|
Name |
Accession |
Description |
Interval |
E-value |
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
99-608 |
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: 963.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 99 DTHWTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALLHCLTTSRARALV 178
Cdd:cd05939 1 DRHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 179 FgsemasaicevhasldpslslfcsgswepgavppstEHLDPLLKDAPKHLPSCPDKGFTDKLFYIYTSGTTGLPKAAIV 258
Cdd:cd05939 81 F------------------------------------NLLDPLLTQSSTEPPSQDDVNFRDKLFYIYTSGTTGLPKAAVI 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 259 VHSRYYRMAALVYYGFRMRPNDIVYDCLPLYHSAGNIVGIGQCLLHGMTVVIRKKFSASRFWDDCIKYNCTIVQYIGELC 338
Cdd:cd05939 125 VHSRYYRIAAGAYYAFGMRPEDVVYDCLPLYHSAGGIMGVGQALLHGSTVVIRKKFSASNFWDDCVKYNCTIVQYIGEIC 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 339 RYLLNQPPREAENQHQVRMALGNGLRQSIWTNFSSRFHIPQVAEFYGATECNCSLGNFDSQVGACGFNSRILSFVYPIRL 418
Cdd:cd05939 205 RYLLAQPPSEEEQKHNVRLAVGNGLRPQIWEQFVRRFGIPQIGEFYGATEGNSSLVNIDNHVGACGFNSRILPSVYPIRL 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 419 VRVNEDTMELIRGPDGVCIPCQPGEPGQLVGRIIQKDPLRRFDGYLNQGANNKKIAKDVFKKGDQAYLTGDVLVMDELGY 498
Cdd:cd05939 285 IKVDEDTGELIRDSDGLCIPCQPGEPGLLVGKIIQNDPLRRFDGYVNEGATNKKIARDVFKKGDSAFLSGDVLVMDELGY 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 499 LYFRDRTGDTFRWKGENVSTTEVEGTLSRLLDMADVAVYGVEVPGTEGRAGMAAVASPTGNCDLERFAQVLEKELPLYAR 578
Cdd:cd05939 365 LYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVYGVEVPGVEGRAGMAAIVDPERKVDLDRFSAVLAKSLPPYAR 444
|
490 500 510
....*....|....*....|....*....|
gi 40807357 579 PIFLRLLPELHKTGTYKFQKTELRKEGFDP 608
Cdd:cd05939 445 PQFIRLLPEVDKTGTFKLQKTDLQKEGYDP 474
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
73-643 |
0e+00 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 710.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 73 RRTVPILFASTVRRHPDKTALIFEgtDTHWTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGVE 152
Cdd:PRK08279 36 KRSLGDVFEEAAARHPDRPALLFE--DQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 153 AALINTNLRRDALLHCLTTSRARALVFGSEMASAICEVHASLDPSLSLFCSGSwEPGAVPPSTEHLDPLLKDAPKHLP-S 231
Cdd:PRK08279 114 VALLNTQQRGAVLAHSLNLVDAKHLIVGEELVEAFEEARADLARPPRLWVAGG-DTLDDPEGYEDLAAAAAGAPTTNPaS 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 232 CPDKGFTDKLFYIYTSGTTGLPKAAIVVHSRYYRMAAlvyyGF----RMRPNDIVYDCLPLYHSAGNIVGIGQCLLHGMT 307
Cdd:PRK08279 193 RSGVTAKDTAFYIYTSGTTGLPKAAVMSHMRWLKAMG----GFggllRLTPDDVLYCCLPLYHNTGGTVAWSSVLAAGAT 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 308 VVIRKKFSASRFWDDCIKYNCTIVQYIGELCRYLLNQPPREAENQHQVRMALGNGLRQSIWTNFSSRFHIPQVAEFYGAT 387
Cdd:PRK08279 269 LALRRKFSASRFWDDVRRYRATAFQYIGELCRYLLNQPPKPTDRDHRLRLMIGNGLRPDIWDEFQQRFGIPRILEFYAAS 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 388 ECNCSLGNFDSQVGACGFNSRILSfvYPIRLVRVNEDTMELIRGPDGVCIPCQPGEPGQLVGRIIQKdplRRFDGYLNQG 467
Cdd:PRK08279 349 EGNVGFINVFNFDGTVGRVPLWLA--HPYAIVKYDVDTGEPVRDADGRCIKVKPGEVGLLIGRITDR---GPFDGYTDPE 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 468 ANNKKIAKDVFKKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLDMADVAVYGVEVPGTEGR 547
Cdd:PRK08279 424 ASEKKILRDVFKKGDAWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVATTEVENALSGFPGVEEAVVYGVEVPGTDGR 503
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 548 AGMAA-VASPTGNCDLERFAQVLEKELPLYARPIFLRLLPELHKTGTYKFQKTELRKEGFDPAIVKDPLFYLDAQKGRYV 626
Cdd:PRK08279 504 AGMAAiVLADGAEFDLAALAAHLYERLPAYAVPLFVRLVPELETTGTFKYRKVDLRKEGFDPSKVDDPLYVLDPGSGGYV 583
|
570
....*....|....*..
gi 40807357 627 PLDQEAYSRIQAGEEKL 643
Cdd:PRK08279 584 PLTAELYAEIAAGKFRL 600
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
99-608 |
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: 699.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 99 DTHWTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALLHCLTTSRARALV 178
Cdd:cd05940 1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 179 FgsemasaicevhasldpslslfcsgswepgavppstehldpllkdapkhlpscpdkgftDKLFYIYTSGTTGLPKAAIV 258
Cdd:cd05940 81 V-----------------------------------------------------------DAALYIYTSGTTGLPKAAII 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 259 VHSRYYRMAALVYYGFRMRPNDIVYDCLPLYHSAGNIVGIGQCLLHGMTVVIRKKFSASRFWDDCIKYNCTIVQYIGELC 338
Cdd:cd05940 102 SHRRAWRGGAFFAGSGGALPSDVLYTCLPLYHSTALIVGWSACLASGATLVIRKKFSASNFWDDIRKYQATIFQYIGELC 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 339 RYLLNQPPREAENQHQVRMALGNGLRQSIWTNFSSRFHIPQVAEFYGATECNCSLGNFDSQVGACGFNSRILSFVYPIRL 418
Cdd:cd05940 182 RYLLNQPPKPTERKHKVRMIFGNGLRPDIWEEFKERFGVPRIAEFYAATEGNSGFINFFGKPGAIGRNPSLLRKVAPLAL 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 419 VRVNEDTMELIRGPDGVCIPCQPGEPGQLVGRIIqkdPLRRFDGYLNQGANNKKIAKDVFKKGDQAYLTGDVLVMDELGY 498
Cdd:cd05940 262 VKYDLESGEPIRDAEGRCIKVPRGEPGLLISRIN---PLEPFDGYTDPAATEKKILRDVFKKGDAWFNTGDLMRLDGEGF 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 499 LYFRDRTGDTFRWKGENVSTTEVEGTLSRLLDMADVAVYGVEVPGTEGRAGMAAVA-SPTGNCDLERFAQVLEKELPLYA 577
Cdd:cd05940 339 WYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQVPGTDGRAGMAAIVlQPNEEFDLSALAAHLEKNLPGYA 418
|
490 500 510
....*....|....*....|....*....|.
gi 40807357 578 RPIFLRLLPELHKTGTYKFQKTELRKEGFDP 608
Cdd:cd05940 419 RPLFLRLQPEMEITGTFKQQKVDLRNEGFDP 449
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
103-633 |
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: 583.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 103 TFRQLDEYSSSVAN-FLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALLHCLTTSRARALVFGS 181
Cdd:cd05938 7 TYRDVDRRSNQAARaLLAHAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAKVLVVAP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 182 EMASAICEVHASL-DPSLSLFCSGswePGAVPPSTEHLDPLLKDA-----PKHLPSCPDkgFTDKLFYIYTSGTTGLPKA 255
Cdd:cd05938 87 ELQEAVEEVLPALrADGVSVWYLS---HTSNTEGVISLLDKVDAAsdepvPASLRAHVT--IKSPALYIYTSGTTGLPKA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 256 AIVVHSRYYRMAAlVYYGFRMRPNDIVYDCLPLYHSAGNIVGIGQCLLHGMTVVIRKKFSASRFWDDCIKYNCTIVQYIG 335
Cdd:cd05938 162 ARISHLRVLQCSG-FLSLCGVTADDVIYITLPLYHSSGFLLGIGGCIELGATCVLKPKFSASQFWDDCRKHNVTVIQYIG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 336 ELCRYLLNQPPREAENQHQVRMALGNGLRQSIWTNFSSRFHIPQVAEFYGATECNCSLGNFDSQVGACGFNSRILSFVYP 415
Cdd:cd05938 241 ELLRYLCNQPQSPNDRDHKVRLAIGNGLRADVWREFLRRFGPIRIREFYGSTEGNIGFFNYTGKIGAVGRVSYLYKLLFP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 416 IRLVRVNEDTMELIRGPDGVCIPCQPGEPGQLVGRIIQKDPlrrFDGYL-NQGANNKKIAKDVFKKGDQAYLTGDVLVMD 494
Cdd:cd05938 321 FELIKFDVEKEEPVRDAQGFCIPVAKGEPGLLVAKITQQSP---FLGYAgDKEQTEKKLLRDVFKKGDVYFNTGDLLVQD 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 495 ELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLDMADVAVYGVEVPGTEGRAGMAAVA-SPTGNCDLERFAQVLEKEL 573
Cdd:cd05938 398 QQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVYGVTVPGHEGRIGMAAVKlKPGHEFDGKKLYQHVREYL 477
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 574 PLYARPIFLRLLPELHKTGTYKFQKTELRKEGFDPAIVKDPLFYLDAQKGRYVPLDQEAY 633
Cdd:cd05938 478 PAYARPRFLRIQDSLEITGTFKQQKVRLVEEGFNPSIISDPLYFLDETQKTYVPLTPDIY 537
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
102-608 |
1.51e-152 |
|
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: 448.42 E-value: 1.51e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 102 WTFRQLDEYSSSVANFLQ-ARGLASGDVAAIFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALLHCLTTSRARALVfg 180
Cdd:cd05937 6 WTYSETYDLVLRYAHWLHdDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLSGSRFVI-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 181 semasaicevhasldpslslfcsgswepgavppstehLDPllkDAPKHLpscpdkgftdklfyIYTSGTTGLPKAAIVVH 260
Cdd:cd05937 84 -------------------------------------VDP---DDPAIL--------------IYTSGTTGLPKAAAISW 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 261 SRYYRMAALVYYGFRMRPNDIVYDCLPLYHSAGNIVGIGQCLLHGMTVVIRKKFSASRFWDDCIKYNCTIVQYIGELCRY 340
Cdd:cd05937 110 RRTLVTSNLLSHDLNLKNGDRTYTCMPLYHGTAAFLGACNCLMSGGTLALSRKFSASQFWKDVRDSGATIIQYVGELCRY 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 341 LLNQPPREAENQHQVRMALGNGLRQSIWTNFSSRFHIPQVAEFYGATECNCSLGNFDS---QVGACGFNSRILSFVY--P 415
Cdd:cd05937 190 LLSTPPSPYDRDHKVRVAWGNGLRPDIWERFRERFNVPEIGEFYAATEGVFALTNHNVgdfGAGAIGHHGLIRRWKFenQ 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 416 IRLVRVNEDTMELIRGP-DGVCIPCQPGEPGQLVGRiIQKDPLRRFDGYL-NQGANNKKIAKDVFKKGDQAYLTGDVLVM 493
Cdd:cd05937 270 VVLVKMDPETDDPIRDPkTGFCVRAPVGEPGEMLGR-VPFKNREAFQGYLhNEDATESKLVRDVFRKGDIYFRTGDLLRQ 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 494 DELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLDMADVAVYGVEVPGTEGRAGMAAV-----ASPTGNCDLERFAQV 568
Cdd:cd05937 349 DADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGVKVPGHDGRAGCAAItleesSAVPTEFTKSLLASL 428
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 40807357 569 LEKELPLYARPIFLRLLPELHKTGTYKFQKTELRKEGFDP 608
Cdd:cd05937 429 ARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVLRDEGVDP 468
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
79-604 |
3.94e-93 |
|
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: 294.80 E-value: 3.94e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 79 LFASTVRRHPDKTALIFEGTdtHWTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGVEAALINT 158
Cdd:COG0318 4 LLRRAAARHPDRPALVFGGR--RLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 159 NLRRDALLHCLTTSRARALVFgsemasaicevhasldpslslfcsgswepgavppstehldpllkdapkhlpscpdkgft 238
