|
Name |
Accession |
Description |
Interval |
E-value |
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
27-448 |
4.77e-79 |
|
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: 259.06 E-value: 4.77e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 27 PITYGALWAELGERSLAMMAR-FETDRAVALQSDHGAETSIVELALLRAK-IPVlslPAFFT--REQSRHAIALCGAdpd 102
Cdd:cd05907 5 PITWAEFAEEVRALAKGLIALgVEPGDRVAILSRNRPEWTIADLAILAIGaVPV---PIYPTssAEQIAYILNDSEA--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 103 piqspsgtarsrRSASVPLPRGTARITFTSGSTGTPKGICLSADHMLTVAQSIVAAVGAEHAGRHLALLPPGILLETVAG 182
Cdd:cd05907 79 ------------KALFVEDPDDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPATEGDRHLSFLPLAHVFERRAG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 183 FFPTLLAGGCYVCPPQAMIGFADpfrpdfvkaatiIAEQRITSLILVPEYLEGL---VRVMETTGLR--------LPLLT 251
Cdd:cd05907 147 LYVPLLAGARIYFASSAETLLDD------------LSEVRPTVFLAVPRVWEKVyaaIKVKAVPGLKrklfdlavGGRLR 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 252 LVAVGGARTSIPLMDRARRLGLPIRQGYGLTECASVVSLQDAGDDDPSSVGRCLPHMTVRVADDGEIILDGP-VCLG--- 327
Cdd:cd05907 215 FAASGGAPLPAELLHFFRALGIPVYEGYGLTETSAVVTLNPPGDNRIGTVGKPLPGVEVRIADDGEILVRGPnVMLGyyk 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 328 -----AVGGEAPGsPLQTGDIGSIDSDGRLHIEGRKSNLIITSFGRNISPEWVEAALVEQPEVMQAMVYGDGLPTPAALL 402
Cdd:cd05907 295 npeatAEALDADG-WLHTGDLGEIDEDGFLHITGRKKDLIITSGGKNISPEPIENALKASPLISQAVVIGDGRPFLVALI 373
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2741210702 403 VP-----------------------SHPDADLAAAVA--RANEKLPAYAQISAWREAAH-FTPMNGQLTGNG 448
Cdd:cd05907 374 VPdpealeawaeehgiaytdvaelaANPAVRAEIEAAveAANARLSRYEQIKKFLLLPEpFTIENGELTPTL 445
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
15-392 |
1.15e-56 |
|
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: 199.27 E-value: 1.15e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 15 PQRIALDAlDGAPITYgalwAELGERSLAMMARF------ETDRaVALQSDHGAETSIVELALLRAKIPVLSLPAFFTRE 88
Cdd:COG0318 13 PDRPALVF-GGRRLTY----AELDARARRLAAALralgvgPGDR-VALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 89 QSRHAIALCGAdpdpiqspsgtarsrrSASVplprgTARITFTSGSTGTPKGICLSADHMLTVAQSIVAAVGAEHAGRHL 168
Cdd:COG0318 87 ELAYILEDSGA----------------RALV-----TALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 169 ALLPP----GIlletVAGFFPTLLAGGCYVCPPqamigfadpfRPDFVKAATIIAEQRITSLILVPEYLEGLVRVMETTG 244
Cdd:COG0318 146 VALPLfhvfGL----TVGLLAPLLAGATLVLLP----------RFDPERVLELIERERVTVLFGVPTMLARLLRHPEFAR 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 245 LRLPLLTLVAVGGARTSIPLMDRAR-RLGLPIRQGYGLTECASVVSL--QDAGDDDPSSVGRCLPHMTVRVADD------ 315
Cdd:COG0318 212 YDLSSLRLVVSGGAPLPPELLERFEeRFGVRIVEGYGLTETSPVVTVnpEDPGERRPGSVGRPLPGVEVRIVDEdgrelp 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 316 ----GEIILDGP-VCLGAVG-GEAPGSPLQ-----TGDIGSIDSDGRLHIEGRKSNLIITSfGRNISPEWVEAALVEQPE 384
Cdd:COG0318 292 pgevGEIVVRGPnVMKGYWNdPEATAEAFRdgwlrTGDLGRLDEDGYLYIVGRKKDMIISG-GENVYPAEVEEVLAAHPG 370
|
....*...
gi 2741210702 385 VMQAMVYG 392
Cdd:COG0318 371 VAEAAVVG 378
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
125-392 |
2.51e-50 |
|
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: 178.63 E-value: 2.51e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 125 TARITFTSGSTGTPKGICLSADHMLTVAQSIVAAVGAEHAGRHLALLPPG-ILLetVAGFFPTLLAGGCYVCPPqamigf 203
Cdd:cd04433 2 PALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFhIGG--LFGLLGALLAGGTVVLLP------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 204 adpfRPDFVKAATIIAEQRITSLILVPEYLEGLVRVMETTGLRLPLLTLVAVGGARTSIPLMDRA-RRLGLPIRQGYGLT 282
Cdd:cd04433 74 ----KFDPEAALELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGAPLPPELLERFeEAPGIKLVNGYGLT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 283 ECASVVSLQDAGDDD--PSSVGRCLPHMTVRVADD----------GEIILDGPVC-LGAVG-GEAPGSPLQ-----TGDI 343
Cdd:cd04433 150 ETGGTVATGPPDDDArkPGSVGRPVPGVEVRIVDPdggelppgeiGELVVRGPSVmKGYWNnPEATAAVDEdgwyrTGDL 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2741210702 344 GSIDSDGRLHIEGRKSNLIITSfGRNISPEWVEAALVEQPEVMQAMVYG 392
Cdd:cd04433 230 GRLDEDGYLYIVGRLKDMIKSG-GENVYPAEVEAVLLGHPGVAEAAVVG 277
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
125-404 |
4.92e-43 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 164.12 E-value: 4.92e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 125 TARITFTSGSTGTPKGICLSADHMLTVAQSIVAAVGAEHAGRHLALLPPGILLETVAGFFptLLAGGCyvcppqaMIGFA 204
Cdd:COG1022 185 LATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFLPLAHVFERTVSYY--ALAAGA-------TVAFA 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 205 DpfRPDFVKAAtiIAEQRITSLILVPEYLEGL-----VRVMETTGLRLPLLTL-VAVGGAR-------TSIPLMDRARR- 270
Cdd:COG1022 256 E--SPDTLAED--LREVKPTFMLAVPRVWEKVyagiqAKAEEAGGLKRKLFRWaLAVGRRYararlagKSPSLLLRLKHa 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 271 --------------------------------------LGLPIRQGYGLTECASVVSLQDAGDDDPSSVGRCLPHMTVRV 312
Cdd:COG1022 332 ladklvfsklrealggrlrfavsggaalgpelarffraLGIPVLEGYGLTETSPVITVNRPGDNRIGTVGPPLPGVEVKI 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 313 ADDGEIILDGP-VCLG-----AVGGEAPGSP--LQTGDIGSIDSDGRLHIEGRKSNLIITSFGRNISPEWVEAALVEQPE 384
Cdd:COG1022 412 AEDGEILVRGPnVMKGyyknpEATAEAFDADgwLHTGDIGELDEDGFLRITGRKKDLIVTSGGKNVAPQPIENALKASPL 491
|
330 340
....*....|....*....|
gi 2741210702 385 VMQAMVYGDGLPTPAALLVP 404
Cdd:COG1022 492 IEQAVVVGDGRPFLAALIVP 511
|
|
| PqqC |
COG5424 |
Pyrroloquinoline quinone (PQQ) biosynthesis protein C [Coenzyme transport and metabolism]; |
466-678 |
7.60e-42 |
|
Pyrroloquinoline quinone (PQQ) biosynthesis protein C [Coenzyme transport and metabolism];
Pssm-ID: 444176 Cd Length: 228 Bit Score: 151.58 E-value: 7.60e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 466 FFTELEARTvrERLRFLAVPQLQAGLNGTISRGAYLDYLEQAYHHVRHTVPLMQAARARLTDRaDIVAALDDYIAEETG- 544
Cdd:COG5424 7 FEARLRAEI--ARRYLLKHPFLQRLREGKLTREQLRAFALQRYHYVKHFPRYLAAILSRCPDE-ELRRALLENLYEEDGe 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 545 -----HEEWILSDIAAAGGDAEAVRASKPGPATAAMVDHAYARIANGNAMAFFGMVYVLESVSVAFATRGAAAVAKKLGL 619
Cdd:COG5424 84 gpeegHIELWLRFAEALGLDREEVDARPPLPETRAAVDAYVNFCRRRSLLEAVAASLTAEGFAPEISRERLEGLLEHYGL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2741210702 620 P-PQAFTYLTSHGALDQEHMTFFANLVNGL-DDPADRDAILSMAQEIFGLFGGIFAAIELE 678
Cdd:COG5424 164 PdEEALEYFRLHAELDPRHAEEALELVLRLaDTPEDQEAALEAARFKLDLLWAFLDALYRA 224
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
126-392 |
1.38e-38 |
|
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: 148.53 E-value: 1.38e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 126 ARITFTSGSTGTPKGICLSADHMLTVAQSIVAAVGAEHAGRHLALLPpgiLLETVAG---FFPTLLAGGCYVCPPQamig 202
Cdd:cd17631 101 ALLMYTSGTTGRPKGAMLTHRNLLWNAVNALAALDLGPDDVLLVVAP---LFHIGGLgvfTLPTLLRGGTVVILRK---- 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 203 fadpFRPDfvKAATIIAEQRITSLILVPEYLEGLVRVMETTGLRLPLLTLVAVGGARTSIPLMDRARRLGLPIRQGYGLT 282
Cdd:cd17631 174 ----FDPE--TVLDLIERHRVTSFFLVPTMIQALLQHPRFATTDLSSLRAVIYGGAPMPERLLRALQARGVKFVQGYGMT 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 283 ECASVVSLQDAGDDD--PSSVGRCLPHMTVRVADD----------GEIILDGP-VCLGAVGGEAP------GSPLQTGDI 343
Cdd:cd17631 248 ETSPGVTFLSPEDHRrkLGSAGRPVFFVEVRIVDPdgrevppgevGEIVVRGPhVMAGYWNRPEAtaaafrDGWFHTGDL 327
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2741210702 344 GSIDSDGRLHIEGRKSNLIITSfGRNISPEWVEAALVEQPEVMQAMVYG 392
Cdd:cd17631 328 GRLDEDGYLYIVDRKKDMIISG-GENVYPAEVEDVLYEHPAVAEVAVIG 375
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
124-432 |
1.94e-38 |
|
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: 145.17 E-value: 1.94e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 124 GTARITFTSGSTGTPKGIclsadhMLTVAQSIVAAVGAehaGRHLALLPPGILLET-----VAGFFP---TLLAGGcyvc 195
Cdd:cd17630 1 RLATVILTSGSTGTPKAV------VHTAANLLASAAGL---HSRLGFGGGDSWLLSlplyhVGGLAIlvrSLLAGA---- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 196 pPQAMIGFADPFRPDfvkaatiIAEQRITSLILVPEYLEglvRVMETTGLRLPLLTL--VAVGGARTSIPLMDRARRLGL 273
Cdd:cd17630 68 -ELVLLERNQALAED-------LAPPGVTHVSLVPTQLQ---RLLDSGQGPAALKSLraVLLGGAPIPPELLERAADRGI 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 274 PIRQGYGLTECASVVSLQDAGDDDPSSVGRCLPHMTVRVADDGEIILDGP-VCLGAVGGEAPGSPL-----QTGDIGSID 347
Cdd:cd17630 137 PLYTTYGMTETASQVATKRPDGFGRGGVGVLLPGRELRIVEDGEIWVGGAsLAMGYLRGQLVPEFNedgwfTTKDLGELH 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 348 SDGRLHIEGRKSNLIItSFGRNISPEWVEAALVEQPEVMQAMVYGDGLPT----PAALLVpSHPDADLAAAVARANEKLP 423
Cdd:cd17630 217 ADGRLTVLGRADNMII-SGGENIQPEEIEAALAAHPAVRDAFVVGVPDEElgqrPVAVIV-GRGPADPAELRAWLKDKLA 294
|
....*....
gi 2741210702 424 AYAQISAWR 432
Cdd:cd17630 295 RFKLPKRIY 303
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
15-365 |
1.96e-36 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 141.68 E-value: 1.96e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 15 PQRIALDALDGAPITYgalwAELGERSLAMMARF-----ETDRAVALQSDHGAETSIVELALLRAKIPVLSLPAFFTREQ 89
Cdd:pfam00501 9 PDKTALEVGEGRRLTY----RELDERANRLAAGLralgvGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 90 SRHAIALCGA------------------------------DPDPIQSPS---GTARSRRSASVPLPRGTAR----ITFTS 132
Cdd:pfam00501 85 LAYILEDSGAkvlitddalkleellealgklevvklvlvlDRDPVLKEEplpEEAKPADVPPPPPPPPDPDdlayIIYTS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 133 GSTGTPKGICLSADHMLTVAQSI----VAAVGAEHAGRHLALLPPGILLETVAGFFPTLLAGGCYVCPPqamiGFADPFR 208
Cdd:pfam00501 165 GTTGKPKGVMLTHRNLVANVLSIkrvrPRGFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVVLPP----GFPALDP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 209 PDFVKAatiIAEQRITSLILVPEYLEGLVRVMETTGLRLPLLTLVAVGGARTSIPLMDRAR-RLGLPIRQGYGLTECASV 287
Cdd:pfam00501 241 AALLEL---IERYKVTVLYGVPTLLNMLLEAGAPKRALLSSLRLVLSGGAPLPPELARRFReLFGGALVNGYGLTETTGV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 288 VSLQDAGDDD---PSSVGRCLPHMTVRVADD-----------GEIILDGP-VCLGAVGGEA-------PGSPLQTGDIGS 345
Cdd:pfam00501 318 VTTPLPLDEDlrsLGSVGRPLPGTEVKIVDDetgepvppgepGELCVRGPgVMKGYLNDPEltaeafdEDGWYRTGDLGR 397
|
410 420
....*....|....*....|
gi 2741210702 346 IDSDGRLHIEGRKSNLIITS 365
Cdd:pfam00501 398 RDEDGYLEIVGRKKDQIKLG 417
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
15-392 |
3.59e-36 |
|
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: 141.93 E-value: 3.59e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 15 PQRIALdALDGAPITYGALWaelgERSLAMMARFET------DRaVALQSDHGAETSIVELALLRAKIPVLSLPAFFTRE 88
Cdd:cd05936 13 PDKTAL-IFMGRKLTYRELD----ALAEAFAAGLQNlgvqpgDR-VALMLPNCPQFPIAYFGALKAGAVVVPLNPLYTPR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 89 QSRHAIALCGA----DPDPIQSPSGTARSRRSASVPLPRGTARITFTSGSTGTPKGICLSADHMLTVAQSIVAAVGAEHA 164
Cdd:cd05936 87 ELEHILNDSGAkaliVAVSFTDLLAAGAPLGERVALTPEDVAVLQYTSGTTGVPKGAMLTHRNLVANALQIKAWLEDLLE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 165 G--RHLALLPP-GILLETVAGFFPtLLAGGCYVCPPQamigfadpFRP-DFVKAatiIAEQRITSLILVPEYLEGLVRVM 240
Cdd:cd05936 167 GddVVLAALPLfHVFGLTVALLLP-LALGATIVLIPR--------FRPiGVLKE---IRKHRVTIFPGVPTMYIALLNAP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 241 ETTGLRLPLLTLVAVGGARTSIPLMDR-ARRLGLPIRQGYGLTECASVVSL-QDAGDDDPSSVGRCLPHMTVRVADD--- 315
Cdd:cd05936 235 EFKKRDFSSLRLCISGGAPLPVEVAERfEELTGVPIVEGYGLTETSPVVAVnPLDGPRKPGSIGIPLPGTEVKIVDDdge 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 316 -------GEIILDGP-VCLG-----------AVGGEapgspLQTGDIGSIDSDGRLHIEGRKSNLIITSfGRNISPEWVE 376
Cdd:cd05936 315 elppgevGELWVRGPqVMKGywnrpeetaeaFVDGW-----LRTGDIGYMDEDGYFFIVDRKKDMIIVG-GFNVYPREVE 388
|
410
....*....|....*.
gi 2741210702 377 AALVEQPEVMQAMVYG 392
Cdd:cd05936 389 EVLYEHPAVAEAAVVG 404
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
18-406 |
1.10e-32 |
|
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: 132.34 E-value: 1.10e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 18 IALDALDGAPITYgalwAELGERSLAMMARF------ETDRaVALQSDHGAETSIVELALLRAKIPVLSLPAFFT-REQS 90
Cdd:cd05911 1 AQIDADTGKELTY----AQLRTLSRRLAAGLrklglkKGDV-VGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTaDELA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 91 RH---------------------AIALCGAD---------PDPIQSPSGTARSRRSAS---VPLPRG-----TARITFTS 132
Cdd:cd05911 76 HQlkiskpkviftdpdglekvkeAAKELGPKdkiivlddkPDGVLSIEDLLSPTLGEEdedLPPPLKdgkddTAAILYSS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 133 GSTGTPKGICLSADHMLTVAQSIVAAVGaEHAGRH---LALLPpgilLETVAGFFPTLLAG--GC--YVCPpqamigfad 205
Cdd:cd05911 156 GTTGLPKGVCLSHRNLIANLSQVQTFLY-GNDGSNdviLGFLP----LYHIYGLFTTLASLlnGAtvIIMP--------- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 206 pfRPDFVKAATIIAEQRITSLILVPEYLEGLVRVMETTGLRLPLLTLVAVGGARTSIPLMDR--ARRLGLPIRQGYGLTE 283
Cdd:cd05911 222 --KFDSELFLDLIEKYKITFLYLVPPIAAALAKSPLLDKYDLSSLRVILSGGAPLSKELQELlaKRFPNATIKQGYGMTE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 284 CASVVSLQDAGDDDPSSVGRCLPHMTVRVADD-----------GEIILDGP-VCLGAVGGEA-------PGSPLQTGDIG 344
Cdd:cd05911 300 TGGILTVNPDGDDKPGSVGRLLPNVEAKIVDDdgkdslgpnepGEICVRGPqVMKGYYNNPEatketfdEDGWLHTGDIG 379
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2741210702 345 SIDSDGRLHIEGRKSNLiITSFGRNISPEWVEAALVEQPEVMQAMVYG--DGLPT--PAALLVPSH 406
Cdd:cd05911 380 YFDEDGYLYIVDRKKEL-IKYKGFQVAPAELEAVLLEHPGVADAAVIGipDEVSGelPRAYVVRKP 444
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
117-405 |
5.73e-32 |
|
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: 130.28 E-value: 5.73e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 117 ASVPLPRGTARITFTSGSTGTPKGICLSADHMLTVAQSIVAAVGAEHAGRHLALLPPGILLETVAGFFPTLLAGgcyvcp 196
Cdd:cd05932 131 RPTRFPEQLATLIYTSGTTGQPKGVMLTFGSFAWAAQAGIEHIGTEENDRMLSYLPLAHVTERVFVEGGSLYGG------ 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 197 pqAMIGFA---DPFRPDFVKA-ATI------------------IAEQRITSLILVPeYLEGLVRVMETTGLRLPLLTLVA 254
Cdd:cd05932 205 --VLVAFAeslDTFVEDVQRArPTLffsvprlwtkfqqgvqdkIPQQKLNLLLKIP-VVNSLVKRKVLKGLGLDQCRLAG 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 255 VGGARTSIPLMDRARRLGLPIRQGYGLTECASVVSLQDAGDDDPSSVGRCLPHMTVRVADDGEIILDGPVCLGAVGGEAP 334
Cdd:cd05932 282 CGSAPVPPALLEWYRSLGLNILEAYGMTENFAYSHLNYPGRDKIGTVGNAGPGVEVRISEDGEILVRSPALMMGYYKDPE 361
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2741210702 335 GSP--------LQTGDIGSIDSDGRLHIEGRKSNLIITSFGRNISPEWVEAALVEQPEVMQAMVYGDGLPTPAALLVPS 405
Cdd:cd05932 362 ATAeaftadgfLRTGDKGELDADGNLTITGRVKDIFKTSKGKYVAPAPIENKLAEHDRVEMVCVIGSGLPAPLALVVLS 440
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
35-392 |
3.03e-31 |
|
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: 126.69 E-value: 3.03e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 35 AELGERSLAMMAR-----FETDRAVALQSDHGAETSIVELALLRAKIPVLslpaFFTREQSRHAIALCGADPDPIQSpsg 109
Cdd:cd05912 5 AELFEEVSRLAEHlaalgVRKGDRVALLSKNSIEMILLIHALWLLGAEAV----LLNTRLTPNELAFQLKDSDVKLD--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 110 tarsrrsasvplprGTARITFTSGSTGTPKGICLSADHMLTVAQSIVAAVGAEHAGRHLALLPpgilLETVAGFfPTLLA 189
Cdd:cd05912 78 --------------DIATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGLTEDDNWLCALP----LFHISGL-SILMR 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 190 GGCYVCPpqamIGFADPFRPDFVKaaTIIAEQRITSLILVPEYLEglvRVMETTGLRLPL-LTLVAVGGARTSIPLMDRA 268
Cdd:cd05912 139 SVIYGMT----VYLVDKFDAEQVL--HLINSGKVTIISVVPTMLQ---RLLEILGEGYPNnLRCILLGGGPAPKPLLEQC 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 269 RRLGLPIRQGYGLTECAS-VVSL--QDAgDDDPSSVGRCLPHMTVRVADD-------GEIILDGPVCLGAVGGEAPGSP- 337
Cdd:cd05912 210 KEKGIPVYQSYGMTETCSqIVTLspEDA-LNKIGSAGKPLFPVELKIEDDgqppyevGEILLKGPNVTKGYLNRPDATEe 288
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2741210702 338 ------LQTGDIGSIDSDGRLHIEGRKSNLIItSFGRNISPEWVEAALVEQPEVMQAMVYG 392
Cdd:cd05912 289 sfengwFKTGDIGYLDEEGFLYVLDRRSDLII-SGGENIYPAEIEEVLLSHPAIKEAGVVG 348
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
125-429 |
7.49e-29 |
|
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: 120.24 E-value: 7.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 125 TARITFTSGSTGTPKGICLSADHMLTVAQSIVAAVGAEHAGRHLALLPPGILLETVAGFFPTLLAGgcyvcppqAMIGFA 204
Cdd:cd05914 91 VALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLLGKGDKILSILPLHHIYPLTFTLLLPLLNG--------AHVVFL 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 205 DPFRPDFVKAatiIAEQRITSLILVPEYLEGL-VRVMET------TGLRLPL------------------------LTLV 253
Cdd:cd05914 163 DKIPSAKIIA---LAFAQVTPTLGVPVPLVIEkIFKMDIipkltlKKFKFKLakkinnrkirklafkkvheafggnIKEF 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 254 AVGGARTSIPLMDRARRLGLPIRQGYGLTECASVVSLQDAGDDDPSSVGRCLPHMTVRVAD------DGEIILDGP-VCL 326
Cdd:cd05914 240 VIGGAKINPDVEEFLRTIGFPYTIGYGMTETAPIISYSPPNRIRLGSAGKVIDGVEVRIDSpdpatgEGEIIVRGPnVMK 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 327 GAVGGEA-------PGSPLQTGDIGSIDSDGRLHIEGRKSNLIITSFGRNISPEWVEAALVEQPEVMQAMVY---GDG-- 394
Cdd:cd05914 320 GYYKNPEataeafdKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSSGKNIYPEEIEAKINNMPFVLESLVVvqeKKLva 399
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 2741210702 395 --LPTPA-----ALLVPSHPDADLAAAVARANEKLPAYAQIS 429
Cdd:cd05914 400 laYIDPDfldvkALKQRNIIDAIKWEVRDKVNQKVPNYKKIS 441
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
104-392 |
3.10e-28 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 119.19 E-value: 3.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 104 IQSPSGTARSRRSASVPlPRGTAR--ITFTSGSTGTPKGICLSADHMLTVAQSIVAAVGAEHAGRHLALLP----PGILL 177
Cdd:PRK06839 129 ITSLKEIEDRKIDNFVE-KNESASfiICYTSGTTGKPKGAVLTQENMFWNALNNTFAIDLTMHDRSIVLLPlfhiGGIGL 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 178 ETvagfFPTLLAGGCYVCPpqamigfaDPFRPDfvKAATIIAEQRITSLILVPEYLEGLVRVMETTGLRLPLLTLVAVGG 257
Cdd:PRK06839 208 FA----FPTLFAGGVIIVP--------RKFEPT--KALSMIEKHKVTVVMGVPTIHQALINCSKFETTNLQSVRWFYNGG 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 258 ARTSIPLMDRARRLGLPIRQGYGLTECASVVS--LQDAGDDDPSSVGRCLPHMTVRVADD----------GEIILDGPVC 325
Cdd:PRK06839 274 APCPEELMREFIDRGFLFGQGFGMTETSPTVFmlSEEDARRKVGSIGKPVLFCDYELIDEnknkvevgevGELLIRGPNV 353
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2741210702 326 LGAVGGEAPGSP-------LQTGDIGSIDSDGRLHIEGRKSNLIItSFGRNISPEWVEAALVEQPEVMQAMVYG 392
Cdd:PRK06839 354 MKEYWNRPDATEetiqdgwLCTGDLARVDEDGFVYIVGRKKEMII-SGGENIYPLEVEQVINKLSDVYEVAVVG 426
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
29-392 |
3.76e-28 |
|
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: 117.87 E-value: 3.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 29 TYGALwAELGERSLAMMA--RFETDRAVALQSDHGAETSIVELALLRAKIPVLSLPAFFTREQSRHAiaLCGADPDPIQS 106
Cdd:cd05903 3 TYSEL-DTRADRLAAGLAalGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFI--LRRAKAKVFVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 107 PSgtaRSRRSASVPLPRGTARITFTSGSTGTPKGICLSADHMLTVAQSIVAAVGAEHAGRHLALLPPGILLETVAGFFPT 186
Cdd:cd05903 80 PE---RFRQFDPAAMPDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPGDVFLVASPMAHQTGFVYGFTLP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 187 LLAGGCYVcppqamigFADPFRPDfvKAATIIAEQRITSLILVPEYLEGLVRVMETTGLRLPLLTLVAVGGARTSIPLMD 266
Cdd:cd05903 157 LLLGAPVV--------LQDIWDPD--KALALMREHGVTFMMGATPFLTDLLNAVEEAGEPLSRLRTFVCGGATVPRSLAR 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 267 RA-RRLGLPIRQGYGLTECASVVSLQDAGDDDPSSV--GRCLPHMTVRVADD----------GEIILDGP-VCLG----- 327
Cdd:cd05903 227 RAaELLGAKVCSAYGSTECPGAVTSITPAPEDRRLYtdGRPLPGVEIKVVDDtgatlapgveGELLSRGPsVFLGyldrp 306
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2741210702 328 -AVGGEAPGSPLQTGDIGSIDSDGRLHIEGRKSNLIITSfGRNISPEWVEAALVEQPEVMQAMVYG 392
Cdd:cd05903 307 dLTADAAPEGWFRTGDLARLDEDGYLRITGRSKDIIIRG-GENIPVLEVEDLLLGHPGVIEAAVVA 371
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
26-392 |
5.63e-28 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 119.13 E-value: 5.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 26 APITYgaLWAeLGERSLAMmarfETDRAVALQSDHGAETSIVELALLRakIPVLSLPAFFTREQSRHAIALCGA-DPDPI 104
Cdd:PLN02860 85 APLNY--RWS-FEEAKSAM----LLVRPVMLVTDETCSSWYEELQNDR--LPSLMWQVFLESPSSSVFIFLNSFlTTEML 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 105 QSPSGTARSRRSASVPlpRGTARITFTSGSTGTPKGICLSadHMLTVAQSI--VAAVGAEHAGRHLALLPpgilLETVAG 182
Cdd:PLN02860 156 KQRALGTTELDYAWAP--DDAVLICFTSGTTGRPKGVTIS--HSALIVQSLakIAIVGYGEDDVYLHTAP----LCHIGG 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 183 F---FPTLLAGGCYVcppqamigfadpFRPDFVKAATI--IAEQRITSLILVPEYLEGLVRVMETTGLR--LPLLTLVAV 255
Cdd:PLN02860 228 LssaLAMLMVGACHV------------LLPKFDAKAALqaIKQHNVTSMITVPAMMADLISLTRKSMTWkvFPSVRKILN 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 256 GGARTSIPLMDRARRLgLP---IRQGYGLTE-CASV--------------VSLQDAGDDDPSS--------VGRCLPHMT 309
Cdd:PLN02860 296 GGGSLSSRLLPDAKKL-FPnakLFSAYGMTEaCSSLtfmtlhdptlespkQTLQTVNQTKSSSvhqpqgvcVGKPAPHVE 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 310 VRVADD-----GEIILDGPVCLGAVGGEAPGSP--------LQTGDIGSIDSDGRLHIEGRkSNLIITSFGRNISPEWVE 376
Cdd:PLN02860 375 LKIGLDessrvGRILTRGPHVMLGYWGQNSETAsvlsndgwLDTGDIGWIDKAGNLWLIGR-SNDRIKTGGENVYPEEVE 453
|
410
....*....|....*.
