|
Name |
Accession |
Description |
Interval |
E-value |
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
33-427 |
0e+00 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 755.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 33 TQLLDPMLAEAPTTPLAQaPGKGMDDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADVLYDCLPLYHSAG 112
Cdd:cd05939 81 FNLLDPLLTQSSTEPPSQ-DDVNFRDKLFYIYTSGTTGLPKAAVIVHSRYYRIAAGAYYAFGMRPEDVVYDCLPLYHSAG 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 113 NIMGVGQCVIYGLTVVLRKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVEQRHRVRLAVGNGLRPAIWEEFTQ 192
Cdd:cd05939 160 GIMGVGQALLHGSTVVIRKKFSASNFWDDCVKYNCTIVQYIGEICRYLLAQPPSEEEQKHNVRLAVGNGLRPQIWEQFVR 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 193 RFGVPQIGEFYGATECNCSIANMDGKVGSCGFNSRILTHVYPIRLVKVNEDTMEPLRDSEGLCIPCQPGEPGLLVGQINQ 272
Cdd:cd05939 240 RFGIPQIGEFYGATEGNSSLVNIDNHVGACGFNSRILPSVYPIRLIKVDEDTGELIRDSDGLCIPCQPGEPGLLVGKIIQ 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 273 QDPLRRFDGYVSDSATNKKIAHSVFRKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTD 352
Cdd:cd05939 320 NDPLRRFDGYVNEGATNKKIARDVFKKGDSAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLED 399
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907189430 353 VAVYGVAVPGVEGKAGMAAIADPHSQLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQKTRLQREGFDP 427
Cdd:cd05939 400 VVVYGVEVPGVEGRAGMAAIVDPERKVDLDRFSAVLAKSLPPYARPQFIRLLPEVDKTGTFKLQKTDLQKEGYDP 474
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
2-462 |
0e+00 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 587.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 2 AAAVAEVSEQLGKSLLKFCSGDlgPESILPDTQL-LDPMLAEAPTTPLAQAPGKGMDDRLFYIYTSGTTGLPKAAIVVHS 80
Cdd:PRK08279 145 VEAFEEARADLARPPRLWVAGG--DTLDDPEGYEdLAAAAAGAPTTNPASRSGVTAKDTAFYIYTSGTTGLPKAAVMSHM 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 81 RYYR-IAAFGHhSYSMRAADVLYDCLPLYHSAGNIMGVGQCVIYGLTVVLRKKFSASRFWDDCVKYNCTVVQYIGEICRY 159
Cdd:PRK08279 223 RWLKaMGGFGG-LLRLTPDDVLYCCLPLYHNTGGTVAWSSVLAAGATLALRRKFSASRFWDDVRRYRATAFQYIGELCRY 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 160 LLRQPVRDVEQRHRVRLAVGNGLRPAIWEEFTQRFGVPQIGEFYGATECNCSIANMDGKVGSCGFNSRILTHvyPIRLVK 239
Cdd:PRK08279 302 LLNQPPKPTDRDHRLRLMIGNGLRPDIWDEFQQRFGIPRILEFYAASEGNVGFINVFNFDGTVGRVPLWLAH--PYAIVK 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 240 VNEDTMEPLRDSEGLCIPCQPGEPGLLVGQINqqdPLRRFDGYVSDSATNKKIAHSVFRKGDSAYLSGDVLVMDELGYMY 319
Cdd:PRK08279 380 YDVDTGEPVRDADGRCIKVKPGEVGLLIGRIT---DRGPFDGYTDPEASEKKILRDVFKKGDAWFNTGDLMRDDGFGHAQ 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 320 FRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPGVEGKAGMAAI-ADPHSQLDPNSMYQELQKVLASYARP 398
Cdd:PRK08279 457 FVDRLGDTFRWKGENVATTEVENALSGFPGVEEAVVYGVEVPGTDGRAGMAAIvLADGAEFDLAALAAHLYERLPAYAVP 536
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907189430 399 IFLRLLPQVDTTGTFKIQKTRLQREGFDPRQTSDRLFFLDLKQGRYVPLDERVHARICAGDFSL 462
Cdd:PRK08279 537 LFVRLVPELETTGTFKYRKVDLRKEGFDPSKVDDPLYVLDPGSGGYVPLTAELYAEIAAGKFRL 600
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
58-427 |
0e+00 |
|
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 581.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 58 DRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADVLYDCLPLYHSAGNIMGVGQCVIYGLTVVLRKKFSASR 137
Cdd:cd05940 82 DAALYIYTSGTTGLPKAAIISHRRAWRGGAFFAGSGGALPSDVLYTCLPLYHSTALIVGWSACLASGATLVIRKKFSASN 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 138 FWDDCVKYNCTVVQYIGEICRYLLRQPVRDVEQRHRVRLAVGNGLRPAIWEEFTQRFGVPQIGEFYGATECNCSIANMDG 217
Cdd:cd05940 162 FWDDIRKYQATIFQYIGELCRYLLNQPPKPTERKHKVRMIFGNGLRPDIWEEFKERFGVPRIAEFYAATEGNSGFINFFG 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 218 KVGSCGFNSRILTHVYPIRLVKVNEDTMEPLRDSEGLCIPCQPGEPGLLVGQINqqdPLRRFDGYVSDSATNKKIAHSVF 297
Cdd:cd05940 242 KPGAIGRNPSLLRKVAPLALVKYDLESGEPIRDAEGRCIKVPRGEPGLLISRIN---PLEPFDGYTDPAATEKKILRDVF 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 298 RKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPGVEGKAGMAAIADPHS 377
Cdd:cd05940 319 KKGDAWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQVPGTDGRAGMAAIVLQPN 398
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1907189430 378 Q-LDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQKTRLQREGFDP 427
Cdd:cd05940 399 EeFDLSALAAHLEKNLPGYARPLFLRLQPEMEITGTFKQQKVDLRNEGFDP 449
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
24-449 |
0e+00 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 519.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 24 LGPESILPDTQLLDPMLAEAPTTPLAQ---APGKGMDDRLfYIYTSGTTGLPKAAIVVHSRYYRIAAFgHHSYSMRAADV 100
Cdd:cd05938 109 LSHTSNTEGVISLLDKVDAASDEPVPAslrAHVTIKSPAL-YIYTSGTTGLPKAARISHLRVLQCSGF-LSLCGVTADDV 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 101 LYDCLPLYHSAGNIMGVGQCVIYGLTVVLRKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVEQRHRVRLAVGN 180
Cdd:cd05938 187 IYITLPLYHSSGFLLGIGGCIELGATCVLKPKFSASQFWDDCRKHNVTVIQYIGELLRYLCNQPQSPNDRDHKVRLAIGN 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 181 GLRPAIWEEFTQRFGVPQIGEFYGATECNCSIANMDGKVGSCGFNSRILTHVYPIRLVKVNEDTMEPLRDSEGLCIPCQP 260
Cdd:cd05938 267 GLRADVWREFLRRFGPIRIREFYGSTEGNIGFFNYTGKIGAVGRVSYLYKLLFPFELIKFDVEKEEPVRDAQGFCIPVAK 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 261 GEPGLLVGQINQQDPlrrFDGYVSDSA-TNKKIAHSVFRKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTE 339
Cdd:cd05938 347 GEPGLLVAKITQQSP---FLGYAGDKEqTEKKLLRDVFKKGDVYFNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTE 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 340 VEAVLSRLLGQTDVAVYGVAVPGVEGKAGMAAI--ADPHsQLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQK 417
Cdd:cd05938 424 VADVLGLLDFLQEVNVYGVTVPGHEGRIGMAAVklKPGH-EFDGKKLYQHVREYLPAYARPRFLRIQDSLEITGTFKQQK 502
|
410 420 430
....*....|....*....|....*....|..
gi 1907189430 418 TRLQREGFDPRQTSDRLFFLDLKQGRYVPLDE 449
Cdd:cd05938 503 VRLVEEGFNPSIISDPLYFLDETQKTYVPLTP 534
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
57-427 |
1.14e-124 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 370.61 E-value: 1.14e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 57 DDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADVLYDCLPLYHSAGNIMGVGQCVIYGLTVVLRKKFSAS 136
Cdd:cd05937 87 DDPAILIYTSGTTGLPKAAAISWRRTLVTSNLLSHDLNLKNGDRTYTCMPLYHGTAAFLGACNCLMSGGTLALSRKFSAS 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 137 RFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVEQRHRVRLAVGNGLRPAIWEEFTQRFGVPQIGEFYGATECNCSIANM- 215
Cdd:cd05937 167 QFWKDVRDSGATIIQYVGELCRYLLSTPPSPYDRDHKVRVAWGNGLRPDIWERFRERFNVPEIGEFYAATEGVFALTNHn 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 216 --DGKVGSCGFNSRILTHVY--PIRLVKVNEDTMEPLRD-SEGLCIPCQPGEPGLLVGQINqQDPLRRFDGYVSDS-ATN 289
Cdd:cd05937 247 vgDFGAGAIGHHGLIRRWKFenQVVLVKMDPETDDPIRDpKTGFCVRAPVGEPGEMLGRVP-FKNREAFQGYLHNEdATE 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 290 KKIAHSVFRKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPGVEGKAGM 369
Cdd:cd05937 326 SKLVRDVFRKGDIYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGVKVPGHDGRAGC 405
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907189430 370 AAI-----ADPHSQLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQKTRLQREGFDP 427
Cdd:cd05937 406 AAItleesSAVPTEFTKSLLASLARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVLRDEGVDP 468
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
63-421 |
4.19e-70 |
|
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: 228.72 E-value: 4.19e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 63 IYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADVLYDCLPLYHSAGNIMGVGQCVIYGLTVVLRKKFSASRFWDDC 142
Cdd:cd05934 87 LYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLLPRFSASRFWSDV 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 143 VKYNCTVVQYIGEICRYLLRQPVRDVEQRHRVRLAVGNGLRPAIWEEFTQRFGVPqIGEFYGATECNCSIAN---MDGKV 219
Cdd:cd05934 167 RRYGATVTNYLGAMLSYLLAQPPSPDDRAHRLRAAYGAPNPPELHEEFEERFGVR-LLEGYGMTETIVGVIGprdEPRRP 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 220 GSCGfnsrilthvYPIRLVKVNedtmepLRDSEGLciPCQPGEPGLLVgqINQQDPLRRFDGYVSD-SATNKKIAHSVFR 298
Cdd:cd05934 246 GSIG---------RPAPGYEVR------IVDDDGQ--ELPAGEPGELV--IRGLRGWGFFKGYYNMpEATAEAMRNGWFH 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 299 KGDSAYlsgdvlvMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPGVEGKAGMAAIADPHSQ 378
Cdd:cd05934 307 TGDLGY-------RDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGET 379
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1907189430 379 LDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQKTRLQ 421
Cdd:cd05934 380 LDPEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
61-423 |
8.66e-66 |
|
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: 218.14 E-value: 8.66e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 61 FYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADVLYDCLPLYHSAGNIMGVGQCVIYGLTVVLRKKFSASRFWD 140
Cdd:COG0318 104 LILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLPRFDPERVLE 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 141 DCVKYNCTVVQYIGEICRYLLRQPVRDVEQRHRVRLAV--GNGLRPAIWEEFTQRFGVPqIGEFYGATECNCSIA----- 213
Cdd:COG0318 184 LIERERVTVLFGVPTMLARLLRHPEFARYDLSSLRLVVsgGAPLPPELLERFEERFGVR-IVEGYGLTETSPVVTvnped 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 214 NMDGKVGSCGfnsRILTHVyPIRLVkvnedtmeplrDSEGlcIPCQPGEPGLLVGQINQQdplrrFDGYVSD-SATNKKI 292
Cdd:COG0318 263 PGERRPGSVG---RPLPGV-EVRIV-----------DEDG--RELPPGEVGEIVVRGPNV-----MKGYWNDpEATAEAF 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 293 AHSVFRkgdsaylSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPgVEGKAGMAAI 372
Cdd:COG0318 321 RDGWLR-------TGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDE-KWGERVVAFV 392
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1907189430 373 -ADPHSQLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQKTRLQRE 423
Cdd:COG0318 393 vLRPGAELDAEELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRER 444
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
58-416 |
4.71e-63 |
|
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: 207.52 E-value: 4.71e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 58 DRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADVLYDCLPLYHSAGnIMGVGQCVIYGLTVVLRKKFSASR 137
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGG-LFGLLGALLAGGTVVLLPKFDPEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 138 FWDDCVKYNCTVVQYIGEICRYLLRQPVRDVEQRHRVRLAVGNG--LRPAIWEEFTQRFGVPqIGEFYGATECNCSIA-- 213
Cdd:cd04433 80 ALELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGapLPPELLERFEEAPGIK-LVNGYGLTETGGTVAtg 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 214 ---NMDGKVGSCGFnsrilthvyPIRLVKVNedtmepLRDSEGlcIPCQPGEPGLLVGQINQqdplrRFDGYVSDSATNK 290
Cdd:cd04433 159 ppdDDARKPGSVGR---------PVPGVEVR------IVDPDG--GELPPGEIGELVVRGPS-----VMKGYWNNPEATA 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 291 kiahsvFRKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPgVEGKAGMA 370
Cdd:cd04433 217 ------AVDEDGWYRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDP-EWGERVVA 289
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1907189430 371 AI-ADPHSQLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQ 416
Cdd:cd04433 290 VVvLRPGADLDAEELRAHVRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
41-433 |
1.27e-59 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 204.22 E-value: 1.27e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 41 AEAPTTPLAQAPGkgmdDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADVLYDCLPLYHSAGNIMGVgQC 120
Cdd:PRK06155 168 LDAPAPAAAVQPG----DTAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADDVLYTTLPLFHTNALNAFF-QA 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 121 VIYGLTVVLRKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVEQRHRVRLAVGNGLRPAIWEEFTQRFGVPQIg 200
Cdd:PRK06155 243 LLAGATYVLEPRFSASGFWPAVRRHGATVTYLLGAMVSILLSQPARESDRAHRVRVALGPGVPAALHAAFRERFGVDLL- 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 201 EFYGATECNCSIANM--DGKVGSC-----GFNSRILthvypirlvkvnedtmeplrDSEGLCIPcqPGEPGLLVGQINQq 273
Cdd:PRK06155 322 DGYGSTETNFVIAVThgSQRPGSMgrlapGFEARVV--------------------DEHDQELP--DGEPGELLLRADE- 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 274 dPLRRFDGYVSDSAtnKKIAhsVFRkgDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDV 353
Cdd:PRK06155 379 -PFAFATGYFGMPE--KTVE--AWR--NLWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAA 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 354 AVYGVAVPGVEGKAGMAAIADPHSQLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQKTRLQREGFDPrQTSDR 433
Cdd:PRK06155 452 AVFPVPSELGEDEVMAAVVLRDGTALEPVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVLREQGVTA-DTWDR 530
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
30-458 |
2.61e-59 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 203.33 E-value: 2.61e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 30 LPDTQLLD---PMLAE--APTTPLAQAPGKGMDDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADVLYDC 104
Cdd:PRK13388 118 LPGVRVLDvdtPAYAElvAAAGALTPHREVDAMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLTRDDVCYVS 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 105 LPLYHSAGNIMGVGQCVIYGLTVVLRKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVEQRHRVRLAVGNGLRP 184
Cdd:PRK13388 198 MPLFHSNAVMAGWAPAVASGAAVALPAKFSASGFLDDVRRYGATYFNYVGKPLAYILATPERPDDADNPLRVAFGNEASP 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 185 AIWEEFTQRFGVpQIGEFYGATECNCSIANMDGK-VGSCGfnsrilthvypiR----LVKVNEDTMEPlrdseglCIPCQ 259
Cdd:PRK13388 278 RDIAEFSRRFGC-QVEDGYGSSEGAVIVVREPGTpPGSIG------------RgapgVAIYNPETLTE-------CAVAR 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 260 PGEPGLL------VGQI-NQQDPlRRFDGYVSD-SATNKKIAHSVFRKGDSAYLSGDvlvmdelGYMYFRDRSGDTFRWR 331
Cdd:PRK13388 338 FDAHGALlnadeaIGELvNTAGA-GFFEGYYNNpEATAERMRHGMYWSGDLAYRDAD-------GWIYFAGRTADWMRVD 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 332 GENVSTTEVEAVLSRLLGQTDVAVYGVAVPGVeGKAGMAAI--ADPHSqLDPNSMYQEL--QKVLASYARPIFLRLLPQV 407
Cdd:PRK13388 410 GENLSAAPIERILLRHPAINRVAVYAVPDERV-GDQVMAALvlRDGAT-FDPDAFAAFLaaQPDLGTKAWPRYVRIAADL 487
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1907189430 408 DTTGTFKIQKTRLQREGFdpRQTSDRLFFLDLKQGRYVPLDERVHARICAG 458
Cdd:PRK13388 488 PSTATNKVLKRELIAQGW--ATGDPVTLWVRRGGPAYRLMSEPAKAALAAE 536
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
33-426 |
5.01e-56 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 194.13 E-value: 5.01e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 33 TQLLDPmLAEAPTTPLAQAPgkgmDDRLFYIYTSGTTGLPKAAIVVHSRyyrIAAFGH---HSYSMRAADVLYDCLPLYH 109
Cdd:PRK07867 133 ADELAA-HRDAEPPFRVADP----DDLFMLIFTSGTSGDPKAVRCTHRK---VASAGVmlaQRFGLGPDDVCYVSMPLFH 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 110 SAGNIMGVGQCVIYGLTVVLRKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVEQRHRVRLAVGNGLRPAIWEE 189
Cdd:PRK07867 205 SNAVMAGWAVALAAGASIALRRKFSASGFLPDVRRYGATYANYVGKPLSYVLATPERPDDADNPLRIVYGNEGAPGDIAR 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 190 FTQRFGVpQIGEFYGATECNCSIANM-DGKVGSCGfnsrilthVYPIRLVKVNEDTMEPlrdseglCIPCQPGEPGLL-- 266
Cdd:PRK07867 285 FARRFGC-VVVDGFGSTEGGVAITRTpDTPPGALG--------PLPPGVAIVDPDTGTE-------CPPAEDADGRLLna 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 267 ---VGQ-INQQDPlRRFDGYVSDS-ATNKKIAHSVFRKGDSAYlsgdvlvMDELGYMYFRDRSGDTFRWRGENVSTTEVE 341
Cdd:PRK07867 349 deaIGElVNTAGP-GGFEGYYNDPeADAERMRGGVYWSGDLAY-------RDADGYAYFAGRLGDWMRVDGENLGTAPIE 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 342 AVLSRLLGQTDVAVYGVAVPGVeGKAGMAAIA-DPHSQLDPNSMYQEL--QKVLASYARPIFLRLLPQVDTTGTFKIQKT 418
Cdd:PRK07867 421 RILLRYPDATEVAVYAVPDPVV-GDQVMAALVlAPGAKFDPDAFAEFLaaQPDLGPKQWPSYVRVCAELPRTATFKVLKR 499
|
....*...
gi 1907189430 419 RLQREGFD 426
Cdd:PRK07867 500 QLSAEGVD 507
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
2-331 |
4.66e-37 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 140.53 E-value: 4.66e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 2 AAAVAEVSEQLGKSLLKFCSGDLGPESILPDTQLLDPMLAEAPTTPLAQApgkgmDDRLFYIYTSGTTGLPKAAIVVH-- 79
Cdd:pfam00501 105 LEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVPPPPPPPPDP-----DDLAYIIYTSGTTGKPKGVMLTHrn 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 80 --SRYYRIAAFGHHSYSMRAADVLYDCLPLYHSAGNIMGVGQCVIYGLTVVLRKKFSA---SRFWDDCVKYNCTVVQYIG 154
Cdd:pfam00501 180 lvANVLSIKRVRPRGFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVVLPPGFPAldpAALLELIERYKVTVLYGVP 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 155 EICRYLLRQPV--RDVEQRHRVRLAVGNGLRPAIWEEFTQRFGvPQIGEFYGATECNCSIANMD------GKVGSCGfns 226
Cdd:pfam00501 260 TLLNMLLEAGApkRALLSSLRLVLSGGAPLPPELARRFRELFG-GALVNGYGLTETTGVVTTPLpldedlRSLGSVG--- 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 227 RILTHVypiRLVKVNEDTMEPLRdseglcipcqPGEPG-LLVGQINQqdplrrFDGYVSD-SATNKKIahsvfrKGDSAY 304
Cdd:pfam00501 336 RPLPGT---EVKIVDDETGEPVP----------PGEPGeLCVRGPGV------MKGYLNDpELTAEAF------DEDGWY 390
|
330 340
....*....|....*....|....*..
gi 1907189430 305 LSGDVLVMDELGYMYFRDRSGDTFRWR 331
Cdd:pfam00501 391 RTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
26-416 |
9.22e-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: 126.94 E-value: 9.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 26 PESILPDTQLLDPmLAEAPTTPLAQAPGKGMDDRLFYIYTSGTTGLPKAAIVVHSRYyrIA----AFGHHSYSMRAADVL 101
Cdd:cd05911 116 PDGVLSIEDLLSP-TLGEEDEDLPPPLKDGKDDTAAILYSSGTTGLPKGVCLSHRNL--IAnlsqVQTFLYGNDGSNDVI 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 102 YDCLPLYHSAGNIMGVGqCVIYGLTVVLRKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVEQRHRVR-LAVGN 180
Cdd:cd05911 193 LGFLPLYHIYGLFTTLA-SLLNGATVIIMPKFDSELFLDLIEKYKITFLYLVPPIAAALAKSPLLDKYDLSSLRvILSGG 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 181 G-LRPAIWEEFTQRFGVPQIGEFYGATECNCSIA---NMDGKVGSCGfnsrILTHVYPIRLVkvNEDTMEPLrdseglci 256
Cdd:cd05911 272 ApLSKELQELLAKRFPNATIKQGYGMTETGGILTvnpDGDDKPGSVG----RLLPNVEAKIV--DDDGKDSL-------- 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 257 pcQPGEPG-LLV--GQInqqdplrrFDGYVSD-SATNKKIAHSVFRKgdsaylSGDVLVMDELGYMYFRDRSGDTFRWRG 332
Cdd:cd05911 338 --GPNEPGeICVrgPQV--------MKGYYNNpEATKETFDEDGWLH------TGDIGYFDEDGYLYIVDRKKELIKYKG 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 333 ENVSTTEVEAVLSRLLGQTDVAVYGVAVPgVEGKAGMAAIA-DPHSQLDPNSMYQELQKVLASY----ARPIFLRLLPQv 407
Cdd:cd05911 402 FQVAPAELEAVLLEHPGVADAAVIGIPDE-VSGELPRAYVVrKPGEKLTEKEVKDYVAKKVASYkqlrGGVVFVDEIPK- 479
|
....*....
gi 1907189430 408 dtTGTFKIQ 416
Cdd:cd05911 480 --SASGKIL 486
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
56-417 |
1.00e-31 |
|
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: 125.80 E-value: 1.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 56 MDDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADVLYDCLPLYHSAGNIMGVGQCVIYGLTVVLRKKFSA 135
Cdd:cd17631 97 FDDLALLMYTSGTTGRPKGAMLTHRNLLWNAVNALAALDLGPDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVILRKFDP 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 136 SRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVEQRHRVRLAVGNG--LRPAIWEEFtQRFGVpQIGEFYGATECNCSIA 213
Cdd:cd17631 177 ETVLDLIERHRVTSFFLVPTMIQALLQHPRFATTDLSSLRAVIYGGapMPERLLRAL-QARGV-KFVQGYGMTETSPGVT 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 214 NMD-----GKVGSCGfnsRILTHVyPIRLVKVNEDtmeplrdseglciPCQPGEpgllVGQINQQDPLrRFDGYVSDSAT 288
Cdd:cd17631 255 FLSpedhrRKLGSAG---RPVFFV-EVRIVDPDGR-------------EVPPGE----VGEIVVRGPH-VMAGYWNRPEA 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 289 NKKiahsVFRKGdsAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGvaVPGVE-GKA 367
Cdd:cd17631 313 TAA----AFRDG--WFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIG--VPDEKwGEA 384
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1907189430 368 GMAAIA-DPHSQLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQK 417
Cdd:cd17631 385 VVAVVVpRPGAELDEDELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
57-420 |
1.42e-29 |
|
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: 119.75 E-value: 1.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 57 DDRLFYIYTSGTTGLPKAAIVVHSryyriAAFGHHSYS-----MRAADVLY---DCLPLYHSAGNIMGVgqcVIYGLTVV 128
Cdd:cd05972 81 EDPALIYFTSGTTGLPKGVLHTHS-----YPLGHIPTAaywlgLRPDDIHWniaDPGWAKGAWSSFFGP---WLLGATVF 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 129 L--RKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQpvrDVEQRHRVRL----AVGNGLRPAIWEEFTQRFGVPqIGEF 202
Cdd:cd05972 153 VyeGPRFDAERILELLERYGVTSFCGPPTAYRMLIKQ---DLSSYKFSHLrlvvSAGEPLNPEVIEWWRAATGLP-IRDG 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 203 YGATECNCSIAN---MDGKVGSCGFNsrilTHVYPIRLVkvnedtmeplrDSEGLciPCQPGEPGLLVGQINqqdPLRRF 279
Cdd:cd05972 229 YGQTETGLTVGNfpdMPVKPGSMGRP----TPGYDVAII-----------DDDGR--ELPPGEEGDIAIKLP---PPGLF 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 280 DGYVSDSATNKKiahsVFRKGdsAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVA 359
Cdd:cd05972 289 LGYVGDPEKTEA----SIRGD--YYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSP 362
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907189430 360 VPgVEGKAGMAAIADPHSQLDPNSMYQELQ----KVLASYARPIFLRLLPQVDTTGTFKIQKTRL 420
Cdd:cd05972 363 DP-VRGEVVKAFVVLTSGYEPSEELAEELQghvkKVLAPYKYPREIEFVEELPKTISGKIRRVEL 426
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
37-421 |
1.86e-29 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 120.56 E-value: 1.86e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 37 DPMLAEAPTTpLAQAPGKGMDDRLFYIYTSGTTGLPKAAIVVHsryYRIAAFGHHSY---SMRAADVLYDCLPLYHSAGN 113
Cdd:PRK08008 154 TQLKAQQPAT-LCYAPPLSTDDTAEILFTSGTTSRPKGVVITH---YNLRFAGYYSAwqcALRDDDVYLTVMPAFHIDCQ 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 114 IMGVGQCVIYGLTVVLRKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVEQRHRVR-----LAVGNGLRpaiwE 188
Cdd:PRK08008 230 CTAAMAAFSAGATFVLLEKYSARAFWGQVCKYRATITECIPMMIRTLMVQPPSANDRQHCLRevmfyLNLSDQEK----D 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 189 EFTQRFGVpQIGEFYGATEcncSIANMDG----------KVGSCGFNsrilthvYPIRLVKVNEDTMEPLRDSEgLCIpc 258
Cdd:PRK08008 306 AFEERFGV-RLLTSYGMTE---TIVGIIGdrpgdkrrwpSIGRPGFC-------YEAEIRDDHNRPLPAGEIGE-ICI-- 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 259 qPGEPGLLVgqinqqdplrrFDGYVSD-SATNKKI-AHSVFRKGDSAYlsgdvlvMDELGYMYFRDRSGDTFRWRGENVS 336
Cdd:PRK08008 372 -KGVPGKTI-----------FKEYYLDpKATAKVLeADGWLHTGDTGY-------VDEEGFFYFVDRRCNMIKRGGENVS 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 337 TTEVEAVLSRLLGQTDVAVYGVAVPgVEGKAGMA-AIADPHSQLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKI 415
Cdd:PRK08008 433 CVELENIIATHPKIQDIVVVGIKDS-IRDEAIKAfVVLNEGETLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKI 511
|
....*.