Cdd:COG0318 82 RLTAEELAYILEDSGARALVT----------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 239 dkLFYIYTSGTTGLPKAAIVVHSRYYRMAALVYYGFRMRPNDIVYDCLPLYHSAGNIVGIGQCLLHGMTVVIRKKFSASR 318
Cdd:COG0318 103 --ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLPRFDPER 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 319 FWDDCIKYNCTIVQYIGELCRYLLNQPPREAENQHQVRMAL--GNGLRQSIWTNFSSRFHIPqVAEFYGATECN--CSLG 394
Cdd:COG0318 181 VLELIERERVTVLFGVPTMLARLLRHPEFARYDLSSLRLVVsgGAPLPPELLERFEERFGVR-IVEGYGLTETSpvVTVN 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 395 NFDSQ---VGACGFnsrilsfvyPIRLVRVnedtmeLIRGPDGvcIPCQPGEPGQLVGR---IiqkdplrrFDGYLNQGA 468
Cdd:COG0318 260 PEDPGerrPGSVGR---------PLPGVEV------RIVDEDG--RELPPGEVGEIVVRgpnV--------MKGYWNDPE 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 469 NNKKiakdVFKKGdqAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLDMADVAVYGVEVPGTeGRA 548
Cdd:COG0318 315 ATAE----AFRDG--WLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKW-GER 387
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 40807357 549 GMAAV-ASPTGNCDLERFAQVLEKELPLYARPIFLRLLPELHKTGTYKFQKTELRKE 604
Cdd:COG0318 388 VVAFVvLRPGAELDAEELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRER 444
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
74-609 |
4.27e-88 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 284.73 E-value: 4.27e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 74 RTVPILFASTVRRHPDKTALIFEGTdtHWTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGVEA 153
Cdd:PRK06155 21 RTLPAMLARQAERYPDRPLLVFGGT--RWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 154 ALINTNLRRDALLHCLTTSRARALVFGSEMASAICEVHASLDPSLSLFCSGSWEPGAVPP--STEHLDPLLKDAPkhlps 231
Cdd:PRK06155 99 VPINTALRGPQLEHILRNSGARLLVVEAALLAALEAADPGDLPLPAVWLLDAPASVSVPAgwSTAPLPPLDAPAP----- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 232 CPDKGFTDKLFYIYTSGTTGLPKAAIVVHSRYYRMAALVYYGFRMRPNDIVYDCLPLYHS-AGNivGIGQCLLHGMTVVI 310
Cdd:PRK06155 174 AAAVQPGDTAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADDVLYTTLPLFHTnALN--AFFQALLAGATYVL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 311 RKKFSASRFWDDCIKYNCTIVQYIGELCRYLLNQPPREAENQHQVRMALGNGLRQSIWTNFSSRFHIPqVAEFYGATECN 390
Cdd:PRK06155 252 EPRFSASGFWPAVRRHGATVTYLLGAMVSILLSQPARESDRAHRVRVALGPGVPAALHAAFRERFGVD-LLDGYGSTETN 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 391 CSLG-NFDSQVG------ACGFNSRIlsfvypirlvrVNEDTMELirgpdgvcipcQPGEPGQLVGRiiQKDPLRRFDGY 463
Cdd:PRK06155 331 FVIAvTHGSQRPgsmgrlAPGFEARV-----------VDEHDQEL-----------PDGEPGELLLR--ADEPFAFATGY 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 464 LNQGANNKKIAKDVFkkgdqaYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLDMADVAVYGVEVPG 543
Cdd:PRK06155 387 FGMPEKTVEAWRNLW------FHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSEL 460
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 544 TEGRAgMAAVASPTGNC----DLERFAqvlEKELPLYARPIFLRLLPELHKTGTYKFQKTELRKEGFDPA 609
Cdd:PRK06155 461 GEDEV-MAAVVLRDGTAlepvALVRHC---EPRLAYFAVPRYVEFVAALPKTENGKVQKFVLREQGVTAD 526
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
99-602 |
9.51e-83 |
|
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: 266.85 E-value: 9.51e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 99 DTHWTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALLHCLTTSRARALV 178
Cdd:cd05934 1 GRRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 179 fgsemasaicevhasldpslslfcsgswepgavppstehldpllkdapkhlpscpdkgfTDKLFYIYTSGTTGLPKAAIV 258
Cdd:cd05934 81 -----------------------------------------------------------VDPASILYTSGTTGPPKGVVI 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 259 VHSRYYRMAALVYYGFRMRPNDIVYDCLPLYHSAGNIVGIGQCLLHGMTVVIRKKFSASRFWDDCIKYNCTIVQYIGELC 338
Cdd:cd05934 102 THANLTFAGYYSARRFGLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLLPRFSASRFWSDVRRYGATVTNYLGAML 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 339 RYLLNQPPREAENQHQVRMALGNGLRQSIWTNFSSRFHIPqVAEFYGATECNCSLgnfdsqVGACGFNSRILSFVYPIRL 418
Cdd:cd05934 182 SYLLAQPPSPDDRAHRLRAAYGAPNPPELHEEFEERFGVR-LLEGYGMTETIVGV------IGPRDEPRRPGSIGRPAPG 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 419 VRVnedtmeLIRGPDGVciPCQPGEPGQLVGRIIQkdPLRRFDGYLNQGANNKKIAKDVFkkgdqaYLTGDVLVMDELGY 498
Cdd:cd05934 255 YEV------RIVDDDGQ--ELPAGEPGELVIRGLR--GWGFFKGYYNMPEATAEAMRNGW------FHTGDLGYRDADGF 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 499 LYFRDRTGDTFRWKGENVSTTEVEGTLSRLLDMADVAVYGVEVPGTEGRAGMAAVASPTGNCDLERFAQVLEKELPLYAR 578
Cdd:cd05934 319 FYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLDPEELFAFCEGQLAYFKV 398
|
490 500
....*....|....*....|....
gi 40807357 579 PIFLRLLPELHKTGTYKFQKTELR 602
Cdd:cd05934 399 PRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
80-512 |
3.12e-64 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 217.95 E-value: 3.12e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 80 FASTVRRHPDKTALIFeGTDTHWTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGVEAALINTN 159
Cdd:pfam00501 1 LERQAARTPDKTALEV-GEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 160 LRRDALLHCLTTSRARALVFGSE-MASAICEVHASLDPSLSLFCSGSWEPGAVPPSTEHLDPLLKDAPKHLPSCPDkgft 238
Cdd:pfam00501 80 LPAEELAYILEDSGAKVLITDDAlKLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVPPPPPPPPDPD---- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 239 DKLFYIYTSGTTGLPKAAIVVH----SRYYRMAALVYYGFRMRPNDIVYDCLPLYHSAGNIVGIGQCLLHGMTVVIRKKF 314
Cdd:pfam00501 156 DLAYIIYTSGTTGKPKGVMLTHrnlvANVLSIKRVRPRGFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVVLPPGF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 315 SA---SRFWDDCIKYNCTIVQYIGELCRYLLNQPPREAENQHQVRMAL--GNGLRQSIWTNFSSRFhIPQVAEFYGATEC 389
Cdd:pfam00501 236 PAldpAALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSSLRLVLsgGAPLPPELARRFRELF-GGALVNGYGLTET 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 390 NC------SLGNFDSQVGACGFnsrilsfvyPIRLVR---VNEDTMElirgpdgvciPCQPGEPGQLV--GRIIQKdplr 458
Cdd:pfam00501 315 TGvvttplPLDEDLRSLGSVGR---------PLPGTEvkiVDDETGE----------PVPPGEPGELCvrGPGVMK---- 371
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 40807357 459 rfdGYLNQ-GANNKKIAKDVFkkgdqaYLTGDVLVMDELGYLYFRDRTGDTFRWK 512
Cdd:pfam00501 372 ---GYLNDpELTAEAFDEDGW------YRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
241-597 |
3.46e-61 |
|
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: 207.14 E-value: 3.46e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 241 LFYIYTSGTTGLPKAAIVVHSRYYRMAALVYYGFRMRPNDIVYDCLPLYHSAGnIVGIGQCLLHGMTVVIRKKFSASRFW 320
Cdd:cd04433 3 ALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGG-LFGLLGALLAGGTVVLLPKFDPEAAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 321 DDCIKYNCTIVQYIGELCRYLLNQPPREAENQHQVRMALGNG--LRQSIWTNFSSRFHIPqVAEFYGATECNCSL----- 393
Cdd:cd04433 82 ELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGapLPPELLERFEEAPGIK-LVNGYGLTETGGTVatgpp 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 394 GNFDSQVGACGFnsrilsfvyPIRLVRVNedtmelIRGPDGvcIPCQPGEPGQLVGRIIQkdplrRFDGYLNQGANNKki 473
Cdd:cd04433 161 DDDARKPGSVGR---------PVPGVEVR------IVDPDG--GELPPGEIGELVVRGPS-----VMKGYWNNPEATA-- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 474 akdvFKKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLDMADVAVYGVEVPgTEGRAGMAAV 553
Cdd:cd04433 217 ----AVDEDGWYRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDP-EWGERVVAVV 291
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 40807357 554 -ASPTGNCDLERFAQVLEKELPLYARPIFLRLLPELHKTGTYKFQ 597
Cdd:cd04433 292 vLRPGADLDAEELRAHVRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
73-631 |
3.06e-56 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 199.14 E-value: 3.06e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 73 RRTVPILFAStvRRHPDKTALIFEgtDTHWTFRQLDEYSSSVANFLQARgLASGDVA--AIFMENRNEFvGLWLGMAKLG 150
Cdd:PRK07867 4 APTVAELLLP--LAEDDDRGLYFE--DSFTSWREHIRGSAARAAALRAR-LDPTRPPhvGVLLDNTPEF-SLLLGAAALS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 151 --VEAALINTN----LRRDALL-HC---LTTSRARALVFGSEMASAICEVHAsldpslslfcsgswepgavPPSTEHLDP 220
Cdd:PRK07867 78 giVPVGLNPTRrgaaLARDIAHaDCqlvLTESAHAELLDGLDPGVRVINVDS-------------------PAWADELAA 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 221 LLKDAPKHLPSCPDkgftDKLFYIYTSGTTGLPKAAIVVHSRYYRMAALVYYGFRMRPNDIVYDCLPLYHSAGNIVGIGQ 300
Cdd:PRK07867 139 HRDAEPPFRVADPD----DLFMLIFTSGTSGDPKAVRCTHRKVASAGVMLAQRFGLGPDDVCYVSMPLFHSNAVMAGWAV 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 301 CLLHGMTVVIRKKFSASRFWDDCIKYNCTIVQYIGELCRYLLNQPPREAENQHQVRMALGNGLRQSIWTNFSSRFHIpQV 380
Cdd:PRK07867 215 ALAAGASIALRRKFSASGFLPDVRRYGATYANYVGKPLSYVLATPERPDDADNPLRIVYGNEGAPGDIARFARRFGC-VV 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 381 AEFYGATECNCSLGNF-DSQVGACGfnsrilsfvypirlvrvnedtmeliRGPDGVCI-------PCQPGEPG------- 445
Cdd:PRK07867 294 VDGFGSTEGGVAITRTpDTPPGALG-------------------------PLPPGVAIvdpdtgtECPPAEDAdgrllna 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 446 -QLVGRIIQKDPLRRFDGYLN-QGANNKKIAKDVFKKGDQAYltgdvlvMDELGYLYFRDRTGDTFRWKGENVSTTEVEG 523
Cdd:PRK07867 349 dEAIGELVNTAGPGGFEGYYNdPEADAERMRGGVYWSGDLAY-------RDADGYAYFAGRLGDWMRVDGENLGTAPIER 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 524 TLSRLLDMADVAVYGVEVPgTEGRAGMAAVA-SPTGNCDLERFAQVL--EKELPLYARPIFLRLLPELHKTGTYKFQKTE 600
Cdd:PRK07867 422 ILLRYPDATEVAVYAVPDP-VVGDQVMAALVlAPGAKFDPDAFAEFLaaQPDLGPKQWPSYVRVCAELPRTATFKVLKRQ 500
|
570 580 590
....*....|....*....|....*....|..