gi 2741210702 377 AALVEQPEVMQAMVYG 392
Cdd:PLN02860 454 AVLSQHPGVASVVVVG 469
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
29-390 |
7.56e-28 |
|
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: 116.60 E-value: 7.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 29 TYGalwaELGERS------LAMMARFETDRAVALQSDHGAETSIVELALLRAK---IPV-LSLPA--------------F 84
Cdd:TIGR01733 1 TYR----ELDERAnrlarhLRAAGGVGPGDRVAVLLERSAELVVAILAVLKAGaayVPLdPAYPAerlafiledagarlL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 85 FTREQSRHAIA---LCGADPDPIQSPSGTARSR--RSASVPLPRGTARITFTSGSTGTPKGICLSADHMLTVAQSIVAAV 159
Cdd:TIGR01733 77 LTDSALASRLAglvLPVILLDPLELAALDDAPAppPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 160 GAEHAGRHLALLPPGILLeTVAGFFPTLLAGGCYVCPPQAMIgfadpfRPDFVKAATIIAEQRITSLILVPEYLEGLVRV 239
Cdd:TIGR01733 157 GLDPDDRVLQFASLSFDA-SVEEIFGALLAGATLVVPPEDEE------RDDAALLAALIAEHPVTVLNLTPSLLALLAAA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 240 METtglRLPLLTLVAVGGARTSIPLMDRARRLGLPIR--QGYGLTEC-----ASVVSLQDAGDDDPSSVGRCLPHMTVRV 312
Cdd:TIGR01733 230 LPP---ALASLRLVILGGEALTPALVDRWRARGPGARliNLYGPTETtvwstATLVDPDDAPRESPVPIGRPLANTRLYV 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 313 ADD----------GEIILDGP-VCLGAVGGEA---------PGSPLQ------TGDIGSIDSDGRLHIEGRKSNLI-ITs 365
Cdd:TIGR01733 307 LDDdlrpvpvgvvGELYIGGPgVARGYLNRPEltaerfvpdPFAGGDgarlyrTGDLVRYLPDGNLEFLGRIDDQVkIR- 385
|
410 420
....*....|....*....|....*
gi 2741210702 366 fGRNISPEWVEAALVEQPEVMQAMV 390
Cdd:TIGR01733 386 -GYRIELGEIEAALLRHPGVREAVV 409
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
15-425 |
7.91e-28 |
|
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: 116.86 E-value: 7.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 15 PQRIALDAlDGAPITYgalwAELGERSLAMmARF------ETDRAVALQSDHGAETSIVELALLRAK---IPV-LSLPA- 83
Cdd:cd05930 1 PDAVAVVD-GDQSLTY----AELDARANRL-ARYlrergvGPGDLVAVLLERSLEMVVAILAVLKAGaayVPLdPSYPAe 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 84 --FFTREQSRHAIALCGADpDPiqspsgtarsrrsasvplprgtARITFTSGSTGTPKGICLSadHmltvaQSIVAAVga 161
Cdd:cd05930 75 rlAYILEDSGAKLVLTDPD-DL----------------------AYVIYTSGSTGKPKGVMVE--H-----RGLVNLL-- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 162 EHAGRHLALLPPGILLET--------VAGFFPTLLAGGCYVCPPQAMIGfadpfrpDFVKAATIIAEQRITSLILVPEYL 233
Cdd:cd05930 123 LWMQEAYPLTPGDRVLQFtsfsfdvsVWEIFGALLAGATLVVLPEEVRK-------DPEALADLLAEEGITVLHLTPSLL 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 234 EGLVRVMETTglRLPLLTLVAVGGARTSIPLMDRARRLGLPIR--QGYGLTECASVVSLQ----DAGDDDPSSVGRCLPH 307
Cdd:cd05930 196 RLLLQELELA--ALPSLRLVLVGGEALPPDLVRRWRELLPGARlvNLYGPTEATVDATYYrvppDDEEDGRVPIGRPIPN 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 308 MTVRVADD----------GEIILDGP-VCLGAVGGEA------------PGSPL-QTGDIGSIDSDGRLHIEGRKSNLI- 362
Cdd:cd05930 274 TRVYVLDEnlrpvppgvpGELYIGGAgLARGYLNRPEltaerfvpnpfgPGERMyRTGDLVRWLPDGNLEFLGRIDDQVk 353
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2741210702 363 ITsfGRNISPEWVEAALVEQPEVMQAMV----YGDGLPTPAALLVPSHPDADLAAA-VARANEKLPAY 425
Cdd:cd05930 354 IR--GYRIELGEIEAALLAHPGVREAAVvareDGDGEKRLVAYVVPDEGGELDEEElRAHLAERLPDY 419
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
119-392 |
1.72e-25 |
|
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: 110.48 E-value: 1.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 119 VPLPRGTARITFTSGSTGTPKGICLSADHMLTVAQSIVAAVGAEHAGRHLALLP----PGIlletVAGFFPTLLAGGCYV 194
Cdd:cd05926 145 VPLPDDLALILHTSGTTGRPKGVPLTHRNLAASATNITNTYKLTPDDRTLVVMPlfhvHGL----VASLLSTLAAGGSVV 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 195 CPPqamiGF-ADPFRPDFVKAatiiaeqRITSLILVP---EYLegLVRVMETTGLRLPLLTLVAVGGARTSIPLMDRA-R 269
Cdd:cd05926 221 LPP----RFsASTFWPDVRDY-------NATWYTAVPtihQIL--LNRPEPNPESPPPKLRFIRSCSASLPPAVLEALeA 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 270 RLGLPIRQGYGLTECASVVSLQ--DAGDDDPSSVGRclPHMT-VRVADD----------GEIILDGP-VCLGAVGGEA-- 333
Cdd:cd05926 288 TFGAPVLEAYGMTEAAHQMTSNplPPGPRKPGSVGK--PVGVeVRILDEdgeilppgvvGEICLRGPnVTRGYLNNPEan 365
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2741210702 334 -----PGSPLQTGDIGSIDSDGRLHIEGRKSNLIITSfGRNISPEWVEAALVEQPEVMQAMVYG 392
Cdd:cd05926 366 aeaafKDGWFRTGDLGYLDADGYLFLTGRIKELINRG-GEKISPLEVDGVLLSHPAVLEAVAFG 428
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
122-408 |
3.32e-25 |
|
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: 109.73 E-value: 3.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 122 PRGTARITFTSGSTGTPKGICLSADHMLTVAQSIVAAVGAEHAGRHLALLPP----GIlleTVAGFFPtLLAGGCYVCPP 197
Cdd:cd05909 146 PDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPFfhsfGL---TGCLWLP-LLSGIKVVFHP 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 198 QAMigfadpfrpDFVKAATIIAEQRITSLILVPEYLEGLVRVMETTglRLPLLTLVAVGGARTSIPLMDRA-RRLGLPIR 276
Cdd:cd05909 222 NPL---------DYKKIPELIYDKKATILLGTPTFLRGYARAAHPE--DFSSLRLVVAGAEKLKDTLRQEFqEKFGIRIL 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 277 QGYGLTECASVVSLQDAG-DDDPSSVGRCLPHMTVR-----------VADDGEIILDGP-VCLGAVGGEAPGSPLQ---- 339
Cdd:cd05909 291 EGYGTTECSPVISVNTPQsPNKEGTVGRPLPGMEVKivsvetheevpIGEGGLLLVRGPnVMLGYLNEPELTSFAFgdgw 370
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2741210702 340 --TGDIGSIDSDGRLHIEGRKSNliitsFGRnISPEWVEAALVEQpevmqamVYGDGLPTPAALLVPSHPD 408
Cdd:cd05909 371 ydTGDIGKIDGEGFLTITGRLSR-----FAK-IAGEMVSLEAIED-------ILSEILPEDNEVAVVSVPD 428
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
125-392 |
1.06e-24 |
|
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: 105.66 E-value: 1.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 125 TARITFTSGSTGTPKGICLSADHMLTVAQSIVAAVGAEHAGRHLALLPPGILLETVAGFFPTLLAGGCYVcpPQAMIgfa 204
Cdd:cd17638 2 VSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIINPFFHTFGYKAGIVACLLTGATVV--PVAVF--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 205 dpfrpDFVKAATIIAEQRITSLILVPEYLEGLVRVMETTGLRLPLLTLVAVGGARTSIPLMDRAR-RLGL-PIRQGYGLT 282
Cdd:cd17638 77 -----DVDAILEAIERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVTGAATVPVELVRRMRsELGFeTVLTAYGLT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 283 ECAsVVSLQDAGDDD---PSSVGRCLPHMTVRVADDGEIILDGP-VCLGAVGGEAPGSP-------LQTGDIGSIDSDGR 351
Cdd:cd17638 152 EAG-VATMCRPGDDAetvATTCGRACPGFEVRIADDGEVLVRGYnVMQGYLDDPEATAEaidadgwLHTGDVGELDERGY 230
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2741210702 352 LHIEGRKSNLIITSfGRNISPEWVEAALVEQPEVMQAMVYG 392
Cdd:cd17638 231 LRITDRLKDMYIVG-GFNVYPAEVEGALAEHPGVAQVAVIG 270
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
125-407 |
1.33e-24 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 107.74 E-value: 1.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 125 TARITFTSGSTGTPKGIclsadhMLTVAQSIVAAVG-AEHAGRH-----LALLPpgilLETVAGFfPTLLAGGCYVCPPQ 198
Cdd:PRK03640 143 VATIMYTSGTTGKPKGV------IQTYGNHWWSAVGsALNLGLTeddcwLAAVP----IFHISGL-SILMRSVIYGMRVV 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 199 AMigfaDPFRPDFVKAAtiIAEQRITSLILVPEYLEGLVRVMETTG----LRLPLLtlvavGGARTSIPLMDRARRLGLP 274
Cdd:PRK03640 212 LV----EKFDAEKINKL--LQTGGVTIISVVSTMLQRLLERLGEGTypssFRCMLL-----GGGPAPKPLLEQCKEKGIP 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 275 IRQGYGLTECAS-VVSLqDAGD--DDPSSVGRCLPHMTVRVADD---------GEIILDGP-VCLGAVGGEAP------G 335
Cdd:PRK03640 281 VYQSYGMTETASqIVTL-SPEDalTKLGSAGKPLFPCELKIEKDgvvvppfeeGEIVVKGPnVTKGYLNREDAtretfqD 359
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2741210702 336 SPLQTGDIGSIDSDGRLHIEGRKSNLIItSFGRNISPEWVEAALVEQPEVMQAMVYGDGLPT----PAALLVPSHP 407
Cdd:PRK03640 360 GWFKTGDIGYLDEEGFLYVLDRRSDLII-SGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKwgqvPVAFVVKSGE 434
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
121-392 |
6.97e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 105.84 E-value: 6.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 121 LPRGTARITFTSGSTGTPKGICLSADHMLTVAQSIVAAVGAEHAGRHLALLPpgilLETVAG--FFPTLLAGGCYVcppq 198
Cdd:PRK06188 166 LPPDIAGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTP----LSHAGGafFLPTLLRGGTVI---- 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 199 amigFADPFRPDFVKAAtiIAEQRITSLILVPEYLEGLvrvMETTGLR---LPLLTLVAVGGARTS-IPLMDRARRLGLP 274
Cdd:PRK06188 238 ----VLAKFDPAEVLRA--IEEQRITATFLVPTMIYAL---LDHPDLRtrdLSSLETVYYGASPMSpVRLAEAIERFGPI 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 275 IRQGYGLTECASVVSLQDAGDDDP------SSVGRCLPHMTVRVADD----------GEIILDGPVCLG------AVGGE 332
Cdd:PRK06188 309 FAQYYGQTEAPMVITYLRKRDHDPddpkrlTSCGRPTPGLRVALLDEdgrevaqgevGEICVRGPLVMDgywnrpEETAE 388
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2741210702 333 A-PGSPLQTGDIGSIDSDGRLHIEGRKSNLIITSfGRNISPEWVEAALVEQPEVMQAMVYG 392
Cdd:PRK06188 389 AfRDGWLHTGDVAREDEDGFYYIVDRKKDMIVTG-GFNVFPREVEDVLAEHPAVAQVAVIG 448
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
122-407 |
1.01e-23 |
|
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: 105.37 E-value: 1.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 122 PRGTARITFTSGSTGTPKGICLSadHmltvaQSIVAAVGA------EHAG---RHLALLPPGILLETVAGFfpTLLAGGC 192
Cdd:cd17639 87 PDDLACIMYTSGSTGNPKGVMLT--H-----GNLVAGIAGlgdrvpELLGpddRYLAYLPLAHIFELAAEN--VCLYRGG 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 193 yvcppqaMIGFADP-----------------FRP----------DFVKAAtIIAE--------------------QRITS 225
Cdd:cd17639 158 -------TIGYGSPrtltdkskrgckgdlteFKPtlmvgvpaiwDTIRKG-VLAKlnpmgglkrtlfwtayqsklKALKE 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 226 LILVPeYLEGLV--RVMETTGLRLPLLTlvaVGGArtsiPLMDRARR----LGLPIRQGYGLTECASVVSLQDAGDDDPS 299
Cdd:cd17639 230 GPGTP-LLDELVfkKVRAALGGRLRYML---SGGA----PLSADTQEflniVLCPVIQGYGLTETCAGGTVQDPGDLETG 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 300 SVGRCLPHMTVRVAD-------------DGEIILDGP-VCLG-----AVGGEA--PGSPLQTGDIGSIDSDGRLHIEGRK 358
Cdd:cd17639 302 RVGPPLPCCEIKLVDweeggystdkpppRGEILIRGPnVFKGyyknpEKTKEAfdGDGWFHTGDIGEFHPDGTLKIIDRK 381
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 2741210702 359 SNLIITSFGRNISPEWVEAALVEQPEVMQAMVYGDGL-PTPAALLVPSHP 407
Cdd:cd17639 382 KDLVKLQNGEYIALEKLESIYRSNPLVNNICVYADPDkSYPVAIVVPNEK 431
|
|
| Haem_oxygenas_2 |
pfam14518 |
Iron-containing redox enzyme; The CADD, Chlamydia protein associating with death domains, ... |
501-663 |
1.11e-23 |
|
Iron-containing redox enzyme; The CADD, Chlamydia protein associating with death domains, crystal structure reveals a dimer of seven-helical bundles. Each bundle contains a di-iron centre adjacent to an internal cavity that forms an active site similar to that of methane mono-oxygenase hydrolase.
Pssm-ID: 434009 Cd Length: 178 Bit Score: 98.61 E-value: 1.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 501 LDYLEQAYHHVRHTVPLMQAARARLTDRaDIVAALDDYIAEETG-------HEEWILSDIAAAGGDAEAVRASKPGPATA 573
Cdd:pfam14518 1 REFLRQRYPYVLVFADWLALVIPRLPDG-RAKAALVENLWEELGdgdpernHVELFRRLLAALGLDPEYLEYLPELPETL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 574 AMVDHAYARIAN-GNAMAFFGMVYVLESVSVAFATRgAAAVAKKLGLPPQAFTYLTSHGALDQEHM-TFFANLVNGLDD- 650
Cdd:pfam14518 80 ALVNLMSLFGLHrRLRGALLGALAALELTSPPPALR-LAKGLRRLGLDDEALYYFDEHVEIDAAHAqMALEDVLEPLADe 158
|
170
....*....|....
gi 2741210702 651 -PADRDAILSMAQE 663
Cdd:pfam14518 159 ePELAQDVLFGARR 172
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
125-392 |
1.94e-23 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 104.60 E-value: 1.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 125 TARITFTSGSTGTPKGICLSADHMLTVAQSIVAAVGAEHAGRHLALLPpgilletvagFFPT----------LLAGGCYV 194
Cdd:PRK07656 168 VADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLAANP----------FFHVfgykagvnapLMRGATIL 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 195 CPPQamigfadpFRPDfvKAATIIAEQRITSLILVPEYLEGLVRVMETTGLRLPLLTLVAVGGArtSIP--LMDRAR-RL 271
Cdd:PRK07656 238 PLPV--------FDPD--EVFRLIETERITVLPGPPTMYNSLLQHPDRSAEDLSSLRLAVTGAA--SMPvaLLERFEsEL 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 272 GLP-IRQGYGLTECASVVSLQDAGDD---DPSSVGRCLPHMTVRVAD----------DGEIILDGP-VCLGAVGGEA--- 333
Cdd:PRK07656 306 GVDiVLTGYGLSEASGVTTFNRLDDDrktVAGTIGTAIAGVENKIVNelgeevpvgeVGELLVRGPnVMKGYYDDPEata 385
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2741210702 334 ----PGSPLQTGDIGSIDSDGRLHIEGRKSNLIITSfGRNISPEWVEAALVEQPEVMQAMVYG 392
Cdd:PRK07656 386 aaidADGWLHTGDLGRLDEEGYLYIVDRKKDMFIVG-GFNVYPAEVEEVLYEHPAVAEAAVIG 447
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
111-426 |
9.96e-23 |
|
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: 101.75 E-value: 9.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 111 ARSRRSASVPLPRGTARITFTSGSTGTPKGICLSADHMLTVAQSIVAAVGAEHAGRHLALLPpgilLETVAGFF---PTL 187
Cdd:cd05922 105 ARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADDRALTVLP----LSYDYGLSvlnTHL 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 188 LAGGCYVCPPQAMIGfadpfrPDFVKAatiIAEQRITSLILVPeYLEGLVRVMETTGLRLPLLTLVAVGGARTSIPLMDR 267
Cdd:cd05922 181 LRGATLVLTNDGVLD------DAFWED---LREHGATGLAGVP-STYAMLTRLGFDPAKLPSLRYLTQAGGRLPQETIAR 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 268 ARRL--GLPIRQGYGLTECASVVSLQDAG--DDDPSSVGRCLPHMTVRVADD----------GEIILDGPvcLGAVG--- 330
Cdd:cd05922 251 LRELlpGAQVYVMYGQTEATRRMTYLPPEriLEKPGSIGLAIPGGEFEILDDdgtptppgepGEIVHRGP--NVMKGywn 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 331 -------GEAPGSPLQTGDIGSIDSDGRLHIEGRKSNlIITSFGRNISPEWVEAALVEQPEVMQAMVYGDGLPTPA--AL 401
Cdd:cd05922 329 dppyrrkEGRGGGVLHTGDLARRDEDGFLFIVGRRDR-MIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDPLGEklAL 407
|
330 340
....*....|....*....|....*
gi 2741210702 402 LVPSHPDADLAAAVARANEKLPAYA 426
Cdd:cd05922 408 FVTAPDKIDPKDVLRSLAERLPPYK 432
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
125-392 |
1.78e-22 |
|
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: 100.49 E-value: 1.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 125 TARITFTSGSTGTPKGICLSADHMLTVAQSIVAAVGAEHAGRHLALLPPGILLETVAGFFPTLLAGGCYVcppqamIGFA 204
Cdd:cd05972 83 PALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGLRPDDIHWNIADPGWAKGAWSSFFGPWLLGATVF------VYEG 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 205 DPFRPDfvKAATIIAEQRITSLILVPEYLEGLVRVmETTGLRLPLLTLVAVGGARTSIPLMDRARR-LGLPIRQGYGLTE 283
Cdd:cd05972 157 PRFDAE--RILELLERYGVTSFCGPPTAYRMLIKQ-DLSSYKFSHLRLVVSAGEPLNPEVIEWWRAaTGLPIRDGYGQTE 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 284 CASVVSLQDAGDDDPSSVGRCLPHMTVRVADD----------GEIILD-GPVCL--GAVGGEAP------GSPLQTGDIG 344
Cdd:cd05972 234 TGLTVGNFPDMPVKPGSMGRPTPGYDVAIIDDdgrelppgeeGDIAIKlPPPGLflGYVGDPEKteasirGDYYLTGDRA 313
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2741210702 345 SIDSDGRLHIEGRKSNLIITSfGRNISPEWVEAALVEQPEVMQAMVYG 392
Cdd:cd05972 314 YRDEDGYFWFVGRADDIIKSS-GYRIGPFEVESALLEHPAVAEAAVVG 360
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
15-392 |
1.91e-22 |
|
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: 101.43 E-value: 1.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 15 PQRIAL-DALDGAPITYGALWAELgERSLAMMAR--FETDRAVALQSDHGAETSIVELALLRAK-IPVL--------SLP 82
Cdd:cd05923 15 PDACAIaDPARGLRLTYSELRARI-EAVAARLHArgLRPGQRVAVVLPNSVEAVIALLALHRLGaVPALinprlkaaELA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 83 AFFTREQSRHAIALCGADPDPIQSPSGTARSRRSASV----------------PLPRGTARITFTSGSTGTPKGICLSAD 146
Cdd:cd05923 94 ELIERGEMTAAVIAVDAQVMDAIFQSGVRVLALSDLVglgepesagpliedppREPEQPAFVFYTSGTTGLPKGAVIPQR 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 147 HMLTVAQSIVAAVGAEHaGRH---LALLPpgilLETVAGFFPTL---LAGGCYVCPPQAmigfadpFRPdfVKAATIIAE 220
Cdd:cd05923 174 AAESRVLFMSTQAGLRH-GRHnvvLGLMP----LYHVIGFFAVLvaaLALDGTYVVVEE-------FDP--ADALKLIEQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 221 QRITSLILVPEYLEGLVRVMETTGLRLPLLTLVAVGGARTSIPLMDRARR-LGLPIRQGYGLTECASVVSLQDAGdddPS 299
Cdd:cd05923 240 ERVTSLFATPTHLDALAAAAEFAGLKLSSLRHVTFAGATMPDAVLERVNQhLPGEKVNIYGTTEAMNSLYMRDAR---TG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 300 SVGRCLPHMTVRVA-------------DDGEIILDGPVCLGAVG----GEAPGSPLQ-----TGDIGSIDSDGRLHIEGR 357
Cdd:cd05923 317 TEMRPGFFSEVRIVriggspdealangEEGELIVAAAADAAFTGylnqPEATAKKLQdgwyrTGDVGYVDPSGDVRILGR 396
|
410 420 430
....*....|....*....|....*....|....*
gi 2741210702 358 KSNLIITSfGRNISPEWVEAALVEQPEVMQAMVYG 392
Cdd:cd05923 397 VDDMIISG-GENIHPSEIERVLSRHPGVTEVVVIG 430
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
125-404 |
3.13e-22 |
|
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: 101.06 E-value: 3.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 125 TARITFTSGSTGTPKGICLSadHMltvaqSIVAAVGAEHAGRHLALLPPGILLETVAGFFPtllAGGCYVCPPQAMIGFA 204
Cdd:cd17642 186 VALIMNSSGSTGLPKGVQLT--HK-----NIVARFSHARDPIFGNQIIPDTAILTVIPFHH---GFGMFTTLGYLICGFR 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 205 DPFRPDFVKAATIIAEQ--RITSLILVPEYLEGLVRVMETTGLRLPLLTLVAVGGARTSIPLMDR-ARRLGLP-IRQGYG 280
Cdd:cd17642 256 VVLMYKFEEELFLRSLQdyKVQSALLVPTLFAFFAKSTLVDKYDLSNLHEIASGGAPLSKEVGEAvAKRFKLPgIRQGYG 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 281 LTECASVVSLQDAGDDDPSSVGRCLPHMTVRVAD-----------DGEIILDGPVCL-GAVGGEAPGSP-------LQTG 341
Cdd:cd17642 336 LTETTSAILITPEGDDKPGAVGKVVPFFYAKVVDldtgktlgpneRGELCVKGPMIMkGYVNNPEATKAlidkdgwLHSG 415
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2741210702 342 DIGSIDSDGRLHIEGRKSNLIITSfGRNISPEWVEAALVEQPEVMQAMVYgdGLPTPAALLVP 404
Cdd:cd17642 416 DIAYYDEDGHFFIVDRLKSLIKYK-GYQVPPAELESILLQHPKIFDAGVA--GIPDEDAGELP 475
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
91-392 |
3.29e-22 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 100.65 E-value: 3.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 91 RHAIALCGADPDPIQSPSG---TARSRRSASVPLP----RGTARITFTSGSTGTPKGICLSADHMLTVAQSIVAAVGAEH 163
Cdd:PRK06187 128 RTVIVEGDGPAAPLAPEVGeyeELLAAASDTFDFPdideNDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSR 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 164 AGRHLALLPPGILLETVAGFFPTLlAGGCYVCPpqamigfaDPFRPDfvKAATIIAEQRITSLILVPEYLEGLVRVMETT 243
Cdd:PRK06187 208 DDVYLVIVPMFHVHAWGLPYLALM-AGAKQVIP--------RRFDPE--NLLDLIETERVTFFFAVPTIWQMLLKAPRAY 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 244 GLRLPLLTLVAVGGARTSIPLMDRAR-RLGLPIRQGYGLTECASVVSLQDAGDDDP------SSVGRCLPHMTVRVADD- 315
Cdd:PRK06187 277 FVDFSSLRLVIYGGAALPPALLREFKeKFGIDLVQGYGMTETSPVVSVLPPEDQLPgqwtkrRSAGRPLPGVEARIVDDd 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 316 -----------GEIILDGP-VCLGAVGGEAP------GSPLQTGDIGSIDSDGRLHIEGRKSNLIItSFGRNISPEWVEA 377
Cdd:PRK06187 357 gdelppdggevGEIIVRGPwLMQGYWNRPEAtaetidGGWLHTGDVGYIDEDGYLYITDRIKDVII-SGGENIYPRELED 435
|
330
....*....|....*
gi 2741210702 378 ALVEQPEVMQAMVYG 392
Cdd:PRK06187 436 ALYGHPAVAEVAVIG 450
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
15-441 |
8.03e-22 |
|
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: 98.86 E-value: 8.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 15 PQRIALDAlDGAPITYGALWaelgERSLAMMARF-----ETDRAVALQSDHGAETSIVELALLRAKIPVLSLPAFFTREQ 89
Cdd:cd05945 5 PDRPAVVE-GGRTLTYRELK----ERADALAAALaslglDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 90 SRHAIALCG-----ADPDPiqspsgtarsrrsasvplprgTARITFTSGSTGTPKGICLSADHMLTVAQSIVA------- 157
Cdd:cd05945 80 IREILDAAKpalliADGDD---------------------NAYIIFTSGSTGRPKGVQISHDNLVSFTNWMLSdfplgpg 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 158 AVGAEHAGRHLALlppgilleTVAGFFPTLLAGGCYVCPPQAMIG-FADPFRpdfvkaatIIAEQRITSLILVPEYLEGL 236
Cdd:cd05945 139 DVFLNQAPFSFDL--------SVMDLYPALASGATLVPVPRDATAdPKQLFR--------FLAEHGITVWVSTPSFAAMC 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 237 vrvmettgLRLPLLTLVAVGGARTSI----PL-MDRARRL-----GLPIRQGYGLTEC-----ASVVSLQDAGDDDPSSV 301
Cdd:cd05945 203 --------LLSPTFTPESLPSLRHFLfcgeVLpHKTARALqqrfpDARIYNTYGPTEAtvavtYIEVTPEVLDGYDRLPI 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 302 GRCLPHMTVRVADD----------GEIILDGP-VCLGAVG-GEAPGSPL---------QTGDIGSIDSDGRLHIEGRKSN 360
Cdd:cd05945 275 GYAKPGAKLVILDEdgrpvppgekGELVISGPsVSKGYLNnPEKTAAAFfpdegqrayRTGDLVRLEADGLLFYRGRLDF 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 361 LIITSfGRNISPEWVEAALVEQPEVMQAMVY----GDGLPTPAALLVPSHPDADLAAAVARA--NEKLPAYAQISAWREA 434
Cdd:cd05945 355 QVKLN-GYRIELEEIEAALRQVPGVKEAVVVpkykGEKVTELIAFVVPKPGAEAGLTKAIKAelAERLPPYMIPRRFVYL 433
|
....*..
gi 2741210702 435 AHFtPMN 441
Cdd:cd05945 434 DEL-PLN 439
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
204-431 |
1.51e-21 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 98.14 E-value: 1.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 204 ADPFRPDFVkaatiiaeqritsLILVPEYLEglvRVMETTGLRLPLLTLVAVGGARTSIPLMDRARRLGLPIRQGYGLTE 283
Cdd:PRK07445 202 LPPNPSDFF-------------LSLVPTQLQ---RLLQLRPQWLAQFRTILLGGAPAWPSLLEQARQLQLRLAPTYGMTE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 284 CAS-VVSL--QD--AGDDdpsSVGRCLPH--MTVRVADDGEIILDGP-VCLGAVGG-EAPGSPLQTGDIGSIDSDGRLHI 354
Cdd:PRK07445 266 TASqIATLkpDDflAGNN---SSGQVLPHaqITIPANQTGNITIQAQsLALGYYPQiLDSQGIFETDDLGYLDAQGYLHI 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 355 EGRKSNLIITSfGRNISPEWVEAALVEQPEVMQAMVYgdGLPTP------AALLVPSHPDADLAAAVARANEKLPAYAQI 428
Cdd:PRK07445 343 LGRNSQKIITG-GENVYPAEVEAAILATGLVQDVCVL--GLPDPhwgevvTAIYVPKDPSISLEELKTAIKDQLSPFKQP 419
|
...
gi 2741210702 429 SAW 431
Cdd:PRK07445 420 KHW 422
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
16-405 |
1.78e-21 |
|
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: 97.75 E-value: 1.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 16 QRIALDAlDGAPITYGALWAELG---ERSLAMMARFETDRaVALQSDHGAETSIVELALLRAKIPVLSLPAFFTREQSRH 92
Cdd:cd05941 1 DRIAIVD-DGDSITYADLVARAArlaNRLLALGKDLRGDR-VAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 93 AIAlcgaDPDPiqspsgtarsrrsaSVPLPRgtARITFTSGSTGTPKGICLSADHMLTVAQSIVAAVGAEHAGRHLALLP 172
Cdd:cd05941 79 VIT----DSEP--------------SLVLDP--ALILYTSGTTGRPKGVVLTHANLAANVRALVDAWRWTEDDVLLHVLP 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 173 pgilLETVAGFF----PTLLAGGCYVcppqamigfadpFRPDF--VKAATIIAEQRITSLILVP-------EYLEGLVRV 239
Cdd:cd05941 139 ----LHHVHGLVnallCPLFAGASVE------------FLPKFdpKEVAISRLMPSITVFMGVPtiytrllQYYEAHFTD 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 240 METT------GLRLplltLVAvGGARTSIPLMDR-ARRLGLPIRQGYGLTECASVVSLQDAGDDDPSSVGRCLPHMTVRV 312
Cdd:cd05941 203 PQFAraaaaeRLRL----MVS-GSAALPVPTLEEwEAITGHTLLERYGMTEIGMALSNPLDGERRPGTVGMPLPGVQARI 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 313 ADD-----------GEIILDGP-VCLG-----AVGGEA--PGSPLQTGDIGSIDSDGRLHIEGRKSNLIITSFGRNISPE 373
Cdd:cd05941 278 VDEetgeplprgevGEIQVRGPsVFKEywnkpEATKEEftDDGWFKTGDLGVVDEDGYYWILGRSSVDIIKSGGYKVSAL 357
|
410 420 430
....*....|....*....|....*....|....*.
gi 2741210702 374 WVEAALVEQPEVMQAMVYGDGLPT----PAALLVPS 405
Cdd:cd05941 358 EIERVLLAHPGVSECAVIGVPDPDwgerVVAVVVLR 393
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
128-392 |
3.60e-21 |
|
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: 95.03 E-value: 3.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 128 ITFTSGSTGTPKGICLSADHMLTVAQSIVAAVGAEHAGRHLALLPpgilLETVAGF---FPTLLAGGCYVcppqamigFA 204
Cdd:cd17637 5 IIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLP----LFHIAGLnlaLATFHAGGANV--------VM 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 205 DPFRPDfvKAATIIAEQRITSLILVPEYLEGLVRVMETTGLRLPLLTLVavggarTSIPLMDRARRL----GLPIRQGYG 280
Cdd:cd17637 73 EKFDPA--EALELIEEEKVTLMGSFPPILSNLLDAAEKSGVDLSSLRHV------LGLDAPETIQRFeettGATFWSLYG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 281 LTECASVVSLQDAgDDDPSSVGRCLPHMTVRVADDgeiiLDGPVCLGAVGGEAPGSPL---------------------Q 339
Cdd:cd17637 145 QTETSGLVTLSPY-RERPGSAGRPGPLVRVRIVDD----NDRPVPAGETGEIVVRGPLvfqgywnlpeltaytfrngwhH 219
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2741210702 340 TGDIGSIDSDGRLHIEGRKSNL-IITSFGRNISPEWVEAALVEQPEVMQAMVYG 392
Cdd:cd17637 220 TGDLGRFDEDGYLWYAGRKPEKeLIKPGGENVYPAEVEKVILEHPAIAEVCVIG 273
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
14-390 |
4.42e-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: 97.03 E-value: 4.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 14 DPQRIALdALDGAPITYgalwAELGERSLAMMARFET-----DRAVALQSDHGAETSIVELALLRAKIPVLSLPAFFTRE 88
Cdd:cd17651 8 TPDAPAL-VAEGRRLTY----AELDRRANRLAHRLRArgvgpGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 89 QSRHAIALCG------------------ADPDPIQSPSGTARSRRSASVPL-PRGTARITFTSGSTGTPKGICLSADHML 149
Cdd:cd17651 83 RLAFMLADAGpvlvlthpalagelavelVAVTLLDQPGAAAGADAEPDPALdADDLAYVIYTSGSTGRPKGVVMPHRSLA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 150 TVAQSIVAAVGAEHAGRHLALLPPGI---LLETvagfFPTLLAGGCYVCPPqamigfaDPFRPDFVKAATIIAEQRITSL 226
Cdd:cd17651 163 NLVAWQARASSLGPGARTLQFAGLGFdvsVQEI----FSTLCAGATLVLPP-------EEVRTDPPALAAWLDEQRISRV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 227 ILVPEYLEGLVRVMETTGLRLPLLTLVAVGGARTSI-PLMDR--ARRLGLPIRQGYGLTECASVVSLQDAGD----DDPS 299
Cdd:cd17651 232 FLPTVALRALAEHGRPLGVRLAALRYLLTGGEQLVLtEDLREfcAGLPGLRLHNHYGPTETHVVTALSLPGDpaawPAPP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 300 SVGRCLPHMTVRVADDGeiilDGPVCLGAVG-------GEAPG-----------------SPLQ----TGDIGSIDSDGR 351
Cdd:cd17651 312 PIGRPIDNTRVYVLDAA----LRPVPPGVPGelyiggaGLARGylnrpeltaerfvpdpfVPGArmyrTGDLARWLPDGE 387
|
410 420 430
....*....|....*....|....*....|....*....
gi 2741210702 352 LHIEGRKSNLIITSfGRNISPEWVEAALVEQPEVMQAMV 390
Cdd:cd17651 388 LEFLGRADDQVKIR-GFRIELGEIEAALARHPGVREAVV 425
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
15-426 |
4.49e-21 |
|
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: 96.61 E-value: 4.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 15 PQRIALDALDGApITYGalwaELGERSLAMMARF-----ETDRAVALQSDHGAETSIVELALLRAkipvlslpafftreq 89
Cdd:cd17653 11 PDAVAVESLGGS-LTYG----ELDAASNALANRLlqlgvVPGDVVPLLSDRSLEMLVAILAILKA--------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 90 srHAiALCGADP----DPIQSPSGTARSRRSASVPLPRGTARITFTSGSTGTPKGICLSADHMLTVAQSIVAAVGAEHAG 165
Cdd:cd17653 71 --GA-AYVPLDAklpsARIQAILRTSGATLLLTTDSPDDLAYIIFTSGSTGIPKGVMVPHRGVLNYVSQPPARLDVGPGS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 166 RHLALLPPG---ILLEtvagFFPTLLAGGCYVcppqamigFADPFRPDFVKAATiiaeqrITSLILVPEYLEGLVRVmet 242
Cdd:cd17653 148 RVAQVLSIAfdaCIGE----IFSTLCNGGTLV--------LADPSDPFAHVART------VDALMSTPSILSTLSPQ--- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 243 tglRLPLLTLVAVGGARTSIPLMDRArRLGLPIRQGYGLTECASVVSLQDAGDDDPSSVGRCLPHMTVRVAD-------- 314
Cdd:cd17653 207 ---DFPNLKTIFLGGEAVPPSLLDRW-SPGRRLYNAYGPTECTISSTMTELLPGQPVTIGKPIPNSTCYILDadlqpvpe 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 315 --DGEIILDGP-VCLGAVGGEA------------PGSPL-QTGDIGSIDSDGRLHIEGRKSNLI-ITSFGRNIsPEWVEA 377
Cdd:cd17653 283 gvVGEICISGVqVARGYLGNPAltaskfvpdpfwPGSRMyRTGDYGRWTEDGGLEFLGREDNQVkVRGFRINL-EEIEEV 361
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 2741210702 378 ALVEQPEVMQ--AMVYGDGLptpAALLVPSHPDADLAAAVARanEKLPAYA 426
Cdd:cd17653 362 VLQSQPEVTQaaAIVVNGRL---VAFVTPETVDVDGLRSELA--KHLPSYA 407
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
66-392 |
4.95e-21 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 97.72 E-value: 4.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 66 IVELALLRAKIPVLSLPAFFTREQSRHAI----ALCGADPDPiqspsgtarSRRSASVPLPRGTARITFTSGSTGTPKGI 141
Cdd:PRK07529 161 VVEVDLARYLPGPKRLAVPLIRRKAHARIldfdAELARQPGD---------RLFSGRPIGPDDVAAYFHTGGTTGMPKLA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 142 CLSADHMLTVAQSIVAAVGAEHAGRHLALLPpgilLETVAGFFPTLLA----GGCYVCPPQAmiGFADP-FRPDFVKaat 216
Cdd:PRK07529 232 QHTHGNEVANAWLGALLLGLGPGDTVFCGLP----LFHVNALLVTGLAplarGAHVVLATPQ--GYRGPgVIANFWK--- 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 217 IIAEQRITSLILVPEYLEGLVRVmETTGLRLPLLTLVAVGGARTSIPLMDR-ARRLGLPIRQGYGLTECASVVSLQDA-G 294
Cdd:PRK07529 303 IVERYRINFLSGVPTVYAALLQV-PVDGHDISSLRYALCGAAPLPVEVFRRfEAATGVRIVEGYGLTEATCVSSVNPPdG 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 295 DDDPSSVGRCLPHMTVRVA---------------DDGEIILDGP-VCLGAVGGEAPGSP------LQTGDIGSIDSDGRL 352
Cdd:PRK07529 382 ERRIGSVGLRLPYQRVRVVilddagrylrdcavdEVGVLCIAGPnVFSGYLEAAHNKGLwledgwLNTGDLGRIDADGYF 461
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 2741210702 353 HIEGRKSNLIITSfGRNISPEWVEAALVEQPEVMQAMVYG 392
Cdd:PRK07529 462 WLTGRAKDLIIRG-GHNIDPAAIEEALLRHPAVALAAAVG 500
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
28-404 |
1.07e-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: 95.50 E-value: 1.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 28 ITYGALWAEL-----GERSLAMMArfetDRAVALQSDHGAETSIVELALLRAkipvlslpafftreqsrhaialcGAdpd 102
Cdd:cd17640 6 ITYKDLYQEIldfaaGLRSLGVKA----GEKVALFADNSPRWLIADQGIMAL-----------------------GA--- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 103 pIQSPSGTARS--------RRSASVPL-----PRGTARITFTSGSTGTPKGICLSADHMLTVAQSIVAAVGAEHAGRHLA 169
Cdd:cd17640 56 -VDVVRGSDSSveellyilNHSESVALvvendSDDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQPGDRFLS 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 170 LLPPGILLETVAGFFptLLAGGC---YVCPPQAMIGFADpFRPDFvkaatiiaeqritsLILVPEYLEGL-------VRV 239
Cdd:cd17640 135 ILPIWHSYERSAEYF--IFACGCsqaYTSIRTLKDDLKR-VKPHY--------------IVSVPRLWESLysgiqkqVSK 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 240 METTGLRLPLLTL------VAVGGARTSIPLMDR-ARRLGLPIRQGYGLTECASVVSLQDAGDDDPSSVGRCLPHMTVRV 312
Cdd:cd17640 198 SSPIKQFLFLFFLsggifkFGISGGGALPPHVDTfFEAIGIEVLNGYGLTETSPVVSARRLKCNVRGSVGRPLPGTEIKI 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 313 AD-----------DGEIILDGP-VCLG-----AVGGEAPGSP--LQTGDIGSIDSDGRLHIEGRKSNLIITSFGRNISPE 373
Cdd:cd17640 278 VDpegnvvlppgeKGIVWVRGPqVMKGyyknpEATSKVLDSDgwFNTGDLGWLTCGGELVLTGRAKDTIVLSNGENVEPQ 357
|
410 420 430
....*....|....*....|....*....|.
