVPIeDKEFGHRPVA-VVEYDANAGE-TNLAEWVK 429
Cdd:PRK12316 2392 RA---DGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQ-DGASGKQLVAyVVPDDAAEDLlAELRAWLA 2467
|
490 500 510
....*....|....*....|....*....|.
gi 489936067 430 DKLARFQQPVCWLTLPPELKAGGIKISRRAL 460
Cdd:PRK12316 2468 ARLPAYMVPAHWVVLERLPLNPNGKLDRKAL 2498
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
27-460 |
9.54e-21 |
|
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: 94.72 E-value: 9.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 27 RQVRA--KAPALRLNDEALSWSELCARIDHLASGFAAQGVEEGDGVLLRAWNHPRALLAWLALLQCGARVLPVNPQLPQS 104
Cdd:cd17651 3 RQAARtpDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 105 LLDALVPD------LT---LRFALDLEAAIALPELSPLQMKSLPGDHAAAWLPERLSTMTLTSGSTGLPKAAV--HTCQA 173
Cdd:cd17651 83 RLAFMLADagpvlvLThpaLAGELAVELVAVTLLDQPGAAAGADAEPDPALDADDLAYVIYTSGSTGRPKGVVmpHRSLA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 174 HLASAQGVLSLMPFGAEDDwLLSLPLFHVSGQGIlWRWLFAGARMTVRD---KQPLDQMLAGC----THASLVPTQLWRL 246
Cdd:cd17651 163 NLVAWQARASSLGPGARTL-QFAGLGFDVSVQEI-FSTLCAGATLVLPPeevRTDPPALAAWLdeqrISRVFLPTVALRA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 247 LVN------NTPVTLKAVLLGGAAIPVELTEQ---AREQGIRCWCGYGLTEfASTVCAKEADGLAD-------VGSALPG 310
Cdd:cd17651 241 LAEhgrplgVRLAALRYLLTGGEQLVLTEDLRefcAGLPGLRLHNHYGPTE-THVVTALSLPGDPAawpapppIGRPIDN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 311 REVRIVND-----------EVWLRAASMAQGYWRNGQLM-------PLVNAEGWFATRDRGV-LKDGKLTIVGRMDNLFF 371
Cdd:cd17651 320 TRVYVLDAalrpvppgvpgELYIGGAGLARGYLNRPELTaerfvpdPFVPGARMYRTGDLARwLPDGELEFLGRADDQVK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 372 SGGEGIQPEEVERVIAAHPHVLQAFIVPIEDKEFGHRPVAVVEYDANAGET--NLAEWVKDKLARFQQP--VCWL-TLPp 446
Cdd:cd17651 400 IRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPEAPVDaaELRAALATHLPEYMVPsaFVLLdALP- 478
|
490
....*....|....
gi 489936067 447 eLKAGGiKISRRAL 460
Cdd:cd17651 479 -LTPNG-KLDRRAL 490
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
33-460 |
1.25e-20 |
|
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: 94.24 E-value: 1.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 33 APALRLNDEALSWSELCARIDHLASGFAAQGVEEGDGVLLRAWNHPRALLAWLALLQCGARVLPVNPQLP----QSLLDA 108
Cdd:cd05945 7 RPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPaeriREILDA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 109 LVPDLtlrfaldLEAAialpelsplqmkslPGDHAAawlperlstMTLTSGSTGLPKAAVHTCQAHLASAQGVLSLMPFG 188
Cdd:cd05945 87 AKPAL-------LIAD--------------GDDNAY---------IIFTSGSTGRPKGVQISHDNLVSFTNWMLSDFPLG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 189 AEDDWLLSLPL-FHVSGQGILWRWLFAGA-----RMTVRDKQPLDQMLA--GCTHASLVPTqLWRLL-------VNNTPv 253
Cdd:cd05945 137 PGDVFLNQAPFsFDLSVMDLYPALASGATlvpvpRDATADPKQLFRFLAehGITVWVSTPS-FAAMCllsptftPESLP- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 254 TLKAVLLGGAAIPVELTE--QAREQGIRCWCGYGLTE--FASTVCAKEADGLAD-----VGSALPGREVRIVND------ 318
Cdd:cd05945 215 SLRHFLFCGEVLPHKTARalQQRFPDARIYNTYGPTEatVAVTYIEVTPEVLDGydrlpIGYAKPGAKLVILDEdgrpvp 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 319 -----EVWLRAASMAQGYWRNgqlmPLVNAE--------GWFATRDRG-VLKDGKLTIVGRMDNLFFSGGEGIQPEEVER 384
Cdd:cd05945 295 pgekgELVISGPSVSKGYLNN----PEKTAAaffpdegqRAYRTGDLVrLEADGLLFYRGRLDFQVKLNGYRIELEEIEA 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 385 VIAAHPHVLQAFIVPIEDKEFGHRPVAVVEYDANAGETNLAEW---VKDKLARFQQPVCWLTLP-PELKAGGiKISRRAL 460
Cdd:cd05945 371 ALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPGAEAGLTKAIkaeLAERLPPYMIPRRFVYLDeLPLNANG-KIDRKAL 449
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
157-438 |
1.52e-20 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 94.68 E-value: 1.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 157 TSGSTGLPKAAVHT---CQAHLASAQGVLSLMPFGAEDdWLLSLPLFHVSGQGI-LWRWLFAGARM----TVRDKQPLDQ 228
Cdd:PRK05605 227 TSGTTGKPKGAQLThrnLFANAAQGKAWVPGLGDGPER-VLAALPMFHAYGLTLcLTLAVSIGGELvllpAPDIDLILDA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 229 M-------LAGcthaslVPTQLWRLLV----NNTPVT-LKAVLLGGAAIPVELTEQAREQ-GIRCWCGYGLTEFASTVCA 295
Cdd:PRK05605 306 MkkhpptwLPG------VPPLYEKIAEaaeeRGVDLSgVRNAFSGAMALPVSTVELWEKLtGGLLVEGYGLTETSPIIVG 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 296 K---EADGLADVGSALPGREVRIVN-------------DEVWLRAASMAQGYWRNGQLMPLVNAEGWFATRDRGVLK-DG 358
Cdd:PRK05605 380 NpmsDDRRPGYVGVPFPDTEVRIVDpedpdetmpdgeeGELLVRGPQVFKGYWNRPEETAKSFLDGWFRTGDVVVMEeDG 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 359 KLTIVGRMDNLFFSGGEGIQPEEVERVIAAHPHVLQAFIVPIEDKEFGHRPVA--VVEYDANAGETNLAEWVKDKLARFQ 436
Cdd:PRK05605 460 FIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAavVLEPGAALDPEGLRAYCREHLTRYK 539
|
..
gi 489936067 437 QP 438
Cdd:PRK05605 540 VP 541
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
153-462 |
1.70e-20 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 94.32 E-value: 1.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 153 TMTLTSGSTGLPKAAVHTCQAHLASAQGVLSLMPFGAEDDWLLSLPLFHVSGQGILWRWLFAGA-----RMTVRDKQPLD 227
Cdd:PLN03102 190 SLNYTSGTTADPKGVVISHRGAYLSTLSAIIGWEMGTCPVYLWTLPMFHCNGWTFTWGTAARGGtsvcmRHVTAPEIYKN 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 228 QMLAGCTHASLVPTqLWRLLV--NNTPVTLKA----VLLGGAAIPVELTEQAREQGIRCWCGYGLTEFASTV--CAKEAD 299
Cdd:PLN03102 270 IEMHNVTHMCCVPT-VFNILLkgNSLDLSPRSgpvhVLTGGSPPPAALVKKVQRLGFQVMHAYGLTEATGPVlfCEWQDE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 300 ---------------------GLADVGSALPGREVRIVND-----EVWLRAASMAQGYWRNGQLMPLVNAEGWFATRDRG 353
Cdd:PLN03102 349 wnrlpenqqmelkarqgvsilGLADVDVKNKETQESVPRDgktmgEIVIKGSSIMKGYLKNPKATSEAFKHGWLNTGDVG 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 354 VLK-DGKLTIVGRMDNLFFSGGEGIQPEEVERVIAAHPHVLQAFIVPIEDKEFGHRPVAVV------------EYDANAG 420
Cdd:PLN03102 429 VIHpDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVvlekgettkedrVDKLVTR 508
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 489936067 421 ETNLAEWVKDKLARFQQP---VCWLTLPpelKAGGIKISRRALSD 462
Cdd:PLN03102 509 ERDLIEYCRENLPHFMCPrkvVFLQELP---KNGNGKILKPKLRD 550
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
23-400 |
2.17e-20 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 95.23 E-value: 2.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 23 WRHWRQVRAKAPALRLNDEALSWSELCARIDHLASGFAAQGVEEGDGVLLRAWNHPRALLAWLALLQCGARVLPVNPQLP 102
Cdd:PRK12467 518 IEAQARQHPERPALVFGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYP 597
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 103 QSLLDALVPDLTLRFALDLEAAIALPELsPLQMKSLPGDHAAAWL-------------PERLSTMTLTSGSTGLPKAAVH 169
Cdd:PRK12467 598 QDRLAYMLDDSGVRLLLTQSHLLAQLPV-PAGLRSLCLDEPADLLcgysghnpevaldPDNLAYVIYTSGSTGQPKGVAI 676
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 170 TCQAHLASAQGVLSLMPFGAEDDWLL-SLPLFHVSGQGILWRwLFAGARMTVRDKQPL---DQMLA-----GCTHASLVP 240
Cdd:PRK12467 677 SHGALANYVCVIAERLQLAADDSMLMvSTFAFDLGVTELFGA-LASGATLHLLPPDCArdaEAFAAlmadqGVTVLKIVP 755
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 241 TQlWRLLVNNT----PVTLKAVLLGGAAIPVELTEQARE--QGIRCWCGYGLTEFASTV----CAKEA--DGLADVGSAL 308
Cdd:PRK12467 756 SH-LQALLQASrvalPRPQRALVCGGEALQVDLLARVRAlgPGARLINHYGPTETTVGVstyeLSDEErdFGNVPIGQPL 834
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 309 PGREVRI-----------VNDEVWLRAASMAQGYWRNGQLM-------PL-VNAEGWFATRDRG-VLKDGKLTIVGRMDN 368
Cdd:PRK12467 835 ANLGLYIldhylnpvpvgVVGELYIGGAGLARGYHRRPALTaerfvpdPFgADGGRLYRTGDLArYRADGVIEYLGRMDH 914
|
410 420 430
....*....|....*....|....*....|..
gi 489936067 369 LFFSGGEGIQPEEVERVIAAHPHVLQAFIVPI 400
Cdd:PRK12467 915 QVKIRGFRIELGEIEARLLAQPGVREAVVLAQ 946
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
41-406 |
2.21e-20 |
|
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: 93.58 E-value: 2.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 41 EALSWSELCARIDHLASGFAAQGVEEGDGVLLRAWNHPRALLAWLALLQCGArvlpVNpqLPQSLlDALVPDLTLRFAlD 120
Cdd:cd17640 4 KRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGA----VD--VVRGS-DSSVEELLYILN-H 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 121 LEAAIALPELSPlqmkslpgdhaaawlpERLSTMTLTSGSTGLPKAAVHTCQAHLASAQGVLSLMPFGAEDDWLLSLPLF 200
Cdd:cd17640 76 SESVALVVENDS----------------DDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQPGDRFLSILPIW 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 201 H---------VSGQGI---------------------------LWRWLFAGARMTVRDKQPLDQMLAGCThaslvptqlw 244
Cdd:cd17640 140 HsyersaeyfIFACGCsqaytsirtlkddlkrvkphyivsvprLWESLYSGIQKQVSKSSPIKQFLFLFF---------- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 245 rLLVNNtpvtLKAVLLGGAAIPVELTEQAREQGIRCWCGYGLTEFASTVCAKEADG--LADVGSALPGREVRIVNDE--- 319
Cdd:cd17640 210 -LSGGI----FKFGISGGGALPPHVDTFFEAIGIEVLNGYGLTETSPVVSARRLKCnvRGSVGRPLPGTEIKIVDPEgnv 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 320 ---------VWLRAASMAQGYWRNGQLMPLV-NAEGWFATRDRGVL-KDGKLTIVGRM-DNLFFSGGEGIQPEEVERVIA 387
Cdd:cd17640 285 vlppgekgiVWVRGPQVMKGYYKNPEATSKVlDSDGWFNTGDLGWLtCGGELVLTGRAkDTIVLSNGENVEPQPIEEALM 364
|
410
....*....|....*....
gi 489936067 388 AHPHVLQAFIVPIEDKEFG 406
Cdd:cd17640 365 RSPFIEQIMVVGQDQKRLG 383
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
151-462 |
2.60e-20 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 93.89 E-value: 2.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 151 LSTMTLTSGSTGLPKAAVHTCQ---AHLASaqgvlSLMPFGAED----DWLLSLPLFHVSG-QGILWRWLFAGARMTVRD 222
Cdd:PLN02330 186 LCALPFSSGTTGISKGVMLTHRnlvANLCS-----SLFSVGPEMigqvVTLGLIPFFHIYGiTGICCATLRNKGKVVVMS 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 223 KQPLDQMLAG-----CTHASLVPTQLWRLLVNN-------TPVTLKAVLLGGAAIPVELTE--QAREQGIRCWCGYGLTE 288
Cdd:PLN02330 261 RFELRTFLNAlitqeVSFAPIVPPIILNLVKNPiveefdlSKLKLQAIMTAAAPLAPELLTafEAKFPGVQVQEAYGLTE 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 289 FaSTVCAKEAD-----GLA---DVGSALPGREVRIVN------------DEVWLRAASMAQGYWRNGQLMP-LVNAEGWF 347
Cdd:PLN02330 341 H-SCITLTHGDpekghGIAkknSVGFILPNLEVKFIDpdtgrslpkntpGELCVRSQCVMQGYYNNKEETDrTIDEDGWL 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 348 ATRDRGVL-KDGKLTIVGRMDNLFFSGGEGIQPEEVERVIAAHPHVLQAFIVPIEDKEFGHRPVA--VVEYDANAGETNL 424
Cdd:PLN02330 420 HTGDIGYIdDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAAcvVINPKAKESEEDI 499
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 489936067 425 AEWVKDKLARFQQ--PVCWLTLPPELKAGgiKISRRALSD 462
Cdd:PLN02330 500 LNFVAANVAHYKKvrVVQFVDSIPKSLSG--KIMRRLLKE 537
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
43-462 |
3.45e-20 |
|
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: 92.40 E-value: 3.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 43 LSWSELCARIDHLASGFAAQGVEEGDGVLLRAWNHPRALLAWLALLQCGARVLPVNPQLPqslldalVPDLTLRF-ALDL 121
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLG-------PKDIEYRLeAAGA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 122 EAAIALPElsplqmkslpgdhaaawlpeRLSTMTLTSGSTGLPKAAVHTCQ---AHLASAQGVLSLMPfgaeDD--WLLS 196
Cdd:cd05972 74 KAIVTDAE--------------------DPALIYFTSGTTGLPKGVLHTHSyplGHIPTAAYWLGLRP----DDihWNIA 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 197 LP--LFHVSGqGILWRWLfAGARMTVRDKQPLDQMLA-------GCTHASLVPTqLWRLLVNNTP-----VTLKAVLLGG 262
Cdd:cd05972 130 DPgwAKGAWS-SFFGPWL-LGATVFVYEGPRFDAERIlelleryGVTSFCGPPT-AYRMLIKQDLssykfSHLRLVVSAG 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 263 AAIPVELTEQAREQ-GIRCWCGYGLTEFASTV----CAKEADGlaDVGSALPGREVRIVNDE-------------VWLRA 324
Cdd:cd05972 207 EPLNPEVIEWWRAAtGLPIRDGYGQTETGLTVgnfpDMPVKPG--SMGRPTPGYDVAIIDDDgrelppgeegdiaIKLPP 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 325 ASMAQGYWRNGQLMPLVNAEGWFATRDRGVL-KDGKLTIVGRMDNLFFSGGEGIQPEEVERVIAAHPHVLQAFIVPIEDK 403
Cdd:cd05972 285 PGLFLGYVGDPEKTEASIRGDYYLTGDRAYRdEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDP 364
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489936067 404 EFGHRPVAVVEYDANAGETN-----LAEWVKDKLARFQQPVCwLTLPPEL--KAGGiKISRRALSD 462
Cdd:cd05972 365 VRGEVVKAFVVLTSGYEPSEelaeeLQGHVKKVLAPYKYPRE-IEFVEELpkTISG-KIRRVELRD 428
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
44-438 |
4.26e-20 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 92.85 E-value: 4.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 44 SWSELCARIDHLASGFAAQGVEEGDGVLLRAWNHPRALLAWLALLQCGARVLPVNPQL-PQS------------------ 104
Cdd:PRK07008 41 TYRDCERRAKQLAQALAALGVEPGDRVGTLAWNGYRHLEAYYGVSGSGAVCHTINPRLfPEQiayivnhaedryvlfdlt 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 105 ---LLDALVPDL-TLRFALDLEAAIALPELS-PLQ-----MKSLPGDHAAAWLPERL-STMTLTSGSTGLPKAAVHTCQA 173
Cdd:PRK07008 121 flpLVDALAPQCpNVKGWVAMTDAAHLPAGStPLLcyetlVGAQDGDYDWPRFDENQaSSLCYTSGTTGNPKGALYSHRS 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 174 HL--ASAQGVLSLMPFGAEDDWLLSLPLFHVSGQGILWRWLFAGARMTV----RDKQPLDQMLA--GCTHASLVPTqLWR 245
Cdd:PRK07008 201 TVlhAYGAALPDAMGLSARDAVLPVVPMFHVNAWGLPYSAPLTGAKLVLpgpdLDGKSLYELIEaeRVTFSAGVPT-VWL 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 246 LLVNNTP------VTLKAVLLGGAAIPVELTEQAREQ-GIRCWCGYGLTEFA--STVCAKEADGLADV-----------G 305
Cdd:PRK07008 280 GLLNHMReaglrfSTLRRTVIGGSACPPAMIRTFEDEyGVEVIHAWGMTEMSplGTLCKLKWKHSQLPldeqrkllekqG 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 306 SALPGREVRIVND-------------EVWLRAASMAQGYWRNGQlMPLVNaeGWFATRDRGVL-KDGKLTIVGRMDNLFF 371
Cdd:PRK07008 360 RVIYGVDMKIVGDdgrelpwdgkafgDLQVRGPWVIDRYFRGDA-SPLVD--GWFPTGDVATIdADGFMQITDRSKDVIK 436
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489936067 372 SGGEGIQPEEVERVIAAHPHVLQAFIVPIEDKEFGHRPVAVV--EYDANAGETNLAEWVKDKLARFQQP 438
Cdd:PRK07008 437 SGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLVVvkRPGAEVTREELLAFYEGKVAKWWIP 505
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
55-399 |
4.33e-20 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 93.56 E-value: 4.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 55 LASGFAAQGVEEGDGVLLRAWNHPRALLAWLALLQCGARVLPVNPQL-----------PQSLLDALVPDLTLRFALD--L 121
Cdd:PRK06060 43 LGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELhrddhalaarnTEPALVVTSDALRDRFQPSrvA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 122 EAAIALPELS---PLQMKSLPGDHAAawlperlsTMTLTSGSTGLPKAAVHT-CQAHL---ASAQGVLSLMPfgaEDDWL 194
Cdd:PRK06060 123 EAAELMSEAArvaPGGYEPMGGDALA--------YATYTSGTTGPPKAAIHRhADPLTfvdAMCRKALRLTP---EDTGL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 195 LSLPLFHVSGQG-ILWRWLFAGARMTVrDKQPLDQMLAGCTHASLVPTQLW-------RLLVNNTP---VTLKAVLLGGA 263
Cdd:PRK06060 192 CSARMYFAYGLGnSVWFPLATGGSAVI-NSAPVTPEAAAILSARFGPSVLYgvpnffaRVIDSCSPdsfRSLRCVVSAGE 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 264 AIPVELTEQARE--QGIRCWCGYGLTEFASTVCAKEADG--LADVGSALPGREVRIV-----------NDEVWLRAASMA 328
Cdd:PRK06060 271 ALELGLAERLMEffGGIPILDGIGSTEVGQTFVSNRVDEwrLGTLGRVLPPYEIRVVapdgttagpgvEGDLWVRGPAIA 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 329 QGYWRNGQlmPLVNAEGWFATRDRGVLK-DGKLTIVGRMDNLFFSGGEGIQPEEVERVIAAHPHV--------------- 392
Cdd:PRK06060 351 KGYWNRPD--SPVANEGWLDTRDRVCIDsDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVaeaavvavrestgas 428
|
....*...