gi 40807357 601 LRKEGFDPAivkDPLF-YLDAQKGRYVPLDQE 631
Cdd:PRK07867 501 LSAEGVDCA---DPVWwIRRLTPSDYAALADE 529
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
75-602 |
2.36e-54 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 193.86 E-value: 2.36e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 75 TVPILFASTVRRHPDKTALIFEGTDthWTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGVEAA 154
Cdd:PRK06187 7 TIGRILRHGARKHPDKEAVYFDGRR--TTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 155 LINTNLRRDALLHCLTTSRARALVFGSEMASAICEVHASLDPSLSLFCSGSWEPGAVPPSTEHLDPLLKDAPKHLPScPD 234
Cdd:PRK06187 85 PINIRLKPEEIAYILNDAEDRVVLVDSEFVPLLAAILPQLPTVRTVIVEGDGPAAPLAPEVGEYEELLAAASDTFDF-PD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 235 KGFTDKLFYIYTSGTTGLPKAAIVVHSRYYRMAALVYYGFRMRPNDIVYDCLPLYHSAGniVGIG-QCLLHGMTVVIRKK 313
Cdd:PRK06187 164 IDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVPMFHVHA--WGLPyLALMAGAKQVIPRR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 314 FSASRFWDDCIKYNCTIVQYIGELCRYLLNQPPREAENQHQVRMAL--GNGLRQSIWTNFSSRFHIpQVAEFYGATECnC 391
Cdd:PRK06187 242 FDPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYFVDFSSLRLVIygGAALPPALLREFKEKFGI-DLVQGYGMTET-S 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 392 SLGNF---DSQVGacGFNSRILSFVYPIRLVRVNedtmelIRGPDGVCIPCQPGEPGQLVGR---IIQkdplrrfdGYLN 465
Cdd:PRK06187 320 PVVSVlppEDQLP--GQWTKRRSAGRPLPGVEAR------IVDDDGDELPPDGGEVGEIIVRgpwLMQ--------GYWN 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 466 Q-GANNKKIAKDvfkkgdqAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLDMADVAVYGV----- 539
Cdd:PRK06187 384 RpEATAETIDGG-------WLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVpdekw 456
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 40807357 540 -EVPGT--EGRAGMAAVASptgncDLERFaqvLEKELPLYARPIFLRLLPELHKTGTYKFQKTELR 602
Cdd:PRK06187 457 gERPVAvvVLKPGATLDAK-----ELRAF---LRGRLAKFKLPKRIAFVDELPRTSVGKILKRVLR 514
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
84-639 |
9.80e-53 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 189.85 E-value: 9.80e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 84 VRRHPDKTALIFEGTDthWTFRQLDEYSSSVANFLqaRGLASGDV---AAIFMENRNEFVgLWLGMAKLGvEAAL--INT 158
Cdd:PRK13388 11 DRAGDDTIAVRYGDRT--WTWREVLAEAAARAAAL--IALADPDRplhVGVLLGNTPEML-FWLAAAALG-GYVLvgLNT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 159 NLRRDALLHCLTTSRARALVFGSEMASAIcevhASLD-PSLSLFCSGSWE-PGAVPPSTEhLDPLLKDAPKHLpscpdkg 236
Cdd:PRK13388 85 TRRGAALAADIRRADCQLLVTDAEHRPLL----DGLDlPGVRVLDVDTPAyAELVAAAGA-LTPHREVDAMDP------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 237 ftdkLFYIYTSGTTGLPKAAIVVHSRYYRMAALVYYGFRMRPNDIVYDCLPLYHSAGNIVGIGQCLLHGMTVVIRKKFSA 316
Cdd:PRK13388 153 ----FMLIFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLTRDDVCYVSMPLFHSNAVMAGWAPAVASGAAVALPAKFSA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 317 SRFWDDCIKYNCTIVQYIGELCRYLLNQPPREAENQHQVRMALGNGLRQSIWTNFSSRFHIpQVAEFYGATECNC----- 391
Cdd:PRK13388 229 SGFLDDVRRYGATYFNYVGKPLAYILATPERPDDADNPLRVAFGNEASPRDIAEFSRRFGC-QVEDGYGSSEGAVivvre 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 392 ------SLGnfdsqVGACGfnsrilsfvypirLVRVNEDTMElirgpdgVCIPCQPGEPGQL------VGRIIQKDPLRR 459
Cdd:PRK13388 308 pgtppgSIG-----RGAPG-------------VAIYNPETLT-------ECAVARFDAHGALlnadeaIGELVNTAGAGF 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 460 FDGYLN-QGANNKKIAKDVFKKGDQAYLtgdvlvmDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLDMADVAVYG 538
Cdd:PRK13388 363 FEGYYNnPEATAERMRHGMYWSGDLAYR-------DADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYA 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 539 VEVPGTeGRAGMAA-VASPTGNCDLERFAQVL--EKELPLYARPIFLRLLPELHKTGTYKFQKTELRKEGFDPAivkDPL 615
Cdd:PRK13388 436 VPDERV-GDQVMAAlVLRDGATFDPDAFAAFLaaQPDLGTKAWPRYVRIAADLPSTATNKVLKRELIAQGWATG---DPV 511
|
570 580
....*....|....*....|....*
gi 40807357 616 F-YLDAQKGRYVPLDQEAYSRIQAG 639
Cdd:PRK13388 512 TlWVRRGGPAYRLMSEPAKAALAAE 536
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
83-598 |
2.21e-49 |
|
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: 178.19 E-value: 2.21e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 83 TVRRHPDKTALIFEGTDthWTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGVEAALINTNLRR 162
Cdd:cd17631 4 RARRHPDRTALVFGGRS--LTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 163 DALLHCLTTSRARALVfgsemasaicevhasldpslslfcsgswepgavppstehldpllkdapkhlpscpdkgftDKLF 242
Cdd:cd17631 82 PEVAYILADSGAKVLF------------------------------------------------------------DDLA 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 243 YI-YTSGTTGLPKAAIVVHSRYYRMAALVYYGFRMRPNDIVYDCLPLYHSAGNIVGIGQCLLHGMTVVIRKKFSASRFWD 321
Cdd:cd17631 102 LLmYTSGTTGRPKGAMLTHRNLLWNAVNALAALDLGPDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVILRKFDPETVLD 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 322 DCIKYNCTIVQYIGELCRYLLNQPPREAENQHQVRMALGNG------LRQSIWtnfssRFHiPQVAEFYGATECN---CS 392
Cdd:cd17631 182 LIERHRVTSFFLVPTMIQALLQHPRFATTDLSSLRAVIYGGapmperLLRALQ-----ARG-VKFVQGYGMTETSpgvTF 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 393 LGNFDSQ--VGACGfnsrilsfvYPIRLVRVNedtmelIRGPDGVciPCQPGEPGQLVGRIIQkdplrRFDGYLNQGANN 470
Cdd:cd17631 256 LSPEDHRrkLGSAG---------RPVFFVEVR------IVDPDGR--EVPPGEVGEIVVRGPH-----VMAGYWNRPEAT 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 471 KKiakdVFKKGdqAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLDMADVAVYGVEVPgTEGRAGM 550
Cdd:cd17631 314 AA----AFRDG--WFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDE-KWGEAVV 386
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 40807357 551 AAVA-SPTGNCDLERFAQVLEKELPLYARPIFLRLLPELHKTGTYKFQK 598
Cdd:cd17631 387 AVVVpRPGAELDEDELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
98-553 |
3.19e-48 |
|
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: 176.25 E-value: 3.19e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 98 TDTHWTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALLHCLTTSRARAL 177
Cdd:cd05911 7 TGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 178 VFGSEMASAICEVHASLDPSLSLFCSGSWEPGAVPPSTEhLDPLLKDAPKHLPSCPDKGFTDKLFYIYTSGTTGLPKAAI 257
Cdd:cd05911 87 FTDPDGLEKVKEAAKELGPKDKIIVLDDKPDGVLSIEDL-LSPTLGEEDEDLPPPLKDGKDDTAAILYSSGTTGLPKGVC 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 258 VVHSRYYRMAALVYYGFR--MRPNDIVYDCLPLYHSAGnIVGIGQCLLHGMTVVIRKKFSASRFWDDCIKYNCTIVQYIG 335
Cdd:cd05911 166 LSHRNLIANLSQVQTFLYgnDGSNDVILGFLPLYHIYG-LFTTLASLLNGATVIIMPKFDSELFLDLIEKYKITFLYLVP 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 336 ELCRYLLNQPPREAENQHQVRMAL--GNGLRQSIWTNFSSRFHIPQVAEFYGATECNCSLG---NFDSQVGACGfnsRIL 410
Cdd:cd05911 245 PIAAALAKSPLLDKYDLSSLRVILsgGAPLSKELQELLAKRFPNATIKQGYGMTETGGILTvnpDGDDKPGSVG---RLL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 411 SFVypirLVR-VNEDTMELirgpdgvcipCQPGEPGQLVGRIIQKdplrrFDGYL-NQGANNKKIAKDVFkkgdqaYLTG 488
Cdd:cd05911 322 PNV----EAKiVDDDGKDS----------LGPNEPGEICVRGPQV-----MKGYYnNPEATKETFDEDGW------LHTG 376
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 40807357 489 DVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLDMADVAVYGVEVPgTEGRAGMAAV 553
Cdd:cd05911 377 DIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDE-VSGELPRAYV 440
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
79-602 |
1.08e-47 |
|
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: 174.29 E-value: 1.08e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 79 LFASTVRRHPDKTALIFEGTDthWTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGVEAALINT 158
Cdd:cd05936 4 LLEEAARRFPDKTALIFMGRK--LTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 159 NLRRDALLHCLTTSRARALVFGSEMASAIcevhasldpslslfcsgswEPGAVPPSTEHLDPllkdapkhlpscpdkgfT 238
Cdd:cd05936 82 LYTPRELEHILNDSGAKALIVAVSFTDLL-------------------AAGAPLGERVALTP-----------------E 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 239 DKLFYIYTSGTTGLPKAAIVVHSRYYR--MAALVYYGFRMRPNDIVYDCLPLYHSAGNIVGIGQCLLHGMTVVIRKKFSA 316
Cdd:cd05936 126 DVAVLQYTSGTTGVPKGAMLTHRNLVAnaLQIKAWLEDLLEGDDVVLAALPLFHVFGLTVALLLPLALGATIVLIPRFRP 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 317 SRFWDDCIKYNCTIVQ-----YIGelcryLLNQPPREAENQHQVRMALGNG--LRQSIWTNFSSRFHIPqVAEFYGATEC 389
Cdd:cd05936 206 IGVLKEIRKHRVTIFPgvptmYIA-----LLNAPEFKKRDFSSLRLCISGGapLPVEVAERFEELTGVP-IVEGYGLTET 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 390 ncslgnfdSQVGAC---GFNSRILSFVYPIRlvrvneDTMELIRGPDGVCIPcqPGEpgqlVGRIIQKDPlRRFDGYLNQ 466
Cdd:cd05936 280 --------SPVVAVnplDGPRKPGSIGIPLP------GTEVKIVDDDGEELP--PGE----VGELWVRGP-QVMKGYWNR 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 467 GANNKKiakdVFKKGdqAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLDMADVAVYGV--EVPGT 544
Cdd:cd05936 339 PEETAE----AFVDG--WLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVpdPYSGE 412
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 40807357 545 EGRAgmAAVASPTGNCDLERFAQVLEKELPLYARPIFLRLLPELHKTGTYKFQKTELR 602
Cdd:cd05936 413 AVKA--FVVLKEGASLTEEEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
84-603 |
1.51e-44 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 167.60 E-value: 1.51e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 84 VRRHPDKTALIFE---GTDTHWTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGVEAALINTNL 160
Cdd:COG0365 19 AEGRGDKVALIWEgedGEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPVFPGF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 161 RRDALLHCLTTSRARALV---------FGSEMASAICEVHASLDPSLSLFCSGSWEPGAVPPSTEHLDPLLKDAPKHLPs 231
Cdd:COG0365 99 GAEALADRIEDAEAKVLItadgglrggKVIDLKEKVDEALEELPSLEHVIVVGRTGADVPMEGDLDWDELLAAASAEFE- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 232 CPDKGFTDKLFYIYTSGTTGLPKAaiVVHS-RYYRMAALVY--YGFRMRPNDIVY---DClplyhsaGNIVGIGQC---- 301
Cdd:COG0365 178 PEPTDADDPLFILYTSGTTGKPKG--VVHThGGYLVHAATTakYVLDLKPGDVFWctaDI-------GWATGHSYIvygp 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 302 LLHGMTVVI---RKKF-SASRFWDDCIKYNCTIvqyigeLC------RYLLNQPPREAEnQH---QVRMALGNG--LRQS 366
Cdd:COG0365 249 LLNGATVVLyegRPDFpDPGRLWELIEKYGVTV------FFtaptaiRALMKAGDEPLK-KYdlsSLRLLGSAGepLNPE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 367 IWTNFSSRFHIPqVAEFYGATECNCSLGNF----DSQVGACGFnsrilsfvyPIRLVRVnedtmeLIRGPDGVciPCQPG 442
Cdd:COG0365 322 VWEWWYEAVGVP-IVDGWGQTETGGIFISNlpglPVKPGSMGK---------PVPGYDV------AVVDEDGN--PVPPG 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 443 EPGQLVgriIQKDPLRRFDGYLNqgaNNKKIAKDVFKKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVE 522
Cdd:COG0365 384 EEGELV---IKGPWPGMFRGYWN---DPERYRETYFGRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIE 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 523 GTLSRLLDMADVAVYGVEVPGTegraGMAAVA------SPTGNCDLER--FAQVlEKELPLYARPIFLRLLPELHKTGTY 594
Cdd:COG0365 458 SALVSHPAVAEAAVVGVPDEIR----GQVVKAfvvlkpGVEPSDELAKelQAHV-REELGPYAYPREIEFVDELPKTRSG 532
|
....*....