gi 2741210702 374 WVEAALVEQPEVMQAMVYGDGLPTPAALLVP 404
Cdd:cd17640 358 PIEEALMRSPFIEQIMVVGQDQKRLGALIVP 388
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
14-390 |
1.20e-20 |
|
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: 95.76 E-value: 1.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 14 DPQRIAL-DALDGAPITYGALWaelgeRSLAMMARFETDR------AVALQSDHGAETSIVELALLRAKIPVLSLPAFFT 86
Cdd:cd05904 18 HPSRPALiDAATGRALTYAELE-----RRVRRLAAGLAKRggrkgdVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLST 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 87 REQSRHAIALCGA-----------------------DPDPIQSPSGTARSRRSASVPLPR------GTARITFTSGSTGT 137
Cdd:cd05904 93 PAEIAKQVKDSGAklafttaelaeklaslalpvvllDSAEFDSLSFSDLLFEADEAEPPVvvikqdDVAALLYSSGTTGR 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 138 PKGICLSADHMLTVAQSIVAAVG--AEHAGRHLALLPP----GILLETVAgffpTLLAGGCYVcppqAMIGFadpfrpDF 211
Cdd:cd05904 173 SKGVMLTHRNLIAMVAQFVAGEGsnSDSEDVFLCVLPMfhiyGLSSFALG----LLRLGATVV----VMPRF------DL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 212 VKAATIIAEQRITSLILVPEYLEGLVRVMETTGLRLPLLTLVAVGGARTSIPLMDR-ARRL-GLPIRQGYGLTE---CAS 286
Cdd:cd05904 239 EELLAAIERYKVTHLPVVPPIVLALVKSPIVDKYDLSSLRQIMSGAAPLGKELIEAfRAKFpNVDLGQGYGMTEstgVVA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 287 VVSLQDAGDDDPSSVGRCLPHMTVRVAD-----------DGEIILDGPVCL-GAVGGEA-------PGSPLQTGDIGSID 347
Cdd:cd05904 319 MCFAPEKDRAKYGSVGRLVPNVEAKIVDpetgeslppnqTGELWIRGPSIMkGYLNNPEataatidKEGWLHTGDLCYID 398
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 2741210702 348 SDGRLHIEGRKSNLIITSfGRNISPEWVEAALVEQPEVMQAMV 390
Cdd:cd05904 399 EDGYLFIVDRLKELIKYK-GFQVAPAELEALLLSHPEILDAAV 440
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
131-404 |
1.56e-20 |
|
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: 93.70 E-value: 1.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 131 TSGSTGTPKgiclsadhmlTVAQSIVAAVGAEHAGRHLALLPP------GILLETVAGFFPTLLA----GGCYVCPPQAm 200
Cdd:cd05944 10 TGGTTGTPK----------LAQHTHSNEVYNAWMLALNSLFDPddvllcGLPLFHVNGSVVTLLTplasGAHVVLAGPA- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 201 iGFADP-FRPDFVKaatIIAEQRITSLILVPEYLEGLVRVmeTTGLRLPLLTLVAVGGArtSIPLMDRAR---RLGLPIR 276
Cdd:cd05944 79 -GYRNPgLFDNFWK---LVERYRITSLSTVPTVYAALLQV--PVNADISSLRFAMSGAA--PLPVELRARfedATGLPVV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 277 QGYGLTECASVVSLQ-DAGDDDPSSVGRCLPHMTVRVA---DDGEIILD------GPVCL-------------GAVGGEA 333
Cdd:cd05944 151 EGYGLTEATCLVAVNpPDGPKRPGSVGLRLPYARVRIKvldGVGRLLRDcapdevGEICVagpgvfggylyteGNKNAFV 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2741210702 334 PGSPLQTGDIGSIDSDGRLHIEGRKSNLIITSfGRNISPEWVEAALVEQPEVMQAMVYGDglPTPAALLVP 404
Cdd:cd05944 231 ADGWLNTGDLGRLDADGYLFITGRAKDLIIRG-GHNIDPALIEEALLRHPAVAFAGAVGQ--PDAHAGELP 298
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
122-402 |
2.17e-20 |
|
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341296 [Multi-domain] Cd Length: 569 Bit Score: 95.57 E-value: 2.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 122 PRGTARITFTSGSTGTPKGICLSADHMLTVAQSIVAAVGAEHAGRHLALLPPGILLETVAGFFPTLLAGGCYVCPPQAMI 201
Cdd:cd17641 157 GEDVAVLCTTSGTTGKPKLAMLSHGNFLGHCAAYLAADPLGPGDEYVSVLPLPWIGEQMYSVGQALVCGFIVNFPEEPET 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 202 GFAD--PFRPDFVKAATIIAEQRITSL------------ILVPEYLEGLVRVMET--------TGLRL-----------P 248
Cdd:cd17641 237 MMEDlrEIGPTFVLLPPRVWEGIAADVrarmmdatpfkrFMFELGMKLGLRALDRgkrgrpvsLWLRLaswladallfrP 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 249 L--------LTLVAVGGARTSIPLMDRARRLGLPIRQGYGLTECASVVSLQDAGDDDPSSVGRCLPHMTVRVADDGEIIL 320
Cdd:cd17641 317 LrdrlgfsrLRSAATGGAALGPDTFRFFHAIGVPLKQLYGQTELAGAYTVHRDGDVDPDTVGVPFPGTEVRIDEVGEILV 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 321 DGP-VCLGAVG-GEAPGSP------LQTGDIGSIDSDGRLHIEGRKSNLIITSFGRNISPEWVEAALVEQPEVMQAMVYG 392
Cdd:cd17641 397 RSPgVFVGYYKnPEATAEDfdedgwLHTGDAGYFKENGHLVVIDRAKDVGTTSDGTRFSPQFIENKLKFSPYIAEAVVLG 476
|
330
....*....|
gi 2741210702 393 DGLPTPAALL 402
Cdd:cd17641 477 AGRPYLTAFI 486
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
120-408 |
1.62e-19 |
|
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: 92.66 E-value: 1.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 120 PLPRGTARITFTSGSTGTPKGIclsadhMLTVAQSIVAAVGAEHAG----------RHLALLPPGILLETVAGFFpTLLA 189
Cdd:cd05927 111 PKPEDLATICYTSGTTGNPKGV------MLTHGNIVSNVAGVFKILeilnkinptdVYISYLPLAHIFERVVEAL-FLYH 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 190 GGCyvcppqamIGFadpFRPDFVKAATIIAEQRITSLILVPEYLE--------------GLVRVM-------------ET 242
Cdd:cd05927 184 GAK--------IGF---YSGDIRLLLDDIKALKPTVFPGVPRVLNriydkifnkvqakgPLKRKLfnfalnyklaelrSG 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 243 TGLRLPL----------------LTLVAVGGARTSIPLMDRARR-LGLPIRQGYGLTECASVVSLQDAGDDDPSSVGRCL 305
Cdd:cd05927 253 VVRASPFwdklvfnkikqalggnVRLMLTGSAPLSPEVLEFLRVaLGCPVLEGYGQTECTAGATLTLPGDTSVGHVGGPL 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 306 PHMTVRVAD-------------DGEIILDGP-VCLG----------AVGGEApgsPLQTGDIGSIDSDGRLHIEGRKSNL 361
Cdd:cd05927 333 PCAEVKLVDvpemnydakdpnpRGEVCIRGPnVFSGyykdpektaeALDEDG---WLHTGDIGEWLPNGTLKIIDRKKNI 409
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 2741210702 362 IITSFGRNISPEWVEAALVEQPEVMQAMVYGDGL-PTPAALLVPsHPD 408
Cdd:cd05927 410 FKLSQGEYVAPEKIENIYARSPFVAQIFVYGDSLkSFLVAIVVP-DPD 456
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
15-390 |
2.36e-19 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 91.47 E-value: 2.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 15 PQRIALdALDGAPITygalWAELGERSLAMMARF-----ETDRAVALQSDHGAETSIVELALLRAKIPVLSL-PAFFTRE 88
Cdd:PRK09029 17 PQAIAL-RLNDEVLT----WQQLCARIDQLAAGFaqqgvVEGSGVALRGKNSPETLLAYLALLQCGARVLPLnPQLPQPL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 89 QS--------RHAIALCGAD-PDPIQSPSGTARSRRSASVPLPRGTARITFTSGSTGTPKGICLSADHMLTVAQSIVAAV 159
Cdd:PRK09029 92 LEellpsltlDFALVLEGENtFSALTSLHLQLVEGAHAVAWQPQRLATMTLTSGSTGLPKAAVHTAQAHLASAEGVLSLM 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 160 GAEHAGRHLALLPpgilLETVAG---FFPTLLAGGCYVCPPQAmigfadPFRPDFVKAatiiaeqriTSLILVPEYLEgl 236
Cdd:PRK09029 172 PFTAQDSWLLSLP----LFHVSGqgiVWRWLYAGATLVVRDKQ------PLEQALAGC---------THASLVPTQLW-- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 237 vRVMETTGLRLpLLTLVAVGGArtSIP--LMDRARRLGlpIRQ--GYGLTECASVVSLQDAgdDDPSSVGRCLPHMTVRV 312
Cdd:PRK09029 231 -RLLDNRSEPL-SLKAVLLGGA--AIPveLTEQAEQQG--IRCwcGYGLTEMASTVCAKRA--DGLAGVGSPLPGREVKL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 313 ADDgEIILDGPvCLgAVG----GEApgSPL-------QTGDIGSIDsDGRLHIEGRKSNLIItSFGRNISPEWVEAALVE 381
Cdd:PRK09029 303 VDG-EIWLRGA-SL-ALGywrqGQL--VPLvndegwfATRDRGEWQ-NGELTILGRLDNLFF-SGGEGIQPEEIERVINQ 375
|
....*....
gi 2741210702 382 QPEVMQAMV 390
Cdd:PRK09029 376 HPLVQQVFV 384
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
122-444 |
2.81e-19 |
|
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: 91.28 E-value: 2.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 122 PRGTARITFTSGSTGTPKGICLSADHMLTVAQSIVAAVGAEHAGRHLALLPPG--ILLEtvaGFFPTLLAGGCYVCPPQA 199
Cdd:cd17649 93 PRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAERYGLTPGDRELQFASFNfdGAHE---QLLPPLICGACVVLRPDE 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 200 MIGFADPFrpdfvkaATIIAEQRITSLILVPEYLEGLVRVMETTGLRLPL-LTLVAVGGARTSIPLMDRARRLGLPIRQG 278
Cdd:cd17649 170 LWASADEL-------AEMVRELGVTVLDLPPAYLQQLAEEADRTGDGRPPsLRLYIFGGEALSPELLRRWLKAPVRLFNA 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 279 YGLTEcASVVSL-----QDAGDDDPSS-VGRCLPHMTVRVAD-DGEIILDGPVCLGAVGGE------------------- 332
Cdd:cd17649 243 YGPTE-ATVTPLvwkceAGAARAGASMpIGRPLGGRSAYILDaDLNPVPVGVTGELYIGGEglargylgrpeltaerfvp 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 333 ----APGSPL-QTGDIGSIDSDGRLHIEGRKSNLI-ITSFgrNISPEWVEAALVEQPEVMQAMVY---GDGLPTPAALLV 403
Cdd:cd17649 322 dpfgAPGSRLyRTGDLARWRDDGVIEYLGRVDHQVkIRGF--RIELGEIEAALLEHPGVREAAVValdGAGGKQLVAYVV 399
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 2741210702 404 PSHPDADLAAAVARAN---EKLPAYAQISAWREAAHF--TPmNGQL 444
Cdd:cd17649 400 LRAAAAQPELRAQLRTalrASLPDYMVPAHLVFLARLplTP-NGKL 444
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
15-433 |
4.05e-19 |
|
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: 90.80 E-value: 4.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 15 PQRIALdALDGAPITYgalwAELGERSLAMMARF-----ETDRAVALQSDHGAETSIVELALLRAKIPVLSL----PA-- 83
Cdd:cd17646 12 PDAPAV-VDEGRTLTY----RELDERANRLAHLLrargvGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLdpgyPAdr 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 84 ------------FFTREQSRHAIALCGADPDPIQSPSGTARSRRSASVPLPRGTARITFTSGSTGTPKGICLSADHMLTV 151
Cdd:cd17646 87 laymladagpavVLTTADLAARLPAGGDVALLGDEALAAPPATPPLVPPRPDNLAYVIYTSGSTGRPKGVMVTHAGIVNR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 152 AQSIVAAVGAEHAGRHLALLPPGILLeTVAGFFPTLLAGGCYVCPPQAmiGFADPfrpdfVKAATIIAEQRITSLILVPE 231
Cdd:cd17646 167 LLWMQDEYPLGPGDRVLQKTPLSFDV-SVWELFWPLVAGARLVVARPG--GHRDP-----AYLAALIREHGVTTCHFVPS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 232 YLEGLVRvmETTGLRLPLLTLVAVGGARTSIPLMDR-ARRLGLPIRQGYGLTECA-SVVSLQDAGDDDPSSV--GRCLPH 307
Cdd:cd17646 239 MLRVFLA--EPAAGSCASLRRVFCSGEALPPELAARfLALPGAELHNLYGPTEAAiDVTHWPVRGPAETPSVpiGRPVPN 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 308 MTVRVADD----------GEIILDG-PVCLGAVGGEA------------PGSPL-QTGDIGSIDSDGRLHIEGRKSNLII 363
Cdd:cd17646 317 TRLYVLDDalrpvpvgvpGELYLGGvQLARGYLGRPAltaerfvpdpfgPGSRMyRTGDLARWRPDGALEFLGRSDDQVK 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2741210702 364 TSfGRNISPEWVEAALVEQPEVMQAMVYGDGLPTPAALLV------PSHPDADLAAAVARANEKLPAYAQISAWRE 433
Cdd:cd17646 397 IR-GFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVgyvvpaAGAAGPDTAALRAHLAERLPEYMVPAAFVV 471
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
117-407 |
4.64e-19 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 91.72 E-value: 4.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 117 ASVPLPRGTARITFTSGSTGTPKGICLSADHMLTVAQSIVAAV-GAEHAGRHLALLPPGILLETVAGffPTLLAGGCyvc 195
Cdd:PLN02387 244 PDLPSPNDIAVIMYTSGSTGLPKGVMMTHGNIVATVAGVMTVVpKLGKNDVYLAYLPLAHILELAAE--SVMAAVGA--- 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 196 ppqaMIGFADPFR----PDFVKAATI--IAEQRITSLILVPEYL----EGLVRVMETTG--------------------- 244
Cdd:PLN02387 319 ----AIGYGSPLTltdtSNKIKKGTKgdASALKPTLMTAVPAILdrvrDGVRKKVDAKGglakklfdiaykrrlaaiegs 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 245 -------------------LRLPL---LTLVAVGGArtsiPLMDRARR-----LGLPIRQGYGLTE-CASVVSLQDagdD 296
Cdd:PLN02387 395 wfgawglekllwdalvfkkIRAVLggrIRFMLSGGA----PLSGDTQRfinicLGAPIGQGYGLTEtCAGATFSEW---D 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 297 DPSsVGRC---LPHMTV----------RVADD----GEIILDGP-VCLGAVGGEAPGSP-----------LQTGDIGSID 347
Cdd:PLN02387 468 DTS-VGRVgppLPCCYVklvsweeggyLISDKpmprGEIVIGGPsVTLGYFKNQEKTDEvykvdergmrwFYTGDIGQFH 546
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2741210702 348 SDGRLHIEGRKSNLIITSFGRNISPEWVEAALVEQPEVMQAMVYGDGLPT-PAALLVPSHP 407
Cdd:PLN02387 547 PDGCLEIIDRKKDIVKLQHGEYVSLGKVEAALSVSPYVDNIMVHADPFHSyCVALVVPSQQ 607
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
14-392 |
5.95e-19 |
|
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: 90.46 E-value: 5.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 14 DPQRIALdALDGAPITYgalwAELGERSLAMMARFET------DRAVaLQSDHGAETSIVELALLRA-KIPVLSLPAFFT 86
Cdd:cd05920 28 HPDRIAV-VDGDRRLTY----RELDRRADRLAAGLRGlgirpgDRVV-VQLPNVAEFVVLFFALLRLgAVPVLALPSHRR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 87 REQS---RHAIALCGADPDPIQSPSGTARSRRSA-SVPLPrgtARITFTSGSTGTPKGICLSADHMLTVAQSIVAAVGAE 162
Cdd:cd05920 102 SELSafcAHAEAVAYIVPDRHAGFDHRALARELAeSIPEV---ALFLLSGGTTGTPKLIPRTHNDYAYNVRASAEVCGLD 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 163 HAGRHLALLP---------PGILletvagffPTLLAGGCYVcppqamigFADPFRPDfvKAATIIAEQRITSLILVPEYL 233
Cdd:cd05920 179 QDTVYLAVLPaahnfplacPGVL--------GTLLAGGRVV--------LAPDPSPD--AAFPLIEREGVTVTALVPALV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 234 EGLVRVMETTGLRLPLLTLVAVGGARTSIPLMDRARR-LGLPIRQGYGLTE-CASVVSLQDAGDDDPSSVGRCL-PHMTV 310
Cdd:cd05920 241 SLWLDAAASRRADLSSLRLLQVGGARLSPALARRVPPvLGCTLQQVFGMAEgLLNYTRLDDPDEVIIHTQGRPMsPDDEI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 311 RVADD----------GEIILDGPVCL-GAVGGEA-------PGSPLQTGDIGSIDSDGRLHIEGRKSNLIITSfGRNISP 372
Cdd:cd05920 321 RVVDEegnpvppgeeGELLTRGPYTIrGYYRAPEhnaraftPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRG-GEKIAA 399
|
410 420
....*....|....*....|
gi 2741210702 373 EWVEAALVEQPEVMQAMVYG 392
Cdd:cd05920 400 EEVENLLLRHPAVHDAAVVA 419
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
125-400 |
7.00e-19 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 90.73 E-value: 7.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 125 TARITFTSGSTGTPKGICLSADHMLTVAQSIVAAVGAEHAGRHLALLPPgilletVAGFFPTLlaGGCYVCPPqamigfA 204
Cdd:PRK09274 176 MAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEIDLPTFPL------FALFGPAL--GMTSVIPD------M 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 205 DPFRPDFVKAATI---IAEQRITSLILVPEYLEGLVRVMETTGLRLPLLTLVAVGGARTSIPLMDRARRL---GLPIRQG 278
Cdd:PRK09274 242 DPTRPATVDPAKLfaaIERYGVTNLFGSPALLERLGRYGEANGIKLPSLRRVISAGAPVPIAVIERFRAMlppDAEILTP 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 279 YGLTEC---ASVVS---------LQDAGDDdpSSVGRCLPHMTVRV-----------ADD--------GEIILDGPVC-- 325
Cdd:PRK09274 322 YGATEAlpiSSIESreilfatraATDNGAG--ICVGRPVDGVEVRIiaisdapipewDDAlrlatgeiGEIVVAGPMVtr 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 326 ----------LGAVGGEAPGSPLQTGDIGSIDSDGRLHIEGRKSNLIITsFGRNISPEWVEAALVEQPEVMQ-AMVygdG 394
Cdd:PRK09274 400 syynrpeatrLAKIPDGQGDVWHRMGDLGYLDAQGRLWFCGRKAHRVET-AGGTLYTIPCERIFNTHPGVKRsALV---G 475
|
....*.
gi 2741210702 395 LPTPAA 400
Cdd:PRK09274 476 VGVPGA 481
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
51-398 |
7.50e-19 |
|
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: 89.80 E-value: 7.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 51 DRaVALQSDHGAETSIVELALLRAKIPVLSLPAFFTREQSRHAIALCGAdpdpiqspsgtarsrRSASVPLPRGTARITF 130
Cdd:cd05971 32 DR-VGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGA---------------SALVTDGSDDPALIIY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 131 TSGSTGTPKGiCLSADHMLtvaqsIVAAVGAEHAgrHLALLPPGILLETVA----------GFFPTLLAGGCYV-CPPQa 199
Cdd:cd05971 96 TSGTTGPPKG-ALHAHRVL-----LGHLPGVQFP--FNLFPRDGDLYWTPAdwawigglldVLLPSLYFGVPVLaHRMT- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 200 migfadPFRPDfvKAATIIAEQRITSLILVPEYLEGLVRVMETTGLRLPLLTLVAVGGARTSIPLMDRARR-LGLPIRQG 278
Cdd:cd05971 167 ------KFDPK--AALDLMSRYGVTTAFLPPTALKMMRQQGEQLKHAQVKLRAIATGGESLGEELLGWAREqFGVEVNEF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 279 YGLTECASVV-SLQDAGDDDPSSVGRCLPHMTVRVADD-GEIILDGPVclGAVGGEAP--------------------GS 336
Cdd:cd05971 239 YGQTECNLVIgNCSALFPIKPGSMGKPIPGHRVAIVDDnGTPLPPGEV--GEIAVELPdpvaflgywnnpsatekkmaGD 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2741210702 337 PLQTGDIGSIDSDGRLHIEGRKSNlIITSFGRNISPEWVEAALVEQPEVMQAMVYgdGLPTP 398
Cdd:cd05971 317 WLLTGDLGRKDSDGYFWYVGRDDD-VITSSGYRIGPAEIEECLLKHPAVLMAAVV--GIPDP 375
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
128-392 |
8.09e-19 |
|
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: 87.85 E-value: 8.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 128 ITFTSGSTGTPKGICLSADHMLtvaQSIVAAVGAEHAGRHLALLPPGILLETVA--GFFPTLLAGGCYVcppqAMIGFad 205
Cdd:cd17633 5 IGFTSGTTGLPKAYYRSERSWI---ESFVCNEDLFNISGEDAILAPGPLSHSLFlyGAISALYLGGTFI----GQRKF-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 206 pfrpDFVKAATIIAEQRITSLILVPEYLEGLVRVMEttglrlPLLTLVAV-GGARTSIPLMDRARRLGLP---IRQGYGL 281
Cdd:cd17633 76 ----NPKSWIRKINQYNATVIYLVPTMLQALARTLE------PESKIKSIfSSGQKLFESTKKKLKNIFPkanLIEFYGT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 282 TECASVVSLQDAGDDDPSSVGRCLPHMTVRV--ADDGEI---------ILDGPVclgAVGGEAPGSPLQTGDIGSIDSDG 350
Cdd:cd17633 146 SELSFITYNFNQESRPPNSVGRPFPNVEIEIrnADGGEIgkifvksemVFSGYV---RGGFSNPDGWMSVGDIGYVDEEG 222
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2741210702 351 RLHIEGRKSNLIITSfGRNISPEWVEAALVEQPEVMQAMVYG 392
Cdd:cd17633 223 YLYLVGRESDMIIIG-GINIFPTEIESVLKAIPGIEEAIVVG 263
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
14-408 |
9.64e-19 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 89.93 E-value: 9.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 14 DPQRIALDALDGAPITYGALwaelgERSLAMMARF-------ETDRaVALQSDHGAETSIVELALLRAKIPVLSL----- 81
Cdd:PRK07514 15 DRDAPFIETPDGLRYTYGDL-----DAASARLANLlvalgvkPGDR-VAVQVEKSPEALALYLATLRAGAVFLPLntayt 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 82 ------------PAFFTREQSRHA----IAL-CGA------DPDPIQSPSGTARSRRSASVPLPRGT---ARITFTSGST 135
Cdd:PRK07514 89 laeldyfigdaePALVVCDPANFAwlskIAAaAGAphvetlDADGTGSLLEAAAAAPDDFETVPRGAddlAAILYTSGTT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 136 GTPKGICLSADHMLTVAQSIVAAVGAEHAGRHLALLPpgilLETVAGFF----PTLLAGGcyvcppqAMIgfadpFRPDF 211
Cdd:PRK07514 169 GRSKGAMLSHGNLLSNALTLVDYWRFTPDDVLIHALP----IFHTHGLFvatnVALLAGA-------SMI-----FLPKF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 212 VKAATIIAEQRITSLILVPEYLeglVRVmettgLRLPLLTLVAVGGART----SIPLM-----DRARRLGLPIRQGYGLT 282
Cdd:PRK07514 233 DPDAVLALMPRATVMMGVPTFY---TRL-----LQEPRLTREAAAHMRLfisgSAPLLaethrEFQERTGHAILERYGMT 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 283 ECASVVSLQDAGDDDPSSVGRCLPHMTVRVAD--DGEiildgPVCLGAVGG-EAPGsP---------------------- 337
Cdd:PRK07514 305 ETNMNTSNPYDGERRAGTVGFPLPGVSLRVTDpeTGA-----ELPPGEIGMiEVKG-Pnvfkgywrmpektaeefradgf 378
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2741210702 338 LQTGDIGSIDSDGRLHIEGRKSNLIITSfGRNISPEWVEAALVEQPEVMQAMVYGdglptpaallVPsHPD 408
Cdd:PRK07514 379 FITGDLGKIDERGYVHIVGRGKDLIISG-GYNVYPKEVEGEIDELPGVVESAVIG----------VP-HPD 437
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
123-391 |
1.81e-18 |
|
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: 87.32 E-value: 1.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 123 RGTARITFTSGSTGTPKGICLSADHMLTVAQSIVAAVGAEHAGRHLALLPPGILLETVAGFFPTLLAGGCYVcppqamIG 202
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCV------TG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 203 FADPFRPDFVKAATIIAeqrITSLILVPEYLEGLVRVMETTGLRLPLLTLVAVGGARtsiPLMDRARRLGL----PIRQG 278
Cdd:cd17635 75 GENTTYKSLFKILTTNA---VTTTCLVPTLLSKLVSELKSANATVPSLRLIGYGGSR---AIAADVRFIEAtgltNTAQV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 279 YGLTECASVVSLQ-DAGDDDPSSVGRCLPHMTVRVAD----------DGEIILDGPVCLGAVGGEAPGSP-------LQT 340
Cdd:cd17635 149 YGLSETGTALCLPtDDDSIEINAVGRPYPGVDVYLAAtdgiagpsasFGTIWIKSPANMLGYWNNPERTAevlidgwVNT 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2741210702 341 GDIGSIDSDGRLHIEGRKSnLIITSFGRNISPEWVEAALVEQPEVMQAMVY 391
Cdd:cd17635 229 GDLGERREDGFLFITGRSS-ESINCGGVKIAPDEVERIAEGVSGVQECACY 278
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
125-359 |
2.17e-18 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 89.98 E-value: 2.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 125 TARITFTSGSTGTPKGICLSADHMLTVAQSIVAAVGAEHAGRHLALLPP----GIlleTVAGFFPTLLagGCyvcppqAM 200
Cdd:PRK08633 784 TATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSSLPFfhsfGL---TVTLWLPLLE--GI------KV 852
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 201 IGFADPFrpDFVKAATIIAEQRITSLILVPEYLEGLVRVMETTGLRLPLLTLVAVGGARTSIPLMDRAR-RLGLPIRQGY 279
Cdd:PRK08633 853 VYHPDPT--DALGIAKLVAKHRATILLGTPTFLRLYLRNKKLHPLMFASLRLVVAGAEKLKPEVADAFEeKFGIRILEGY 930
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 280 GLTECASV--VSLQDAGDDD--------PSSVGRCLPHMTVRVAD-----------DGEIILDGP-VCLGAVGGEAPGSP 337
Cdd:PRK08633 931 GATETSPVasVNLPDVLAADfkrqtgskEGSVGMPLPGVAVRIVDpetfeelppgeDGLILIGGPqVMKGYLGDPEKTAE 1010
|
250 260 270
....*....|....*....|....*....|..
gi 2741210702 338 L----------QTGDIGSIDSDGRLHIEGRKS 359
Cdd:PRK08633 1011 VikdidgigwyVTGDKGHLDEDGFLTITDRYS 1042
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
99-392 |
2.60e-18 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 88.96 E-value: 2.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 99 ADPDPIQSPSGTARSRRSAsvPLPRGTARITFTSGSTGTPKGICLSADhmlTVAQSIVAAVGAEHAGR-HLALLPPGILL 177
Cdd:PRK13295 175 ITPAWEQEPDAPAILARLR--PGPDDVTQLIYTSGTTGEPKGVMHTAN---TLMANIVPYAERLGLGAdDVILMASPMAH 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 178 ETvaGF-----FPTLLaggcyvcppQAMIGFADPFRPDfvKAATIIAEQRITSLILVPEYLEGLVRVMETTGLRLPLLTL 252
Cdd:PRK13295 250 QT--GFmyglmMPVML---------GATAVLQDIWDPA--RAAELIRTEGVTFTMASTPFLTDLTRAVKESGRPVSSLRT 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 253 VAVGGARTSIPLMDRARR-LGLPIRQGYGLTECASVVSLQDAGDDDPSSV--GRCLPHMTVRVADD----------GEII 319
Cdd:PRK13295 317 FLCAGAPIPGALVERARAaLGAKIVSAWGMTENGAVTLTKLDDPDERASTtdGCPLPGVEVRVVDAdgaplpagqiGRLQ 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 320 LDGPVCLGAV-------GGEAPGSpLQTGDIGSIDSDGRLHIEGRKSNLIITSfGRNISPEWVEAALVEQPEVMQAMVYG 392
Cdd:PRK13295 397 VRGCSNFGGYlkrpqlnGTDADGW-FDTGDLARIDADGYIRISGRSKDVIIRG-GENIPVVEIEALLYRHPAIAQVAIVA 474
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
111-425 |
3.54e-18 |
|
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: 87.69 E-value: 3.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 111 ARSRRSASVPLPRGTARITFTSGSTGTPKGICLSADHMLTVAQSIVAAVGAEHAGRHLALLPPGiLLETVAGFFPTLLAG 190
Cdd:cd17652 81 ADARPALLLTTPDNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQIAAFDVGPGSRVLQFASPS-FDASVWELLMALLAG 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 191 GCYVCPPQAMIGFADPFrpdfvkaATIIAEQRITSLILVPEYLeglvRVMETTGLrLPLLTLVaVGGARTSIPLMDR--- 267
Cdd:cd17652 160 ATLVLAPAEELLPGEPL-------ADLLREHRITHVTLPPAAL----AALPPDDL-PDLRTLV-VAGEACPAELVDRwap 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 268 ARRLglpiRQGYGLTECASVVSLQDA-GDDDPSSVGRCLPHMTVRVADD----------GEIILDGP-VCLGAVGGEA-- 333
Cdd:cd17652 227 GRRM----INAYGPTETTVCATMAGPlPGGGVPPIGRPVPGTRVYVLDArlrpvppgvpGELYIAGAgLARGYLNRPGlt 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 334 -----------PGSPL-QTGDIGSIDSDGRLHIEGRKSNLIITSfGRNISPEWVEAALVEQPEVMQA--MVYGDGLPTP- 398
Cdd:cd17652 303 aerfvadpfgaPGSRMyRTGDLARWRADGQLEFLGRADDQVKIR-GFRIELGEVEAALTEHPGVAEAvvVVRDDRPGDKr 381
|
330 340
....*....|....*....|....*....