gi 489936067 393 -LQAFIVP 399
Cdd:PRK06060 429 tLQAFLVA 436
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
28-406 |
1.13e-19 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 91.61 E-value: 1.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 28 QVRAKAPALRLND--EALSWSELCARIDHLASGFAAQGVEEGDGVLLRAWNHPRALLAWLALLQCGARVLPVNPQLPQSL 105
Cdd:PRK05857 25 RQQPEAIALRRCDgtSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLPIAA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 106 LDalvpdltlRFALDLEAAIALP--------ELSPLQMKSLP--------GDHAAAWLPERLS-------------TMTL 156
Cdd:PRK05857 105 IE--------RFCQITDPAAALVapgskmasSAVPEALHSIPviavdiaaVTRESEHSLDAASlagnadqgsedplAMIF 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 157 TSGSTGLPKAAVHTCQAHLA-----SAQGvLSLMPFGAEDDWLLSLPLFHVSGqgiLWrW----LFAGARMTVRDKQ--P 225
Cdd:PRK05857 177 TSGTTGEPKAVLLANRTFFAvpdilQKEG-LNWVTWVVGETTYSPLPATHIGG---LW-WiltcLMHGGLCVTGGENttS 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 226 LDQMLAG--CTHASLVPTQLWRL-----LVNNTPVTLKAVLLGGA---AIPVELTEQAreqGIRCWCGYGLTEFAST-VC 294
Cdd:PRK05857 252 LLEILTTnaVATTCLVPTLLSKLvselkSANATVPSLRLVGYGGSraiAADVRFIEAT---GVRTAQVYGLSETGCTaLC 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 295 AKEADG------LADVGSALPGREVRIVNDE-----------------VWLRAASMAQGYWRNGQLMPLVNAEGWFATRD 351
Cdd:PRK05857 329 LPTDDGsivkieAGAVGRPYPGVDVYLAATDgigptapgagpsasfgtLWIKSPANMLGYWNNPERTAEVLIDGWVNTGD 408
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 489936067 352 ---RGvlKDGKLTIVGRMDNLFFSGGEGIQPEEVERVIAAHPHVLQAFIVPIEDKEFG 406
Cdd:PRK05857 409 lleRR--EDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFG 464
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
44-422 |
1.67e-19 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 91.35 E-value: 1.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 44 SWSELCARIDHLASGFAAQGVEEGDGVLLRAWNHPRALLAWLALLQCGARVLPVNPQL-PQSLL--------DALVPDLT 114
Cdd:PRK06018 41 TYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLfPEQIAwiinhaedRVVITDLT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 115 LRFALD--------LEAAIALPELSPLQMKSLP-------------GDHAAAWLPERLST-MTLTSGSTGLPKAAV---- 168
Cdd:PRK06018 121 FVPILEkiadklpsVERYVVLTDAAHMPQTTLKnavayeewiaeadGDFAWKTFDENTAAgMCYTSGTTGDPKGVLyshr 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 169 ----HTCQAHLASAQGVlslmpfGAEDDWLLSLPLFHVSGQGILW-------RWLFAGARMtvrDKQPLDQMLAG--CTH 235
Cdd:PRK06018 201 snvlHALMANNGDALGT------SAADTMLPVVPLFHANSWGIAFsapsmgtKLVMPGAKL---DGASVYELLDTekVTF 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 236 ASLVPTqLWRLLV------NNTPVTLKAVLLGGAAIPVELTEQAREQGIRCWCGYGLTEFA--STVCA-----------K 296
Cdd:PRK06018 272 TAGVPT-VWLMLLqymekeGLKLPHLKMVVCGGSAMPRSMIKAFEDMGVEVRHAWGMTEMSplGTLAAlkppfsklpgdA 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 297 EADGLADVGSALPGREVRIVNDE-------------VWLRAASMAQGYWRNGQlmPLVNAEGWFATRDRGVL-KDGKLTI 362
Cdd:PRK06018 351 RLDVLQKQGYPPFGVEMKITDDAgkelpwdgktfgrLKVRGPAVAAAYYRVDG--EILDDDGFFDTGDVATIdAYGYMRI 428
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 363 VGRMDNLFFSGGEGIQPEEVERVIAAHPHVLQAFIVPIEDKEFGHRPVAVVEydANAGET 422
Cdd:PRK06018 429 TDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQ--LKPGET 486
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
33-460 |
5.38e-19 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 90.79 E-value: 5.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 33 APALRLNDEALSWSELCARIDHLASGFAAQGVEEGDGVLLRAWNHPRALLAWLALLQCGARVLPVNPQLPQSLLDALVPD 112
Cdd:PRK12316 3073 AVALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLED 3152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 113 LTLRFALDlEAAIALPELSPLQMKSL-PGDHAAA-------WLPERLSTMTLTSGSTGLPKAAVHTCQAHLASAQGVLSL 184
Cdd:PRK12316 3153 SGAQLLLS-QSHLRLPLAQGVQVLDLdRGDENYAeanpairTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQA 3231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 185 MPFGAEDDWLLSLPLFHVSGQGILWRWLFAGARMTVRDKQP----------LDQMLAGCTHAslVPTQLWRLLVNNTP-- 252
Cdd:PRK12316 3232 YGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDwrdpallvelINSEGVDVLHA--YPSMLQAFLEEEDAhr 3309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 253 -VTLKAVLLGGAAIPVELTEQAREQGiRCWCGYGLTEFASTV----CAKEADGLADVGSALPGREVRIVND--------- 318
Cdd:PRK12316 3310 cTSLKRIVCGGEALPADLQQQVFAGL-PLYNLYGPTEATITVthwqCVEEGKDAVPIGRPIANRACYILDGslepvpvga 3388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 319 --EVWLRAASMAQGYWRNGQLM-------PLVNAEGWFATRDRGVLK-DGKLTIVGRMDNLFFSGGEGIQPEEVERVIAA 388
Cdd:PRK12316 3389 lgELYLGGEGLARGYHNRPGLTaerfvpdPFVPGERLYRTGDLARYRaDGVIEYIGRVDHQVKIRGFRIELGEIEARLLE 3468
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489936067 389 HPHVLQAFIVPIEdkefGHRPVAVVEYDANAGETN--LAEWVKDKLARFQQPVCWLTLPP-ELKAGGiKISRRAL 460
Cdd:PRK12316 3469 HPWVREAVVLAVD----GRQLVAYVVPEDEAGDLReaLKAHLKASLPEYMVPAHLLFLERmPLTPNG-KLDRKAL 3538
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
145-413 |
7.28e-19 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 89.47 E-value: 7.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 145 AWLPERLSTMTLTSGSTGLPKAAVHTCQAHLASAQGVLSLMPFGAEDDWLLSLPLFHVSGQGILWRWLFAGARMTVRDK- 223
Cdd:PLN02860 168 AWAPDDAVLICFTSGTTGRPKGVTISHSALIVQSLAKIAIVGYGEDDVYLHTAPLCHIGGLSSALAMLMVGACHVLLPKf 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 224 ------QPLDQMlaGCTHASLVPTQLWRLL-VNNTPVT------LKAVLLGGAAIPVELTEQARE--QGIRCWCGYGLTE 288
Cdd:PLN02860 248 dakaalQAIKQH--NVTSMITVPAMMADLIsLTRKSMTwkvfpsVRKILNGGGSLSSRLLPDAKKlfPNAKLFSAYGMTE 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 289 FASTV---------CAKEADGLAD----------------VGSALPGREVRIVNDE------VWLRAASMAQGYWRNGQL 337
Cdd:PLN02860 326 ACSSLtfmtlhdptLESPKQTLQTvnqtksssvhqpqgvcVGKPAPHVELKIGLDEssrvgrILTRGPHVMLGYWGQNSE 405
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489936067 338 MPLV-NAEGWFATRDRGVLKD-GKLTIVGRMDNLFFSGGEGIQPEEVERVIAAHPHVLQAFIVPIEDKEFGHRPVAVV 413
Cdd:PLN02860 406 TASVlSNDGWLDTGDIGWIDKaGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEMVVACV 483
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
43-438 |
1.20e-18 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 88.71 E-value: 1.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 43 LSWSELCARIDHLASGFAAQGVEEGDGVLLRAWNHPRALLAWLALLQCGARVLPVNPQ---------LPQS--------- 104
Cdd:PRK08315 44 WTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVTINPAyrlseleyaLNQSgckaliaad 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 105 ---------LLDALVPDLTLRFALDLEAAiALPELSPL---------------QMKSLPGDHAAAWLPERLST------- 153
Cdd:PRK08315 124 gfkdsdyvaMLYELAPELATCEPGQLQSA-RLPELRRViflgdekhpgmlnfdELLALGRAVDDAELAARQATldpddpi 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 154 -MTLTSGSTGLPKAAVHTcqaH---LASAQGVLSLMPFGAEDDWLLSLPLFHVSGQ--GILwrwlfA----GARMTVrdk 223
Cdd:PRK08315 203 nIQYTSGTTGFPKGATLT---HrniLNNGYFIGEAMKLTEEDRLCIPVPLYHCFGMvlGNL-----AcvthGATMVY--- 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 224 qPLD-----QMLA-----GCThaSL--VPTQLWRLLvnNTPV-------TLKAVLLGGAAIPVELTEQ------AREQGI 278
Cdd:PRK08315 272 -PGEgfdplATLAaveeeRCT--ALygVPTMFIAEL--DHPDfarfdlsSLRTGIMAGSPCPIEVMKRvidkmhMSEVTI 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 279 rcwcGYGLTEfASTV-CAKEADGLAD-----VGSALPGREVRIVND------------EVWLRAASMAQGYWRngqlMP- 339
Cdd:PRK08315 347 ----AYGMTE-TSPVsTQTRTDDPLEkrvttVGRALPHLEVKIVDPetgetvprgeqgELCTRGYSVMKGYWN----DPe 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 340 ----LVNAEGWFATRDRGVL-KDGKLTIVGRMDNLFFSGGEGIQPEEVERVIAAHPHVLQAFIVPIEDKEFGHRPVA--V 412
Cdd:PRK08315 418 ktaeAIDADGWMHTGDLAVMdEEGYVNIVGRIKDMIIRGGENIYPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAwiI 497
|
490 500
....*....|....*....|....*.
gi 489936067 413 VEYDANAGETNLAEWVKDKLARFQQP 438
Cdd:PRK08315 498 LRPGATLTEEDVRDFCRGKIAHYKIP 523
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
30-460 |
1.30e-18 |
|
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: 87.76 E-value: 1.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 30 RAKAPALRLNDEALSWSELCARIDHLASGFAAQGVEEGD--GVLLRawNHPRALLAWLALLQCGARVLPVNPQLPQSLLD 107
Cdd:cd12115 12 TPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESrvGVCLE--RTPDLVVALLAVLKAGAAYVPLDPAYPPERLR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 108 ALVPdltlrfalDLEAAIALPElsplqmkslpgdhaaawlPERLSTMTLTSGSTGLPKAAVHT----------CQAHLAS 177
Cdd:cd12115 90 FILE--------DAQARLVLTD------------------PDDLAYVIYTSGSTGRPKGVAIEhrnaaaflqwAAAAFSA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 178 AQ--GVLSLMPFGaeddwlLSLPLFHVSGQgilwrwLFAGARMTVRDK--QPLDQ-MLAGCTHASLVPTQLWRLL-VNNT 251
Cdd:cd12115 144 EElaGVLASTSIC------FDLSVFELFGP------LATGGKVVLADNvlALPDLpAAAEVTLINTVPSAAAELLrHDAL 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 252 PVTLKAVLLGGAAIPVELTE--QAREQGIRCWCGYGLTEFA--STVCA--KEADGLADVGSALPGREVRIVND------- 318
Cdd:cd12115 212 PASVRVVNLAGEPLPRDLVQrlYARLQVERVVNLYGPSEDTtySTVAPvpPGASGEVSIGRPLANTQAYVLDRalqpvpl 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 319 ----EVWLRAASMAQGYWRNGQLMP---LVNAEG----WFATRDRG-VLKDGKLTIVGRMDNLFFSGGEGIQPEEVERVI 386
Cdd:cd12115 292 gvpgELYIGGAGVARGYLGRPGLTAerfLPDPFGpgarLYRTGDLVrWRPDGLLEFLGRADNQVKVRGFRIELGEIEAAL 371
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489936067 387 AAHPHVLQAFIVPIEDKEFGHRPVAVVEYDANAG--ETNLAEWVKDKLARFQQPVCWLTLP--PELKAGgiKISRRAL 460
Cdd:cd12115 372 RSIPGVREAVVVAIGDAAGERRLVAYIVAEPGAAglVEDLRRHLGTRLPAYMVPSRFVRLDalPLTPNG--KIDRSAL 447
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
25-459 |
1.55e-18 |
|
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: 88.06 E-value: 1.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 25 HWRQVRAKAPALR-LND-----EALSWSELCARIDHLASGFAAQGvEEGDGVLLRAwnhPRALLAWLALLQC-GARVLPV 97
Cdd:cd05931 1 RRAAARPDRPAYTfLDDeggreETLTYAELDRRARAIAARLQAVG-KPGDRVLLLA---PPGLDFVAAFLGClYAGAIAV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 98 ---NPQLPQSL--LDALVPDLTLRFALDLEAAIAL--------PELSPLQMK---SLPGDHAAAWLPERLSTMTL----- 156
Cdd:cd05931 77 plpPPTPGRHAerLAAILADAGPRVVLTTAAALAAvrafaasrPAAGTPRLLvvdLLPDTSAADWPPPSPDPDDIaylqy 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 157 TSGSTGLPKAAVHTCQAHLASAQGVLSLMPFGAEDDWLLSLPLFHVSG--QGIL---------------------WRWL- 212
Cdd:cd05931 157 TSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGliGGLLtplysggpsvlmspaaflrrpLRWLr 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 213 --------------FA----GARMTVRDKQPLDqmLAGcthaslvptqlWRLLVN-NTPV---TLK-------------- 256
Cdd:cd05931 237 lisryratisaapnFAydlcVRRVRDEDLEGLD--LSS-----------WRVALNgAEPVrpaTLRrfaeafapfgfrpe 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 257 ----------AVLL---GGAAIPVELTEQAREQgircwcgYGLTEFASTVCAKEADGLADVGSALPGREVRIVND----- 318
Cdd:cd05931 304 afrpsyglaeATLFvsgGPPGTGPVVLRVDRDA-------LAGRAVAVAADDPAARELVSCGRPLPDQEVRIVDPetgre 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 319 -------EVWLRAASMAQGYWRNGQLMPLVN-------AEGWFATRDRGVLKDGKLTIVGRMDNLFFSGGEGIQPEEVER 384
Cdd:cd05931 377 lpdgevgEIWVRGPSVASGYWGRPEATAETFgalaatdEGGWLRTGDLGFLHDGELYITGRLKDLIIVRGRNHYPQDIEA 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 385 VIAAHPHVLQ-----AFIVPIEDKEfghRPVAVVEYDANAGETNLAEwVKDKL-----ARFQQPVCWLTLppeLKAGGI- 453
Cdd:cd05931 457 TAEEAHPALRpgcvaAFSVPDDGEE---RLVVVAEVERGADPADLAA-IAAAIraavaREHGVAPADVVL---VRPGSIp 529
|
570
....*....|.
gi 489936067 454 -----KISRRA 459
Cdd:cd05931 530 rtssgKIQRRA 540
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
28-462 |
2.90e-18 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 87.05 E-value: 2.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 28 QVRAKAPALRL--NDEALSWSELCARIDHLASGFAAQGVEEGDGVLLRAWNHPRALLAWLALLQCGARVLPVNPQLPQSL 105
Cdd:PRK13391 8 QTTPDKPAVIMasTGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 106 LDALVPD------LTLRFALDLEAAIA--LPELSPLQMKSLPGD--------HAAAWLP------ERLST-MTLTSGSTG 162
Cdd:PRK13391 88 AAYIVDDsgaralITSAAKLDVARALLkqCPGVRHRLVLDGDGElegfvgyaEAVAGLPatpiadESLGTdMLYSSGTTG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 163 LPKAAVhtcqAHLASAQ--------GVL-SLMPFGAEDDWLLSLPLFHVSGQgilwRWLFAGARM----TVRDKQPLDQM 229
Cdd:PRK13391 168 RPKGIK----RPLPEQPpdtplpltAFLqRLWGFRSDMVYLSPAPLYHSAPQ----RAVMLVIRLggtvIVMEHFDAEQY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 230 LA-----GCTHASLVPTQLWRLLVNNTPV-------TLKAVLLGGAAIPVelteQAREQGIRcWCG------YGLTEFA- 290
Cdd:PRK13391 240 LAlieeyGVTHTQLVPTMFSRMLKLPEEVrdkydlsSLEVAIHAAAPCPP----QVKEQMID-WWGpiiheyYAATEGLg 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 291 STVCAKEaDGLA---DVGSALPGrEVRIVND-----------EVWLRAASMAQgYWRNgqlmPLVNAE------GWFATR 350
Cdd:PRK13391 315 FTACDSE-EWLAhpgTVGRAMFG-DLHILDDdgaelppgepgTIWFEGGRPFE-YLND----PAKTAEarhpdgTWSTVG 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 351 DRGVL-KDGKLTIVGRMDNLFFSGGEGIQPEEVERVIAAHPHVLQAFIVPIEDKEFGHRPVAVVE----YDANAG-ETNL 424
Cdd:PRK13391 388 DIGYVdEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQpvdgVDPGPAlAAEL 467
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 489936067 425 AEWVKDKLARFQQP--VCWLTLPPELKAGgiKISRRALSD 462
Cdd:PRK13391 468 IAFCRQRLSRQKCPrsIDFEDELPRLPTG--KLYKRLLRD 505
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
148-429 |
2.67e-17 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 84.77 E-value: 2.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 148 PERLSTMTLTSGSTGLPKAAVHTCQAHLASAQGVLSLMPFGAEDDWLLSLPLFHV-----------SGQGI--------- 207
Cdd:PLN02736 220 PEDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTKFYPSDVHISYLPLAHIyervnqivmlhYGVAVgfyqgdnlk 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 208 ------------------LWRWLFAGARMTVRDKQPLDQMLAGCTHAS--------LVPTQLWRLLVNNTpvtLKAVLLG 261
Cdd:PLN02736 300 lmddlaalrptifcsvprLYNRIYDGITNAVKESGGLKERLFNAAYNAkkqalengKNPSPMWDRLVFNK---IKAKLGG 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 262 -------GAA-IPVELTEQAREQ-GIRCWCGYGLTEFASTVCA-KEADGL-ADVGSALPGREVRIVN------------- 317
Cdd:PLN02736 377 rvrfmssGASpLSPDVMEFLRICfGGRVLEGYGMTETSCVISGmDEGDNLsGHVGSPNPACEVKLVDvpemnytsedqpy 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 318 --DEVWLRAASMAQGYWRNG-QLMPLVNAEGWFATRDRGV-LKDGKLTIVGRMDNLF-FSGGEGIQPEEVERVIAAHPHV 392
Cdd:PLN02736 457 prGEICVRGPIIFKGYYKDEvQTREVIDEDGWLHTGDIGLwLPGGRLKIIDRKKNIFkLAQGEYIAPEKIENVYAKCKFV 536
|
330 340 350
....*....|....*....|....*....|....*..
gi 489936067 393 LQAFivpIEDKEFGHRPVAVVEYDanagETNLAEWVK 429
Cdd:PLN02736 537 AQCF---VYGDSLNSSLVAVVVVD----PEVLKAWAA 566
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
34-460 |
3.95e-17 |
|
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: 83.37 E-value: 3.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 34 PALRLNDEALSWSELCARIDHLASGFAAQGVEEGDGVLLRAWNHPRALLAWLALLQCGARVLPVNPQLPqslldalvPDL 113
Cdd:cd17645 15 VAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYP--------GER 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 114 TLRFALDLEAAIALPElsplqmkslpgdhaaawlPERLSTMTLTSGSTGLPK-------AAVHTCQAHlASAQGVlslmp 186
Cdd:cd17645 87 IAYMLADSSAKILLTN------------------PDDLAYVIYTSGSTGLPKgvmiehhNLVNLCEWH-RPYFGV----- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 187 fGAEDDwllSLPLFHVSGQGILWR---WLFAGARMTVRD---KQPLDQMLAGC-THA---SLVPTQLWRLLVNNTPVTLK 256
Cdd:cd17645 143 -TPADK---SLVYASFSFDASAWEifpHLTAGAALHVVPserRLDLDALNDYFnQEGitiSFLPTGAAEQFMQLDNQSLR 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 257 AVLLGGAAIPVelteqAREQGIRCWCGYGLTEFASTVCAKEAD---GLADVGSALPGREVRIVND-----------EVWL 322
Cdd:cd17645 219 VLLTGGDKLKK-----IERKGYKLVNNYGPTENTVVATSFEIDkpyANIPIGKPIDNTRVYILDEalqlqpigvagELCI 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 323 RAASMAQGYWRNGQLM-------PLVNAEGWFATRDRG-VLKDGKLTIVGRMDNLFFSGGEGIQPEEVERVIAAHPHVLQ 394
Cdd:cd17645 294 AGEGLARGYLNRPELTaekfivhPFVPGERMYRTGDLAkFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIEL 373
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489936067 395 AFIVPIEDKefGHRP--VAVVEYDANAGETNLAEWVKDKLARFQQPVCWLTLPP-ELKAGGiKISRRAL 460
Cdd:cd17645 374 AAVLAKEDA--DGRKylVAYVTAPEEIPHEELREWLKNDLPDYMIPTYFVHLKAlPLTANG-KVDRKAL 439
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
148-460 |
4.95e-17 |
|
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: 83.25 E-value: 4.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 148 PERLSTMTLTSGSTGLPKAAVHTCQAHLASAQGVLSLMPFGAEDDWLLSLPL-FHVSGQGILWRWLfAGARMTVRDKQ-- 224
Cdd:cd17644 105 PENLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEYGITSSDRVLQFASIaFDVAAEEIYVTLL-SGATLVLRPEEmr 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 225 -PLDQMLAGCTHASL----VPTQLWRLLVN-------NTPVTLKAVLLGGAAIPVELTEQARE---QGIRCWCGYGLTE- 288
Cdd:cd17644 184 sSLEDFVQYIQQWQLtvlsLPPAYWHLLVLelllstiDLPSSLRLVIVGGEAVQPELVRQWQKnvgNFIQLINVYGPTEa 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 289 -FASTVCAKEADGLADVGSALPGR-----EVRI-----------VNDEVWLRAASMAQGYWRNGQLM-------PLVNAE 344
Cdd:cd17644 264 tIAATVCRLTQLTERNITSVPIGRpiantQVYIldenlqpvpvgVPGELHIGGVGLARGYLNRPELTaekfishPFNSSE 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 345 G--WFATRDRG-VLKDGKLTIVGRMDNLFFSGGEGIQPEEVERVIAAHPHVLQAFIVPIEDKEFGHRPVA--VVEYDANA 419
Cdd:cd17644 344 SerLYKTGDLArYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAyiVPHYEESP 423
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 489936067 420 GETNLAEWVKDKLARFQQP---VCWLTLPpeLKAGGiKISRRAL 460
Cdd:cd17644 424 STVELRQFLKAKLPDYMIPsafVVLEELP--LTPNG-KIDRRAL 464
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
148-389 |
6.88e-17 |
|
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: 82.76 E-value: 6.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 148 PERLSTMTLTSGSTGLPKAAVHTCQAHLASAQGVLSLMPFGAEDDWLLSLPLFHVSG-QGILWRWLFAGARMtVRDKQPL 226
Cdd:cd05909 146 PDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPFFHSFGlTGCLWLPLLSGIKV-VFHPNPL 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 227 D-----QML--AGCTHASLVPTQLWRLLVNNTP---VTLKAVLLGGAAIPVELTEQARE-QGIRCWCGYGLTEfASTVCA 295
Cdd:cd05909 225 DykkipELIydKKATILLGTPTFLRGYARAAHPedfSSLRLVVAGAEKLKDTLRQEFQEkFGIRILEGYGTTE-CSPVIS 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 296 ---KEADGLAD-VGSALPGREVRIVNDE------------VWLRAASMAQGYWRNGQLMPLVNAEGWFATRDRGVL-KDG 358
Cdd:cd05909 304 vntPQSPNKEGtVGRPLPGMEVKIVSVEtheevpigegglLLVRGPNVMLGYLNEPELTSFAFGDGWYDTGDIGKIdGEG 383
|
250 260 270
....*....|....*....|....*....|.