gi 1907189430 416 QKTRLQ 421
Cdd:PRK08008 512 IKKNLK 517
|
|
| PRK07868 |
PRK07868 |
acyl-CoA synthetase; Validated |
23-455 |
4.15e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236121 [Multi-domain] Cd Length: 994 Bit Score: 120.98 E-value: 4.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 23 DLGPESILPDTQLLDPMLAEAPTTpLAQAPGKGMDdrLFYIYTSGTTGLPKAAIVVHSRYyRIAAFGHHSY-SMRAADVL 101
Cdd:PRK07868 574 DLPDDADVIDMEKIDPDAVELPGW-YRPNPGLARD--LAFIAFSTAGGELVAKQITNYRW-ALSAFGTASAaALDRRDTV 649
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 102 YdCL-PLYHSAGNIMGVGQCVIYGLTVVLRKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVEQRHRVRLAVGN 180
Cdd:PRK07868 650 Y-CLtPLHHESGLLVSLGGAVVGGSRIALSRGLDPDRFVQEVRQYGVTVVSYTWAMLREVVDDPAFVLHGNHPVRLFIGS 728
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 181 GLRPAIWEEFTQRFGVPQIGEFYGATECNCSIANMDG-KVGSCGfnsRILTHVYPIRLVKVNEDTMEPLRDSEGLCIPCQ 259
Cdd:PRK07868 729 GMPTGLWERVVEAFAPAHVVEFFATTDGQAVLANVSGaKIGSKG---RPLPGAGRVELAAYDPEHDLILEDDRGFVRRAE 805
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 260 PGEPGLLVGqinqqdplrRFDGYVSDSATNKKiahSVFRKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTE 339
Cdd:PRK07868 806 VNEVGVLLA---------RARGPIDPTASVKR---GVFAPADTWISTEYLFRRDDDGDYWLVDRRGSVIRTARGPVYTEP 873
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 340 VEAVLSRlLGQTDVAV-YGVAVPGVEgkAGMAAIA-DPHSQLDPnsmyQELQKVLASYA---RPIFLRLLPQVDTTGTFK 414
Cdd:PRK07868 874 VTDALGR-IGGVDLAVtYGVEVGGRQ--LAVAAVTlRPGAAITA----ADLTEALASLPvglGPDIVHVVPEIPLSATYR 946
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1907189430 415 IQKTRLQREGFdPRqTSDRLFFLDLKQGRYVPLDERVHARI 455
Cdd:PRK07868 947 PTVSALRAAGI-PK-PGRQAWYFDPETNRYRRLTPAVRAEL 985
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
1-431 |
3.96e-28 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 117.13 E-value: 3.96e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 1 MAAAVAEVSEQLGKSLLKFCSGDLGPESILPDTQLLDPMLAEAPTT-PLAQAPGkgmDDRLFYIYTSGTTGLPKAaiVVH 79
Cdd:COG0365 130 LKEKVDEALEELPSLEHVIVVGRTGADVPMEGDLDWDELLAAASAEfEPEPTDA---DDPLFILYTSGTTGKPKG--VVH 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 80 S-RYYRIAA--FGHHSYSMRAADVLY---DClplyhsaGNIMGVGQCVIYGL----TVVL---RKKF-SASRFWDDCVKY 145
Cdd:COG0365 205 ThGGYLVHAatTAKYVLDLKPGDVFWctaDI-------GWATGHSYIVYGPLlngaTVVLyegRPDFpDPGRLWELIEKY 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 146 NCTVvqyigeIC------RYLLRQPVRDVEQRHRVRL----AVGNGLRPAIWEEFTQRFGVPqIGEFYGATECNCSIAN- 214
Cdd:COG0365 278 GVTV------FFtaptaiRALMKAGDEPLKKYDLSSLrllgSAGEPLNPEVWEWWYEAVGVP-IVDGWGQTETGGIFISn 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 215 ---MDGKVGSCGFnsrilthvyPIRLVKVNedtmepLRDSEGlcIPCQPGEPGLLVgqinqqdpLRR-----FDGYVSDS 286
Cdd:COG0365 351 lpgLPVKPGSMGK---------PVPGYDVA------VVDEDG--NPVPPGEEGELV--------IKGpwpgmFRGYWNDP 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 287 ATNKKiahSVFRKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVygVAVPGVEGK 366
Cdd:COG0365 406 ERYRE---TYFGRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAV--VGVPDEIRG 480
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907189430 367 AGMAA--IADPHSQLDPNsMYQELQ----KVLASYARP---IFLRLLPqvdTTGTFKIQKTRLQR--EGFDPRQTS 431
Cdd:COG0365 481 QVVKAfvVLKPGVEPSDE-LAKELQahvrEELGPYAYPreiEFVDELP---KTRSGKIMRRLLRKiaEGRPLGDTS 552
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
3-420 |
4.08e-28 |
|
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: 116.64 E-value: 4.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 3 AAVAEVSEQLGKSLLKFCSGDLGPesilpdtqlLDPMLAEAPTTPLAQAPgkgmDDRLFyIYTSGTTGLPKAAIVVHSRy 82
Cdd:cd05926 109 LAILELALDVGVLIRAPSAESLSN---------LLADKKNAKSEGVPLPD----DLALI-LHTSGTTGRPKGVPLTHRN- 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 83 yrIAAFGHH---SYSMRAADVLYDCLPLYHSAGNIMGVGQCVIYGLTVVLRKKFSASRFWDDCVKYNCTVVQYIGEICRY 159
Cdd:cd05926 174 --LAASATNitnTYKLTPDDRTLVVMPLFHVHGLVASLLSTLAAGGSVVLPPRFSASTFWPDVRDYNATWYTAVPTIHQI 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 160 LLRQPVRDVEQRH---RVRLAVGNGLRPAIWEEFTQRFGVPQIgEFYGATE------CNCSIANMDgKVGSCGFNS---- 226
Cdd:cd05926 252 LLNRPEPNPESPPpklRFIRSCSASLPPAVLEALEATFGAPVL-EAYGMTEaahqmtSNPLPPGPR-KPGSVGKPVgvev 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 227 RILthvypirlvkvnedtmeplrDSEGLciPCQPGEpgllVGQINQQDPlRRFDGYVSDSATNKKIAHSV--FRKGDSAY 304
Cdd:cd05926 330 RIL--------------------DEDGE--ILPPGV----VGEICLRGP-NVTRGYLNNPEANAEAAFKDgwFRTGDLGY 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 305 LsgdvlvmDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPgVEGKAGMAAI-ADPHSQLDPNS 383
Cdd:cd05926 383 L-------DADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDE-KYGEEVAAAVvLREGASVTEEE 454
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1907189430 384 MYQELQKVLASYARP---IFLRLLPQvdtTGTFKIQKTRL 420
Cdd:cd05926 455 LRAFCRKHLAAFKVPkkvYFVDELPK---TATGKIQRRKV 491
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
40-421 |
1.04e-26 |
|
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: 112.27 E-value: 1.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 40 LAEAPTTPLAQAPGKgmDDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSY--SMRAADVLYDCLPLYHSAGNIMGV 117
Cdd:cd05936 110 LAAGAPLGERVALTP--EDVAVLQYTSGTTGVPKGAMLTHRNLVANALQIKAWLedLLEGDDVVLAALPLFHVFGLTVAL 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 118 GQCVIYGLTVVLRKKFSASRFWDDCVKYNCTVVQ-----YIGeicryLLRQPVRDVEQRHRVRLAVGNG--LRPAIWEEF 190
Cdd:cd05936 188 LLPLALGATIVLIPRFRPIGVLKEIRKHRVTIFPgvptmYIA-----LLNAPEFKKRDFSSLRLCISGGapLPVEVAERF 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 191 TQRFGVPqIGEFYGATECNCSIA-N-MDG--KVGSCGfnsrilthvYPIRLVKVNedtmepLRDSEGLCIPcqPGEPGLL 266
Cdd:cd05936 263 EELTGVP-IVEGYGLTETSPVVAvNpLDGprKPGSIG---------IPLPGTEVK------IVDDDGEELP--PGEVGEL 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 267 VgqinqqdpLR---RFDGYVSDSATNKKiahsVFRKGdsAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAV 343
Cdd:cd05936 325 W--------VRgpqVMKGYWNRPEETAE----AFVDG--WLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEV 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 344 LSRLLGQTDVAVYGVAVP--GVEGKAgmAAIADPHSQLDPNSMYQELQKVLASYARP---IFLRLLPQvDTTGtfKIQKT 418
Cdd:cd05936 391 LYEHPAVAEAAVVGVPDPysGEAVKA--FVVLKEGASLTEEEIIAFCREQLAGYKVPrqvEFRDELPK-SAVG--KILRR 465
|
...
gi 1907189430 419 RLQ 421
Cdd:cd05936 466 ELR 468
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
57-421 |
1.29e-26 |
|
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: 111.40 E-value: 1.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 57 DDRLFYIYTSGTTGLPKAAIVVHSRYYRIA-AFGHHSYSMRAADVLYDCLPLYHSAG---NIMGVGQCviyGLTVVLRKK 132
Cdd:cd05919 91 DDIAYLLYSSGTTGPPKGVMHAHRDPLLFAdAMAREALGLTPGDRVFSSAKMFFGYGlgnSLWFPLAV---GASAVLNPG 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 133 F-SASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVEQRHRVRLAV--GNGLRPAIWEEFTQRFGVPqIGEFYGATEC- 208
Cdd:cd05919 168 WpTAERVLATLARFRPTVLYGVPTFYANLLDSCAGSPDALRSLRLCVsaGEALPRGLGERWMEHFGGP-ILDGIGATEVg 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 209 NCSIANMDGKV--GSCGfnsRILTHvYPIRLVkvnedtmeplrDSEGLCIPcqPGEPGLLVGQINQQDPlrrfdGYVSDS 286
Cdd:cd05919 247 HIFLSNRPGAWrlGSTG---RPVPG-YEIRLV-----------DEEGHTIP--PGEEGDLLVRGPSAAV-----GYWNNP 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 287 ATNKKiahsVFRKGdsAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVygVAVPGVEGK 366
Cdd:cd05919 305 EKSRA----TFNGG--WYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAV--VAVPESTGL 376
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 367 AGMAAIADPHSQLDPN-----SMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQKTRLQ 421
Cdd:cd05919 377 SRLTAFVVLKSPAAPQeslarDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKLR 436
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
5-417 |
6.98e-26 |
|
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: 110.28 E-value: 6.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 5 VAEVSEQLGKSLLKFCSGDLGPESILPDTQLLDPMlAEAPTTPLAQAPGKGMDDRLFYiYTSGTTGLPKaaIVVHSRYYr 84
Cdd:cd05970 135 IEKAAPECPSKPKLVWVGDPVPEGWIDFRKLIKNA-SPDFERPTANSYPCGEDILLVY-FSSGTTGMPK--MVEHDFTY- 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 85 iaAFGHHSYSMRAADVLYDCLplyHSAGNIMGVGQCV---IYG-------LTVVLRKKFSASRFWDDCVKYNCTVVQYIG 154
Cdd:cd05970 210 --PLGHIVTAKYWQNVREGGL---HLTVADTGWGKAVwgkIYGqwiagaaVFVYDYDKFDPKALLEKLSKYGVTTFCAPP 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 155 EICRYLLRQPVRDVEQRhRVRLAV--GNGLRPAIWEEFTQRFGVpQIGEFYGATECNCSIAN---MDGKVGSCGFNsril 229
Cdd:cd05970 285 TIYRFLIREDLSRYDLS-SLRYCTtaGEALNPEVFNTFKEKTGI-KLMEGFGQTETTLTIATfpwMEPKPGSMGKP---- 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 230 THVYPIRLVkvnedtmeplrDSEGLciPCQPGEPGLLVGQINQQDPLRRFDGYVSDSATNKKIAHsvfrkgDSAYLSGDV 309
Cdd:cd05970 359 APGYEIDLI-----------DREGR--SCEAGEEGEIVIRTSKGKPVGLFGGYYKDAEKTAEVWH------DGYYHTGDA 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 310 LVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPgVEGKAGMAAIADPHSQLDPNSMYQELQ 389
Cdd:cd05970 420 AWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDP-IRGQVVKATIVLAKGYEPSEELKKELQ 498
|
410 420 430
....*....|....*....|....*....|..
gi 1907189430 390 ----KVLASYARPIFLRLLPQVDTTGTFKIQK 417
Cdd:cd05970 499 dhvkKVTAPYKYPRIVEFVDELPKTISGKIRR 530
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
43-421 |
8.09e-26 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 109.99 E-value: 8.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 43 APTTPLAQAPGKGMDDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADVLYDCLPLYHSAGNIMGVGQCVI 122
Cdd:PRK07656 152 AAGDPAERAPEVDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLAANPFFHVFGYKAGVNAPLM 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 123 YGLTVVLRKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVEQRHRVRLAVGNG--LRPAIWEEFTQRFGVPQIG 200
Cdd:PRK07656 232 RGATILPLPVFDPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSAEDLSSLRLAVTGAasMPVALLERFESELGVDIVL 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 201 EFYGATECnCSIANM-----DGKV--GSCGfnsrilthvYPIRLVKvnedtmepLRDSEGLCIPCQPGEPGLLVgqinqq 273
Cdd:PRK07656 312 TGYGLSEA-SGVTTFnrlddDRKTvaGTIG---------TAIAGVE--------NKIVNELGEEVPVGEVGELL------ 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 274 dpLRRFD---GYVSDS-ATnkkiAHSVfrKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLG 349
Cdd:PRK07656 368 --VRGPNvmkGYYDDPeAT----AAAI--DADGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPA 439
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907189430 350 QTDVAVYGVAVPGVeGKAGMA-AIADPHSQLDPNSMYQELQKVLASYARP---IFLRLLPqVDTTGtfKIQKTRLQ 421
Cdd:PRK07656 440 VAEAAVIGVPDERL-GEVGKAyVVLKPGAELTEEELIAYCREHLAKYKVPrsiEFLDELP-KNATG--KVLKRALR 511
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
22-423 |
2.69e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 105.27 E-value: 2.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 22 GDLGPESILPDTQLLDPMLAEAPTTPLAqaPGKGMDDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADVL 101
Cdd:PRK06187 134 GDGPAAPLAPEVGEYEELLAAASDTFDF--PDIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVY 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 102 YDCLPLYHSAGniMGVGQCVIY-GLTVVLRKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVEQRHRVRLAV-- 178
Cdd:PRK06187 212 LVIVPMFHVHA--WGLPYLALMaGAKQVIPRRFDPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYFVDFSSLRLVIyg 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 179 GNGLRPAIWEEFTQRFGVpQIGEFYGATECncsianmdGKVGSCGFNSRILTHVYPIRL----------VKVNEDTMEPL 248
Cdd:PRK06187 290 GAALPPALLREFKEKFGI-DLVQGYGMTET--------SPVVSVLPPEDQLPGQWTKRRsagrplpgveARIVDDDGDEL 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 249 rdseglciPCQPGEPGLLV--GQINQQdplrrfdGYVSD-SATNKKIAhsvfrkgDSAYLSGDVLVMDELGYMYFRDRSG 325
Cdd:PRK06187 361 --------PPDGGEVGEIIvrGPWLMQ-------GYWNRpEATAETID-------GGWLHTGDVGYIDEDGYLYITDRIK 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 326 DTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGV----------AVpgVEGKAGMaaiadphsQLDPNSMYQELQKVLASY 395
Cdd:PRK06187 419 DVIISGGENIYPRELEDALYGHPAVAEVAVIGVpdekwgerpvAV--VVLKPGA--------TLDAKELRAFLRGRLAKF 488
|
410 420
....*....|....*....|....*...
gi 1907189430 396 ARPIFLRLLPQVDTTGTFKIQKTRLqRE 423
Cdd:PRK06187 489 KLPKRIAFVDELPRTSVGKILKRVL-RE 515
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
55-422 |
1.30e-21 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 96.73 E-value: 1.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 55 GMDDRLFYIYTSGTTGLPKAAIVVHsryyRIaAFGHhsysmraADVLYDCLPLYHSAGNIM----------GVGQCVI-- 122
Cdd:cd05971 86 GSDDPALIIYTSGTTGPPKGALHAH----RV-LLGH-------LPGVQFPFNLFPRDGDLYwtpadwawigGLLDVLLps 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 123 --YGLTVVLRK--KFSASRFWDDCVKYNCTVVqYIGEICRYLLRQpVRDVEQRHRVRL-AVGNGLRPAIWEEF---TQRF 194
Cdd:cd05971 154 lyFGVPVLAHRmtKFDPKAALDLMSRYGVTTA-FLPPTALKMMRQ-QGEQLKHAQVKLrAIATGGESLGEELLgwaREQF 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 195 GVPqIGEFYGATECNCSIAN----MDGKVGSCGfnsriltHVYPIRLVKVNEDTMEPLrdseglcipcQPGEPGLLVgqI 270
Cdd:cd05971 232 GVE-VNEFYGQTECNLVIGNcsalFPIKPGSMG-------KPIPGHRVAIVDDNGTPL----------PPGEVGEIA--V 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 271 NQQDPLrRFDGYVSD-SATNKKIAHSVFRKGDSAYLSGDvlvmdelGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLG 349
Cdd:cd05971 292 ELPDPV-AFLGYWNNpSATEKKMAGDWLLTGDLGRKDSD-------GYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPA 363
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907189430 350 QTDVAVYGVAVPgVEGKAGMAAIADPHSQLDPNSMYQELQKV----LASYARPIFLRLLPQVDTTGTFKIQKTRLQR 422
Cdd:cd05971 364 VLMAAVVGIPDP-IRGEIVKAFVVLNPGETPSDALAREIQELvktrLAAHEYPREIEFVNELPRTATGKIRRRELRA 439
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
63-420 |
2.85e-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: 95.82 E-value: 2.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 63 IYTSGTTGLPKAaiVVHSRyYRIAAFGH---HSYSMRAADVLYDCLPLYHSAGNIMGVgQCVIY-GLTVVLRKKFSASRF 138
Cdd:cd05941 95 LYTSGTTGRPKG--VVLTH-ANLAANVRalvDAWRWTEDDVLLHVLPLHHVHGLVNAL-LCPLFaGASVEFLPKFDPKEV 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 139 WDDCVKYNCTVVQYIGEICRYLLRQPVRDVEQR--------HRVRLAV-GNG-LRPAIWEEFTQRFGVPqIGEFYGATEC 208
Cdd:cd05941 171 AISRLMPSITVFMGVPTIYTRLLQYYEAHFTDPqfaraaaaERLRLMVsGSAaLPVPTLEEWEAITGHT-LLERYGMTEI 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 209 NCSIAN-MDG--KVGSCGFnsrilthvyPIRLVK---VNEDTMEPL-RDSEG-LCIPcqpgEPGLlvgqinqqdplrrFD 280
Cdd:cd05941 250 GMALSNpLDGerRPGTVGM---------PLPGVQariVDEETGEPLpRGEVGeIQVR----GPSV-------------FK 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 281 GYVSDSATNKKiahsVFRkGDSAYLSGDVLVMDELGYMYFRDR-SGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVA 359
Cdd:cd05941 304 EYWNKPEATKE----EFT-DDGWFKTGDLGVVDEDGYYWILGRsSVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVP 378
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907189430 360 VPgVEGKAGMAAIA--DPHSQLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQKTRL 420
Cdd:cd05941 379 DP-DWGERVVAVVVlrAGAAALSLEELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKEL 440
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
59-415 |
4.14e-21 |
|
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: 93.62 E-value: 4.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 59 RLFYI-YTSGTTGLPKAaivvhsrYYR-----IAAF--GHHSYSMRAADVLYDCLPLYHSaGNIMGVGQCVIYGLTVVLR 130
Cdd:cd17633 1 NPFYIgFTSGTTGLPKA-------YYRserswIESFvcNEDLFNISGEDAILAPGPLSHS-LFLYGAISALYLGGTFIGQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 131 KKFSASRFWDDCVKYNCTVVQYIGEicryLLRQPVRDVEQRHRVR--LAVGNGLRPAIWEEFTQRFGVPQIGEFYGATEC 208
Cdd:cd17633 73 RKFNPKSWIRKINQYNATVIYLVPT----MLQALARTLEPESKIKsiFSSGQKLFESTKKKLKNIFPKANLIEFYGTSEL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 209 NCSIANMDG---KVGSCGfnsRILTHVyPIRLvkvnedtmeplRDSEGlcipcqpGEPGLLVGQINQqdplrRFDGYVSD 285
Cdd:cd17633 149 SFITYNFNQesrPPNSVG---RPFPNV-EIEI-----------RNADG-------GEIGKIFVKSEM-----VFSGYVRG 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 286 SATNKkiaHSVFRKGDSAYLsgdvlvmDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGV------- 358
Cdd:cd17633 202 GFSNP---DGWMSVGDIGYV-------DEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIpdarfge 271
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907189430 359 -AVPGVEGKagmaaiadphsQLDPNSMYQELQKVLASYARP---IFLRLLPQvdtTGTFKI 415
Cdd:cd17633 272 iAVALYSGD-----------KLTYKQLKRFLKQKLSRYEIPkkiIFVDSLPY---TSSGKI 318
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
63-423 |
8.45e-21 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 94.64 E-value: 8.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 63 IYTSGTTGLPKAAIvvhsryyriAAFGHHSYS---------MRAADVLYDCLPLYHSAG-NIMGVGqcVIYGLTVVLRKK 132
Cdd:PRK03640 147 MYTSGTTGKPKGVI---------QTYGNHWWSavgsalnlgLTEDDCWLAAVPIFHISGlSILMRS--VIYGMRVVLVEK 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 133 FSASRFWDDCVKYNCT---VVQYigeicryLLRQPVRDVEQRH-----RVRLaVGNGLRPAIWEEFTQRFGVPQIgEFYG 204
Cdd:PRK03640 216 FDAEKINKLLQTGGVTiisVVST-------MLQRLLERLGEGTypssfRCML-LGGGPAPKPLLEQCKEKGIPVY-QSYG 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 205 ATECNCSIANMD-----GKVGSCG---FNSRIlthvypirlvKVNEDTMEplrdseglCIPCQPGE-----PGLLVGQIN 271
Cdd:PRK03640 287 MTETASQIVTLSpedalTKLGSAGkplFPCEL----------KIEKDGVV--------VPPFEEGEivvkgPNVTKGYLN 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 272 QQDplrrfdgyvsdsATNKKIAHSVFRKGDSAYLsgdvlvmDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQT 351
Cdd:PRK03640 349 RED------------ATRETFQDGWFKTGDIGYL-------DEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVA 409
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907189430 352 DVAVYGVAvpgvEGKAGMAAIAD--PHSQLDPNSMYQELQKVLASYARP---IFLRLLPQvdtTGTFKIQKTRLQRE 423
Cdd:PRK03640 410 EAGVVGVP----DDKWGQVPVAFvvKSGEVTEEELRHFCEEKLAKYKVPkrfYFVEELPR---NASGKLLRHELKQL 479
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
63-422 |
2.11e-20 |
|
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: 92.79 E-value: 2.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 63 IYTSGTTGLPKAAIVvhsryyriaAFGHHSYSMRAADV---LYD------CLPLYHSAG-NIMGVGqcVIYGLTVVLRKK 132
Cdd:cd05912 83 MYTSGTTGKPKGVQQ---------TFGNHWWSAIGSALnlgLTEddnwlcALPLFHISGlSILMRS--VIYGMTVYLVDK 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 133 FSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVEQRHRVRLaVGNGLRPAIWEEFTQRFGVPqIGEFYGATE----- 207
Cdd:cd05912 152 FDAEQVLHLINSGKVTIISVVPTMLQRLLEILGEGYPNNLRCIL-LGGGPAPKPLLEQCKEKGIP-VYQSYGMTEtcsqi 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 208 CNCSIANMDGKVGSCG---FNSRilthvypIRLVKVNEDtmeplrdseglciPCQPGE-----PGLLVGQINQQDplrrf 279