gi 2741210702 399 -AALLVPSHPDADLAAA-VARANEKLPAY 425
Cdd:cd17652 382 lVAYVVPAPGAAPTAAElRAHLAERLPGY 410
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
128-392 |
3.73e-18 |
|
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: 86.56 E-value: 3.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 128 ITFTSGSTGTPKGICLSADHMLTVAQSIVAAVGAEHAGRhLALLPP-----GILLETVAgffptLLAGGCYVCPPqamig 202
Cdd:cd05917 7 IQFTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDR-LCIPVPlfhcfGSVLGVLA-----CLTHGATMVFP----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 203 fADPFRPDFVKAAtiIAEQRITSLILVPeyleglvrVMETTGLRLPLLTLVAVGGARTSI--------PLMDRAR-RLGL 273
Cdd:cd05917 76 -SPSFDPLAVLEA--IEKEKCTALHGVP--------TMFIAELEHPDFDKFDLSSLRTGImagapcppELMKRVIeVMNM 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 274 P-IRQGYGLTEcASVVSLQDAGDDDP----SSVGRCLPHMTVRVAD-DGEIILD----GPVC-------LG--------- 327
Cdd:cd05917 145 KdVTIAYGMTE-TSPVSTQTRTDDSIekrvNTVGRIMPHTEAKIVDpEGGIVPPvgvpGELCirgysvmKGywndpekta 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2741210702 328 -AVGGEapgSPLQTGDIGSIDSDGRLHIEGRKSNLIITSfGRNISPEWVEAALVEQPEVMQAMVYG 392
Cdd:cd05917 224 eAIDGD---GWLHTGDLAVMDEDGYCRIVGRIKDMIIRG-GENIYPREIEEFLHTHPKVSDVQVVG 285
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
122-392 |
5.60e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 87.63 E-value: 5.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 122 PRGTARITFTSGSTGTPKGICLSADHMLTVAQSIVAAVGAEHAGRhlaLLPPGILLETVAGFFPtllagGCYVCPPQAMI 201
Cdd:PRK06145 148 PTDLVRLMYTSGTTDRPKGVMHSYGNLHWKSIDHVIALGLTASER---LLVVGPLYHVGAFDLP-----GIAVLWVGGTL 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 202 GFADPFRPDFVKAAtiIAEQRITSLILVPEYLEGLVRVMETTGLRLPLLTLVAVGGARTSiplMDRARRLGLPIRQG--- 278
Cdd:PRK06145 220 RIHREFDPEAVLAA--IERHRLTCAWMAPVMLSRVLTVPDRDRFDLDSLAWCIGGGEKTP---ESRIRDFTRVFTRAryi 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 279 --YGLTECASVVSLQDAGD--DDPSSVGRCLPHMTVRVADD----------GEIILDGP-VCLG------AVGGEAPGSP 337
Cdd:PRK06145 295 daYGLTETCSGDTLMEAGReiEKIGSTGRALAHVEIRIADGagrwlppnmkGEICMRGPkVTKGywkdpeKTAEAFYGDW 374
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2741210702 338 LQTGDIGSIDSDGRLHIEGRKSNLIITSfGRNISPEWVEAALVEQPEVMQAMVYG 392
Cdd:PRK06145 375 FRSGDVGYLDEEGFLYLTDRKKDMIISG-GENIASSEVERVIYELPEVAEAAVIG 428
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
111-684 |
8.80e-18 |
|
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: 87.99 E-value: 8.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 111 ARSRRSASVPLPRGTAR----ITFTSGSTGTPKGICLSADHMLTVAQSIVAAVGAEHAGRHLALLPPGILLeTVAGFFPT 186
Cdd:COG1020 601 ALAAEPATNPPVPVTPDdlayVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFASLSFDA-SVWEIFGA 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 187 LLAGGCYVCPPQAMigfadpfRPDFVKAATIIAEQRITSLILVPEYLEGLVrvmETTGLRLPLLTLVAVGGARTSIPLMD 266
Cdd:COG1020 680 LLSGATLVLAPPEA-------RRDPAALAELLARHRVTVLNLTPSLLRALL---DAAPEALPSLRLVLVGGEALPPELVR 749
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 267 RARRL--GLPIRQGYGLTECASVVSLQDAGDDDPSS----VGRCLPHMTVRVADD----------GEIILDGP-VCLGAV 329
Cdd:COG1020 750 RWRARlpGARLVNLYGPTETTVDSTYYEVTPPDADGgsvpIGRPIANTRVYVLDAhlqpvpvgvpGELYIGGAgLARGYL 829
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 330 G-------------GEAPGSPL-QTGDIGSIDSDGRLHIEGRKSNLI-ITSFgRnISPEWVEAALVEQPEVMQA--MVYG 392
Cdd:COG1020 830 NrpeltaerfvadpFGFPGARLyRTGDLARWLPDGNLEFLGRADDQVkIRGF-R-IELGEIEAALLQHPGVREAvvVARE 907
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 393 DGLPTPA-ALLVPSHPDADLAAAVARANEKLPAYAQISAWREAAHFTPMngqLTGNGRLRRaaiaaayLNGPPLFFTELE 471
Cdd:COG1020 908 DAPGDKRlVAYVVPEAGAAAAAALLRLALALLLPPYMVPAAVVLLLPLP---LTGNGKLDR-------LALPAPAAAAAA 977
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 472 ARTVRERLRFLAVPQLQAGLNGTISRGAYLDYLEQAYHHVRHTVPLMQAARARLTDRADIVAALDDYIAEETGHEEWILS 551
Cdd:COG1020 978 AAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLLFLAAAAAAAAAAAAAAAA 1057
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 552 DIAAAGGDAEAVRASKPGPATAAMVDHAYARIANGNAMAFFGMVYVLESVSVAFATRGAAAVAKKLGLPPQAFTYLTSHG 631
Cdd:COG1020 1058 AAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLALLLLLALLLALLAALRARRAVRQEGPR 1137
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 2741210702 632 ALDQEHMTFFANLVNGLDDPADRDAILSMAQEIFGLFGGIFAAIELEPAHAHA 684
Cdd:COG1020 1138 LRLLVALAAALALAALLALLLAAAAAAAELLAAAALLLLLALLLLALLLLLLL 1190
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
126-392 |
2.31e-17 |
|
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: 85.76 E-value: 2.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 126 ARITFTSGSTGTPKGICLS----ADHMLTVAQSIVAAVGAE----------HAgrHLALLPpgilletvagfFPTLLAGG 191
Cdd:cd12119 166 AAICYTSGTTGNPKGVVYShrslVLHAMAALLTDGLGLSESdvvlpvvpmfHV--NAWGLP-----------YAAAMVGA 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 192 CYVCPpqamigfaDPFrPDFVKAATIIAEQRITSLILVPEYLEGLVRVMETTGLRLPLLTLVAVGGARTSIPLMDRARRL 271
Cdd:cd12119 233 KLVLP--------GPY-LDPASLAELIEREGVTFAAGVPTVWQGLLDHLEANGRDLSSLRRVVIGGSAVPRSLIEAFEER 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 272 GLPIRQGYGLTE---CASVVSLQDAGDDDP--------SSVGRCLPHMTVRVADD------------GEIILDGP-VCLG 327
Cdd:cd12119 304 GVRVIHAWGMTEtspLGTVARPPSEHSNLSedeqlalrAKQGRPVPGVELRIVDDdgrelpwdgkavGELQVRGPwVTKS 383
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2741210702 328 AVGGEAPGSP------LQTGDIGSIDSDGRLHIEGRkSNLIITSFGRNISPEWVEAALVEQPEVMQAMVYG 392
Cdd:cd12119 384 YYKNDEESEAltedgwLRTGDVATIDEDGYLTITDR-SKDVIKSGGEWISSVELENAIMAHPAVAEAAVIG 453
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
128-390 |
2.63e-17 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 85.55 E-value: 2.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 128 ITFTSGSTGTPKGICLS-ADHMLTVAQSIVAAVGAEHAGRHLALLPPGILLETVAGFFPTLLAGGCyvcppqaMIGFADp 206
Cdd:COG0365 189 ILYTSGTTGKPKGVVHThGGYLVHAATTAKYVLDLKPGDVFWCTADIGWATGHSYIVYGPLLNGAT-------VVLYEG- 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 207 fRPDFVKAAT---IIAEQRITSLILVPEYLEGLVRVMETTGLRLPLLTLVAVG--GARTSIPLMDRARR-LGLPIRQGYG 280
Cdd:COG0365 261 -RPDFPDPGRlweLIEKYGVTVFFTAPTAIRALMKAGDEPLKKYDLSSLRLLGsaGEPLNPEVWEWWYEaVGVPIVDGWG 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 281 LTECASVVSLQDAGDD-DPSSVGRCLPHMTVRVADDgeiilDG-PVCLGAVG-----GEAPGSPLQ-------------- 339
Cdd:COG0365 340 QTETGGIFISNLPGLPvKPGSMGKPVPGYDVAVVDE-----DGnPVPPGEEGelvikGPWPGMFRGywndperyretyfg 414
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 2741210702 340 -------TGDIGSIDSDGRLHIEGRKSNLIITSfGRNISPEWVEAALVEQPEVMQAMV 390
Cdd:COG0365 415 rfpgwyrTGDGARRDEDGYFWILGRSDDVINVS-GHRIGTAEIESALVSHPAVAEAAV 471
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
15-438 |
5.49e-17 |
|
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: 84.24 E-value: 5.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 15 PQRIALDALDGApITYGalwaELGERSLAMMARF-----ETDRAVALQSDHGAETSIVELALLRAK---IPV-LSLPAff 85
Cdd:cd12114 1 PDATAVICGDGT-LTYG----ELAERARRVAGALkaagvRPGDLVAVTLPKGPEQVVAVLGILAAGaayVPVdIDQPA-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 86 TREQ------SRHAIALCGADPDPIQSPSGTARSRRSASVPLPRGTAR---------ITFTSGSTGTPKGICLSADHMLT 150
Cdd:cd12114 74 ARREailadaGARLVLTDGPDAQLDVAVFDVLILDLDALAAPAPPPPVdvapddlayVIFTSGSTGTPKGVMISHRAALN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 151 VAQSIVAAVGAEHAGRHLALLPPGILLeTVAGFFPTLLAGGCYVCPPQAMigfadpfRPDFVKAATIIAEQRITSLILVP 230
Cdd:cd12114 154 TILDINRRFAVGPDDRVLALSSLSFDL-SVYDIFGALSAGATLVLPDEAR-------RRDPAHWAELIERHGVTLWNSVP 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 231 EYLEGLVRVMETTGLRLPLLTLVAVGGARTSIPLMDRARRLGLPIRQ---GyGLTECA--SVVSLQDAGDDDPSSV--GR 303
Cdd:cd12114 226 ALLEMLLDVLEAAQALLPSLRLVLLSGDWIPLDLPARLRALAPDARLislG-GATEASiwSIYHPIDEVPPDWRSIpyGR 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 304 CLPHMTVRVADD----------GEIILDGP-VCLGAVGGEA-----------PGSPLQTGDIGSIDSDGRLHIEGRKSNL 361
Cdd:cd12114 305 PLANQRYRVLDPrgrdcpdwvpGELWIGGRgVALGYLGDPEltaarfvthpdGERLYRTGDLGRYRPDGTLEFLGRRDGQ 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 362 IITSfGRNISPEWVEAALVEQPEVMQA--MVYGDGLPTPAALLVPSHPDADLAAAV---ARANEKLPAYAQISA--WREA 434
Cdd:cd12114 385 VKVR-GYRIELGEIEAALQAHPGVARAvvVVLGDPGGKRLAAFVVPDNDGTPIAPDalrAFLAQTLPAYMIPSRviALEA 463
|
....
gi 2741210702 435 AHFT 438
Cdd:cd12114 464 LPLT 467
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
101-392 |
5.72e-17 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 83.17 E-value: 5.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 101 PDPIQSPSGTARSRRSASV--PLPRGTARITFTSGSTGTPKGICLSADHMLTVAQSIVAAVGAEhaGRHLALLPPgillE 178
Cdd:PRK07824 11 PVPAQDERRAALLRDALRVgePIDDDVALVVATSGTTGTPKGAMLTAAALTASADATHDRLGGP--GQWLLALPA----H 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 179 TVAGF---FPTLLAGGCYVCPPQAMiGFaDPfrPDFVKA-ATIIAEQRITSLilVPEYLEGLVRVMETTGlRLPLLTLVA 254
Cdd:PRK07824 85 HIAGLqvlVRSVIAGSEPVELDVSA-GF-DP--TALPRAvAELGGGRRYTSL--VPMQLAKALDDPAATA-ALAELDAVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 255 VGGARTSIPLMDRARRLGLPIRQGYGLTE-CASVVslQDagdddpssvGRCLPHMTVRVaDDGEIILDGPVClgAVGGEA 333
Cdd:PRK07824 158 VGGGPAPAPVLDAAAAAGINVVRTYGMSEtSGGCV--YD---------GVPLDGVRVRV-EDGRIALGGPTL--AKGYRN 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2741210702 334 PGSP--------LQTGDIGSIDsDGRLHIEGRKSNlIITSFGRNISPEWVEAALVEQPEVMQAMVYG 392
Cdd:PRK07824 224 PVDPdpfaepgwFRTDDLGALD-DGVLTVLGRADD-AISTGGLTVLPQVVEAALATHPAVADCAVFG 288
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
128-392 |
7.83e-17 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 84.05 E-value: 7.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 128 ITFTSGSTGTPKGICLSADHMLTVAQSIVAAVGAEHAGRHLALLPPGILLETVAGFFPTLLAGGCYVCPpqamigfADPF 207
Cdd:PRK12583 206 IQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCVPVPLYHCFGMVLANLGCMTVGACLVYP-------NEAF 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 208 RPDFVKAAtiIAEQRITSLILVPEYLEGLVRVMETTGLRLPLLTLVAVGGARTSIPLMDRA-RRLGLP-IRQGYGLTEcA 285
Cdd:PRK12583 279 DPLATLQA--VEEERCTALYGVPTMFIAELDHPQRGNFDLSSLRTGIMAGAPCPIEVMRRVmDEMHMAeVQIAYGMTE-T 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 286 SVVSLQDAGDDD----PSSVGRCLPHMTVRVAD-DGEIILDGP----------VCLG--------AVGGEAPGSpLQTGD 342
Cdd:PRK12583 356 SPVSLQTTAADDlerrVETVGRTQPHLEVKVVDpDGATVPRGEigelctrgysVMKGywnnpeatAESIDEDGW-MHTGD 434
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2741210702 343 IGSIDSDGRLHIEGRKSNLIITSfGRNISPEWVEAALVEQPEVMQAMVYG 392
Cdd:PRK12583 435 LATMDEQGYVRIVGRSKDMIIRG-GENIYPREIEEFLFTHPAVADVQVFG 483
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
15-390 |
1.38e-16 |
|
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: 83.02 E-value: 1.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 15 PQRIALDALDGApITYgalwAELGERSLAMMAR-----FETDRAVALQSDHGAETSIVELALLRAK---IPV-LSLPAFF 85
Cdd:cd12117 11 PDAVAVVYGDRS-LTY----AELNERANRLARRlraagVGPGDVVGVLAERSPELVVALLAVLKAGaayVPLdPELPAER 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 86 TR---EQSRHAIALC------GADPDPIQSPSGTARSRRSASVPLPRG----TARITFTSGSTGTPKGICLSadHmltva 152
Cdd:cd12117 86 LAfmlADAGAKVLLTdrslagRAGGLEVAVVIDEALDAGPAGNPAVPVspddLAYVMYTSGSTGRPKGVAVT--H----- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 153 QSIVAAVgaeHAGRHLALLPPGILLET------VAGF--FPTLLAGG-CYVCPPQAMIgfadpfRPDFVKAAtiIAEQRI 223
Cdd:cd12117 159 RGVVRLV---KNTNYVTLGPDDRVLQTsplafdASTFeiWGALLNGArLVLAPKGTLL------DPDALGAL--IAEEGV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 224 TSLIL-----------VPEYLEGLVRVMettglrlplltlvaVGGARTSIPLMDRARRL--GLPIRQGYGLTECASVVS- 289
Cdd:cd12117 228 TVLWLtaalfnqladeDPECFAGLRELL--------------TGGEVVSPPHVRRVLAAcpGLRLVNGYGPTENTTFTTs 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 290 -LQDAGDDDPSSV--GRCLPHMTVRVADD----------GEIILDGP-VCLGAVGGEA------------PGSPL-QTGD 342
Cdd:cd12117 294 hVVTELDEVAGSIpiGRPIANTRVYVLDEdgrpvppgvpGELYVGGDgLALGYLNRPAltaerfvadpfgPGERLyRTGD 373
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 2741210702 343 IGSIDSDGRLHIEGRKSNLI-ITSFgrNISPEWVEAALVEQPEVMQAMV 390
Cdd:cd12117 374 LARWLPDGRLEFLGRIDDQVkIRGF--RIELGEIEAALRAHPGVREAVV 420
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
119-396 |
1.87e-16 |
|
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: 82.51 E-value: 1.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 119 VPLPRGTARITFTSGSTGTPKGICLSADHMLTVAQSIVAAVGAEHAGRHLALLPPgilletVAGFFPTLlaGGCYVCPPq 198
Cdd:cd05910 81 IPKADEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGEVDLATFPL------FALFGPAL--GLTSVIPD- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 199 amigfADPFRPDFVKAATI---IAEQRITSLILVPEYLEGLVRVMETTGLRLPLLTLVAVGGARTSIPLMDRARRL---G 272
Cdd:cd05910 152 -----MDPTRPARADPQKLvgaIRQYGVSIVFGSPALLERVARYCAQHGITLPSLRRVLSAGAPVPIALAARLRKMlsdE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 273 LPIRQGYGLTECASVVSLQD----AGDDDPSS------VGRCLPHMTVRV--ADD-----------------GEIILDGP 323
Cdd:cd05910 227 AEILTPYGATEALPVSSIGSrellATTTAATSggagtcVGRPIPGVRVRIieIDDepiaewddtlelprgeiGEITVTGP 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 324 VC------------LGAVGGEAPGSPLQTGDIGSIDSDGRLHIEGRKSNLIITsFGRNISPEWVEAALVEQPEVMQAMVY 391
Cdd:cd05910 307 TVtptyvnrpvataLAKIDDNSEGFWHRMGDLGYLDDEGRLWFCGRKAHRVIT-TGGTLYTEPVERVFNTHPGVRRSALV 385
|
....*
gi 2741210702 392 GDGLP 396
Cdd:cd05910 386 GVGKP 390
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
130-402 |
2.87e-16 |
|
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: 82.41 E-value: 2.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 130 FTSGSTGTPKGICLSADHMLTVAQsivaavgaeHAGRHLALLPPGILLETVAGFFP-------------TLLAGGCyvcp 196
Cdd:cd05933 157 YTSGTTGMPKGVMLSHDNITWTAK---------AASQHMDLRPATVGQESVVSYLPlshiaaqildiwlPIKVGGQ---- 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 197 pqamIGFADPfrpDFVKA--ATIIAEQRITSLILVPEYLEGLVRVMET-----TGLRLPLLTLVAVGGARTSIPLM---- 265
Cdd:cd05933 224 ----VYFAQP---DALKGtlVKTLREVRPTAFMGVPRVWEKIQEKMKAvgaksGTLKRKIASWAKGVGLETNLKLMgges 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 266 -----------------------DRARR------------------LGLPIRQGYGLTECASVVSLQDAGDDDPSSVGRC 304
Cdd:cd05933 297 psplfyrlakklvfkkvrkalglDRCQKfftgaapisretlefflsLNIPIMELYGMSETSGPHTISNPQAYRLLSCGKA 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 305 LPHMTVRV----AD-DGEIILDG-PVCLGAVGGEAPGSP-------LQTGDIGSIDSDGRLHIEGRKSNLIITSFGRNIS 371
Cdd:cd05933 377 LPGCKTKIhnpdADgIGEICFWGrHVFMGYLNMEDKTEEaidedgwLHSGDLGKLDEDGFLYITGRIKELIITAGGENVP 456
|
330 340 350
....*....|....*....|....*....|..
gi 2741210702 372 PEWVEAALVEQ-PEVMQAMVYGDGLPTPAALL 402
Cdd:cd05933 457 PVPIEDAVKKElPIISNAMLIGDKRKFLSMLL 488
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
98-392 |
4.65e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 81.51 E-value: 4.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 98 GADPDPIQSPSGTARS-----RRSASVPLPRGTAR---ITFTSGSTGTPKGICLSADHMLTVAQSIVAAVGaehagrhla 169
Cdd:PRK07788 174 GGNPDDDEPSGSTDETlddliAGSSTAPLPKPPKPggiVILTSGTTGTPKGAPRPEPSPLAPLAGLLSRVP--------- 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 170 lLPPGILLETVAGFFPTL--------LAGGCYVCppqamigfadpFRPDFVKAATI--IAEQRITSLILVPEYLEGLVRV 239
Cdd:PRK07788 245 -FRAGETTLLPAPMFHATgwahltlaMALGSTVV-----------LRRRFDPEATLedIAKHKATALVVVPVMLSRILDL 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 240 METTGLRLPL--LTLVAVGGARTSIPLMDRA-RRLGLPIRQGYGLTEC--ASVVSLQDAGDDdPSSVGRCLPHMTVRVAD 314
Cdd:PRK07788 313 GPEVLAKYDTssLKIIFVSGSALSPELATRAlEAFGPVLYNLYGSTEVafATIATPEDLAEA-PGTVGRPPKGVTVKILD 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 315 DGeiilDGPVCLGAVG-----GEAP-------GSP------LQTGDIGSIDSDGRLHIEGRKSNLIItSFGRNISPEWVE 376
Cdd:PRK07788 392 EN----GNEVPRGVVGrifvgNGFPfegytdgRDKqiidglLSSGDVGYFDEDGLLFVDGRDDDMIV-SGGENVFPAEVE 466
|
330
....*....|....*.
gi 2741210702 377 AALVEQPEVMQAMVYG 392
Cdd:PRK07788 467 DLLAGHPDVVEAAVIG 482
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
2-390 |
6.15e-16 |
|
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: 81.35 E-value: 6.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 2 PLFQAIAAHAAADPQRIALdaLDGA-PITYgalwAELGERSLAMMARFET------DRAVaLQSDHGAETSIVELALLRA 74
Cdd:COG1021 26 TLGDLLRRRAERHPDRIAV--VDGErRLSY----AELDRRADRLAAGLLAlglrpgDRVV-VQLPNVAEFVIVFFALFRA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 75 K-IPVLSLPA--------FFTREQS----------------------------RHAIALcgADPDPIQSPSGTARSRRSA 117
Cdd:COG1021 99 GaIPVFALPAhrraeishFAEQSEAvayiipdrhrgfdyralarelqaevpslRHVLVV--GDAGEFTSLDALLAAPADL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 118 SVPLPRGT--ARITFTSGSTGTPKGI-CLSADHMLTVAQSiVAAVGAEHAGRHLALLP---------PGILletvaGffp 185
Cdd:COG1021 177 SEPRPDPDdvAFFQLSGGTTGLPKLIpRTHDDYLYSVRAS-AEICGLDADTVYLAALPaahnfplssPGVL-----G--- 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 186 TLLAGGCYVcppqamigFADPFRPDfvKAATIIAEQRITSLILVPEYLEGLVRVMETTGLRLPLLTLVAVGGARTSIPLM 265
Cdd:COG1021 248 VLYAGGTVV--------LAPDPSPD--TAFPLIERERVTVTALVPPLALLWLDAAERSRYDLSSLRVLQVGGAKLSPELA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 266 DRAR-RLGLPIRQGYGLTEcaSVVSLQDAGDDDP---SSVGRCL-PHMTVRVADDgeiilDG-PVCLGAVG-----GeaP 334
Cdd:COG1021 318 RRVRpALGCTLQQVFGMAE--GLVNYTRLDDPEEvilTTQGRPIsPDDEVRIVDE-----DGnPVPPGEVGelltrG--P 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2741210702 335 G-------SPLQ------------TGDIGSIDSDGRLHIEGRKSNLIITSfGRNISPEWVEAALVEQPEVMQAMV 390
Cdd:COG1021 389 YtirgyyrAPEHnaraftpdgfyrTGDLVRRTPDGYLVVEGRAKDQINRG-GEKIAAEEVENLLLAHPAVHDAAV 462
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
125-392 |
7.69e-16 |
|
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: 80.41 E-value: 7.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 125 TARITFTSGSTGTPKGICLSADHMLTVAQSIVAAVGAEHAGRHLALLPPGILLETVAGFFPTLLAGGCYVCPPQamigF- 203
Cdd:cd05934 83 PASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLLPR----Fs 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 204 ADPFRPDfvkaatiIAEQRITSLILVPeyleglvrVMETTGLRLPLL------TLVAVGGARTSIPLMDRA-RRLGLPIR 276
Cdd:cd05934 159 ASRFWSD-------VRRYGATVTNYLG--------AMLSYLLAQPPSpddrahRLRAAYGAPNPPELHEEFeERFGVRLL 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 277 QGYGLTECASVVSLQDAGDDDPSSVGRCLPHMTVRVADD----------GEIILDGPVCLGAVGG-----EA-----PGS 336
Cdd:cd05934 224 EGYGMTETIVGVIGPRDEPRRPGSIGRPAPGYEVRIVDDdgqelpagepGELVIRGLRGWGFFKGyynmpEAtaeamRNG 303
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2741210702 337 PLQTGDIGSIDSDGRLHIEGRKSNLIITSfGRNISPEWVEAALVEQPEVMQAMVYG 392
Cdd:cd05934 304 WFHTGDLGYRDADGFFYFVDRKKDMIRRR-GENISSAEVERAILRHPAVREAAVVA 358
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
126-392 |
3.52e-15 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 79.02 E-value: 3.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 126 ARITFTSGSTGTPKGIclsadhMLTvAQSIVAAVGAEHAGRHLA-----LLP-PgilLETVAGFF----PTLLAGGCYVc 195
Cdd:PRK06087 190 AAVLFTSGTEGLPKGV------MLT-HNNILASERAYCARLNLTwqdvfMMPaP---LGHATGFLhgvtAPFLIGARSV- 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 196 ppqamigFADPFRPDfvKAATIIAEQRITSLILVPEYLEGLVRVMETTGLRLPLLTLVAVGGARTSIPLMDRARRLGLPI 275
Cdd:PRK06087 259 -------LLDIFTPD--ACLALLEQQRCTCMLGATPFIYDLLNLLEKQPADLSALRFFLCGGTTIPKKVARECQQRGIKL 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 276 RQGYGLTECA--SVVSLQDAGDDDPSSVGRCLPHMTVRVADD----------GEIILDGP-VCLGAVGG-EAPGSPLQ-- 339
Cdd:PRK06087 330 LSVYGSTESSphAVVNLDDPLSRFMHTDGYAAAGVEIKVVDEarktlppgceGEEASRGPnVFMGYLDEpELTARALDee 409
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2741210702 340 ----TGDIGSIDSDGRLHIEGRKSNLIITSfGRNISPEWVEAALVEQPEVMQAMVYG 392
Cdd:PRK06087 410 gwyySGDLCRMDEAGYIKITGRKKDIIVRG-GENISSREVEDILLQHPKIHDACVVA 465
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
80-406 |
1.41e-14 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 77.45 E-value: 1.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 80 SLPAFFTREQSRHAIALCGADPDPIQS-PSGTA--------------RSRRSASVPLPRGTARITFTSGSTGTPKGICLS 144
Cdd:PLN02736 163 TLLSCLSEIPSVRLIVVVGGADEPLPSlPSGTGveivtyskllaqgrSSPQPFRPPKPEDVATICYTSGTTGTPKGVVLT 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 145 adHMLTVAQSIVAAVGAEH--AGRHLALLPPGILLETVaGFFPTLLAGgcyvcppqAMIGFadpFRPDFVKAATIIAEQR 222
Cdd:PLN02736 243 --HGNLIANVAGSSLSTKFypSDVHISYLPLAHIYERV-NQIVMLHYG--------VAVGF---YQGDNLKLMDDLAALR 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 223 ITSLILVPE-----YLEGLVRVMETTGLRLPLLTLV------AVGGARTSIPLMDR------ARRLGLPIR--------- 276
Cdd:PLN02736 309 PTIFCSVPRlynriYDGITNAVKESGGLKERLFNAAynakkqALENGKNPSPMWDRlvfnkiKAKLGGRVRfmssgaspl 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 277 -----------------QGYGLTECASVVSLQDAGDDDPSSVGRCLPHMTVRVAD--------------DGEIILDGP-V 324
Cdd:PLN02736 389 spdvmeflricfggrvlEGYGMTETSCVISGMDEGDNLSGHVGSPNPACEVKLVDvpemnytsedqpypRGEICVRGPiI 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 325 CLGAVGGEA-------PGSPLQTGDIGSIDSDGRLHIEGRKSNLIITSFGRNISPEWVEAALVEQPEVMQAMVYGDGL-P 396
Cdd:PLN02736 469 FKGYYKDEVqtrevidEDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLAQGEYIAPEKIENVYAKCKFVAQCFVYGDSLnS 548
|
410
....*....|
gi 2741210702 397 TPAALLVPSH 406
Cdd:PLN02736 549 SLVAVVVVDP 558
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
130-392 |
2.94e-14 |
|
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: 75.63 E-value: 2.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 130 FTSGSTGTPKGICLSADHMLTVAQSIVAAVGAEHAGRHLALLPPG--------ILLETVAGFFPTLLAGGcyvcppqami 201
Cdd:cd05973 95 FTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRPEDSFWNAADPGwayglyyaITGPLALGHPTILLEGG---------- 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 202 gfadpFRPDFVkaATIIAEQRITSLILVPEYLEGLVRVMETTGLRLPLLTLVAVGGARTSIPLMDR--ARRLGLPIRQGY 279
Cdd:cd05973 165 -----FSVEST--WRVIERLGVTNLAGSPTAYRLLMAAGAEVPARPKGRLRRVSSAGEPLTPEVIRwfDAALGVPIHDHY 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 280 GLTECASVVSlQDAGDDDP---SSVGRCLPHMTVRVADDGEIILdGPVCLGAVGGEAPGSPL------------------ 338
Cdd:cd05973 238 GQTELGMVLA-NHHALEHPvhaGSAGRAMPGWRVAVLDDDGDEL-GPGEPGRLAIDIANSPLmwfrgyqlpdtpaidggy 315
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2741210702 339 -QTGDIGSIDSDGRLHIEGRKSNLIITSfGRNISPEWVEAALVEQPEVMQAMVYG 392
Cdd:cd05973 316 yLTGDTVEFDPDGSFSFIGRADDVITMS-GYRIGPFDVESALIEHPAVAEAAVIG 369
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
130-392 |
3.73e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 75.59 E-value: 3.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 130 FTSGSTGTPKGICLSADHMLTVAQSIVAAVGAEHAGRhlaLLPPGILLET--VAGFFPTLLAGGCYVCPPQamigfadpF 207
Cdd:PRK07638 150 FTSGSTGKPKAFLRAQQSWLHSFDCNVHDFHMKREDS---VLIAGTLVHSlfLYGAISTLYVGQTVHLMRK--------F 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 208 RPDFVKAAtiIAEQRITSLILVPEYLEGLVRVMETtgLRLPLLtlVAVGGARTSIPLMDRA--RRLGLPIRQGYGLTECA 285
Cdd:PRK07638 219 IPNQVLDK--LETENISVMYTVPTMLESLYKENRV--IENKMK--IISSGAKWEAEAKEKIknIFPYAKLYEFYGASELS 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 286 SVVSLQDAGDD-DPSSVGRCLPHMTVRVAD-DGEIILDGPV----------CLGAVGGEAPGSPLQ------TGDIGSID 347
Cdd:PRK07638 293 FVTALVDEESErRPNSVGRPFHNVQVRICNeAGEEVQKGEIgtvyvkspqfFMGYIIGGVLARELNadgwmtVRDVGYED 372
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2741210702 348 SDGRLHIEGRKSNLIITSfGRNISPEWVEAALVEQPEVMQAMVYG 392
Cdd:PRK07638 373 EEGFIYIVGREKNMILFG-GINIFPEEIESVLHEHPAVDEIVVIG 416
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
41-392 |
5.28e-14 |
|
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: 74.85 E-value: 5.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 41 SLAMMARfETDRAVALQSDHGAETSiVELALLRAKIPVLSLPAFftreqsrhAIALCGA---------DPDPIQSPSGTA 111
Cdd:cd05969 2 TFAQLKV-LSARFANVLKSLGVGKG-DRVFVLSPRSPELYFSML--------GIGKIGAvicplfsafGPEAIRDRLENS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 112 RSRRSASVP------LPRGTARITFTSGSTGTPKGICLSADHMLTVAQSivaavgaehAGRHLALLP---------PGIL 176
Cdd:cd05969 72 EAKVLITTEelyertDPEDPTLLHYTSGTTGTPKGVLHVHDAMIFYYFT---------GKYVLDLHPddiywctadPGWV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 177 LETVAGFFPTLLAGgcyvCPpqaMIGFADPFRPDfvKAATIIAEQRITSLILVPEYLEGLVR--VMETTGLRLPLLTLVA 254
Cdd:cd05969 143 TGTVYGIWAPWLNG----VT---NVVYEGRFDAE--SWYGIIERVKVTVWYTAPTAIRMLMKegDELARKYDLSSLRFIH 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 255 VGGArtsiPLMDRARR-----LGLPIRQGYGLTECASVVSLQDAGDD-DPSSVGRCLPHMTVRVAD----------DGEI 318
Cdd:cd05969 214 SVGE----PLNPEAIRwgmevFGVPIHDTWWQTETGSIMIANYPCMPiKPGSMGKPLPGVKAAVVDengnelppgtKGIL 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 319 IL--DGPVCLGAVGGEA-------PGSPLQTGDIGSIDSDGRLHIEGRKSNLIITSfGRNISPEWVEAALVEQPEVMQAM 389
Cdd:cd05969 290 ALkpGWPSMFRGIWNDEeryknsfIDGWYLTGDLAYRDEDGYFWFVGRADDIIKTS-GHRVGPFEVESALMEHPAVAEAG 368
|
...
gi 2741210702 390 VYG 392
Cdd:cd05969 369 VIG 371
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
95-399 |
1.52e-13 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 73.88 E-value: 1.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 95 ALCGADPD--PIQSPSGTARSRRSASVPLPRGT----ARITFTSGSTGTPKGICLSadH---MLTVAQsivaavgaehaG 165
Cdd:PRK05605 185 ALTGPAPGtvPWETLVDAAIGGDGSDVSHPRPTpddvALILYTSGTTGKPKGAQLT--HrnlFANAAQ-----------G 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 166 RH-LALLPPGIllETVAGFFPTLLAGGCYVCPPQAM-IG----FADPFRPDFVKAAtiIAEQRITSLILVPEYLEGLVRV 239
Cdd:PRK05605 252 KAwVPGLGDGP--ERVLAALPMFHAYGLTLCLTLAVsIGgelvLLPAPDIDLILDA--MKKHPPTWLPGVPPLYEKIAEA 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 240 METTGLRLPLLTlVAVGGArTSIPLMDRAR---RLGLPIRQGYGLTECASVVSLQDAGDD-DPSSVGRCLPHMTVRVAD- 314
Cdd:PRK05605 328 AEERGVDLSGVR-NAFSGA-MALPVSTVELwekLTGGLLVEGYGLTETSPIIVGNPMSDDrRPGYVGVPFPDTEVRIVDp 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 315 -----------DGEIILDGP-VCLGAVGGEAPGSP------LQTGDIGSIDSDGRLHIEGRKSNLIITSfGRNISPEWVE 376
Cdd:PRK05605 406 edpdetmpdgeEGELLVRGPqVFKGYWNRPEETAKsfldgwFRTGDVVVMEEDGFIRIVDRIKELIITG-GFNVYPAEVE 484
|
330 340
....*....|....*....|...