gi 489936067 359 KLTIVGRMDNLFFSGGEGIQPEEVERVIAAH 389
Cdd:cd05909 384 FLTITGRLSRFAKIAGEMVSLEAIEDILSEI 414
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
107-396 |
1.07e-16 |
|
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: 82.33 E-value: 1.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 107 DALVPDLTLRFALDLEAAIALPELSPLQmkslPGDHAAawlperlstMTLTSGSTGLPKAAVHTCQAHLASAQGVLSLMP 186
Cdd:cd05906 138 LSGLPGIRVLSIEELLDTAADHDLPQSR----PDDLAL---------LMLTSGSTGFPKAVPLTHRNILARSAGKIQHNG 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 187 FGAEDDWLLSLPLFHVSGqgILWRWLFAgarmtvrdkqpldqMLAGC----THASLV---PTQLWRL------------- 246
Cdd:cd05906 205 LTPQDVFLNWVPLDHVGG--LVELHLRA--------------VYLGCqqvhVPTEEIladPLRWLDLidryrvtitwapn 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 247 ----LVNN-----TPVT-----LKAVLLGG----AAIPVELTEQAREQGIRCWC---GYGLTEFAS-----TVCAKE--- 297
Cdd:cd05906 269 fafaLLNDlleeiEDGTwdlssLRYLVNAGeavvAKTIRRLLRLLEPYGLPPDAirpAFGMTETCSgviysRSFPTYdhs 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 298 -ADGLADVGSALPGREVRIVNDE-----------VWLRAASMAQGYWRNgqlmPLVNAE-----GWFATRDRGVLKDGKL 360
Cdd:cd05906 349 qALEFVSLGRPIPGVSMRIVDDEgqllpegevgrLQVRGPVVTKGYYNN----PEANAEaftedGWFRTGDLGFLDNGNL 424
|
330 340 350
....*....|....*....|....*....|....*.
gi 489936067 361 TIVGRMDNLFFSGGEGIQPEEVERVIAAHPHVLQAF 396
Cdd:cd05906 425 TITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPSF 460
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
33-448 |
1.84e-16 |
|
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: 81.55 E-value: 1.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 33 APALRLNDEALSWSELCARIDHLASGFAAQGVEEGD--GVLLRawNHPRALLAWLALLQCGARVLPVNPQLPQSLLDALV 110
Cdd:cd12114 3 ATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDlvAVTLP--KGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 111 PDLTLRFAL-DLEAAIALPELSPLQMKSLPGDHAAAWLPERLSTMTL------TSGSTGLPKAAVHTCQAHLASAQGVLS 183
Cdd:cd12114 81 ADAGARLVLtDGPDAQLDVAVFDVLILDLDALAAPAPPPPVDVAPDDlayvifTSGSTGTPKGVMISHRAALNTILDINR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 184 LMPFGAEDDWL-LS-----LPLFHVSGQgilwrwLFAGARMTV----RDKQPLDQMLAGCTHA----SLVPTQLWRLL-- 247
Cdd:cd12114 161 RFAVGPDDRVLaLSslsfdLSVYDIFGA------LSAGATLVLpdeaRRRDPAHWAELIERHGvtlwNSVPALLEMLLdv 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 248 ---VNNTPVTLKAVLLGGAAIPVELTEQAREQGIRC---WCGyGLTEFA--STVC--AKEADGLADV--GSALPGREVRI 315
Cdd:cd12114 235 leaAQALLPSLRLVLLSGDWIPLDLPARLRALAPDArliSLG-GATEASiwSIYHpiDEVPPDWRSIpyGRPLANQRYRV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 316 VND-----------EVWLRAASMAQGYWRNGQL-----MPLVNAEGWFATRDRGVLK-DGKLTIVGRMDNLFFSGGEGIQ 378
Cdd:cd12114 314 LDPrgrdcpdwvpgELWIGGRGVALGYLGDPELtaarfVTHPDGERLYRTGDLGRYRpDGTLEFLGRRDGQVKVRGYRIE 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 379 PEEVERVIAAHPHVLQAFIVPIEDKEfGHRPVAVVEYDaNAGETNLAEWVKDKLArfqQPVCWLTLPPEL 448
Cdd:cd12114 394 LGEIEAALQAHPGVARAVVVVLGDPG-GKRLAAFVVPD-NDGTPIAPDALRAFLA---QTLPAYMIPSRV 458
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
109-462 |
1.84e-16 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 81.85 E-value: 1.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 109 LVPDLTLRFALDLEAAIALPelsplQMKSLPGDHAAawlPERLSTMTLTSGSTGLPKAAVHTCQAHLASAQ-------GV 181
Cdd:PRK08751 176 LVPEYRINGAIRFREALALG-----RKHSMPTLQIE---PDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQqahqwlaGT 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 182 LSLMPfgAEDDWLLSLPLFHV---SGQGILWRwLFAGARMTV---RDKQPLDQMLAGC--THASLVPTQLWRLLvnNTP- 252
Cdd:PRK08751 248 GKLEE--GCEVVITALPLYHIfalTANGLVFM-KIGGCNHLIsnpRDMPGFVKELKKTrfTAFTGVNTLFNGLL--NTPg 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 253 ------VTLKAVLLGGAAIPVELTEQARE-QGIRCWCGYGLTEFASTVCA-----KEADGlaDVGSALPGREVRIVND-- 318
Cdd:PRK08751 323 fdqidfSSLKMTLGGGMAVQRSVAERWKQvTGLTLVEAYGLTETSPAACInpltlKEYNG--SIGLPIPSTDACIKDDag 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 319 ---------EVWLRAASMAQGYWRNG-QLMPLVNAEGWFATRDRGVL-KDGKLTIVGRMDNLFFSGGEGIQPEEVERVIA 387
Cdd:PRK08751 401 tvlaigeigELCIKGPQVMKGYWKRPeETAKVMDADGWLHTGDIARMdEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIA 480
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489936067 388 AHPHVLQAFIVPIEDKEFGHR-PVAVVEYDANAGETNLAEWVKDKLARFQQP--VCWLTLPPELKAGgiKISRRALSD 462
Cdd:PRK08751 481 MMPGVLEVAAVGVPDEKSGEIvKVVIVKKDPALTAEDVKAHARANLTGYKQPriIEFRKELPKTNVG--KILRRELRD 556
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
148-431 |
2.26e-16 |
|
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: 81.49 E-value: 2.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 148 PERLSTMTLTSGSTGLPKAAVHTcQAHLASAQGVLSLMPFGA----EDDWLLS-LPLFHVSGQGILWRWLFAGARM---- 218
Cdd:cd05927 113 PEDLATICYTSGTTGNPKGVMLT-HGNIVSNVAGVFKILEILnkinPTDVYISyLPLAHIFERVVEALFLYHGAKIgfys 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 219 ----------------------------------TVRDKQPLDQML---------AGCTHASLVPTQLWRLLV-NNTPVT 254
Cdd:cd05927 192 gdirlllddikalkptvfpgvprvlnriydkifnKVQAKGPLKRKLfnfalnyklAELRSGVVRASPFWDKLVfNKIKQA 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 255 L----KAVLLGGAAIPVELTEQAReqGIRCWC---GYGLTE-FASTVCAKEADGLA-DVGSALPGREVRIVN-------- 317
Cdd:cd05927 272 LggnvRLMLTGSAPLSPEVLEFLR--VALGCPvleGYGQTEcTAGATLTLPGDTSVgHVGGPLPCAEVKLVDvpemnyda 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 318 ------DEVWLRAASMAQGYWRNGQLMP-LVNAEGWFATRDRG-VLKDGKLTIVGRMDNLF-FSGGEGIQPEEVERVIAA 388
Cdd:cd05927 350 kdpnprGEVCIRGPNVFSGYYKDPEKTAeALDEDGWLHTGDIGeWLPNGTLKIIDRKKNIFkLSQGEYVAPEKIENIYAR 429
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 489936067 389 HPHVLQAFIVPIEDKEFghrPVAVVEYDanagETNLAEWVKDK 431
Cdd:cd05927 430 SPFVAQIFVYGDSLKSF---LVAIVVPD----PDVLKEWAASK 465
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
157-467 |
2.38e-16 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 81.43 E-value: 2.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 157 TSGSTGLPKAAVHTCQAHLASAQGVL----SLMPFGAEDD-WLLSLPLFHVSGQGILWRWLFA-GARMTVRDKQPLDQML 230
Cdd:PLN02574 206 SSGTTGASKGVVLTHRNLIAMVELFVrfeaSQYEYPGSDNvYLAALPMFHIYGLSLFVVGLLSlGSTIVVMRRFDASDMV 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 231 A-----GCTHASLVPTQLWRLLVNNTPV------TLKAVLLGGAAIPVELTEQARE--QGIRCWCGYGLTEFAST----V 293
Cdd:PLN02574 286 KvidrfKVTHFPVVPPILMALTKKAKGVcgevlkSLKQVSCGAAPLSGKFIQDFVQtlPHVDFIQGYGMTESTAVgtrgF 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 294 CAKEADGLADVGSALPGREVRIVN------------DEVWLRAASMAQGYWRNGQLMPL-VNAEGWFATRDRGVL-KDGK 359
Cdd:PLN02574 366 NTEKLSKYSSVGLLAPNMQAKVVDwstgcllppgncGELWIQGPGVMKGYLNNPKATQStIDKDGWLRTGDIAYFdEDGY 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 360 LTIVGRMDNLFFSGGEGIQPEEVERVIAAHPHVLQAFIVPIEDKEFGHRPVAVVEYDANAG--ETNLAEWVKDKLARFQQ 437
Cdd:PLN02574 446 LYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQGSTlsQEAVINYVAKQVAPYKK 525
|
330 340 350
....*....|....*....|....*....|..
gi 489936067 438 --PVCWLTLPPELKAGgiKISRRALSDWVSAS 467
Cdd:PLN02574 526 vrKVVFVQSIPKSPAG--KILRRELKRSLTNS 555
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
33-460 |
2.44e-16 |
|
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: 80.99 E-value: 2.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 33 APALRLNDEALSWSELCARIDHLASGFAAQGVE-EGDGVLLRAWNHPRALLAWLALLQCGARVLPVNPQLPQSLLDALVP 111
Cdd:cd05958 1 RTCLRSPEREWTYRDLLALANRIANVLVGELGIvPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 112 DLTLRFALDLEAAIAlpelsplqmkslpGDHAAAWlperlstmTLTSGSTGLPKAAVHTCQAHLASAQG----VLSLMPf 187
Cdd:cd05958 81 KARITVALCAHALTA-------------SDDICIL--------AFTSGTTGAPKATMHFHRDPLASADRyavnVLRLRE- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 188 gaEDDWLLSLPLFHVSGQG-ILWRWLFAGARMTVRDKQPLDQMLAgcTHASLVPTQLWrllvnNTPVTLKAVLLG----- 261
Cdd:cd05958 139 --DDRFVGSPPLAFTFGLGgVLLFPFGVGASGVLLEEATPDLLLS--AIARYKPTVLF-----TAPTAYRAMLAHpdaag 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 262 ------------GAAIPVELTEQAREQ-GIRCWCGYGLTE-FASTVCAKEADG-LADVGSALPGREVRIVND-------- 318
Cdd:cd05958 210 pdlsslrkcvsaGEALPAALHRAWKEAtGIPIIDGIGSTEmFHIFISARPGDArPGATGKPVPGYEAKVVDDegnpvpdg 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 319 EVWLRAASMAQGYWRNGQLMPLVNAE-GWFATRDRGVLK-DGKLTIVGRMDNLFFSGGEGIQPEEVERVIAAHPHVLQAF 396
Cdd:cd05958 290 TIGRLAVRGPTGCRYLADKRQRTYVQgGWNITGDTYSRDpDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECA 369
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489936067 397 IVPIEDKEFGHRPVA--VVEYDANAGET---NLAEWVKDKLARFQQP--VCWLTLPPELKAGgiKISRRAL 460
Cdd:cd05958 370 VVGHPDESRGVVVKAfvVLRPGVIPGPVlarELQDHAKAHIAPYKYPraIEFVTELPRTATG--KLQRFAL 438
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
255-462 |
3.64e-16 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 80.96 E-value: 3.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 255 LKAVLLGGAAIPVELTEQARE-QGIRCWCGYGLTEFASTVCAKEADG--LADVGSALPGREVRIVND-----------EV 320
Cdd:PRK05677 328 LKLTLSGGMALQLATAERWKEvTGCAICEGYGMTETSPVVSVNPSQAiqVGTIGIPVPSTLCKVIDDdgnelplgevgEL 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 321 WLRAASMAQGYW-RNGQLMPLVNAEGWFATRDRGVLK-DGKLTIVGRMDNLFFSGGEGIQPEEVERVIAAHPHVLQAFIV 398
Cdd:PRK05677 408 CVKGPQVMKGYWqRPEATDEILDSDGWLKTGDIALIQeDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAI 487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489936067 399 PIEDKEFGH--RPVAVVEYDANAGETNLAEWVKDKLARFQQP--VCWLTLPPELKAGgiKISRRALSD 462
Cdd:PRK05677 488 GVPDEKSGEaiKVFVVVKPGETLTKEQVMEHMRANLTGYKVPkaVEFRDELPTTNVG--KILRRELRD 553
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
149-460 |
5.34e-16 |
|
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: 80.26 E-value: 5.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 149 ERLSTMTLTSGSTGLPKAAVHTCQ---AHLASAQGVLSLMPFGAEDDWLLSLPLFHVSGQGILWRWLFAGAR---MTVRD 222
Cdd:cd17642 184 EQVALIMNSSGSTGLPKGVQLTHKnivARFSHARDPIFGNQIIPDTAILTVIPFHHGFGMFTTLGYLICGFRvvlMYKFE 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 223 KQPLDQMLAG--CTHASLVPTqLWRLLVNNTPV------TLKAVLLGGAAIPVELTEQAREQ----GIRCwcGYGLTEFA 290
Cdd:cd17642 264 EELFLRSLQDykVQSALLVPT-LFAFFAKSTLVdkydlsNLHEIASGGAPLSKEVGEAVAKRfklpGIRQ--GYGLTETT 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 291 STVCA--KEADGLADVGSALPGREVRIVN------------DEVWLRAASMAQGYWRNGQLM-PLVNAEGWFATRDRGVL 355
Cdd:cd17642 341 SAILItpEGDDKPGAVGKVVPFFYAKVVDldtgktlgpnerGELCVKGPMIMKGYVNNPEATkALIDKDGWLHSGDIAYY 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 356 -KDGKLTIVGRMDNLFFSGGEGIQPEEVERVIAAHPHVLQAFIVPIEDKEFGHRPVAVV--EYDANAGETNLAEWVKDKL 432
Cdd:cd17642 421 dEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVvlEAGKTMTEKEVMDYVASQV 500
|
330 340 350
....*....|....*....|....*....|.
gi 489936067 433 A---RFQQPVCWLTLPPELKAGgiKISRRAL 460
Cdd:cd17642 501 StakRLRGGVKFVDEVPKGLTG--KIDRRKI 529
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
148-460 |
7.62e-16 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 80.08 E-value: 7.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 148 PER-LSTMTLTSGSTGLPKAAVHTCQAHLASA-QGVLSLMPFGAEDDWLLS-LPLFHVSGQ-GILWRWLFAGARMTVRDK 223
Cdd:PRK06710 204 PENdLALLQYTGGTTGFPKGVMLTHKNLVSNTlMGVQWLYNCKEGEEVVLGvLPFFHVYGMtAVMNLSIMQGYKMVLIPK 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 224 QPLDQMLAGCTHASLV-----PTQLWRLLvnNTPV-------TLKAVLLGGAAIPVELTEQ-AREQGIRCWCGYGLTEFA 290
Cdd:PRK06710 284 FDMKMVFEAIKKHKVTlfpgaPTIYIALL--NSPLlkeydisSIRACISGSAPLPVEVQEKfETVTGGKLVEGYGLTESS 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 291 STVCAK---EADGLADVGSALPGREVRIVN------------DEVWLRAASMAQGYWRNGQLMPLVNAEGWFATRDRGVL 355
Cdd:PRK06710 362 PVTHSNflwEKRVPGSIGVPWPDTEAMIMSletgealppgeiGEIVVKGPQIMKGYWNKPEETAAVLQDGWLHTGDVGYM 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 356 -KDGKLTIVGRMDNLFFSGGEGIQPEEVERVIAAHPHVLQAFIVPIEDKEFGH--RPVAVVEYDANAGETNLAEWVKDKL 432
Cdd:PRK06710 442 dEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGEtvKAFVVLKEGTECSEEELNQFARKYL 521
|
330 340
....*....|....*....|....*....
gi 489936067 433 ARFQQPVCWlTLPPELKAGGI-KISRRAL 460
Cdd:PRK06710 522 AAYKVPKVY-EFRDELPKTTVgKILRRVL 549
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
157-438 |
1.05e-15 |
|
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: 78.11 E-value: 1.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 157 TSGSTGLPKAAVHTCQAHLASAQGVLSLMPFGAEDDWLLSLPLFHVSGQ-GILWRWLFAGARMTVR--DKQPLDQMLA-- 231
Cdd:cd17636 8 TAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTVFLNSGPLFHIGTLmFTLATFHAGGTNVFVRrvDAEEVLELIEae 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 232 GCTHASLVPT---QLWRLLVNNTP--VTLKAVL---LGGAAIPVELTEQAREQGircwcGYGLTEFA--STVCAKEADGL 301
Cdd:cd17636 88 RCTHAFLLPPtidQIVELNADGLYdlSSLRSSPaapEWNDMATVDTSPWGRKPG-----GYGQTEVMglATFAALGGGAI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 302 ADVGSALPGREVRIVND-----------EVWLRAASMAQGYWRNgqlmPLVNAE----GWFATRDRGV-LKDGKLTIVGR 365
Cdd:cd17636 163 GGAGRPSPLVQVRILDEdgrevpdgevgEIVARGPTVMAGYWNR----PEVNARrtrgGWHHTNDLGRrEPDGSLSFVGP 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489936067 366 MDNLFFSGGEGIQPEEVERVIAAHPHVLQAFIVPIEDKEFGHRPVAVV--EYDANAGETNLAEWVKDKLARFQQP 438
Cdd:cd17636 239 KTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVvlKPGASVTEAELIEHCRARIASYKKP 313
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
154-438 |
1.72e-15 |
|
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: 77.81 E-value: 1.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 154 MTLTSGSTGLPKAaVHTCQAHLASAQGVLSLMPFGAEDD---------------WLLSLPLFHVSGQgilWRWLFA---- 214
Cdd:cd05924 8 ILYTGGTTGMPKG-VMWRQEDIFRMLMGGADFGTGEFTPsedahkaaaaaagtvMFPAPPLMHGTGS---WTAFGGllgg 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 215 GARMTVRDKQPLDQMLA-----GCTHASLVPTQLWRLLV------NNTPVT-LKAVLLGGAAipveLTEQAREQGIRCWC 282
Cdd:cd05924 84 QTVVLPDDRFDPEEVWRtiekhKVTSMTIVGDAMARPLIdalrdaGPYDLSsLFAISSGGAL----LSPEVKQGLLELVP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 283 ------GYGLTEFASTVCAKEADGLADVGS-ALPGREVRIVNDEV-----------WL-RAASMAQGYWRN----GQLMP 339
Cdd:cd05924 160 nitlvdAFGSSETGFTGSGHSAGSGPETGPfTRANPDTVVLDDDGrvvppgsggvgWIaRRGHIPLGYYGDeaktAETFP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 340 LVNAEGWFATRDRG-VLKDGKLTIVGRMDNLFFSGGEGIQPEEVERVIAAHPHVLQAFIVPIEDKEFGHRPVAVVEYDAN 418
Cdd:cd05924 240 EVDGVRYAVPGDRAtVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQEVVAVVQLREG 319
|
330 340
....*....|....*....|..
gi 489936067 419 AG--ETNLAEWVKDKLARFQQP 438
Cdd:cd05924 320 AGvdLEELREHCRTRIARYKLP 341
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
30-466 |
1.45e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 75.94 E-value: 1.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 30 RAKAPALRLNDEALSWSELCARIDHLASGFAAQGVEEGDGVLLRAWNHPRALLAWLALLQCGARVLPVN----------- 98
Cdd:PRK06164 23 RPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNtryrshevahi 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 99 --------------------PQLPQSLLDALVPDLTLRFALDlEAAIALPELSPLQMKSLPGDHAAAWL---------PE 149
Cdd:PRK06164 103 lgrgrarwlvvwpgfkgidfAAILAAVPPDALPPLRAIAVVD-DAADATPAPAPGARVQLFALPDPAPPaaageraadPD 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 150 RLSTMTLTSGSTGLPKAAVHTCQAHLASAQGVLSLMPFGAEDDWLLSLPLFHVSGQGILWRWLFAGARMTVRD----KQP 225
Cdd:PRK06164 182 AGALLFTTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFGFSTLLGALAGGAPLVCEPvfdaART 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 226 LDQML-AGCTHAsLVPTQLWRLLVNNTPVTL---KAVLLGGAAIP---VELTEQAREQGIRCWCGYGLTEFASTVCAKEA 298
Cdd:PRK06164 262 ARALRrHRVTHT-FGNDEMLRRILDTAGERAdfpSARLFGFASFApalGELAALARARGVPLTGLYGSSEVQALVALQPA 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 299 DGLADV----GSAL--PGREVRIVN------------DEVWLRAASMAQGYWRNGQLMP-LVNAEGWFATRDRGVLK-DG 358
Cdd:PRK06164 341 TDPVSVriegGGRPasPEARVRARDpqdgallpdgesGEIEIRAPSLMRGYLDNPDATArALTDDGYFRTGDLGYTRgDG 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 359 KLTIVGRMDNLFFSGGEGIQPEEVERVIAAHPHVLQAFIVPIEDKEFGhRPVAVV--EYDANAGETNLAEWVKDKLARFQ 436
Cdd:PRK06164 421 QFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGATRDGKT-VPVAFVipTDGASPDEAGLMAACREALAGFK 499
|
490 500 510
....*....|....*....|....*....|...