Cdd:cd05912 230 VTLSPEDALNKIGSAGkplFPVE-------LKIEDDGQP-------------PYEVGEillkgPNVTKGYLNRPD----- 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 280 dgyvsdsATNKKIAHSVFRKGDSAYLsgdvlvmDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVygVA 359
Cdd:cd05912 285 -------ATEESFENGWFKTGDIGYL-------DEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGV--VG 348
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907189430 360 VPgvEGKAGMAAIA--DPHSQLDPNSMYQELQKVLASYARP---IFLRLLPQvdtTGTFKIQKTRLQR 422
Cdd:cd05912 349 IP--DDKWGQVPVAfvVSERPISEEELIAYCSEKLAKYKVPkkiYFVDELPR---TASGKLLRHELKQ 411
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
64-421 |
2.67e-19 |
|
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: 88.87 E-value: 2.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 64 YTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADVLYDCLPLYHSAGNIMGVGQCVIYGLTVVL-RKKFSASRFWDDC 142
Cdd:cd05917 9 FTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLCIPVPLFHCFGSVLGVLACLTHGATMVFpSPSFDPLAVLEAI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 143 VKYNCTVVQ-----YIGEicrylLRQPVRDVEQRHRVRLAV--GNGLRPAIWEEFTQRFGVPQIGEFYGATECNCSIAN- 214
Cdd:cd05917 89 EKEKCTALHgvptmFIAE-----LEHPDFDKFDLSSLRTGImaGAPCPPELMKRVIEVMNMKDVTIAYGMTETSPVSTQt 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 215 -----MDGKVGSCGfnsRILTHVYpirlVKVnedtmeplRDSEGLCIPcQPGEPGLLVgqinqqdpLRRFD---GYVSD- 285
Cdd:cd05917 164 rtddsIEKRVNTVG---RIMPHTE----AKI--------VDPEGGIVP-PVGVPGELC--------IRGYSvmkGYWNDp 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 286 SATNKKIahsvfrKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPGVeG 365
Cdd:cd05917 220 EKTAEAI------DGDGWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERY-G 292
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907189430 366 KAGMAAIA-DPHSQLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQKTRLQ 421
Cdd:cd05917 293 EEVCAWIRlKEGAELTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
22-421 |
6.92e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 89.10 E-value: 6.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 22 GDLGPESILPDTQLLDPMLAEAPTTPLAQAPGKGMDDRLFYIYTSGTTGLPKAAIVVHSRYYRIAA-FGHHSYSMRAADV 100
Cdd:PRK09088 100 GDDAVAAGRTDVEDLAAFIASADALEPADTPSIPPERVSLILFTSGTSGQPKGVMLSERNLQQTAHnFGVLGRVDAHSSF 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 101 LYDClPLYHSAGNIMGVGQCVIYGLTVVLRKKFSASRFWDDCVKYNCTVVQYIG--EICRYLLRQPVRDVEQ-RHRVRLA 177
Cdd:PRK09088 180 LCDA-PMFHIIGLITSVRPVLAVGGSILVSNGFEPKRTLGRLGDPALGITHYFCvpQMAQAFRAQPGFDAAAlRHLTALF 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 178 VGNGLRPAI----WEE----FTQRFGVPQIGEFYGATeCNCSIanMDGKVGSCGfnsrILTHVYPIRLVKVNEdtmeplR 249
Cdd:PRK09088 259 TGGAPHAAEdilgWLDdgipMVDGFGMSEAGTVFGMS-VDCDV--IRAKAGAAG----IPTPTVQTRVVDDQG------N 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 250 DseglcipCQPGEPG--LLVGQinqqdplRRFDGYVSDSATNKKIahsvfRKGDSAYLSGDVLVMDELGYMYFRDRSGDT 327
Cdd:PRK09088 326 D-------CPAGVPGelLLRGP-------NLSPGYWRRPQATARA-----FTGDGWFRTGDIARRDADGFFWVVDRKKDM 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 328 FRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPGvEGKAGMAAIA-DPHSQLDPNSMYQELQKVLASYARPIFLRLLPQ 406
Cdd:PRK09088 387 FISGGENVYPAEIEAVLADHPGIRECAVVGMADAQ-WGEVGYLAIVpADGAPLDLERIRSHLSTRLAKYKVPKHLRLVDA 465
|
410
....*....|....*
gi 1907189430 407 VDTTGTFKIQKTRLQ 421
Cdd:PRK09088 466 LPRTASGKLQKARLR 480
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
36-415 |
2.08e-18 |
|
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: 87.15 E-value: 2.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 36 LDPMLAEAPTTPLAQAPG-------KGMDDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADVLYDCLPLY 108
Cdd:cd05935 56 INPMLKERELEYILNDSGakvavvgSELDDLALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPSDVILACLPLF 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 109 HSAGNIMGVGQCVIYGLTVVLRKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPvrDVEQRHRVRLAV----GNGLRP 184
Cdd:cd05935 136 HVTGFVGSLNTAVYVGGTYVLMARWDRETALELIEKYKVTFWTNIPTMLVDLLATP--EFKTRDLSSLKVltggGAPMPP 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 185 AIWEEFTQRFGVPQIgEFYGATEcNCSianmdgkvgscgfnsriLTHVYPIRLVKVNEDTMePLRDSEGLCIPCQPGE-- 262
Cdd:cd05935 214 AVAEKLLKLTGLRFV-EGYGLTE-TMS-----------------QTHTNPPLRPKLQCLGI-P*FGVDARVIDIETGRel 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 263 PGLLVGQINQQDPlRRFDGYVSDSATNKKIAhsVFRKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEA 342
Cdd:cd05935 274 PPNEVGEIVVRGP-QIFKGYWNRPEETEESF--IEIKGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEA 350
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907189430 343 VLSRLLGQTDVAVYGVAVP--GVEGKAGMAAIADPHSQLDPNSMYQELQKVLASYARP---IFLRLLPQvdtTGTFKI 415
Cdd:cd05935 351 KLYKHPAI*EVCVISVPDErvGEEVKAFIVLRPEYRGKVTEEDIIEWAREQMAAYKYPrevEFVDELPR---SASGKI 425
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
57-415 |
2.32e-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: 341246 [Multi-domain] Cd Length: 457 Bit Score: 87.11 E-value: 2.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 57 DDRLFYIYTSGTTGLPKAAIVVHsRYYRIAAFGHHSY-SMRAADVLYDCLPLYHSAGnIMGVGQCVIYGLTVVLRKKFSA 135
Cdd:cd05922 117 EDLALLLYTSGSTGSPKLVRLSH-QNLLANARSIAEYlGITADDRALTVLPLSYDYG-LSVLNTHLLRGATLVLTNDGVL 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 136 SR-FWDDCVKYNCT---VVQYIGEICRYLLRQP-----VRDVEQrhrvrlaVGNGLRPAIWEEFTQRFGVPQIGEFYGAT 206
Cdd:cd05922 195 DDaFWEDLREHGATglaGVPSTYAMLTRLGFDPaklpsLRYLTQ-------AGGRLPQETIARLRELLPGAQVYVMYGQT 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 207 ECNCSIANMDG-----KVGSCGfnsrilthvypirlVKVNEDTMEPLRDSEGlciPCQPGEPGLLVgqinqqdpLRR--- 278
Cdd:cd05922 268 EATRRMTYLPPerileKPGSIG--------------LAIPGGEFEILDDDGT---PTPPGEPGEIV--------HRGpnv 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 279 FDGYVSDSATNKKIAhsvfRKGDSAYlSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGV 358
Cdd:cd05922 323 MKGYWNDPPYRRKEG----RGGGVLH-TGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGL 397
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907189430 359 AVPGVEGKAgMAAIADPHSQLDPNSMYqeLQKVLASYARPIFLRLLPQVDTTGTFKI 415
Cdd:cd05922 398 PDPLGEKLA-LFVTAPDKIDPKDVLRS--LAERLPPYKVPATVRVVDELPLTASGKV 451
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
38-420 |
9.86e-18 |
|
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: 85.50 E-value: 9.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 38 PMLAEAPTTPlaqapgkgmDDRLFYIYTSGTTGLPKAAIVVHSRYYRIA-AFGHHSYSMRAADVLYDCLPLYHSagniMG 116
Cdd:cd05959 153 EQLKPAATHA---------DDPAFWLYSSGSTGRPKGVVHLHADIYWTAeLYARNVLGIREDDVCFSAAKLFFA----YG 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 117 VGQCVIY----GLTVVLRKKF-SASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVEQRHRVRLAV--GNGLRPAIWEE 189
Cdd:cd05959 220 LGNSLTFplsvGATTVLMPERpTPAAVFKRIRRYRPTVFFGVPTLYAAMLAAPNLPSRDLSSLRLCVsaGEALPAEVGER 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 190 FTQRFGVpQIGEFYGATEC-NCSIANMDGKV--GSCGfnsrilTHV--YPIRLVkvnEDTMEPLRDSEglcipcqPGE-- 262
Cdd:cd05959 300 WKARFGL-DILDGIGSTEMlHIFLSNRPGRVryGTTG------KPVpgYEVELR---DEDGGDVADGE-------PGEly 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 263 ---PGLLVGQINQQDPLRR-FDGYvsdsatnkkiahsvfrkgdsAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTT 338
Cdd:cd05959 363 vrgPSSATMYWNNRDKTRDtFQGE--------------------WTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPF 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 339 EVEAVLsrllgQTDVAVYGVAVPGVEGKAGM----AAIADPHSQLDPNSMYQELQK----VLASYARP---IFLRLLPQv 407
Cdd:cd05959 423 EVESAL-----VQHPAVLEAAVVGVEDEDGLtkpkAFVVLRPGYEDSEALEEELKEfvkdRLAPYKYPrwiVFVDELPK- 496
|
410
....*....|...
gi 1907189430 408 dtTGTFKIQKTRL 420
Cdd:cd05959 497 --TATGKIQRFKL 507
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
56-361 |
9.97e-17 |
|
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: 82.16 E-value: 9.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 56 MDDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADVLYDCLPLYHSAGNIMGVGQCVIYGLTVVLRK-KFS 134
Cdd:cd05969 88 PEDPTLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLDLHPDDIYWCTADPGWVTGTVYGIWAPWLNGVTNVVYEgRFD 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 135 ASRFWDDCVKYNCTVVQYIGEICRYLLR---QPVRDVEQRH-RVRLAVGNGLRPAI--WEEftQRFGVPqIGEFYGATEC 208
Cdd:cd05969 168 AESWYGIIERVKVTVWYTAPTAIRMLMKegdELARKYDLSSlRFIHSVGEPLNPEAirWGM--EVFGVP-IHDTWWQTET 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 209 NC-SIAN---MDGKVGSCGfnsrilthvYPIRLVK--VNEDTMEPLRDSEGLCIPCQPGEPGLLVGQINQQDplrRFDGY 282
Cdd:cd05969 245 GSiMIANypcMPIKPGSMG---------KPLPGVKaaVVDENGNELPPGTKGILALKPGWPSMFRGIWNDEE---RYKNS 312
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907189430 283 vsdsatnkkiahsvFRKGdsAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVP 361
Cdd:cd05969 313 --------------FIDG--WYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDP 375
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
31-420 |
1.39e-16 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 82.05 E-value: 1.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 31 PDTQLLDPMLA--EAPTTPLAQAPGKgmddrlfYIYTSGTTGLPK-----AAIVVHSRYY---RIAAFGHHSySMRAadV 100
Cdd:PRK12406 131 AGAIDWEGWLAqqEPYDGPPVPQPQS-------MIYTSGTTGHPKgvrraAPTPEQAAAAeqmRALIYGLKP-GIRA--L 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 101 LYDclPLYHSAGNIMGVgQCVIYGLTVVLRKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQP--VR---DVEQ-RHRV 174
Cdd:PRK12406 201 LTG--PLYHSAPNAYGL-RAGRLGGVLVLQPRFDPEELLQLIERHRITHMHMVPTMFIRLLKLPeeVRakyDVSSlRHVI 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 175 RLAvgnGLRPA-IWEEFTQRFGvPQIGEFYGATECncsianmdGKVGSCGfNSRILTHvyPIRLVKVNEDTMEPLRDSEG 253
Cdd:PRK12406 278 HAA---APCPAdVKRAMIEWWG-PVIYEYYGSTES--------GAVTFAT-SEDALSH--PGTVGKAAPGAELRFVDEDG 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 254 LCIPcqPGEPGllvgqinqqDPLRRFDGYVSDSATNKKIAHSVFRKGDsAYLSGDVLVMDELGYMYFRDRSGDTFRWRGE 333
Cdd:PRK12406 343 RPLP--QGEIG---------EIYSRIAGNPDFTYHNKPEKRAEIDRGG-FITSGDVGYLDADGYLFLCDRKRDMVISGGV 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 334 NVSTTEVEAVLSRLLGQTDVAVYGvaVPGVE-GKAGMAAI-ADPHSQLDPNSMYQELQKVLASYARPIFLRLLPQVDTTG 411
Cdd:PRK12406 411 NIYPAEIEAVLHAVPGVHDCAVFG--IPDAEfGEALMAVVePQPGATLDEADIRAQLKARLAGYKVPKHIEIMAELPRED 488
|
....*....
gi 1907189430 412 TFKIQKTRL 420
Cdd:PRK12406 489 SGKIFKRRL 497
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
20-420 |
2.48e-16 |
|
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: 80.88 E-value: 2.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 20 CSGDLGPESILPDTQLlDPMLAEAPTTPLA-QAPGKGMddrlfyIYTSGTTGLPKA------AIVVHSRYYRIAAFGhhs 92
Cdd:cd05929 94 CGLFTGGGALDGLEDY-EAAEGGSPETPIEdEAAGWKM------LYSGGTTGRPKGikrglpGGPPDNDTLMAAALG--- 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 93 YSMRAADVLYDCLPLYHSAGNI--MGVgqcVIYGLTVVLRKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQP--VRDV 168
Cdd:cd05929 164 FGPGADSVYLSPAPLYHAAPFRwsMTA---LFMGGTLVLMEKFDPEEFLRLIERYRVTFAQFVPTMFVRLLKLPeaVRNA 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 169 EQRHRVRLAVGNGLRPAIW-EEFTQRFGVPQIGEFYGATECNcsianmdgkvGSCGFNS-RILTHvyPIRLVKVNEDTME 246
Cdd:cd05929 241 YDLSSLKRVIHAAAPCPPWvKEQWIDWGGPIIWEYYGGTEGQ----------GLTIINGeEWLTH--PGSVGRAVLGKVH 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 247 pLRDSEGLciPCQPGEPGLLVgqinqqdplrrFDGYVSDSATNK--KIAHSVFRKGDSAYlsGDVLVMDELGYMYFRDRS 324
Cdd:cd05929 309 -ILDEDGN--EVPPGEIGEVY-----------FANGPGFEYTNDpeKTAAARNEGGWSTL--GDVGYLDEDGYLYLTDRR 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 325 GDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGvaVPGVE-GKAGMAAIaDPHSQLDPNSMYQE-----LQKVLASYARP 398
Cdd:cd05929 373 SDMIISGGVNIYPQEIENALIAHPKVLDAAVVG--VPDEElGQRVHAVV-QPAPGADAGTALAEeliafLRDRLSRYKCP 449
|
410 420
....*....|....*....|....*
gi 1907189430 399 ---IFLRLLPQVDTTgtfKIQKTRL 420
Cdd:cd05929 450 rsiEFVAELPRDDTG---KLYRRLL 471
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
27-398 |
2.82e-16 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 81.20 E-value: 2.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 27 ESILPDTQLLDPMLAEAPTtplaqaPGKgmDDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHH--SYSMRAADVLYDC 104
Cdd:PRK05605 197 ETLVDAAIGGDGSDVSHPR------PTP--DDVALILYTSGTTGKPKGAQLTHRNLFANAAQGKAwvPGLGDGPERVLAA 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 105 LPLYHSAGNIMGVGQCVIYGLTVVLRKKFSASRFWDDCVKYNCTVVQYIGEIcrYllrQPVRDVEQRHRVRLavgNGLRP 184
Cdd:PRK05605 269 LPMFHAYGLTLCLTLAVSIGGELVLLPAPDIDLILDAMKKHPPTWLPGVPPL--Y---EKIAEAAEERGVDL---SGVRN 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 185 AI-------------WEEFTQRFGVpqigEFYGATECN----CSIANMDGKVGSCG--FNSRIlthvypIRLVkvneDTM 245
Cdd:PRK05605 341 AFsgamalpvstvelWEKLTGGLLV----EGYGLTETSpiivGNPMSDDRRPGYVGvpFPDTE------VRIV----DPE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 246 EPLRDseglcIPcqPGEPG-LLVgqinqQDPlRRFDGYVSDSATNKKIAHsvfrkgDSAYLSGDVLVMDELGYMYFRDRS 324
Cdd:PRK05605 407 DPDET-----MP--DGEEGeLLV-----RGP-QVFKGYWNRPEETAKSFL------DGWFRTGDVVVMEEDGFIRIVDRI 467
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907189430 325 GDTFRWRGENVSTTEVEAVLSRLLGQTDVAVygVAVPGVEGKAGMAA--IADPHSQLDPNSMYQELQKVLASYARP 398
Cdd:PRK05605 468 KELIITGGFNVYPAEVEEVLREHPGVEDAAV--VGLPREDGSEEVVAavVLEPGAALDPEGLRAYCREHLTRYKVP 541
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
2-409 |
2.95e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 81.13 E-value: 2.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 2 AAAVAEVSEQLGKSLLKFCSGDLGPESIlPDTQLLDPMLAEAPTTPLAQAPGKGMddrlFYIYTSGTTGLPKAAIVVH-S 80
Cdd:PRK07788 157 TDLLSALPPDLGRLRAWGGNPDDDEPSG-STDETLDDLIAGSSTAPLPKPPKPGG----IVILTSGTTGTPKGAPRPEpS 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 81 RYYRIAAFGHHsYSMRAADVLYDCLPLYHSagniMGVGQCVI---YGLTVVLRKKFSASRFWDDCVKYNCTVVQYIGEIC 157
Cdd:PRK07788 232 PLAPLAGLLSR-VPFRAGETTLLPAPMFHA----TGWAHLTLamaLGSTVVLRRRFDPEATLEDIAKHKATALVVVPVML 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 158 RYLLRQPvRDVEQRH-----RVRLAVGNGLRPAIWEEFTQRFGvPQIGEFYGATECN-CSIANMD------GKVGScgfn 225
Cdd:PRK07788 307 SRILDLG-PEVLAKYdtsslKIIFVSGSALSPELATRALEAFG-PVLYNLYGSTEVAfATIATPEdlaeapGTVGR---- 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 226 srilthvyPIRLVKVNedtmepLRDSEGLCIPcqPGEPG-LLVGQINQqdplrrFDGYVSDSatNKKIAHSVFRKGDSAY 304
Cdd:PRK07788 381 --------PPKGVTVK------ILDENGNEVP--RGVVGrIFVGNGFP------FEGYTDGR--DKQIIDGLLSSGDVGY 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 305 LsgdvlvmDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGvaVPGVEGKAGMAA--IADPHSQLDPN 382
Cdd:PRK07788 437 F-------DEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIG--VDDEEFGQRLRAfvVKAPGAALDED 507
|
410 420 430
....*....|....*....|....*....|
gi 1907189430 383 SMYQELQKVLASYARP---IFLRLLPQVDT 409
Cdd:PRK07788 508 AIKDYVRDNLARYKVPrdvVFLDELPRNPT 537
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
57-361 |
4.85e-16 |
|
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: 80.07 E-value: 4.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 57 DDRLFYIYTSGTTGLPKAAIVVH----SRYYRIAAFghhsYSMRAADVLYDCLPLYHSAGNIMGVGQCVIYGLTVVLR-- 130
Cdd:cd05909 147 DDPAVILFTSGSEGLPKGVVLSHknllANVEQITAI----FDPNPEDVVFGALPFFHSFGLTGCLWLPLLSGIKVVFHpn 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 131 ----KKFSasRFWDDcvkYNCTVVQYIGEICRYLLR--QPvrdvEQRHRVRLAV--GNGLRPAIWEEFTQRFGVPqIGEF 202
Cdd:cd05909 223 pldyKKIP--ELIYD---KKATILLGTPTFLRGYARaaHP----EDFSSLRLVVagAEKLKDTLRQEFQEKFGIR-ILEG 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 203 YGATEC----NCSIANMDGKVGSCGfnsRILTHVyPIRLVKVnedtmeplrdsEGLCiPCQPGEPGLLVGQINQqdplrR 278
Cdd:cd05909 293 YGTTECspviSVNTPQSPNKEGTVG---RPLPGM-EVKIVSV-----------ETHE-EVPIGEGGLLLVRGPN-----V 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 279 FDGYVSDSatnkkiAHSVFRKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQtDVAVYGV 358
Cdd:cd05909 352 MLGYLNEP------ELTSFAFGDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEILPE-DNEVAVV 424
|
...
gi 1907189430 359 AVP 361
Cdd:cd05909 425 SVP 427
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
25-358 |
6.22e-16 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 79.93 E-value: 6.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 25 GPESILPDTQLLDPMLAEAPTTPLAQAP-GKGMDDRLFyIYTSGTTGLPKAAIVVHSryyRIAAFGHH---SYSMRAADV 100
Cdd:PRK05852 144 GGDSGPSGGTLSVHLDAATEPTPATSTPeGLRPDDAMI-MFTGGTTGLPKMVPWTHA---NIASSVRAiitGYRLSPRDA 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 101 LYDCLPLYHSAGNIMGVGQCVIYGLTVVL--RKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVEQRHRVRL-- 176
Cdd:PRK05852 220 TVAVMPLYHGHGLIAALLATLASGGAVLLpaRGRFSAHTFWDDIKAVGATWYTAVPTIHQILLERAATEPSGRKPAALrf 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 177 --AVGNGLRPAIWEEFTQRFGVPQIgEFYGATECNCSIANMDGKVGSCGFNSRILTHVypirlvkVNEDTMEPLR--DSE 252
Cdd:PRK05852 300 irSCSAPLTAETAQALQTEFAAPVV-CAFGMTEATHQVTTTQIEGIGQTENPVVSTGL-------VGRSTGAQIRivGSD 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 253 GLciPCQPGEpgllVGQINQQDP--LRrfdGYVSDSA-TNKKIAHSVFRKGDSAYLSGDvlvmdelGYMYFRDRSGDTFR 329
Cdd:PRK05852 372 GL--PLPAGA----VGEVWLRGTtvVR---GYLGDPTiTAANFTDGWLRTGDLGSLSAA-------GDLSIRGRIKELIN 435
|
330 340
....*....|....*....|....*....
gi 1907189430 330 WRGENVSTTEVEAVLSRLLGQTDVAVYGV 358
Cdd:PRK05852 436 RGGEKISPERVEGVLASHPNVMEAAVFGV 464
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
36-422 |
8.55e-16 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 79.61 E-value: 8.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 36 LDPMLAEAPTTPLAQAPGKGMDDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADVLYDCLPLYHSAGNIM 115
Cdd:PRK07529 192 FDAELARQPGDRLFSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPGDTVFCGLPLFHVNALLV 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 116 GVGQCVIYGLTVVL------RKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPV--RDVEQrhrVRLAVGNG--LRPA 185
Cdd:PRK07529 272 TGLAPLARGAHVVLatpqgyRGPGVIANFWKIVERYRINFLSGVPTVYAALLQVPVdgHDISS---LRYALCGAapLPVE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 186 IWEEFTQRFGVPqIGEFYGATECNC--SIANMDG--KVGSCGFnsRI-LTHVypiRLVKVNEDTmEPLRDseglcipCQP 260
Cdd:PRK07529 349 VFRRFEAATGVR-IVEGYGLTEATCvsSVNPPDGerRIGSVGL--RLpYQRV---RVVILDDAG-RYLRD-------CAV 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 261 GEPGLLVgqinQQDPlRRFDGYVsDSATNKKIahsvfRKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEV 340
Cdd:PRK07529 415 DEVGVLC----IAGP-NVFSGYL-EAAHNKGL-----WLEDGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAI 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 341 EAVLSRLlgqtdvavygvavPGVegkAGMAAIA--DPHS--------QLDPNSMYQELQkvLASYAR---------PIFL 401
Cdd:PRK07529 484 EEALLRH-------------PAV---ALAAAVGrpDAHAgelpvayvQLKPGASATEAE--LLAFARdhiaeraavPKHV 545
|
410 420
....*....|....*....|.