gi 2741210702 377 AALVEQPEVMQAMVYgdGLPTPA 399
Cdd:PRK05605 485 EVLREHPGVEDAAVV--GLPRED 505
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
125-404 |
1.97e-13 |
|
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: 72.90 E-value: 1.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 125 TARITFTSGSTGTPKGICLSADHMLTVAQSI-VAAVGAEHAGRHLALLPPGILLETVAGFFPTLLAGGCYVCPPQAMigf 203
Cdd:cd05958 99 ICILAFTSGTTGAPKATMHFHRDPLASADRYaVNVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEEAT--- 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 204 adpfrPDfvKAATIIAEQRITSLILVPEYLEGLVRVMETTGLRLPLLTLVAVGGARTSIPLMDRARR-LGLPIRQGYGLT 282
Cdd:cd05958 176 -----PD--LLLSAIARYKPTVLFTAPTAYRAMLAHPDAAGPDLSSLRKCVSAGEALPAALHRAWKEaTGIPIIDGIGST 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 283 ECASVVSLQDAGDDDPSSVGRCLPHMTVRVADD-GEIILDGPVCLGAVGGEA--------------PGSPLQTGDIGSID 347
Cdd:cd05958 249 EMFHIFISARPGDARPGATGKPVPGYEAKVVDDeGNPVPDGTIGRLAVRGPTgcryladkrqrtyvQGGWNITGDTYSRD 328
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2741210702 348 SDGRLHIEGRKSNLIITSfGRNISPEWVEAALVEQPEVMQAMVYgdGLPTPAALLVP 404
Cdd:cd05958 329 PDGYFRHQGRSDDMIVSG-GYNIAPPEVEDVLLQHPAVAECAVV--GHPDESRGVVV 382
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
120-385 |
3.98e-13 |
|
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: 72.31 E-value: 3.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 120 PLPRGTARITFTSGSTGTPKGICLSADHMLTVAQSIVAAVGAEHAGRHLALLPpgilLETVAG-----FFPTLLAGGCYV 194
Cdd:cd05906 164 SRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVP----LDHVGGlvelhLRAVYLGCQQVH 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 195 CPPQAMIgfADPFRpdFVKaatIIAEQRIT-------SLILVPEYLEglvRVMETTGLRLPLLTLVaVGG----ARTSIP 263
Cdd:cd05906 240 VPTEEIL--ADPLR--WLD---LIDRYRVTitwapnfAFALLNDLLE---EIEDGTWDLSSLRYLV-NAGeavvAKTIRR 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 264 LMDRARRLGLP---IRQGYGLTECASVV------SLQDAGDDDP-SSVGRCLPHMTVRVADD----------GEIILDGP 323
Cdd:cd05906 309 LLRLLEPYGLPpdaIRPAFGMTETCSGViysrsfPTYDHSQALEfVSLGRPIPGVSMRIVDDegqllpegevGRLQVRGP 388
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 324 VCLG------AVGGEA--PGSPLQTGDIGSIDsDGRLHIEGRKSNLIITSfGRNISPEWVEAALVEQPEV 385
Cdd:cd05906 389 VVTKgyynnpEANAEAftEDGWFRTGDLGFLD-NGNLTITGRTKDTIIVN-GVNYYSHEIEAAVEEVPGV 456
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
15-407 |
5.28e-13 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 73.07 E-value: 5.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 15 PQRIALdALDGAPITYGALWAELGERSLAMMAR-FETDRAVALQSDHGAETSIVELALLRAKIPVLSLPAFFTREQSRHA 93
Cdd:PRK12316 4565 PDAVAV-VFDEEKLTYAELNRRANRLAHALIARgVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYM 4643
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 94 IALCGAD--------------PDPIQS----PSG--TARSRRSASVPL-PRGTARITFTSGSTGTPKGICLSADHMLTVA 152
Cdd:PRK12316 4644 MEDSGAAllltqshllqrlpiPDGLASlaldRDEdwEGFPAHDPAVRLhPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHL 4723
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 153 QSIVAAVGAEHAGRHLALLPPGILLeTVAGFFPTLLAGGCYVCPPQamiGFADPfrpdfvkAATI--IAEQRITSLILVP 230
Cdd:PRK12316 4724 HATGERYELTPDDRVLQFMSFSFDG-SHEGLYHPLINGASVVIRDD---SLWDP-------ERLYaeIHEHRVTVLVFPP 4792
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 231 EYLEGLVRVMETTGlRLPLLTLVAVGGARTSIPLMDRARRLGLPIR--QGYGLTECASVVSLQDAGDDDPSS-----VGR 303
Cdd:PRK12316 4793 VYLQQLAEHAERDG-EPPSLRVYCFGGEAVAQASYDLAWRALKPVYlfNGYGPTETTVTVLLWKARDGDACGaaympIGT 4871
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 304 CLPHMTVRVADDGEiildGPVCLGAVG-----GE-----------------------APGSPL-QTGDIGSIDSDGRLHI 354
Cdd:PRK12316 4872 PLGNRSGYVLDGQL----NPLPVGVAGelylgGEgvargylerpaltaerfvpdpfgAPGGRLyRTGDLARYRADGVIDY 4947
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 2741210702 355 EGRKSNLI-ITSFgrNISPEWVEAALVEQPEVMQAMVY---GDGLPTPAALLVPSHP 407
Cdd:PRK12316 4948 LGRVDHQVkIRGF--RIELGEIEARLREHPAVREAVVIaqeGAVGKQLVGYVVPQDP 5002
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
15-425 |
6.22e-13 |
|
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: 71.57 E-value: 6.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 15 PQRIALdALDGAPITYGalwaELGERS--LAMMARFE---TDRAVALQSDHGAETSIVELALLRAKIPVLSLPAFFTREQ 89
Cdd:cd17643 1 PEAVAV-VDEDRRLTYG----ELDARAnrLARTLRAEgvgPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 90 SRHAIAlcgadpdpiqspsgtaRSRRSASVPLPRGTARITFTSGSTGTPKGIclsadhmlTVAQSIVAAVGAeHAGRHLA 169
Cdd:cd17643 76 IAFILA----------------DSGPSLLLTDPDDLAYVIYTSGSTGRPKGV--------VVSHANVLALFA-ATQRWFG 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 170 LLPPGI-LLETVAGF-------FPTLLAGGCYVCPPQAMigfadpfRPDFVKAATIIAEQRITSLILVPEYLEGLVRVME 241
Cdd:cd17643 131 FNEDDVwTLFHSYAFdfsvweiWGALLHGGRLVVVPYEV-------ARSPEDFARLLRDEGVTVLNQTPSAFYQLVEAAD 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 242 TTGLRLPLLTLVAVGGARTSIPLMDR-ARRLGLPIRQ---GYGLTEcASV------VSLQDAGDDDPSSVGRCLPHMTVR 311
Cdd:cd17643 204 RDGRDPLALRYVIFGGEALEAAMLRPwAGRFGLDRPQlvnMYGITE-TTVhvtfrpLDAADLPAAAASPIGRPLPGLRVY 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 312 VADD----------GEIILDGP-VCLGAVGGEA-------------PGSPL-QTGDIGSIDSDGRLHIEGRKSNLIITSf 366
Cdd:cd17643 283 VLDAdgrpvppgvvGELYVSGAgVARGYLGRPEltaerfvanpfggPGSRMyRTGDLARRLPDGELEYLGRADEQVKIR- 361
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2741210702 367 GRNISPEWVEAALVEQPEVMQAMV----YGDGLPTPAALLVP-SHPDADLAAAVARANEKLPAY 425
Cdd:cd17643 362 GFRIELGEIEAALATHPSVRDAAVivreDEPGDTRLVAYVVAdDGAAADIAELRALLKELLPDY 425
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
54-390 |
6.29e-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: 71.34 E-value: 6.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 54 VALQSDHGAETSIVELALLRAKIPVLSLPAFFTREQSRHAIALCGADpdpiqspsgtarsrrsASVPLPRGTARITFTSG 133
Cdd:cd17650 40 VGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYMLEDSGAK----------------LLLTQPEDLAYVIYTSG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 134 STGTPKGIclsadhMLTvAQSIVAAVGAEHAGRHLALLPPGIL------LETVAG-FFPTLLAGGC-YVCPpqamigfaD 205
Cdd:cd17650 104 TTGKPKGV------MVE-HRNVAHAAHAWRREYELDSFPVRLLqmasfsFDVFAGdFARSLLNGGTlVICP--------D 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 206 PFRPDFVKAATIIAEQRITSLILVPEYLEGLVRVMETTGLRLPLLTLVAVGGARTSIP-LMDRARRLGLPIR--QGYGLT 282
Cdd:cd17650 169 EVKLDPAALYDLILKSRITLMESTPALIRPVMAYVYRNGLDLSAMRLLIVGSDGCKAQdFKTLAARFGQGMRiiNSYGVT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 283 EcASVVSLQDAGDDDP------SSVGRCLPHMTVRVADD----------GEIILDGP-VCLGAVGGE------------A 333
Cdd:cd17650 249 E-ATIDSTYYEEGRDPlgdsanVPIGRPLPNTAMYVLDErlqpqpvgvaGELYIGGAgVARGYLNRPeltaerfvenpfA 327
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 2741210702 334 PGSPL-QTGDIGSIDSDGRLHIEGRKSNLIITSfGRNISPEWVEAALVEQPEVMQAMV 390
Cdd:cd17650 328 PGERMyRTGDLARWRADGNVELLGRVDHQVKIR-GFRIELGEIESQLARHPAIDEAVV 384
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
15-388 |
7.46e-13 |
|
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: 71.50 E-value: 7.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 15 PQRIALDALDGAPITYGAL-WAELGERSLAMMARFETD----RAVALQSDHGAETSIVELALLRAK-IPV-LSLPA-FFT 86
Cdd:cd05931 7 PDRPAYTFLDDEGGREETLtYAELDRRARAIAARLQAVgkpgDRVLLLAPPGLDFVAAFLGCLYAGaIAVpLPPPTpGRH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 87 REQSRHAIALCGA-----DPDPIQSPSGTARSRRSASVPL---------------------PRGTARITFTSGSTGTPKG 140
Cdd:cd05931 87 AERLAAILADAGPrvvltTAAALAAVRAFAASRPAAGTPRllvvdllpdtsaadwpppspdPDDIAYLQYTSGSTGTPKG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 141 ICLSADHMLTVAQSIVAAVGAEHAGRHLALLPP----GIlletVAGFFPTLLAGG-CYVCPPQAMIgfADPFRpdFVKAa 215
Cdd:cd05931 167 VVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLyhdmGL----IGGLLTPLYSGGpSVLMSPAAFL--RRPLR--WLRL- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 216 tiIAEQRITsLILVP----EYLEGLVRVMETTGLRLPLLTLVAVGGARTSIPLMDR-ARR---LGLP---IRQGYGLTEC 284
Cdd:cd05931 238 --ISRYRAT-ISAAPnfayDLCVRRVRDEDLEGLDLSSWRVALNGAEPVRPATLRRfAEAfapFGFRpeaFRPSYGLAEA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 285 ASVVSLQDAGD---------------------DDPS-----SVGRCLPHMTVRVADD-----------GEIILDGP-VCL 326
Cdd:cd05931 315 TLFVSGGPPGTgpvvlrvdrdalagravavaaDDPAarelvSCGRPLPDQEVRIVDPetgrelpdgevGEIWVRGPsVAS 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2741210702 327 G-------------AVGGEAPGSPLQTGDIGSIdSDGRLHIEGRKSNLIITSfGRNISPEWVEAALVEQPEVMQA 388
Cdd:cd05931 395 GywgrpeataetfgALAATDEGGWLRTGDLGFL-HDGELYITGRLKDLIIVR-GRNHYPQDIEATAEEAHPALRP 467
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
122-381 |
8.55e-13 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 71.39 E-value: 8.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 122 PRGTARITFTSGSTGTPKGICLSADHMLTVAQSIVAAVGAEHAGRHLALLPP----GIlleTVAGFFPtLLAGGCYVcpp 197
Cdd:PRK06334 182 PEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSFLPPfhayGF---NSCTLFP-LLSGVPVV--- 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 198 qamigFA-DPFRPDfvKAATIIAEQRITSLILVPEYLEGLVRVMETTGLRLPLLTLVAVGGARTSIPLMDRARRL--GLP 274
Cdd:PRK06334 255 -----FAyNPLYPK--KIVEMIDEAKVTFLGSTPVFFDYILKTAKKQESCLPSLRFVVIGGDAFKDSLYQEALKTfpHIQ 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 275 IRQGYGLTECASVVSLQDAGD-DDPSSVGRCLPHMTVRVADDGEIIldgPVCLGAVG--------------GEAPGSPL- 338
Cdd:PRK06334 328 LRQGYGTTECSPVITINTVNSpKHESCVGMPIRGMDVLIVSEETKV---PVSSGETGlvltrgtslfsgylGEDFGQGFv 404
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2741210702 339 --------QTGDIGSIDSDGRLHIEGRKSNLIITSfGRNISPEWVEAALVE 381
Cdd:PRK06334 405 elggetwyVTGDLGYVDRHGELFLKGRLSRFVKIG-AEMVSLEALESILME 454
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
111-357 |
9.74e-13 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 71.92 E-value: 9.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 111 ARSRRSASVPLPRGTARITFTSGSTGTPKGICLSADHMLTVAQSIVAAVGAEHAGRHLALLP--------PGILLETVAG 182
Cdd:PRK06814 781 RFPLVYFCNRDPDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARIDFSPEDKVFNALPvfhsfgltGGLVLPLLSG 860
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 183 FfPTLLaggcYVCPPQAMIgfadpfRPDFVKA--ATIiaeqritsLILVPEYLEGLVRVMETTGLRLplLTLVaVGGARt 260
Cdd:PRK06814 861 V-KVFL----YPSPLHYRI------IPELIYDtnATI--------LFGTDTFLNGYARYAHPYDFRS--LRYV-FAGAE- 917
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 261 siPLMDRARRL-----GLPIRQGYGLTECASVVSLQDAGDDDPSSVGRCLPHMTVR------VADDGEIILDGP-VCLGA 328
Cdd:PRK06814 918 --KVKEETRQTwmekfGIRILEGYGVTETAPVIALNTPMHNKAGTVGRLLPGIEYRlepvpgIDEGGRLFVRGPnVMLGY 995
|
250 260 270
....*....|....*....|....*....|....*.
gi 2741210702 329 VGGEAPGS--PLQ-----TGDIGSIDSDGRLHIEGR 357
Cdd:PRK06814 996 LRAENPGVlePPAdgwydTGDIVTIDEEGFITIKGR 1031
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
15-407 |
1.18e-12 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 71.73 E-value: 1.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 15 PQRIALdALDGAPITYGALWAELGErsLAMMARFE---TDRAVALQSDHGAETSIVELALLRAKIPVLSLPAFFTREQSR 91
Cdd:PRK12467 526 PERPAL-VFGEQVLSYAELNRQANR--LAHVLIAAgvgPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLA 602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 92 HAI-------------------------ALCGADPDPIQSpsgtARSRRSASVPL-PRGTARITFTSGSTGTPKGICLSA 145
Cdd:PRK12467 603 YMLddsgvrllltqshllaqlpvpaglrSLCLDEPADLLC----GYSGHNPEVALdPDNLAYVIYTSGSTGQPKGVAISH 678
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 146 DHMLTVAQSIVAAVGAEHAGRHLALLPPGILLeTVAGFFPTLLAGGCYVCPPQAMIGFADPFrpdfvkaATIIAEQRITS 225
Cdd:PRK12467 679 GALANYVCVIAERLQLAADDSMLMVSTFAFDL-GVTELFGALASGATLHLLPPDCARDAEAF-------AALMADQGVTV 750
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 226 LILVPEYLEGLVRVMETTGLRlPLLTLVaVGGARTSIPLMDRARRLGLPIR--QGYGLTECASVVSLQDAGDDD----PS 299
Cdd:PRK12467 751 LKIVPSHLQALLQASRVALPR-PQRALV-CGGEALQVDLLARVRALGPGARliNHYGPTETTVGVSTYELSDEErdfgNV 828
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 300 SVGRCLPHMTVRvaddgeiILDG---PVCLGAVG-----GE-----------------------APGSPL-QTGDIGSID 347
Cdd:PRK12467 829 PIGQPLANLGLY-------ILDHylnPVPVGVVGelyigGAglargyhrrpaltaerfvpdpfgADGGRLyRTGDLARYR 901
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2741210702 348 SDGRLHIEGRKSNLIITSfGRNISPEWVEAALVEQPEVMQAMVY---GDGLPTPAALLVPSHP 407
Cdd:PRK12467 902 ADGVIEYLGRMDHQVKIR-GFRIELGEIEARLLAQPGVREAVVLaqpGDAGLQLVAYLVPAAV 963
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
15-426 |
1.69e-12 |
|
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: 70.04 E-value: 1.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 15 PQRIALDALDGApITYgalwAELGERSLAMMAR-----FETDRAVALQSDHGAETSIVELALLRAKIPVLSLPAFFTREQ 89
Cdd:cd12115 13 PDAIALVCGDES-LTY----AELNRRANRLAARlraagVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPER 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 90 SRHAIAlcgadpdpiqspsgtaRSRRSASVPLPRGTARITFTSGSTGTPKGICLSADHMLTVAQSIVAAVGAEHAGRHLA 169
Cdd:cd12115 88 LRFILE----------------DAQARLVLTDPDDLAYVIYTSGSTGRPKGVAIEHRNAAAFLQWAAAAFSAEELAGVLA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 170 LLPPGILLeTVAGFFPTLLAGGCYVCPPQAMIGFADPFRPDfvkaatiiaeqriTSLI-LVPEYLEGLVRVME-TTGLRl 247
Cdd:cd12115 152 STSICFDL-SVFELFGPLATGGKVVLADNVLALPDLPAAAE-------------VTLInTVPSAAAELLRHDAlPASVR- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 248 plltLVAVGGARTSIPLMDRARRLgLPIRQG---YGLTECA--SVVSLQDAGDDDPSSVGRCLPHMTVRVADD------- 315
Cdd:cd12115 217 ----VVNLAGEPLPRDLVQRLYAR-LQVERVvnlYGPSEDTtySTVAPVPPGASGEVSIGRPLANTQAYVLDRalqpvpl 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 316 ---GEIILDGP-VCLGAVG------------GEAPGSPL-QTGDIGSIDSDGRLHIEGRKSNLIITSfGRNISPEWVEAA 378
Cdd:cd12115 292 gvpGELYIGGAgVARGYLGrpgltaerflpdPFGPGARLyRTGDLVRWRPDGLLEFLGRADNQVKVR-GFRIELGEIEAA 370
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 2741210702 379 LVEQPEVMQA--MVYGDGLPTP--AALLVPSHPDADLAAA-VARANEKLPAYA 426
Cdd:cd12115 371 LRSIPGVREAvvVAIGDAAGERrlVAYIVAEPGAAGLVEDlRRHLGTRLPAYM 423
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
29-392 |
1.98e-12 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 70.11 E-value: 1.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 29 TYGALWaeLGERSLAMMARFETDRAVALQSDHGAETSIVELALLR-------AKIPVLSLPaffT----REQSRHAIALC 97
Cdd:PRK12406 53 AYAAMR--LGAYAVPVNWHFKPEEIAYILEDSGARVLIAHADLLHglasalpAGVTVLSVP---TppeiAAAYRISPALL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 98 GADPDPIQSPSGTARSRRSASVPLPrGTARITFTSGSTGTPKGICLSADhmlTVAQSIVAAVGAEHA-GrhlalLPPGIL 176
Cdd:PRK12406 128 TPPAGAIDWEGWLAQQEPYDGPPVP-QPQSMIYTSGTTGHPKGVRRAAP---TPEQAAAAEQMRALIyG-----LKPGIR 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 177 letvagffpTLLAGGCYVCPPQAM------IGFADPFRPDFVKAAT--IIAEQRITSLILVPEYLEGLVRVMETTGLRLP 248
Cdd:PRK12406 199 ---------ALLTGPLYHSAPNAYglragrLGGVLVLQPRFDPEELlqLIERHRITHMHMVPTMFIRLLKLPEEVRAKYD 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 249 LLTLVAVGGARTSIPlMDRARRL----GLPIRQGYGLTEcASVVSLQDAGD--DDPSSVGRCLPHMTVR-VADDGEIILD 321
Cdd:PRK12406 270 VSSLRHVIHAAAPCP-ADVKRAMiewwGPVIYEYYGSTE-SGAVTFATSEDalSHPGTVGKAAPGAELRfVDEDGRPLPQ 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 322 GPVclGAVGGEAPGSPLQT-------------------GDIGSIDSDGRLHIEGRKSNLIItSFGRNISPEWVEAALVEQ 382
Cdd:PRK12406 348 GEI--GEIYSRIAGNPDFTyhnkpekraeidrggfitsGDVGYLDADGYLFLCDRKRDMVI-SGGVNIYPAEIEAVLHAV 424
|
410
....*....|
gi 2741210702 383 PEVMQAMVYG 392
Cdd:PRK12406 425 PGVHDCAVFG 434
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
130-404 |
2.06e-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: 69.52 E-value: 2.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 130 FTSGSTGTPKGICLSADHMLTVAQSIVAAVGAEHAGRHLALLPPGILLETVAGFFPTLLAGGCYVCPPQAmigfadpfRP 209
Cdd:cd05974 92 FTSGTTSKPKLVEHTHRSYPVGHLSTMYWIGLKPGDVHWNISSPGWAKHAWSCFFAPWNAGATVFLFNYA--------RF 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 210 DFVKAATIIAEQRITSLILVPEYLEGLVRvMETTGLRLPLLTLVAVGGartsiPL----MDRARRL-GLPIRQGYGLTEC 284
Cdd:cd05974 164 DAKRVLAALVRYGVTTLCAPPTVWRMLIQ-QDLASFDVKLREVVGAGE-----PLnpevIEQVRRAwGLTIRDGYGQTET 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 285 ASVVSLQDAGDDDPSSVGRCLPHMTVRV-------ADDGEIILD----GPVCL--------GAVGGEAPGSPLQTGDIGS 345
Cdd:cd05974 238 TALVGNSPGQPVKAGSMGRPLPGYRVALldpdgapATEGEVALDlgdtRPVGLmkgyagdpDKTAHAMRGGYYRTGDIAM 317
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2741210702 346 IDSDGRLHIEGRKSNLIITSFGRnISPEWVEAALVEQPEVMQAMVYGDglPTPAALLVP 404
Cdd:cd05974 318 RDEDGYLTYVGRADDVFKSSDYR-ISPFELESVLIEHPAVAEAAVVPS--PDPVRLSVP 373
|
|
| TenA |
COG0819 |
Aminopyrimidine aminohydrolase TenA (thiamine salvage pathway) [Coenzyme transport and ... |
466-665 |
3.24e-12 |
|
Aminopyrimidine aminohydrolase TenA (thiamine salvage pathway) [Coenzyme transport and metabolism];
Pssm-ID: 440581 [Multi-domain] Cd Length: 218 Bit Score: 66.44 E-value: 3.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 466 FFTELEARTVRERLRFLAVPQLQAGLNGTISRGAYLDYLEQAYHHVRHTVPLMQAARARLTDRADIVAALDdyIAEETGH 545
Cdd:COG0819 3 FSERLREAAAPIWEAILEHPFVQGLADGTLPREAFRHYLVQDYLYLEHFARALALAAAKAPDLEDMRFLAG--LAAGLLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 546 EE--WILSDIAAAGGDAEAVRASKPGPATAAMVDHAYARIANGNAMAFFGMVYVLEsvsvafatRGAAAVAKKL---GLP 620
Cdd:COG0819 81 VElaLHERYAAELGISEEELEATPPSPTTRAYTSYLLAAAASGDYAELLAALLPCE--------WGYAEIGKRLaerPLP 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2741210702 621 PQAF--TYLTSHGAldqehmTFFANLVNGLDDPADR------DAILSMAQEIF 665
Cdd:COG0819 153 PDHPyaEWIETYAS------EEFQELVEWLIALLDRlaatasEAERERLEEAF 199
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
34-392 |
4.46e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 68.86 E-value: 4.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 34 WAELGERSLAMMARFETDRAVALQSDHGAETSIVELALLRAKIPVLSLPAFFTREQSRH------AIALCGADPD----- 102
Cdd:PRK07787 28 RSDLAGAATAVAERVAGARRVAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAERRHiladsgAQAWLGPAPDdpagl 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 103 PIQSPSGTARSRRSASVPLPRGTARITFTSGSTGTPKGICLSAdhmLTVAQSIVAAVGA---------EHAgrhlalLPP 173
Cdd:PRK07787 108 PHVPVRLHARSWHRYPEPDPDAPALIVYTSGTTGPPKGVVLSR---RAIAADLDALAEAwqwtaddvlVHG------LPL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 174 GILLETVAGFFPTLLAGGCYVcppqamigFADPFRPDFVKAAtiiAEQRITSLILVPEYLEGLVRVMETTGLRLPLLTLV 253
Cdd:PRK07787 179 FHVHGLVLGVLGPLRIGNRFV--------HTGRPTPEAYAQA---LSEGGTLYFGVPTVWSRIAADPEAARALRGARLLV 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 254 AvGGARTSIPLMDRARRL-GLPIRQGYGLTECASVVSLQDAGDDDPSSVGRCLPHMTVRVAD--------DGEIILDGPV 324
Cdd:PRK07787 248 S-GSAALPVPVFDRLAALtGHRPVERYGMTETLITLSTRADGERRPGWVGLPLAGVETRLVDedggpvphDGETVGELQV 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 325 CLGAVGGEAPGSP------------LQTGDIGSIDSDGRLHIEGRKSNLIITSFGRNISPEWVEAALVEQPEVMQAMVYG 392
Cdd:PRK07787 327 RGPTLFDGYLNRPdataaaftadgwFRTGDVAVVDPDGMHRIVGRESTDLIKSGGYRIGAGEIETALLGHPGVREAAVVG 406
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
26-362 |
1.02e-11 |
|
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: 67.50 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 26 APITYGALWAELGERSLAMMARFET-DRAVALQSDHGAETSIVELALLRAKIPVLSLPAFFTREQSRHAIALCG-----A 99
Cdd:cd17654 15 TTVSYADLAEKISNLSNFLRKKFQTeERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKCHvsyllQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 100 DPDPIQSPSGTARSRRSASVPLPRGTARITFTSGSTGTPKGIclsadhmLTVAQSIVAAVgaEHAGRHLALLPPGILLET 179
Cdd:cd17654 95 NKELDNAPLSFTPEHRHFNIRTDECLAYVIHTSGTTGTPKIV-------AVPHKCILPNI--QHFRSLFNITSEDILFLT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 180 --------VAGFFPTLLAGGCYVCPPQAMigfadpfRPDFVKAATIIAE-QRITSLILVPEYLEGL--VRVMETTGLRLP 248
Cdd:cd17654 166 spltfdpsVVEIFLSLSSGATLLIVPTSV-------KVLPSKLADILFKrHRITVLQATPTLFRRFgsQSIKSTVLSATS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 249 LLTLVAVGGARTSIPLMDRARR---LGLPIRQGYGLTECASVVSLQDAGDDD-PSSVGRCLPHMTVRVADDGEIILDGPV 324
Cdd:cd17654 239 SLRVLALGGEPFPSLVILSSWRgkgNRTRIFNIYGITEVSCWALAYKVPEEDsPVQLGSPLLGTVIEVRDQNGSEGTGQV 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 2741210702 325 clgAVGGEAPGSPLQ------------TGDIGSIdSDGRLHIEGRKSNLI 362
Cdd:cd17654 319 ---FLGGLNRVCILDdevtvpkgtmraTGDFVTV-KDGELFFLGRKDSQI 364
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
125-392 |
1.08e-11 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 67.94 E-value: 1.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 125 TARITFTSGSTGTPKGICLSADHMLTVAQSIV-------AAVGAEHAgrHLALLPP----GILLetvagFFPTLLAGGCY 193
Cdd:PLN02574 200 VAAIMYSSGTTGASKGVVLTHRNLIAMVELFVrfeasqyEYPGSDNV--YLAALPMfhiyGLSL-----FVVGLLSLGST 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 194 VCppqAMIGFadpfrpDFVKAATIIAEQRITSLILVPEYLEGLVRVME-TTGLRLPLLTLVAVGGARTSIPLMDRARRLg 272
Cdd:PLN02574 273 IV---VMRRF------DASDMVKVIDRFKVTHFPVVPPILMALTKKAKgVCGEVLKSLKQVSCGAAPLSGKFIQDFVQT- 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 273 LP---IRQGYGLTECASVVS--LQDAGDDDPSSVGRCLPHMTVRVAD-----------DGEIILDGPVCLGA--VGGEAP 334
Cdd:PLN02574 343 LPhvdFIQGYGMTESTAVGTrgFNTEKLSKYSSVGLLAPNMQAKVVDwstgcllppgnCGELWIQGPGVMKGylNNPKAT 422
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2741210702 335 GSP------LQTGDIGSIDSDGRLHIEGRKSNlIITSFGRNISPEWVEAALVEQPEVMQAMVYG 392
Cdd:PLN02574 423 QSTidkdgwLRTGDIAYFDEDGYLYIVDRLKE-IIKYKGFQIAPADLEAVLISHPEIIDAAVTA 485
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
126-407 |
1.38e-11 |
|
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: 67.10 E-value: 1.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 126 ARITFTSGSTGTPKGICLSADHMLTVAQSIvaavgaehAGRHLALLPPGILLETVAGFFPTLLAGGCY---VCPPQAMIg 202
Cdd:cd05919 94 AYLLYSSGTTGPPKGVMHAHRDPLLFADAM--------AREALGLTPGDRVFSSAKMFFGYGLGNSLWfplAVGASAVL- 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 203 faDPFRPDFVKAATIIAEQRITSLILVPEYLEGLVRVMETTGLRLPLLTLVAVGGARTSIPLMDR-ARRLGLPIRQGYGL 281
Cdd:cd05919 165 --NPGWPTAERVLATLARFRPTVLYGVPTFYANLLDSCAGSPDALRSLRLCVSAGEALPRGLGERwMEHFGGPILDGIGA 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 282 TECASVVSLQDAGDDDPSSVGRCLPHMTVR-VADDGEIILDGPVCLGAVGGEA--------PGSP--------LQTGDIG 344
Cdd:cd05919 243 TEVGHIFLSNRPGAWRLGSTGRPVPGYEIRlVDEEGHTIPPGEEGDLLVRGPSaavgywnnPEKSratfnggwYRTGDKF 322
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2741210702 345 SIDSDGRLHIEGRKSNLIITSfGRNISPEWVEAALVEQPEVMQAMVYG----DGLPTPAALLVPSHP 407
Cdd:cd05919 323 CRDADGWYTHAGRADDMLKVG-GQWVSPVEVESLIIQHPAVAEAAVVAvpesTGLSRLTAFVVLKSP 388
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
15-574 |
1.52e-11 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 68.06 E-value: 1.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 15 PQRIALDAlDGAPITYGALWAELGERSLAMMAR-FETDRAVALQSDHGAETSIVELALLRAKIPVLSLPAFFTREQSRHA 93
Cdd:PRK12316 2017 PEAIAVVF-GDQHLSYAELDSRANRLAHRLRARgVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYM 2095
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 94 IALCGADPDPIQS--------PSGTAR-------------SRRSASVPLPRGTARITFTSGSTGTPKGICLSADHMLTVA 152
Cdd:PRK12316 2096 LEDSGAALLLTQRhllerlplPAGVARlpldrdaewadypDTAPAVQLAGENLAYVIYTSGSTGLPKGVAVSHGALVAHC 2175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 153 QSIVAAVGAEHAGRHLALLPPGiLLETVAGFFPTLLAGGcyvcppQAMIGFADPFRPDFVKAAtiIAEQRITSLILVPEY 232
Cdd:PRK12316 2176 QAAGERYELSPADCELQFMSFS-FDGAHEQWFHPLLNGA------RVLIRDDELWDPEQLYDE--MERHGVTILDFPPVY 2246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 233 LEGLVRVMETTGLRLPLLTLVaVGGARTSIPLMDRARRLGLPIR--QGYGLTECASVVSLQDAGDDDPSsvGRCLPHMTV 310
Cdd:PRK12316 2247 LQQLAEHAERDGRPPAVRVYC-FGGEAVPAASLRLAWEALRPVYlfNGYGPTEAVVTPLLWKCRPQDPC--GAAYVPIGR 2323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 311 RVADDGEIILD-----------GPVCLGAVG--------------------GEAPGSPL-QTGDIGSIDSDGRLHIEGRK 358
Cdd:PRK12316 2324 ALGNRRAYILDadlnllapgmaGELYLGGEGlargylnrpgltaerfvpdpFSASGERLyRTGDLARYRADGVVEYLGRI 2403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 359 SNLI-ITSFgrNISPEWVEAALVEQPEVMQAMVY---GDGLPTPAALLVPSHP-DADLAAAVARANEKLPAYAQISAWR- 432
Cdd:PRK12316 2404 DHQVkIRGF--RIELGEIEARLQAHPAVREAVVVaqdGASGKQLVAYVVPDDAaEDLLAELRAWLAARLPAYMVPAHWVv 2481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 433 -EAAHFTPmNGQLTGNGRLRRAAIAAAYLNGPPLffTELEARTVRERLRFLAVPQLQAGLNgTISRGAYLDYLEQAYHHV 511
Cdd:PRK12316 2482 lERLPLNP-NGKLDRKALPKPDVSQLRQAYVAPQ--EGLEQRLAAIWQAVLKVEQVGLDDH-FFELGGHSLLATQVVSRV 2557
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2741210702 512 RHTVPLMQAARARLtdradivaalddyiaeetghEEWILSDIAAAGGDAEAVRASKPGPATAA 574
Cdd:PRK12316 2558 RQDLGLEVPLRILF--------------------ERPTLAAFAASLESGQTSRAPVLQKVTRV 2600
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
130-392 |
1.65e-11 |
|
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: 66.94 E-value: 1.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 130 FTSGSTGTPKGICLSADHMLTVAQSIVAAVGAEHAGRHLALLPpgilLETVAGF-FPTLLA--GGCYVCPPQamigfadp 206