gi 489936067 437 QPVCWLTL---PPELKAGGIKISRRALSDWVSA 466
Cdd:PRK06164 500 VPARVQVVeafPVTESANGAKIQKHRLREMAQA 532
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
31-401 |
1.75e-14 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 76.53 E-value: 1.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 31 AKAPALRLNDEALSWSELCARIDHLASGFAAQGVEEGDGVLLRAWNHPRALLAWLALLQCGARVLPVNPQLPQSLLDALV 110
Cdd:PRK12316 4565 PDAVAVVFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMM 4644
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 111 PDLtlRFALDLEAAIALPEL-SPLQMKSLPGDHAAAW------------LPERLSTMTLTSGSTGLPKAA---VHTCQAH 174
Cdd:PRK12316 4645 EDS--GAALLLTQSHLLQRLpIPDGLASLALDRDEDWegfpahdpavrlHPDNLAYVIYTSGSTGRPKGVavsHGSLVNH 4722
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 175 LASAQGVLSLMPfgaeDDWLLSLPLFHVSGQGILWRW-LFAGARMTVRDKQPLD------QML-AGCTHASLVPTQLWRL 246
Cdd:PRK12316 4723 LHATGERYELTP----DDRVLQFMSFSFDGSHEGLYHpLINGASVVIRDDSLWDperlyaEIHeHRVTVLVFPPVYLQQL 4798
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 247 L----VNNTPVTLKAVLLGGAAIPVELTEQA--REQGIRCWCGYGLTEFASTV-CAKEADGLAD------VGSALPGREV 313
Cdd:PRK12316 4799 AehaeRDGEPPSLRVYCFGGEAVAQASYDLAwrALKPVYLFNGYGPTETTVTVlLWKARDGDACgaaympIGTPLGNRSG 4878
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 314 RIVND-----------EVWLRAASMAQGYWRNgqlmPLVNAEGWFA----------------TRDRGvlkDGKLTIVGRM 366
Cdd:PRK12316 4879 YVLDGqlnplpvgvagELYLGGEGVARGYLER----PALTAERFVPdpfgapggrlyrtgdlARYRA---DGVIDYLGRV 4951
|
410 420 430
....*....|....*....|....*....|....*
gi 489936067 367 DNLFFSGGEGIQPEEVERVIAAHPHVLQAFIVPIE 401
Cdd:PRK12316 4952 DHQVKIRGFRIELGEIEARLREHPAVREAVVIAQE 4986
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
157-462 |
6.93e-14 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 73.93 E-value: 6.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 157 TSGSTGLPKAAVHT---CQAHLASAQGVLSLMPFGAEDDWLLSLPLFHVsgqgilwrwlFAgarMTV------------- 220
Cdd:PRK08974 214 TGGTTGVAKGAMLThrnMLANLEQAKAAYGPLLHPGKELVVTALPLYHI----------FA---LTVncllfielggqnl 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 221 -----RD---------KQPLdqmlagcTHASLVPTqLWRLLVNNTPV------TLKAVLLGGAAIPVELTEQARE-QGIR 279
Cdd:PRK08974 281 litnpRDipgfvkelkKYPF-------TAITGVNT-LFNALLNNEEFqeldfsSLKLSVGGGMAVQQAVAERWVKlTGQY 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 280 CWCGYGLTEFASTVCA-----KEADGlaDVGSALPGREVRIVND-----------EVWLRAASMAQGYWRNGQLMPLVNA 343
Cdd:PRK08974 353 LLEGYGLTECSPLVSVnpydlDYYSG--SIGLPVPSTEIKLVDDdgnevppgepgELWVKGPQVMLGYWQRPEATDEVIK 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 344 EGWFATRDRGVL-KDGKLTIVGRMDNLFFSGGEGIQPEEVERVIAAHPHVLQAFIVPIEDKEFGHR-PVAVVEYDANAGE 421
Cdd:PRK08974 431 DGWLATGDIAVMdEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAvKIFVVKKDPSLTE 510
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 489936067 422 TNLAEWVKDKLARFQQP--VCWLTLPPELKAGgiKISRRALSD 462
Cdd:PRK08974 511 EELITHCRRHLTGYKVPklVEFRDELPKSNVG--KILRRELRD 551
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
2-399 |
8.24e-14 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 74.31 E-value: 8.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 2 TQQERPDsVSLSGLIQpsdwpwrhwRQVRA--KAPALRLNDEALSWSELCARIDHLASGFAAQGVEEGDGVllrAWNHPR 79
Cdd:PRK10252 451 TAVEIPE-TTLSALVA---------QQAAKtpDAPALADARYQFSYREMREQVVALANLLRERGVKPGDSV---AVALPR 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 80 ALLAWLALL---QCGARVLPVNPQLPQSLLDALV----PDLTLRFALDLEAAIALPELSPLQMKSLPGDHAAAWL----P 148
Cdd:PRK10252 518 SVFLTLALHaivEAGAAWLPLDTGYPDDRLKMMLedarPSLLITTADQLPRFADVPDLTSLCYNAPLAPQGAAPLqlsqP 597
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 149 ERLSTMTLTSGSTGLPKAAVHTCQAHLASAQGVLSLMPFGAEDDWLLSLPL-FHVSGQGILWRwLFAGARMTV------R 221
Cdd:PRK10252 598 HHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTADDVVLQKTPCsFDVSVWEFFWP-FIAGAKLVMaepeahR 676
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 222 DKQPLDQMLA--GCTHASLVPTQLWRLLVNNTP-------VTLKAVLLGGAAIPVELT-EQAREQGIRCWCGYGLTEFAS 291
Cdd:PRK10252 677 DPLAMQQFFAeyGVTTTHFVPSMLAAFVASLTPegarqscASLRQVFCSGEALPADLCrEWQQLTGAPLHNLYGPTEAAV 756
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 292 TVCA--KEADGLADV-GSALP-GREV-----RIVND-----------EVWLRAASMAQGYWRNGQLM-------PLVNAE 344
Cdd:PRK10252 757 DVSWypAFGEELAAVrGSSVPiGYPVwntglRILDArmrpvppgvagDLYLTGIQLAQGYLGRPDLTasrfiadPFAPGE 836
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 489936067 345 GWFATRDRGV-LKDGKLTIVGRMDNLFFSGGEGIQPEEVERVIAAHPHVLQAFIVP 399
Cdd:PRK10252 837 RMYRTGDVARwLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAVTHA 892
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
109-462 |
9.99e-14 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 73.32 E-value: 9.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 109 LVPDLTLRFALDLEAAIALPELSPLQMKSLPGDHAAawlperlsTMTLTSGSTGLPKAAVHTCQAHLASAQGVLSLM-PF 187
Cdd:PRK12492 175 MVPAYHLPQAVPFKQALRQGRGLSLKPVPVGLDDIA--------VLQYTGGTTGLAKGAMLTHGNLVANMLQVRACLsQL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 188 GAEDDWLLS---------LPLFHVsgqgilwrWLFAGARMTVrdkqpldqMLAGcTHASLVPT-----------QLWR-- 245
Cdd:PRK12492 247 GPDGQPLMKegqevmiapLPLYHI--------YAFTANCMCM--------MVSG-NHNVLITNprdipgfikelGKWRfs 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 246 -LLVNNT--------P-------VTLKAVLLGGAAIpVELTEQAREQ--GIRCWCGYGLTEFASTVCAK---EADGLADV 304
Cdd:PRK12492 310 aLLGLNTlfvalmdhPgfkdldfSALKLTNSGGTAL-VKATAERWEQltGCTIVEGYGLTETSPVASTNpygELARLGTV 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 305 GSALPGREVRIVND-----------EVWLRAASMAQGYW-RNGQLMPLVNAEGWFATRDRGVL-KDGKLTIVGRMDNLFF 371
Cdd:PRK12492 389 GIPVPGTALKVIDDdgnelplgergELCIKGPQVMKGYWqQPEATAEALDAEGWFKTGDIAVIdPDGFVRIVDRKKDLII 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 372 SGGEGIQPEEVERVIAAHPHVLQAFIVPIEDKEFGHR-PVAVVEYDANAGETNLAEWVKDKLARFQQP---VCWLTLPpe 447
Cdd:PRK12492 469 VSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAvKLFVVARDPGLSVEELKAYCKENFTGYKVPkhiVLRDSLP-- 546
|
410
....*....|....*
gi 489936067 448 LKAGGiKISRRALSD 462
Cdd:PRK12492 547 MTPVG-KILRRELRD 560
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
148-433 |
1.05e-13 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 73.80 E-value: 1.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 148 PERLSTMTLTSGSTGLPKAAVHTCQAHLASAQGVLSLMPFGAEDDWLLSLPLFHVSG-QGILWRWLFAGARMtVRDKQPL 226
Cdd:PRK08633 781 PDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSSLPFFHSFGlTVTLWLPLLEGIKV-VYHPDPT 859
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 227 DqmlaGCTHASLV-----------PTQLwRLLVNNTPV------TLKAVLLGGAAIPVELTEQAREQ-GIRCWCGYGLTE 288
Cdd:PRK08633 860 D----ALGIAKLVakhratillgtPTFL-RLYLRNKKLhplmfaSLRLVVAGAEKLKPEVADAFEEKfGIRILEGYGATE 934
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 289 FASTVCAKEADGLAD------------VGSALPGREVRIVNDE------------VWLRAASMAQGYWRNGQL----MPL 340
Cdd:PRK08633 935 TSPVASVNLPDVLAAdfkrqtgskegsVGMPLPGVAVRIVDPEtfeelppgedglILIGGPQVMKGYLGDPEKtaevIKD 1014
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 341 VNAEGWFATRDRGVL-KDGKLTIVGRMDNlfFS--GGE----GIQPEEVERVIAAHPHVLQAFIVPIEDKefGHRPVAVV 413
Cdd:PRK08633 1015 IDGIGWYVTGDKGHLdEDGFLTITDRYSR--FAkiGGEmvplGAVEEELAKALGGEEVVFAVTAVPDEKK--GEKLVVLH 1090
|
330 340
....*....|....*....|
gi 489936067 414 EYDANAGETnlaewVKDKLA 433
Cdd:PRK08633 1091 TCGAEDVEE-----LKRAIK 1105
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
154-436 |
1.31e-13 |
|
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: 72.85 E-value: 1.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 154 MTLTSGSTGLPKAAVHTCQ-AHL-ASAQGVLSLMPFGAEDDWLLSLPLFHVSGQGILWR-WLFAGARMTVR----DKQPL 226
Cdd:cd05915 158 MAYTTGTTGLPKGVVYSHRaLVLhSLAASLVDGTALSEKDVVLPVVPMFHVNAWCLPYAaTLVGAKQVLPGprldPASLV 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 227 DQMLA-GCTHASLVPTQLwRLLVN-------NTPVTLKaVLLGGAAIPVELTEQAREQGIRCWCGYGLTEF--ASTVCA- 295
Cdd:cd05915 238 ELFDGeGVTFTAGVPTVW-LALADylestghRLKTLRR-LVVGGSAAPRSLIARFERMGVEVRQGYGLTETspVVVQNFv 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 296 ---------------KEADGLADVGSALP------------GREVRIVNdevwLRAASMAQGYWRNGQLMPLVNAEG-WF 347
Cdd:cd05915 316 kshleslseeekltlKAKTGLPIPLVRLRvadeegrpvpkdGKALGEVQ----LKGPWITGGYYGNEEATRSALTPDgFF 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 348 ATRDRGVLK-DGKLTIVGRMDNLFFSGGEGIQPEEVERVIAAHPHVLQAFIVPIEDKEFGHRPVAVVEY-DANAGETNLA 425
Cdd:cd05915 392 RTGDIAVWDeEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVVVPrGEKPTPEELN 471
|
330
....*....|.
gi 489936067 426 EWVKDKLARFQ 436
Cdd:cd05915 472 EHLLKAGFAKW 482
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
33-438 |
1.50e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 72.61 E-value: 1.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 33 APALRLNDEALSWSELCARIDHLASGFAAQGVEEGDGVLLRAWNHPRALLAWLALLQcgARVLPVN------PQLPQSLL 106
Cdd:PRK07798 19 RVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFK--ARAVPVNvnyryvEDELRYLL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 107 D-----ALV-------------PDLT----------------LRFALDLEAAIALPELSPLQMKSLPGDHaaawlperls 152
Cdd:PRK07798 97 DdsdavALVyerefaprvaevlPRLPklrtlvvvedgsgndlLPGAVDYEDALAAGSPERDFGERSPDDL---------- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 153 TMTLTSGSTGLPK----------------------AAVHTCQAHLASAQGvlslmpfGAEDDWLLSLPLFHVSGQGILWR 210
Cdd:PRK07798 167 YLLYTGGTTGMPKgvmwrqedifrvllggrdfatgEPIEDEEELAKRAAA-------GPGMRRFPAPPLMHGAGQWAAFA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 211 WLFAGARMTVRDKQPLDqmlagcthaslvPTQLWRLL----VNNTPVT----------------------LKAVLLGGAA 264
Cdd:PRK07798 240 ALFSGQTVVLLPDVRFD------------ADEVWRTIerekVNVITIVgdamarplldaleargpydlssLFAIASGGAL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 265 ipveLTEQAREQgircWC----------GYGLTE--FASTVCAKEADGLADVGSALPGREVRIVNDEV-----------W 321
Cdd:PRK07798 308 ----FSPSVKEA----LLellpnvvltdSIGSSEtgFGGSGTVAKGAVHTGGPRFTIGPRTVVLDEDGnpvepgsgeigW 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 322 L-RAASMAQGYW----RNGQLMPLVNAEGWFATRDRG-VLKDGKLTIVGRMDNLFFSGGEGIQPEEVERVIAAHPHVLQA 395
Cdd:PRK07798 380 IaRRGHIPLGYYkdpeKTAETFPTIDGVRYAIPGDRArVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADA 459
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 489936067 396 FIVPIEDKEFGHRPVAVVEYDANAG--ETNLAEWVKDKLARFQQP 438
Cdd:PRK07798 460 LVVGVPDERWGQEVVAVVQLREGARpdLAELRAHCRSSLAGYKVP 504
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
255-462 |
2.31e-13 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 71.98 E-value: 2.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 255 LKAVLLGGAAIPVELTEQAREQgIRCWC--GYGLTEFASTVCAKEADGLA---DVGSALPGREVRIVND----------- 318
Cdd:PRK07059 329 LIVANGGGMAVQRPVAERWLEM-TGCPIteGYGLSETSPVATCNPVDATEfsgTIGLPLPSTEVSIRDDdgndlplgepg 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 319 EVWLRAASMAQGYW-RNGQLMPLVNAEGWFATRDRGVL-KDGKLTIVGRMDNLFFSGGEGIQPEEVERVIAAHPHVLQAF 396
Cdd:PRK07059 408 EICIRGPQVMAGYWnRPDETAKVMTADGFFRTGDVGVMdERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVA 487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489936067 397 IVPIEDKEFGHRPVA-VVEYDANAGETNLAEWVKDKLARFQQP--VCWLTLPPELKAGgiKISRRALSD 462
Cdd:PRK07059 488 AVGVPDEHSGEAVKLfVVKKDPALTEEDVKAFCKERLTNYKRPkfVEFRTELPKTNVG--KILRRELRD 554
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
157-413 |
3.62e-13 |
|
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: 71.48 E-value: 3.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 157 TSGSTGLPKAAVHTCQAHLASAQGVLSLMP-FGAEDDWLLS-LPLFHV---SGQGILwrwLFAGARMTVRDKQPL-DQML 230
Cdd:cd17639 96 TSGSTGNPKGVMLTHGNLVAGIAGLGDRVPeLLGPDDRYLAyLPLAHIfelAAENVC---LYRGGTIGYGSPRTLtDKSK 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 231 AGC---------THASLVP-----------------------------------------TQLWRLLVNNTP--VT---L 255
Cdd:cd17639 173 RGCkgdltefkpTLMVGVPaiwdtirkgvlaklnpmgglkrtlfwtayqsklkalkegpgTPLLDELVFKKVraALggrL 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 256 KAVLLGGAAipveLTEQAREQGIRCWC----GYGLTEfasTVCAKEADGLAD-----VGSALPGREVRIVN--------- 317
Cdd:cd17639 253 RYMLSGGAP----LSADTQEFLNIVLCpviqGYGLTE---TCAGGTVQDPGDletgrVGPPLPCCEIKLVDweeggystd 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 318 -----DEVWLRAASMAQGYWRNGQLMPLV-NAEGWFATRDRG-VLKDGKLTIVGRMDNLF-FSGGEGIQPEEVERVIAAH 389
Cdd:cd17639 326 kppprGEILIRGPNVFKGYYKNPEKTKEAfDGDGWFHTGDIGeFHPDGTLKIIDRKKDLVkLQNGEYIALEKLESIYRSN 405
|
330 340
....*....|....*....|....*.
gi 489936067 390 PHVLQ--AFIVPIEDKefghrPVAVV 413
Cdd:cd17639 406 PLVNNicVYADPDKSY-----PVAIV 426
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
157-413 |
3.65e-13 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 71.74 E-value: 3.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 157 TSGSTGLPKAAVHTCQAHLASAQGVLSLMPFGAEDD--WLLSLPLFHVSGQGILWRWLFAGARMTVRDKQPLDQMLAGCT 234
Cdd:PRK05620 189 STGTTGAPKGVVYSHRSLYLQSLSLRTTDSLAVTHGesFLCCVPIYHVLSWGVPLAAFMSGTPLVFPGPDLSAPTLAKII 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 235 HASL------VPTqLW-RLLVN---NTP--VTLKAVLLGGAAIPVELTEQAREQG----IRCWcgyGLTEfASTV--CAK 296
Cdd:PRK05620 269 ATAMprvahgVPT-LWiQLMVHylkNPPerMSLQEIYVGGSAVPPILIKAWEERYgvdvVHVW---GMTE-TSPVgtVAR 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 297 EADGLADVGSAL----PGR-----EVRIVND------------EVWLRAASMAQGYW-----RNGQLMPLVN-------- 342
Cdd:PRK05620 344 PPSGVSGEARWAyrvsQGRfpaslEYRIVNDgqvmestdrnegEIQVRGNWVTASYYhspteEGGGAASTFRgedvedan 423
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489936067 343 ----AEGWFATRDRG-VLKDGKLTIVGRMDNLFFSGGEGIQPEEVERVIAAHPHVLQAFIVPIEDKEFGHRPVAVV 413
Cdd:PRK05620 424 drftADGWLRTGDVGsVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLAVT 499
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
13-462 |
4.20e-13 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 72.12 E-value: 4.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 13 SGLIQPSDWPWRHW--RQV--RAKAPALRLNDEALSWSELCARIDHLASGFAAQGVEEGDGVLLRAWNHPRALLAWLALL 88
Cdd:PRK12467 3087 TAAAYPSERLVHQLieAQVarTPEAPALVFGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVL 3166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 89 QCGARVLPVNPQLPQSLLDALVPDLTLRFALDLEAAIA-LPELSPLQMKSLPGDHAAAWLPERLSTMTL---------TS 158
Cdd:PRK12467 3167 KAGGAYVPLDPEYPRERLAYMIEDSGVKLLLTQAHLLEqLPAPAGDTALTLDRLDLNGYSENNPSTRVMgenlayviyTS 3246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 159 GSTGLPKAAVHTCQAHLASAQGVLSLMPFGAEDDWLLSLPLfhvSGQGILWRW---LFAGARMTVRDKQPLD------QM 229
Cdd:PRK12467 3247 GSTGKPKGVGVRHGALANHLCWIAEAYELDANDRVLLFMSF---SFDGAQERFlwtLICGGCLVVRDNDLWDpeelwqAI 3323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 230 LA-GCTHASLVPTQLWRLLVNNTP---VTLKAVLLGGAAIPVELTEQAREQGIRCWC--GYGLTEFASTV----CAKEAD 299
Cdd:PRK12467 3324 HAhRISIACFPPAYLQQFAEDAGGadcASLDIYVFGGEAVPPAAFEQVKRKLKPRGLtnGYGPTEAVVTVtlwkCGGDAV 3403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 300 GLAD---VGSALPGREVRI-----------VNDEVWLRAASMAQGYWRNGQLMP--------LVNAEGWFATRDRG-VLK 356
Cdd:PRK12467 3404 CEAPyapIGRPVAGRSIYVldgqlnpvpvgVAGELYIGGVGLARGYHQRPSLTAerfvadpfSGSGGRLYRTGDLArYRA 3483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 357 DGKLTIVGRMDNLFFSGGEGIQPEEVERVIAAHPHVLQAFIVPIeDKEFGHRPVAVVEYDANAGEtnLAEWVKDKLAR-- 434
Cdd:PRK12467 3484 DGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLAR-DGAGGKQLVAYVVPADPQGD--WRETLRDHLAAsl 3560
|
490 500 510
....*....|....*....|....*....|..