gi 1907189430 402 RLLPQVDTTGTFKIQKTRLQR 422
Cdd:PRK07529 546 RILDALPKTAVGKIFKPALRR 566
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
37-419 |
8.94e-16 |
|
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341289 [Multi-domain] Cd Length: 587 Bit Score: 79.54 E-value: 8.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 37 DPMLAEAPT--TPLAQAPgkgmDDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFG-HHSYSMRAADVLYdclpLYHSAGN 113
Cdd:cd17634 214 RDLIAKASPehQPEAMNA----EDPLFILYTSGTTGKPKGVLHTTGGYLVYAATTmKYVFDYGPGDIYW----CTADVGW 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 114 IMGvGQCVIY-----GLTVVLRKKF----SASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVEqRH-----RVRLAVG 179
Cdd:cd17634 286 VTG-HSYLLYgplacGATTLLYEGVpnwpTPARMWQVVDKHGVNILYTAPTAIRALMAAGDDAIE-GTdrsslRILGSVG 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 180 NGLRPAIWEEFTQRFG---VPQIGEFYGATECNCSIANMDGKVGSCGFNSRILTHVYPIRLVKVNEDTMEPLRDSE-GLC 255
Cdd:cd17634 364 EPINPEAYEWYWKKIGkekCPVVDTWWQTETGGFMITPLPGAIELKAGSATRPVFGVQPAVVDNEGHPQPGGTEGNlVIT 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 256 IPCQPGEPGLLvgqinqQDPLRRFDGYvsdsatnkkiahsvFRKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENV 335
Cdd:cd17634 444 DPWPGQTRTLF------GDHERFEQTY--------------FSTFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRL 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 336 STTEVEAVLSRLLGQTDVAVYGVAVPgVEGKAGMAAIADPHSQLDPNSMYQEL-QKVLASYARPIFLRLLPQVDTtgtfk 414
Cdd:cd17634 504 GTAEIESVLVAHPKVAEAAVVGIPHA-IKGQAPYAYVVLNHGVEPSPELYAELrNWVRKEIGPLATPDVVHWVDS----- 577
|
....*
gi 1907189430 415 IQKTR 419
Cdd:cd17634 578 LPKTR 582
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
46-406 |
1.17e-15 |
|
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: 79.09 E-value: 1.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 46 TPLAQAPGKGMDDRLFYIYTSGTTGLPKAAIVVH-SRYYRIAAFGHHS-YSMRAADVLYDCLPLYHSAGNIMGVGQCVIY 123
Cdd:cd05923 139 GPLIEDPPREPEQPAFVFYTSGTTGLPKGAVIPQrAAESRVLFMSTQAgLRHGRHNVVLGLMPLYHVIGFFAVLVAALAL 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 124 GLTVVLRKKFSASRfwddcvkynctVVQYIGE---ICRYL-----------LRQPVRDVEQRHRVRLAvGNGLRPAIWEE 189
Cdd:cd05923 219 DGTYVVVEEFDPAD-----------ALKLIEQervTSLFAtpthldalaaaAEFAGLKLSSLRHVTFA-GATMPDAVLER 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 190 FTQRFGVPQIgEFYGATECNCSIANMDGKVGSC---GFNSRIlthvypiRLVKVNEDTMEPLRDSEGLCIPCQPGEPGLL 266
Cdd:cd05923 287 VNQHLPGEKV-NIYGTTEAMNSLYMRDARTGTEmrpGFFSEV-------RIVRIGGSPDEALANGEEGELIVAAAADAAF 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 267 VGQINQQDplrrfdgyvsdsATNKKIAHSVFRKGDSAYL--SGDVLVMDELGYMYFrdrSGdtfrwrGENVSTTEVEAVL 344
Cdd:cd05923 359 TGYLNQPE------------ATAKKLQDGWYRTGDVGYVdpSGDVRILGRVDDMII---SG------GENIHPSEIERVL 417
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 345 SRLLGQTDVAVYGVAvpgvEGKAGMAAIADPHSQLDPNSMyQELQKV-----LASYARP---IFLRLLPQ 406
Cdd:cd05923 418 SRHPGVTEVVVIGVA----DERWGQSVTACVVPREGTLSA-DELDQFcraseLADFKRPrryFFLDELPK 482
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
25-358 |
1.37e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 78.82 E-value: 1.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 25 GPESILPDTQLLDPMLAEAPTTPLAQAPGkgmDDRLFYIYTSGTTGLPKAAIVVH----SRYYR-IAAFGhhsysMRAAD 99
Cdd:PRK08316 142 GREAPGGWLDFADWAEAGSVAEPDVELAD---DDLAQILYTSGTESLPKGAMLTHraliAEYVScIVAGD-----MSADD 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 100 VLYDCLPLYHSAGniMGV--GQCVIYGLTVVLRKKFSASRFWDDCVKYNC-------TVvqYIGeicryLLRQPVRDveq 170
Cdd:PRK08316 214 IPLHALPLYHCAQ--LDVflGPYLYVGATNVILDAPDPELILRTIEAERItsffappTV--WIS-----LLRHPDFD--- 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 171 rhRVRLAvgnGLRPA----------IWEEFTQRFgvPQIG--EFYGATEcncsIANM---------DGKVGSCG---FN- 225
Cdd:PRK08316 282 --TRDLS---SLRKGyygasimpveVLKELRERL--PGLRfyNCYGQTE----IAPLatvlgpeehLRRPGSAGrpvLNv 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 226 -SRIlthvypirlvkVNEDtMEPLrdseglcipcQPGEPGLLVGQINQQdplrrFDGYVSDSAtnkKIAHSvFRKGdsAY 304
Cdd:PRK08316 351 eTRV-----------VDDD-GNDV----------APGEVGEIVHRSPQL-----MLGYWDDPE---KTAEA-FRGG--WF 397
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1907189430 305 LSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGV 358
Cdd:PRK08316 398 HSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGL 451
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
63-417 |
1.45e-15 |
|
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: 77.54 E-value: 1.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 63 IYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADVLYDCLPLYHSAGNIMGVGQCVIYGLTVVLRKKFSASRFWDDC 142
Cdd:cd17638 6 MFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIINPFFHTFGYKAGIVACLLTGATVVPVAVFDVDAILEAI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 143 VKYNCTVVQYIGEICRYLLRQPVRDVEQRHRVRLAV-GNGLRPAIW-EEFTQRFGVPQIGEFYGATECNCSianmdgkvg 220
Cdd:cd17638 86 ERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVtGAATVPVELvRRMRSELGFETVLTAYGLTEAGVA--------- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 221 scgfnsrilthvypirlvkvnedTM-EPLRDSEGLCIPCQPGEPGLLVGQINQQDPLRR----FDGYVSD-SATNKKIah 294
Cdd:cd17638 157 -----------------------TMcRPGDDAETVATTCGRACPGFEVRIADDGEVLVRgynvMQGYLDDpEATAEAI-- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 295 svfrKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPGVeGKAGMA-AIA 373
Cdd:cd17638 212 ----DADGWLHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERM-GEVGKAfVVA 286
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1907189430 374 DPHSQLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQK 417
Cdd:cd17638 287 RPGVTLTEEDVIAWCRERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
30-420 |
1.55e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 78.63 E-value: 1.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 30 LPDTQLLDPMLA---EAPTTPLAQAPGKGMDDRLFYIYT-SGTTGLPKaaIVVHS-----RYYRIAAfghHSYSMRAADV 100
Cdd:PRK06164 150 TPAPAPGARVQLfalPDPAPPAAAGERAADPDAGALLFTtSGTTSGPK--LVLHRqatllRHARAIA---RAYGYDPGAV 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 101 LYDCLPLYHSAGNIMGVGqCVIYGLTVVLRKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVEQRHRVRLAVGN 180
Cdd:PRK06164 225 LLAALPFCGVFGFSTLLG-ALAGGAPLVCEPVFDAARTARALRRHRVTHTFGNDEMLRRILDTAGERADFPSARLFGFAS 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 181 gLRPAiWEEFTQRF---GVPQIGeFYGATECncsIANMDGKVGSCGFNSRIL---THVYPIRLVKVnedtmeplRDSEGL 254
Cdd:PRK06164 304 -FAPA-LGELAALArarGVPLTG-LYGSSEV---QALVALQPATDPVSVRIEgggRPASPEARVRA--------RDPQDG 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 255 CIpCQPGEPGllvgQINQQDPlRRFDGYVSD-SATNKKI-AHSVFRKGDSAYLSGDvlvmdelGYMYFRDRSGDTFRWRG 332
Cdd:PRK06164 370 AL-LPDGESG----EIEIRAP-SLMRGYLDNpDATARALtDDGYFRTGDLGYTRGD-------GQFVYQTRMGDSLRLGG 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 333 ENVSTTEVEAVLSRLLGQTDVAVYGVAvpgVEGKAGMAA--IADPHSQLDPNSMYQELQKVLASY---ARPIFLRLLPQV 407
Cdd:PRK06164 437 FLVNPAEIEHALEALPGVAAAQVVGAT---RDGKTVPVAfvIPTDGASPDEAGLMAACREALAGFkvpARVQVVEAFPVT 513
|
410
....*....|...
gi 1907189430 408 DTTGTFKIQKTRL 420
Cdd:PRK06164 514 ESANGAKIQKHRL 526
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
63-420 |
1.79e-15 |
|
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: 78.19 E-value: 1.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 63 IYTSGTTGLPKAAIVVHSR-YYRIAAFGHHsYSMRAADVLYDCLPLYHSAGNIMGVGQCVIYGLTVVLRKKFSASRFWDD 141
Cdd:cd05903 99 LFTSGTTGEPKGVMHSHNTlSASIRQYAER-LGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQDIWDPDKALAL 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 142 CVKYNCTVVQ----YIGEICRYLLRQPvrDVEQRHRVRLAVGNGLRPAIWEEFTQRFGVpQIGEFYGATECNcsianmdG 217
Cdd:cd05903 178 MREHGVTFMMgatpFLTDLLNAVEEAG--EPLSRLRTFVCGGATVPRSLARRAAELLGA-KVCSAYGSTECP-------G 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 218 KVGSC--GFNSRIL-THVYPIRLVKVNedtmepLRDSEGLCIPcqPGEpgllVGQINQQDPlRRFDGYVSDSATNKKIAH 294
Cdd:cd05903 248 AVTSItpAPEDRRLyTDGRPLPGVEIK------VVDDTGATLA--PGV----EGELLSRGP-SVFLGYLDRPDLTADAAP 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 295 SVFrkgdsaYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVygVAVPgvEGKAGMAAIA- 373
Cdd:cd05903 315 EGW------FRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAV--VALP--DERLGERACAv 384
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1907189430 374 ----DPHSqLDPNSMYQELQKV-LASYARPIFLRLLPQVDTTGTFKIQKTRL 420
Cdd:cd05903 385 vvtkSGAL-LTFDELVAYLDRQgVAKQYWPERLVHVDDLPRTPSGKVQKFRL 435
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
57-422 |
2.08e-15 |
|
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: 78.12 E-value: 2.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 57 DDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAF-------GHHSYSMRAADVLYDClplyhSAGNIMGvgqCVIYGLTVVL 129
Cdd:cd17653 105 DDLAYIIFTSGSTGIPKGVMVPHRGVLNYVSQpparldvGPGSRVAQVLSIAFDA-----CIGEIFS---TLCNGGTLVL 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 130 RkkfSASRFWDDcVKYNCTVVQYIGEICRYLlrqPVRDVEQRHRVRLAvGNGLRPAIWEEFTqrfGVPQIGEFYGATECN 209
Cdd:cd17653 177 A---DPSDPFAH-VARTVDALMSTPSILSTL---SPQDFPNLKTIFLG-GEAVPPSLLDRWS---PGRRLYNAYGPTECT 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 210 CSIAN---MDGKVGSCGfnsrilthvYPIRLVKV---NEDTMEPLRDSEG-LCIpcqpGEPGLLVGQINQQdplrrfdgy 282
Cdd:cd17653 246 ISSTMtelLPGQPVTIG---------KPIPNSTCyilDADLQPVPEGVVGeICI----SGVQVARGYLGNP--------- 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 283 vsdSATNKKIAHSVFRKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQtdvaVYGVAVPG 362
Cdd:cd17653 304 ---ALTASKFVPDPFWPGSRMYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEVVLQSQPE----VTQAAAIV 376
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 363 VEGKagMAAIADPHSqLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQKTRLQR 422
Cdd:cd17653 377 VNGR--LVAFVTPET-VDVDGLRSELAKHLPSYAVPDRIIALDSFPLTANGKVDRKALRE 433
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
25-422 |
7.45e-15 |
|
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: 76.40 E-value: 7.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 25 GPESIlpdTQLLDPMLAEAPTTPLAQApGKGMDDRLFYIYTSGTTGLPKaAIVVHSRYyrIAAFghHSYSMRAADVLYDc 104
Cdd:cd05973 60 GPKAI---EHRLRTSGARLVVTDAANR-HKLDSDPFVMMFTSGTTGLPK-GVPVPLRA--LAAF--GAYLRDAVDLRPE- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 105 lplyHSAGNIMGVGQCviYGL-------------TVVLRKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVrDVEQR 171
Cdd:cd05973 130 ----DSFWNAADPGWA--YGLyyaitgplalghpTILLEGGFSVESTWRVIERLGVTNLAGSPTAYRLLMAAGA-EVPAR 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 172 HRVRLAV----GNGLRPAIWEEFTQRFGVPqIGEFYGATECNCSIANMDG-----KVGSCGFnsrilthVYP-IRLVKVN 241
Cdd:cd05973 203 PKGRLRRvssaGEPLTPEVIRWFDAALGVP-IHDHYGQTELGMVLANHHAlehpvHAGSAGR-------AMPgWRVAVLD 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 242 EDTMEPLrdseglcipcqPGEPGLLVGQInQQDPLRRFDGYvsdsatnkkiahsvFRKGDSA-----YLSGDVLVMDELG 316
Cdd:cd05973 275 DDGDELG-----------PGEPGRLAIDI-ANSPLMWFRGY--------------QLPDTPAidggyYLTGDTVEFDPDG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 317 YMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPG----VEGKAGMAAIADPHSQLDpNSMYQELQKVL 392
Cdd:cd05973 329 SFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPErtevVKAFVVLRGGHEGTPALA-DELQLHVKKRL 407
|
410 420 430
....*....|....*....|....*....|
gi 1907189430 393 ASYARPIFLRLLPQVDTTGTFKIQKTRLQR 422
Cdd:cd05973 408 SAHAYPRTIHFVDELPKTPSGKIQRFLLRR 437
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
40-425 |
1.37e-14 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 75.68 E-value: 1.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 40 LAEAPTTPLAQAPgKGMDDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADVLYDCLPLYHSAGNIMGVGQ 119
Cdd:PRK07514 140 AAAAAPDDFETVP-RGADDLAAILYTSGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPDDVLIHALPIFHTHGLFVATNV 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 120 CVIYGLTVVLRKKFSAsrfwDDCVKY--NCTVVqyIGEICRY--LLRQPVRDVEQRHRVRLAVgNGLRPAIWE---EFTQ 192
Cdd:PRK07514 219 ALLAGASMIFLPKFDP----DAVLALmpRATVM--MGVPTFYtrLLQEPRLTREAAAHMRLFI-SGSAPLLAEthrEFQE 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 193 RFGVPqIGEFYGATECNCSIAN-MDGK--VGSCGFnsrilthvyPIRLVKV---NEDTMEPLrdseglcipcQPGEpgll 266
Cdd:PRK07514 292 RTGHA-ILERYGMTETNMNTSNpYDGErrAGTVGF---------PLPGVSLrvtDPETGAEL----------PPGE---- 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 267 VGQINQQDPlRRFDGY--VSDsatnkKIAHSvFRkGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVL 344
Cdd:PRK07514 348 IGMIEVKGP-NVFKGYwrMPE-----KTAEE-FR-ADGFFITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEI 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 345 SRLLGQTDVAVYGVAVPGVeGKAGMAA-IADPHSQLDPNSMYQELQKVLASYARP---IFLRLLPQvDTTGtfKIQKTRL 420
Cdd:PRK07514 420 DELPGVVESAVIGVPHPDF-GEGVTAVvVPKPGAALDEAAILAALKGRLARFKQPkrvFFVDELPR-NTMG--KVQKNLL 495
|
....*
gi 1907189430 421 qREGF 425
Cdd:PRK07514 496 -REQY 499
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
2-428 |
1.52e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 75.85 E-value: 1.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 2 AAAVAEVSEQLgKSLLKFCSGDLGPEsilpdtqlLDPMLAEAPTTPLAQAPGKgMDDRLFYIYTSGTTGLPKAAIVVHSR 81
Cdd:PRK07470 118 AAAVRAASPDL-THVVAIGGARAGLD--------YEALVARHLGARVANAAVD-HDDPCWFFFTSGTTGRPKAAVLTHGQ 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 82 YyriaAF-------------GHHSYSMRAAdvlydclPLYHSAGnIMGVGQcVIYGLTVVL--RKKFSASRFWDDCVKYN 146
Cdd:PRK07470 188 M----AFvitnhladlmpgtTEQDASLVVA-------PLSHGAG-IHQLCQ-VARGAATVLlpSERFDPAEVWALVERHR 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 147 CTVVQYIGEICRYLLRQPVRDVEQRHRVRLAVGNGlRPAIWEEftQRFGVPQIG----EFYGATECNCSIANM------- 215
Cdd:PRK07470 255 VTNLFTVPTILKMLVEHPAVDRYDHSSLRYVIYAG-APMYRAD--QKRALAKLGkvlvQYFGLGEVTGNITVLppalhda 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 216 -DG---KVGSCGFnsrilthvypirlvkvnEDT-ME-PLRDSEGLciPCQPGEpgllVGQINQQDPlRRFDGYVSDSATN 289
Cdd:PRK07470 332 eDGpdaRIGTCGF-----------------ERTgMEvQIQDDEGR--ELPPGE----TGEICVIGP-AVFAGYYNNPEAN 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 290 KKiahsVFRKGdsAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPgVEGKAGM 369
Cdd:PRK07470 388 AK----AFRDG--WFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDP-VWGEVGV 460
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907189430 370 AA-IADPHSQLDPNSMYQELQKVLASYARP---IFLRLLPQvdtTGTFKIQKtRLQREGFDPR 428
Cdd:PRK07470 461 AVcVARDGAPVDEAELLAWLDGKVARYKLPkrfFFWDALPK---SGYGKITK-KMVREELEER 519
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
57-420 |
1.53e-14 |
|
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: 75.26 E-value: 1.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 57 DDRLFY-IYTSGTTGLPKAAIVVHsryyriAAFGHHSYSMRAAdvlY-----DCLPLYHSAGNIMGVGQ---CVIYGLTV 127
Cdd:cd05930 92 PDDLAYvIYTSGSTGKPKGVMVEH------RGLVNLLLWMQEA---YpltpgDRVLQFTSFSFDVSVWEifgALLAGATL 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 128 VLRKK---FSASRFWDDCVKYNCTVVQYIGEICRYLLRQPvrDVEQRHRVRLAV--GNGLRPAIWEEFTQRFGVPQIGEF 202
Cdd:cd05930 163 VVLPEevrKDPEALADLLAEEGITVLHLTPSLLRLLLQEL--ELAALPSLRLVLvgGEALPPDLVRRWRELLPGARLVNL 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 203 YGATECNcsianmdgkvgscgfnsrILTHVYPIRLVKVNEDTM---EPLRDSeGLCI------PCQPGEPG-LLVG--QI 270
Cdd:cd05930 241 YGPTEAT------------------VDATYYRVPPDDEEDGRVpigRPIPNT-RVYVldenlrPVPPGVPGeLYIGgaGL 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 271 NQqdplrrfdGYVSDSA-TNKKIAHSVFRKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLG 349
Cdd:cd05930 302 AR--------GYLNRPElTAERFVPNPFGPGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPG 373
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907189430 350 QTDVAVygVAVPGVEGKAGMAA--IADPHSQLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQKTRL 420
Cdd:cd05930 374 VREAAV--VAREDGDGEKRLVAyvVPDEGGELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
1-425 |
1.74e-14 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 75.58 E-value: 1.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 1 MAAAVAEVSEQLGKSLLkfcSGDLGPESILPdtqlLDPMLAEA-PTTPLAQAPGkgmDDRLFYIYTSGTTGLPKAAIVVH 79
Cdd:PRK07786 127 VATAVRDIVPLLSTVVV---AGGSSDDSVLG----YEDLLAEAgPAHAPVDIPN---DSPALIMYTSGTTGRPKGAVLTH 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 80 SRYYRIAAfgHHSYSMRA---ADVLYDCLPLYHSAGnIMGVGQCVIYGLTVVLR--KKFSASRFWDDCVKYNCTVV---- 150
Cdd:PRK07786 197 ANLTGQAM--TCLRTNGAdinSDVGFVGVPLFHIAG-IGSMLPGLLLGAPTVIYplGAFDPGQLLDVLEAEKVTGIflvp 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 151 -QYIGeICRYLLRQPvRDVEQRhrvrlAVGNGLRPA---IWEEFTQRFGVPQIGEFYGATECNCSIANMDG-----KVGS 221
Cdd:PRK07786 274 aQWQA-VCAEQQARP-RDLALR-----VLSWGAAPAsdtLLRQMAATFPEAQILAAFGQTEMSPVTCMLLGedairKLGS 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 222 CGfnsriltHVYPIRLVKVNEDTMEPLrdseglcipcQPGEpgllVGQINQQDPlrrfdGYVSDSATNKKIAHSVFRKGd 301
Cdd:PRK07786 347 VG-------KVIPTVAARVVDENMNDV----------PVGE----VGEIVYRAP-----TLMSGYWNNPEATAEAFAGG- 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 302 sAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVA------VPgvegkAGMAAIADP 375
Cdd:PRK07786 400 -WFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRAdekwgeVP-----VAVAAVRND 473
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1907189430 376 HSQLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQKTRLqREGF 425
Cdd:PRK07786 474 DAALTLEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKVLKTEL-RERY 522
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
58-422 |
1.97e-14 |
|
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: 73.90 E-value: 1.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 58 DRLFYIYTSGTTGLPKAaiVVHSRYYRIAAF--GHHSYSMRAADVLYDCLPLYHSAGnIMGVGQCVIYGLTVVLRKKFSA 135
Cdd:cd17630 1 RLATVILTSGSTGTPKA--VVHTAANLLASAagLHSRLGFGGGDSWLLSLPLYHVGG-LAILVRSLLAGAELVLLERNQA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 136 SRfwDDCVKYNCTVVQYIGEICRYLLRQPvRDVEQRHRVR-LAVGNGlrpAIWEEFTQRF---GVPqIGEFYGATE---C 208
Cdd:cd17630 78 LA--EDLAPPGVTHVSLVPTQLQRLLDSG-QGPAALKSLRaVLLGGA---PIPPELLERAadrGIP-LYTTYGMTEtasQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 209 NCSIANMDGKVGSCGfnsRILTHVyPIRLVKVNEDtmeplrdseglcipcQPGEPGLLVGQINQQDPLRRFDGyvsdsat 288
Cdd:cd17630 151 VATKRPDGFGRGGVG---VLLPGR-ELRIVEDGEI---------------WVGGASLAMGYLRGQLVPEFNED------- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 289 nkkiahSVFRKGDSAYLSGDvlvmdelGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPgvegKAG 368
Cdd:cd17630 205 ------GWFTTKDLGELHAD-------GRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDE----ELG 267
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907189430 369 MAAIA--DPHSQLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQKTRLQR 422
Cdd:cd17630 268 QRPVAviVGRGPADPAELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRA 323
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
45-422 |
2.05e-14 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 75.18 E-value: 2.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 45 TTPLAQAPGKGMDDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADVLYDCLPLYHSagniMGVGQCVIYG 124
Cdd:PRK13382 184 AAHAGQRPEPTGRKGRVILLTSGTTGTPKGARRSGPGGIGTLKAILDRTPWRAEEPTVIVAPMFHA----WGFSQLVLAA 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 125 L---TVVLRKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQP--VRDVEQRHRVRLAVGNG--LRPAIWEEFTQRFGvP 197
Cdd:PRK13382 260 SlacTIVTRRRFDPEATLDLIDRHRATGLAVVPVMFDRIMDLPaeVRNRYSGRSLRFAAASGsrMRPDVVIAFMDQFG-D 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 198 QIGEFYGATECN-CSIANMDGkvgscgfnsrilTHVYPIRLVKVNEDTMEPLRDSEGLCIPcqPGEpgllVGQI----NQ 272
Cdd:PRK13382 339 VIYNNYNATEAGmIATATPAD------------LRAAPDTAGRPAEGTEIRILDQDFREVP--TGE----VGTIfvrnDT 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 273 QdplrrFDGYVSDSATNkkiahsvFRKGDSAylSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTD 352
Cdd:PRK13382 401 Q-----FDGYTSGSTKD-------FHDGFMA--SGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAE 466
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 353 VAVYGVAVPGVEGKAGMAAIADPHSQLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQKTRLQR 422
Cdd:PRK13382 467 AAVIGVDDEQYGQRLAAFVVLKPGASATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQA 536
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
57-422 |
2.54e-14 |
|
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: 74.05 E-value: 2.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 57 DDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADVLYDCLPLYHSAGNIMGVGQCVIYGLTVVL------R 130
Cdd:cd05944 2 DDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVVLagpagyR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 131 KKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPV-RDVEQrhrVRLAVGNG--LRPAIWEEFTQRFGVPqIGEFYGATE 207
Cdd:cd05944 82 NPGLFDNFWKLVERYRITSLSTVPTVYAALLQVPVnADISS---LRFAMSGAapLPVELRARFEDATGLP-VVEGYGLTE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 208 CNCSIA----NMDGKVGSCGFNsrilthvYPIRLVKVNEDtmeplrDSEGLCI-PCQPGEpgllVGQINQQDPlRRFDGY 282
Cdd:cd05944 158 ATCLVAvnppDGPKRPGSVGLR-------LPYARVRIKVL------DGVGRLLrDCAPDE----VGEICVAGP-GVFGGY 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 283 V-SDSATNKKIAHSVFRKGDSAYLsgdvlvmDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRllgQTDVAVYGvAVP 361
Cdd:cd05944 220 LyTEGNKNAFVADGWLNTGDLGRL-------DADGYLFITGRAKDLIIRGGHNIDPALIEEALLR---HPAVAFAG-AVG 288