Cdd:cd12118 140 YTSGTTGRPKGVVYHHRGAYLNALANILEWEMKQHPVYLWTLP----MFHCNGWcFPWTVAavGGTNVCLRK-------- 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 207 frpdfVKAATI---IAEQRITSLILVPEYLEGLVRVMETTGLRLPLLTLVAVGGARTSIPLMDRARRLGLPIRQGYGLTE 283
Cdd:cd12118 208 -----VDAKAIydlIEKHKVTHFCGAPTVLNMLANAPPSDARPLPHRVHVMTAGAPPPAAVLAKMEELGFDVTHVYGLTE 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 284 C---ASVVSLQDAGDDDPSS----------VGRCL--------PHMTVRVADD----GEIILDGPVC-LGAVGGEAP--- 334
Cdd:cd12118 283 TygpATVCAWKPEWDELPTEerarlkarqgVRYVGleevdvldPETMKPVPRDgktiGEIVFRGNIVmKGYLKNPEAtae 362
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2741210702 335 ---GSPLQTGDIGSIDSDGRLHIEGRkSNLIITSFGRNISPEWVEAALVEQPEVMQAMVYG 392
Cdd:cd12118 363 afrGGWFHSGDLAVIHPDGYIEIKDR-SKDIIISGGENISSVEVEGVLYKHPAVLEAAVVA 422
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
126-392 |
1.70e-11 |
|
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: 66.73 E-value: 1.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 126 ARITFTSGSTGTPKGICLSADHMLTVAQSIVAAVGAEHAGRHLALLPpgilLETVAGFFPTLLA----GGCYVcppqaMI 201
Cdd:cd05935 87 ALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPSDVILACLP----LFHVTGFVGSLNTavyvGGTYV-----LM 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 202 GfadpfRPDFVKAATIIAEQRITSLILVPEYLEGLVRVMETTGLRLPLLTLVAVGGARTSIPLMDRARRL-GLPIRQGYG 280
Cdd:cd05935 158 A-----RWDRETALELIEKYKVTFWTNIPTMLVDLLATPEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLtGLRFVEGYG 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 281 LTECASVVSLQ-----------------DAGDDDPSSvGRCLPhmtvrVADDGEIILDGPV--------------CLGAV 329
Cdd:cd05935 233 LTETMSQTHTNpplrpklqclgip*fgvDARVIDIET-GRELP-----PNEVGEIVVRGPQifkgywnrpeeteeSFIEI 306
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2741210702 330 GGEapgSPLQTGDIGSIDSDGRLHIEGRKSNLIITSfGRNISPEWVEAALVEQPEVMQAMVYG 392
Cdd:cd05935 307 KGR---RFFRTGDLGYMDEEGYFFFVDRVKRMINVS-GFKVWPAEVEAKLYKHPAI*EVCVIS 365
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
128-392 |
2.09e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 66.75 E-value: 2.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 128 ITFTSGSTGTPKGICLSADHMLTVAQSIVAAVGAEHAGRHLALLPPGILLETVAGFFPTLLAGGCyvcppqamIGFADPF 207
Cdd:PRK09088 140 ILFTSGTSGQPKGVMLSERNLQQTAHNFGVLGRVDAHSSFLCDAPMFHIIGLITSVRPVLAVGGS--------ILVSNGF 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 208 RPDFVKAATIIAEQRITSLILVPEYLEGLVRVMETTGLRLPLLTLVAVGGARTSIPLMDRARRLGLPIRQGYGLTECASV 287
Cdd:PRK09088 212 EPKRTLGRLGDPALGITHYFCVPQMAQAFRAQPGFDAAALRHLTALFTGGAPHAAEDILGWLDDGIPMVDGFGMSEAGTV 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 288 VSLQ-DAG--DDDPSSVGRCLPHMTVRVADD----------GEIILDGP-VCLG--------AVGGEAPGSpLQTGDIGS 345
Cdd:PRK09088 292 FGMSvDCDviRAKAGAAGIPTPTVQTRVVDDqgndcpagvpGELLLRGPnLSPGywrrpqatARAFTGDGW-FRTGDIAR 370
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2741210702 346 IDSDGRLHIEGRKSNLIItSFGRNISPEWVEAALVEQPEVMQAMVYG 392
Cdd:PRK09088 371 RDADGFFWVVDRKKDMFI-SGGENVYPAEIEAVLADHPGIRECAVVG 416
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
117-392 |
2.13e-11 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 66.72 E-value: 2.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 117 ASVPLPRGT-ARITFTSGSTGTPKGICLSADHMLTVAQSIVAAVGAEHAGRHLALLPPGILLETVAGFFPTLLAGGCYVC 195
Cdd:PRK07786 167 APVDIPNDSpALIMYTSGTTGRPKGAVLTHANLTGQAMTCLRTNGADINSDVGFVGVPLFHIAGIGSMLPGLLLGAPTVI 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 196 PPqamIGFADPfrpdfVKAATIIAEQRITSLILVPEYLEGLVRVMETTGLRLPLLTLvAVGGARTSIPLMDR--ARRLGL 273
Cdd:PRK07786 247 YP---LGAFDP-----GQLLDVLEAEKVTGIFLVPAQWQAVCAEQQARPRDLALRVL-SWGAAPASDTLLRQmaATFPEA 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 274 PIRQGYGLTECASVVSLQDaGDD---DPSSVGRCLPHMTVRVADD----------GEIILDGPVCLG-------AVGGEA 333
Cdd:PRK07786 318 QILAAFGQTEMSPVTCMLL-GEDairKLGSVGKVIPTVAARVVDEnmndvpvgevGEIVYRAPTLMSgywnnpeATAEAF 396
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2741210702 334 PGSPLQTGDIGSIDSDGRLHIEGRKSNLIItSFGRNISPEWVEAALVEQPEVMQAMVYG 392
Cdd:PRK07786 397 AGGWFHSGDLVRQDEEGYVWVVDRKKDMII-SGGENIYCAEVENVLASHPDIVEVAVIG 454
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
128-392 |
2.44e-11 |
|
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: 65.40 E-value: 2.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 128 ITFTSGSTGTPKGICLSadHMLTVAQSIVAAVG--AEHAGRHLALLPP---GILLETVAgffpTLLAGGCYVCPPQAmig 202
Cdd:cd17636 5 AIYTAAFSGRPNGALLS--HQALLAQALVLAVLqaIDEGTVFLNSGPLfhiGTLMFTLA----TFHAGGTNVFVRRV--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 203 fadpfrpDFVKAATIIAEQRITSLILVPEYLEGLVRVMETTGLRLPllTLVAVGGARTSIPLM--DRA---RRLGlpirq 277
Cdd:cd17636 76 -------DAEEVLELIEAERCTHAFLLPPTIDQIVELNADGLYDLS--SLRSSPAAPEWNDMAtvDTSpwgRKPG----- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 278 GYGLTECASVVSLQDAGDDDPSSVGRCLPHMTVRVADD----------GEIILDGP-VCLGAVGgeAPGSPLQ------- 339
Cdd:cd17636 142 GYGQTEVMGLATFAALGGGAIGGAGRPSPLVQVRILDEdgrevpdgevGEIVARGPtVMAGYWN--RPEVNARrtrggwh 219
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2741210702 340 -TGDIGSIDSDGRLHIEGRKSNLiITSFGRNISPEWVEAALVEQPEVMQAMVYG 392
Cdd:cd17636 220 hTNDLGRREPDGSLSFVGPKTRM-IKSGAENIYPAEVERCLRQHPAVADAAVIG 272
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
15-358 |
3.15e-11 |
|
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: 66.03 E-value: 3.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 15 PQRIALDALDGaPITYgalwAELGERSLAMMARF-----ETDRAVALQSDHGAETSIVELALLRAK---IPV-LSLPAFF 85
Cdd:cd05918 13 PDAPAVCAWDG-SLTY----AELDRLSSRLAHHLrslgvGPGVFVPLCFEKSKWAVVAMLAVLKAGgafVPLdPSHPLQR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 86 TR---EQSRHAIALCgADPDpiqspsgtarsrrsasvplprGTARITFTSGSTGTPKGICLSADHMLTVAQSIVAAVGAE 162
Cdd:cd05918 88 LQeilQDTGAKVVLT-SSPS---------------------DAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRALGLT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 163 HAGRHLALLPPGI---LLEtvagFFPTLLAGGCyVCPPqamigfADPFRPDFVkaATIIAEQRITSLILVPeyleglvRV 239
Cdd:cd05918 146 SESRVLQFASYTFdvsILE----IFTTLAAGGC-LCIP------SEEDRLNDL--AGFINRLRVTWAFLTP-------SV 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 240 METTGLR-LPLLTLVAVGG--ARTSI--PLMDRARrlglpIRQGYGLTECASVVSLQDAGDD-DPSSVGRCLPhMTVRVA 313
Cdd:cd05918 206 ARLLDPEdVPSLRTLVLGGeaLTQSDvdTWADRVR-----LINAYGPAECTIAATVSPVVPStDPRNIGRPLG-ATCWVV 279
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2741210702 314 DD------------GEIILDGPV---------------------CLGAVGGEAPGSPLQTGDIGSIDSDGRLHIEGRK 358
Cdd:cd05918 280 DPdnhdrlvpigavGELLIEGPIlargylndpektaaafiedpaWLKQEGSGRGRRLYRTGDLVRYNPDGSLEYVGRK 357
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
95-391 |
6.40e-11 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 65.16 E-value: 6.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 95 ALCGADPDP--------IQSPSGTARSRRSASVPLPRGTAR-------------ITFTSGSTGTPKGICLSADHMLTVAQ 153
Cdd:PRK06155 131 ALEAADPGDlplpavwlLDAPASVSVPAGWSTAPLPPLDAPapaaavqpgdtaaILYTSGTTGPSKGVCCPHAQFYWWGR 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 154 SIVAAVGAEHAGRHLALLPpgiLLETVA--GFFPTLLAGGCYVCPPQamigF-ADPFRPDfvkaatiIAEQRITSLILVP 230
Cdd:PRK06155 211 NSAEDLEIGADDVLYTTLP---LFHTNAlnAFFQALLAGATYVLEPR----FsASGFWPA-------VRRHGATVTYLLG 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 231 EYLEGLVRVMETTGLRLPLLTlVAVGGARTSIPLMDRARRLGLPIRQGYGLTECASVVSLqDAGDDDPSSVGRCLPHMTV 310
Cdd:PRK06155 277 AMVSILLSQPARESDRAHRVR-VALGPGVPAALHAAFRERFGVDLLDGYGSTETNFVIAV-THGSQRPGSMGRLAPGFEA 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 311 RVADD----------GEIIL--DGPVCLGAVGGEAPGSPLQ--------TGDIGSIDSDGRLHIEGRKSNlIITSFGRNI 370
Cdd:PRK06155 355 RVVDEhdqelpdgepGELLLraDEPFAFATGYFGMPEKTVEawrnlwfhTGDRVVRDADGWFRFVDRIKD-AIRRRGENI 433
|
330 340
....*....|....*....|.
gi 2741210702 371 SPEWVEAALVEQPEVMQAMVY 391
Cdd:PRK06155 434 SSFEVEQVLLSHPAVAAAAVF 454
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
128-392 |
7.87e-11 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 65.22 E-value: 7.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 128 ITFTSGSTGTPKGICLSADHMLTVAQSIVAAVGAEHAGRhLALLPP-----GILLETVAgffpTLLAGGCYVCPpqamig 202
Cdd:PRK08315 204 IQYTSGTTGFPKGATLTHRNILNNGYFIGEAMKLTEEDR-LCIPVPlyhcfGMVLGNLA----CVTHGATMVYP------ 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 203 fADPFRPDFVKAAtiIAEQRITSLILVPeyleglvrVMETTGLRLPLLTLVAVGGARTSI--------PLMDRA-RRLGL 273
Cdd:PRK08315 273 -GEGFDPLATLAA--VEEERCTALYGVP--------TMFIAELDHPDFARFDLSSLRTGImagspcpiEVMKRViDKMHM 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 274 P-IRQGYGLTECaSVVSLQDAGDDD----PSSVGRCLPHMTVRVAD--DGEII---LDGPVC-------LGAVGGEA--- 333
Cdd:PRK08315 342 SeVTIAYGMTET-SPVSTQTRTDDPlekrVTTVGRALPHLEVKIVDpeTGETVprgEQGELCtrgysvmKGYWNDPEkta 420
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2741210702 334 ----PGSPLQTGDIGSIDSDGRLHIEGRKSNLIITSfGRNISPEWVEAALVEQPEVMQAMVYG 392
Cdd:PRK08315 421 eaidADGWMHTGDLAVMDEEGYVNIVGRIKDMIIRG-GENIYPREIEEFLYTHPKIQDVQVVG 482
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
51-392 |
7.94e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 65.06 E-value: 7.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 51 DRAVALQSDHGAETSIVE-----LALLRAKIPVLSLPAFFtreqsRHAIALCGADPDPIQSPSGTarsrrSASVPLPRGT 125
Cdd:PRK06178 138 DQLAPVVEQVRAETSLRHvivtsLADVLPAEPTLPLPDSL-----RAPRLAAAGAIDLLPALRAC-----TAPVPLPPPA 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 126 ----ARITFTSGSTGTPKGICLSADHML-TVAQSIVAAVGAEHAGRHLALLPP--------GILLETVAGFFPTLLAggc 192
Cdd:PRK06178 208 ldalAALNYTGGTTGMPKGCEHTQRDMVyTAAAAYAVAVVGGEDSVFLSFLPEfwiagenfGLLFPLFSGATLVLLA--- 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 193 yvcppqamigfadpfRPDFVKAATIIAEQRITSLILVpeyLEGLVRVMETTGL-RLPLLTLVAVGGARTSIPLMDRARR- 270
Cdd:PRK06178 285 ---------------RWDAVAFMAAVERYRVTRTVML---VDNAVELMDHPRFaEYDLSSLRQVRVVSFVKKLNPDYRQr 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 271 ----LGLPIRQG-YGLTE---CASVVSLQDAGDDD----PSSVGRCLPHMTVRVAD-----------DGEIILDGPVCLG 327
Cdd:PRK06178 347 wralTGSVLAEAaWGMTEthtCDTFTAGFQDDDFDllsqPVFVGLPVPGTEFKICDfetgellplgaEGEIVVRTPSLLK 426
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2741210702 328 AVGGEAPGSP-------LQTGDIGSIDSDGRLHIEGRKSNLIITSfGRNISPEWVEAALVEQPEVMQAMVYG 392
Cdd:PRK06178 427 GYWNKPEATAealrdgwLHTGDIGKIDEQGFLHYLGRRKEMLKVN-GMSVFPSEVEALLGQHPAVLGSAVVG 497
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
125-408 |
9.98e-11 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 65.00 E-value: 9.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 125 TARITFTSGSTGTPKGI-----CLSADhMLTVAQSIVAAVGAEHAG-RHLALLPPGILLE-TVAGFFptlLAGGCYVC-- 195
Cdd:PTZ00216 266 LALIMYTSGTTGDPKGVmhthgSLTAG-ILALEDRLNDLIGPPEEDeTYCSYLPLAHIMEfGVTNIF---LARGALIGfg 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 196 -PPQAMIGFADPfRPDFVkaatiiaEQRITSLILVPEYLEGLVRVMETtglRLP-----------------LLTLV---- 253
Cdd:PTZ00216 342 sPRTLTDTFARP-HGDLT-------EFRPVFLIGVPRIFDTIKKAVEA---KLPpvgslkrrvfdhayqsrLRALKegkd 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 254 -------------AVGGARTSI------PLMDRARR-----LGlPIRQGYGLTECASVVSLQDAGDDDPSSVGRCLPHMT 309
Cdd:PTZ00216 411 tpywnekvfsaprAVLGGRVRAmlsgggPLSAATQEfvnvvFG-MVIQGWGLTETVCCGGIQRTGDLEPNAVGQLLKGVE 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 310 VRVAD-------D-----GEIILDGPVCLG------AVGGEA--PGSPLQTGDIGSIDSDGRLHIEGRksnliITSFGRN 369
Cdd:PTZ00216 490 MKLLDteeykhtDtpeprGEILLRGPFLFKgyykqeELTREVldEDGWFHTGDVGSIAANGTLRIIGR-----VKALAKN 564
|
330 340 350
....*....|....*....|....*....|....*....
gi 2741210702 370 ISPEWVeaALveqpEVMQAMVYGDGLPTPAALLVPSHPD 408
Cdd:PTZ00216 565 CLGEYI--AL----EALEALYGQNELVVPNGVCVLVHPA 597
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
122-390 |
1.59e-10 |
|
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: 63.99 E-value: 1.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 122 PRGTARITFTSGSTGTPKGICLSADHMLTVAQSIVAAVGAEHAGRhlALLPPGILLETVAG-FFPTLLAGGCYVCPPQAM 200
Cdd:cd17644 105 PENLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEYGITSSDR--VLQFASIAFDVAAEeIYVTLLSGATLVLRPEEM 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 201 igFADPfrPDFVKaatIIAEQRITSLILVPEYLEGLVRVMETTGLRLP-LLTLVAVGGARTSIPLMDRARRLGLPIRQ-- 277
Cdd:cd17644 183 --RSSL--EDFVQ---YIQQWQLTVLSLPPAYWHLLVLELLLSTIDLPsSLRLVIVGGEAVQPELVRQWQKNVGNFIQli 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 278 -GYGLTECASVVSLQDAGDDDPSS-----VGRCLPHMTVRVADD----------GEIILDGpvcLGAVGG---------- 331
Cdd:cd17644 256 nVYGPTEATIAATVCRLTQLTERNitsvpIGRPIANTQVYILDEnlqpvpvgvpGELHIGG---VGLARGylnrpeltae 332
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2741210702 332 --------EAPGSPL-QTGDIGSIDSDGRLHIEGRKSNLI-ITSFgrNISPEWVEAALVEQPEVMQAMV 390
Cdd:cd17644 333 kfishpfnSSESERLyKTGDLARYLPDGNIEYLGRIDNQVkIRGF--RIELGEIEAVLSQHNDVKTAVV 399
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
130-392 |
3.52e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 62.75 E-value: 3.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 130 FTSGSTGTPKGICLSADHMLTVAQSIVAAV--GAEHAGRHLALLP----PGI--LLETVAGFFPTLLAggcyvcppqami 201
Cdd:PRK07470 170 FTSGTTGRPKAAVLTHGQMAFVITNHLADLmpGTTEQDASLVVAPlshgAGIhqLCQVARGAATVLLP------------ 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 202 gfADPFRPDFVKAatIIAEQRITSLILVPEYLEGLVRVMETTGLRLPLLTLVAVGGARTSIPLMDRA-RRLGLPIRQGYG 280
Cdd:PRK07470 238 --SERFDPAEVWA--LVERHRVTNLFTVPTILKMLVEHPAVDRYDHSSLRYVIYAGAPMYRADQKRAlAKLGKVLVQYFG 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 281 LTECASVVS-----LQDAGDDDPSSVGRC-LPH--MTVRVADD----------GEIILDGPvclgAVGGEAPGSP----- 337
Cdd:PRK07470 314 LGEVTGNITvlppaLHDAEDGPDARIGTCgFERtgMEVQIQDDegrelppgetGEICVIGP----AVFAGYYNNPeanak 389
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2741210702 338 ------LQTGDIGSIDSDGRLHIEGRKSNLIItSFGRNISPEWVEAALVEQPEVMQAMVYG 392
Cdd:PRK07470 390 afrdgwFRTGDLGHLDARGFLYITGRASDMYI-SGGSNVYPREIEEKLLTHPAVSEVAVLG 449
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
15-448 |
4.34e-10 |
|
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: 62.31 E-value: 4.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 15 PQRIALDALDGaPITYgalwAELGERSLAMMARFET-----DRAVALQSDHGAETSIVELALLRAKIPVLSLPAFFTR-- 87
Cdd:cd12116 1 PDATAVRDDDR-SLSY----AELDERANRLAARLRArgvgpGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPAdr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 88 -----EQSRHAIALC----------GADPDPIQSPSGTARSRRSASVPLPRGTARITFTSGSTGTPKGICLSADHMLTVA 152
Cdd:cd12116 76 lryilEDAEPALVLTddalpdrlpaGLPVLLLALAAAAAAPAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 153 QSIVAAVGAEHAGRHLALLPPGI---LLETvagFFPtLLAGG-CYVCPPQAmigfadpfRPDFVKAATIIAEQRITSLIL 228
Cdd:cd12116 156 HSMRERLGLGPGDRLLAVTTYAFdisLLEL---LLP-LLAGArVVIAPRET--------QRDPEALARLIEAHSITVMQA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 229 VPeyleGLVRVMETTGLR-LPLLTLVaVGGARTSIPLmdrARRLGLPIRQG---YGLTEC---ASVVSLQDAgdDDPSSV 301
Cdd:cd12116 224 TP----ATWRMLLDAGWQgRAGLTAL-CGGEALPPDL---AARLLSRVGSLwnlYGPTETtiwSTAARVTAA--AGPIPI 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 302 GRCLPHMTVRVADD----------GEIILDGP-VCLGAVGGEA-------------PGSPL-QTGDIGSIDSDGRLHIEG 356
Cdd:cd12116 294 GRPLANTQVYVLDAalrpvppgvpGELYIGGDgVAQGYLGRPAltaerfvpdpfagPGSRLyRTGDLVRRRADGRLEYLG 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 357 RKSNLIITSfGRNISPEWVEAALVEQPEVMQAMVY---GDGLPTPAALLVPSHPDADLAAA-VARANEKLPAYAQISAWR 432
Cdd:cd12116 374 RADGQVKIR-GHRIELGEIEAALAAHPGVAQAAVVvreDGGDRRLVAYVVLKAGAAPDAAAlRAHLRATLPAYMVPSAFV 452
|
490
....*....|....*.
gi 2741210702 433 EAAHFTpmngqLTGNG 448
Cdd:cd12116 453 RLDALP-----LTANG 463
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
15-390 |
4.35e-10 |
|
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: 62.73 E-value: 4.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 15 PQRIALdALDGAPITYGalwaELGERSlAMMARF------ETDRAVALQSDHGAETSIVELALLRAKIPVLSL-PAF--- 84
Cdd:cd17655 11 PDHTAV-VFEDQTLTYR----ELNERA-NQLARTlrekgvGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIdPDYpee 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 85 --------------FTREQSRHAIALCGadpDPIQSPSGTARSRRSASVPLP---RGTARITFTSGSTGTPKGIclsadh 147
Cdd:cd17655 85 riqyiledsgadilLTQSHLQPPIAFIG---LIDLLDEDTIYHEESENLEPVsksDDLAYVIYTSGSTGKPKGV------ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 148 MLT---VAQSIVAAVGAEHAGRHL--ALLPPGILLETVAGFFPTLLAGGCYVCPPQAMIGFADPFRpdfvkaaTIIAEQR 222
Cdd:cd17655 156 MIEhrgVVNLVEWANKVIYQGEHLrvALFASISFDASVTEIFASLLSGNTLYIVRKETVLDGQALT-------QYIRQNR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 223 ITSLILVPEYLEGLVRVMETTGlrLPLLTLVaVGGARTSIPLMDR---ARRLGLPIRQGYGLTE---CASVVSLQDAGDD 296
Cdd:cd17655 229 ITIIDLTPAHLKLLDAADDSEG--LSLKHLI-VGGEALSTELAKKiieLFGTNPTITNAYGPTEttvDASIYQYEPETDQ 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 297 DPS-SVGRCLPHMTVRVADDGEIILD----GPVClgaVGGE----------------------APGSPL-QTGDIGSIDS 348
Cdd:cd17655 306 QVSvPIGKPLGNTRIYILDQYGRPQPvgvaGELY---IGGEgvargylnrpeltaekfvddpfVPGERMyRTGDLARWLP 382
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2741210702 349 DGrlHIE--GRKSNLIITSfGRNISPEWVEAALVEQPEVMQAMV 390
Cdd:cd17655 383 DG--NIEflGRIDHQVKIR-GYRIELGEIEARLLQHPDIKEAVV 423
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
91-392 |
6.04e-10 |
|
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: 62.01 E-value: 6.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 91 RHAIALCGADPDPIQS------PSGTARSRRSASVPLPRGTArITFTSGSTGTPKGICLSADHMLTVAQSIVAAVGAEHA 164
Cdd:cd05929 88 KAAALVCGLFTGGGALdgledyEAAEGGSPETPIEDEAAGWK-MLYSGGTTGRPKGIKRGLPGGPPDNDTLMAAALGFGP 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 165 GRHLALLPPGILLETV--AGFFPTLLAGGCYVcppqAMIGFaDPFRpdFVKAatiIAEQRITSLILVPEYLEGLVRVMET 242
Cdd:cd05929 167 GADSVYLSPAPLYHAApfRWSMTALFMGGTLV----LMEKF-DPEE--FLRL---IERYRVTFAQFVPTMFVRLLKLPEA 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 243 TGLRLPLLTLVAV--GGARTSIPLMDRARRLGLP-IRQGYGLTECASVVSLQdaGDD---DPSSVGR-CLPHMTVRVADD 315
Cdd:cd05929 237 VRNAYDLSSLKRVihAAAPCPPWVKEQWIDWGGPiIWEYYGGTEGQGLTIIN--GEEwltHPGSVGRaVLGKVHILDEDG 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 316 GEIildGPVCLGAVGGEAPGS------PLQT------------GDIGSIDSDGRLHIEGRKSNLIItSFGRNISPEWVEA 377
Cdd:cd05929 315 NEV---PPGEIGEVYFANGPGfeytndPEKTaaarneggwstlGDVGYLDEDGYLYLTDRRSDMII-SGGVNIYPQEIEN 390
|
330
....*....|....*
gi 2741210702 378 ALVEQPEVMQAMVYG 392
Cdd:cd05929 391 ALIAHPKVLDAAVVG 405
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
104-398 |
6.24e-10 |
|
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: 62.13 E-value: 6.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 104 IQSPSGTARSRRSASVPLPRGTARITFTSGSTGTPKGIclSADHMLTVAQSIVAAV--GAEHAGRHLALLPPGILLETVA 181
Cdd:cd05970 166 IKNASPDFERPTANSYPCGEDILLVYFSSGTTGMPKMV--EHDFTYPLGHIVTAKYwqNVREGGLHLTVADTGWGKAVWG 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 182 GFFPTLLAGgCYVcppqaMIGFADPFRPDfvKAATIIAEQRITSLILVPEYLEGLVRvMETTGLRLPLLTLVAVGGARTS 261
Cdd:cd05970 244 KIYGQWIAG-AAV-----FVYDYDKFDPK--ALLEKLSKYGVTTFCAPPTIYRFLIR-EDLSRYDLSSLRYCTTAGEALN 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 262 IPLMDRARRL-GLPIRQGYGLTECASVVSLQDAGDDDPSSVGRCLPHMTVRVAD----------DGEIIL--DGPVCLGA 328
Cdd:cd05970 315 PEVFNTFKEKtGIKLMEGFGQTETTLTIATFPWMEPKPGSMGKPAPGYEIDLIDregrsceageEGEIVIrtSKGKPVGL 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 329 VGG-----EAPGSPLQ-----TGDIGSIDSDGRLHIEGRKSNLIITSfGRNISPEWVEAALVEQPEVMQAMVygDGLPTP 398
Cdd:cd05970 395 FGGyykdaEKTAEVWHdgyyhTGDAAWMDEDGYLWFVGRTDDLIKSS-GYRIGPFEVESALIQHPAVLECAV--TGVPDP 471
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
130-404 |
7.99e-10 |
|
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: 61.62 E-value: 7.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 130 FTSGSTGTPKGIClsadHMltvaQSIVAAVGAEHAGRHLALLPPGILLETVAGFFPTLLAGGCYvCPpqAMIGFADPFRP 209
Cdd:cd05959 170 YSSGSTGRPKGVV----HL----HADIYWTAELYARNVLGIREDDVCFSAAKLFFAYGLGNSLT-FP--LSVGATTVLMP 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 210 DFVKAATI---IAEQRITSLILVPEYLEGLVRVMETTGLRLPLLTLVAVGGARTSIPLMDRAR-RLGLPIRQGYGLTECA 285
Cdd:cd05959 239 ERPTPAAVfkrIRRYRPTVFFGVPTLYAAMLAAPNLPSRDLSSLRLCVSAGEALPAEVGERWKaRFGLDILDGIGSTEML 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 286 SVVSLQDAGDDDPSSVGRCLPHMTVR-VADDGEIILDGPVCLGAVGGEAP----------------GSPLQTGDIGSIDS 348
Cdd:cd05959 319 HIFLSNRPGRVRYGTTGKPVPGYEVElRDEDGGDVADGEPGELYVRGPSSatmywnnrdktrdtfqGEWTRTGDKYVRDD 398
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 349 DGRLHIEGRKSNLIITSfGRNISPEWVEAALVEQPEVMQAMVYG----DGLPTPAALLVP 404
Cdd:cd05959 399 DGFYTYAGRADDMLKVS-GIWVSPFEVESALVQHPAVLEAAVVGvedeDGLTKPKAFVVL 457
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
126-392 |
8.50e-10 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 61.61 E-value: 8.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 126 ARITFTSGSTGTPKGICLSADHMLT-VAQSIVAAVGAEHAGRHLALLP-P--GILLETVAG-FFPTLLAGGCYVCPPQAM 200
Cdd:PRK08974 209 AFLQYTGGTTGVAKGAMLTHRNMLAnLEQAKAAYGPLLHPGKELVVTAlPlyHIFALTVNClLFIELGGQNLLITNPRDI 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 201 igfadpfrPDFVKAatiIAEQRITSLILVPEYLEGLVRVMETTGLRLPLLTLVAVGGARTSIPLMDRARRL-GLPIRQGY 279
Cdd:PRK08974 289 --------PGFVKE---LKKYPFTAITGVNTLFNALLNNEEFQELDFSSLKLSVGGGMAVQQAVAERWVKLtGQYLLEGY 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 280 GLTECASVVSLQDAGDDDPS-SVGRCLPHMTVRVADD----------GEIILDGP-VCLG------AVGGEAPGSPLQTG 341
Cdd:PRK08974 358 GLTECSPLVSVNPYDLDYYSgSIGLPVPSTEIKLVDDdgnevppgepGELWVKGPqVMLGywqrpeATDEVIKDGWLATG 437
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2741210702 342 DIGSIDSDGRLHIEGRKSNLIITSfGRNISPEWVEAALVEQPEVMQAMVYG 392
Cdd:PRK08974 438 DIAVMDEEGFLRIVDRKKDMILVS-GFNVYPNEIEDVVMLHPKVLEVAAVG 487
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
128-398 |
1.44e-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: 60.94 E-value: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 128 ITFTSGSTGTPKgiclsadhMLTVAQSiVAAVGAEHAGRHLALLPP----------GILLETVAGFFPTLLAGGCYVCP- 196
Cdd:cd05928 179 IYFTSGTTGSPK--------MAEHSHS-SLGLGLKVNGRYWLDLTAsdimwntsdtGWIKSAWSSLFEPWIQGACVFVHh 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 197 -PQamigfadpFRPDFVkaATIIAEQRITSLILVPEYLEGLVRvMETTGLRLPLLTLVAVGGARTSIPLMDRARRL-GLP 274
Cdd:cd05928 250 lPR--------FDPLVI--LKTLSSYPITTFCGAPTVYRMLVQ-QDLSSYKFPSLQHCVTGGEPLNPEVLEKWKAQtGLD 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 275 IRQGYGLTECASVVSLQDAGDDDPSSVGRCLPHMTVRVADD----------GEIIL----DGPVCL--GAVGG-EAPGSP 337
Cdd:cd05928 319 IYEGYGQTETGLICANFKGMKIKPGSMGKASPPYDVQIIDDngnvlppgteGDIGIrvkpIRPFGLfsGYVDNpEKTAAT 398
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2741210702 338 LQ-----TGDIGSIDSDGRLHIEGRKSNLIITSfGRNISPEWVEAALVEQPEVMQAMVYGDglPTP 398
Cdd:cd05928 399 IRgdfylTGDRGIMDEDGYFWFMGRADDVINSS-GYRIGPFEVESALIEHPAVVESAVVSS--PDP 461
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
115-388 |
1.59e-09 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 61.26 E-value: 1.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 115 RSASVPL-PRGTARITFTSGSTGTPKGICLSADHMLTVAQSIVAAVGAEHAGRHLALLPPGILLETVAGFFPTLLAGG-- 191
Cdd:PRK08043 356 RLAQVKQqPEDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPNDRFMSALPLFHSFGLTVGLFTPLLTGAev 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 192 -CYVCPPQAMIgfadpfRPDFVkaatiiAEQRITSLILVPEYLEGLVRVMETTGL-RLPLLtlvaVGGARTsipLMDRAR 269
Cdd:PRK08043 436 fLYPSPLHYRI------VPELV------YDRNCTVLFGTSTFLGNYARFANPYDFaRLRYV----VAGAEK---LQESTK 496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 270 RL-----GLPIRQGYGLTECASVVSLQDAGDDDPSSVGRCLPHMTVR------VADDGEIILDGP-VCLGAVGGEAPG-- 335
Cdd:PRK08043 497 QLwqdkfGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARllsvpgIEQGGRLQLKGPnIMNGYLRVEKPGvl 576
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2741210702 336 -SP-------------LQTGDIGSIDSDGRLHIEGRKSNLIITSfGRNISPEWVEA-ALVEQPEVMQA 388
Cdd:PRK08043 577 eVPtaenargemergwYDTGDIVRFDEQGFVQIQGRAKRFAKIA-GEMVSLEMVEQlALGVSPDKQHA 643
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
250-392 |
2.02e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 60.55 E-value: 2.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 250 LTLVAVGGARTSIPLMDRARRL-GLPIRQGYGLTECASVVSLQDAGDDDPSSVGRCLPHMTVRVADD----------GEI 318
Cdd:PRK05677 328 LKLTLSGGMALQLATAERWKEVtGCAICEGYGMTETSPVVSVNPSQAIQVGTIGIPVPSTLCKVIDDdgnelplgevGEL 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 319 ILDGPVCLGAVgGEAPGSP---------LQTGDIGSIDSDGRLHIEGRKSNLIITSfGRNISPEWVEAALVEQPEVMQAM 389
Cdd:PRK05677 408 CVKGPQVMKGY-WQRPEATdeildsdgwLKTGDIALIQEDGYMRIVDRKKDMILVS-GFNVYPNELEDVLAALPGVLQCA 485
|
...