gi 489936067 435 --FQQPVCWLTLP--PELKAGgiKISRRALSD 462
Cdd:PRK12467 3561 pdYMVPAQLLVLAamPLGPNG--KVDRKALPD 3590
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
24-468 |
5.00e-13 |
|
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: 71.03 E-value: 5.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 24 RHWRQVRAKAPALRLNDEALSWSELCARIDHLASGFAAQGVEEGD-----------------GVLlRAwnhprallawla 86
Cdd:cd05918 6 EERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVfvplcfekskwavvamlAVL-KA------------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 87 llqcGARVLPVNPQLPQSLLDALVPDLtlrfaldlEAAIALpelsplqmKSLPGDHA-AAWlperlstmtlTSGSTGLPK 165
Cdd:cd05918 73 ----GGAFVPLDPSHPLQRLQEILQDT--------GAKVVL--------TSSPSDAAyVIF----------TSGSTGKPK 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 166 AAVHTCQAHLASAQGVLSLMPFGAEDDWL-LSLPLFHVSGQGILWRWLFAGarmTV---RDKQPLDQmLAGC------TH 235
Cdd:cd05918 123 GVVIEHRALSTSALAHGRALGLTSESRVLqFASYTFDVSILEIFTTLAAGG---CLcipSEEDRLND-LAGFinrlrvTW 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 236 ASLVPTqLWRLLVNNTPVTLKAVLLGGAAIPVELTEQArEQGIRCWCGYGLTEfaSTVCA--KEADGLAD---VGSALPG 310
Cdd:cd05918 199 AFLTPS-VARLLDPEDVPSLRTLVLGGEALTQSDVDTW-ADRVRLINAYGPAE--CTIAAtvSPVVPSTDprnIGRPLGA 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 311 ReVRIVND-------------EVWLRAASMAQGYWRN------GQLMPLVNAEGWFATRDRGVLK---------DGKLTI 362
Cdd:cd05918 275 T-CWVVDPdnhdrlvpigavgELLIEGPILARGYLNDpektaaAFIEDPAWLKQEGSGRGRRLYRtgdlvrynpDGSLEY 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 363 VGRMDNLFFSGGEGIQPEEVERVIAAHPHVLQ---AFIVPIEDKEFGHRPVAVVEYDANAGETN---------------- 423
Cdd:cd05918 354 VGRKDTQVKIRGQRVELGEIEHHLRQSLPGAKevvVEVVKPKDGSSSPQLVAFVVLDGSSSGSGdgdslflepsdefral 433
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 489936067 424 ---LAEWVKDKLARFQQPVCWLTLP--PELKAGgiKISRRALSDWVSASS 468
Cdd:cd05918 434 vaeLRSKLRQRLPSYMVPSVFLPLShlPLTASG--KIDRRALRELAESLS 481
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
33-460 |
5.21e-13 |
|
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: 70.57 E-value: 5.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 33 APALRLNDEALSWSELCARIDHLASGFAAQGVEEGDGVLLRAWNHPRALLAWLALLQCGARVLPVNPQLPQSLLDALvpd 112
Cdd:cd17650 3 AIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYM--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 113 ltlrfALDLEAAIALPElsplqmkslpgdhaaawlPERLSTMTLTSGSTGLPKAAVHTcQAHLASAQgvlslmpFGAEDD 192
Cdd:cd17650 80 -----LEDSGAKLLLTQ------------------PEDLAYVIYTSGTTGKPKGVMVE-HRNVAHAA-------HAWRRE 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 193 W-LLSLPLFHVS--------GQGILWRWLFAGARM------TVRDKQPLDQML--AGCTHASLVPTqLWRLLVNN----- 250
Cdd:cd17650 129 YeLDSFPVRLLQmasfsfdvFAGDFARSLLNGGTLvicpdeVKLDPAALYDLIlkSRITLMESTPA-LIRPVMAYvyrng 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 251 -TPVTLKAVLLGG----AAIPVELTEQAReQGIRCWCGYGLTEFA--STVCAKEADGLAD-----VGSALPGREVRIVND 318
Cdd:cd17650 208 lDLSAMRLLIVGSdgckAQDFKTLAARFG-QGMRIINSYGVTEATidSTYYEEGRDPLGDsanvpIGRPLPNTAMYVLDE 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 319 -----------EVWLRAASMAQGYWRNGQLM-------PLVNAEGWFATRDRGV-LKDGKLTIVGRMDNLFFSGGEGIQP 379
Cdd:cd17650 287 rlqpqpvgvagELYIGGAGVARGYLNRPELTaerfvenPFAPGERMYRTGDLARwRADGNVELLGRVDHQVKIRGFRIEL 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 380 EEVERVIAAHPHVLQAFIVPIEDKEFGHRPVAVVEYDANAGETNLAEWVKDKLARFQQPVCWLTLPPELKAGGIKISRRA 459
Cdd:cd17650 367 GEIESQLARHPAIDEAVVAVREDKGGEARLCAYVVAAATLNTAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRA 446
|
.
gi 489936067 460 L 460
Cdd:cd17650 447 L 447
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
2-401 |
5.45e-13 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 71.73 E-value: 5.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 2 TQQERPDSVSLSGLIQpsdwpwrhwRQVRA--KAPALRLNDEALSWSELCARIDHLASGFAAQGVEEGDGVLLRAWNHPR 79
Cdd:PRK12467 1566 THTGYPLARLVHQLIE---------DQAAAtpEAVALVFGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLE 1636
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 80 ALLAWLALLQCGARVLPVNPQLPQSLLDALVPDLTLRfaLDLEAAIALPEL-SPLQMKSLPGDHAAAWL----------- 147
Cdd:PRK12467 1637 MVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIE--LLLTQSHLQARLpLPDGLRSLVLDQEDDWLegysdsnpavn 1714
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 148 --PERLSTMTLTSGSTGLPKAAVHTCQAHLASAQGVLSLMPFGAEDDWLLSLPL-FHVSGQGILWRwLFAGARMTV---- 220
Cdd:PRK12467 1715 laPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTSFaFDVSVWELFWP-LINGARLVIappg 1793
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 221 --RDKQPLDQMLA--GCTHASLVPTQLWRLLVNN----TPVTLKAVLLGGAAIPVELTEQAREQ--GIRCWCGYGLTEFA 290
Cdd:PRK12467 1794 ahRDPEQLIQLIErqQVTTLHFVPSMLQQLLQMDeqveHPLSLRRVVCGGEALEVEALRPWLERlpDTGLFNLYGPTETA 1873
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 291 STVCAKEADGLAD-------VGSALPGREVRIVND-----------EVWLRAASMAQGYWRNgqlmPLVNAEGWFA---- 348
Cdd:PRK12467 1874 VDVTHWTCRRKDLegrdsvpIGQPIANLSTYILDAslnpvpigvagELYLGGVGLARGYLNR----PALTAERFVAdpfg 1949
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489936067 349 ------------TRDRGvlkDGKLTIVGRMDNLFFSGGEGIQPEEVERVIAAHPHVLQAFIVPIE 401
Cdd:PRK12467 1950 tvgsrlyrtgdlARYRA---DGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIAQD 2011
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
111-413 |
6.72e-13 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 70.78 E-value: 6.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 111 PDLTLRFALDLEAAialpELSPLQMKSLPGDHAAawLPerlstmtLTSGSTGLPKAAVHTCQAHLAS-AQGVLSLMP--- 186
Cdd:PLN02246 154 PEGCLHFSELTQAD----ENELPEVEISPDDVVA--LP-------YSSGTTGLPKGVMLTHKGLVTSvAQQVDGENPnly 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 187 FGAEDDWLLSLPLFHV-SGQGILWRWLFAGARMTVRDKQPLDQMLA-----GCTHASLVPTQLwrLLVNNTPVT------ 254
Cdd:PLN02246 221 FHSDDVILCVLPMFHIySLNSVLLCGLRVGAAILIMPKFEIGALLEliqrhKVTIAPFVPPIV--LAIAKSPVVekydls 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 255 -LKAVLLGGAAIPVELTE--QAREQGIRCWCGYGLTE----------FA-------STVC--------AKEADglADVGS 306
Cdd:PLN02246 299 sIRMVLSGAAPLGKELEDafRAKLPNAVLGQGYGMTEagpvlamclaFAkepfpvkSGSCgtvvrnaeLKIVD--PETGA 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 307 ALPgrevRIVNDEVWLRAASMAQGYWRNGQ-LMPLVNAEGWFATRDRG-VLKDGKLTIVGRMDNLFFSGGEGIQPEEVER 384
Cdd:PLN02246 377 SLP----RNQPGEICIRGPQIMKGYLNDPEaTANTIDKDGWLHTGDIGyIDDDDELFIVDRLKELIKYKGFQVAPAELEA 452
|
330 340
....*....|....*....|....*....
gi 489936067 385 VIAAHPHVLQAFIVPIEDKEFGHRPVAVV 413
Cdd:PLN02246 453 LLISHPSIADAAVVPMKDEVAGEVPVAFV 481
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
43-437 |
1.68e-12 |
|
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: 69.13 E-value: 1.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 43 LSWSELCARIDHLASGFAAQGVEEGDGVLLRAWNHPRALLAWLALLQCGARVLPVNPQL-PQSLLDALVPDLTLRFALDL 121
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLtPDDLRDRVDRGGAVYAAVDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 122 EAAIALPELsplqmkslpgdhaaawlperlstMTLTSGSTGLPKAAVHTcqaHLASAQGVLSLMPF----GAEDDWLLSL 197
Cdd:cd05974 81 NTHADDPML-----------------------LYFTSGTTSKPKLVEHT---HRSYPVGHLSTMYWiglkPGDVHWNISS 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 198 PLFHVSGQGILWRWLFAGARMTVRDKQPLD-----QMLAGCTHASL-VPTQLWRLLVN----NTPVTLKAVLLGGAAIPV 267
Cdd:cd05974 135 PGWAKHAWSCFFAPWNAGATVFLFNYARFDakrvlAALVRYGVTTLcAPPTVWRMLIQqdlaSFDVKLREVVGAGEPLNP 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 268 ELTEQAREQ-GIRCWCGYGLTEFASTVCAKEADGL--ADVGSALPGREVRIVN--------DEVWL-----RAASMAQGY 331
Cdd:cd05974 215 EVIEQVRRAwGLTIRDGYGQTETTALVGNSPGQPVkaGSMGRPLPGYRVALLDpdgapateGEVALdlgdtRPVGLMKGY 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 332 WRNGQLMPLVNAEGWFATRDRGVL-KDGKLTIVGRMDNLFFSGGEGIQPEEVERVIAAHPHVLQAFIVPIEDKEFGHRPV 410
Cdd:cd05974 295 AGDPDKTAHAMRGGYYRTGDIAMRdEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPK 374
|
410 420 430
....*....|....*....|....*....|..
gi 489936067 411 AVVEYDANAGET-----NLAEWVKDKLARFQQ 437
Cdd:cd05974 375 AFIVLRAGYEPSpetalEIFRFSRERLAPYKR 406
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
33-460 |
2.79e-12 |
|
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: 68.51 E-value: 2.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 33 APALRLNDEALSWSELCARIDHLASGFAAQGVEEGDGVLLRAWNHPRALLAWLALLQCGARVLPVNPQLPQSLLDALVPD 112
Cdd:cd17655 13 HTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEERIQYILED 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 113 LTLRFAL---DLEAAIALPELSPL----QMKSLPGDH-AAAWLPERLSTMTLTSGSTGLPKAAVHTCQA--HLASaqGVL 182
Cdd:cd17655 93 SGADILLtqsHLQPPIAFIGLIDLldedTIYHEESENlEPVSKSDDLAYVIYTSGSTGKPKGVMIEHRGvvNLVE--WAN 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 183 SLMPFGAEDDWLLSLPL-FHVSGQGILWRWLFAGARMTVRDKQPLDQML-------AGCTHASLVPTQLwRLLVNN---T 251
Cdd:cd17655 171 KVIYQGEHLRVALFASIsFDASVTEIFASLLSGNTLYIVRKETVLDGQAltqyirqNRITIIDLTPAHL-KLLDAAddsE 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 252 PVTLKAVLLGGAAIPVELTEQAREQ---GIRCWCGYGLTEfaSTVCA------KEADGLADV--GSALPGREVRIVND-- 318
Cdd:cd17655 250 GLSLKHLIVGGEALSTELAKKIIELfgtNPTITNAYGPTE--TTVDAsiyqyePETDQQVSVpiGKPLGNTRIYILDQyg 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 319 ---------EVWLRAASMAQGYWRNGQLM-------PLVNAEGWFATRDRG-VLKDGKLTIVGRMDNLFFSGGEGIQPEE 381
Cdd:cd17655 328 rpqpvgvagELYIGGEGVARGYLNRPELTaekfvddPFVPGERMYRTGDLArWLPDGNIEFLGRIDHQVKIRGYRIELGE 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 382 VERVIAAHPHVLQAFIVPIEDKEFGHRPVAVVEYDANAGETNLAEWVKDKLARFQQPVCWLTL---PpeLKAGGiKISRR 458
Cdd:cd17655 408 IEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEKELPVAQLREFLARELPDYMIPSYFIKLdeiP--LTPNG-KVDRK 484
|
..
gi 489936067 459 AL 460
Cdd:cd17655 485 AL 486
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
43-463 |
3.02e-12 |
|
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: 68.30 E-value: 3.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 43 LSWSELCARIDHLASGFAAQGVEEGDGVLLRAWNHPRALLAWLALLQCGARVLPvnpqlpqsLLDALVPDlTLRFALDLE 122
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICP--------LFSAFGPE-AIRDRLENS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 123 AA---IALPELsplqmkslpgdhAAAWLPERLSTMTLTSGSTGLPKAAVHTCQA---HLASAQGVLSLMPfgaeDD--WL 194
Cdd:cd05969 72 EAkvlITTEEL------------YERTDPEDPTLLHYTSGTTGTPKGVLHVHDAmifYYFTGKYVLDLHP----DDiyWC 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 195 LSLPLFhVSGQ--GILWRWLfAGARMTVRDKQ--------PLDQMlaGCTHASLVPTQLWRLLVNNTPV-------TLKA 257
Cdd:cd05969 136 TADPGW-VTGTvyGIWAPWL-NGVTNVVYEGRfdaeswygIIERV--KVTVWYTAPTAIRMLMKEGDELarkydlsSLRF 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 258 VLLGGAAIPVELTEQAREQ-GIRCWCGYGLTEFASTVCAKEADGLADVGS---ALPGREVRIVNDE-----------VWL 322
Cdd:cd05969 212 IHSVGEPLNPEAIRWGMEVfGVPIHDTWWQTETGSIMIANYPCMPIKPGSmgkPLPGVKAAVVDENgnelppgtkgiLAL 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 323 RAA--SMAQGYWRNGQLMPLVNAEGWFATRDRGVL-KDGKLTIVGRMDNLFFSGGEGIQPEEVERVIAAHPHVLQAFIVP 399
Cdd:cd05969 292 KPGwpSMFRGIWNDEERYKNSFIDGWYLTGDLAYRdEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIG 371
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489936067 400 IEDKEFGHRPVA--VVEYDANAGE---TNLAEWVKDKLARFQQP--VCWLTLPPELKAGgiKISRRALSDW 463
Cdd:cd05969 372 KPDPLRGEIIKAfiSLKEGFEPSDelkEEIINFVRQKLGAHVAPreIEFVDNLPKTRSG--KIMRRVLKAK 440
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
148-431 |
4.64e-12 |
|
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: 68.22 E-value: 4.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 148 PERLSTMTLTSGSTGLPKAAVHTCQAHLASAQGVLSLMPFGAEDDWLLSLPL------FHVSGQGI-------------- 207
Cdd:cd17641 157 GEDVAVLCTTSGTTGKPKLAMLSHGNFLGHCAAYLAADPLGPGDEYVSVLPLpwigeqMYSVGQALvcgfivnfpeepet 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 208 ------------------LWRWLFAGARMTVRDKQPLDQML----------AGCTHASLVPTQLW-------------RL 246
Cdd:cd17641 237 mmedlreigptfvllpprVWEGIAADVRARMMDATPFKRFMfelgmklglrALDRGKRGRPVSLWlrlaswladallfRP 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 247 LVNNTPVT-LKAVLLGGAAIPVELTEQAREQGIRCWCGYGLTEFASTVCAkEADGLAD---VGSALPGREVRIVND-EVW 321
Cdd:cd17641 317 LRDRLGFSrLRSAATGGAALGPDTFRFFHAIGVPLKQLYGQTELAGAYTV-HRDGDVDpdtVGVPFPGTEVRIDEVgEIL 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 322 LRAASMAQGYWRNGQLMPL-VNAEGWFATRDRGVLK-DGKLTIVGRMDNLF-FSGGEGIQPEEVERVIAAHPHVLQAFIv 398
Cdd:cd17641 396 VRSPGVFVGYYKNPEATAEdFDEDGWLHTGDAGYFKeNGHLVVIDRAKDVGtTSDGTRFSPQFIENKLKFSPYIAEAVV- 474
|
330 340 350
....*....|....*....|....*....|....*.