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 362 GVEGKAGMAAIAdpHSQLDPNSMYQELQkvLASYAR---------PIFLRLLPQVDTTGTFKIQKTRLQR 422
Cdd:cd05944 289 QPDAHAGELPVA--YVQLKPGAVVEEEE--LLAWARdhvperaavPKHIEVLEELPVTAVGKVFKPALRA 354
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
57-420 |
2.55e-14 |
|
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: 74.82 E-value: 2.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 57 DDRLFYIYTSGTTGLPKAAIVVHSRYYRIA-AFGHHSYSMRAADVLYDCLPLYHSagniMGVGQCVIY----GLTVVLRK 131
Cdd:cd05958 97 DDICILAFTSGTTGAPKATMHFHRDPLASAdRYAVNVLRLREDDRFVGSPPLAFT----FGLGGVLLFpfgvGASGVLLE 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 132 KFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVEQRHRVRLAV--GNGLRPAIWEEFTQRFGVPQIgEFYGATEC- 208
Cdd:cd05958 173 EATPDLLLSAIARYKPTVLFTAPTAYRAMLAHPDAAGPDLSSLRKCVsaGEALPAALHRAWKEATGIPII-DGIGSTEMf 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 209 NCSIANMDGkvgscgfnsriltHVYPIRLVKVNEDTMEPLRDSEGLCIPcqPGEPGLLVgqinqqdpLRRFDGYVSDSat 288
Cdd:cd05958 252 HIFISARPG-------------DARPGATGKPVPGYEAKVVDDEGNPVP--DGTIGRLA--------VRGPTGCRYLA-- 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 289 nKKIAHSVFRKGDSAylSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPG------ 362
Cdd:cd05958 307 -DKRQRTYVQGGWNI--TGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESrgvvvk 383
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907189430 363 --VEGKAGMAAIADPHSQLdpnsmyQELQK-VLASYARPIFLRLLPQVDTTGTFKIQKTRL 420
Cdd:cd05958 384 afVVLRPGVIPGPVLAREL------QDHAKaHIAPYKYPRAIEFVTELPRTATGKLQRFAL 438
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
54-422 |
3.11e-14 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 74.51 E-value: 3.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 54 KGMDDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADVLYDCLPLYHSAGNIMGVGQCVIYGLTVVLRKKF 133
Cdd:PRK06839 146 KNESASFIICYTSGTTGKPKGAVLTQENMFWNALNNTFAIDLTMHDRSIVLLPLFHIGGIGLFAFPTLFAGGVIIVPRKF 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 134 SASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVEQRHRVRLAVgNGLRPA---IWEEFTQRfGVPqIGEFYGATECNC 210
Cdd:PRK06839 226 EPTKALSMIEKHKVTVVMGVPTIHQALINCSKFETTNLQSVRWFY-NGGAPCpeeLMREFIDR-GFL-FGQGFGMTETSP 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 211 S---IANMDG--KVGSCG----FNSrilthvypIRLVKVNEDTMEplrdseglcipcqPGEpgllVGQINQQDPLRRFDG 281
Cdd:PRK06839 303 TvfmLSEEDArrKVGSIGkpvlFCD--------YELIDENKNKVE-------------VGE----VGELLIRGPNVMKEY 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 282 YVSDSATNKKIAhsvfrkgDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGvaVP 361
Cdd:PRK06839 358 WNRPDATEETIQ-------DGWLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVG--RQ 428
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907189430 362 GVE-GKAGMAAIA-DPHSQLDPNSMYQELQKVLASYARP---IFLRLLPQvDTTGtfKIQKTRLQR 422
Cdd:PRK06839 429 HVKwGEIPIAFIVkKSSSVLIEKDVIEHCRLFLAKYKIPkeiVFLKELPK-NATG--KIQKAQLVN 491
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
64-423 |
5.71e-14 |
|
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: 74.04 E-value: 5.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 64 YTSGTTGLPKAAIVVHSRY-YRIAAFGHHSYSMRAADVLY---DCLPLYHSAGNIMG---VGQCVIygltVVLRKKFSAS 136
Cdd:cd05928 181 FTSGTTGSPKMAEHSHSSLgLGLKVNGRYWLDLTASDIMWntsDTGWIKSAWSSLFEpwiQGACVF----VHHLPRFDPL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 137 RFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVE-QRHRVRLAVGNGLRPAIWEEFTQRFGVpQIGEFYGATECNCSIANM 215
Cdd:cd05928 257 VILKTLSSYPITTFCGAPTVYRMLVQQDLSSYKfPSLQHCVTGGEPLNPEVLEKWKAQTGL-DIYEGYGQTETGLICANF 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 216 DG---KVGSCGFNSRilthVYPIRLVkvnedtmeplrDSEGLCIPcqPGEPGLLVGQINQQDPLRRFDGYVSDSatnKKI 292
Cdd:cd05928 336 KGmkiKPGSMGKASP----PYDVQII-----------DDNGNVLP--PGTEGDIGIRVKPIRPFGLFSGYVDNP---EKT 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 293 AHSvfRKGDsAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPgVEGKAGMAAI 372
Cdd:cd05928 396 AAT--IRGD-FYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDP-IRGEVVKAFV 471
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907189430 373 --ADPHSQLDPNSMYQELQ----KVLASYARPIFLRLLPQVDTTGTFKIQKTRLQRE 423
Cdd:cd05928 472 vlAPQFLSHDPEQLTKELQqhvkSVTAPYKYPRKVEFVQELPKTVTGKIQRNELRDK 528
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
57-423 |
6.93e-14 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 73.65 E-value: 6.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 57 DDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADVLYDCLPLYHSAGNIMGVGQCVIYGLTVVL-RKKFSA 135
Cdd:PRK12583 201 DDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCVPVPLYHCFGMVLANLGCMTVGACLVYpNEAFDP 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 136 SRFWDDCVKYNCTVVQ-----YIGEicrylLRQPVRDVEQRHRVRLAV--GNGLRPAIWEEFTQRFGVPQIGEFYGATEC 208
Cdd:PRK12583 281 LATLQAVEEERCTALYgvptmFIAE-----LDHPQRGNFDLSSLRTGImaGAPCPIEVMRRVMDEMHMAEVQIAYGMTET 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 209 N------CSIANMDGKVGSCGfnsRILTHVYpirlVKVnedtmeplRDSEGLCIPcqPGEPGLLVgqinqqdplrrFDGY 282
Cdd:PRK12583 356 SpvslqtTAADDLERRVETVG---RTQPHLE----VKV--------VDPDGATVP--RGEIGELC-----------TRGY 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 283 V-------SDSATNKKIahsvfrKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAV 355
Cdd:PRK12583 408 SvmkgywnNPEATAESI------DEDGWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQV 481
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 356 YGvaVPGVE-GKAGMAAIA-DPHSQLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQKTRLqRE 423
Cdd:PRK12583 482 FG--VPDEKyGEEIVAWVRlHPGHAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRM-RE 548
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
43-423 |
8.67e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 73.38 E-value: 8.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 43 APTTPLAQAPGKGMDDRLFYIYTSGTTGLPKAAIVVHSRYY-----RIAAFGhhsysMRAADVLYDCLPLYHsagnimgV 117
Cdd:PRK06145 135 QGGLEIPPQAAVAPTDLVRLMYTSGTTDRPKGVMHSYGNLHwksidHVIALG-----LTASERLLVVGPLYH-------V 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 118 GQCVIYGLTVV-------LRKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVEQRHRVRLAVGNGLR-PAI-WE 188
Cdd:PRK06145 203 GAFDLPGIAVLwvggtlrIHREFDPEAVLAAIERHRLTCAWMAPVMLSRVLTVPDRDRFDLDSLAWCIGGGEKtPESrIR 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 189 EFTQRFGVPQIGEFYGATECNCSIANMDG-----KVGSCGfnsRILTHVyPIRLvkvnedtmeplRDSEGLCIPcqPGEP 263
Cdd:PRK06145 283 DFTRVFTRARYIDAYGLTETCSGDTLMEAgreieKIGSTG---RALAHV-EIRI-----------ADGAGRWLP--PNMK 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 264 GllvgQINQQDPlRRFDGYVSDSatnKKIAHSVFrkgDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAV 343
Cdd:PRK06145 346 G----EICMRGP-KVTKGYWKDP---EKTAEAFY---GDWFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERV 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 344 LSRLLGQTDVAVYGVAVPGVEGKAGMAAIADPHSQLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQKTRLQRE 423
Cdd:PRK06145 415 IYELPEVAEAAVIGVHDDRWGERITAVVVLNPGATLTLEALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVLRDE 494
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
32-423 |
3.24e-13 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 71.62 E-value: 3.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 32 DTQLLDPMLAEAP-TTPLAQAPGKGMDDRLFYIYTSGTTGLPKAaiVVHSRYYRIAAFghHSYSMR----AADVLYDCLP 106
Cdd:PRK13295 171 EALLITPAWEQEPdAPAILARLRPGPDDVTQLIYTSGTTGEPKG--VMHTANTLMANI--VPYAERlglgADDVILMASP 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 107 LYHSAGNIMGVGQCVIYGLTVVLRKKFSASRFWD----DCVKYNCTVVQYIGEICRyLLRQPVRDVEQRhRVRLAVGNGL 182
Cdd:PRK13295 247 MAHQTGFMYGLMMPVMLGATAVLQDIWDPARAAElirtEGVTFTMASTPFLTDLTR-AVKESGRPVSSL-RTFLCAGAPI 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 183 RPAIWEEFTQRFGVpQIGEFYGATECNC----SIANMDGKVGScgfnsrilTHVYPIRLVKVNedtmepLRDSEGLCIPc 258
Cdd:PRK13295 325 PGALVERARAALGA-KIVSAWGMTENGAvtltKLDDPDERAST--------TDGCPLPGVEVR------VVDADGAPLP- 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 259 qPGEPGLLV--GQINqqdplrrFDGYVSDSATNKKIAHSVFRKGDSAYLSGDvlvmdelGYMYFRDRSGDTFRWRGENVS 336
Cdd:PRK13295 389 -AGQIGRLQvrGCSN-------FGGYLKRPQLNGTDADGWFDTGDLARIDAD-------GYIRISGRSKDVIIRGGENIP 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 337 TTEVEAVLSRLLGQTDVAVygVAVPgvEGKAGMAAIA----DPHSQLDPNSM--YQELQKVLASYArPIFLRLLPQVDTT 410
Cdd:PRK13295 454 VVEIEALLYRHPAIAQVAI--VAYP--DERLGERACAfvvpRPGQSLDFEEMveFLKAQKVAKQYI-PERLVVRDALPRT 528
|
410
....*....|...
gi 1907189430 411 GTFKIQKTRLQRE 423
Cdd:PRK13295 529 PSGKIQKFRLREM 541
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
3-358 |
3.82e-13 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 71.09 E-value: 3.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 3 AAVAEVSEQLGKSL---LKFCSGDLGPesiLPDTQLLDPMLAEAPTTPLA-QAPGKGMddrlfyIYTSGTTGLPK----- 73
Cdd:PRK08276 91 AALADTAAELAAELpagVPLLLVVAGP---VPGFRSYEEALAAQPDTPIAdETAGADM------LYSSGTTGRPKgikrp 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 74 ----AAIVVHSRYYRIAAFGHHSYsmrAADVLYDCLPLYHSAGN--IMGVGQCviyGLTVVLRKKFSASRFWDDCVKYNC 147
Cdd:PRK08276 162 lpglDPDEAPGMMLALLGFGMYGG---PDSVYLSPAPLYHTAPLrfGMSALAL---GGTVVVMEKFDAEEALALIERYRV 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 148 TVVQYIGEICRYLLRQPvRDVEQRHRVRlavgnGLRPAI----------------WeeftqrFGvPQIGEFYGATECN-- 209
Cdd:PRK08276 236 THSQLVPTMFVRMLKLP-EEVRARYDVS-----SLRVAIhaaapcpvevkramidW------WG-PIIHEYYASSEGGgv 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 210 --CSIANMDGKVGSCGfnsRILTHVypirlVKVNEDTMEPLrdseglciPcqPGEPGLLVGQINQQDplrrFDgYVSDSA 287
Cdd:PRK08276 303 tvITSEDWLAHPGSVG---KAVLGE-----VRILDEDGNEL--------P--PGEIGTVYFEMDGYP----FE-YHNDPE 359
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907189430 288 TNKKIAHsvfRKGDSAYlsGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGV 358
Cdd:PRK08276 360 KTAAARN---PHGWVTV--GDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGV 425
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
52-361 |
1.71e-12 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 69.95 E-value: 1.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 52 PGKGMDDRLFYIYTSGTTGLPKAAIVVHsryYRIAA--------FGhhsysMRAADVLYDCLPLYHSagnimgvgqcviY 123
Cdd:PRK08633 777 PTFKPDDTATIIFSSGSEGEPKGVMLSH---HNILSnieqisdvFN-----LRNDDVILSSLPFFHS------------F 836
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 124 GLTV----VLRKKFSASRFWD--D-------CVKYNCTVVQYIGEICRYLLRQPVRDVEQRHRVRLAVGNG--LRPAIWE 188
Cdd:PRK08633 837 GLTVtlwlPLLEGIKVVYHPDptDalgiaklVAKHRATILLGTPTFLRLYLRNKKLHPLMFASLRLVVAGAekLKPEVAD 916
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 189 EFTQRFGVPqIGEFYGATEC------NCSIANMDG-------KVGSCGfnsriltHVYPIRLVK-VNEDTMEPLrdsegl 254
Cdd:PRK08633 917 AFEEKFGIR-ILEGYGATETspvasvNLPDVLAADfkrqtgsKEGSVG-------MPLPGVAVRiVDPETFEEL------ 982
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 255 cipcQPGEPGL-LVGQINqqdplrRFDGYVSDSA-TNKKIAHSvfrKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRG 332
Cdd:PRK08633 983 ----PPGEDGLiLIGGPQ------VMKGYLGDPEkTAEVIKDI---DGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGG 1049
|
330 340
....*....|....*....|....*....
gi 1907189430 333 ENVSTTEVEAVLSRLLGQTDVAVYGVAVP 361
Cdd:PRK08633 1050 EMVPLGAVEEELAKALGGEEVVFAVTAVP 1078
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
46-423 |
2.84e-12 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 68.62 E-value: 2.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 46 TPLAQAPGKGMDDRLFYIYTSGTTGLPKAAIVVHSRYYriaaFGHHSYSMR----AADVLYDCLPLYHSAGNIMGVGQCV 121
Cdd:PRK06087 176 EPLTTAITTHGDELAAVLFTSGTEGLPKGVMLTHNNIL----ASERAYCARlnltWQDVFMMPAPLGHATGFLHGVTAPF 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 122 IYGLTVVLRKKFSASRFWDDCVKYNCTVVQ----YIGEICRYLLRQPVrDVEQRhRVRLAVGNGLRPAIWEEfTQRFGVp 197
Cdd:PRK06087 252 LIGARSVLLDIFTPDACLALLEQQRCTCMLgatpFIYDLLNLLEKQPA-DLSAL-RFFLCGGTTIPKKVARE-CQQRGI- 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 198 QIGEFYGATE-CNCSIANMDGKVGSCGFNSRILTHVYPIRLVKVNEDTmeplrdseglcIPCqpGEPGLLVGQINQQdpl 276
Cdd:PRK06087 328 KLLSVYGSTEsSPHAVVNLDDPLSRFMHTDGYAAAGVEIKVVDEARKT-----------LPP--GCEGEEASRGPNV--- 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 277 rrFDGYVSD-SATNKKIahsvfrKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAV 355
Cdd:PRK06087 392 --FMGYLDEpELTARAL------DEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACV 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 356 ygVAVP----GvEGKAGMAAIADPHSQLdpnsmyqELQKVLASYAR--------PIFLRLLPQVDTTGTFKIQKTRLQRE 423
Cdd:PRK06087 464 --VAMPderlG-ERSCAYVVLKAPHHSL-------TLEEVVAFFSRkrvakykyPEHIVVIDKLPRTASGKIQKFLLRKD 533
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
64-423 |
9.10e-12 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 66.98 E-value: 9.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 64 YTSGTTGLPKAAIVVHSRYYRIAAFG-HHSYS-MRAADVLYDCLPLYHSAGNIMGVGQCVIYGLTVVLRKKFSASRFWDD 141
Cdd:PRK06710 213 YTGGTTGFPKGVMLTHKNLVSNTLMGvQWLYNcKEGEEVVLGVLPFFHVYGMTAVMNLSIMQGYKMVLIPKFDMKMVFEA 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 142 CVKYNCTVVQYIGEICRYLLRQPVRDVEQRHRVRLAV-GNGLRPAIWEEFTQRFGVPQIGEFYGATEcncsianmdgkvg 220
Cdd:PRK06710 293 IKKHKVTLFPGAPTIYIALLNSPLLKEYDISSIRACIsGSAPLPVEVQEKFETVTGGKLVEGYGLTE------------- 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 221 scgfnSRILTHVYPIRLVKVNEDTMEPLRDSEGLCIPCQPGE---PGLlVGQINQQDPlRRFDGYVSDSATNKKIAHsvf 297
Cdd:PRK06710 360 -----SSPVTHSNFLWEKRVPGSIGVPWPDTEAMIMSLETGEalpPGE-IGEIVVKGP-QIMKGYWNKPEETAAVLQ--- 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 298 rkgDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPGVEGKAGMAAIADPHS 377
Cdd:PRK06710 430 ---DGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVLKEGT 506
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1907189430 378 QLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQKTRLQRE 423
Cdd:PRK06710 507 ECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVLIEE 552
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
64-355 |
1.10e-11 |
|
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: 66.49 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 64 YTSGTTGLPKAAIVVHSRYyrIAAF-GHHSY--SMRAADVLYDC-LPLYHSAGnIMGVGQCVI-YGLTVVLRKKFSASRF 138
Cdd:cd05904 165 YSSGTTGRSKGVMLTHRNL--IAMVaQFVAGegSNSDSEDVFLCvLPMFHIYG-LSSFALGLLrLGATVVVMPRFDLEEL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 139 WDDCVKYNCTVVQYIGEICRYLLRQPVRDVEQRHRVRlAVGNG---LRPAIWEEFTQRFGVPQIGEFYGATECNCSIANM 215
Cdd:cd05904 242 LAAIERYKVTHLPVVPPIVLALVKSPIVDKYDLSSLR-QIMSGaapLGKELIEAFRAKFPNVDLGQGYGMTESTGVVAMC 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 216 D------GKVGSCGFnsrilthVYPIRLVK-VNEDTMEPLRdseglciPCQPGEpgLLV-G-QINQqdplrrfdGYVSD- 285
Cdd:cd05904 321 FapekdrAKYGSVGR-------LVPNVEAKiVDPETGESLP-------PNQTGE--LWIrGpSIMK--------GYLNNp 376
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 286 SATNKKIahsvfrKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAV 355
Cdd:cd05904 377 EATAATI------DKEGWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAV 440
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
64-358 |
1.62e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 66.16 E-value: 1.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 64 YTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADVLYDCLPLYHSAGNImgVGQCVIYGLTVVLRKKFSASRFWDDCV 143
Cdd:PRK06188 175 YTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLSHAGGAF--FLPTLLRGGTVIVLAKFDPAEVLRAIE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 144 KYNCTVVQYIGEICRYLLRQPvrDVEQRHRVRLAV----GNGLRPAIWEEFTQRFGvPQIGEFYGATECNCSIANMD--- 216
Cdd:PRK06188 253 EQRITATFLVPTMIYALLDHP--DLRTRDLSSLETvyygASPMSPVRLAEAIERFG-PIFAQYYGQTEAPMVITYLRkrd 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 217 ------GKVGSCGFnsrilthvyPIRLVKVNedtmepLRDSEGLCIPcqPGEPGllvgQINQQDPLRrFDGYVSDSATNK 290
Cdd:PRK06188 330 hdpddpKRLTSCGR---------PTPGLRVA------LLDEDGREVA--QGEVG----EICVRGPLV-MDGYWNRPEETA 387
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907189430 291 KiahsVFRKGdsaYL-SGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGV 358
Cdd:PRK06188 388 E----AFRDG---WLhTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGV 449
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
26-355 |
2.00e-11 |
|
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: 65.36 E-value: 2.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 26 PESILPDTQLLDPMLAEAPTTPLAQAPGKGmDDRLFYIYTSGTTGLPKAAIVVH----------SRYY------RIAAFg 89
Cdd:TIGR01733 90 VLPVILLDPLELAALDDAPAPPPPDAPSGP-DDLAYVIYTSGSTGRPKGVVVTHrslvnllawlARRYgldpddRVLQF- 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 90 hHSYSMRAAdVLYDCLPLYHsagnimGVGQCVIYGltVVLRKKFSASRFWDDcvKYNCTVVQYIGEICRYLLRQPVRDVE 169
Cdd:TIGR01733 168 -ASLSFDAS-VEEIFGALLA------GATLVVPPE--DEERDDAALLAALIA--EHPVTVLNLTPSLLALLAAALPPALA 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 170 QRHRVrLAVGNGLRPAIWEEFTQRFGVPQIGEFYGATECN--CSIANMDGKVGSCGFNSRI---LTHVypiRLVKVNEDT 244
Cdd:TIGR01733 236 SLRLV-ILGGEALTPALVDRWRARGPGARLINLYGPTETTvwSTATLVDPDDAPRESPVPIgrpLANT---RLYVLDDDL 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 245 MeplrdseglciPCQPGEPG-LLVGQINqqdpLRRfdGYVSDSA-TNKKIAHSVFRKGDSA--YLSGDVLVMDELGYMYF 320
Cdd:TIGR01733 312 R-----------PVPVGVVGeLYIGGPG----VAR--GYLNRPElTAERFVPDPFAGGDGArlYRTGDLVRYLPDGNLEF 374
|
330 340 350
....*....|....*....|....*....|....*
gi 1907189430 321 RDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAV 355
Cdd:TIGR01733 375 LGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
29-344 |
2.38e-11 |
|
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: 65.28 E-value: 2.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 29 ILPDTQLLDP-----MLAEAPTTPLAQAPGKGMDDRLFYIYTSGTTGLPKaaIVVHSryYRIAAFGHHS----YSMRAAD 99
Cdd:cd05974 52 VIPATTLLTPddlrdRVDRGGAVYAAVDENTHADDPMLLYFTSGTTSKPK--LVEHT--HRSYPVGHLStmywIGLKPGD 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 100 VLYD-CLPLY--HSAGNIMG---VGQCVIygltVVLRKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVEQRHR 173
Cdd:cd05974 128 VHWNiSSPGWakHAWSCFFApwnAGATVF----LFNYARFDAKRVLAALVRYGVTTLCAPPTVWRMLIQQDLASFDVKLR 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 174 VRLAVGNGLRPAIWEEFTQRFGVpQIGEFYGATECNCSIANMDG---KVGSCGfnsrilthvYPIRLVKVNedtmepLRD 250
Cdd:cd05974 204 EVVGAGEPLNPEVIEQVRRAWGL-TIRDGYGQTETTALVGNSPGqpvKAGSMG---------RPLPGYRVA------LLD 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 251 SEGLciPCQPGEPGLLVGQINqqdPLRRFDGYVSDSAtnkKIAHSVfrkGDSAYLSGDVLVMDELGYMYFRDRSGDTFRW 330
Cdd:cd05974 268 PDGA--PATEGEVALDLGDTR---PVGLMKGYAGDPD---KTAHAM---RGGYYRTGDIAMRDEDGYLTYVGRADDVFKS 336
|
330
....*....|....
gi 1907189430 331 RGENVSTTEVEAVL 344
Cdd:cd05974 337 SDYRISPFELESVL 350
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
41-367 |
2.79e-11 |
|
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.
Pssm-ID: 341272 [Multi-domain] Cd Length: 610 Bit Score: 65.59 E-value: 2.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 41 AEAPTTPLAQAPGKGMDDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFG-HHSYSMRAADVLYdclpLYHSAGNIMG--- 116
Cdd:cd05968 220 DEEKETAGDGAERTESEDPLMIIYTSGTTGKPKGTVHVHAGFPLKAAQDmYFQFDLKPGDLLT----WFTDLGWMMGpwl 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 117 VGQCVIYGLTVVLRKKF----SASRFWDDCVKYNCTVVQYIGEICRYLL---RQPVRdVEQRHRVRLAVGNG--LRPAIW 187
Cdd:cd05968 296 IFGGLILGATMVLYDGApdhpKADRLWRMVEDHEITHLGLSPTLIRALKprgDAPVN-AHDLSSLRVLGSTGepWNPEPW 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 188 EEFTQRFG---VPqIGEFYGATECNCSI--ANMDGKVGSCGFNSrilthVYPIRLVKVNEDTMEPLRDSEGLCIPCQPGe 262
Cdd:cd05968 375 NWLFETVGkgrNP-IINYSGGTEISGGIlgNVLIKPIKPSSFNG-----PVPGMKADVLDESGKPARPEVGELVLLAPW- 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 263 PGLLVGqiNQQDPLRRFDGYvsdsatnkkiahsvFRKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEA 342
Cdd:cd05968 448 PGMTRG--FWRDEDRYLETY--------------WSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIES 511
|
330 340
....*....|....*....|....*
gi 1907189430 343 VLSRLLGQTDVAVYGVAVPgVEGKA 367
Cdd:cd05968 512 VLNAHPAVLESAAIGVPHP-VKGEA 535
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
2-371 |
4.02e-11 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 65.10 E-value: 4.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 2 AAAVAEVSEQLGKSLLKFcsgDLGPESILPDTQLLDPMLAEAPTTPLAQAP-GKGMddrlfyIYTSGTTGLPKAAivvhs 80
Cdd:PRK13391 107 LDVARALLKQCPGVRHRL---VLDGDGELEGFVGYAEAVAGLPATPIADESlGTDM------LYSSGTTGRPKGI----- 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 81 ryYR------------IAAFGHHSYSMRAADVLYDCLPLYHSA-GNIMGVGQCViyGLTVVLRKKFSASRFWDDCVKYNC 147
Cdd:PRK13391 173 --KRplpeqppdtplpLTAFLQRLWGFRSDMVYLSPAPLYHSApQRAVMLVIRL--GGTVIVMEHFDAEQYLALIEEYGV 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 148 TVVQYIGEICRYLLRQPvRDVEQRHRVrlavgNGLRPAIW----------EEFTQRFGvPQIGEFYGATECN----CSIA 213
Cdd:PRK13391 249 THTQLVPTMFSRMLKLP-EEVRDKYDL-----SSLEVAIHaaapcppqvkEQMIDWWG-PIIHEYYAATEGLgftaCDSE 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 214 NMDGKVGSCGfnsRILTHVYPIRlvkvnEDTMEplrdseglciPCQPGEPgllvGQINQQDPlRRFDgYVSDSAtnkKIA 293
Cdd:PRK13391 322 EWLAHPGTVG---RAMFGDLHIL-----DDDGA----------ELPPGEP----GTIWFEGG-RPFE-YLNDPA---KTA 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 294 HSvfRKGDSAY-LSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGV-------------- 358
Cdd:PRK13391 375 EA--RHPDGTWsTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVpnedlgeevkavvq 452
|
410
....*....|...