gi 40807357 595 KFQKTELRK 603
Cdd:COG0365 533 KIMRRLLRK 541
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
74-604 |
3.55e-44 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 165.46 E-value: 3.55e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 74 RTVPILFASTVRRHPDKTALIFEGTDThwTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGveA 153
Cdd:PRK07656 5 MTLPELLARAARRFGDKEAYVFGDQRL--TYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAG--A 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 154 ALI--NTNLRRDALLHCLTTSRARALVFGSEMASAICEVHASLdPSLSLFCSGSWEPGAVPPSTEH-LDPLLKDAPKHLP 230
Cdd:PRK07656 81 VVVplNTRYTADEAAYILARGDAKALFVLGLFLGVDYSATTRL-PALEHVVICETEEDDPHTEKMKtFTDFLAAGDPAER 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 231 SCPDKGfTDKLFYIYTSGTTGLPKAAIVVHSRYYRMAALVYYGFRMRPNDIVYDCLPLYHSAGNIVGIGQCLLHGMTVVI 310
Cdd:PRK07656 160 APEVDP-DDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLAANPFFHVFGYKAGVNAPLMRGATILP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 311 RKKFSASRFWDDCIKYNCTIVQYIGELCRYLLNQPPREAENQHQVRMALGNG--LRQSIWTNFSSRFHIPQVAEFYGATE 388
Cdd:PRK07656 239 LPVFDPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSAEDLSSLRLAVTGAasMPVALLERFESELGVDIVLTGYGLSE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 389 CN-----CSLGN-FDSQVGACGfnsrilsfvYPIRLVRVNedtmelIRGPDGVCIPcqPGEPGQLVGR---IIQ---KDP 456
Cdd:PRK07656 319 ASgvttfNRLDDdRKTVAGTIG---------TAIAGVENK------IVNELGEEVP--VGEVGELLVRgpnVMKgyyDDP 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 457 LR-----RFDGYLNqgannkkiakdvfkkgdqaylTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLDM 531
Cdd:PRK07656 382 EAtaaaiDADGWLH---------------------TGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAV 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 532 ADVAVYGVEVPGTeGRAGMAAVASPTGncdlerfAQVLEKELPLYAR--------PIFLRLLPELHKTGTYKFQKTELRK 603
Cdd:PRK07656 441 AEAAVIGVPDERL-GEVGKAYVVLKPG-------AELTEEELIAYCRehlakykvPRSIEFLDELPKNATGKVLKRALRE 512
|
.
gi 40807357 604 E 604
Cdd:PRK07656 513 K 513
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
73-604 |
1.01e-42 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 161.64 E-value: 1.01e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 73 RRTVPILFASTVRRHPDKTALIFEgtDTHWTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGVE 152
Cdd:PRK08316 10 RQTIGDILRRSARRYPDKTALVFG--DRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 153 AALINTNLRRDALLHCLTTSRARALVFGSEMASAIcEVHASLDPSLSLFCSGSWEPGAVPPSTEHLDPLLKDAPKHLPSc 232
Cdd:PRK08316 88 HVPVNFMLTGEELAYILDHSGARAFLVDPALAPTA-EAALALLPVDTLILSLVLGGREAPGGWLDFADWAEAGSVAEPD- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 233 PDKGFTDKLFYIYTSGTTGLPKAAIVVHSryyrmaALV--YYG----FRMRPNDIVYDCLPLYHSAGNIVGIGQCLLHGM 306
Cdd:PRK08316 166 VELADDDLAQILYTSGTESLPKGAMLTHR------ALIaeYVScivaGDMSADDIPLHALPLYHCAQLDVFLGPYLYVGA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 307 TVVIRKKFSASRFWDDCIKYNCTI------VqYIGelcryLLNQPPREAENQHQVR----------MALGNGLRQsiwtn 370
Cdd:PRK08316 240 TNVILDAPDPELILRTIEAERITSffapptV-WIS-----LLRHPDFDTRDLSSLRkgyygasimpVEVLKELRE----- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 371 fssrfHIPQVA--EFYGATEC---NCSLG--NFDSQVGACGfnsRILSFVYpirlVRVNEDTMElirgpdgvciPCQPGE 443
Cdd:PRK08316 309 -----RLPGLRfyNCYGQTEIaplATVLGpeEHLRRPGSAG---RPVLNVE----TRVVDDDGN----------DVAPGE 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 444 PGQLVGRIIQKdplrrFDGYLNQGAnnkKIAkDVFKKGdqAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEG 523
Cdd:PRK08316 367 VGEIVHRSPQL-----MLGYWDDPE---KTA-EAFRGG--WFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEE 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 524 TLSRLLDMADVAVYGVEVPgtegRAGMA--AVASPTGNCDLERfAQVLE---KELPLYARPIFLRLLPELHKTGTYKFQK 598
Cdd:PRK08316 436 ALYTHPAVAEVAVIGLPDP----KWIEAvtAVVVPKAGATVTE-DELIAhcrARLAGFKVPKRVIFVDELPRNPSGKILK 510
|
....*.
gi 40807357 599 TELRKE 604
Cdd:PRK08316 511 RELRER 516
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
88-603 |
1.57e-42 |
|
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: 160.56 E-value: 1.57e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 88 PDKTALIFEGTDTHWTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALLH 167
Cdd:cd05926 1 PDAPALVVPGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 168 CLTTSRARALV-----FGSEMASAICEVHASLDPSlslFCSGSwepGAVPPSTEHLDPLLKDAPKHLPSCPDKGfTDKLF 242
Cdd:cd05926 81 YLADLGSKLVLtpkgeLGPASRAASKLGLAILELA---LDVGV---LIRAPSAESLSNLLADKKNAKSEGVPLP-DDLAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 243 YIYTSGTTGLPKAAIVVHSRYYRMAALVYYGFRMRPNDIVYDCLPLYHSAGNIVGIGQCLLHGMTVVIRKKFSASRFWDD 322
Cdd:cd05926 154 ILHTSGTTGRPKGVPLTHRNLAASATNITNTYKLTPDDRTLVVMPLFHVHGLVASLLSTLAAGGSVVLPPRFSASTFWPD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 323 CIKYNCTIVQYIGELCRYLLNQPPREAENQHQ----VRMAlGNGLRQSIWTNFSSRFHIPqVAEFYGATECNcslgnfdS 398
Cdd:cd05926 234 VRDYNATWYTAVPTIHQILLNRPEPNPESPPPklrfIRSC-SASLPPAVLEALEATFGAP-VLEAYGMTEAA-------H 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 399 QVgacgFNSRILSFVYPIRLVRVNEDTMELIRGPDGvcipcQPGEPGQlVGRIIQKDPlRRFDGYLNQGANNKKIAK--D 476
Cdd:cd05926 305 QM----TSNPLPPGPRKPGSVGKPVGVEVRILDEDG-----EILPPGV-VGEICLRGP-NVTRGYLNNPEANAEAAFkdG 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 477 VFKKGDQAYLtgdvlvmDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLDMADVAVYGV--EVPGTEGRAGMAAVA 554
Cdd:cd05926 374 WFRTGDLGYL-------DADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVpdEKYGEEVAAAVVLRE 446
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 40807357 555 SPTgnCDLERFAQVLEKELPLYARPIFLRLLPELHKTGTYKFQKTELRK 603
Cdd:cd05926 447 GAS--VTEEELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKVAE 493
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
52-602 |
1.51e-41 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 157.92 E-value: 1.51e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 52 DIFGGlvllkvkAKVRQCLQERrtvpilfastVRRHPDKTALIFE---GTDTHWTFRQLDEYSSSVANFLQARGLASGDV 128
Cdd:PRK08008 2 DIVGG-------QHLRQMWDDL----------ADVYGHKTALIFEssgGVVRRYSYLELNEEINRTANLFYSLGIRKGDK 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 129 AAIFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALLHCLTTSRARALVFGSEMASAICEVHASLDPSLS-LFCSGSWE 207
Cdd:PRK08008 65 VALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASLLVTSAQFYPMYRQIQQEDATPLRhICLTRVAL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 208 PGAvpPSTEHLDPLLKDAPKHLPSCPDKGFTDKLFYIYTSGTTGLPKAAIVVHsryYRMAALVYYG---FRMRPNDIVYD 284
Cdd:PRK08008 145 PAD--DGVSSFTQLKAQQPATLCYAPPLSTDDTAEILFTSGTTSRPKGVVITH---YNLRFAGYYSawqCALRDDDVYLT 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 285 CLPLYHSAGNIVGIGQCLLHGMTVVIRKKFSASRFWDDCIKYNCTIVQYIGELCRYLLNQPPREAENQHQVR-----MAL 359
Cdd:PRK08008 220 VMPAFHIDCQCTAAMAAFSAGATFVLLEKYSARAFWGQVCKYRATITECIPMMIRTLMVQPPSANDRQHCLRevmfyLNL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 360 GNGLRQSiwtnFSSRFHIpQVAEFYGATECNCSL-GNFDSQ------VGACGFNsrilsfvYPIRLvrVNEDTMELIRGP 432
Cdd:PRK08008 300 SDQEKDA----FEERFGV-RLLTSYGMTETIVGIiGDRPGDkrrwpsIGRPGFC-------YEAEI--RDDHNRPLPAGE 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 433 DG-VCIpcqPGEPGQLVgriiqkdplrrFDGYLNQGANNKKIAkdvfkKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRW 511
Cdd:PRK08008 366 IGeICI---KGVPGKTI-----------FKEYYLDPKATAKVL-----EADGWLHTGDTGYVDEEGFFYFVDRRCNMIKR 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 512 KGENVSTTEVEGTLSRLLDMADVAVYGVEVPGTEGRAGMAAVASPTGNCDLERFAQVLEKELPLYARPIFLRLLPELHKT 591
Cdd:PRK08008 427 GGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRN 506
|
570
....*....|.