gi 2741210702 390 VYG 392
Cdd:PRK05677 486 AIG 488
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
122-392 |
2.27e-09 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 60.48 E-value: 2.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 122 PRGTArITFTSGSTGTPKGIClsadhmltvaqsivaavgaehagRHLALLPPGILLeTVAGFFPTLL---AGGCYVCP-- 196
Cdd:PRK13391 154 SLGTD-MLYSSGTTGRPKGIK-----------------------RPLPEQPPDTPL-PLTAFLQRLWgfrSDMVYLSPap 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 197 -----PQAMIGFA----------DPFRPDfvKAATIIAEQRITSLILVPEYLEGLVRVMETTGLRLPLLTL-VAVGGART 260
Cdd:PRK13391 209 lyhsaPQRAVMLVirlggtvivmEHFDAE--QYLALIEEYGVTHTQLVPTMFSRMLKLPEEVRDKYDLSSLeVAIHAAAP 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 261 SIPLMDRA--RRLGLPIRQGYGLTEC--ASVVSLQDAgDDDPSSVGRCLpHMTVRVADDgeiilDGPVCLGAVGGE---A 333
Cdd:PRK13391 287 CPPQVKEQmiDWWGPIIHEYYAATEGlgFTACDSEEW-LAHPGTVGRAM-FGDLHILDD-----DGAELPPGEPGTiwfE 359
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2741210702 334 PGSPLQ--------------------TGDIGSIDSDGRLHIEGRKSNLIItSFGRNISPEWVEAALVEQPEVMQAMVYG 392
Cdd:PRK13391 360 GGRPFEylndpaktaearhpdgtwstVGDIGYVDEDGYLYLTDRAAFMII-SGGVNIYPQEAENLLITHPKVADAAVFG 437
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
122-392 |
2.45e-09 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 60.28 E-value: 2.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 122 PRGTARITFTSGSTGTPKGICLSADHMLTVAQSI---VAAVGAEHAGRHLAL--LPPGILLETVAGFFPTLLAGGC--YV 194
Cdd:PRK08751 207 PDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAhqwLAGTGKLEEGCEVVItaLPLYHIFALTANGLVFMKIGGCnhLI 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 195 CPPQAMigfadpfrPDFVKAatiIAEQRITSLILVPEYLEGLVRVMETTGLRLPLLTLVAVGGARTSIPLMDRARRL-GL 273
Cdd:PRK08751 287 SNPRDM--------PGFVKE---LKKTRFTAFTGVNTLFNGLLNTPGFDQIDFSSLKMTLGGGMAVQRSVAERWKQVtGL 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 274 PIRQGYGLTE-----CASVVSLQDAGdddpSSVGRCLPHMTVRVADD----------GEIILDGPVCLG---------AV 329
Cdd:PRK08751 356 TLVEAYGLTEtspaaCINPLTLKEYN----GSIGLPIPSTDACIKDDagtvlaigeiGELCIKGPQVMKgywkrpeetAK 431
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2741210702 330 GGEAPGSpLQTGDIGSIDSDGRLHIEGRKSNLIITSfGRNISPEWVEAALVEQPEVMQAMVYG 392
Cdd:PRK08751 432 VMDADGW-LHTGDIARMDEQGFVYIVDRKKDMILVS-GFNVYPNEIEDVIAMMPGVLEVAAVG 492
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
110-392 |
4.82e-09 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 59.24 E-value: 4.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 110 TARSRRSASVPLPRGTARITF-TSGSTGTPKGIclsadhmlTVAQSIVAAVGAE---------HAGRHLALLPP------ 173
Cdd:PRK13383 160 TAGAEESGGRPAVAAPGRIVLlTSGTTGKPKGV--------PRAPQLRSAVGVWvtildrtrlRTGSRISVAMPmfhglg 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 174 -GILLETVAgffptllAGGCYVCppqamigfadpfRPDFVKAATI--IAEQRITSLILVPEYLEGLVRVMETTGLR--LP 248
Cdd:PRK13383 232 lGMLMLTIA-------LGGTVLT------------HRHFDAEAALaqASLHRADAFTAVPVVLARILELPPRVRARnpLP 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 249 LLTLVAVGGARTSIPLMDR-ARRLGLPIRQGYGLTEC-----ASVVSLQDAgdddPSSVGRCLPHMTVRVAD-DGEIIld 321
Cdd:PRK13383 293 QLRVVMSSGDRLDPTLGQRfMDTYGDILYNGYGSTEVgigalATPADLRDA----PETVGKPVAGCPVRILDrNNRPV-- 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 322 GPVCLGA--VGGEAPGSPL-------------QTGDIGSIDSDGRLHIEGRKSNLIItSFGRNISPEWVEAALVEQPEVM 386
Cdd:PRK13383 367 GPRVTGRifVGGELAGTRYtdgggkavvdgmtSTGDMGYLDNAGRLFIVGREDDMII-SGGENVYPRAVENALAAHPAVA 445
|
....*.
gi 2741210702 387 QAMVYG 392
Cdd:PRK13383 446 DNAVIG 451
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
15-391 |
5.74e-09 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 59.25 E-value: 5.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 15 PQRIALDALDG-APITYGALWAELGERSLAMMARFETDRA-VALQSDHGAETSIVELALLR--------------AKI-- 76
Cdd:PRK05857 28 PEAIALRRCDGtSALRYRELVAEVGGLAADLRAQSVSRGSrVLVISDNGPETYLSVLACAKlgaiavmadgnlpiAAIer 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 77 ------PVLSLPAFFTREQSRHAIALCGADPD-PIQSPSGTARSRRSASVPLPRGTAR--------ITFTSGSTGTPKGI 141
Cdd:PRK05857 108 fcqitdPAAALVAPGSKMASSAVPEALHSIPViAVDIAAVTRESEHSLDAASLAGNADqgsedplaMIFTSGTTGEPKAV 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 142 CLsADHMLTVAQSIVAAVGaehagrhLALLPpGILLETVAGFFPTLLAGGCYVCPPQAMIGFADPFRPDFVKAAT-IIAE 220
Cdd:PRK05857 188 LL-ANRTFFAVPDILQKEG-------LNWVT-WVVGETTYSPLPATHIGGLWWILTCLMHGGLCVTGGENTTSLLeILTT 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 221 QRITSLILVPEYLEGLVRVMETTGLRLPLLTLVAVGGARTSIPLMDRARRLGLPIRQGYGLTE--CASVVSLQDAGD--- 295
Cdd:PRK05857 259 NAVATTCLVPTLLSKLVSELKSANATVPSLRLVGYGGSRAIAADVRFIEATGVRTAQVYGLSEtgCTALCLPTDDGSivk 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 296 DDPSSVGRCLPHMTVRVADDGEiilDGPVCLGAVGGEAPG-----SP---------------------LQTGDIGSIDSD 349
Cdd:PRK05857 339 IEAGAVGRPYPGVDVYLAATDG---IGPTAPGAGPSASFGtlwikSPanmlgywnnpertaevlidgwVNTGDLLERRED 415
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 2741210702 350 GRLHIEGRKSNLIItSFGRNISPEWVEAALVEQPEVMQAMVY 391
Cdd:PRK05857 416 GFFYIKGRSSEMII-CGGVNIAPDEVDRIAEGVSGVREAACY 456
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
15-398 |
9.33e-09 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 58.48 E-value: 9.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 15 PQRIA-LDALDGAPITYgalwAELGERSLAMM-----ARFETDRAVALQSDHGAETSIVELALLRAKIPVLSLPAFFTRE 88
Cdd:PRK13390 11 PDRPAvIVAETGEQVSY----RQLDDDSAALArvlydAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 89 QSRHAIALCGADP-------DPIQSPSGTARSRR------------------SASVPL---PRGtARITFTSGSTGTPKG 140
Cdd:PRK13390 87 EADYIVGDSGARVlvasaalDGLAAKVGADLPLRlsfggeidgfgsfeaalaGAGPRLteqPCG-AVMLYSSGTTGFPKG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 141 IclsadhmltvaqsivaavGAEHAGRHLAllPPGILLETVAGFFPTLLAGGCYVcpPQAMIGFADPFR------------ 208
Cdd:PRK13390 166 I------------------QPDLPGRDVD--APGDPIVAIARAFYDISESDIYY--SSAPIYHAAPLRwcsmvhalggtv 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 209 ---PDFVKAATI--IAEQRITSLILVPEYLEGLVRVMETTGLRLPLLTLVAVGGARTSIPLMDRARR---LGLPIRQGYG 280
Cdd:PRK13390 224 vlaKRFDAQATLghVERYRITVTQMVPTMFVRLLKLDADVRTRYDVSSLRAVIHAAAPCPVDVKHAMidwLGPIVYEYYS 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 281 LTEcASVVSLQDAGD--DDPSSVGRCLPHMTVRVADDGEIILDGPVclGAV-------------------GGEAPGSPLQ 339
Cdd:PRK13390 304 STE-AHGMTFIDSPDwlAHPGSVGRSVLGDLHICDDDGNELPAGRI--GTVyferdrlpfrylndpektaAAQHPAHPFW 380
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2741210702 340 T--GDIGSIDSDGRLHIEGRKSNLIItSFGRNISPEWVEAALVEQPEVMQAMVYgdGLPTP 398
Cdd:PRK13390 381 TtvGDLGSVDEDGYLYLADRKSFMII-SGGVNIYPQETENALTMHPAVHDVAVI--GVPDP 438
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
126-392 |
1.07e-08 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 58.22 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 126 ARITFTSGSTGTPKGICLSadHMLTVAQSIVAAVG-AEHAGRHLALLPpgilletVAGFFPTLLAGGCYVCPPQA----M 200
Cdd:PRK06018 180 AGMCYTSGTTGDPKGVLYS--HRSNVLHALMANNGdALGTSAADTMLP-------VVPLFHANSWGIAFSAPSMGtklvM 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 201 IGFadpfRPDFVKAATIIAEQRITSLILVPEYLEGLVRVMETTGLRLPLLTLVAVGGARTSIPLMDRARRLGLPIRQGYG 280
Cdd:PRK06018 251 PGA----KLDGASVYELLDTEKVTFTAGVPTVWLMLLQYMEKEGLKLPHLKMVVCGGSAMPRSMIKAFEDMGVEVRHAWG 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 281 LTECA---SVVSLQDAGDDDPSSV--------GRCLPHMTVRVADD------------GEIILDGPVCLGA---VGGE-- 332
Cdd:PRK06018 327 MTEMSplgTLAALKPPFSKLPGDArldvlqkqGYPPFGVEMKITDDagkelpwdgktfGRLKVRGPAVAAAyyrVDGEil 406
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2741210702 333 -APGSpLQTGDIGSIDSDGRLHIEGRkSNLIITSFGRNISPEWVEAALVEQPEVMQAMVYG 392
Cdd:PRK06018 407 dDDGF-FDTGDVATIDAYGYMRITDR-SKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIG 465
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
272-392 |
1.16e-08 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 58.29 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 272 GLPIRQGYGLTECASVVSLQDAGDDDP-SSVGRCLPHMTVRVADD----------GEIILDGPV--------------CL 326
Cdd:PRK12492 358 GCTIVEGYGLTETSPVASTNPYGELARlGTVGIPVPGTALKVIDDdgnelplgerGELCIKGPQvmkgywqqpeataeAL 437
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2741210702 327 GAVGGeapgspLQTGDIGSIDSDGRLHIEGRKSNLIITSfGRNISPEWVEAALVEQPEVMQAMVYG 392
Cdd:PRK12492 438 DAEGW------FKTGDIAVIDPDGFVRIVDRKKDLIIVS-GFNVYPNEIEDVVMAHPKVANCAAIG 496
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
126-398 |
1.24e-08 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 58.12 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 126 ARITFTSGSTGTPKGICLSADHM----LTVAQSIVAAVGAEhagrhlallppgillETVAGFFPTL-LAGGCYVCPPQAM 200
Cdd:PRK06710 209 ALLQYTGGTTGFPKGVMLTHKNLvsntLMGVQWLYNCKEGE---------------EVVLGVLPFFhVYGMTAVMNLSIM 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 201 IGFADPFRPDFVKAATI--IAEQRITSLILVPEYLEGLVRVMETTGLRLPLLTLVAVGGARTSIPLMDRARRL-GLPIRQ 277
Cdd:PRK06710 274 QGYKMVLIPKFDMKMVFeaIKKHKVTLFPGAPTIYIALLNSPLLKEYDISSIRACISGSAPLPVEVQEKFETVtGGKLVE 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 278 GYGLTECASVVSLQDAGDDD-PSSVGRCLPHMTVRV-----------ADDGEIILDGPVCLGAVGGEAPGSP-------L 338
Cdd:PRK06710 354 GYGLTESSPVTHSNFLWEKRvPGSIGVPWPDTEAMImsletgealppGEIGEIVVKGPQIMKGYWNKPEETAavlqdgwL 433
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 339 QTGDIGSIDSDGRLHIEGRKSNLIITSfGRNISPEWVEAALVEQPEVMQAMVYgdGLPTP 398
Cdd:PRK06710 434 HTGDVGYMDEDGFFYVKDRKKDMIVAS-GFNVYPREVEEVLYEHEKVQEVVTI--GVPDP 490
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
128-403 |
1.48e-08 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 57.72 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 128 ITFTSGSTGTPKGICLSadHMLTVAQSIVAAVGAEhagrhLALLPpgILLETVAGF--------FPTLLAGGCYVCPPQA 199
Cdd:PLN03102 191 LNYTSGTTADPKGVVIS--HRGAYLSTLSAIIGWE-----MGTCP--VYLWTLPMFhcngwtftWGTAARGGTSVCMRHV 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 200 MIgfadpfrPDFVKAatiIAEQRITSLILVPEYLEGLVRVMETTGLRLPLLTLVAVGGARTSIPLMDRARRLGLPIRQGY 279
Cdd:PLN03102 262 TA-------PEIYKN---IEMHNVTHMCCVPTVFNILLKGNSLDLSPRSGPVHVLTGGSPPPAALVKKVQRLGFQVMHAY 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 280 GLTECASVV---SLQDAGDDDPSS------VGRCLPHMTVRVAD----------------DGEIILDGPVCL-GAVGGEA 333
Cdd:PLN03102 332 GLTEATGPVlfcEWQDEWNRLPENqqmelkARQGVSILGLADVDvknketqesvprdgktMGEIVIKGSSIMkGYLKNPK 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 334 PGSP------LQTGDIGSIDSDGRLHIEGRKSNLIItSFGRNISPEWVEAALVEQPEVMQAMVYGDGLP----TPAALLV 403
Cdd:PLN03102 412 ATSEafkhgwLNTGDVGVIHPDGHVEIKDRSKDIII-SGGENISSVEVENVLYKYPKVLETAVVAMPHPtwgeTPCAFVV 490
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
126-407 |
2.35e-08 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 57.20 E-value: 2.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 126 ARITFTSGSTGTPKGICLSADHMLTVAQSIVAAVGAEHAGRHLALLPPGILLETVAGFFPTLLAGGCYVCPPQAMIGfAD 205
Cdd:PRK05852 179 AMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHGHGLIAALLATLASGGAVLLPARGRFS-AH 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 206 PFRPDF--VKAATIIAEQRITSLILVPEYLEGLVRVmettglRLPLLTLVAVGGARTSIPLMDRARRLGLPIRQGYGLTE 283
Cdd:PRK05852 258 TFWDDIkaVGATWYTAVPTIHQILLERAATEPSGRK------PAALRFIRSCSAPLTAETAQALQTEFAAPVVCAFGMTE 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 284 CASVVSLQ-----DAGDDDPSSVGRCLPHMTVRV------------ADDGEIILDGP-VCLGAVGGEAPGSP------LQ 339
Cdd:PRK05852 332 ATHQVTTTqiegiGQTENPVVSTGLVGRSTGAQIrivgsdglplpaGAVGEVWLRGTtVVRGYLGDPTITAAnftdgwLR 411
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2741210702 340 TGDIGSIDSDGRLHIEGRKSNLIITSfGRNISPEWVEAALVEQPEVMQAMVYG--DGL--PTPAALLVPSHP 407
Cdd:PRK05852 412 TGDLGSLSAAGDLSIRGRIKELINRG-GEKISPERVEGVLASHPNVMEAAVFGvpDQLygEAVAAVIVPRES 482
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
122-390 |
2.59e-08 |
|
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: 56.64 E-value: 2.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 122 PRGTARITFTSGSTGTPKGICLSADHMLTVAQSIVAAVGAEHAGRHLALLPPGILLE-TVAGFFPTLLAGGCYVCPPQAM 200
Cdd:cd17648 93 STDLAYAIYTSGTTGKPKGVLVEHGSVVNLRTSLSERYFGRDNGDEAVLFFSNYVFDfFVEQMTLALLNGQKLVVPPDEM 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 201 IGFADPFRPdfvkaatIIAEQRITslilvpeYLEGLVRVMETTGL-RLPLLTLVAVGGARTSIPLMDRAR-RLGLPIRQG 278
Cdd:cd17648 173 RFDPDRFYA-------YINREKVT-------YLSGTPSVLQQYDLaRLPHLKRVDAAGEEFTAPVFEKLRsRFAGLIINA 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 279 YGLTECA--SVVSLQDAGDDDPSSVGRCLPHMTVRVADDGEiildGPVCLGAVG-------GEAPG-------------- 335
Cdd:cd17648 239 YGPTETTvtNHKRFFPGDQRFDKSLGRPVRNTKCYVLNDAM----KRVPVGAVGelylggdGVARGylnrpeltaerflp 314
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 336 SPLQ---------------TGDIGSIDSDGRLHIEGRkSNLIITSFGRNISPEWVEAALVEQPEVMQAMV 390
Cdd:cd17648 315 NPFQteqerargrnarlykTGDLVRWLPSGELEYLGR-NDFQVKIRGQRIEPGEVEAALASYPGVRECAV 383
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
126-390 |
5.40e-08 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 56.71 E-value: 5.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 126 ARITFTSGSTGTPKGICLSADHMLTVAQSIVAAVGAEHAGRHLALLPPGILLeTVAGFFPTLLAGGCYVCPPqamigfAD 205
Cdd:PRK12467 3240 AYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDRVLLFMSFSFDG-AQERFLWTLICGGCLVVRD------ND 3312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 206 PFRPDFVKAAtiIAEQRITSLILVPEYLEGLVRVMEttGLRLPLLTLVAVGGARTSIPLMDRARRlGLPIRQ---GYGLT 282
Cdd:PRK12467 3313 LWDPEELWQA--IHAHRISIACFPPAYLQQFAEDAG--GADCASLDIYVFGGEAVPPAAFEQVKR-KLKPRGltnGYGPT 3387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 283 ECASVVSLQDAGDDdpssvGRCLPH---MTVRVADDGEIILDG---PVCLGAVG-------GEAPG-------------- 335
Cdd:PRK12467 3388 EAVVTVTLWKCGGD-----AVCEAPyapIGRPVAGRSIYVLDGqlnPVPVGVAGelyiggvGLARGyhqrpsltaerfva 3462
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2741210702 336 SPL--------QTGDIGSIDSDGRLHIEGRKSNLIITSfGRNISPEWVEAALVEQPEVMQAMV 390
Cdd:PRK12467 3463 DPFsgsggrlyRTGDLARYRADGVIEYLGRIDHQVKIR-GFRIELGEIEARLLQHPSVREAVV 3524
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
130-388 |
6.20e-08 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 55.87 E-value: 6.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 130 FTSGSTGTPKGICLSadHMLTVAQSIVAAvgaehagrhlalLPPGILLETVAGFFPTL---------------LAGGCYV 194
Cdd:PRK07008 183 YTSGTTGNPKGALYS--HRSTVLHAYGAA------------LPDAMGLSARDAVLPVVpmfhvnawglpysapLTGAKLV 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 195 CPPQAMigfadpfrpDFVKAATIIAEQRITSLILVPEYLEGLVRVMETTGLRLPLLTLVAVGGARTSiPLMDRARR--LG 272
Cdd:PRK07008 249 LPGPDL---------DGKSLYELIEAERVTFSAGVPTVWLGLLNHMREAGLRFSTLRRTVIGGSACP-PAMIRTFEdeYG 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 273 LPIRQGYGLTECA---SVVSLQDAGDDDPSSV--------GRCLPHMTVRVADD------------GEIILDGP-VCLGA 328
Cdd:PRK07008 319 VEVIHAWGMTEMSplgTLCKLKWKHSQLPLDEqrkllekqGRVIYGVDMKIVGDdgrelpwdgkafGDLQVRGPwVIDRY 398
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2741210702 329 VGGEapGSPL-----QTGDIGSIDSDGRLHIEGRkSNLIITSFGRNISPEWVEAALVEQPEVMQA 388
Cdd:PRK07008 399 FRGD--ASPLvdgwfPTGDVATIDADGFMQITDR-SKDVIKSGGEWISSIDIENVAVAHPAVAEA 460
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
119-392 |
6.44e-08 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 55.53 E-value: 6.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 119 VPLPRGTARITFTSGSTGTPKGICLSADHMLTVAQSIVAAVgAEHAGRHLALLPPgilLETVAGFFPTLLAGGcYVCPpq 198
Cdd:PRK13382 192 EPTGRKGRVILLTSGTTGTPKGARRSGPGGIGTLKAILDRT-PWRAEEPTVIVAP---MFHAWGFSQLVLAAS-LACT-- 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 199 amIGFADPFRPDfvKAATIIAEQRITSLILVPEYLEGLVRVMETTGLRLPLLTL--VAVGGARTS----IPLMDRarrLG 272
Cdd:PRK13382 265 --IVTRRRFDPE--ATLDLIDRHRATGLAVVPVMFDRIMDLPAEVRNRYSGRSLrfAAASGSRMRpdvvIAFMDQ---FG 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 273 LPIRQGYGLTEcASVVSLQDAGD--DDPSSVGRCLPHMTVRVAD-DGEIILDGPVclGAV--------GGEAPGSP---- 337
Cdd:PRK13382 338 DVIYNNYNATE-AGMIATATPADlrAAPDTAGRPAEGTEIRILDqDFREVPTGEV--GTIfvrndtqfDGYTSGSTkdfh 414
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 2741210702 338 ---LQTGDIGSIDSDGRLHIEGRKSNLIItSFGRNISPEWVEAALVEQPEVMQAMVYG 392
Cdd:PRK13382 415 dgfMASGDVGYLDENGRLFVVGRDDEMIV-SGGENVYPIEVEKTLATHPDVAEAAVIG 471
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
102-405 |
6.87e-08 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 55.81 E-value: 6.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 102 DPIQSPSGTARSRRSASVPLP-RGTARITFTSGSTGTPKgiclSADHMLTVAQSIVAAVgaehAGRHLALLPPGILLETV 180
Cdd:PRK06060 123 EAAELMSEAARVAPGGYEPMGgDALAYATYTSGTTGPPK----AAIHRHADPLTFVDAM----CRKALRLTPEDTGLCSA 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 181 AGFFPTLLagGCYVCPPQAMIGFA--DPFRPDFVKAATIIAEQRITSLILVPEYLEGLVRVMETTGLRLplLTLVAVGGA 258
Cdd:PRK06060 195 RMYFAYGL--GNSVWFPLATGGSAviNSAPVTPEAAAILSARFGPSVLYGVPNFFARVIDSCSPDSFRS--LRCVVSAGE 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 259 RTSIPLMDRARRL--GLPIRQGYGLTECASVVSLQDAGDDDPSSVGRCLPHMTVR-VADDGEIIldGPVCLGAVGGEAP- 334
Cdd:PRK06060 271 ALELGLAERLMEFfgGIPILDGIGSTEVGQTFVSNRVDEWRLGTLGRVLPPYEIRvVAPDGTTA--GPGVEGDLWVRGPa 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 335 ---------------GSPLQTGDIGSIDSDGRLHIEGRKSNLIITSfGRNISPEWVEAALVEQPEVMQAMVYG----DGL 395
Cdd:PRK06060 349 iakgywnrpdspvanEGWLDTRDRVCIDSDGWVTYRCRADDTEVIG-GVNVDPREVERLIIEDEAVAEAAVVAvresTGA 427
|
330
....*....|
gi 2741210702 396 PTPAALLVPS 405
Cdd:PRK06060 428 STLQAFLVAT 437
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
15-444 |
1.25e-07 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 55.35 E-value: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 15 PQRIALdALDGAPITYGALWAELGERSLAMMAR-FETDRAVALQSDHGAETSIVELALLRAKIPVLSLPAFFTREQSRHA 93
Cdd:PRK12316 3071 PDAVAL-AFGEQRLSYAELNRRANRLAHRLIERgVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYM 3149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 94 IALCGADPDPIQS-----------------PSGTARSRRSASVPLPRGTARITFTSGSTGTPKGICLSADHMLTVAQSIV 156
Cdd:PRK12316 3150 LEDSGAQLLLSQShlrlplaqgvqvldldrGDENYAEANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQ 3229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 157 AAVGAEHAGRHLALLPPGILLeTVAGFFPTLLAGGCYVCPPQAmigfadpfrpDFVKAATIIAEQRITSLILVPEYLEGL 236
Cdd:PRK12316 3230 QAYGLGVGDRVLQFTTFSFDV-FVEELFWPLMSGARVVLAGPE----------DWRDPALLVELINSEGVDVLHAYPSML 3298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 237 VRVMETTGL-RLPLLTLVAVGGARTSIPLMDRArRLGLPIRQGYGLTECASVVSLQDAGDDDPSS--VGRCLPHMTVRVA 313
Cdd:PRK12316 3299 QAFLEEEDAhRCTSLKRIVCGGEALPADLQQQV-FAGLPLYNLYGPTEATITVTHWQCVEEGKDAvpIGRPIANRACYIL 3377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 314 DDG-EIILDGPVCLGAVGGE----------------------APGSPL-QTGDIGSIDSDGRLHIEGRKSNLIITSfGRN 369
Cdd:PRK12316 3378 DGSlEPVPVGALGELYLGGEglargyhnrpgltaerfvpdpfVPGERLyRTGDLARYRADGVIEYIGRVDHQVKIR-GFR 3456
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2741210702 370 ISPEWVEAALVEQPEVMQAMVYGDGLPTPAALLVPSHPDADLAAAVARA-NEKLPAYAQISAWR--EAAHFTPmNGQL 444
Cdd:PRK12316 3457 IELGEIEARLLEHPWVREAVVLAVDGRQLVAYVVPEDEAGDLREALKAHlKASLPEYMVPAHLLflERMPLTP-NGKL 3533
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
130-405 |
2.04e-07 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 54.21 E-value: 2.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 130 FTSGSTGTPKGICLSADHMLTVAQSIVAAVGAEHAGR--HLALLPPGILLETVAGFFPTLLAGGCYVcppqAMIGFAdpF 207
Cdd:PLN02330 191 FSSGTTGISKGVMLTHRNLVANLCSSLFSVGPEMIGQvvTLGLIPFFHIYGITGICCATLRNKGKVV----VMSRFE--L 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 208 RPdFVKAatiIAEQRITSLILVPEYLEGLVR--VMETTGLRLPLLTLVAVGGARTSIPLMD--RARRLGLPIRQGYGLTE 283
Cdd:PLN02330 265 RT-FLNA---LITQEVSFAPIVPPIILNLVKnpIVEEFDLSKLKLQAIMTAAAPLAPELLTafEAKFPGVQVQEAYGLTE 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 284 cASVVSLQDaGDDDP-------SSVGRCLPHMTVRVAD-----------DGEIILDGP-VCLGAVGGEAPGSP------- 337
Cdd:PLN02330 341 -HSCITLTH-GDPEKghgiakkNSVGFILPNLEVKFIDpdtgrslpkntPGELCVRSQcVMQGYYNNKEETDRtidedgw 418
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2741210702 338 LQTGDIGSIDSDGRLHIEGRKSNLIITSfGRNISPEWVEAALVEQPEVMQAMVYgdGLPTPAALLVPS 405
Cdd:PLN02330 419 LHTGDIGYIDDDGDIFIVDRIKELIKYK-GFQVAPAELEAILLTHPSVEDAAVV--PLPDEEAGEIPA 483
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
131-404 |
2.27e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 53.98 E-value: 2.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 131 TSGSTGTPKGICLSADHMLTVAQSIVAAVGAEHAGRHLALLP-PGIL-LETVAGffpTLLAGGCYVCPPQAmigfadpfr 208
Cdd:PRK06164 189 TSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPfCGVFgFSTLLG---ALAGGAPLVCEPVF--------- 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 209 pDFVKAATIIAEQRITSLILVPEYlegLVRVMETTGLRLPLLTLVAVGGAR---TSIPLMDRARRLGLPIRQGYGLTECA 285
Cdd:PRK06164 257 -DAARTARALRRHRVTHTFGNDEM---LRRILDTAGERADFPSARLFGFASfapALGELAALARARGVPLTGLYGSSEVQ 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 286 SVVSLQDAgdDDPSSV-----GRCL-PHMTVRVAD-----------DGEIILDGP-VCLGAVGG-EAPGSPL------QT 340
Cdd:PRK06164 333 ALVALQPA--TDPVSVrieggGRPAsPEARVRARDpqdgallpdgeSGEIEIRAPsLMRGYLDNpDATARALtddgyfRT 410
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2741210702 341 GDIGSIDSDGRLHIEGRKSNLIITSfGRNISPEWVEAALVEQPEVMQAMVYG---DGLPTPAALLVP 404
Cdd:PRK06164 411 GDLGYTRGDGQFVYQTRMGDSLRLG-GFLVNPAEIEHALEALPGVAAAQVVGatrDGKTVPVAFVIP 476
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
340-392 |
2.03e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 50.67 E-value: 2.03e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2741210702 340 TGDIGSIDSDGRLHIEGRKSNLIItSFGRNISPEWVEAALVEQPEVMQAMVYG 392
Cdd:PRK08276 373 VGDVGYLDEDGYLYLTDRKSDMII-SGGVNIYPQEIENLLVTHPKVADVAVFG 424
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
14-390 |
2.13e-06 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 51.20 E-value: 2.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 14 DPQRIALdALDGAPITYgalwAELGERSLAMMARFET-----DRAVALQSDHGAETSIVELALLRAKIPVLSL------- 81
Cdd:PRK10252 471 TPDAPAL-ADARYQFSY----REMREQVVALANLLRErgvkpGDSVAVALPRSVFLTLALHAIVEAGAAWLPLdtgypdd 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 82 ----------PAFF--TREQSRHAIALCGADPDPIQSPSgTARSRRSASVPLPRGTARITFTSGSTGTPKGICLSAdhml 149
Cdd:PRK10252 546 rlkmmledarPSLLitTADQLPRFADVPDLTSLCYNAPL-APQGAAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQ---- 620
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 150 tvaQSIVAAVGAEHAgrHLALLPPGILLE--------TVAGFFPTLLAGGCYV-CPPQAmigFADPfrpdfVKAATIIAE 220
Cdd:PRK10252 621 ---TAIVNRLLWMQN--HYPLTADDVVLQktpcsfdvSVWEFFWPFIAGAKLVmAEPEA---HRDP-----LAMQQFFAE 687
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 221 QRITSLILVPEYLEGLVRVMETTGLRLPLLTL--VAVGGARTSIPLMDR-ARRLGLPIRQGYGLTECASVVSLQDAGDDD 297
Cdd:PRK10252 688 YGVTTTHFVPSMLAAFVASLTPEGARQSCASLrqVFCSGEALPADLCREwQQLTGAPLHNLYGPTEAAVDVSWYPAFGEE 767
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 298 PSSV-GRCLPhMTVRVADDGEIILDG---PVCLGAVG--------------GE-------------APGSPL-QTGDIGS 345
Cdd:PRK10252 768 LAAVrGSSVP-IGYPVWNTGLRILDArmrPVPPGVAGdlyltgiqlaqgylGRpdltasrfiadpfAPGERMyRTGDVAR 846
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 2741210702 346 IDSDGRLHIEGRkSNLIITSFGRNISPEWVEAALVEQPEVMQAMV 390
Cdd:PRK10252 847 WLDDGAVEYLGR-SDDQLKIRGQRIELGEIDRAMQALPDVEQAVT 890
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
77-392 |
3.42e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 50.34 E-value: 3.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 77 PVLSLPAFFTREQSRHAIALCGADPdpiqspsgTARSRRSASVPLPRGT-----ARITFTSGSTGTPKGiCLSAdHMlTV 151
Cdd:PRK08314 147 PEIAVPAWLRAEPPLQALAPGGVVA--------WKEALAAGLAPPPHTAgpddlAVLPYTSGTTGVPKG-CMHT-HR-TV 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 152 AQSIVAAV---GAEHAGRHLALLPPGILLETVAGFFPTLLAGGCYVCPPqamigfadpfRPDFVKAATIIAEQRITSLIL 228
Cdd:PRK08314 216 MANAVGSVlwsNSTPESVVLAVLPLFHVTGMVHSMNAPIYAGATVVLMP----------RWDREAAARLIERYRVTHWTN 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 229 VPEYlegLVRVMETTGL-RLPLLTLVAVGGARTSIPlMDRARRL----GLPIRQGYGLTECASVVSLQDAgdDDPSSvgR 303
Cdd:PRK08314 286 IPTM---VVDFLASPGLaERDLSSLRYIGGGGAAMP-EAVAERLkeltGLDYVEGYGLTETMAQTHSNPP--DRPKL--Q 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 304 CL--PHMTV--RVAD-----------DGEIILDGP-VCLG---------AVGGEAPGSP-LQTGDIGSIDSDGRLHIEGR 357
Cdd:PRK08314 358 CLgiPTFGVdaRVIDpetleelppgeVGEIVVHGPqVFKGywnrpeataEAFIEIDGKRfFRTGDLGRMDEEGYFFITDR 437
|
330 340 350
....*....|....*....|....*....|....*
gi 2741210702 358 KSNLIITSfGRNISPEWVEAALVEQPEVMQAMVYG 392
Cdd:PRK08314 438 LKRMINAS-GFKVWPAEVENLLYKHPAIQEACVIA 471
|
|
| HemeO-bac |
cd19166 |
heme oxygenase found in pathogenic bacteria; This subfamily contains bacterial heme oxygenase ... |
494-674 |
3.47e-06 |
|
heme oxygenase found in pathogenic bacteria; This subfamily contains bacterial heme oxygenase (HO, EC 1.14.14.18), where HO is part of a pathway for iron acquisition from host heme and heme products. Most of these proteins have yet to be characterized. HO catalyzes the rate limiting step in the degradation of heme to biliverdin in a multi-step reaction. HO is essential for recycling of iron from heme which is used as a substrate and cofactor for its own degradation to biliverdin, iron, and carbon monoxide. This family includes heme oxygenase (pa-HO) from Pseudomonas aeruginosa, an opportunistic pathogen that causes a variety of systemic infections, particularly in those afflicted with cystic fibrosis, as well as cancer and AIDS patients who are immunosuppressed. Pa-HO, expressed by the PigA gene, is critical for the acquisition of host iron since there is essentially no free iron in mammals, and is unusual since it hydroxylates heme predominantly at the delta-meso heme carbon, while all other well-studied HOs hydroxylate the alpha-meso carbon. Also included in this family is Neisseria meningitidis HO which is substantially different from the human HO, with the reaction product being ferric biliverdin IXalpha rather than reduced iron and free biliverdin IXalpha. HO shares tertiary structure similarity to methane monooxygenase (EC 1.14.13.25), ribonucleotide reductase (EC 1.17.4.1) and thiaminase II (EC 3.5.99.2), but shares little sequence homology.