gi 1907189430 359 AVPGVEGKAGMAA 371
Cdd:PRK13391 453 PVDGVDPGPALAA 465
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
16-358 |
4.19e-11 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 64.82 E-value: 4.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 16 LLKFCSGDLGPE--SILPDTQLLDPMLAEaPTTPLAQAPgkgmDDRLFYIYTSGTTGLPKAAIVVHSRYY-----RIAAF 88
Cdd:PLN02860 134 FLESPSSSVFIFlnSFLTTEMLKQRALGT-TELDYAWAP----DDAVLICFTSGTTGRPKGVTISHSALIvqslaKIAIV 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 89 GHHSysmraADVLYDCLPLYH-----SAGNIMGVGQCViygltvVLRKKFSASRFWD----DCVKYNCTVVQYIGEICRY 159
Cdd:PLN02860 209 GYGE-----DDVYLHTAPLCHigglsSALAMLMVGACH------VLLPKFDAKAALQaikqHNVTSMITVPAMMADLISL 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 160 LLRQPVRDVEQRHRVRLAVGNGLRPAIWEEFTQRFGVPQIGEFYGATECNCSIANMDGKVGSCGFNSRILTHVYPIRLVK 239
Cdd:PLN02860 278 TRKSMTWKVFPSVRKILNGGGSLSSRLLPDAKKLFPNAKLFSAYGMTEACSSLTFMTLHDPTLESPKQTLQTVNQTKSSS 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 240 VNEdtmeplrdSEGLCI----P------CQPGEPGllVGQINQQDP---LRRFDGYVSDSATnkkiahsvfRKGDSAYLS 306
Cdd:PLN02860 358 VHQ--------PQGVCVgkpaPhvelkiGLDESSR--VGRILTRGPhvmLGYWGQNSETASV---------LSNDGWLDT 418
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1907189430 307 GDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGV 358
Cdd:PLN02860 419 GDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGV 470
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
63-361 |
6.38e-11 |
|
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: 63.44 E-value: 6.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 63 IYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADVLYDCLPLYHSAGniMGVGQCVIY--GLTVVLRKkFSASRFWD 140
Cdd:cd17637 6 IHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPLFHIAG--LNLALATFHagGANVVMEK-FDPAEALE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 141 DCVKYNCTVVQYIGEICRYLLrqpvrDVEQRHRVRLAvgnGLR-------PaiweEFTQRFGVPQIGEF---YGATECNC 210
Cdd:cd17637 83 LIEEEKVTLMGSFPPILSNLL-----DAAEKSGVDLS---SLRhvlgldaP----ETIQRFEETTGATFwslYGQTETSG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 211 --SIANMDGKVGSCGfnsRILthvyPIRLVKVNEDTMEPLRdseglcipcqPGEPGllvgQINQQDPLRrFDGYVSDSAT 288
Cdd:cd17637 151 lvTLSPYRERPGSAG---RPG----PLVRVRIVDDNDRPVP----------AGETG----EIVVRGPLV-FQGYWNLPEL 208
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907189430 289 NkkiAHSvFRKGdsAYLSGDVLVMDELGYMYFRDRSG--DTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVP 361
Cdd:cd17637 209 T---AYT-FRNG--WHHTGDLGRFDEDGYLWYAGRKPekELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDP 277
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
57-357 |
1.27e-10 |
|
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: 63.00 E-value: 1.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 57 DDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADVLYDCLPLYHSAGNIMGVGQCVIYGLTVV-------- 128
Cdd:cd05907 87 DDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPATEGDRHLSFLPLAHVFERRAGLYVPLLAGARIYfassaetl 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 129 ---LRKK-----FSASRFWDdcvK-YNCTVVQYIGEICRYLLRQPVRDveqrhRVRLAVGNG--LRPAIwEEFTQRFGVP 197
Cdd:cd05907 167 lddLSEVrptvfLAVPRVWE---KvYAAIKVKAVPGLKRKLFDLAVGG-----RLRFAASGGapLPAEL-LHFFRALGIP 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 198 qIGEFYGATECnCSIANM----DGKVGSCGfnsriltHVYPIRLVKVNEDtmeplrdseglcipcqpGEpgLLV-GQINq 272
Cdd:cd05907 238 -VYEGYGLTET-SAVVTLnppgDNRIGTVG-------KPLPGVEVRIADD-----------------GE--ILVrGPNV- 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 273 qdplrrFDGYVSDSATNKKIAhsvfrKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWR-GENVSTTEVEAVL--SRLLG 349
Cdd:cd05907 289 ------MLGYYKNPEATAEAL-----DADGWLHTGDLGEIDEDGFLHITGRKKDLIITSgGKNISPEPIENALkaSPLIS 357
|
....*...
gi 1907189430 350 QtdVAVYG 357
Cdd:cd05907 358 Q--AVVIG 363
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
36-421 |
1.35e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 63.52 E-value: 1.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 36 LDPMLAEAPTTPLAQAPGKGMDDRLFYIYTSGTTGLPKAaiVVHSR---YYRIAAFGHHSYSMRAADVLYDCLPLYHSAG 112
Cdd:PRK06178 188 IDLLPALRACTAPVPLPPPALDALAALNYTGGTTGMPKG--CEHTQrdmVYTAAAAYAVAVVGGEDSVFLSFLPEFWIAG 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 113 NIMGVGQCVIYGLTVVLRKKFSASRFWDDCVKYNCT----VVQYIGEIC------RYLLR--QPVR--------DVEQRH 172
Cdd:PRK06178 266 ENFGLLFPLFSGATLVLLARWDAVAFMAAVERYRVTrtvmLVDNAVELMdhprfaEYDLSslRQVRvvsfvkklNPDYRQ 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 173 RVRLAVGNGLRPAIWeeftqrfgvpqigefyGATE---CNCSIANMdgKVGSCGFNSRILTHVYPI---RLVKVNEDTME 246
Cdd:PRK06178 346 RWRALTGSVLAEAAW----------------GMTEthtCDTFTAGF--QDDDFDLLSQPVFVGLPVpgtEFKICDFETGE 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 247 PLrdseglciPC-QPGE-----PGLLVGQINQQDplrrfdgyvsdsATnkkiAHSvFRkgDSAYLSGDVLVMDELGYMYF 320
Cdd:PRK06178 408 LL--------PLgAEGEivvrtPSLLKGYWNKPE------------AT----AEA-LR--DGWLHTGDIGKIDEQGFLHY 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 321 RDRSGDTFRWRGENVSTTEVEAvlsrLLGQTDvAVYGVAVPGV--EGKaGMAAIA----DPHSQLDPNSMYQELQKVLAS 394
Cdd:PRK06178 461 LGRRKEMLKVNGMSVFPSEVEA----LLGQHP-AVLGSAVVGRpdPDK-GQVPVAfvqlKPGADLTAAALQAWCRENMAV 534
|
410 420
....*....|....*....|....*..
gi 1907189430 395 YARPIfLRLLPQVDTTGTFKIQKTRLQ 421
Cdd:PRK06178 535 YKVPE-IRIVDALPMTATGKVRKQDLQ 560
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
51-358 |
5.16e-10 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 61.40 E-value: 5.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 51 APGKGMDDRLFYIYTSGTTGLPKAAIVVHSRYyrIAA------FGHHSYSMRAADVLY-DCLPLYHSAGNIMGVGQCVIY 123
Cdd:PLN02574 192 KPVIKQDDVAAIMYSSGTTGASKGVVLTHRNL--IAMvelfvrFEASQYEYPGSDNVYlAALPMFHIYGLSLFVVGLLSL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 124 GLTVVLRKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVEQRHRVRLAVGNGLRPA---IWEEFTQRFGVPQIG 200
Cdd:PLN02574 270 GSTIVVMRRFDASDMVKVIDRFKVTHFPVVPPILMALTKKAKGVCGEVLKSLKQVSCGAAPLsgkFIQDFVQTLPHVDFI 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 201 EFYGATEcncSIAnmdgkVGSCGFNSRILTHVYPIRLVKVNedtMEP--LRDSEGLCIPcqPGE--------PGLLVGQI 270
Cdd:PLN02574 350 QGYGMTE---STA-----VGTRGFNTEKLSKYSSVGLLAPN---MQAkvVDWSTGCLLP--PGNcgelwiqgPGVMKGYL 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 271 NqqdplrrfDGYVSDSATNKkiahsvfrkgDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQ 350
Cdd:PLN02574 417 N--------NPKATQSTIDK----------DGWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEI 478
|
....*...
gi 1907189430 351 TDVAVYGV 358
Cdd:PLN02574 479 IDAAVTAV 486
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
21-415 |
6.23e-10 |
|
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: 61.21 E-value: 6.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 21 SGDLGPESIlPDTQLLDPMLAEAPTTPLAqaPGKGMDDRLFYIYTSGTTGLPKAAIVVHS----------RYYRIAAFGH 90
Cdd:cd17651 103 AGELAVELV-AVTLLDQPGAAAGADAEPD--PALDADDLAYVIYTSGSTGRPKGVVMPHRslanlvawqaRASSLGPGAR 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 91 HS-YSMRAADVlydclplyhSAGNIMGVgqcVIYGLTVVLRK---KFSASRFWDDCVKYNCTVV----QYIGEICRYLLR 162
Cdd:cd17651 180 TLqFAGLGFDV---------SVQEIFST---LCAGATLVLPPeevRTDPPALAAWLDEQRISRVflptVALRALAEHGRP 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 163 QPVRDVEQRHRV----RLAVGNGLRpaiweEFTQRFGVPQIGEFYGATEcncsianmdgkvgscgfnsrilTHVypirlV 238
Cdd:cd17651 248 LGVRLAALRYLLtggeQLVLTEDLR-----EFCAGLPGLRLHNHYGPTE----------------------THV-----V 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 239 KVNEDTMEPLRDSEGLCI-----------------PCQPGEPG-LLVGQinqqDPLRRfdGYVSDSA-TNKKIAHSVFRK 299
Cdd:cd17651 296 TALSLPGDPAAWPAPPPIgrpidntrvyvldaalrPVPPGVPGeLYIGG----AGLAR--GYLNRPElTAERFVPDPFVP 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 300 GDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVygVAVPGVEGKAGMAA--IADPHS 377
Cdd:cd17651 370 GARMYRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVV--LAREDRPGEKRLVAyvVGDPEA 447
|
410 420 430
....*....|....*....|....*....|....*...
gi 1907189430 378 QLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKI 415
Cdd:cd17651 448 PVDAAELRAALATHLPEYMVPSAFVLLDALPLTPNGKL 485
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
63-358 |
9.49e-10 |
|
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: 60.62 E-value: 9.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 63 IYTSGTTGLPKAAIVVHSRYyrIAAFGHHSYSMRAADVLYD-----CLPLYHSAGNIMGVGQcVIYGLTVVLRKKFSASR 137
Cdd:cd17642 190 MNSSGSTGLPKGVQLTHKNI--VARFSHARDPIFGNQIIPDtailtVIPFHHGFGMFTTLGY-LICGFRVVLMYKFEEEL 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 138 FWDDCVKYNCTVVQYIGEICRYLLRQPVRD-VEQRHRVRLAVGNG-LRPAIWEEFTQRFGVPQIGEFYGATECNCSI--- 212
Cdd:cd17642 267 FLRSLQDYKVQSALLVPTLFAFFAKSTLVDkYDLSNLHEIASGGApLSKEVGEAVAKRFKLPGIRQGYGLTETTSAIlit 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 213 ANMDGKVGSCGfnsriltHVYPIRLVKVnedtMEPlrDSEGLCIPCQPGE-----PGLLVGQINQQDplrrfdgyvsdsA 287
Cdd:cd17642 347 PEGDDKPGAVG-------KVVPFFYAKV----VDL--DTGKTLGPNERGElcvkgPMIMKGYVNNPE------------A 401
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907189430 288 TNKKIAHsvfrkgDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGV 358
Cdd:cd17642 402 TKALIDK------DGWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGI 466
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
25-361 |
1.02e-09 |
|
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: 60.39 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 25 GPESILPDTQLL-DPMLAEAPTTPLAQAPgKGMDDRLFYIYTSGTTGLPKAaIVVHSRYYRIAAFGH-HSYSMRAADVLY 102
Cdd:cd12118 101 EAKVLFVDREFEyEDLLAEGDPDFEWIPP-ADEWDPIALNYTSGTTGRPKG-VVYHHRGAYLNALANiLEWEMKQHPVYL 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 103 DCLPLYHSAG--NIMGVGqcVIYGLTVVLRKkFSASRFWDDCVKYNCT-------VVQYIGEiCRYLLRQPVRdveqrHR 173
Cdd:cd12118 179 WTLPMFHCNGwcFPWTVA--AVGGTNVCLRK-VDAKAIYDLIEKHKVThfcgaptVLNMLAN-APPSDARPLP-----HR 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 174 VRLAVGNGLRPAIWEEFTQRFGVpQIGEFYGATECNcsianmdGKVGSC---------------GFNSRI-LTHVYPIRL 237
Cdd:cd12118 250 VHVMTAGAPPPAAVLAKMEELGF-DVTHVYGLTETY-------GPATVCawkpewdelpteeraRLKARQgVRYVGLEEV 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 238 VKVNEDTMEPL-RDSEGLcipcqpGEPgLLVGQINQQdplrrfdGYVSDSATNKKiahsVFRKGdsAYLSGDVLVMDELG 316
Cdd:cd12118 322 DVLDPETMKPVpRDGKTI------GEI-VFRGNIVMK-------GYLKNPEATAE----AFRGG--WFHSGDLAVIHPDG 381
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1907189430 317 YMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVygVAVP 361
Cdd:cd12118 382 YIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAV--VARP 424
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
57-358 |
1.27e-09 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 60.45 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 57 DDRLFYIYTSGTTGLPKAAIVVHSRYyrIA----AFGHHSYSMR-AADVLYDCLPLYHsagnimgvgqcvIYGLTVvlrk 131
Cdd:PRK08974 206 EDLAFLQYTGGTTGVAKGAMLTHRNM--LAnleqAKAAYGPLLHpGKELVVTALPLYH------------IFALTV---- 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 132 kfsasrfwddcvkyNCTVVQYIGeICRYLLRQPvRDVE------QRHRV---------------------------RLAV 178
Cdd:PRK08974 268 --------------NCLLFIELG-GQNLLITNP-RDIPgfvkelKKYPFtaitgvntlfnallnneefqeldfsslKLSV 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 179 GNGL--RPAI---WEEFTQRFgvpqIGEFYGATECN----CSIANMDGKVGSCGFnsrilthvyPIrlvkvnEDTMEPLR 249
Cdd:PRK08974 332 GGGMavQQAVaerWVKLTGQY----LLEGYGLTECSplvsVNPYDLDYYSGSIGL---------PV------PSTEIKLV 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 250 DSEGLCIPcqPGEPGLLVG---QINQ---QDPlrrfdgyvsdSATNKkiahsVFRKGdsaYLS-GDVLVMDELGYMYFRD 322
Cdd:PRK08974 393 DDDGNEVP--PGEPGELWVkgpQVMLgywQRP----------EATDE-----VIKDG---WLAtGDIAVMDEEGFLRIVD 452
|
330 340 350
....*....|....*....|....*....|....*.
gi 1907189430 323 RSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGV 358
Cdd:PRK08974 453 RKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGV 488
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
47-421 |
1.47e-09 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 60.02 E-value: 1.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 47 PLAQAP-GKGMddrlfyIYTSGTTGLPKA------AIVVHSRYYRIAAFGHHSYSMRAADVLYDCLPLYHSAgNIMGVGQ 119
Cdd:PRK13390 143 RLTEQPcGAVM------LYSSGTTGFPKGiqpdlpGRDVDAPGDPIVAIARAFYDISESDIYYSSAPIYHAA-PLRWCSM 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 120 CVIYGLTVVLRKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQpvrDVEQRHRVRL----AVGNGLRPA---IWEEFTQ 192
Cdd:PRK13390 216 VHALGGTVVLAKRFDAQATLGHVERYRITVTQMVPTMFVRLLKL---DADVRTRYDVsslrAVIHAAAPCpvdVKHAMID 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 193 RFGvPQIGEFYGATECNcSIANMD-----GKVGSCGFNSRILTHVYpirlvkvnedtmeplrDSEGLCIPCqpGEPGLLV 267
Cdd:PRK13390 293 WLG-PIVYEYYSSTEAH-GMTFIDspdwlAHPGSVGRSVLGDLHIC----------------DDDGNELPA--GRIGTVY 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 268 GQINQQdPLRrfdgYVSD---SATNKKIAHSVFRKgdsaylSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVL 344
Cdd:PRK13390 353 FERDRL-PFR----YLNDpekTAAAQHPAHPFWTT------VGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENAL 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 345 SRLLGQTDVAVYGVAVP--GVEGKAGMAAIA--DPHSQLdPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQKTRL 420
Cdd:PRK13390 422 TMHPAVHDVAVIGVPDPemGEQVKAVIQLVEgiRGSDEL-ARELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLL 500
|
.
gi 1907189430 421 Q 421
Cdd:PRK13390 501 R 501
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
25-358 |
1.83e-09 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 59.91 E-value: 1.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 25 GPESILPDTQLLDPMLAEAPTTplAQAPGKGMDDRLFYIYTSGTTGLPKAAIVVHSryyriAAFGHHS---YSM--RAAD 99
Cdd:PRK04319 175 EDVEEGPGTLDFNALMEQASDE--FDIEWTDREDGAILHYTSGSTGKPKGVLHVHN-----AMLQHYQtgkYVLdlHEDD 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 100 VlYDCL---------------PLYHSAGNimgvgqcviygltVVLRKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQP 164
Cdd:PRK04319 248 V-YWCTadpgwvtgtsygifaPWLNGATN-------------VIDGGRFSPERWYRILEDYKVTVWYTAPTAIRMLMGAG 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 165 VrDVEQRH-----RVRLAVGNGLRP-AIWeeFTQR-FGVPqIGEFYGATECNCS-IAN---MDGKVGSCGfnsRILTHVY 233
Cdd:PRK04319 314 D-DLVKKYdlsslRHILSVGEPLNPeVVR--WGMKvFGLP-IHDNWWMTETGGImIANypaMDIKPGSMG---KPLPGIE 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 234 pIRLVKVNEDTMEPLRDSEgLCIpcQPGEPGLLVGQINQQDplrRFDGYvsdsatnkkiahsvFRKGdsAYLSGDVLVMD 313
Cdd:PRK04319 387 -AAIVDDQGNELPPNRMGN-LAI--KKGWPSMMRGIWNNPE---KYESY--------------FAGD--WYVSGDSAYMD 443
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1907189430 314 ELGYMYFRDRSGDTFRWRGENVSTTEVEavlSRLLGQTDVAVYGV 358
Cdd:PRK04319 444 EDGYFWFQGRVDDVIKTSGERVGPFEVE---SKLMEHPAVAEAGV 485
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
64-361 |
4.09e-09 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 58.88 E-value: 4.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 64 YTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADVLYDCLPLYHSAGNIMGVGQCVIYGLTVVLRkKFSASRFWDDCV 143
Cdd:PLN03102 193 YTSGTTADPKGVVISHRGAYLSTLSAIIGWEMGTCPVYLWTLPMFHCNGWTFTWGTAARGGTSVCMR-HVTAPEIYKNIE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 144 KYNCTVVQYIGEICRYLLRQPVRDveQRHR---VRLAVGNGLRPAIWEEFTQRFGVpQIGEFYGATECNcsianmdGKVG 220
Cdd:PLN03102 272 MHNVTHMCCVPTVFNILLKGNSLD--LSPRsgpVHVLTGGSPPPAALVKKVQRLGF-QVMHAYGLTEAT-------GPVL 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 221 SCGFN---SRILTH----------VYPIRLVKV---NEDTMEPL-RDSEGLcipcqpGEPgLLVGQINQQdplrrfdGYV 283
Cdd:PLN03102 342 FCEWQdewNRLPENqqmelkarqgVSILGLADVdvkNKETQESVpRDGKTM------GEI-VIKGSSIMK-------GYL 407
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907189430 284 SdsatNKKIAHSVFRKGdsaYL-SGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVygVAVP 361
Cdd:PLN03102 408 K----NPKATSEAFKHG---WLnTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAV--VAMP 477
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
57-358 |
1.32e-08 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 57.19 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 57 DDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYS-----MRAADVLYDCLPLYH----SAGNI--MGVGqcviyGL 125
Cdd:PRK08751 208 DDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQWLAgtgklEEGCEVVITALPLYHifalTANGLvfMKIG-----GC 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 126 TVVLRKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVEQRHRVRLAVGNGL--RPAIWEEFTQRFGVPQIgEFY 203
Cdd:PRK08751 283 NHLISNPRDMPGFVKELKKTRFTAFTGVNTLFNGLLNTPGFDQIDFSSLKMTLGGGMavQRSVAERWKQVTGLTLV-EAY 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 204 GATECNcsianmdgkVGSCgfnsrilthVYPIRLVKVNEDTMEPLrDSEGLCIPCQPGEpGLLVGQINQ---QDPlRRFD 280
Cdd:PRK08751 362 GLTETS---------PAAC---------INPLTLKEYNGSIGLPI-PSTDACIKDDAGT-VLAIGEIGElciKGP-QVMK 420
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907189430 281 GYVSDSATNKKIAHSvfrkgDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGV 358
Cdd:PRK08751 421 GYWKRPEETAKVMDA-----DGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGV 493
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
58-407 |
1.95e-08 |
|
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: 55.85 E-value: 1.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 58 DRLFYIYTSGTTGLPKAAIVVHSRYYRI----AAFGHHSYSM---------RAAD-VLYDCLPLYHSAGNIMGVGQcVIY 123
Cdd:cd05924 4 DDLYILYTGGTTGMPKGVMWRQEDIFRMlmggADFGTGEFTPsedahkaaaAAAGtVMFPAPPLMHGTGSWTAFGG-LLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 124 GLTVVL-RKKFSASRFWDDCVKYNCTVVQYIGEIcryLLRQPVRDVEQRHRVRL----AVGNGlrPAIW-EEFTQRF--G 195
Cdd:cd05924 83 GQTVVLpDDRFDPEEVWRTIEKHKVTSMTIVGDA---MARPLIDALRDAGPYDLsslfAISSG--GALLsPEVKQGLleL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 196 VPQIG--EFYGATEcncSIANMDGKVGSCGFNSRILTHVYPiRLVKVNEDTMEPLRDSEGlcipcqpgepgllVGQINQQ 273
Cdd:cd05924 158 VPNITlvDAFGSSE---TGFTGSGHSAGSGPETGPFTRANP-DTVVLDDDGRVVPPGSGG-------------VGWIARR 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 274 D--PLrrfdGYVSDSatnKKIAHSVFRKGDSAY-LSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQ 350
Cdd:cd05924 221 GhiPL----GYYGDE---AKTAETFPEVDGVRYaVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAV 293
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907189430 351 TDVAVYGVAVP--GVEgkagMAAI--ADPHSQLDPNSMYQELQKVLASYARPIFLRLLPQV 407
Cdd:cd05924 294 YDVLVVGRPDErwGQE----VVAVvqLREGAGVDLEELREHCRTRIARYKLPKQVVFVDEI 350
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
57-420 |
2.22e-08 |
|
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: 56.16 E-value: 2.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 57 DDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADVLYdclpLYHSAG------NIMGVgqcVIYGLTVVLR 130
Cdd:cd17643 93 DDLAYVIYTSGSTGRPKGVVVSHANVLALFAATQRWFGFNEDDVWT----LFHSYAfdfsvwEIWGA---LLHGGRLVVV 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 131 KKF---SASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVEQRHRVRLAV--GNGLRPAIWEEFTQRFGV--PQIGEFY 203
Cdd:cd17643 166 PYEvarSPEDFARLLRDEGVTVLNQTPSAFYQLVEAADRDGRDPLALRYVIfgGEALEAAMLRPWAGRFGLdrPQLVNMY 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 204 GATEcncsianmdgkvgscgfnSRILTHVYPIRLVKVNEDTMEP-----------LRDSEGLCIPcqPGEPGLLV----- 267
Cdd:cd17643 246 GITE------------------TTVHVTFRPLDAADLPAAAASPigrplpglrvyVLDADGRPVP--PGVVGELYvsgag 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 268 ---GQINQQD-PLRRFdgyVSDSATNkkiahsvfrKGDSAYLSGDV---LVMDELGYMyfrDRSGDTFRWRGENVSTTEV 340
Cdd:cd17643 306 varGYLGRPElTAERF---VANPFGG---------PGSRMYRTGDLarrLPDGELEYL---GRADEQVKIRGFRIELGEI 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 341 EAVLSRLLGQTDVAVygVAVPGVEGKAGMAA--IADPHSQLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQKT 418
Cdd:cd17643 371 EAALATHPSVRDAAV--IVREDEPGDTRLVAyvVADDGAAADIAELRALLKELLPDYMVPARYVPLDALPLTVNGKLDRA 448
|
..
gi 1907189430 419 RL 420
Cdd:cd17643 449 AL 450
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
48-420 |
3.22e-08 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 55.78 E-value: 3.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 48 LAQAPGKGMDDRLFYIYTSGTTGLPKAAIVVHSRYYRIA----AFGHHSYSMRAADVLYDCLPLYHSAG------NIMGV 117
Cdd:PRK05857 160 LAGNADQGSEDPLAMIFTSGTTGEPKAVLLANRTFFAVPdilqKEGLNWVTWVVGETTYSPLPATHIGGlwwiltCLMHG 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 118 GQCVIYG-LTVVLRKKFSASRfwddcVKYNCTVVQYIGEICrYLLRQPVRDVEQrhrVRLAVGNGLRpAIWEE--FTQRF 194
Cdd:PRK05857 240 GLCVTGGeNTTSLLEILTTNA-----VATTCLVPTLLSKLV-SELKSANATVPS---LRLVGYGGSR-AIAADvrFIEAT 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 195 GVpQIGEFYGATECNCSIANMDGKVGSCgfnSRI----LTHVYPirLVKVNedtmepLRDSEGLCIPCQPGEPGLLVGQI 270
Cdd:PRK05857 310 GV-RTAQVYGLSETGCTALCLPTDDGSI---VKIeagaVGRPYP--GVDVY------LAATDGIGPTAPGAGPSASFGTL 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 271 NQQDPLRRFdGYVSDSATNKKIAhsvfrkGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQ 350
Cdd:PRK05857 378 WIKSPANML-GYWNNPERTAEVL------IDGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGV 450
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907189430 351 TDVAVYGVAVPGVEGKAGMAAIadPHSQLDPNSMYQELQKVLASY-------ARPIFLRLLPQVDTTGTFKIQKTRL 420
Cdd:PRK05857 451 REAACYEIPDEEFGALVGLAVV--ASAELDESAARALKHTIAARFrresepmARPSTIVIVTDIPRTQSGKVMRASL 525
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
339-414 |
3.44e-08 |
|
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.