gi 40807357 592 GTYKFQKTELR 602
Cdd:PRK08008 507 CSGKIIKKNLK 517
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
68-603 |
2.22e-35 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 140.68 E-value: 2.22e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 68 QCLQERRTVpilFASTVRRH----PDKTALIFEGTDTHWtfRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLW 143
Cdd:PRK07786 10 QPYLARRQN---WVNQLARHalmqPDAPALRFLGNTTTW--RELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 144 LGMAKLGVEAALINTNLRRDALLHCLTTSRARALVFGSEMASAICEVHAsLDPSLSLFCSGSWEPGAVPPSTEhlDPLLK 223
Cdd:PRK07786 85 LAANMLGAIAVPVNFRLTPPEIAFLVSDCGAHVVVTEAALAPVATAVRD-IVPLLSTVVVAGGSSDDSVLGYE--DLLAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 224 DAPKHLP-SCPDKgfTDKLFyIYTSGTTGLPKAAIVVHSRYYRMAALVYYGFRM-RPNDIVYDCLPLYHSAGnIVGIGQC 301
Cdd:PRK07786 162 AGPAHAPvDIPND--SPALI-MYTSGTTGRPKGAVLTHANLTGQAMTCLRTNGAdINSDVGFVGVPLFHIAG-IGSMLPG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 302 LLHGMTVVIR--KKFSASRFWDDCIKYNCTIVQYIGELCRYLLNQPprEAENQHQVRMALGNG--------LRQsiwtnF 371
Cdd:PRK07786 238 LLLGAPTVIYplGAFDPGQLLDVLEAEKVTGIFLVPAQWQAVCAEQ--QARPRDLALRVLSWGaapasdtlLRQ-----M 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 372 SSRFHIPQVAEFYGATECN---CSLGNFDS--QVGACGfnsrilsFVYPIRLVRVNEDTMELIrgpdgvcipcQPGEpgq 446
Cdd:PRK07786 311 AATFPEAQILAAFGQTEMSpvtCMLLGEDAirKLGSVG-------KVIPTVAARVVDENMNDV----------PVGE--- 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 447 lVGRIIQKDPlRRFDGYLnqgaNNKKIAKDVFKKGdqAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLS 526
Cdd:PRK07786 371 -VGEIVYRAP-TLMSGYW----NNPEATAEAFAGG--WFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLA 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 527 RLLDMADVAVYG------VEVPgtegrAGMAAVASPTGNCDLERFAQVLEKELPLYARPIFLRLLPELHKTGTYKFQKTE 600
Cdd:PRK07786 443 SHPDIVEVAVIGradekwGEVP-----VAVAAVRNDDAALTLEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKVLKTE 517
|
...
gi 40807357 601 LRK 603
Cdd:PRK07786 518 LRE 520
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
102-603 |
2.77e-34 |
|
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: 135.54 E-value: 2.77e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 102 WTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALLHCLTTSRARALVFGS 181
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 182 EmasaicevhasldpslslfcsgswepgavppstehldpllkdapkhlpscpdkgftDKLFYIYTSGTTGLPKAAIVVHS 261
Cdd:cd05972 81 E--------------------------------------------------------DPALIYFTSGTTGLPKGVLHTHS 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 262 ryYRMAALVYYGF--RMRPNDIVY---DCLPLYHSAGNIVGIgqcLLHGMTVVI--RKKFSASRFWDDCIKYNCTIVQYI 334
Cdd:cd05972 105 --YPLGHIPTAAYwlGLRPDDIHWniaDPGWAKGAWSSFFGP---WLLGATVFVyeGPRFDAERILELLERYGVTSFCGP 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 335 GELCRYLLNQPPREAENQH-QVRMALGNGLRQSIWTNFSSRFHIPqVAEFYGATECNCSLGNF---DSQVGACGfnsril 410
Cdd:cd05972 180 PTAYRMLIKQDLSSYKFSHlRLVVSAGEPLNPEVIEWWRAATGLP-IRDGYGQTETGLTVGNFpdmPVKPGSMG------ 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 411 sfvYPIRLVRVnedtmELIRGpDGVciPCQPGEPGQLVgriIQKDPLRRFDGYLNqganNKKIAKDVFKKGdqAYLTGDV 490
Cdd:cd05972 253 ---RPTPGYDV-----AIIDD-DGR--ELPPGEEGDIA---IKLPPPGLFLGYVG----DPEKTEASIRGD--YYLTGDR 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 491 LVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLDMADVAVYGVEVPgTEGRAGMAAVASPTGNCDLERFAQVLE 570
Cdd:cd05972 313 AYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDP-VRGEVVKAFVVLTSGYEPSEELAEELQ 391
|
490 500 510
....*....|....*....|....*....|....*..
gi 40807357 571 ----KELPLYARPIFLRLLPELHKTGTYKFQKTELRK 603
Cdd:cd05972 392 ghvkKVLAPYKYPREIEFVEELPKTISGKIRRVELRD 428
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
88-602 |
7.18e-34 |
|
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: 135.57 E-value: 7.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 88 PDKTALIfeGTDTHWTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALLH 167
Cdd:cd05959 18 GDKTAFI--DDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 168 CLTTSRARALVFGSEMASAICEVHASLDPSL-SLFCSGSWEPGAVPPSTEHLDPLLKDAPKHLPSCPDkgftDKLFYIYT 246
Cdd:cd05959 96 YLEDSRARVVVVSGELAPVLAAALTKSEHTLvVLIVSGGAGPEAGALLLAELVAAEAEQLKPAATHAD----DPAFWLYS 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 247 SGTTGLPKAAIVVHSRYYRMAALvyYG---FRMRPNDIVYDCLPLYHSagniVGIGQCLLH----GMTVVIRKKF-SASR 318
Cdd:cd05959 172 SGSTGRPKGVVHLHADIYWTAEL--YArnvLGIREDDVCFSAAKLFFA----YGLGNSLTFplsvGATTVLMPERpTPAA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 319 FWDDCIKYNCTIVQYIGELCRYLLNQPPREAENQHQVRMAL--GNGLRQSIWTNFSSRFHIpQVAEFYGATEC-NCSLGN 395
Cdd:cd05959 246 VFKRIRRYRPTVFFGVPTLYAAMLAAPNLPSRDLSSLRLCVsaGEALPAEVGERWKARFGL-DILDGIGSTEMlHIFLSN 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 396 F--DSQVGACGFNsrilsfV--YPIRLvrvnedtmeliRGPDGVCIPcqPGEPGQLvgriiqkdpLRRFDGYLNQGANNK 471
Cdd:cd05959 325 RpgRVRYGTTGKP------VpgYEVEL-----------RDEDGGDVA--DGEPGEL---------YVRGPSSATMYWNNR 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 472 KIAKDVFKKGdqAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLDMADVAVYGVEVPgtEGRAGMA 551
Cdd:cd05959 377 DKTRDTFQGE--WTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDE--DGLTKPK 452
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 40807357 552 AVASPTGNCDL-----ERFAQVLEKELPLYARPIFLRLLPELHKTGTYKFQKTELR 602
Cdd:cd05959 453 AFVVLRPGYEDsealeEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
84-602 |
2.49e-32 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 131.35 E-value: 2.49e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 84 VRRHPDKTALIFEGTDTHWTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGVEAALINTNLRRD 163
Cdd:PRK13391 7 AQTTPDKPAVIMASTGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 164 ALLHCLTTSRARALVfGSEMASAICEVHASLDPSLSLfCSGSWEPGAVPPSTEhldplLKDAPKHLPSCP--DKGFTDKL 241
Cdd:PRK13391 87 EAAYIVDDSGARALI-TSAAKLDVARALLKQCPGVRH-RLVLDGDGELEGFVG-----YAEAVAGLPATPiaDESLGTDM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 242 FyiYTSGTTGLPKAAI-------VVHSRYYRMAALVYYGFRmrpNDIVYDC-LPLYHSAGN-IVGIGQCLlhGMTVVIRK 312
Cdd:PRK13391 160 L--YSSGTTGRPKGIKrplpeqpPDTPLPLTAFLQRLWGFR---SDMVYLSpAPLYHSAPQrAVMLVIRL--GGTVIVME 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 313 KFSASRFWDDCIKYNCTIVQYIGELCRYLLnQPPREAENQHQVrmalgNGLRQSI-----------------WTnfssrf 375
Cdd:PRK13391 233 HFDAEQYLALIEEYGVTHTQLVPTMFSRML-KLPEEVRDKYDL-----SSLEVAIhaaapcppqvkeqmidwWG------ 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 376 hiPQVAEFYGATECNcslgnfdsqvGACGFNSRiLSFVYPIRLVRVNEDTMElIRGPDGVciPCQPGEPGQlvgriIQKD 455
Cdd:PRK13391 301 --PIIHEYYAATEGL----------GFTACDSE-EWLAHPGTVGRAMFGDLH-ILDDDGA--ELPPGEPGT-----IWFE 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 456 PLRRFDgYLNQGANNKKiAKDvfkkGDQAYLT-GDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLDMADV 534
Cdd:PRK13391 360 GGRPFE-YLNDPAKTAE-ARH----PDGTWSTvGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADA 433
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 40807357 535 AVYGV--EVPGTEGRAGMAAVASPTGNCDL-ERFAQVLEKELPLYARPIFLRLLPELHKTGTYKFQKTELR 602
Cdd:PRK13391 434 AVFGVpnEDLGEEVKAVVQPVDGVDPGPALaAELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLLR 504
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
90-602 |
1.00e-31 |
|
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: 128.35 E-value: 1.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 90 KTALIfeGTDTHWTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALLHCL 169
Cdd:cd05919 1 KTAFY--AADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 170 TTSRARALVFGsemASAICevhasldpslslfcsgswepgavppstehldpllkdapkhlpscpdkgftdklFYIYTSGT 249
Cdd:cd05919 79 RDCEARLVVTS---ADDIA-----------------------------------------------------YLLYSSGT 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 250 TGLPKAAIVVHSRYYRMA-ALVYYGFRMRPNDIVYDCLPLY--HSAGNIVGIGqcLLHGMTVVIRKKF-SASRFWDDCIK 325
Cdd:cd05919 103 TGPPKGVMHAHRDPLLFAdAMAREALGLTPGDRVFSSAKMFfgYGLGNSLWFP--LAVGASAVLNPGWpTAERVLATLAR 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 326 YNCTIVQYIGELCRYLLNQPPREAENQHQVRMAL--GNGLRQSIWTNFSSRFHIPqVAEFYGATEC-NCSLGNFDSQV-- 400
Cdd:cd05919 181 FRPTVLYGVPTFYANLLDSCAGSPDALRSLRLCVsaGEALPRGLGERWMEHFGGP-ILDGIGATEVgHIFLSNRPGAWrl 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 401 GACGfnsRILSFvYPIRLVrvnedtmelirGPDGVCIPcqPGEPGQLVGRIIQKDPlrrfdGYLNqganNKKIAKDVFKK 480
Cdd:cd05919 260 GSTG---RPVPG-YEIRLV-----------DEEGHTIP--PGEEGDLLVRGPSAAV-----GYWN----NPEKSRATFNG 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 481 GdqAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLDMADVAVygVEVPGTEGRAGMAAVASPTGNC 560
Cdd:cd05919 314 G--WYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAV--VAVPESTGLSRLTAFVVLKSPA 389
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 40807357 561 D-----LERFAQVLEKELPLYARPIFLRLLPELHKTGTYKFQKTELR 602
Cdd:cd05919 390 ApqeslARDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKLR 436
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
84-604 |
1.27e-31 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 128.54 E-value: 1.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 84 VRRHPDKTALIFEGTDthWTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGVEAALINTNLRRD 163
Cdd:PRK03640 12 AFLTPDRTAIEFEEKK--VTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSRE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 164 ALLHCLTTSRARALVfgsemasaicevhasldpslslfCSGSWEPGAVPPSTEHLDPLLKDAPKHLPSCPDKGFTDKLFY 243
Cdd:PRK03640 90 ELLWQLDDAEVKCLI-----------------------TDDDFEAKLIPGISVKFAELMNGPKEEAEIQEEFDLDEVATI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 244 IYTSGTTGLPKAAIVVHSRYYRMA---ALvyyGFRMRPNDIVYDCLPLYHSAG-NIvgIGQCLLHGMTVVIRKKFSASRF 319
Cdd:PRK03640 147 MYTSGTTGKPKGVIQTYGNHWWSAvgsAL---NLGLTEDDCWLAAVPIFHISGlSI--LMRSVIYGMRVVLVEKFDAEKI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 320 WDDCIKYNCTIVQYIGELCRYLLNQPPREAENQHQVRMALGNG------LRQSiwtnfsSRFHIPqVAEFYGATECNcsl 393
Cdd:PRK03640 222 NKLLQTGGVTIISVVSTMLQRLLERLGEGTYPSSFRCMLLGGGpapkplLEQC------KEKGIP-VYQSYGMTETA--- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 394 gnfdSQVGAcgfnsriLSFvypirlvrvnEDTMELIrG-------PDGVCI-----PCQPGEPGQLV--GRIIQKdplrr 459