Pssm-ID: 350857 [Multi-domain] Cd Length: 182 Bit Score: 48.01 E-value: 3.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 494 TISRGAYLDYLeQAYHHVRHTVplmqaarARLTDRADIVAALDDYiaEETGHEEWILSDIAAAGGDAEAVraskPGPATA 573
Cdd:cd19166 26 FLTLADYARFL-AAQYGFYAPL-------EAALAAALLAALLPDL--AARRRLPLLAADLAALGLAPPAP----AAAPLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 574 AMVDHAYAriangnamafFGMVYVLESvsvafATRGAA----AVAKKLGLPPQAFTYLTSHGALDQEHMTFFANLVNGLD 649
Cdd:cd19166 92 ALPSLAAA----------LGALYVLEG-----STLGGRviarRLAKLLGLADFGARFLAGYGEGTGARWRAFLAALEAAA 156
|
170 180
....*....|....*....|....*.
gi 2741210702 650 -DPADRDAILSMAQEIFGLFGGIFAA 674
Cdd:cd19166 157 lTPADEDAAVAGARATFALFEAALAA 182
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
15-390 |
3.62e-06 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 49.89 E-value: 3.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 15 PQRIALDALdGAPITYGALWAE---------------------LGERSLAMMARF-----------------ETDRAVAL 56
Cdd:PRK04813 16 PDFPAYDYL-GEKLTYGQLKEDsdalaafidslklpdkspiivFGHMSPEMLATFlgavkaghayipvdvssPAERIEMI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 57 QSDHGAET--SIVELALLRAKIPVLSLPAFftreqsrHAIALCGADPDPIQSPSGTarsrrsasvplprGTARITFTSGS 134
Cdd:PRK04813 95 IEVAKPSLiiATEELPLEILGIPVITLDEL-------KDIFATGNPYDFDHAVKGD-------------DNYYIIFTSGT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 135 TGTPKGICLSADHMLTVAQSIVAAVGAEHAGRHLALLPPGILLeTVAGFFPTLLAGGCYVCPPQAMIGfadpfrpDFVKA 214
Cdd:PRK04813 155 TGKPKGVQISHDNLVSFTNWMLEDFALPEGPQFLNQAPYSFDL-SVMDLYPTLASGGTLVALPKDMTA-------NFKQL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 215 ATIIAEQRITSLILVPEYLEglVRVMETT--GLRLPLLTLVAVGG----ARTSIPLMDR---ARrlglpIRQGYGLTECA 285
Cdd:PRK04813 227 FETLPQLPINVWVSTPSFAD--MCLLDPSfnEEHLPNLTHFLFCGeelpHKTAKKLLERfpsAT-----IYNTYGPTEAT 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 286 SVVSLQDAGDD-----DPSSVGRCLPHMTVRVAD----------DGEIILDGP-VCLGAVGGEA---------PGSP-LQ 339
Cdd:PRK04813 300 VAVTSIEITDEmldqyKRLPIGYAKPDSPLLIIDeegtklpdgeQGEIVISGPsVSKGYLNNPEktaeafftfDGQPaYH 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 2741210702 340 TGDIGSIDsDGRLHIEGR-----KSNliitsfGRNISPEWVEAALVEQPEVMQAMV 390
Cdd:PRK04813 380 TGDAGYLE-DGLLFYQGRidfqiKLN------GYRIELEEIEQNLRQSSYVESAVV 428
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
128-392 |
4.02e-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: 341248 [Multi-domain] Cd Length: 364 Bit Score: 49.69 E-value: 4.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 128 ITFTSGSTGTPKGICL-----------SADHMLTVAQSIVAAVGAEHAGRHLALLPPGILLE---TVAGFFptLLAGGCY 193
Cdd:cd05924 8 ILYTGGTTGMPKGVMWrqedifrmlmgGADFGTGEFTPSEDAHKAAAAAAGTVMFPAPPLMHgtgSWTAFG--GLLGGQT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 194 VCPPQamigfaDPFRPDFVKAAtiIAEQRITSLILVPE-YLEGLVRVMETTGLR-LPLLTLVAVGGARTSIPLMDRARRL 271
Cdd:cd05924 86 VVLPD------DRFDPEEVWRT--IEKHKVTSMTIVGDaMARPLIDALRDAGPYdLSSLFAISSGGALLSPEVKQGLLEL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 272 --GLPIRQGYGLTECASVVSLQDAGDDDPSSVGRCLPHMTVRVADDGEIILDGPVCLGAVG--GEAP----GSPLQT--- 340
Cdd:cd05924 158 vpNITLVDAFGSSETGFTGSGHSAGSGPETGPFTRANPDTVVLDDDGRVVPPGSGGVGWIArrGHIPlgyyGDEAKTaet 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2741210702 341 ------------GDIGSIDSDGRLHIEGRKSNLIITSfGRNISPEWVEAALVEQPEVMQAMVYG 392
Cdd:cd05924 238 fpevdgvryavpGDRATVEADGTVTLLGRGSVCINTG-GEKVFPEEVEEALKSHPAVYDVLVVG 300
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
133-388 |
6.28e-06 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 49.22 E-value: 6.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 133 GSTGTPKGICLS-ADHMLTVAQSiVAAVGAEHAGRHLALLP---------PGILletvaGFFptlLAGGCYVCP--PQAM 200
Cdd:PRK10946 192 GSTGTPKLIPRThNDYYYSVRRS-VEICGFTPQTRYLCALPaahnypmssPGAL-----GVF---LAGGTVVLApdPSAT 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 201 IGFAdpfrpdfvkaatIIAEQRITSLILVPEYLEGLVRVMETTGLRLPL--LTLVAVGGARTSIPLmdrARR----LGLP 274
Cdd:PRK10946 263 LCFP------------LIEKHQVNVTALVPPAVSLWLQAIAEGGSRAQLasLKLLQVGGARLSETL---ARRipaeLGCQ 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 275 IRQGYGLTEcaSVVSLQDAGDDDP---SSVGRCL-PHMTVRVAD-DGEIILDGPVclGAVGGEAP-------GSPLQ--- 339
Cdd:PRK10946 328 LQQVFGMAE--GLVNYTRLDDSDErifTTQGRPMsPDDEVWVADaDGNPLPQGEV--GRLMTRGPytfrgyyKSPQHnas 403
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 2741210702 340 ---------TGDIGSIDSDGRLHIEGRKSNLiITSFGRNISPEWVEAALVEQPEVMQA 388
Cdd:PRK10946 404 afdangfycSGDLVSIDPDGYITVVGREKDQ-INRGGEKIAAEEIENLLLRHPAVIHA 460
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
340-408 |
1.55e-05 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 48.27 E-value: 1.55e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2741210702 340 TGDIGSIDSDGRLHIEGRKSNLIITSFGRNISPEWVEAALVEQPEVMQAMVYGDGLPTPAALLVPSHPD 408
Cdd:PLN02430 497 TGDIGEILPNGVLKIIDRKKNLIKLSQGEYVALEYLENVYGQNPIVEDIWVYGDSFKSMLVAVVVPNEE 565
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
125-378 |
2.38e-05 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 47.30 E-value: 2.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 125 TARITFTSGSTGTPKGICLSADHMLTVAQSIVAAVGAE-HAGRHLALLPpgiLLETVA--GFFPTLLAGGCYVCPPQAMI 201
Cdd:PRK07768 154 LALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEFDvETDVMVSWLP---LFHDMGmvGFLTVPMYFGAELVKVTPMD 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 202 GFADPfrpdfVKAATIIAEQRITsLILVPEYLEGLV-RVME--TTGLRLPLLTL-VAVGGARTSIP-----LMDRARRLG 272
Cdd:PRK07768 231 FLRDP-----LLWAELISKYRGT-MTAAPNFAYALLaRRLRrqAKPGAFDLSSLrFALNGAEPIDPadvedLLDAGARFG 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 273 LP---IRQGYGLTECASVVSLQDAG--------DDD---------PS---------SVGRCLPHMTVRVADD-------- 315
Cdd:PRK07768 305 LRpeaILPAYGMAEATLAVSFSPCGaglvvdevDADllaalrravPAtkgntrrlaTLGPPLPGLEVRVVDEdgqvlppr 384
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2741210702 316 --GEIILDGPV-------CLGAVGGEAPGSPLQTGDIGSIDSDGRLHIEGRKSNLIITSfGRNISPEWVEAA 378
Cdd:PRK07768 385 gvGVIELRGESvtpgyltMDGFIPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMA-GRNIYPTDIERA 455
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
128-392 |
2.89e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 47.19 E-value: 2.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 128 ITFTSGSTGTPKGICLSADHMLTVA---------QSI-----VAAVGAEHAGRHLALLPPGILLETVAGFFPTLLAGGCY 193
Cdd:PRK07798 168 LLYTGGTTGMPKGVMWRQEDIFRVLlggrdfatgEPIedeeeLAKRAAAGPGMRRFPAPPLMHGAGQWAAFAALFSGQTV 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 194 VCPPQamigfaDPFRPDFVKAAtiIAEQRITSLILVPE-YLEGLVRVMETTG-LRLPLLTLVAVGGARTSIPLMDRARRL 271
Cdd:PRK07798 248 VLLPD------VRFDADEVWRT--IEREKVNVITIVGDaMARPLLDALEARGpYDLSSLFAIASGGALFSPSVKEALLEL 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 272 gLP---IRQGYGLTE---CASVVSLQDAGDDDPSSVGrcLPHMTVRVADDGEIILDGPVCLG--AVGGEAP----GSPLQ 339
Cdd:PRK07798 320 -LPnvvLTDSIGSSEtgfGGSGTVAKGAVHTGGPRFT--IGPRTVVLDEDGNPVEPGSGEIGwiARRGHIPlgyyKDPEK 396
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2741210702 340 T---------------GDIGSIDSDGRLHIEGRKSnLIITSFGRNISPEWVEAALVEQPEVMQAMVYG 392
Cdd:PRK07798 397 TaetfptidgvryaipGDRARVEADGTITLLGRGS-VCINTGGEKVFPEEVEEALKAHPDVADALVVG 463
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
130-390 |
2.99e-05 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 47.15 E-value: 2.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 130 FTSGSTGTPKGICLSADHMLTVAQSIVAAVGAEHAGRHLALLPpgilletvagFFPTllAGGCYVCPPQAMIGFADPFRP 209
Cdd:PLN02479 202 YTSGTTASPKGVVLHHRGAYLMALSNALIWGMNEGAVYLWTLP----------MFHC--NGWCFTWTLAALCGTNICLRQ 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 210 DFVKAA-TIIAEQRITSLILVPEYLEGLVRV-METTGLRLPLLTLVAVGGARTSIPLMDRARRLGLPIRQGYGLTEC--- 284
Cdd:PLN02479 270 VTAKAIySAIANYGVTHFCAAPVVLNTIVNApKSETILPLPRVVHVMTAGAAPPPSVLFAMSEKGFRVTHTYGLSETygp 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 285 ASVVSLQDAGDDDPSSVGRCL------------------PHMTVRVADDG----EIILDGPVCLGA------VGGEA-PG 335
Cdd:PLN02479 350 STVCAWKPEWDSLPPEEQARLnarqgvryiglegldvvdTKTMKPVPADGktmgEIVMRGNMVMKGylknpkANEEAfAN 429
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2741210702 336 SPLQTGDIGSIDSDGRLHIEGRKSNLIItSFGRNISPEWVEAALVEQPEVMQAMV 390
Cdd:PLN02479 430 GWFHSGDLGVKHPDGYIEIKDRSKDIII-SGGENISSLEVENVVYTHPAVLEASV 483
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
110-381 |
6.89e-05 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 45.91 E-value: 6.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 110 TARSRRSASV-PLPRGT-ARITFTSGSTGTPKGICLSADHMLTVAQSIVAAVGAEHAG-RHLALLPP------GILLETV 180
Cdd:PRK05851 137 AAHTNRSASLtPPDSGGpAVLQGTAGSTGTPRTAILSPGAVLSNLRGLNARVGLDAATdVGCSWLPLyhdmglAFLLTAA 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 181 AGFFPTLLAggcyvcPPQAMIgfADPFRpdfvkAATIIAEQRITsLILVPEYLEGLV-----RVmetTGLRLPLLTLVAV 255
Cdd:PRK05851 217 LAGAPLWLA------PTTAFS--ASPFR-----WLSWLSDSRAT-LTAAPNFAYNLIgkyarRV---SDVDLGALRVALN 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 256 GGARTSIPLMDR----ARRLGLPIRQ---GYGLTE--CASVVSLQDAG-------DDDPSS------VGRCLPHMTVRVA 313
Cdd:PRK05851 280 GGEPVDCDGFERfataMAPFGFDAGAaapSYGLAEstCAVTVPVPGIGlrvdevtTDDGSGarrhavLGNPIPGMEVRIS 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 314 -----------DDGEIILDGPVCLGAVGGEAPGSP---LQTGDIGSIdSDGRLHIEGRKSNLIiTSFGRNISPEWVE--A 377
Cdd:PRK05851 360 pgdgaagvagrEIGEIEIRGASMMSGYLGQAPIDPddwFPTGDLGYL-VDGGLVVCGRAKELI-TVAGRNIFPTEIErvA 437
|
....
gi 2741210702 378 ALVE 381
Cdd:PRK05851 438 AQVR 441
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
128-390 |
8.73e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 45.71 E-value: 8.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 128 ITFTSGSTGTPKGICLsadH----MLTVAQSIVAAVGAEHAgrhlallppgILLETVAGF------FPTLLA--GGCYVC 195
Cdd:PRK08162 187 LNYTSGTTGNPKGVVY---HhrgaYLNALSNILAWGMPKHP----------VYLWTLPMFhcngwcFPWTVAarAGTNVC 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 196 PPQamigfadpFRPDFVKAAtiIAEQRITSLILVPEYLEGLVRVMETT--GLRLPLLTLVAvgGARTSIPLMDRARRLGL 273
Cdd:PRK08162 254 LRK--------VDPKLIFDL--IREHGVTHYCGAPIVLSALINAPAEWraGIDHPVHAMVA--GAAPPAAVIAKMEEIGF 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 274 PIRQGYGLTEC---ASVVSLQDAGDDDP--------SSVG-RCLPHMTVRVADD-------------GEIILDGPVCLG- 327
Cdd:PRK08162 322 DLTHVYGLTETygpATVCAWQPEWDALPlderaqlkARQGvRYPLQEGVTVLDPdtmqpvpadgetiGEIMFRGNIVMKg 401
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2741210702 328 ------AVGGEAPGSPLQTGDIGSIDSDGRLHIEGRKSNLIItSFGRNISPEWVEAALVEQPEVMQAMV 390
Cdd:PRK08162 402 ylknpkATEEAFAGGWFHTGDLAVLHPDGYIKIKDRSKDIII-SGGENISSIEVEDVLYRHPAVLVAAV 469
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
122-323 |
1.14e-04 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 45.42 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 122 PRGTARITFTSGSTGTPKGIcLSADHMLTVAQSIVAAVGAEHAGRhlallPPGILLE------TVAG---FFPTLLAGGC 192
Cdd:PRK12582 219 PDTVAKYLFTSGSTGMPKAV-INTQRMMCANIAMQEQLRPREPDP-----PPPVSLDwmpwnhTMGGnanFNGLLWGGGT 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 193 YvcppqamigFADPFRPDFVKAATIIAEQRITSLIL---VPEYLEGLVRVMET-TGLRLPL---LTLVAVGGARTSIPLM 265
Cdd:PRK12582 293 L---------YIDDGKPLPGMFEETIRNLREISPTVygnVPAGYAMLAEAMEKdDALRRSFfknLRLMAYGGATLSDDLY 363
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2741210702 266 DRARRLG-------LPIRQGYGLTECASVVSLQDAGDDDPSSVGRCLPHMTVRVADDG---EIILDGP 323
Cdd:PRK12582 364 ERMQALAvrttghrIPFYTGYGATETAPTTTGTHWDTERVGLIGLPLPGVELKLAPVGdkyEVRVKGP 431
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
277-391 |
1.24e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 45.03 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 277 QGYGLTE--CASV-VSLQDAGDddpssVGRCLPHMTVRVADD----GEIILdgpvclgavggEAPGSPLQTGDIGSIDSD 349
Cdd:PRK08308 241 QQYGCSEagCVSIcPDMKSHLD-----LGNPLPHVSVSAGSDenapEEIVV-----------KMGDKEIFTKDLGYKSER 304
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2741210702 350 GRLHIEGRKSNLIITSfGRNISPEWVEAALVEQPEVMQAMVY 391
Cdd:PRK08308 305 GTLHFMGRMDDVINVS-GLNVYPIEVEDVMLRLPGVQEAVVY 345
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
122-448 |
1.38e-04 |
|
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: 44.85 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 122 PRGTARITFTSGSTGTPKGICLSADHMLTVA---QSIVAAVGAEHAGRHLALLPPGILLEtvagFFPTLLAGGCYVCPPQ 198
Cdd:cd17645 103 PDDLAYVIYTSGSTGLPKGVMIEHHNLVNLCewhRPYFGVTPADKSLVYASFSFDASAWE----IFPHLTAGAALHVVPS 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 199 AMigfadpfRPDFVKAATIIAEQRITSLILVPEYLEGLVRvMETTGLRLpLLTlvavGGARtsiplMDRARRLGLPIRQG 278
Cdd:cd17645 179 ER-------RLDLDALNDYFNQEGITISFLPTGAAEQFMQ-LDNQSLRV-LLT----GGDK-----LKKIERKGYKLVNN 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 279 YGLTECASVVSLQDAGDDDPS-SVGRCLPHMTVRVADDG----EIILDGPVCLGAVG-------------------GEAP 334
Cdd:cd17645 241 YGPTENTVVATSFEIDKPYANiPIGKPIDNTRVYILDEAlqlqPIGVAGELCIAGEGlargylnrpeltaekfivhPFVP 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 335 GSPL-QTGDIGSIDSDGRLHIEGRKSNLIITSfGRNISPEWVEAALVEQPEVMQAMVY----GDGLPTPAALLVPSHpDA 409
Cdd:cd17645 321 GERMyRTGDLAKFLPDGNIEFLGRLDQQVKIR-GYRIEPGEIEPFLMNHPLIELAAVLakedADGRKYLVAYVTAPE-EI 398
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 2741210702 410 DLAAAVARANEKLPAYAQisawreAAHFTPMNG-QLTGNG 448
Cdd:cd17645 399 PHEELREWLKNDLPDYMI------PTYFVHLKAlPLTANG 432
|
|
| TENA_THI-4 |
pfam03070 |
TENA/THI-4/PQQC family; Members of this family are found in all the three major phyla of life: ... |
492-625 |
2.22e-04 |
|
TENA/THI-4/PQQC family; Members of this family are found in all the three major phyla of life: archaebacteria, eubacteria, and eukaryotes. In Bacillus subtilis, TENA is one of a number of proteins that enhance the expression of extracellular enzymes, such as alkaline protease, neutral protease and levansucrase. The THI-4 protein, which is involved in thiamine biosynthesis, is also a member of this family. The C-terminal part of these proteins consistently show significant sequence similarity to TENA proteins. This similarity was first noted with the Neurospora crassa THI-4. This family includes bacterial coenzyme PQQ synthesis protein C or PQQC proteins. Pyrroloquinoline quinone (PQQ) is the prosthetic group of several bacterial enzymes,including methanol dehydrogenase of methylotrophs and the glucose dehydrogenase of a number of bacteria. PQQC has been found to be required in the synthesis of PQQ but its function is unclear. The exact molecular function of members of this family is uncertain.
Pssm-ID: 397272 [Multi-domain] Cd Length: 210 Bit Score: 43.11 E-value: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 492 NGTISRGAYLDYLEQAYHHVRHTVPLMQAARARLTDRADIvAALDDYIAEETGHE-EWILSDIAAAGGDAEAVRASKPGP 570
Cdd:pfam03070 22 KGTLPREQFQGYVIQDYLYLVNFARVLAIIASKSPDLEVR-REWENRIVDHDGNEiELHLRLAEALGLSREDLSAYKPLP 100
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2741210702 571 ATAAMVDHAYARIANGNAMAFFGMVYVLESVsvafatrgAAAVAKKLGLPPQAFT 625
Cdd:pfam03070 101 ATRAYVRYLLDFARRGSWLEAVAALLPCLFV--------YQEIASRLGEKIRALE 147
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
126-390 |
2.65e-04 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 44.39 E-value: 2.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 126 ARITFTSGSTGTPKGICLSADHMLTVAQSIVAAVGAEHAGRHLALLPPGILLETVAGFFPtLLAGGCYVCPpqAMIGFAD 205
Cdd:PRK05691 1276 AYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKAPISFDVSVWECFWP-LITGCRLVLA--GPGEHRD 1352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 206 PFRpdfvkAATIIAEQRITSLILVPEYLEGLV---RVMETTGLRLplltlVAVGGARTSIPLMDRARRL--GLPIRQGYG 280
Cdd:PRK05691 1353 PQR-----IAELVQQYGVTTLHFVPPLLQLFIdepLAAACTSLRR-----LFSGGEALPAELRNRVLQRlpQVQLHNRYG 1422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 281 LTECA-SVVSLQDAGDD-DPSSVGRCLPHMTVRVADdGEIIL-----DGPVCLGAVG---------------------GE 332
Cdd:PRK05691 1423 PTETAiNVTHWQCQAEDgERSPIGRPLGNVLCRVLD-AELNLlppgvAGELCIGGAGlargylgrpaltaerfvpdplGE 1501
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 2741210702 333 APGSPLQTGDIGSIDSDGRLHIEGRKSNLIITSfGRNISPEWVEAALVEQPEVMQAMV 390
Cdd:PRK05691 1502 DGARLYRTGDRARWNADGALEYLGRLDQQVKLR-GFRVEPEEIQARLLAQPGVAQAAV 1558
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
122-390 |
3.15e-04 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 44.18 E-value: 3.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 122 PRGTARITFTSGSTGTPKGICLSADHMLTVAQSIVAAVGAEHAGRHLALLPPGILLeTVAGFFPTLLAGGCYVCPPQami 201
Cdd:PRK12316 654 PENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDV-SVWEFFWPLMSGARLVVAAP--- 729
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 202 gfADPFRPDfvKAATIIAEQRITSLILVPEYLEGLVR---VMETTGLRlplltLVAVGGARTSIPLMDR--ARRLGLPIR 276
Cdd:PRK12316 730 --GDHRDPA--KLVELINREGVDTLHFVPSMLQAFLQdedVASCTSLR-----RIVCSGEALPADAQEQvfAKLPQAGLY 800
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 277 QGYGLTECASVV---SLQDAGDDDPsSVGRCLphmtvrvADDGEIILDG---PVCLGAVG-------GEAPG-------- 335
Cdd:PRK12316 801 NLYGPTEAAIDVthwTCVEEGGDSV-PIGRPI-------ANLACYILDAnlePVPVGVLGelylagrGLARGyhgrpglt 872
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2741210702 336 ------SPL-------QTGDIGSIDSDGRLHIEGRKSNLIITSfGRNISPEWVEAALVEQPEVMQAMV 390
Cdd:PRK12316 873 aerfvpSPFvagermyRTGDLARYRADGVIEYAGRIDHQVKLR-GLRIELGEIEARLLEHPWVREAAV 939
|
|
| TenA_PqqC |
cd19370 |
TenA_like proteins, including PqqC and CADD; This family contains proteins with similarity to ... |
471-674 |
3.88e-04 |
|
TenA_like proteins, including PqqC and CADD; This family contains proteins with similarity to TenA, and includes bacterial coenzyme pyrroloquinoline quinone (PQQ) synthesis protein C or PQQC proteins. PQQ is the prosthetic group of several bacterial enzymes, including methanol dehydrogenase of methylotrophs and the glucose dehydrogenase of a number of bacteria. PQQC catalyzes the last step of PQQ biogenesis which involves a ring closure and an eight-electron oxidation of the substrate [3a-(2-amino-2-carboxyethyl)-4,5-dioxo-4,5,6,7,8,9-hexahydroquinoline-7,9-dicarboxylic acid (AHQQ)]. The exact molecular function of members of this family is unclear. Also belonging to this family is Chlamydia protein CADD (Chlamydia protein Associating with Death Domains), a redox protein toxin unique to Chlamydia species, which modulates host cell apoptosis; its redox activity and death domain binding ability may be required for this biological activity. CADD may have a role in folate metabolism.
Pssm-ID: 381705 Cd Length: 219 Bit Score: 42.58 E-value: 3.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 471 EARTVRERLRFLAVPQLQAGLNGTISRGAYLDYLEQAYHHVRhTVPLMQAARARLTDRADIVAALDDYIA------EETG 544
Cdd:cd19370 6 ELRRIKGDRYHNHHPFHVAMHNGTLTKEQLQGYVANRYYYQK-TIPKKLSAIMARCDDAQTRRKWLQNILdedgghGEPG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 545 HEEWILSDIAAAGGDAEAVRASKPGPATAAMVDhAYARIANGNA-MAFFGMVYVLESVsvafATRGAAAVAKKL------ 617
Cdd:cd19370 85 HIELWLRLGEALGLTRELLSERHPLPATRFAVD-TYLNFARRASwLEAAASSLSEEFA----PQRIQSRLDSWLqhynsp 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2741210702 618 GLPPQAFTYLTSHGALDQEHMTFFANLVNG-LDDPADRDAILSMAQEIFGLFGGIFAA 674
Cdd:cd19370 160 WIKEEGYFFFRSELSQDVRHAREGLALAEAyCDSAEKQNRVLEALQFKLDILWSMLDA 217
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
338-392 |
6.87e-04 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 42.85 E-value: 6.87e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2741210702 338 LQTGDIGSIDSDGRLHIEGRKSNlIITSFGRNISPEWVEAALVEQPEVMQAMVYG 392
Cdd:PRK05620 432 LRTGDVGSVTRDGFLTIHDRARD-VIRSGGEWIYSAQLENYIMAAPEVVECAVIG 485
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
302-385 |
8.47e-04 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 42.68 E-value: 8.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 302 GRCLPHMTVRVADD----------GEIILDGP-VCLGAVGGE------APGSPLQTGDIGSIdSDGRLHIEGRKSNLIIT 364
Cdd:PRK09192 388 GKALPGHEIEIRNEagmplpervvGHICVRGPsLMSGYFRDEesqdvlAADGWLDTGDLGYL-LDGYLYITGRAKDLIII 466
|
90 100
....*....|....*....|.
gi 2741210702 365 SfGRNISPEWVEAALVEQPEV 385
Cdd:PRK09192 467 N-GRNIWPQDIEWIAEQEPEL 486
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
269-392 |
1.79e-03 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 41.59 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 269 RRLGLPIRQGYGLTEcaSVVSLQDagdDDPS------SVGRCLPHMTVRVADD-------GEIildGPVCLGAVGG---- 331
Cdd:PRK08008 309 ERFGVRLLTSYGMTE--TIVGIIG---DRPGdkrrwpSIGRPGFCYEAEIRDDhnrplpaGEI---GEICIKGVPGktif 380
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2741210702 332 -------EA------PGSPLQTGDIGSIDSDGRLHIEGRKSNLIITSfGRNISPEWVEAALVEQPEVMQAMVYG 392
Cdd:PRK08008 381 keyyldpKAtakvleADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRG-GENVSCVELENIIATHPKIQDIVVVG 453
|
|
| Heme_oxygenase |
pfam01126 |
Heme oxygenase; |
491-674 |
3.21e-03 |
|
Heme oxygenase;
Pssm-ID: 395895 Cd Length: 204 Bit Score: 39.27 E-value: 3.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 491 LNGTISRGAYLDYLEQAYHhvrhtvpLMQAARARLTDRADIVAALDDYIAEeTGHEEWILSDIAA-AGGDAEAVRasKPG 569
Cdd:pfam01126 28 LKGVVDKDAYAKLLANLYF-------VYSALEEELERNRDSPVAAPIYFPE-LNRKAALERDLAYlYGADWRADI--QDS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 570 PATAAMVDHaYARIANGNAMAFFGMVYVLEsvsvaFATRGAAAVAKK-----LGLPPQAFTYLTSHGALDQE--HMTFFA 642
Cdd:pfam01126 98 PATQEYVPR-IREIGNESPELLVAHAYTRY-----LGDLSGGQLLKKiaqraLGLPPGEGTAFYEFEGISDRkvFKQEYR 171
|
170 180 190
....*....|....*....|....*....|...
gi 2741210702 643 NLVNGL-DDPADRDAILSMAQEIFGLFGGIFAA 674
Cdd:pfam01126 172 EALNALeLDDEARARAVEEANDAFALNIQVFRE 204
|
|
| TenA_PqqC-like |
cd16099 |
TenA-like proteins including TenA_C and TenA_E proteins, as well as pyrroloquinoline quinone ... |
492-598 |
4.15e-03 |
|
TenA-like proteins including TenA_C and TenA_E proteins, as well as pyrroloquinoline quinone (PQQ) synthesis protein C; TenA proteins participate in thiamin metabolism and can be classified into two classes: TenA_C which has an active site Cys, and TenA_E which does not; TenA_E proteins often have a pair of structurally conserved Glu residues in the active site. TenA_C proteins (EC 3.5.99.2) catalyze the hydrolysis of the thiamin breakdown product amino-HMP (4-amino-5-amino-methyl-2-methylpyrimidine) to 4-amino-5-hydroxymethyl-2-methylpyrimidine (HMP) in a thiamin salvage pathway; the role of TenA_E proteins is less clear. Arabidopsis thaliana TenA_E hydrolyzes amino-HMP to AMP, and the N-formyl derivative of amino-HMP to amino-HMP, but does not hydrolyze thiamin. Bacillus subtilis TenA_C can hydrolyze amino-HMP to AMP and can catalyze the hydrolysis of thiamin. Saccharomyces cerevisiae THI20 includes a C-terminal tetrameric TenA-like domain fused to an N-terminal ThiD domain, and participates in thiamin biosynthesis, degradation and salvage; the TenA-like domain catalyzes the production of HMP from thiamin degradation products (salvage). Bacillus halodurans TenA_C participates in a salvage pathway where the thiamine degradation product 2-methyl-4-formylamino-5-aminomethylpyrimidine (formylamino-HMP) is hydrolyzed first to amino-HMP by the YlmB protein, and the amino-HMP is then hydrolyzed by TenA to produce HMP. Helicobacter pylori TenA_C is also thought to catalyze a salvage reaction but the pyrimidine substrate has not yet been identified. It has also been suggested that TenA proteins act as transcriptional regulators based on changes in gene-expression patterns when TenA is overexpressed in Bacillus subtilis, however this effect may be indirect; Pyrococcus furiosus TenA_E lacks appropriate surface charges for DNA interactions. This family also includes bacterial coenzyme pyrroloquinoline quinone (PQQ) synthesis protein C (PQQC), an oxidase involved in the final step of PQQ biosynthesis, and CADD, a Chlamydia protein that interacts with death receptors.
Pssm-ID: 381691 [Multi-domain] Cd Length: 196 Bit Score: 38.87 E-value: 4.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 492 NGTISRGAYLDYLEQAYHHVRHTVPLMQAARARLTDRAD---IVAALDDYIAEETGHEEWIlsdiAAAGGDAEAVRASKP 568
Cdd:cd16099 16 AGTLPREKFRYYLAQDYYYLKDFARALALAAAKAPDLELrtfLAELINVLDDELELHEKLL----AELGISEEDLSEAEP 91
|
90 100 110
....*....|....*....|....*....|
gi 2741210702 569 GPATAAMVDHAYARIANGNAMAffGMVYVL 598
Cdd:cd16099 92 NPATLAYTNHLLRVAARGTPAE--GLAALL 119
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
130-392 |
6.28e-03 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 39.88 E-value: 6.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 130 FTSGSTGTPKGICLSADHMLTVAQSivaavgaehaGRH-LALLP---------PGILLETVAGFFPTLLAGGcyvcppqA 199
Cdd:PRK04319 212 YTSGSTGKPKGVLHVHNAMLQHYQT----------GKYvLDLHEddvywctadPGWVTGTSYGIFAPWLNGA-------T 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 200 MIGFADPFRPDFvkAATIIAEQRITSLILVPEYLEGLVRVME--TTGLRLPLLTLVA-VGGartsiPLMDRARR-----L 271
Cdd:PRK04319 275 NVIDGGRFSPER--WYRILEDYKVTVWYTAPTAIRMLMGAGDdlVKKYDLSSLRHILsVGE-----PLNPEVVRwgmkvF 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741210702 272 GLPIRQGYGLTEC-ASVVSLQDAGDDDPSSVGRCLPHMTVRVADDGEiildGPVCLGAVGGEA--PGSPLQ--------- 339
Cdd:PRK04319 348 GLPIHDNWWMTETgGIMIANYPAMDIKPGSMGKPLPGIEAAIVDDQG----NELPPNRMGNLAikKGWPSMmrgiwnnpe 423
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2741210702 340 ------------TGDIGSIDSDGRLHIEGRKSNLIITSfGRNISPEWVEAALVEQPEVMQAMVYG 392
Cdd:PRK04319 424 kyesyfagdwyvSGDSAYMDEDGYFWFQGRVDDVIKTS-GERVGPFEVESKLMEHPAVAEAGVIG 487
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
333-381 |
6.95e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 39.54 E-value: 6.95e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2741210702 333 APGSP----LQTGDIGSIdSDGRLHIEGRKSNLIITsFGRNISPEWVEAALVE 381
Cdd:PRK05850 430 SPGTPegpwLRTGDLGFI-SEGELFIVGRIKDLLIV-DGRNHYPDDIEATIQE 480
|
|
| |