gi 489936067 399 piedkeFGH-RP--VAVVEYDAnageTNLAEWVKDK 431
Cdd:cd17641 475 ------LGAgRPylTAFICIDY----AIVGKWAEQR 500
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
33-435 |
5.19e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 67.78 E-value: 5.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 33 APALRLNDEALSWSELCARIDHLASGFAAQ---GVEEGDGVLLRawNHPRALLAWLALLQCGARVLPVNP---------- 99
Cdd:PRK07867 19 DRGLYFEDSFTSWREHIRGSAARAAALRARldpTRPPHVGVLLD--NTPEFSLLLGAAALSGIVPVGLNPtrrgaalard 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 100 ------QL------PQSLLDALVPDLTLrfaLDLEAAIALPELSPLQMKSLPgdhAAAWLPERLSTMTLTSGSTGLPKAA 167
Cdd:PRK07867 97 iahadcQLvltesaHAELLDGLDPGVRV---INVDSPAWADELAAHRDAEPP---FRVADPDDLFMLIFTSGTSGDPKAV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 168 VHTcQAHLASAQGVLSLMpFG--AEDDWLLSLPLFHvsGQGILWRW---LFAGARMTVRDKQPLDQMLA-----GCTHAS 237
Cdd:PRK07867 171 RCT-HRKVASAGVMLAQR-FGlgPDDVCYVSMPLFH--SNAVMAGWavaLAAGASIALRRKFSASGFLPdvrryGATYAN 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 238 LVPTQLWRLLVnnTPV-------TLKAVLlGGAAIPVELTEQAREQGIRCWCGYGLTE----FAST-------------- 292
Cdd:PRK07867 247 YVGKPLSYVLA--TPErpddadnPLRIVY-GNEGAPGDIARFARRFGCVVVDGFGSTEggvaITRTpdtppgalgplppg 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 293 VCAKEADGLADVGSALPGREVRIVNDE-----VWLRAASMAQGYWRNgqlmPLVNAE----GWF-----ATRDrgvlKDG 358
Cdd:PRK07867 324 VAIVDPDTGTECPPAEDADGRLLNADEaigelVNTAGPGGFEGYYND----PEADAErmrgGVYwsgdlAYRD----ADG 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489936067 359 KLTIVGRMDNLFFSGGEGIQPEEVERVIAAHPHVLQAFIVPIEDKEFGHRPVAVVEYDANagetnlAEWVKDKLARF 435
Cdd:PRK07867 396 YAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVMAALVLAPG------AKFDPDAFAEF 466
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
44-387 |
8.62e-12 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 67.33 E-value: 8.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 44 SWSELCARIDHLASGFAAQGVEEGDGVLLRAWNHPRALLAWLALLQCGARVLPVNPQLPQSLLDALVPDLTLRFA-LDLE 122
Cdd:PRK07768 31 TWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASLTMLHQPTPRTDLAVWAEDTLRVIGmIGAK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 123 AAI-------ALPELSPLQMKSLPGDHAAAWLPER--------LSTMTLTSGSTGLPKAAVHTCQAHLASAQGVLSLMPF 187
Cdd:PRK07768 111 AVVvgepflaAAPVLEEKGIRVLTVADLLAADPIDpvetgeddLALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEF 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 188 GAEDDWLLS-LPLFHVSGQ-GILwrwlfagarmTVrdkqpldQMLAGCTHASLVPTQ------LW--------------- 244
Cdd:PRK07768 191 DVETDVMVSwLPLFHDMGMvGFL----------TV-------PMYFGAELVKVTPMDflrdplLWaeliskyrgtmtaap 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 245 --------RLLVNNTPV------TLKAVLLGGAAIPV----ELTEQAREQGIR---CWCGYGLTE--------------- 288
Cdd:PRK07768 254 nfayallaRRLRRQAKPgafdlsSLRFALNGAEPIDPadveDLLDAGARFGLRpeaILPAYGMAEatlavsfspcgaglv 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 289 -------------FASTVCAKEADGLADVGSALPGREVRIVND-----------EVWLRAASMAQGYWRNGQLMPLVNAE 344
Cdd:PRK07768 334 vdevdadllaalrRAVPATKGNTRRLATLGPPLPGLEVRVVDEdgqvlpprgvgVIELRGESVTPGYLTMDGFIPAQDAD 413
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 489936067 345 GWFATRDRGVLKD-GKLTIVGRMDNLFFSGGEGIQPEEVERVIA 387
Cdd:PRK07768 414 GWLDTGDLGYLTEeGEVVVCGRVKDVIIMAGRNIYPTDIERAAA 457
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
157-413 |
1.39e-11 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 66.33 E-value: 1.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 157 TSGSTGLPKAAVHTCQAHLASAQGVLSLMPFGAEDDWLLS-LPLFHVSGQGILWRWLFAGARM-----------TVRDKQ 224
Cdd:PRK05851 160 TAGSTGTPRTAILSPGAVLSNLRGLNARVGLDAATDVGCSwLPLYHDMGLAFLLTAALAGAPLwlapttafsasPFRWLS 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 225 PLDQMLAGCTHA-----SLVPTQLWRLlvnnTPVTLKAV---LLGGAAIPVE-----LTEQAReQGIRCWC---GYGLTE 288
Cdd:PRK05851 240 WLSDSRATLTAApnfayNLIGKYARRV----SDVDLGALrvaLNGGEPVDCDgferfATAMAP-FGFDAGAaapSYGLAE 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 289 FASTVCAKE-ADGL----------------ADVGSALPGREVRI--------VND----EVWLRAASMAQGYWrnGQlmP 339
Cdd:PRK05851 315 STCAVTVPVpGIGLrvdevttddgsgarrhAVLGNPIPGMEVRIspgdgaagVAGreigEIEIRGASMMSGYL--GQ--A 390
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489936067 340 LVNAEGWFATRDRGVLKDGKLTIVGRMDNLFFSGGEGIQPEEVERVIAAHPHVLQAFIVPIEDKEFGHRPVAVV 413
Cdd:PRK05851 391 PIDPDDWFPTGDLGYLVDGGLVVCGRAKELITVAGRNIFPTEIERVAAQVRGVREGAVVAVGTGEGSARPGLVI 464
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
33-460 |
2.13e-11 |
|
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: 65.96 E-value: 2.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 33 APALRLNDEALSWSELCARIDHLASGFAAQGVEEGDGVLLRAWNHPRALLAWLALLQCGARVLPVNPQLPQ--------- 103
Cdd:cd17656 4 AVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEerriyimld 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 104 SLLDALVPDLTLRFALDLEAAIALPElSPLQMKSLPGDHAAAWLPERLSTMTLTSGSTGLPKAAV--HTCQAHLASAQGV 181
Cdd:cd17656 84 SGVRVVLTQRHLKSKLSFNKSTILLE-DPSISQEDTSNIDYINNSDDLLYIIYTSGTTGKPKGVQleHKNMVNLLHFERE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 182 LSLMPFGaeDDWL-LSLPLFHVSGQGILWRWLFAGARMTVRD--KQPLDQMLAGC----THASLVPTQLWRLL------V 248
Cdd:cd17656 163 KTNINFS--DKVLqFATCSFDVCYQEIFSTLLSGGTLYIIREetKRDVEQLFDLVkrhnIEVVFLPVAFLKFIfserefI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 249 NNTPVTLKAVLLGGAAIPV--ELTEQAREQGIRCWCGYGLTEfASTVCA------KEADGLADVGSALPGREVRIVND-- 318
Cdd:cd17656 241 NRFPTCVKHIITAGEQLVItnEFKEMLHEHNVHLHNHYGPSE-THVVTTytinpeAEIPELPPIGKPISNTWIYILDQeq 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 319 ---------EVWLRAASMAQGYWRNGQLM-------PLVNAEGWFATRDRG-VLKDGKLTIVGRMDNLFFSGGEGIQPEE 381
Cdd:cd17656 320 qlqpqgivgELYISGASVARGYLNRQELTaekffpdPFDPNERMYRTGDLArYLPDGNIEFLGRADHQVKIRGYRIELGE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 382 VERVIAAHPHVLQAFIVPIEDKEFGHRPVAVVEYDANAGETNLAEWVKDKLARFQQPVCWLTLPP-ELKAGGiKISRRAL 460
Cdd:cd17656 400 IEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFVMEQELNISQLREYLAKQLPEYMIPSFFVPLDQlPLTPNG-KVDRKAL 478
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
24-460 |
2.25e-11 |
|
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: 65.97 E-value: 2.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 24 RHWRQVRAKAPALRLNDE-----ALSWSELCARIDHLASGFAAQGVEEGDGVLLRAWNHPRALLAWLALLQCGARVLP-- 96
Cdd:cd05968 68 DKWLADTRTRPALRWEGEdgtsrTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPif 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 97 -------VNPQLPQSLLDAL-VPDLTLR-----------------------------FALDLEAAIALPELSPLQMKSlP 139
Cdd:cd05968 148 sgfgkeaAATRLQDAEAKALiTADGFTRrgrevnlkeeadkacaqcptvekvvvvrhLGNDFTPAKGRDLSYDEEKET-A 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 140 GDHAAAWLPERLSTMTLTSGSTGLPKAAVHT-CQAHLASAQGVLSLMPFGAEDDWLLSLPLFHVSGQGILWRWLFAGARM 218
Cdd:cd05968 227 GDGAERTESEDPLMIIYTSGTTGKPKGTVHVhAGFPLKAAQDMYFQFDLKPGDLLTWFTDLGWMMGPWLIFGGLILGATM 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 219 TVRDKQP-------LDQMLA--GCTHASLVPTqLWRLLV--NNTPVT---LKAV-LLGGAAIPVELTE-----QAREQGI 278
Cdd:cd05968 307 VLYDGAPdhpkadrLWRMVEdhEITHLGLSPT-LIRALKprGDAPVNahdLSSLrVLGSTGEPWNPEPwnwlfETVGKGR 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 279 RCWCGY-GLTE------------------FASTVCAKEADGLADVGSALPGREVRIVNDEVWLraaSMAQGYWRNG---- 335
Cdd:cd05968 386 NPIINYsGGTEisggilgnvlikpikpssFNGPVPGMKADVLDESGKPARPEVGELVLLAPWP---GMTRGFWRDEdryl 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 336 ----QLMPLVNAEGWFATRDrgvlKDGKLTIVGRMDNLFFSGGEGIQPEEVERVIAAHPHVLQAFIVPIEDKEFGHRPV- 410
Cdd:cd05968 463 etywSRFDNVWVHGDFAYYD----EEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVc 538
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 489936067 411 -AVVEYDANAGETN---LAEWVKDKLARFQQPVCWLTLPPELKAGGIKISRRAL 460
Cdd:cd05968 539 fVVLKPGVTPTEALaeeLMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVI 592
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
35-402 |
2.29e-11 |
|
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: 65.41 E-value: 2.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 35 ALRLNDEALSWSELCARIDHLASGFAAQGVEEGDGVLLRAWNHPRALLAWLALLQCGARVLPVNPQLPQSLLDAlvpdlT 114
Cdd:cd17653 15 AVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSARIQA-----I 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 115 LRfalDLEAAIALpelsplqmkSLPGDHAAAWLperlstmTLTSGSTGLPKAAVHTCQAHLASAQGVLSLMPFGAEDDWL 194
Cdd:cd17653 90 LR---TSGATLLL---------TTDSPDDLAYI-------IFTSGSTGIPKGVMVPHRGVLNYVSQPPARLDVGPGSRVA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 195 LSL-PLFHVSgQGILWRWLFAGARMTVRD-KQPLDQMLAGCTHASLVPTQLWRLLVNNTPvTLKAVLLGGAAIPVELTEQ 272
Cdd:cd17653 151 QVLsIAFDAC-IGEIFSTLCNGGTLVLADpSDPFAHVARTVDALMSTPSILSTLSPQDFP-NLKTIFLGGEAVPPSLLDR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 273 AREqGIRCWCGYGLTEfaSTVCAKEADGLADV----GSALPGREVRIVND-----------EVWLRAASMAQGYWRNGQL 337
Cdd:cd17653 229 WSP-GRRLYNAYGPTE--CTISSTMTELLPGQpvtiGKPIPNSTCYILDAdlqpvpegvvgEICISGVQVARGYLGNPAL 305
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489936067 338 -------MPLVNAEGWFATRDRGVL-KDGKLTIVGRMDNLFFSGGEGIQPEEVERVI-AAHPHVLQAFIVPIED 402
Cdd:cd17653 306 taskfvpDPFWPGSRMYRTGDYGRWtEDGGLEFLGREDNQVKVRGFRINLEEIEEVVlQSQPEVTQAAAIVVNG 379
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
41-438 |
2.71e-11 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 65.42 E-value: 2.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 41 EALSWSELCARIDHLASGFAAQGVEEGDGVLLRAWNHPRALLAWLALLQCGARVLPVNPQLPQSLLDALVPDLTLRFald 120
Cdd:PRK13390 23 EQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYIVGDSGARV--- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 121 LEAAIALPELSPLQMKSLP------------GDHAAAW------LPERL--STMTLTSGSTGLPKAAVHTCQAHLASAQG 180
Cdd:PRK13390 100 LVASAALDGLAAKVGADLPlrlsfggeidgfGSFEAALagagprLTEQPcgAVMLYSSGTTGFPKGIQPDLPGRDVDAPG 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 181 ------VLSLMPFGAEDDWLLSLPLFHVS------------GQGILWRWLFAGARMTVRDKQPLdqmlagcTHASLVPTQ 242
Cdd:PRK13390 180 dpivaiARAFYDISESDIYYSSAPIYHAAplrwcsmvhalgGTVVLAKRFDAQATLGHVERYRI-------TVTQMVPTM 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 243 LWRLLVNNTPV-------TLKAVLLGGAAIPVELteqarEQGIRCWCG------YGLTEFASTVCAKEADGLADVGSAlp 309
Cdd:PRK13390 253 FVRLLKLDADVrtrydvsSLRAVIHAAAPCPVDV-----KHAMIDWLGpivyeyYSSTEAHGMTFIDSPDWLAHPGSV-- 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 310 GREV----RIVNDEVW-LRAASMAQGYWRNGQL------MPLVNAEG-------WFATRDRG-VLKDGKLTIVGRMDNLF 370
Cdd:PRK13390 326 GRSVlgdlHICDDDGNeLPAGRIGTVYFERDRLpfrylnDPEKTAAAqhpahpfWTTVGDLGsVDEDGYLYLADRKSFMI 405
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489936067 371 FSGGEGIQPEEVERVIAAHPHVLQAFIVPIEDKEFGHRPVAVVEYDANA-GETNLA----EWVKDKLARFQQP 438
Cdd:PRK13390 406 ISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLVEGIrGSDELAreliDYTRSRIAHYKAP 478
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
25-466 |
5.11e-11 |
|
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: 64.76 E-value: 5.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 25 HWRQVRAKAP--ALRLNDEA---LSWSELCARIDHLASGFAAQGVEEGDGVLLRAWNHPRALLAWLALLQCGARVLPVNP 99
Cdd:cd05921 3 HWARQAPDRTwlAEREGNGGwrrVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 100 QLP---------QSLLDALVPDLTlrFALDLE------AAIALPELSPLQMKSLPGDHAAAWLPERLST----------- 153
Cdd:cd05921 83 AYSlmsqdlaklKHLFELLKPGLV--FAQDAApfaralAAIFPLGTPLVVSRNAVAGRGAISFAELAATpptaavdaafa 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 154 ---------MTLTSGSTGLPKAAVHTCQAHLASAQGVLSLMPFGAED-----DWllsLPLFHVSGQG-----ILWRwlfa 214
Cdd:cd05921 161 avgpdtvakFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFFGEEppvlvDW---LPWNHTFGGNhnfnlVLYN---- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 215 GARMTVRDKQPLDQMLAGC---------THASLVPTQlWRLLVN---NTPV-------TLKAVLLGGAAIP-------VE 268
Cdd:cd05921 234 GGTLYIDDGKPMPGGFEETlrnlreispTVYFNVPAG-WEMLVAaleKDEAlrrrffkRLKLMFYAGAGLSqdvwdrlQA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 269 LTEQAREQGIRCWCGYGLTEFA--STVCAKEADGLADVGSALPGREVRIV-ND---EVWLRAASMAQGYWRNGQLMPLV- 341
Cdd:cd05921 313 LAVATVGERIPMMAGLGATETAptATFTHWPTERSGLIGLPAPGTELKLVpSGgkyEVRVKGPNVTPGYWRQPELTAQAf 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 342 NAEGWFATRDRGVLKDGK-----LTIVGRM-DNLFFSGGE--GIQPEEVERVIAAHPHVLQAfIVPIEDKEF-------- 405
Cdd:cd05921 393 DEEGFYCLGDAAKLADPDdpakgLVFDGRVaEDFKLASGTwvSVGPLRARAVAACAPLVHDA-VVAGEDRAEvgalvfpd 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 406 --GHRPVAVVEYDANAGETNLA---EWVKDKLARFQQP-------VCWLTL---PPELKAGGIK----ISRRALSDWVSA 466
Cdd:cd05921 472 llACRRLVGLQEASDAEVLRHAkvrAAFRDRLAALNGEatgsssrIARALLldePPSIDKGEITdkgyINQRAVLERRAA 551
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
148-430 |
7.54e-11 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 64.45 E-value: 7.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 148 PERLSTMTLTSGSTGLPKAAVHTCQAHLASAQGVLSLM-----PFGAEDDWLLSLPLFHVSGQGILWRWLFAGARM---- 218
Cdd:PLN02430 219 PLDICTIMYTSGTSGDPKGVVLTHEAVATFVRGVDLFMeqfedKMTHDDVYLSFLPLAHILDRMIEEYFFRKGASVgyyh 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 219 ----TVRD-------------------------------------------KQPLDQMLAGCTHASLVPTQ---LWRLLV 248
Cdd:PLN02430 299 gdlnALRDdlmelkptllagvprvferihegiqkalqelnprrrlifnalyKYKLAWMNRGYSHKKASPMAdflAFRKVK 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 249 NNTPVTLKAVLLGGAAIPVELTEQAReqgIRCWC----GYGLTEF--ASTVC-AKEADGLADVGSALPGREVRIVN---- 317
Cdd:PLN02430 379 AKLGGRLRLLISGGAPLSTEIEEFLR---VTSCAfvvqGYGLTETlgPTTLGfPDEMCMLGTVGAPAVYNELRLEEvpem 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 318 ----------DEVWLRAASMAQGYWRNGQLMPLVNAEGWFATRDRG-VLKDGKLTIVGRMDNLF-FSGGEGIQPEEVERV 385
Cdd:PLN02430 456 gydplgepprGEICVRGKCLFSGYYKNPELTEEVMKDGWFHTGDIGeILPNGVLKIIDRKKNLIkLSQGEYVALEYLENV 535
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 489936067 386 IAAHPHVLQAFIVpieDKEFGHRPVAVVeydaNAGETNLAEWVKD 430
Cdd:PLN02430 536 YGQNPIVEDIWVY---GDSFKSMLVAVV----VPNEENTNKWAKD 573
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
148-434 |
1.50e-10 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 63.58 E-value: 1.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 148 PERLSTMTLTSGSTGLPKAAVHTCQAHLASAQGVLSLMPFGAEDDWLLSLPLFHVSGQGI-LWRWLFAGARMTVRdKQPL 226
Cdd:PRK08043 364 PEDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPNDRFMSALPLFHSFGLTVgLFTPLLTGAEVFLY-PSPL 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 227 dqmlagctHASLVPTqlwrlLVNNTPVTlkaVLLGGA---------AIPVE-------------LTEQAREQ-----GIR 279
Cdd:PRK08043 443 --------HYRIVPE-----LVYDRNCT---VLFGTStflgnyarfANPYDfarlryvvagaekLQESTKQLwqdkfGLR 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 280 CWCGYGLTEFASTVC--AKEADGLADVGSALPGREVRIVN-------DEVWLRAASMAQGYWR---NGQLMP--LVNAEG 345
Cdd:PRK08043 507 ILEGYGVTECAPVVSinVPMAAKPGTVGRILPGMDARLLSvpgieqgGRLQLKGPNIMNGYLRvekPGVLEVptAENARG 586
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 346 -----WFATRDRGVLKD-GKLTIVGRMDNLFFSGGEGIQPEEVERV-IAAHPHVLQAfivpiedkefghrpvAVVEYDAN 418
Cdd:PRK08043 587 emergWYDTGDIVRFDEqGFVQIQGRAKRFAKIAGEMVSLEMVEQLaLGVSPDKQHA---------------TAIKSDAS 651
|
330 340
....*....|....*....|.
gi 489936067 419 AGE-----TNLAEWVKDKLAR 434
Cdd:PRK08043 652 KGEalvlfTTDSELTREKLQQ 672
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
154-414 |
8.28e-10 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 60.81 E-value: 8.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 154 MTLTSGSTGLPKAaVHTCQAHLASAqGVLSLMPFG--AEDDWLLSLPLFHvsGQGILWRW---LFAGARMTVRDKQPLDQ 228
Cdd:PRK13388 155 LIFTSGTTGAPKA-VRCSHGRLAFA-GRALTERFGltRDDVCYVSMPLFH--SNAVMAGWapaVASGAAVALPAKFSASG 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 229 MLA-----GCTHASLVPTQLWRLLVnnTPV-------TLKaVLLGGAAIPVELTEQAREQGIRCWCGYGLTEFASTVCAK 296
Cdd:PRK13388 231 FLDdvrryGATYFNYVGKPLAYILA--TPErpddadnPLR-VAFGNEASPRDIAEFSRRFGCQVEDGYGSSEGAVIVVRE 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 297 EADGLADVGSALPGreVRIVNDE--------------------------VWLRAASMAQGYWRNgqlmPLVNAE----GW 346
Cdd:PRK13388 308 PGTPPGSIGRGAPG--VAIYNPEtltecavarfdahgallnadeaigelVNTAGAGFFEGYYNN----PEATAErmrhGM 381
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489936067 347 FATRDRGVL-KDGKLTIVGRMDNLFFSGGEGIQPEEVERVIAAHPHVLQAFIVPIEDKEFGHRPVAVVE 414
Cdd:PRK13388 382 YWSGDLAYRdADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVGDQVMAALV 450
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
99-462 |
1.07e-09 |
|
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: 60.59 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 99 PQLPQSLLDALVPDLTLRFALDLEAAI--ALPELSPLQMKSLPGDhaaawlpERLSTMTLTSGSTGLPKAAVHTCQ---A 173
Cdd:cd05970 140 PECPSKPKLVWVGDPVPEGWIDFRKLIknASPDFERPTANSYPCG-------EDILLVYFSSGTTGMPKMVEHDFTyplG 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 174 HLASAQGVLSLMPFG-----AEDDWLLSlplfhVSGQgILWRWLfAGARMTVRDKQPLD--QMLA-----GCTHASLVPT 241
Cdd:cd05970 213 HIVTAKYWQNVREGGlhltvADTGWGKA-----VWGK-IYGQWI-AGAAVFVYDYDKFDpkALLEklskyGVTTFCAPPT 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 242 qLWRLLVNNTPV-----TLKAVLLGGAAIPVELTEQAREQ-GIRCWCGYGLTEFASTV----CAKEADGlaDVGSALPGR 311
Cdd:cd05970 286 -IYRFLIREDLSrydlsSLRYCTTAGEALNPEVFNTFKEKtGIKLMEGFGQTETTLTIatfpWMEPKPG--SMGKPAPGY 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 312 EVRIVND-----------EVWLRAAS-----MAQGYWRNGQLMPLVNAEGWFATRDRGVL-KDGKLTIVGRMDNLFFSGG 374
Cdd:cd05970 363 EIDLIDRegrsceageegEIVIRTSKgkpvgLFGGYYKDAEKTAEVWHDGYYHTGDAAWMdEDGYLWFVGRTDDLIKSSG 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 375 EGIQPEEVERVIAAHPHVLQAFIVPIEDKEFGH--RPVAVVEYDANAGET---NLAEWVKDKLARFQQPVCwLTLPPEL- 448
Cdd:cd05970 443 YRIGPFEVESALIQHPAVLECAVTGVPDPIRGQvvKATIVLAKGYEPSEElkkELQDHVKKVTAPYKYPRI-VEFVDELp 521
|
410
....*....|....
gi 489936067 449 KAGGIKISRRALSD 462
Cdd:cd05970 522 KTISGKIRRVEIRE 535
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
305-414 |
1.57e-09 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 60.02 E-value: 1.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 305 GSALPGREVRIVNDE-----------VWLRAASMAQGYWRNGQLMPLVNAEGWFATRDRGVLKDGKLTIVGRMDNLFFSG 373
Cdd:PRK09192 388 GKALPGHEIEIRNEAgmplpervvghICVRGPSLMSGYFRDEESQDVLAADGWLDTGDLGYLLDGYLYITGRAKDLIIIN 467
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 489936067 374 GEGIQPEEVERVIAAHPHVLQ----AFIVPIEDKEfghRPVAVVE 414
Cdd:PRK09192 468 GRNIWPQDIEWIAEQEPELRSgdaaAFSIAQENGE---KIVLLVQ 509
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
147-386 |
2.61e-09 |
|
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: 59.42 E-value: 2.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 147 LPERLSTMTLTSGSTGLPKAAVHTCQAHLASAQGVLSLMPFGAEDDWLLSLPLFHVSGqgilwrwLFAGArmtvrdkqpL 226
Cdd:cd05908 104 LADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMG-------LIAFH---------L 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 227 DQMLAGCTHaSLVPTQL-------WRLLVNNTPVT----------------------------LKAVLLGGAAIPVELTE 271
Cdd:cd05908 168 APLIAGMNQ-YLMPTRLfirrpilWLKKASEHKATivsspnfgykyflktlkpekandwdlssIRMILNGAEPIDYELCH 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 272 QAREQ----GIRCWC---GYGLTEFASTVCA------------------------------KEADGLADVGSALPGREVR 314
Cdd:cd05908 247 EFLDHmskyGLKRNAilpVYGLAEASVGASLpkaqspfktitlgrrhvthgepepevdkkdSECLTFVEVGKPIDETDIR 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 315 IVNDE-----------VWLRAASMAQGYWRNGQLMPLV-NAEGWFATRDRGVLKDGKLTIVGRMDNLFFSGGEGIQPEEV 382
Cdd:cd05908 327 ICDEDnkilpdgyighIQIRGKNVTPGYYNNPEATAKVfTDDGWLKTGDLGFIRNGRLVITGREKDIIFVNGQNVYPHDI 406
|
....