Cdd:PRK03640 292 ----SQIVT-------LSP----------EDALTKL-GsagkplfPCELKIekdgvVVPPFEEGEIVvkGPNVTK----- 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 460 fdGYLNQ-GANNKKIAKDVFKKGDQAYLtgdvlvmDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLDMADVAVYG 538
Cdd:PRK03640 345 --GYLNReDATRETFQDGWFKTGDIGYL-------DEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVG 415
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 40807357 539 VEvPGTEGRAGMAAVASpTGNCDLERFAQVLEKELPLYARPIFLRLLPELHKTGTYKFQKTELRKE 604
Cdd:PRK03640 416 VP-DDKWGQVPVAFVVK-SGEVTEEELRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHELKQL 479
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
85-602 |
2.42e-31 |
|
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: 128.77 E-value: 2.42e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 85 RRHPDKTALIF---EGTDTHWTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGVEAALINTNLR 161
Cdd:cd05970 28 KEYPDKLALVWcddAGEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQLT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 162 RDALLHCLTTSRARALVFGSE--MASAICEVHASLdPSLSLFCsgsWEPGAVPPSTEHLDPLLKDAPKHLP---SCPDKG 236
Cdd:cd05970 108 AKDIVYRIESADIKMIVAIAEdnIPEEIEKAAPEC-PSKPKLV---WVGDPVPEGWIDFRKLIKNASPDFErptANSYPC 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 237 FTDKLFYIYTSGTTGLPKaaIVVHSRYYRMAALVY--YGFRMRPNDIvydclplyHSAGNIVGIGQCL--------LHGM 306
Cdd:cd05970 184 GEDILLVYFSSGTTGMPK--MVEHDFTYPLGHIVTakYWQNVREGGL--------HLTVADTGWGKAVwgkiygqwIAGA 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 307 TVVI--RKKFSASRFWDDCIKYNCTIVQYIGELCRYLLNQPpREAENQHQVRMAL--GNGLRQSIWTNFSSRFHIpQVAE 382
Cdd:cd05970 254 AVFVydYDKFDPKALLEKLSKYGVTTFCAPPTIYRFLIRED-LSRYDLSSLRYCTtaGEALNPEVFNTFKEKTGI-KLME 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 383 FYGATECNCSLGNF---DSQVGACGFNSRilsfVYPIRLVRvnedtmelirgPDGVciPCQPGEPGQLVGRIIQKDPLRR 459
Cdd:cd05970 332 GFGQTETTLTIATFpwmEPKPGSMGKPAP----GYEIDLID-----------REGR--SCEAGEEGEIVIRTSKGKPVGL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 460 FDGYlnqGANNKKIAkDVFKKGdqAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLDMADVAVYGV 539
Cdd:cd05970 395 FGGY---YKDAEKTA-EVWHDG--YYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGV 468
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 40807357 540 EVPgtegRAGMAAVASPTGNCDLERfAQVLEKEL--------PLYARPIFLRLLPELHKTGTYKFQKTELR 602
Cdd:cd05970 469 PDP----IRGQVVKATIVLAKGYEP-SEELKKELqdhvkkvtAPYKYPRIVEFVDELPKTISGKIRRVEIR 534
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
75-602 |
4.22e-31 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 127.97 E-value: 4.22e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 75 TVPILFASTVRRHPDKTALIFEGTDTHWTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGVEAA 154
Cdd:PRK12583 19 TIGDAFDATVARFPDREALVVRHQALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 155 LINTNLRRDALLHCLTTSRARALVFGSEMASaiCEVHASLD---PSLSLFCSGSWEPGAVPpsteHLDPLL---KDAPKH 228
Cdd:PRK12583 99 NINPAYRASELEYALGQSGVRWVICADAFKT--SDYHAMLQellPGLAEGQPGALACERLP----ELRGVVslaPAPPPG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 229 LPSCPD-----KGFTDK-LFYI-------------YTSGTTGLPKAAIVVHSRYYRMAALVYYGFRMRPNDIVYDCLPLY 289
Cdd:PRK12583 173 FLAWHElqargETVSREaLAERqasldrddpiniqYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCVPVPLY 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 290 HSAGNIVGIGQCLLHGMTVVI-RKKFSASRFWDDCIKYNCTIVQ-----YIGElcrylLNQPPREAENQHQVRMALGNG- 362
Cdd:PRK12583 253 HCFGMVLANLGCMTVGACLVYpNEAFDPLATLQAVEEERCTALYgvptmFIAE-----LDHPQRGNFDLSSLRTGIMAGa 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 363 ------LRQSIwtnfsSRFHIPQVAEFYGATECNcslgnfdsqvgacgfnsrilsfvyPIRLVRVNEDTMEL-------- 428
Cdd:PRK12583 328 pcpievMRRVM-----DEMHMAEVQIAYGMTETS------------------------PVSLQTTAADDLERrvetvgrt 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 429 -------IRGPDGVCIPcqPGEPGQLVGR---IIQkdplrrfdGYLNqgaNNKKIAKDVFKKGdqaYL-TGDVLVMDELG 497
Cdd:PRK12583 379 qphlevkVVDPDGATVP--RGEIGELCTRgysVMK--------GYWN---NPEATAESIDEDG---WMhTGDLATMDEQG 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 498 YLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLDMADVAVYGveVPGTE-GRAGMAAVA-SPTGNCDLERFAQVLEKELPL 575
Cdd:PRK12583 443 YVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFG--VPDEKyGEEIVAWVRlHPGHAASEEELREFCKARIAH 520
|
570 580
....*....|....*....|....*..
gi 40807357 576 YARPIFLRLLPELHKTGTYKFQKTELR 602
Cdd:PRK12583 521 FKVPRYFRFVDEFPMTVTGKVQKFRMR 547
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
79-603 |
1.14e-30 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 127.38 E-value: 1.14e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 79 LFASTVRRHPDKTALIF--EGTDTH----WTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNE-FVGLWLGMAKlGV 151
Cdd:PRK07529 30 LLSRAAARHPDAPALSFllDADPLDrpetWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPEtHFALWGGEAA-GI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 152 eAALINTNLRRDALLHCLTTSRARALV-----FGSEMASAICEVHASLDPSLSLFCSGSwePGAVPPSTEHLDPLLKdaP 226
Cdd:PRK07529 109 -ANPINPLLEPEQIAELLRAAGAKVLVtlgpfPGTDIWQKVAEVLAALPELRTVVEVDL--ARYLPGPKRLAVPLIR--R 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 227 KH----------LPSCP-DKGFTDKLF-------YIYTSGTTGLPKAAIVVHSRYYRMAALVYYGFRMRPNDIVYDCLPL 288
Cdd:PRK07529 184 KAharildfdaeLARQPgDRLFSGRPIgpddvaaYFHTGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPGDTVFCGLPL 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 289 YHSAGNIVGIGQCLLHGMTVVI------RKKFSASRFWDDCIKYNCTIVQYIGELCRYLLNQPPrEAENQHQVRMALGNG 362
Cdd:PRK07529 264 FHVNALLVTGLAPLARGAHVVLatpqgyRGPGVIANFWKIVERYRINFLSGVPTVYAALLQVPV-DGHDISSLRYALCGA 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 363 --LRQSIWTNFSSRFHIPqVAEFYGATECNC-SLGNF---DSQVGACGfnsriLSFVYP-IRLVRVNEDtmelirGPDGV 435
Cdd:PRK07529 343 apLPVEVFRRFEAATGVR-IVEGYGLTEATCvSSVNPpdgERRIGSVG-----LRLPYQrVRVVILDDA------GRYLR 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 436 ciPCQPGEPGQLVgriIQKDPLrrFDGYLNqGANNKKIAKdvfkkgDQAYL-TGDVLVMDELGYLYFRDRTGDTFRWKGE 514
Cdd:PRK07529 411 --DCAVDEVGVLC---IAGPNV--FSGYLE-AAHNKGLWL------EDGWLnTGDLGRIDADGYFWLTGRAKDLIIRGGH 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 515 NVSTTEVEGTLSRLLDMADVAVYGV------EVPgtegragMAAVASPTGncdlerfAQVLEKELPLYAR---------P 579
Cdd:PRK07529 477 NIDPAAIEEALLRHPAVALAAAVGRpdahagELP-------VAYVQLKPG-------ASATEAELLAFARdhiaeraavP 542
|
570 580
....*....|....*....|....
gi 40807357 580 IFLRLLPELHKTGTYKFQKTELRK 603
Cdd:PRK07529 543 KHVRILDALPKTAVGKIFKPALRR 566
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
74-586 |
1.31e-30 |
|
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: 125.70 E-value: 1.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 74 RTVPILFASTVRRHPDKTALIFEGTDTHWTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGVEA 153
Cdd:cd05923 1 QTVFEMLRRAASRAPDACAIADPARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 154 ALINTNLRRDALLHCLTTSRARALVF--GSEMASAI-----CEVHASLDPSLSLFCSGSwepgavppstehldPLLKDap 226
Cdd:cd05923 81 ALINPRLKAAELAELIERGEMTAAVIavDAQVMDAIfqsgvRVLALSDLVGLGEPESAG--------------PLIED-- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 227 khlpscPDKGFTDKLFYIYTSGTTGLPKAAIVVH----SRYYRMAALVyyGFRMRPNDIVYDCLPLYHSAGNIVGIGQCL 302
Cdd:cd05923 145 ------PPREPEQPAFVFYTSGTTGLPKGAVIPQraaeSRVLFMSTQA--GLRHGRHNVVLGLMPLYHVIGFFAVLVAAL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 303 LHGMTVVIRKKFSASRfwddcikynctIVQYIGEL---CRYL-----------LNQPPREAENQHQVRMAlGNGLRQSIW 368
Cdd:cd05923 217 ALDGTYVVVEEFDPAD-----------ALKLIEQErvtSLFAtpthldalaaaAEFAGLKLSSLRHVTFA-GATMPDAVL 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 369 TNFSSRFHIPQVaEFYGATECNCSLGNFDSQVGAC---GFNSRilsfvypIRLVRVNEDTMELIrgpdgvcipcQPGEPG 445
Cdd:cd05923 285 ERVNQHLPGEKV-NIYGTTEAMNSLYMRDARTGTEmrpGFFSE-------VRIVRIGGSPDEAL----------ANGEEG 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 446 QLvgrIIQKDPLRRFDGYLNQGANNKKiakdvfKKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTL 525
Cdd:cd05923 347 EL---IVAAAADAAFTGYLNQPEATAK------KLQDGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVL 417
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 40807357 526 SRLLDMADVAVYGveVPGTE-GRAGMAAVASPTGNCDLERFAQV-LEKELPLYARP---IFLRLLP 586
Cdd:cd05923 418 SRHPGVTEVVVIG--VADERwGQSVTACVVPREGTLSADELDQFcRASELADFKRPrryFFLDELP 481
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
111-595 |
2.06e-29 |
|
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: 121.78 E-value: 2.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 111 SSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGVEAALI---NTNLRRDALLHCLTTSRARALVFgsemasai 187
Cdd:cd05922 3 VSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRLGLVfvpLNPTLKESVLRYLVADAGGRIVL-------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 188 ceVHASLDPSLSLFCSGSWEPGAVPpSTEHLDPLLKDAPKHLPSCPDKGFtdklfYIYTSGTTGLPKAAIVVHSRYYRMA 267
Cdd:cd05922 75 --ADAGAADRLRDALPASPDPGTVL-DADGIRAARASAPAHEVSHEDLAL-----LLYTSGSTGSPKLVRLSHQNLLANA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 268 ALVYYGFRMRPNDIVYDCLPLYHSAGNIVgIGQCLLHGMTVVIRKKFSASR-FWDDCIKYNCT---IVQYIGELCRYLlN 343
Cdd:cd05922 147 RSIAEYLGITADDRALTVLPLSYDYGLSV-LNTHLLRGATLVLTNDGVLDDaFWEDLREHGATglaGVPSTYAMLTRL-G 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 344 QPPREAENQHQVRMAlGNGLRQSIWTNFSSRFHIPQVAEFYGATECncslgnfdsqvgacgfnSRILSFVYPIRLVRVNE 423
Cdd:cd05922 225 FDPAKLPSLRYLTQA-GGRLPQETIARLRELLPGAQVYVMYGQTEA-----------------TRRMTYLPPERILEKPG 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 424 -------DTMELIRGPDGVciPCQPGEPGQLVGR--IIQKdplrrfdGYLNQGANNKKIAKdvfkKGDQAYlTGDVLVMD 494
Cdd:cd05922 287 siglaipGGEFEILDDDGT--PTPPGEPGEIVHRgpNVMK-------GYWNDPPYRRKEGR----GGGVLH-TGDLARRD 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 495 ELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLDMADVAVYGVEVPGTEGRAgmAAVASPTGNcDLERFAQVLEKELP 574
Cdd:cd05922 353 EDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDPLGEKLA--LFVTAPDKI-DPKDVLRSLAERLP 429
|
490 500
....*....|....*....|.