Pssm-ID: 463804 [Multi-domain] Cd Length: 76 Bit Score: 50.24 E-value: 3.44e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907189430 339 EVEAVLSRLLGQTDVAVYGVAVPgVEGKAGMA-AIADPHSQLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFK 414
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDE-LKGEAPVAfVVLKPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
38-346 |
3.91e-08 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 55.35 E-value: 3.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 38 PMLAEAPTTPLAQA------PGK---GMDDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADVLYDCLPLY 108
Cdd:PRK08314 162 QALAPGGVVAWKEAlaaglaPPPhtaGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVLPLF 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 109 HSAGNIMGVGQCVIYGLTVVLrkkfsASRfWD-----DCV-KYNCTVVQYIGEICRYLLRQPvrDVEQRHRVRLA-VGNG 181
Cdd:PRK08314 242 HVTGMVHSMNAPIYAGATVVL-----MPR-WDreaaaRLIeRYRVTHWTNIPTMVVDFLASP--GLAERDLSSLRyIGGG 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 182 ---LRPAIWEEFTQRFGVPQIgEFYGATECNC-SIAN-MDGKVGSC------GFNSRIlthvypirlvkVNEDTMEPLrd 250
Cdd:PRK08314 314 gaaMPEAVAERLKELTGLDYV-EGYGLTETMAqTHSNpPDRPKLQClgiptfGVDARV-----------IDPETLEEL-- 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 251 seglcipcQPGEpgllVGQINQQDPlRRFDGYVSDSATNKKI-----AHSVFRKGDSAYlsgdvlvMDELGYMYFRDRSG 325
Cdd:PRK08314 380 --------PPGE----VGEIVVHGP-QVFKGYWNRPEATAEAfieidGKRFFRTGDLGR-------MDEEGYFFITDRLK 439
|
330 340
....*....|....*....|.
gi 1907189430 326 DTFRWRGENVSTTEVEAVLSR 346
Cdd:PRK08314 440 RMINASGFKVWPAEVENLLYK 460
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
58-417 |
4.02e-08 |
|
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: 54.96 E-value: 4.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 58 DRLFYIYTSGTTGLPKAAIVVHSRYYriAAFGH---HSYSMRAADVLYDCLPLYHSAGN------IMGVGQCVIYGLTVV 128
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANKTFF--AVPDIlqkEGLNWVVGDVTYLPLPATHIGGLwwiltcLIHGGLCVTGGENTT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 129 LRKKFSASRFWDdcVKYNCTVVQYIGEICRyLLRQPVRDVEQrhrVRLAVGNGLRP-AIWEEFTQRFGVPQIGEFYGATE 207
Cdd:cd17635 80 YKSLFKILTTNA--VTTTCLVPTLLSKLVS-ELKSANATVPS---LRLIGYGGSRAiAADVRFIEATGLTNTAQVYGLSE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 208 CN--CSIANMDG--KVGSCGfnsriltHVYPIRLVKV-NEDTMEPLRDSEGLCIPCQPgepgllvgqinqqdplRRFDGY 282
Cdd:cd17635 154 TGtaLCLPTDDDsiEINAVG-------RPYPGVDVYLaATDGIAGPSASFGTIWIKSP----------------ANMLGY 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 283 VSdsatNKKIAHSVFRKGdsaYL-SGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYgvAVP 361
Cdd:cd17635 211 WN----NPERTAEVLIDG---WVnTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACY--EIS 281
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907189430 362 GVEGKAGMAAIADPHSQLDPNSMYQELQKV---LASYARPIFLRLLPQVDTTGTFKIQK 417
Cdd:cd17635 282 DEEFGELVGLAVVASAELDENAIRALKHTIrreLEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
57-405 |
6.48e-08 |
|
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.
Pssm-ID: 341271 [Multi-domain] Cd Length: 617 Bit Score: 55.01 E-value: 6.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 57 DDRLFYIYTSGTTGLPKAaIVVHSRYYRIAAfghhSYSMRAadvLYDCLP--LYHSAGNImG--VGQCVI-YG------L 125
Cdd:cd05967 230 TDPLYILYTSGTTGKPKG-VVRDNGGHAVAL----NWSMRN---IYGIKPgdVWWAASDV-GwvVGHSYIvYGpllhgaT 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 126 TVVLRKKFS----ASRFWDDCVKYNCTVVQYIGEICRYLLRQP-----VRDVE-QRHRVRLAVGNGLRPAIWEEFTQRFG 195
Cdd:cd05967 301 TVLYEGKPVgtpdPGAFWRVIEKYQVNALFTAPTAIRAIRKEDpdgkyIKKYDlSSLRTLFLAGERLDPPTLEWAENTLG 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 196 VPQIgEFYGATE------CNCS-IANMDGKVGSC-----GFNsrilthvypirlVKVNEDTMEPLRDSE--GLCI--PCQ 259
Cdd:cd05967 381 VPVI-DHWWQTEtgwpitANPVgLEPLPIKAGSPgkpvpGYQ------------VQVLDEDGEPVGPNElgNIVIklPLP 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 260 PGE-PGLLvgqinqQDPLRRFDGYVSDSatnkkiahsvfrkgDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTT 338
Cdd:cd05967 448 PGClLTLW------KNDERFKKLYLSKF--------------PGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTG 507
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907189430 339 EVEAVLSRLLGQTDVAVYGVaVPGVEGKAGMA-AIADPHSQLDPNSMYQELQKV-------LASYARPIFLRLLP 405
Cdd:cd05967 508 EMEESVLSHPAVAECAVVGV-RDELKGQVPLGlVVLKEGVKITAEELEKELVALvreqigpVAAFRLVIFVKRLP 581
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
57-420 |
9.39e-08 |
|
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: 54.01 E-value: 9.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 57 DDRLFYIYTSGTTGLPKAAIVVHS----------RYYRIAAFGHHSYSMR--AADVLYDCLPLYHSAGnimgvGQCVIyg 124
Cdd:cd17650 93 EDLAYVIYTSGTTGKPKGVMVEHRnvahaahawrREYELDSFPVRLLQMAsfSFDVFAGDFARSLLNG-----GTLVI-- 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 125 ltVVLRKKFSASRFWDDCVKYNCTVVQYIGEICRyllrqPVRDVEQRHRVR------LAVGNGLRPAIW-EEFTQRFGVP 197
Cdd:cd17650 166 --CPDEVKLDPAALYDLILKSRITLMESTPALIR-----PVMAYVYRNGLDlsamrlLIVGSDGCKAQDfKTLAARFGQG 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 198 -QIGEFYGATEcncsiANMDGKVGSCGFNSRILTHVYPI-------RLVKVNE-DTMEPLRDSEGLCIpcqpGEPGLLVG 268
Cdd:cd17650 239 mRIINSYGVTE-----ATIDSTYYEEGRDPLGDSANVPIgrplpntAMYVLDErLQPQPVGVAGELYI----GGAGVARG 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 269 QINQQDplrrfdgyvsdsATNKKIAHSVFRKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLL 348
Cdd:cd17650 310 YLNRPE------------LTAERFVENPFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHP 377
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907189430 349 GQTDVAVygVAVPGVEGKAGMAAIADPHSQLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQKTRL 420
Cdd:cd17650 378 AIDEAVV--AVREDKGGEARLCAYVVAAATLNTAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
38-421 |
9.73e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 54.01 E-value: 9.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 38 PMLAEAPTTPlaqAPGKGMDDRLFYI-YTSGTTGLPKAAIVVHSRYyrIAAF--GHHSYSMRAADVLYDCLPLYHSAgNI 114
Cdd:PRK07638 126 RMIEKYLPTY---APIENVQNAPFYMgFTSGSTGKPKAFLRAQQSW--LHSFdcNVHDFHMKREDSVLIAGTLVHSL-FL 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 115 MGVGQCVIYGLTVVLRKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPvRDVEQRHRVrlaVGNGlrpAIW-----EE 189
Cdd:PRK07638 200 YGAISTLYVGQTVHLMRKFIPNQVLDKLETENISVMYTVPTMLESLYKEN-RVIENKMKI---ISSG---AKWeaeakEK 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 190 FTQRFGVPQIGEFYGATECNCSIANMDG----KVGSCGfnsrilTHVYPIRLVKVNEDTMEplrdseglcipCQPGEpgl 265
Cdd:PRK07638 273 IKNIFPYAKLYEFYGASELSFVTALVDEeserRPNSVG------RPFHNVQVRICNEAGEE-----------VQKGE--- 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 266 lVGQINQQDPLRrFDGYVSDSATNKKIAhsvfrkgDSAYLS-GDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVL 344
Cdd:PRK07638 333 -IGTVYVKSPQF-FMGYIIGGVLARELN-------ADGWMTvRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVL 403
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907189430 345 SRLLGQTDVAVYGVAVPgvegKAGMAAIADPHSQLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQKTRLQ 421
Cdd:PRK07638 404 HEHPAVDEIVVIGVPDS----YWGEKPVAIIKGSATKQQLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEAK 476
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
57-420 |
1.49e-07 |
|
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: 53.33 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 57 DDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAAD--VLYDCLPLYHSAGNIMgvgQCVIYGLTVVL---RK 131
Cdd:cd17645 104 DDLAYVIYTSGSTGLPKGVMIEHHNLVNLCEWHRPYFGVTPADksLVYASFSFDASAWEIF---PHLTAGAALHVvpsER 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 132 KFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPvrdvEQRHRVRLAVGNGLRPAIWEEFtqrfgvpQIGEFYGATECN-- 209
Cdd:cd17645 181 RLDLDALNDYFNQEGITISFLPTGAAEQFMQLD----NQSLRVLLTGGDKLKKIERKGY-------KLVNNYGPTENTvv 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 210 CSIANMDGKVGSCGFNSRILThvypIRLVKVNED-TMEPLRDSEGLCIPcqpGEpGLLVGQINQQDplrrfdgyvsdsAT 288
Cdd:cd17645 250 ATSFEIDKPYANIPIGKPIDN----TRVYILDEAlQLQPIGVAGELCIA---GE-GLARGYLNRPE------------LT 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 289 NKKIAHSVFRKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVygVAVPGVEGKAG 368
Cdd:cd17645 310 AEKFIVHPFVPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAV--LAKEDADGRKY 387
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1907189430 369 MAAIADPHSQLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQKTRL 420
Cdd:cd17645 388 LVAYVTAPEEIPHEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
30-420 |
1.87e-07 |
|
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: 53.43 E-value: 1.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 30 LPDTQLLDPMLAEAPTTPLAQAPGKgmDDRLFYIYTSGTTGLPKAAIVVH-SRYYRIAAFgHHSYSMRAADVL------- 101
Cdd:cd17646 113 GDVALLGDEALAAPPATPPLVPPRP--DNLAYVIYTSGSTGRPKGVMVTHaGIVNRLLWM-QDEYPLGPGDRVlqktpls 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 102 YDC------LPLYHSAGNIMGV--GQCVIYGLTVVLRkkfsasrfwDDCVkyncTVVQYIGEICRYLLRQPvrDVEQRHR 173
Cdd:cd17646 190 FDVsvwelfWPLVAGARLVVARpgGHRDPAYLAALIR---------EHGV----TTCHFVPSMLRVFLAEP--AAGSCAS 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 174 VRLAV--GNGLRPAIWEEFTQRFGVPqIGEFYGATE-------CNCSIANMDGKV--GSCGFNSRILthvypirlvkVNE 242
Cdd:cd17646 255 LRRVFcsGEALPPELAARFLALPGAE-LHNLYGPTEaaidvthWPVRGPAETPSVpiGRPVPNTRLY----------VLD 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 243 DTMEplrdseglciPCQPGEPG-LLVGQInqqdPLRRfdGYVSDSA-TNKKIAHSVFRKGDSAYLSGDVLVMDELGYMYF 320
Cdd:cd17646 324 DALR----------PVPVGVPGeLYLGGV----QLAR--GYLGRPAlTAERFVPDPFGPGSRMYRTGDLARWRPDGALEF 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 321 RDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVygVAVPGVEGKAGMAA---IADPHSQLDPNSMYQELQKVLASYAR 397
Cdd:cd17646 388 LGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVV--VARAAPAGAARLVGyvvPAAGAAGPDTAALRAHLAERLPEYMV 465
|
410 420
....*....|....*....|...
gi 1907189430 398 PIFLRLLPQVDTTGTFKIQKTRL 420
Cdd:cd17646 466 PAAFVVLDALPLTANGKLDRAAL 488
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
50-429 |
3.14e-07 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 52.72 E-value: 3.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 50 QAPGKGMDDRLFYIYTSGTTGLPKAAIVVH----SRYYRIAAFGHHSYSMRAAD--VLYDC-LPLYH----SAGNIMGVG 118
Cdd:PRK07059 197 KPVKLGPDDVAFLQYTGGTTGVSKGATLLHrnivANVLQMEAWLQPAFEKKPRPdqLNFVCaLPLYHifalTVCGLLGMR 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 119 QCviyGLTVVLRKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVEQRHRVRLAVGNGL--RPAIWEEFTQRFGV 196
Cdd:PRK07059 277 TG---GRNILIPNPRDIPGFIKELKKYQVHIFPAVNTLYNALLNNPDFDKLDFSKLIVANGGGMavQRPVAERWLEMTGC 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 197 PqIGEFYGATECN----CSIANMDGKVGSCGFnsrilthvyPIrlvkvnEDTMEPLRDSEGLCIPC-QPGE-----PGLL 266
Cdd:PRK07059 354 P-ITEGYGLSETSpvatCNPVDATEFSGTIGL---------PL------PSTEVSIRDDDGNDLPLgEPGEicirgPQVM 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 267 VGQINQQDPLRRF---DGYvsdsatnkkiahsvFRkgdsaylSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAV 343
Cdd:PRK07059 418 AGYWNRPDETAKVmtaDGF--------------FR-------TGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEV 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 344 LSRLLGQTDVAVYGVavpgvegkagmaaiADPHS---------QLDPNSMYQELQKV----LASYARPIFLRLLPQVDTT 410
Cdd:PRK07059 477 VASHPGVLEVAAVGV--------------PDEHSgeavklfvvKKDPALTEEDVKAFckerLTNYKRPKFVEFRTELPKT 542
|
410
....*....|....*....
gi 1907189430 411 GTFKIqktrLQREGFDPRQ 429
Cdd:PRK07059 543 NVGKI----LRRELRDGKA 557
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
21-129 |
4.14e-07 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 52.86 E-value: 4.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 21 SGDLGPESILPDTqlLDPMLAEApttplAQAPGKGMDDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAA-- 98
Cdd:PRK05691 137 AAANAPELLCVDT--LDPALAEA-----WQEPALQPDDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGIDLNpd 209
|
90 100 110
....*....|....*....|....*....|.
gi 1907189430 99 DVLYDCLPLYHSAGNIMGVGQCVIYGLTVVL 129
Cdd:PRK05691 210 DVIVSWLPLYHDMGLIGGLLQPIFSGVPCVL 240
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
57-422 |
5.86e-07 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 51.82 E-value: 5.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 57 DDRLFYIYTSGTTGLPKAAIVVHSRY--YRIAAFgHHSYSMRAADVLY---DClplyhsaGNIMGvGQCVIYG-----LT 126
Cdd:PLN02654 275 EDPLFLLYTSGSTGKPKGVLHTTGGYmvYTATTF-KYAFDYKPTDVYWctaDC-------GWITG-HSYVTYGpmlngAT 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 127 VVLRKKF----SASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVEQRHRVRL----AVGNGLRPAIWEEFTQRFGvpq 198
Cdd:PLN02654 346 VLVFEGApnypDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGDEYVTRHSRKSLrvlgSVGEPINPSAWRWFFNVVG--- 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 199 igefygatECNCSIANMDGKVGSCGFNSRILTHVYP------------IRLVKVNEDTMEPLRDSEG-LCIPCQ-PGEPG 264
Cdd:PLN02654 423 --------DSRCPISDTWWQTETGGFMITPLPGAWPqkpgsatfpffgVQPVIVDEKGKEIEGECSGyLCVKKSwPGAFR 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 265 LLVGQINQQDP--LRRFDGYvsdsatnkkiahsvfrkgdsaYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEA 342
Cdd:PLN02654 495 TLYGDHERYETtyFKPFAGY---------------------YFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVES 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 343 VLSRLLGQTDVAVYGV--AVPGvEGKAGMAAIAD--PHSQLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQKT 418
Cdd:PLN02654 554 ALVSHPQCAEAAVVGIehEVKG-QGIYAFVTLVEgvPYSEELRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRR 632
|
....
gi 1907189430 419 RLQR 422
Cdd:PLN02654 633 ILRK 636
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
57-420 |
1.02e-06 |
|
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: 50.71 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 57 DDRLFYI-YTSGTTGLPKAaiVVHSrYYRIAAFGHHS---YSMRAADVLYdCLPLYHSAGNIMGVGQCVIYGLTVV-LRK 131
Cdd:cd05945 96 GDDNAYIiFTSGSTGRPKG--VQIS-HDNLVSFTNWMlsdFPLGPGDVFL-NQAPFSFDLSVMDLYPALASGATLVpVPR 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 132 KFSAS--RFWDDCVKYNCTV---VQYIGEICrylLRQPVRDVEQRHRVRLAVGNGlrpaiwEEFT--------QRFGVPQ 198
Cdd:cd05945 172 DATADpkQLFRFLAEHGITVwvsTPSFAAMC---LLSPTFTPESLPSLRHFLFCG------EVLPhktaralqQRFPDAR 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 199 IGEFYGATECN--CSIANMDGKVgsCGFNSRIlthvyPIRLVKVNEDTMepLRDSEGLCIPcqPGEPG--LLVGQinqqd 274
Cdd:cd05945 243 IYNTYGPTEATvaVTYIEVTPEV--LDGYDRL-----PIGYAKPGAKLV--ILDEDGRPVP--PGEKGelVISGP----- 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 275 plRRFDGYVSDSATNKKIAHSVfrKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVA 354
Cdd:cd05945 307 --SVSKGYLNNPEKTAAAFFPD--EGQRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAV 382
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907189430 355 VygVAVPGVEGKAGMAAIADPH---SQLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQKTRL 420
Cdd:cd05945 383 V--VPKYKGEKVTELIAFVVPKpgaEAGLTKAIKAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
289-423 |
1.42e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 50.72 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 289 NKKIAHSVFRKGdsAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVygVAVPG------ 362
Cdd:PRK08162 405 NPKATEEAFAGG--WFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAV--VAKPDpkwgev 480
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907189430 363 ----VEGKAGMAAIADphsqldpnsmyqEL----QKVLASYARP--IFLRLLPQvdtTGTFKIQKTRLQRE 423
Cdd:PRK08162 481 pcafVELKDGASATEE------------EIiahcREHLAGFKVPkaVVFGELPK---TSTGKIQKFVLREQ 536
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
57-375 |
1.53e-06 |
|
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: 50.52 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 57 DDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADVLYDCLPLYHSAGNIMGVGQCVIYGLTVVLRKKFSAS 136
Cdd:cd05914 89 DDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLLGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFLDKIPSA 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 137 RFwDDCVKYNCTVV-------------------QYIGEICRYLLRQPVRDVEQRHRVRLAV--------------GNGLR 183
Cdd:cd05914 169 KI-IALAFAQVTPTlgvpvplviekifkmdiipKLTLKKFKFKLAKKINNRKIRKLAFKKVheafggnikefvigGAKIN 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 184 PAIwEEFTQRFGVPQIgEFYGATECN---CSIANMDGKVGSCGFnsrilthvyPIRLVKVNEDTMEPlrdseglcipcQP 260
Cdd:cd05914 248 PDV-EEFLRTIGFPYT-IGYGMTETApiiSYSPPNRIRLGSAGK---------VIDGVEVRIDSPDP-----------AT 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 261 GEPGLLVGQINQqdplrrFDGYVSdsatNKKIAHSVFRKgDSAYLSGDVLVMDELGYMYFRDRSGDTFRW-RGENVSTTE 339
Cdd:cd05914 306 GEGEIIVRGPNV------MKGYYK----NPEATAEAFDK-DGWFHTGDLGKIDAEGYLYIRGRKKEMIVLsSGKNIYPEE 374
|
330 340 350
....*....|....*....|....*....|....*.
gi 1907189430 340 VEAVLSRLlgqTDVAVYGVAVpgVEGKAGMAAIADP 375
Cdd:cd05914 375 IEAKINNM---PFVLESLVVV--QEKKLVALAYIDP 405
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
40-129 |
1.62e-06 |
|
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: 50.31 E-value: 1.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 40 LAEAPTTPLAQAPGKGMDDRLFYIYTSGTTGLPKAAIVVHsryyriAAFGH------HSYSMRAADVLYDCLPLYHSAGN 113
Cdd:cd05931 132 LLPDTSAADWPPPSPDPDDIAYLQYTSGSTGTPKGVVVTH------RNLLAnvrqirRAYGLDPGDVVVSWLPLYHDMGL 205
|
90
....*....|....*.
gi 1907189430 114 IMGVGQCVIYGLTVVL 129
Cdd:cd05931 206 IGGLLTPLYSGGPSVL 221
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
64-423 |
1.78e-06 |
|
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: 50.32 E-value: 1.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 64 YTSGTTGLPKAAIVVHSRYYriaafgHHSYSMRAADVLY----D----CLPLYHsaGNIMGVG-QCVIYGLTVVLRKKF- 133
Cdd:cd12119 170 YTSGTTGNPKGVVYSHRSLV------LHAMAALLTDGLGlsesDvvlpVVPMFH--VNAWGLPyAAAMVGAKLVLPGPYl 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 134 ---SASRFWDdcvKYNCTVVQYIGEICRYLLRQPVR-DVEQRHRVRLAVGNG-LRPAIWEEFTQRfGVPQIgEFYGATE- 207
Cdd:cd12119 242 dpaSLAELIE---REGVTFAAGVPTVWQGLLDHLEAnGRDLSSLRRVVIGGSaVPRSLIEAFEER-GVRVI-HAWGMTEt 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 208 CNCSIAN-----MDGKVGSCGFNSRILTHvYPIRLVK---VNEDTMEPLRDSEGLcipcqpGE-----PGLLVGQINQQD 274
Cdd:cd12119 317 SPLGTVArppseHSNLSEDEQLALRAKQG-RPVPGVElriVDDDGRELPWDGKAV------GElqvrgPWVTKSYYKNDE 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 275 PLRRF--DGYvsdsatnkkiahsvFRkgdsaylSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTD 352
Cdd:cd12119 390 ESEALteDGW--------------LR-------TGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAE 448
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907189430 353 VAVYGVAVPgvegKAG---MAAI-ADPHSQLDPNSMYQELQKVLASYARP---IFLRLLPQvdtTGTFKIQKTRLqRE 423
Cdd:cd12119 449 AAVIGVPHP----KWGerpLAVVvLKEGATVTAEELLEFLADKVAKWWLPddvVFVDEIPK---TSTGKIDKKAL-RE 518
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
1-80 |
1.78e-06 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 50.56 E-value: 1.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 1 MAAAVAEVSEQLgKSLLKFCS----GDLGPESILPDTQLLDPMLAEAPTTPLAQAPGkGMDDRLFYIYTSGTTGLPKAai 76
Cdd:PRK03584 205 RRAKVAELRAAL-PSLEHVVVvpylGPAAAAAALPGALLWEDFLAPAEAAELEFEPV-PFDHPLWILYSSGTTGLPKC-- 280
|
....
gi 1907189430 77 VVHS 80
Cdd:PRK03584 281 IVHG 284
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
53-352 |
1.84e-06 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 50.20 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 53 GKGMDDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADVLYDCLPLYHSAG-NIMGV-----GQCVIYGLT 126
Cdd:PRK06334 179 DKDPEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSFLPPFHAYGfNSCTLfpllsGVPVVFAYN 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 127 VVLRKKFSasRFWDDcvkyncTVVQYIGE---ICRYLLRQPVRDVEQRHRVRLAV--GNGLRPAIWEEFTQRFGVPQIGE 201
Cdd:PRK06334 259 PLYPKKIV--EMIDE------AKVTFLGStpvFFDYILKTAKKQESCLPSLRFVVigGDAFKDSLYQEALKTFPHIQLRQ 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 202 FYGATECN--CSIANMDG-KVGSCgfnsrilthvypirlVKVNEDTMEPLRDSEGLCIPCQPGEPGLLVGQINQQdplrr 278
Cdd:PRK06334 331 GYGTTECSpvITINTVNSpKHESC---------------VGMPIRGMDVLIVSEETKVPVSSGETGLVLTRGTSL----- 390
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907189430 279 FDGYVSDSATNKKIAHSvfrkGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTD 352
Cdd:PRK06334 391 FSGYLGEDFGQGFVELG----GETWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEGFGQNA 460
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
24-421 |
4.61e-06 |
|
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: 49.00 E-value: 4.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 24 LGPESILPDTQLLDPMLAEAPttPLAQAPGKGMDDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADVLYD 103
Cdd:cd05932 106 LPPPSAANCQYQWDDLIAQHP--PLEERPTRFPEQLATLIYTSGTTGQPKGVMLTFGSFAWAAQAGIEHIGTEENDRMLS 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 104 CLPLYHSAGNIMGVGQCVIYGLTV------------VLRKK----FSASRFWddcVKYNCTVVQYIG-EICRYLLRQPVR 166
Cdd:cd05932 184 YLPLAHVTERVFVEGGSLYGGVLVafaesldtfvedVQRARptlfFSVPRLW---TKFQQGVQDKIPqQKLNLLLKIPVV 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 167 DVEQRHRV---------RLAVGNG--LRPAIWEEFtQRFGVPqIGEFYGATEcNCSIANM----DGKVGSCGFNsrilth 231
Cdd:cd05932 261 NSLVKRKVlkglgldqcRLAGCGSapVPPALLEWY-RSLGLN-ILEAYGMTE-NFAYSHLnypgRDKIGTVGNA------ 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 232 vYPIRLVKVNEDTmEPLRDSeglcipcqpgePGLLVGQinqqdplrrfdgYVSDSATNkkiahSVFRKgDSAYLSGDVLV 311
Cdd:cd05932 332 -GPGVEVRISEDG-EILVRS-----------PALMMGY------------YKDPEATA-----EAFTA-DGFLRTGDKGE 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 312 MDELGYMYFRDRSGDTFRW-RGENVSTTEVEAVLSR--------LLGQTDVAVYGVAVPGVEGKAGMAAIA--------- 373
Cdd:cd05932 381 LDADGNLTITGRVKDIFKTsKGKYVAPAPIENKLAEhdrvemvcVIGSGLPAPLALVVLSEEARLRADAFAraeleaslr 460
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907189430 374 ----------DPHSQLDPNSMYQELQKVLASYARPiflrllpqvdttgTFKIQKTRLQ 421
Cdd:cd05932 461 ahlarvnstlDSHEQLAGIVVVKDPWSIDNGILTP-------------TLKIKRNVLE 505
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
20-420 |
4.88e-06 |
|
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: 48.81 E-value: 4.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 20 CSGDLGPESILPDTQLLDPMLAEAPTTPLAQAPGkgMDDRLFYIYTSGTTGLPKAAIVVHSRYYR-IAAFGHHsYSMRAA 98
Cdd:cd12114 91 DGPDAQLDVAVFDVLILDLDALAAPAPPPPVDVA--PDDLAYVIFTSGSTGTPKGVMISHRAALNtILDINRR-FAVGPD 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 99 DVLYDCLPLYH--SAGNIMGVgqcVIYGLTVVL----RKKFSASrfWDDCV-KYNCTVVQYIGEICRYLLRQPVRDVEQR 171
Cdd:cd12114 168 DRVLALSSLSFdlSVYDIFGA---LSAGATLVLpdeaRRRDPAH--WAELIeRHGVTLWNSVPALLEMLLDVLEAAQALL 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 172 HRVRLA------VGNGLRPAIWeeftQRFGVPQIGEFYGATEcncsianmdgkvGScgfnsrILTHVYPIRlvKVNEDTM 245
Cdd:cd12114 243 PSLRLVllsgdwIPLDLPARLR----ALAPDARLISLGGATE------------AS------IWSIYHPID--EVPPDWR 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 246 E-----PLR-------DSEGLciPCQPGEPG-LLVGQIN-----QQDPLRRFDGYVSDSAtnkkiAHSVFRKGDSAYLSG 307
Cdd:cd12114 299 SipygrPLAnqryrvlDPRGR--DCPDWVPGeLWIGGRGvalgyLGDPELTAARFVTHPD-----GERLYRTGDLGRYRP 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 308 DvlvmdelGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPGVEGKAGMAAIADPHSQLDPNSMYQE 387
Cdd:cd12114 372 D-------GTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDPGGKRLAAFVVPDNDGTPIAPDALRAF 444
|
410 420 430
....*....|....*....|....*....|...