gi 489936067 383 ERVI 386
Cdd:cd05908 407 ERIA 410
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
33-223 |
3.76e-09 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 58.73 E-value: 3.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 33 APALRLNDEALSWSELCARIDHLASGFAAQGVEEGD--GVLLRawNHPRALLAWLALLQCGARVLPVNPQLPQsllDALV 110
Cdd:PRK08279 53 RPALLFEDQSISYAELNARANRYAHWAAARGVGKGDvvALLME--NRPEYLAAWLGLAKLGAVVALLNTQQRG---AVLA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 111 PDLTLrfaLDLEAAIALPELSPL--QMKSLPGDHAAAWL--------------------------PERLSTMTL------ 156
Cdd:PRK08279 128 HSLNL---VDAKHLIVGEELVEAfeEARADLARPPRLWVaggdtlddpegyedlaaaaagapttnPASRSGVTAkdtafy 204
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489936067 157 --TSGSTGLPKAAVHTcqaH---LASAQGVLSLMPFGAEDDWLLSLPLFHvsGQGILWRW---LFAGARMTVRDK 223
Cdd:PRK08279 205 iyTSGTTGLPKAAVMS---HmrwLKAMGGFGGLLRLTPDDVLYCCLPLYH--NTGGTVAWssvLAAGATLALRRK 274
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
90-207 |
4.04e-09 |
|
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: 58.84 E-value: 4.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 90 CGARVLPVNPQLpqslLDALVPDL-TLRfALDLEAAIALPELSPLQMKSL-------PGDHAAAWLPERLSTMTL----- 156
Cdd:cd05938 77 CGAKVLVVAPEL----QEAVEEVLpALR-ADGVSVWYLSHTSNTEGVISLldkvdaaSDEPVPASLRAHVTIKSPalyiy 151
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 489936067 157 TSGSTGLPKAAVHTcQAHLASAQGVLSLMPFGAEDDWLLSLPLFHVSGQGI 207
Cdd:cd05938 152 TSGTTGLPKAARIS-HLRVLQCSGFLSLCGVTADDVIYITLPLYHSSGFLL 201
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
157-429 |
4.29e-09 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 59.21 E-value: 4.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 157 TSGSTGLPKAAVHTCQAHLASAQGVLSLMPFGAEDDWLLSLPLFHVSGqgilwrwLFAGARMTvrdkqpldqMLAGCT-- 234
Cdd:PRK06814 801 TSGSEGTPKGVVLSHRNLLANRAQVAARIDFSPEDKVFNALPVFHSFG-------LTGGLVLP---------LLSGVKvf 864
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 235 ------HASLVPTQLWRllVNNTPV--------------------TLKAVLLGgaAIPV-ELTEQ--AREQGIRCWCGYG 285
Cdd:PRK06814 865 lypsplHYRIIPELIYD--TNATILfgtdtflngyaryahpydfrSLRYVFAG--AEKVkEETRQtwMEKFGIRILEGYG 940
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 286 LTEfASTVCAKE---ADGLADVGSALPGREVRIvnDEV---------WLRAASMAQGYWR---NGQLMPLvnAEGWFATR 350
Cdd:PRK06814 941 VTE-TAPVIALNtpmHNKAGTVGRLLPGIEYRL--EPVpgideggrlFVRGPNVMLGYLRaenPGVLEPP--ADGWYDTG 1015
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 351 D-RGVLKDGKLTIVGRMDNLFFSGGEGIQPEEVERVIAA-HPHVLQAfIVPIEDKEFGHRPVAVVEyDANAGETNLAEWV 428
Cdd:PRK06814 1016 DiVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAElWPDALHA-AVSIPDARKGERIILLTT-ASDATRAAFLAHA 1093
|
.
gi 489936067 429 K 429
Cdd:PRK06814 1094 K 1094
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
152-398 |
5.25e-09 |
|
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: 58.25 E-value: 5.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 152 STMTLTSGSTGLPKAAVHT-CQAHLASAQGVLSLMPFGAED-DWLLSLPLFHVSGQGILWRWLFAGA-----RMTVRDKQ 224
Cdd:cd05928 177 MAIYFTSGTTGSPKMAEHShSSLGLGLKVNGRYWLDLTASDiMWNTSDTGWIKSAWSSLFEPWIQGAcvfvhHLPRFDPL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 225 PLDQMLAG--CTHASLVPTqLWRLLVNNTPV-----TLKAVLLGGAAIPVELTEQAREQ-GIRCWCGYGLTEfASTVCA- 295
Cdd:cd05928 257 VILKTLSSypITTFCGAPT-VYRMLVQQDLSsykfpSLQHCVTGGEPLNPEVLEKWKAQtGLDIYEGYGQTE-TGLICAn 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 296 ----KEADGlaDVGSALPGREVRIVND-----------EVWLRAA-----SMAQGYWRNGQLMPLVNAEGWFATRDRGVL 355
Cdd:cd05928 335 fkgmKIKPG--SMGKASPPYDVQIIDDngnvlppgtegDIGIRVKpirpfGLFSGYVDNPEKTAATIRGDFYLTGDRGIM 412
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 489936067 356 -KDGKLTIVGRMDNLFFSGGEGIQPEEVERVIAAHPHVLQAFIV 398
Cdd:cd05928 413 dEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVV 456
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
44-402 |
5.69e-09 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 58.16 E-value: 5.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 44 SWSELCARIDHLASGFAAQGVEEGDGVLLRAWNHPRALLAWLALLQCGARVLPVNPQ---------LPQSLLDALVPD-- 112
Cdd:PRK08008 39 SYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARllreesawiLQNSQASLLVTSaq 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 113 -LTLRFALDLEAAIAL----------PELSPLQMKSLPGDHAAAWLPER--LST-----MTLTSGSTGLPKAAVHT-CQ- 172
Cdd:PRK08008 119 fYPMYRQIQQEDATPLrhicltrvalPADDGVSSFTQLKAQQPATLCYAppLSTddtaeILFTSGTTSRPKGVVIThYNl 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 173 ---AHLASAQGVLSlmpfgaEDDWLLS-LPLFHVSGQ-GILWRWLFAGARMTVRDK--------QPLDQMlAGCTHAslV 239
Cdd:PRK08008 199 rfaGYYSAWQCALR------DDDVYLTvMPAFHIDCQcTAAMAAFSAGATFVLLEKysarafwgQVCKYR-ATITEC--I 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 240 PTQLWRLLVNntPVT-------LKAVLLGgaaipVELTEQAREQ-----GIRCWCGYGLTEfasTVCAKEADGLAD---- 303
Cdd:PRK08008 270 PMMIRTLMVQ--PPSandrqhcLREVMFY-----LNLSDQEKDAfeerfGVRLLTSYGMTE---TIVGIIGDRPGDkrrw 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 304 --VGSALPGREVRIVND-----------EVWLRAA---SMAQGYWRNGQLMPLV-NAEGWFATRDRG-VLKDGKLTIVGR 365
Cdd:PRK08008 340 psIGRPGFCYEAEIRDDhnrplpageigEICIKGVpgkTIFKEYYLDPKATAKVlEADGWLHTGDTGyVDEEGFFYFVDR 419
|
410 420 430
....*....|....*....|....*....|....*..
gi 489936067 366 MDNLFFSGGEGIQPEEVERVIAAHPHVLQAFIVPIED 402
Cdd:PRK08008 420 RCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKD 456
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
33-394 |
7.41e-09 |
|
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: 57.87 E-value: 7.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 33 APALRLN--DEALSWSELCARIDHLASGFAAQGVEEGDGVLLRAWNHPRALLAWLALLQCGARVLPVNPQLPQSLLDALV 110
Cdd:cd17654 5 ALIIDQTtsDTTVSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 111 PDLTLRFALDLEAAIALPELSPLQMKslpgdHAAAWLPERLSTMTLTSGSTGLPK--AAVHTCQAHLAsaQGVLSLMPFG 188
Cdd:cd17654 85 KKCHVSYLLQNKELDNAPLSFTPEHR-----HFNIRTDECLAYVIHTSGTTGTPKivAVPHKCILPNI--QHFRSLFNIT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 189 AEDDWLLSLPL-FHVSGQGILWRWLFAGARMTVRDK--------QPLDQMLAGCTHASLVPTQLWRLLVNNTPVT----- 254
Cdd:cd17654 158 SEDILFLTSPLtFDPSVVEIFLSLSSGATLLIVPTSvkvlpsklADILFKRHRITVLQATPTLFRRFGSQSIKSTvlsat 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 255 --LKAVLLGGAAIPVELTEQAREQ---GIRCWCGYGLTE---FASTVCAKEADGLADVGSALPGREVRIVNDEVW----- 321
Cdd:cd17654 238 ssLRVLALGGEPFPSLVILSSWRGkgnRTRIFNIYGITEvscWALAYKVPEEDSPVQLGSPLLGTVIEVRDQNGSegtgq 317
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489936067 322 LRAASMAQGYWRNGQlMPLVNAEgWFATRDRGVLKDGKLTIVGRMDNLFFSGGEGIQPEEVERVIAAHPHVLQ 394
Cdd:cd17654 318 VFLGGLNRVCILDDE-VTVPKGT-MRATGDFVTVKDGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGVES 388
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
25-361 |
1.00e-08 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 57.58 E-value: 1.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 25 HWRQVRAKAPAL--RLNDEA---LSWSELCARIDHLASGFAAQGVEEGDGVLLRAWNHPRALLAWLALLQCGARVLPVNP 99
Cdd:PRK08180 47 HWAQEAPDRVFLaeRGADGGwrrLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALAAMYAGVPYAPVSP 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 100 QLpqSLLDAlvpDLT-LRFALDL--------------EAAIALPELSPLQM---KSLPGDHAAAWLPERLSTMT------ 155
Cdd:PRK08180 127 AY--SLVSQ---DFGkLRHVLELltpglvfaddgaafARALAAVVPADVEVvavRGAVPGRAATPFAALLATPPtaavda 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 156 --------------LTSGSTGLPKAAVHTcQAHL-ASAQGVLSLMPFGAED-----DWllsLPLFHV-SGQGILWRWLFA 214
Cdd:PRK08180 202 ahaavgpdtiakflFTSGSTGLPKAVINT-HRMLcANQQMLAQTFPFLAEEppvlvDW---LPWNHTfGGNHNLGIVLYN 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 215 GARMTVRDKQPLDQMLAGcTHASL---VPTqlwrlLVNNTPV---------------------TLKAVLLGGAAIPV--- 267
Cdd:PRK08180 278 GGTLYIDDGKPTPGGFDE-TLRNLreiSPT-----VYFNVPKgwemlvpalerdaalrrrffsRLKLLFYAGAALSQdvw 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 268 ----ELTEQAREQGIRCWCGYGLTEFA--STVCAKEADGLADVGSALPGREVRIV-ND---EVWLRAASMAQGYWRNGQL 337
Cdd:PRK08180 352 drldRVAEATCGERIRMMTGLGMTETApsATFTTGPLSRAGNIGLPAPGCEVKLVpVGgklEVRVKGPNVTPGYWRAPEL 431
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 489936067 338 mplvNA-----EGWFATRD-----------RGVLKDGKLT 361
Cdd:PRK08180 432 ----TAeafdeEGYYRSGDavrfvdpadpeRGLMFDGRIA 467
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
6-357 |
2.49e-08 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 56.21 E-value: 2.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 6 RPD-SVSLSGLIQPSDWPWR------HWRQVRAKAPAL-RLNDEALSWSELC-----ARIDHLASGFAAQGVEEGDGVLL 72
Cdd:PRK12582 31 RADgSIVIKSRHPLGPYPRSiphllaKWAAEAPDRPWLaQREPGHGQWRKVTygeakRAVDALAQALLDLGLDPGRPVMI 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 73 RAWNHPRALLAWLALLQCGARVLPVNPqlPQSLL-----------DALVPDLTlrFALD---LEAAIALPELSPLQMKSL 138
Cdd:PRK12582 111 LSGNSIEHALMTLAAMQAGVPAAPVSP--AYSLMshdhaklkhlfDLVKPRVV--FAQSgapFARALAALDLLDVTVVHV 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 139 PGD-------HAAAWL----------------PERLSTMTLTSGSTGLPKAAVHTCQAHLASAQGVLSLMPFGAED---- 191
Cdd:PRK12582 187 TGPgegiasiAFADLAatpptaavaaaiaaitPDTVAKYLFTSGSTGMPKAVINTQRMMCANIAMQEQLRPREPDPpppv 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 192 --DWllsLPLFHVSG-----QGILWrwlfAGARMTVRDKQPLDQMLAGcTHASL---VPTqlwrlLVNNTPV-------- 253
Cdd:PRK12582 267 slDW---MPWNHTMGgnanfNGLLW----GGGTLYIDDGKPLPGMFEE-TIRNLreiSPT-----VYGNVPAgyamlaea 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 254 -------------TLKAVLLGGAAIPVELTE--QA---REQGIRC--WCGYGLTEFASTVC----AKEADGLadVGSALP 309
Cdd:PRK12582 334 mekddalrrsffkNLRLMAYGGATLSDDLYErmQAlavRTTGHRIpfYTGYGATETAPTTTgthwDTERVGL--IGLPLP 411
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 489936067 310 GREVRIVND----EVWLRAASMAQGYWRNGQLMPLV-NAEGWFATRDRGVLKD 357
Cdd:PRK12582 412 GVELKLAPVgdkyEVRVKGPNVTPGYHKDPELTAAAfDEEGFYRLGDAARFVD 464
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
147-460 |
2.84e-08 |
|
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: 55.99 E-value: 2.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 147 LPERLSTMTLTSGSTGLPKAAVHTC------QAHLASAQGVLSLMPF--GAEDDWLLSLpLFHVSGQgilwrwLFAGARM 218
Cdd:cd05973 86 LDSDPFVMMFTSGTTGLPKGVPVPLralaafGAYLRDAVDLRPEDSFwnAADPGWAYGL-YYAITGP------LALGHPT 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 219 TVrdkqpldqmlagcTHASLVPTQLWRLLVN-------NTPVTLKAVLLGGAAIPVELTEQARE----------QGIRcW 281
Cdd:cd05973 159 IL-------------LEGGFSVESTWRVIERlgvtnlaGSPTAYRLLMAAGAEVPARPKGRLRRvssagepltpEVIR-W 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 282 CG----------YGLTEFASTVCAKEADG----LADVGSALPGREVRIVNDE---------------------VWLRaas 326
Cdd:cd05973 225 FDaalgvpihdhYGQTELGMVLANHHALEhpvhAGSAGRAMPGWRVAVLDDDgdelgpgepgrlaidiansplMWFR--- 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 327 maqGYWRNGQLMPlvnAEGWFATRDRGVLK-DGKLTIVGRMDNLFFSGGEGIQPEEVERVIAAHPHVLQAFIVPIEDKEF 405
Cdd:cd05973 302 ---GYQLPDTPAI---DGGYYLTGDTVEFDpDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPER 375
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489936067 406 GHRPVA-VVEYDANAGETNLAE----WVKDKLARFQQP--VCWLTLPPELKAGgiKISRRAL 460
Cdd:cd05973 376 TEVVKAfVVLRGGHEGTPALADelqlHVKKRLSAHAYPrtIHFVDELPKTPSG--KIQRFLL 435
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
35-433 |
4.15e-08 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 55.94 E-value: 4.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 35 ALRLNDEALSWSELCARIDHLASGFAAQGVEEGDGVLLRAWNHPRALLAWLALLQCGARVLPVNPQLPQSLLDALVPD-- 112
Cdd:PRK05691 1149 ALVWDGGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADsg 1228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 113 --LTLRFALDLEAAIALPELSPLQMKSLpgdHAAAWlP----------ERLSTMTLTSGSTGLPKAAVHTCQAHLASAQG 180
Cdd:PRK05691 1229 veLLLTQSHLLERLPQAEGVSAIALDSL---HLDSW-PsqapglhlhgDNLAYVIYTSGSTGQPKGVGNTHAALAERLQW 1304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 181 VLSLMPFGAEDDWLLSLPL-FHVSGQGILWRwLFAGARMTV------RDKQPLDQMLA--GCTHASLVPTqLWRLLVNNT 251
Cdd:PRK05691 1305 MQATYALDDSDVLMQKAPIsFDVSVWECFWP-LITGCRLVLagpgehRDPQRIAELVQqyGVTTLHFVPP-LLQLFIDEP 1382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 252 PVT----LKAVLLGGAAIPVELTEQAREQ--GIRCWCGYGLTEFASTV----CAKEADGLADVGSALPGREVRIVND--- 318
Cdd:PRK05691 1383 LAAactsLRRLFSGGEALPAELRNRVLQRlpQVQLHNRYGPTETAINVthwqCQAEDGERSPIGRPLGNVLCRVLDAeln 1462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 319 --------EVWLRAASMAQGYWRNGQLM-------PLVNA-EGWFATRDRGVLK-DGKLTIVGRMDNLFFSGGEGIQPEE 381
Cdd:PRK05691 1463 llppgvagELCIGGAGLARGYLGRPALTaerfvpdPLGEDgARLYRTGDRARWNaDGALEYLGRLDQQVKLRGFRVEPEE 1542
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 489936067 382 VERVIAAHPHVLQAfIVPIEDKEFGHRPVAVveYDANAGETNLAEWVKDKLA 433
Cdd:PRK05691 1543 IQARLLAQPGVAQA-AVLVREGAAGAQLVGY--YTGEAGQEAEAERLKAALA 1591
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
27-411 |
5.34e-08 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 55.00 E-value: 5.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 27 RQVRAKAPALRLNDEALSWSELCARIDHLASGFAAQGVEEGDGVLLRAWNHPRALLAWLALLQCGarVLPVNPQLP--QS 104
Cdd:PRK10946 33 RHAASDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLG--VAPVNALFShqRS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 105 LLDALVPDLTLR----------FALD--LEAAIA-LPELSPLQMKSLPGDHA-AAWLPERLSTMT-------------LT 157
Cdd:PRK10946 111 ELNAYASQIEPAlliadrqhalFSDDdfLNTLVAeHSSLRVVLLLNDDGEHSlDDAINHPAEDFTatpspadevaffqLS 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 158 SGSTGLPKAAVHTCQAHLASAQGVLSLMPFGAEDDWLLSLPLFH---VSGQGILWRWLFAGARMTVRDKQPLdqmlaGC- 233
Cdd:PRK10946 191 GGSTGTPKLIPRTHNDYYYSVRRSVEICGFTPQTRYLCALPAAHnypMSSPGALGVFLAGGTVVLAPDPSAT-----LCf 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 234 --------THASLVP--TQLWRLLV-----NNTPVTLKAVLLGGAA--------IPVELTEQAREQgircwcgYGLTEfa 290
Cdd:PRK10946 266 pliekhqvNVTALVPpaVSLWLQAIaeggsRAQLASLKLLQVGGARlsetlarrIPAELGCQLQQV-------FGMAE-- 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 291 STVCAKEADGLADVGSALPGR------EVRIVNDEvwlrAASMAQGywRNGQLM-------------PLVNA-----EGW 346
Cdd:PRK10946 337 GLVNYTRLDDSDERIFTTQGRpmspddEVWVADAD----GNPLPQG--EVGRLMtrgpytfrgyyksPQHNAsafdaNGF 410
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489936067 347 FATRDRGVL-KDGKLTIVGRMDNLFFSGGEGIQPEEVERVIAAHPHVLQAFIVPIEDKEFGHRPVA 411
Cdd:PRK10946 411 YCSGDLVSIdPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCA 476
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
305-386 |
5.51e-08 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 55.56 E-value: 5.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 305 GSALPGREVRIVN------------DEVWLRAASMAQGYWRNGQLMP--LVNAEG--WFATRDRGVLKDGKLTIVGRMDN 368
Cdd:PRK05691 373 GRSQPGHAVLIVDpqslevlgdnrvGEIWASGPSIAHGYWRNPEASAktFVEHDGrtWLRTGDLGFLRDGELFVTGRLKD 452
|
90
....*....|....*...
gi 489936067 369 LFFSGGEGIQPEEVERVI 386
Cdd:PRK05691 453 MLIVRGHNLYPQDIEKTV 470
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
153-430 |
7.11e-08 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 54.85 E-value: 7.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 153 TMTLTSGSTGLPKAAVHTCQAHLASAQGVLSLMPF----GAEDDWLLS-LPLFHVSGQGILWRWLFAGA---------RM 218
Cdd:PLN02861 224 TIMYTSGTTGEPKGVILTNRAIIAEVLSTDHLLKVtdrvATEEDSYFSyLPLAHVYDQVIETYCISKGAsigfwqgdiRY 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 219 TVRDKQPL------------DQMLAGC----THASLVPTQLW-------------------------RLLVNNTPVTLKA 257
Cdd:PLN02861 304 LMEDVQALkptifcgvprvyDRIYTGImqkiSSGGMLRKKLFdfaynyklgnlrkglkqeeasprldRLVFDKIKEGLGG 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 258 ---VLLGGAA-IPVELTEQAREqgIRCWC---GYGLTEFAS---TVCAKEADGLADVGSALPGREVRIVN---------- 317
Cdd:PLN02861 384 rvrLLLSGAApLPRHVEEFLRV--TSCSVlsqGYGLTESCGgcfTSIANVFSMVGTVGVPMTTIEARLESvpemgydals 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 318 ----DEVWLRAASMAQGYWRNGQLMPLVNAEGWFATRDRGVLK-DGKLTIVGRMDNLF-FSGGEGIQPEEVERVIAAHPH 391
Cdd:PLN02861 462 dvprGEICLRGNTLFSGYHKRQDLTEEVLIDGWFHTGDIGEWQpNGAMKIIDRKKNIFkLSQGEYVAVENLENTYSRCPL 541
|
330 340 350
....*....|....*....|....*....|....*....
gi 489936067 392 VLQAFIVpieDKEFGHRPVAVVEYDANAgetnLAEWVKD 430
Cdd:PLN02861 542 IASIWVY---GNSFESFLVAVVVPDRQA----LEDWAAN 573
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
348-460 |
9.73e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 53.89 E-value: 9.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 348 ATRDRGVLK-DGKLTIVGRMDNLFFSGGEGIQPEEVERVIAAHPHVLQAFIVPIEDKEFGHRPVAVVEYDANAGETNLAE 426
Cdd:PRK08308 294 FTKDLGYKSeRGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVISHEEIDPVQLRE 373
|
90 100 110
....*....|....*....|....*....|....*.