gi 40807357 575 LYARPIFLRLLPELHKTGTYK 595
Cdd:cd05922 430 PYKVPATVRVVDELPLTASGK 450
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
40-540 |
3.81e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 121.96 E-value: 3.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 40 RFIRVFIKTirrdifGGLVLLKVKAKVRQCLQERRTVPI--LFASTVRRHPDKTALIFE-GTdthWTFRQLDEYSSSVAN 116
Cdd:PRK07788 19 HYLRVMIRS------GAVDLERPDNGLRLAADIRRYGPFagLVAHAARRAPDRAALIDErGT---LTYAELDEQSNALAR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 117 FLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALLHCLTTSRARALVFGSEMASAICEVHASLDP 196
Cdd:PRK07788 90 GLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQLAEVAAREGVKALVYDDEFTDLLSALPPDLGR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 197 SLSLFCSGSWEPgAVPPSTEHLDPLL-KDAPKHLPSCPDKGFtdklFYIYTSGTTGLPKAAIVVHSRYYRMAALVYYGFR 275
Cdd:PRK07788 170 LRAWGGNPDDDE-PSGSTDETLDDLIaGSSTAPLPKPPKPGG----IVILTSGTTGTPKGAPRPEPSPLAPLAGLLSRVP 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 276 MRPNDIVYDCLPLYHSagniVGIGQCLL---HGMTVVIRKKFSASRFWDDCIKYNCTIVQYIGELCRYLLNQPP--REAE 350
Cdd:PRK07788 245 FRAGETTLLPAPMFHA----TGWAHLTLamaLGSTVVLRRRFDPEATLEDIAKHKATALVVVPVMLSRILDLGPevLAKY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 351 NQHQVRM--ALGNGLRQSIWTNFSSRFHiPQVAEFYGATECN-CSLGNFDSQVGACGFNSRilsfvyPIRLVRVNedtme 427
Cdd:PRK07788 321 DTSSLKIifVSGSALSPELATRALEAFG-PVLYNLYGSTEVAfATIATPEDLAEAPGTVGR------PPKGVTVK----- 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 428 lIRGPDGVCIPcqPGEpgqlVGRIIQKDPLrRFDGYLNQGanNKKIAKDVFKKGDQAYLtgdvlvmDELGYLYFRDRTGD 507
Cdd:PRK07788 389 -ILDENGNEVP--RGV----VGRIFVGNGF-PFEGYTDGR--DKQIIDGLLSSGDVGYF-------DEDGLLFVDGRDDD 451
|
490 500 510
....*....|....*....|....*....|...
gi 40807357 508 TFRWKGENVSTTEVEGTLSRLLDMADVAVYGVE 540
Cdd:PRK07788 452 MIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVD 484
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
96-602 |
1.35e-28 |
|
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: 119.07 E-value: 1.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 96 EGTDTHWTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALLHCLTTSRAR 175
Cdd:cd05971 1 KGTPEKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 176 ALVfgsemasaiceVHASLDPSLslfcsgswepgavppstehldpllkdapkhlpscpdkgftdklfYIYTSGTTGLPKA 255
Cdd:cd05971 81 ALV-----------TDGSDDPAL--------------------------------------------IIYTSGTTGPPKG 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 256 AIVVHSRYYRMAALVYYGFRMRPNDivYDCLplYHSA--GNIVGIGQCLL----HGMTVVIRK--KFSASRFWDDCIKYN 327
Cdd:cd05971 106 ALHAHRVLLGHLPGVQFPFNLFPRD--GDLY--WTPAdwAWIGGLLDVLLpslyFGVPVLAHRmtKFDPKAALDLMSRYG 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 328 CTIVQYIGELCRYLLNQPPREAENQHQVRmALGNGlRQSIWTNF----SSRFHIPqVAEFYGATECNCSLGN----FDSQ 399
Cdd:cd05971 182 VTTAFLPPTALKMMRQQGEQLKHAQVKLR-AIATG-GESLGEELlgwaREQFGVE-VNEFYGQTECNLVIGNcsalFPIK 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 400 VGACGFnsrilsfVYPIRLVRVNEDTMElirgpdgvciPCQPGEPGQLVgrIIQKDPLRrFDGYL-NQGANNKKIAKDVF 478
Cdd:cd05971 259 PGSMGK-------PIPGHRVAIVDDNGT----------PLPPGEVGEIA--VELPDPVA-FLGYWnNPSATEKKMAGDWL 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 479 kkgdqayLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLDMADVAVYGV--EVPGTEGRAGMAAVASP 556
Cdd:cd05971 319 -------LTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIpdPIRGEIVKAFVVLNPGE 391
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 40807357 557 TGNCDLERFAQVLEK-ELPLYARPIFLRLLPELHKTGTYKFQKTELR 602
Cdd:cd05971 392 TPSDALAREIQELVKtRLAAHEYPREIEFVNELPRTATGKIRRRELR 438
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
103-603 |
2.18e-28 |
|
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.
Pssm-ID: 341229 [Multi-domain] Cd Length: 437 Bit Score: 118.25 E-value: 2.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 103 TFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALLHCLTTSRARALVFGSE 182
Cdd:cd05903 3 TYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVPER 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 183 MasaicevhasldpslslfcsGSWEPGAVPpstehldpllkDAPKHLpscpdkgftdklfyIYTSGTTGLPKAaiVVHSR 262
Cdd:cd05903 83 F--------------------RQFDPAAMP-----------DAVALL--------------LFTSGTTGEPKG--VMHSH 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 263 YYRMAALVYYGFRM--RPNDIVYDCLPLYHSAGNIVGIGQCLLHGMTVVIRKKFSASRFWDDCIKYNCTIVQ----YIGE 336
Cdd:cd05903 116 NTLSASIRQYAERLglGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQDIWDPDKALALMREHGVTFMMgatpFLTD 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 337 LCRYLLNQPPREAenqhQVRMALGNG------LRQSIWTNFssrfhIPQVAEFYGATECNCSLGNFDSqvGACGFNSRIL 410
Cdd:cd05903 196 LLNAVEEAGEPLS----RLRTFVCGGatvprsLARRAAELL-----GAKVCSAYGSTECPGAVTSITP--APEDRRLYTD 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 411 SFVYPIRLVRVNEDtmelirgpDGVCIPcqPGEPGQLVGRIIQKdplrrFDGYLNQGANNKKIAKDVFkkgdqaYLTGDV 490
Cdd:cd05903 265 GRPLPGVEIKVVDD--------TGATLA--PGVEGELLSRGPSV-----FLGYLDRPDLTADAAPEGW------FRTGDL 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 491 LVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLDMADVAVYGVEVPGTEGRAgmAAVASPTGNC--DLERFAQV 568
Cdd:cd05903 324 ARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERA--CAVVVTKSGAllTFDELVAY 401
|
490 500 510
....*....|....*....|....*....|....*.
gi 40807357 569 LEKE-LPLYARPIFLRLLPELHKTGTYKFQKTELRK 603
Cdd:cd05903 402 LDRQgVAKQYWPERLVHVDDLPRTPSGKVQKFRLRE 437
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
92-539 |
8.19e-28 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 117.70 E-value: 8.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 92 ALIFEGTDTHWTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALLHCLTT 171
Cdd:PRK08276 2 AVIMAPSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 172 SRARALVFGSEMASAICEVHASLDPSLSLFCSGswepGAVPPSTEHLDPLLKDAPKHLPscPDKGFTDKLfyIYTSGTTG 251
Cdd:PRK08276 82 SGAKVLIVSAALADTAAELAAELPAGVPLLLVV----AGPVPGFRSYEEALAAQPDTPI--ADETAGADM--LYSSGTTG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 252 LPKA------AIVVHSRYYRMAALVYYGFRMRPNDIVYDCLPLYHSAgNIVGIGQCLLHGMTVVIRKKFSASRFWDDCIK 325
Cdd:PRK08276 154 RPKGikrplpGLDPDEAPGMMLALLGFGMYGGPDSVYLSPAPLYHTA-PLRFGMSALALGGTVVVMEKFDAEEALALIER 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 326 YNCTIVQYIGELCRYLLNQPP--REAENQHQVRMALGNGL-------RQSI--WTnfssrfhiPQVAEFYGATECNcslg 394
Cdd:PRK08276 233 YRVTHSQLVPTMFVRMLKLPEevRARYDVSSLRVAIHAAApcpvevkRAMIdwWG--------PIIHEYYASSEGG---- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 395 nfdsqvGACGFNSR------------ILSFVypirlvrvnedtmeLIRGPDGVciPCQPGEPGQlvgrIIQKDPLRRFDg 462
Cdd:PRK08276 301 ------GVTVITSEdwlahpgsvgkaVLGEV--------------RILDEDGN--ELPPGEIGT----VYFEMDGYPFE- 353
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 40807357 463 YLNQGANNKKI--AKDVFKKGDQAYLtgdvlvmDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLDMADVAVYGV 539
Cdd:PRK08276 354 YHNDPEKTAAArnPHGWVTVGDVGYL-------DEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGV 425
|
|
| PRK07868 |
PRK07868 |
acyl-CoA synthetase; Validated |
79-639 |
4.21e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236121 [Multi-domain] Cd Length: 994 Bit Score: 117.51 E-value: 4.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 79 LFASTVRRHPDKTALIFEGTdTHwTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGVEAALint 158
Cdd:PRK07868 452 IIAEQARDAPKGEFLLFDGR-VH-TYEAVNRRINNVVRGLIAVGVRQGDRVGVLMETRPSALVAIAALSRLGAVAVL--- 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 159 nLRRDALLhclttsrARALVFGSemASAICEVHASLDPSLSL----FCSGSWE-------PGAVPPSTEHLDPllkDAPK 227
Cdd:PRK07868 527 -MPPDTDL-------AAAVRLGG--VTEIITDPTNLEAARQLpgrvLVLGGGEsrdldlpDDADVIDMEKIDP---DAVE 593
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 228 hLPSC--PDKGFTDKLFYIYTSGTTGLPKAAIVVHSRYyrmaALVYYGF----RMRPNDIVYDCLPLYHSAGNIVGIGQC 301
Cdd:PRK07868 594 -LPGWyrPNPGLARDLAFIAFSTAGGELVAKQITNYRW----ALSAFGTasaaALDRRDTVYCLTPLHHESGLLVSLGGA 668
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 302 LLHGMTVVIRKKFSASRFWDDCIKYNCTIVQYIGELCRYLLNQPPREAENQHQVRMALGNGLRQSIWTNFSSRFHIPQVA 381
Cdd:PRK07868 669 VVGGSRIALSRGLDPDRFVQEVRQYGVTVVSYTWAMLREVVDDPAFVLHGNHPVRLFIGSGMPTGLWERVVEAFAPAHVV 748
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 382 EFYGATECNCSLGNFD-SQVGACGfnsRILSFVYPIRLVRVNEDTMELIRGPDGVCIPCQPGEPGQLVGRIiqkdplrrf 460
Cdd:PRK07868 749 EFFATTDGQAVLANVSgAKIGSKG---RPLPGAGRVELAAYDPEHDLILEDDRGFVRRAEVNEVGVLLARA--------- 816
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 461 DGYLNQGANNKkiaKDVFKKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRL--LDMAdvAVYG 538
Cdd:PRK07868 817 RGPIDPTASVK---RGVFAPADTWISTEYLFRRDDDGDYWLVDRRGSVIRTARGPVYTEPVTDALGRIggVDLA--VTYG 891
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 539 VEVPGTEgrAGMAAV-----ASPTGNCDLERFAqvlekELPLYARPIFLRLLPELHKTGTYKFQKTELRKEGFdPAIVKD 613
Cdd:PRK07868 892 VEVGGRQ--LAVAAVtlrpgAAITAADLTEALA-----SLPVGLGPDIVHVVPEIPLSATYRPTVSALRAAGI-PKPGRQ 963
|
570 580
....*....|....*....|....*.