gi 1907189430 388 LQKVLASYARPIFLRLLPQVDTTGTFKIQKTRL 420
Cdd:cd12114 445 LAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
55-127 |
5.63e-06 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 48.56 E-value: 5.63e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907189430 55 GMDDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADVLYDCLPLYHSAGNIMGVGqCVIYGLTV 127
Cdd:COG1022 181 KPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFLPLAHVFERTVSYY-ALAAGATV 252
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
257-420 |
9.67e-06 |
|
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: 47.97 E-value: 9.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 257 PCQPGEPG-LLVGQinqqDPLRRfdGYVSDSA-TNKKIAHSVFRKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGEN 334
Cdd:cd12117 326 PVPPGVPGeLYVGG----DGLAL--GYLNRPAlTAERFVADPFGPGERLYRTGDLARWLPDGRLEFLGRIDDQVKIRGFR 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 335 VSTTEVEAVLSRLLGQTDVAVygVAVPGVEGKAGMAAIADPHSQLDPNSMYQELQKVLASYARP---IFLRLLPQvdtTG 411
Cdd:cd12117 400 IELGEIEAALRAHPGVREAVV--VVREDAGGDKRLVAYVVAEGALDAAELRAFLRERLPAYMVPaafVVLDELPL---TA 474
|
....*....
gi 1907189430 412 TFKIQKTRL 420
Cdd:cd12117 475 NGKVDRRAL 483
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
63-424 |
1.01e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 47.68 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 63 IYTSGTTGLPKAaiVVHSRyyRIAAFG----HHSYSMRAADVLYDCLPLYHSAGNIMGVGQCVIYGLTVVLRKKFSASRF 138
Cdd:PRK07787 134 VYTSGTTGPPKG--VVLSR--RAIAADldalAEAWQWTADDVLVHGLPLFHVHGLVLGVLGPLRIGNRFVHTGRPTPEAY 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 139 WDDCvKYNCTVvqYIGEICRYllrqpvrdveqrHRV-------------RLAV-GNGLRPA-IWEEFTQRFGVPQIgEFY 203
Cdd:PRK07787 210 AQAL-SEGGTL--YFGVPTVW------------SRIaadpeaaralrgaRLLVsGSAALPVpVFDRLAALTGHRPV-ERY 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 204 GATEC--NCSI-ANMDGKVGSCGFnsrilthvyPIRLVKVNedtmepLRDSEGLCIPCQpGEPgllVGQINQQDPLrRFD 280
Cdd:PRK07787 274 GMTETliTLSTrADGERRPGWVGL---------PLAGVETR------LVDEDGGPVPHD-GET---VGELQVRGPT-LFD 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 281 GYVsdsatNKKIAHSVFRKGDSAYLSGDVLVMDELGYMYFRDR-SGDTFRWRGENVSTTEVEAVlsrLLGQTDVAvyGVA 359
Cdd:PRK07787 334 GYL-----NRPDATAAAFTADGWFRTGDVAVVDPDGMHRIVGReSTDLIKSGGYRIGAGEIETA---LLGHPGVR--EAA 403
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907189430 360 VPGVE----GKAGMAAIAdPHSQLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQKTRLQREG 424
Cdd:PRK07787 404 VVGVPdddlGQRIVAYVV-GADDVAADELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLLSEG 471
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
22-428 |
1.29e-05 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 47.86 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 22 GDLGPESILPDTQLLDPMLAEAPTTPLA-----------QAPGKGM-DDRLFY-IYTSGTTGLPKAAIVVHSRYYRIAAF 88
Cdd:PRK05691 1225 ADSGVELLLTQSHLLERLPQAEGVSAIAldslhldswpsQAPGLHLhGDNLAYvIYTSGSTGQPKGVGNTHAALAERLQW 1304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 89 GHHSYSMRAADVLYDCLPLYHSagniMGVGQC---VIYGLTVVLR---KKFSASRFWDDCVKYNCTVVQYIGEICRYLLR 162
Cdd:PRK05691 1305 MQATYALDDSDVLMQKAPISFD----VSVWECfwpLITGCRLVLAgpgEHRDPQRIAELVQQYGVTTLHFVPPLLQLFID 1380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 163 QPvrDVEQRHRVRLAV--GNGLRPAIWEEFTQRFGVPQIGEFYGATEC-------NCSIAnmDGKVGSCGfnsRILTHVy 233
Cdd:PRK05691 1381 EP--LAAACTSLRRLFsgGEALPAELRNRVLQRLPQVQLHNRYGPTETainvthwQCQAE--DGERSPIG---RPLGNV- 1452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 234 pirLVKVNEDTMEPLrdseglcipcQPGEPG-LLVGQINqqdpLRRfdGYVSDSATNKK--IAHSVFRKGDSAYLSGDVL 310
Cdd:PRK05691 1453 ---LCRVLDAELNLL----------PPGVAGeLCIGGAG----LAR--GYLGRPALTAErfVPDPLGEDGARLYRTGDRA 1513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 311 VMDELGYMYFRDRSGDTFRWRGENVSTTEVEAvlsRLLGQTDVAVYGVAVPgvEGKAGMAAI----ADPHSQLDPNSMYQ 386
Cdd:PRK05691 1514 RWNADGALEYLGRLDQQVKLRGFRVEPEEIQA---RLLAQPGVAQAAVLVR--EGAAGAQLVgyytGEAGQEAEAERLKA 1588
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1907189430 387 ELQKVLASYARPIFLRLLPQVDTTGTFKIQKTRL------QREGFDPR 428
Cdd:PRK05691 1589 ALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRALpepvwqQREHVEPR 1636
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
56-376 |
2.83e-05 |
|
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.
Pssm-ID: 341270 [Multi-domain] Cd Length: 608 Bit Score: 46.40 E-value: 2.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 56 MD--DRLFYIYTSGTTGLPKAaiVVHS----------------------RYYRIAAFG---HHSYsmraadVLYDclPLy 108
Cdd:cd05966 228 MDseDPLFILYTSGSTGKPKG--VVHTtggyllyaattfkyvfdyhpddIYWCTADIGwitGHSY------IVYG--PL- 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 109 hsagnimgvgqcvIYGLTVVLrkkF-------SASRFWDDCVKYNCTVVQYIGEICRYLLRQPvRDVEQRH-----RVRL 176
Cdd:cd05966 297 -------------ANGATTVM---FegtptypDPGRYWDIVEKHKVTIFYTAPTAIRALMKFG-DEWVKKHdlsslRVLG 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 177 AVGNGLRPAIWEEFTQRFG---VPqIGEFYGATEC-NCSIANMDG----KVGSCGFnsrilthvyP---IRLVKVNEDTM 245
Cdd:cd05966 360 SVGEPINPEAWMWYYEVIGkerCP-IVDTWWQTETgGIMITPLPGatplKPGSATR---------PffgIEPAILDEEGN 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 246 EPLRDSEG-LCIPcQPGePGLLVGQINqqDPLRRFDGYvsdsatnkkiahsvFRKGDSAYLSGDVLVMDELGYMYFRDRS 324
Cdd:cd05966 430 EVEGEVEGyLVIK-RPW-PGMARTIYG--DHERYEDTY--------------FSKFPGYYFTGDGARRDEDGYYWITGRV 491
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1907189430 325 GDTFRWRGENVSTTEVEAVLsrllgqtdvavygVAVPGVegkAGMAAIADPH 376
Cdd:cd05966 492 DDVINVSGHRLGTAEVESAL-------------VAHPAV---AEAAVVGRPH 527
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
301-420 |
3.03e-05 |
|
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: 46.17 E-value: 3.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 301 DSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVygVAVPG-VEGKAGMAAIADPHSQL 379
Cdd:cd05920 363 DGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAV--VAMPDeLLGERSCAFVVLRDPPP 440
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1907189430 380 DPNSMYQEL-QKVLASYARPIFLRLLPQVDTTGTFKIQKTRL 420
Cdd:cd05920 441 SAAQLRRFLrERGLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
48-420 |
3.52e-05 |
|
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: 45.82 E-value: 3.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 48 LAQAPgkgmdDRLFY-IYTSGTTGLPKAAIVVHsryyriAAFGHHS------YSMRAADVLYDCLPLYHSAGnIMGVGQC 120
Cdd:cd17649 89 LTHHP-----RQLAYvIYTSGSTGTPKGVAVSH------GPLAAHCqataerYGLTPGDRELQFASFNFDGA-HEQLLPP 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 121 VIYGLTVVLRKK---FSASRFWDDCVKYNCTVVQ----YIGEICRYLLRQPVRDveqRHRVRLAV--GNGLRPAIWEEfT 191
Cdd:cd17649 157 LICGACVVLRPDelwASADELAEMVRELGVTVLDlppaYLQQLAEEADRTGDGR---PPSLRLYIfgGEALSPELLRR-W 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 192 QRFGVPQIGEfYGATECNCSIANMDGKVG-SCGFNSRILTHVYPIRLVKVNEdtmEPLRdseglciPCQPGEPG-LLVGq 269
Cdd:cd17649 233 LKAPVRLFNA-YGPTEATVTPLVWKCEAGaARAGASMPIGRPLGGRSAYILD---ADLN-------PVPVGVTGeLYIG- 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 270 inqQDPLRRfdGYVSDSATNKK--IAHSVFRKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRL 347
Cdd:cd17649 301 ---GEGLAR--GYLGRPELTAErfVPDPFGAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEH 375
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907189430 348 LGQTDVAVygVAVPGVEGK---AGMAAIADPHSQLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQKTRL 420
Cdd:cd17649 376 PGVREAAV--VALDGAGGKqlvAYVVLRAAAAQPELRAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKAL 449
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
26-423 |
3.77e-05 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 45.91 E-value: 3.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 26 PESILPDTQLLDPMLAEAPTTPLAQAPGKGmDDRLFYIYTSGTTGLPKAAIVVHSRyyrIAAFGHHSYSMRAADVLYDC- 104
Cdd:PRK05677 177 PAYHLPQAVKFNDALAKGAGQPVTEANPQA-DDVAVLQYTGGTTGVAKGAMLTHRN---LVANMLQCRALMGSNLNEGCe 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 105 -----LPLYH------SAGNIMGVGQCVIY--------GLTVVLRK-KFSAsrFwddcVKYNCTVVQyigeICRyllRQP 164
Cdd:PRK05677 253 iliapLPLYHiyaftfHCMAMMLIGNHNILisnprdlpAMVKELGKwKFSG--F----VGLNTLFVA----LCN---NEA 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 165 VRDVE-QRHRVRLAVGNGLRPAIWEEFTQRFGVPqIGEFYGATECN--CSIANMDG-KVGSCGFNsrilthvYPIRLVKV 240
Cdd:PRK05677 320 FRKLDfSALKLTLSGGMALQLATAERWKEVTGCA-ICEGYGMTETSpvVSVNPSQAiQVGTIGIP-------VPSTLCKV 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 241 NEDTME--PLRDSEGLCIPcqpgEPGLLVGQINQQDplrrfdgyvsdsATNKKIAHSVFRKgdsaylSGDVLVMDELGYM 318
Cdd:PRK05677 392 IDDDGNelPLGEVGELCVK----GPQVMKGYWQRPE------------ATDEILDSDGWLK------TGDIALIQEDGYM 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 319 YFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAvpgvEGKAGMA----AIADPHSQLDPNSMYQELQKVLAS 394
Cdd:PRK05677 450 RIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVP----DEKSGEAikvfVVVKPGETLTKEQVMEHMRANLTG 525
|
410 420
....*....|....*....|....*....
gi 1907189430 395 YARPIFLRLLPQVDTTGTFKIQKTRLQRE 423
Cdd:PRK05677 526 YKVPKAVEFRDELPTTNVGKILRRELRDE 554
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
64-357 |
4.15e-05 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.
Pssm-ID: 213283 [Multi-domain] Cd Length: 509 Bit Score: 45.88 E-value: 4.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 64 YTSGTTGLPKAAIVVH-SRYYRIAAFGHHSYSMRAADVLYDC-LPLYHSAGnimgvgQCVIY------GLTVVLRKKFSA 135
Cdd:cd05915 160 YTTGTTGLPKGVVYSHrALVLHSLAASLVDGTALSEKDVVLPvVPMFHVNA------WCLPYaatlvgAKQVLPGPRLDP 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 136 SRFWDDCVKYNCTvvQYIGEICRYLLRQPVRDVEQRH---RVRLAVGNGLRPAIWEEFtQRFGVPQIGEFYGATEcncsi 212
Cdd:cd05915 234 ASLVELFDGEGVT--FTAGVPTVWLALADYLESTGHRlktLRRLVVGGSAAPRSLIAR-FERMGVEVRQGYGLTE----- 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 213 anMDGKVGSCGFNSRILTHVYPIRLVKVNEDTMEPLRDSEGLCIPCQPGEPGllVGQINQQDPLRR---FDGYVSDSATN 289
Cdd:cd05915 306 --TSPVVVQNFVKSHLESLSEEEKLTLKAKTGLPIPLVRLRVADEEGRPVPK--DGKALGEVQLKGpwiTGGYYGNEEAT 381
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907189430 290 KKIAhsvFRKGdsAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYG 357
Cdd:cd05915 382 RSAL---TPDG--FFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVA 444
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
2-154 |
4.35e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 45.65 E-value: 4.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 2 AAAVAEVSEQLGKSLLKFCSGDLGPESILPDTQLLDPMLAEAPTTPLaqaPGKGMDDRLFYIYTSGTTGLPKAAIVVHSR 81
Cdd:PRK07798 111 APRVAEVLPRLPKLRTLVVVEDGSGNDLLPGAVDYEDALAAGSPERD---FGERSPDDLYLLYTGGTTGMPKGVMWRQED 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 82 YYRiAAFG------------HHSYSMRAAD----VLYDCLPLYHSAGnIMGVGQCVIYGLTVVL--RKKFSASRFWDDCV 143
Cdd:PRK07798 188 IFR-VLLGgrdfatgepiedEEELAKRAAAgpgmRRFPAPPLMHGAG-QWAAFAALFSGQTVVLlpDVRFDADEVWRTIE 265
|
170
....*....|.
gi 1907189430 144 KYNCTVVQYIG 154
Cdd:PRK07798 266 REKVNVITIVG 276
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
296-415 |
7.41e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 45.03 E-value: 7.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 296 VFRKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYgvavPGVEGKAG--MAAIA 373
Cdd:PRK08308 285 VVKMGDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVY----RGKDPVAGerVKAKV 360
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1907189430 374 DPHSQLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKI 415
Cdd:PRK08308 361 ISHEEIDPVQLREWCIQHLAPYQVPHEIESVTEIPKNANGKV 402
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
306-425 |
1.24e-04 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 44.31 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 306 SGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPGVEGKAGMAAIADPHSQLDPNSMY 385
Cdd:PRK07008 413 TGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLVVVKRPGAEVTREELL 492
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1907189430 386 QELQKVLASYARP---IFLRLLPQvdtTGTFKIQKTRLqREGF 425
Cdd:PRK07008 493 AFYEGKVAKWWIPddvVFVDAIPH---TATGKLQKLKL-REQF 531
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
43-112 |
1.31e-04 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 44.57 E-value: 1.31e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907189430 43 APTTPLAQAPGKGMDDRLFYIYTSGTTGLPKAAIVVH----SRYYRIAA---FGhhsysmrAADVLYDCLPLYHSAG 112
Cdd:PRK06814 779 AGRFPLVYFCNRDPDDPAVILFTSGSEGTPKGVVLSHrnllANRAQVAAridFS-------PEDKVFNALPVFHSFG 848
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
41-420 |
2.63e-04 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 43.79 E-value: 2.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 41 AEAPTTPLaqapgkgMDDRLFY-IYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADVLYDCLPlYHSAGNIMGVGQ 119
Cdd:PRK12316 4684 AHDPAVRL-------HPDNLAYvIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMS-FSFDGSHEGLYH 4755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 120 CVIYGLTVVLRKkfsaSRFWD------DCVKYNCTVVQYIGEICRYLLRQPVRDVE-QRHRVRLAVGNGLRPAIWEEFTQ 192
Cdd:PRK12316 4756 PLINGASVVIRD----DSLWDperlyaEIHEHRVTVLVFPPVYLQQLAEHAERDGEpPSLRVYCFGGEAVAQASYDLAWR 4831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 193 RFGVPQIGEFYGATECNCSIANMDGKVGS-CGFNSRILTHVYPIRLVKVNEDTMEPLrdseglciPC-QPGEpgLLVGqi 270
Cdd:PRK12316 4832 ALKPVYLFNGYGPTETTVTVLLWKARDGDaCGAAYMPIGTPLGNRSGYVLDGQLNPL--------PVgVAGE--LYLG-- 4899
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 271 nqQDPLRRfdGYVSDSA-TNKKIAHSVFRK-GDSAYLSGDVL------VMDELGymyfrdRSGDTFRWRGENVSTTEVEA 342
Cdd:PRK12316 4900 --GEGVAR--GYLERPAlTAERFVPDPFGApGGRLYRTGDLAryradgVIDYLG------RVDHQVKIRGFRIELGEIEA 4969
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 343 vlsRLLGQTDV--AVYgVAVPGVEGK--AGMAAIADPHSQLDP-------NSMYQELQKVLASYARPIFLRLLPQVDTTG 411
Cdd:PRK12316 4970 ---RLREHPAVreAVV-IAQEGAVGKqlVGYVVPQDPALADADeaqaelrDELKAALRERLPEYMVPAHLVFLARMPLTP 5045
|
....*....
gi 1907189430 412 TFKIQKTRL 420
Cdd:PRK12316 5046 NGKLDRKAL 5054
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
63-127 |
2.71e-04 |
|
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: 43.50 E-value: 2.71e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907189430 63 IYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADVLYDC----LPLYHSAGNIMGVGQCVIYGLTV 127
Cdd:cd05933 156 IYTSGTTGMPKGVMLSHDNITWTAKAASQHMDLRPATVGQESvvsyLPLSHIAAQILDIWLPIKVGGQV 224
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
64-128 |
2.97e-04 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 43.26 E-value: 2.97e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907189430 64 YTSGTTGLPKAAIVVHsryYRIAAFGHH-SYSMR--AADVLYDCLPLYHSAGNIMGVGQCVIYGLTVV 128
Cdd:PRK08315 206 YTSGTTGFPKGATLTH---RNILNNGYFiGEAMKltEEDRLCIPVPLYHCFGMVLGNLACVTHGATMV 270
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
30-208 |
3.32e-04 |
|
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: 43.31 E-value: 3.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 30 LPDTQL----LD-PMLAEAPTTPLAQAPGkgmDDRLFY-IYTSGTTGLPKAAIVVH----------SRYY------RIAA 87
Cdd:COG1020 587 LPELGVpvlaLDaLALAAEPATNPPVPVT---PDDLAYvIYTSGSTGRPKGVMVEHralvnllawmQRRYglgpgdRVLQ 663
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 88 FghHSYSmraADVlydclplyhSAGNIMGvgqCVIYGLTVVLRKK---FSASRFWDDCVKYNCTVVQ----YIGEICRYL 160
Cdd:COG1020 664 F--ASLS---FDA---------SVWEIFG---ALLSGATLVLAPPearRDPAALAELLARHRVTVLNltpsLLRALLDAA 726
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1907189430 161 LRQPvrdveqrHRVRLAV--GNGLRPAIWEEFTQRFGVPQIGEFYGATEC 208
Cdd:COG1020 727 PEAL-------PSLRLVLvgGEALPPELVRRWRARLPGARLVNLYGPTET 769
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
306-425 |
4.04e-04 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 42.82 E-value: 4.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 306 SGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVE--AVlsrllGQTDV---AVYGVAVPGVEGKAGMAAIADPHSQLD 380
Cdd:PRK06018 414 TGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLEnlAV-----GHPKVaeaAVIGVYHPKWDERPLLIVQLKPGETAT 488
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1907189430 381 PNSMYQELQKVLASYARP---IFLRLLPQvdtTGTFKIQKTRLqREGF 425
Cdd:PRK06018 489 REEILKYMDGKIAKWWMPddvAFVDAIPH---TATGKILKTAL-REQF 532
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
35-229 |
4.15e-04 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 42.78 E-value: 4.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 35 LLDPMLAEAPTTPlaqapgkgmDDRLFYIYTSGTTGLPKAaiVVHS---------RYYRIAAFGHHSYSMRAadvlydcL 105
Cdd:PRK08043 352 LLMPRLAQVKQQP---------EDAALILFTSGSEGHPKG--VVHShksllanveQIKTIADFTPNDRFMSA-------L 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 106 PLYHSAGNIMGVGQCVIYGLTVVLRKKFSASRFWDDCVkY--NCTVV----QYIGEICRYllRQPVrdveQRHRVRLAVG 179
Cdd:PRK08043 414 PLFHSFGLTVGLFTPLLTGAEVFLYPSPLHYRIVPELV-YdrNCTVLfgtsTFLGNYARF--ANPY----DFARLRYVVA 486
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907189430 180 NGLRPA-----IWEEftqRFGVpQIGEFYGATECNCSIA---NMDGKVGSCGfnsRIL 229
Cdd:PRK08043 487 GAEKLQestkqLWQD---KFGL-RILEGYGVTECAPVVSinvPMAAKPGTVG---RIL 537
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
23-80 |
2.72e-03 |
|
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: 39.97 E-value: 2.72e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907189430 23 DLGPESILPDTQLLDPMLAEAPTTPLAQAPGKG---------MDDRLFY-IYTSGTTGLPKAAIVVHS 80
Cdd:cd12116 82 DAEPALVLTDDALPDRLPAGLPVLLLALAAAAAapaaprtpvSPDDLAYvIYTSGSTGRPKGVVVSHR 149
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
304-423 |
2.73e-03 |
|
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: 40.13 E-value: 2.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 304 YLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVygVAVP----GvEgKAGMAAIADPHSqL 379
Cdd:COG1021 411 YRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAV--VAMPdeylG-E-RSCAFVVPRGEP-L 485
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1907189430 380 DPNSMYQELQ-KVLASYARPIFLRLLPQVDTTGTFKIQKTRLQRE 423
Cdd:COG1021 486 TLAELRRFLReRGLAAFKLPDRLEFVDALPLTAVGKIDKKALRAA 530
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
58-109 |
2.99e-03 |
|
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: 39.89 E-value: 2.99e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907189430 58 DRLFYI-YTSGTTGLPKAAIVVH----SRYYRIAAFGHHSYSMRAADVLYDCLPLYH 109
Cdd:cd05927 114 EDLATIcYTSGTTGNPKGVMLTHgnivSNVAGVFKILEILNKINPTDVYISYLPLAH 170
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
281-344 |
3.86e-03 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 39.83 E-value: 3.86e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907189430 281 GYVSDSATNKKiahsVFRKGdsAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVL 344
Cdd:PLN02479 415 GYLKNPKANEE----AFANG--WFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVV 472
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
35-114 |
4.22e-03 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 39.59 E-value: 4.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189430 35 LLDPMLAEAPTTPlaqaPGKGMDDRLFYIYTSGTTGLPKAAIVVHSR-YYRIAAfghhsysMRAA-------DVLYDCLP 106
Cdd:PRK07768 134 TVADLLAADPIDP----VETGEDDLALMQLTSGSTGSPKAVQITHGNlYANAEA-------MFVAaefdvetDVMVSWLP 202
|
....*...
gi 1907189430 107 LYHSAGNI 114
Cdd:PRK07768 203 LFHDMGMV 210
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
57-109 |
9.71e-03 |
|
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: 38.35 E-value: 9.71e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1907189430 57 DDRLFYIYTSGTTGLPKAAIVVHSRYYR-IAAFGHHSYS-MRAADVLYDCLPLYH 109
Cdd:cd17639 88 DDLACIMYTSGSTGNPKGVMLTHGNLVAgIAGLGDRVPElLGPDDRYLAYLPLAH 142
|
|
| |