gi 489936067 427 WVKDKLARFQQPVCWLTLP--PELKAGgiKISRRAL 460
Cdd:PRK08308 374 WCIQHLAPYQVPHEIESVTeiPKNANG--KVSRKLL 407
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
40-452 |
1.87e-07 |
|
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: 53.13 E-value: 1.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 40 DEALSWSELCARIDHLASGFAAQGVEEGDGVLLRAWNHPRALLAWLALLQCGARVLPVNPQLpqsLLDALVPDLTLRFAL 119
Cdd:cd05940 1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNL---RGESLAHCLNVSSAK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 120 DLEAAIALpelsplqmkslpgdhaaawlperlstMTLTSGSTGLPKAAVHTCQAHLASAQGVLSLMPFGAEDDWLLSLPL 199
Cdd:cd05940 78 HLVVDAAL--------------------------YIYTSGTTGLPKAAIISHRRAWRGGAFFAGSGGALPSDVLYTCLPL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 200 FHVSGQGILW-RWLFAGARMTVRDKQPLDQMLAGCTH--ASLVP--TQLWRLLVNNTPVtlkavllggaaipveltEQAR 274
Cdd:cd05940 132 YHSTALIVGWsACLASGATLVIRKKFSASNFWDDIRKyqATIFQyiGELCRYLLNQPPK-----------------PTER 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 275 EQGIRCWCGYGL-----------------TEF-ASTVCA---------------------------------------KE 297
Cdd:cd05940 195 KHKVRMIFGNGLrpdiweefkerfgvpriAEFyAATEGNsgfinffgkpgaigrnpsllrkvaplalvkydlesgepiRD 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 298 ADGLA-DVGSALPGREVRIVND--------------EVWLRAAsMAQG--YWRNGQLMpLVNAEGWFATRDRgvlkdgkl 360
Cdd:cd05940 275 AEGRCiKVPRGEPGLLISRINPlepfdgytdpaateKKILRDV-FKKGdaWFNTGDLM-RLDGEGFWYFVDR-------- 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 361 tiVGrmdNLFFSGGEGIQPEEVERVIAAHPHVLQAFI--VPIEDKEfGHRPVAVVEYDANAGE--TNLAEWVKDKLARFQ 436
Cdd:cd05940 345 --LG---DTFRWKGENVSTTEVAAVLGAFPGVEEANVygVQVPGTD-GRAGMAAIVLQPNEEFdlSALAAHLEKNLPGYA 418
|
490
....*....|....*.
gi 489936067 437 QPVcWLTLPPELKAGG 452
Cdd:cd05940 419 RPL-FLRLQPEMEITG 433
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
30-316 |
3.71e-07 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 52.59 E-value: 3.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 30 RAKAPALRLNDEALSWSELCARIDHLASGFAAQGVEEGDGVLLRAWNHPRALLAWLALLQCGARVLPVNP-----QLPQS 104
Cdd:PRK09274 29 GGRGADGKLAYDELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGAVPVLVDPgmgikNLKQC 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 105 L----LDALV----------------PDLTLRFALD---------LEAAIALPELSPLQMKSLPGDHAAAwlperlstMT 155
Cdd:PRK09274 109 LaeaqPDAFIgipkahlarrlfgwgkPSVRRLVTVGgrllwggttLATLLRDGAAAPFPMADLAPDDMAA--------IL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 156 LTSGSTGLPKAAVHTCQAHLASAQGVLSLMPFGAEDDWLLSLPLFHvsgqgilwrwLFA---GARMTVRDKQPL------ 226
Cdd:PRK09274 181 FTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEIDLPTFPLFA----------LFGpalGMTSVIPDMDPTrpatvd 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 227 -DQMLA-----GCTHASLVPTqLWRLL----VNNTPV--TLKAVLLGGAAIPVELTEQARE---QGIRCWCGYGLTE--- 288
Cdd:PRK09274 251 pAKLFAaieryGVTNLFGSPA-LLERLgrygEANGIKlpSLRRVISAGAPVPIAVIERFRAmlpPDAEILTPYGATEalp 329
|
330 340 350
....*....|....*....|....*....|....*..
gi 489936067 289 ---------FASTVCAKEADGLADVGSALPGREVRIV 316
Cdd:PRK09274 330 issiesreiLFATRAATDNGAGICVGRPVDGVEVRII 366
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
261-398 |
1.72e-06 |
|
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: 50.43 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 261 GGAAIPVELTEQAREQGIRCWCGYGLTEFAS--TVCAKEADGLADVGSALPGREVRIVND------EVWLRAASMAQGYW 332
Cdd:cd05933 328 GAAPISRETLEFFLSLNIPIMELYGMSETSGphTISNPQAYRLLSCGKALPGCKTKIHNPdadgigEICFWGRHVFMGYL 407
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 333 RNGQ-LMPLVNAEGWFATRDRGVL-KDGKLTIVGRMDNLFF-SGGEGIQPEEVE-RVIAAHPHVLQAFIV 398
Cdd:cd05933 408 NMEDkTEEAIDEDGWLHSGDLGKLdEDGFLYITGRIKELIItAGGENVPPVPIEdAVKKELPIISNAMLI 477
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
148-385 |
2.37e-06 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 50.02 E-value: 2.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 148 PERLSTMTLTSGSTGLPKAAVHTCQAHLASAQGVLSLM-----PFGAEDDWLLSLPLFHVSGQGI------------LWR 210
Cdd:PLN02614 222 KSDICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRLLksanaALTVKDVYLSYLPLAHIFDRVIeecfiqhgaaigFWR 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 211 W--------------------------LFAGARMTVRD-----KQPLD--------QMLAGCTHASLVPTqLWRLLVNNT 251
Cdd:PLN02614 302 GdvklliedlgelkptifcavprvldrVYSGLQKKLSDggflkKFVFDsafsykfgNMKKGQSHVEASPL-CDKLVFNKV 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 252 PVTLKA---VLLGGAAiPVELTEQAREQGIRCwC----GYGLTEFASTVCAK---EADGLADVGSALPGREVRI------ 315
Cdd:PLN02614 381 KQGLGGnvrIILSGAA-PLASHVESFLRVVAC-ChvlqGYGLTESCAGTFVSlpdELDMLGTVGPPVPNVDIRLesvpem 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 316 --------VNDEVWLRAASMAQGYWRNGQLMPLVNAEGWFATRDRGVLK-DGKLTIVGRMDNLF-FSGGEGIQPEEVERV 385
Cdd:PLN02614 459 eydalastPRGEICIRGKTLFSGYYKREDLTKEVLIDGWLHTGDVGEWQpNGSMKIIDRKKNIFkLSQGEYVAVENIENI 538
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
381-438 |
2.42e-06 |
|
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: 45.23 E-value: 2.42e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 381 EVERVIAAHPHVLQAFIVPIEDKEFGHRPVA--VVEYDANAGETNLAEWVKDKLARFQQP 438
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAfvVLKPGVELLEEELVAHVREELGPYAVP 60
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
302-459 |
5.47e-06 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 48.97 E-value: 5.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 302 ADVGSALPGREVrivnDEVWLRAASMAQGYWRNGQLMPLV-------------NAEG------WFATRDRGVLKDGKLTI 362
Cdd:PRK12476 418 PDTGAELPDGEV----GEIWLHGDNIGRGYWGRPEETERTfgaklqsrlaegsHADGaaddgtWLRTGDLGVYLDGELYI 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 363 VGRMDNLFFSGGEGIQPEEVERVIA-AHPHV----LQAFIVPIEDKEfghRPVAVVEYDANAGETNLAEWVKDKLA---- 433
Cdd:PRK12476 494 TGRIADLIVIDGRNHYPQDIEATVAeASPMVrrgyVTAFTVPAEDNE---RLVIVAERAAGTSRADPAPAIDAIRAavsr 570
|
170 180 190
....*....|....*....|....*....|..
gi 489936067 434 RFQQPVCWLTLPPelkAGGI------KISRRA 459
Cdd:PRK12476 571 RHGLAVADVRLVP---AGAIprttsgKLARRA 599
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
43-414 |
7.40e-06 |
|
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: 48.23 E-value: 7.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 43 LSWSELCARIDHLASGFAAQGVEEGDGVLLRAWNHPRALLAWLALLQCGARVLPVNP-----QLPQSLLDAlVPDltlrf 117
Cdd:cd05910 3 LSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPgmgrkNLKQCLQEA-EPD----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 118 aldleAAIALPelsplqmksLPGDHAAawlperlstMTLTSGSTGLPKAAVHTCQAHLASAQGVLSLMPFGAEDDWLLSL 197
Cdd:cd05910 77 -----AFIGIP---------KADEPAA---------ILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGEVDLATF 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 198 PLFHvsgqgilwrwLFAGA-------------RMTVRDKQPLDQMLA--GCTHASLVPTqLWRLLV-----NNTPV-TLK 256
Cdd:cd05910 134 PLFA----------LFGPAlgltsvipdmdptRPARADPQKLVGAIRqyGVSIVFGSPA-LLERVArycaqHGITLpSLR 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 257 AVLLGGAAIPVELTEQARE---QGIRCWCGYGLTE------------FASTVCAKEADGLADVGSALPGREVRIV--ND- 318
Cdd:cd05910 203 RVLSAGAPVPIALAARLRKmlsDEAEILTPYGATEalpvssigsrelLATTTAATSGGAGTCVGRPIPGVRVRIIeiDDe 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 319 -----------------EVWLRAASMAQGYWRNGQLMPLV----NAEG-WFATRDRGVLKD-GKLTIVGRMDNLFFSGGE 375
Cdd:cd05910 283 piaewddtlelprgeigEITVTGPTVTPTYVNRPVATALAkiddNSEGfWHRMGDLGYLDDeGRLWFCGRKAHRVITTGG 362
|
410 420 430
....*....|....*....|....*....|....*....
gi 489936067 376 GIQPEEVERVIAAHPHVLQAFIVPIeDKEFGHRPVAVVE 414
Cdd:cd05910 363 TLYTEPVERVFNTHPGVRRSALVGV-GKPGCQLPVLCVE 400
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
313-415 |
1.94e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 47.24 E-value: 1.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 313 VRIVN------------DEVWLRAASMAQGYWRNGQLMP------LVNA-----EG-WFATRDRGVLKDGKLTIVGRMDN 368
Cdd:PRK05850 381 VRIVDpdtciecpagtvGEIWVHGDNVAAGYWQKPEETErtfgatLVDPspgtpEGpWLRTGDLGFISEGELFIVGRIKD 460
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 489936067 369 LFFSGGEGIQPEEVERVIAA-HPHVLQAFIVPIEDKEfghRPVAVVEY 415
Cdd:PRK05850 461 LLIVDGRNHYPDDIEATIQEiTGGRVAAISVPDDGTE---KLVAIIEL 505
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
40-208 |
2.63e-05 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 46.65 E-value: 2.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 40 DEALSWSELCARIDHLASGFAAQGVEEGDGVLLRAWNHPRALLAWLALLQCGARVLPVNPQLPqslLDALVPDLTLRF-- 117
Cdd:cd05939 1 DRHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLR---LESLLHCITVSKak 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 118 ALDLEAAIALPELSPLQMKSLPGDHAAAWLperlsTMTLTSGSTGLPKAAVHTCQAHLASAQGVLSLMPFGAEDDWLLSL 197
Cdd:cd05939 78 ALIFNLLDPLLTQSSTEPPSQDDVNFRDKL-----FYIYTSGTTGLPKAAVIVHSRYYRIAAGAYYAFGMRPEDVVYDCL 152
|
170
....*....|.
gi 489936067 198 PLFHVSGqGIL 208
Cdd:cd05939 153 PLYHSAG-GIM 162
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
282-399 |
2.75e-05 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 46.65 E-value: 2.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 282 CGY-GLTEFASTVCAKEADGLAD--VGsalpgrevrivndEVWLRAASMAQGYW----------RN--GQLMPLVNAEG- 345
Cdd:PRK07769 393 AGKvGVSEWAVIVDPETASELPDgqIG-------------EIWLHGNNIGTGYWgkpeetaatfQNilKSRLSESHAEGa 459
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489936067 346 -----WFATRDRGVLKDGKLTIVGRMDNLFFSGGEGIQPEEVERVI-----AAHPHVLQAFIVP 399
Cdd:PRK07769 460 pddalWVRTGDYGVYFDGELYITGRVKDLVIIDGRNHYPQDLEYTAqeatkALRTGYVAAFSVP 523
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
305-471 |
3.56e-05 |
|
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: 46.15 E-value: 3.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 305 GSALPGREVRIVNDEVWLRAA--------------SMAQGYWRNGQLMP---LVNAEGWFATRDRGVL-KDGKLTIVGRM 366
Cdd:cd05967 414 GKPVPGYQVQVLDEDGEPVGPnelgniviklplppGCLLTLWKNDERFKklyLSKFPGYYDTGDAGYKdEDGYLFIMGRT 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 367 DNLFFSGGEGIQPEEVERVIAAHPHVLQAFIVPIEDKEFGHRPVAVV------EYDANAGETNLAEWVKDKL---ARFQQ 437
Cdd:cd05967 494 DDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELKGQVPLGLVvlkegvKITAEELEKELVALVREQIgpvAAFRL 573
|
170 180 190
....*....|....*....|....*....|....
gi 489936067 438 PVCWLTLPpelKAGGIKISRRALSDWVSASSLTL 471
Cdd:cd05967 574 VIFVKRLP---KTRSGKILRRTLRKIADGEDYTI 604
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
147-202 |
2.13e-04 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 43.95 E-value: 2.13e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 489936067 147 LPERLSTMTLTSGSTGLPKAAVHTCQAHLASAQGVLSLMP-FGAEDDWLLSLPLFHV 202
Cdd:PLN02387 248 SPNDIAVIMYTSGSTGLPKGVMMTHGNIVATVAGVMTVVPkLGKNDVYLAYLPLAHI 304
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
148-439 |
9.22e-04 |
|
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: 41.62 E-value: 9.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 148 PERLSTMTLTSGSTGLPKAAV--HTCQAHLASAqgvLSLMPFGA--EDDWLLSLPL----FHVSgQGILWrwLFAGARMT 219
Cdd:cd17648 93 STDLAYAIYTSGTTGKPKGVLveHGSVVNLRTS---LSERYFGRdnGDEAVLFFSNyvfdFFVE-QMTLA--LLNGQKLV 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 220 VrdkqPLDQMLA------------GCTHASLVPTQLWRLLVNNTPvTLKAVLLGGAAIPVELTEQAREQ-GIRCWCGYGL 286
Cdd:cd17648 167 V----PPDEMRFdpdrfyayinreKVTYLSGTPSVLQQYDLARLP-HLKRVDAAGEEFTAPVFEKLRSRfAGLIINAYGP 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 287 TEFASTVCAKEADGLA----DVGSALPGREVRIVND-----------EVWLRAASMAQGYWRNGQLMPLVNAEGWFAT-- 349
Cdd:cd17648 242 TETTVTNHKRFFPGDQrfdkSLGRPVRNTKCYVLNDamkrvpvgavgELYLGGDGVARGYLNRPELTAERFLPNPFQTeq 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 350 -RDRGV-------------LKDGKLTIVGRMDNLFFSGGEGIQPEEVERVIAAHPHVLQAFIVPIEDKEFGHRPVA---V 412
Cdd:cd17648 322 eRARGRnarlyktgdlvrwLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAKEDASQAQSRIQkylV 401
|
330 340 350
....*....|....*....|....*....|
gi 489936067 413 VEYDANAG---ETNLAEWVKDKLARFQQPV 439
Cdd:cd17648 402 GYYLPEPGhvpESDLLSFLRAKLPRYMVPA 431
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
348-460 |
1.11e-03 |
|
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: 41.39 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 348 ATRDrgvlKDGKLTIVGRMDNLFFSGGEGIQPEEVERVIAAHPHVLQAFIVPIEDKEFGHRPVA-VVEYDANAGETNLAE 426
Cdd:cd05966 477 ARRD----EDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAfVTLKDGEEPSDELRK 552
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 489936067 427 ----WVKDKLARFQQP--VCWLTLPPELKAGgiKISRRAL 460
Cdd:cd05966 553 elrkHVRKEIGPIATPdkIQFVPGLPKTRSG--KIMRRIL 590
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
305-395 |
1.47e-03 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 41.03 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 305 GSALPGREVRIVND-----------EVWLRAA--SMAQGYWRNGQLMPLVNAEGWF-----ATRDrgvlKDGKLTIVGRM 366
Cdd:PRK04319 379 GKPLPGIEAAIVDDqgnelppnrmgNLAIKKGwpSMMRGIWNNPEKYESYFAGDWYvsgdsAYMD----EDGYFWFQGRV 454
|
90 100
....*....|....*....|....*....
gi 489936067 367 DNLFFSGGEGIQPEEVERVIAAHPHVLQA 395
Cdd:PRK04319 455 DDVIKTSGERVGPFEVESKLMEHPAVAEA 483
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
320-460 |
2.21e-03 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 40.70 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 320 VWLRAASMAQGYWRN-GQLMplvnaegwFATRDRGVL-KDGKLTIVGRMDNLFFSGGEGIQPEEVERVIAAHPHVLQAFI 397
Cdd:PRK10524 455 VWGDDDRFVKTYWSLfGRQV--------YSTFDWGIRdADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAV 526
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489936067 398 VPIEDKEFGHRPVA-VVEYDANAGETNLAEW---------VKDKLARFQQP--VCWLTLPPELKAGgiKISRRAL 460
Cdd:PRK10524 527 VGVKDALKGQVAVAfVVPKDSDSLADREARLalekeimalVDSQLGAVARParVWFVSALPKTRSG--KLLRRAI 599
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
30-460 |
3.11e-03 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 40.54 E-value: 3.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 30 RAKAPALRLNDEALSWSELCARIDHLASGFAAQGVEEGDGVLLRAWNHPRALLAWLALLQCGARVLPVNPQLPQSLLDAL 109
Cdd:PRK05691 2201 TPQAPALTFAGQTLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHYM 2280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 110 VPD----LTLRFALDLEAAIALP--------ELSPLQMKSLPGDHAAAW-LPERLSTMTLTSGSTGLPKAAVhTCQAHLA 176
Cdd:PRK05691 2281 IEDsgigLLLSDRALFEALGELPagvarwclEDDAAALAAYSDAPLPFLsLPQHQAYLIYTSGSTGKPKGVV-VSHGEIA 2359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 177 -SAQGVLSLMPFGAEDDWLLSLPLFHVSGQGILWRWLFAGARMTVR-----DKQPLDQMLA--GCTHASLVP---TQLWR 245
Cdd:PRK05691 2360 mHCQAVIERFGMRADDCELHFYSINFDAASERLLVPLLCGARVVLRaqgqwGAEEICQLIReqQVSILGFTPsygSQLAQ 2439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 246 LLVNN---TPVTLkaVLLGGAAIPVELTEQARE--QGIRCWCGYGLTE-----FASTVCAKEADGLADV--GSALPGREV 313
Cdd:PRK05691 2440 WLAGQgeqLPVRM--CITGGEALTGEHLQRIRQafAPQLFFNAYGPTEtvvmpLACLAPEQLEEGAASVpiGRVVGARVA 2517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 314 RIVND-----------EVWLRAASMAQGYWRNgqlmPLVNAEGWFA------------TRDRGVLK-DGKLTIVGRMDNL 369
Cdd:PRK05691 2518 YILDAdlalvpqgatgELYVGGAGLAQGYHDR----PGLTAERFVAdpfaadggrlyrTGDLVRLRaDGLVEYVGRIDHQ 2593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 370 FFSGGEGIQPEEVERVIAAHPHVLQAFIVPIeDKEFGHRPVA-VVEYDANAGETNLAEW---VKDKLaRFQQP------- 438
Cdd:PRK05691 2594 VKIRGFRIELGEIESRLLEHPAVREAVVLAL-DTPSGKQLAGyLVSAVAGQDDEAQAALreaLKAHL-KQQLPdymvpah 2671
|
490 500
....*....|....*....|...
gi 489936067 439 -VCWLTLPpeLKAGGiKISRRAL 460
Cdd:PRK05691 2672 lILLDSLP--LTANG-KLDRRAL 2691
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
148-204 |
4.42e-03 |
|
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: 39.34 E-value: 4.42e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 489936067 148 PERLSTMTLTSGSTGLPKAAVHTCQAHLASAQGVLSLMPFGAEDDWLLSLPLFHVSG 204
Cdd:cd05937 86 PDDPAILIYTSGTTGLPKAAAISWRRTLVTSNLLSHDLNLKNGDRTYTCMPLYHGTA 142
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
318-414 |
5.28e-03 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 39.11 E-value: 5.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 318 DEVWLRAASMAQGYWRNgqlmPLVNAEGWFA--------TRDRGVLKDGKLTIVGRMDnlfFS---GGEGIQPEEVERVI 386
Cdd:PRK04813 345 GEIVISGPSVSKGYLNN----PEKTAEAFFTfdgqpayhTGDAGYLEDGLLFYQGRID---FQiklNGYRIELEEIEQNL 417
|
90 100
....*....|....*....|....*...
gi 489936067 387 AAHPHVLQAFIVPIEDKEFGHRPVAVVE 414
Cdd:PRK04813 418 RQSSYVESAVVVPYNKDHKVQYLIAYVV 445
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
301-428 |
8.54e-03 |
|
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: 38.48 E-value: 8.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 301 LADVGSALPGREVRIVND------------EVWLRAASMAQGYWR-------------NGQLMPLVNAEGWFATRDRGVL 355
Cdd:cd05905 360 LQDSGKVLPGAQVAIVNPetkglckdgeigEIWVNSPANASGYFLldgetndtfkvfpSTRLSTGITNNSYARTGLLGFL 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936067 356 KDGKLT-----------IVGRMDNLFFSGGEGIQPEEVER-VIAAHPHVLQAFIVPIEdkefgHRPVAVVEYDAnAGETN 423
Cdd:cd05905 440 RPTKCTdlnveehdllfVVGSIDETLEVRGLRHHPSDIEAtVMRVHPYRGRCAVFSIT-----GLVVVVAEQPP-GSEEE 513
|
....*
gi 489936067 424 LAEWV 428
Cdd:cd05905 514 ALDLV 518
|
|
| |