gi 40807357 614 pLFYLDAQKGRYVPLDQEAYSRIQAG 639
Cdd:PRK07868 964 -AWYFDPETNRYRRLTPAVRAELTGG 988
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
79-539 |
5.19e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 115.47 E-value: 5.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 79 LFASTVRRHPDKTALIFegTDTHWTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEfvgLWLGMAklgveAALInT 158
Cdd:PRK06188 17 LLVSALKRYPDRPALVL--GDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPE---VLMAIG-----AAQL-A 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 159 NLRRDAL---------LHCLTTSRARALVFGS----EMASAICEVHASLDPSLSLfcsgswepGAVPPSTEHLDPLLKDA 225
Cdd:PRK06188 86 GLRRTALhplgslddhAYVLEDAGISTLIVDPapfvERALALLARVPSLKHVLTL--------GPVPDGVDLLAAAAKFG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 226 PKHLpsCPDKGFTDKLFYIYTSGTTGLPKAAIVVHSRYYRMAALVYYGFRMRPNDIVYDCLPLYHSAGNIVGIGqcLLHG 305
Cdd:PRK06188 158 PAPL--VAAALPPDIAGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLSHAGGAFFLPT--LLRG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 306 MTVVIRKKFSASRFWDDCIKYNCTIVQYIGELCRYLLNQPPREAENQHQVRMALGNG-------LRQSIwtnfsSRFHiP 378
Cdd:PRK06188 234 GTVIVLAKFDPAEVLRAIEEQRITATFLVPTMIYALLDHPDLRTRDLSSLETVYYGAspmspvrLAEAI-----ERFG-P 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 379 QVAEFYGATECN---CSLGNFD------SQVGACGFnsrilsfvyPIRLVRVNedtmelIRGPDGVCIPcqPGEPGQLVG 449
Cdd:PRK06188 308 IFAQYYGQTEAPmviTYLRKRDhdpddpKRLTSCGR---------PTPGLRVA------LLDEDGREVA--QGEVGEICV 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 450 RiiqkDPLrRFDGYLNQGANNKKiakdVFKKGdqaYL-TGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRL 528
Cdd:PRK06188 371 R----GPL-VMDGYWNRPEETAE----AFRDG---WLhTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEH 438
|
490
....*....|.
gi 40807357 529 LDMADVAVYGV 539
Cdd:PRK06188 439 PAVAQVAVIGV 449
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
85-601 |
6.17e-27 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 114.96 E-value: 6.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 85 RRHPDKTALIfeGTDTHWTFRQLDEYSSSVANFLQAR-GLASGDVAAIFMENRNEFVGLWLGMAKLGVEAALINTNLRRD 163
Cdd:PRK06839 13 YLHPDRIAII--TEEEEMTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTEN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 164 ALLHCLTTSRARALVFGSEMASAICEVH--ASLDPSLSLfcsgswepgavppstEHLDPLLKDAPKHLPscpDKGFTDKL 241
Cdd:PRK06839 91 ELIFQLKDSGTTVLFVEKTFQNMALSMQkvSYVQRVISI---------------TSLKEIEDRKIDNFV---EKNESASF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 242 FYIYTSGTTGLPKAAIVVHSRYYRMAALVYYGFRMRPNDIVYDCLPLYHsagnIVGIG----QCLLHGMTVVIRKKFSAS 317
Cdd:PRK06839 153 IICYTSGTTGKPKGAVLTQENMFWNALNNTFAIDLTMHDRSIVLLPLFH----IGGIGlfafPTLFAGGVIIVPRKFEPT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 318 RFWDDCIKYNCTIVQYIGELCRYLLNQPPREAENQHQVRMALGNG--LRQSIWTNFSSRFHipQVAEFYGATECNCSL-- 393
Cdd:PRK06839 229 KALSMIEKHKVTVVMGVPTIHQALINCSKFETTNLQSVRWFYNGGapCPEELMREFIDRGF--LFGQGFGMTETSPTVfm 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 394 ---GNFDSQVGACGfnsrilsfvYPIRLVRVnedtmELIrGPDGVCIPcqPGEpgqlVGRIIQKDPlRRFDGYLnqgaNN 470
Cdd:PRK06839 307 lseEDARRKVGSIG---------KPVLFCDY-----ELI-DENKNKVE--VGE----VGELLIRGP-NVMKEYW----NR 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 471 KKIAKDVFKKGdqAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLDMADVAVYGVEVPgTEGRAGM 550
Cdd:PRK06839 361 PDATEETIQDG--WLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHV-KWGEIPI 437
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 40807357 551 AAVASPTGncdlerfAQVLEKE--------LPLYARPIFLRLLPELHKTGTYKFQKTEL 601
Cdd:PRK06839 438 AFIVKKSS-------SVLIEKDviehcrlfLAKYKIPKEIVFLKELPKNATGKIQKAQL 489
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
80-604 |
1.63e-26 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 114.07 E-value: 1.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 80 FASTVRRHPDKTALIfEGTDTHWTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGVEAALINTN 159
Cdd:PRK06087 29 WQQTARAMPDKIAVV-DNHGASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 160 LRRDALLHCLTTSRARALvfgsemasaICEvhasldpslSLFCSGSWEPGAVP-----PSTEHLDPLLKDAPKH----LP 230
Cdd:PRK06087 108 WREAELVWVLNKCQAKMF---------FAP---------TLFKQTRPVDLILPlqnqlPQLQQIVGVDKLAPATsslsLS 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 231 SCPDKGFT---------DKLFYI-YTSGTTGLPKAAIVVHSRYyrMAALVYY--GFRMRPNDIVYDCLPLYHSAGNIVGI 298
Cdd:PRK06087 170 QIIADYEPlttaitthgDELAAVlFTSGTEGLPKGVMLTHNNI--LASERAYcaRLNLTWQDVFMMPAPLGHATGFLHGV 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 299 GQCLLHGMTVVIRKKFSAsrfwDDCI----KYNCTIVQ----YIGELCRYLLNQPPREAenqhQVRMALGNG------LR 364
Cdd:PRK06087 248 TAPFLIGARSVLLDIFTP----DACLalleQQRCTCMLgatpFIYDLLNLLEKQPADLS----ALRFFLCGGttipkkVA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 365 QSIWtnfssRFHIpQVAEFYGATE-----------CNCSLGNFDSqVGACGFNSRIlsfvypirlvrVNEDTMELirgpd 433
Cdd:PRK06087 320 RECQ-----QRGI-KLLSVYGSTEssphavvnlddPLSRFMHTDG-YAAAGVEIKV-----------VDEARKTL----- 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 434 gvcipcQPGEPGQLVGRIIQKdplrrFDGYLNQGANNKKIAKDvfkkgDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKG 513
Cdd:PRK06087 377 ------PPGCEGEEASRGPNV-----FMGYLDEPELTARALDE-----EGWYYSGDLCRMDEAGYIKITGRKKDIIVRGG 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 514 ENVSTTEVEGTLSRLLDMADVAVYGVevpgTEGRAG--MAAVASPTGNCDLERFAQVL----EKELPLYARPIFLRLLPE 587
Cdd:PRK06087 441 ENISSREVEDILLQHPKIHDACVVAM----PDERLGerSCAYVVLKAPHHSLTLEEVVaffsRKRVAKYKYPEHIVVIDK 516
|
570
....*....|....*..
gi 40807357 588 LHKTGTYKFQKTELRKE 604
Cdd:PRK06087 517 LPRTASGKIQKFLLRKD 533
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
85-604 |
2.97e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 112.67 E-value: 2.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 85 RRHPDKTALIFEGTDThwTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGVEAALINTNLRRDA 164
Cdd:PRK06145 13 RRTPDRAALVYRDQEI--SYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 165 LLHCLTTSRARALVFGSEMASAICEVH--ASLDPSlslfcsgswepgAVPPSTEHLDPLLKDAPKHlPSCPDkgftDKLF 242
Cdd:PRK06145 91 VAYILGDAGAKLLLVDEEFDAIVALETpkIVIDAA------------AQADSRRLAQGGLEIPPQA-AVAPT----DLVR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 243 YIYTSGTTGLPKAAIVVHSRYYRMAALVYYGFRMRPNDIVYDCLPLYH-SAGNIVGIGqCLLHGMTVVIRKKFSASRFWD 321
Cdd:PRK06145 154 LMYTSGTTDRPKGVMHSYGNLHWKSIDHVIALGLTASERLLVVGPLYHvGAFDLPGIA-VLWVGGTLRIHREFDPEAVLA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 322 DCIKYNCTIVQYIGELCRYLLNQPPREAENQHQVRMALGNGLR--QSIWTNFSSRFHIPQVAEFYGATEcNCSLGNFDSQ 399
Cdd:PRK06145 233 AIERHRLTCAWMAPVMLSRVLTVPDRDRFDLDSLAWCIGGGEKtpESRIRDFTRVFTRARYIDAYGLTE-TCSGDTLMEA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 400 ---VGACGFNSRILSFVyPIRlvrvnedtmelIRGPDGVCIPcqpgePGQlVGRIIQKDPlRRFDGYLNqgaNNKKIAKD 476
Cdd:PRK06145 312 greIEKIGSTGRALAHV-EIR-----------IADGAGRWLP-----PNM-KGEICMRGP-KVTKGYWK---DPEKTAEA 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 477 VFkkgDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLDMADVAVYGVEVPGTEGRAGMAAVASP 556
Cdd:PRK06145 370 FY---GDWFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNP 446
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 40807357 557 TGNCDLERFAQVLEKELPLYARPIFLRLLPELHKTGTYKFQKTELRKE 604
Cdd:PRK06145 447 GATLTLEALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVLRDE 494
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
88-588 |
3.45e-26 |
|
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: 111.85 E-value: 3.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 88 PDKTALIFEgtDTHWTFRQLDEYSSSVANFLQARGLASGDVAAIFMEnRNE--FVGLwLGMAKLGveAALIntnlrrdal 165
Cdd:cd05930 1 PDAVAVVDG--DQSLTYAELDARANRLARYLRERGVGPGDLVAVLLE-RSLemVVAI-LAVLKAG--AAYV--------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 166 lhclttsraralvfgsemasaicevhaSLDPSLslfcsgswepgavPPstEHLDPLLKDA-PKHLPSCPDKgftdkLFY- 243
Cdd:cd05930 66 ---------------------------PLDPSY-------------PA--ERLAYILEDSgAKLVLTDPDD-----LAYv 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 244 IYTSGTTGLPKAAIVVHsryyrmAALVYY--GFRMRPNDIVYDCLPLYHSAGNIVGIGQ---CLLHGMTVVIRKK---FS 315
Cdd:cd05930 99 IYTSGSTGKPKGVMVEH------RGLVNLllWMQEAYPLTPGDRVLQFTSFSFDVSVWEifgALLAGATLVVLPEevrKD 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 316 ASRFWDDCIKYNCTIVQYIGELCRYLLNQPPREAEnqHQVRMAL--GNGLRQSIWTNFSSRFHIPQVAEFYGATECncsl 393
Cdd:cd05930 173 PEALADLLAEEGITVLHLTPSLLRLLLQELELAAL--PSLRLVLvgGEALPPDLVRRWRELLPGARLVNLYGPTEA---- 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 394 gNFDSQVGACGFNSRILSFV---YPIRLVRVnedtmeLIRGPDGvcIPCQPGEPGQL------VGRiiqkdplrrfdGYL 464
Cdd:cd05930 247 -TVDATYYRVPPDDEEDGRVpigRPIPNTRV------YVLDENL--RPVPPGVPGELyiggagLAR-----------GYL 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 465 NQ-GANNKKIAKDVFKKGDQAYLTGDVLVMDELGYLYFRDRTgDT------FRwkgenVSTTEVEGTLSRLLDMADVAVy 537
Cdd:cd05930 307 NRpELTAERFVPNPFGPGERMYRTGDLVRWLPDGNLEFLGRI-DDqvkirgYR-----IELGEIEAALLAHPGVREAAV- 379
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 40807357 538 gVEVPGTEGRAGMAA--VASPTGNCDLERFAQVLEKELPLYARPIFLRLLPEL 588
Cdd:cd05930 380 -VAREDGDGEKRLVAyvVPDEGGELDEEELRAHLAERLPDYMVPSAFVVLDAL 431
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
83-604 |
1.28e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 111.29 E-value: 1.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 83 TVRRHPDKTALIfEGtDTHWTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNE-FVGLWlgmAKLGVEAALINTNLR 161
Cdd:PRK07470 16 AARRFPDRIALV-WG-DRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQmFESMF---AAFRLGAVWVPTNFR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 162 R--DALLHCLTTSRARALVFGS---EMASAICEVHASLDPSLSLfcsgswepGAvPPSTEHLDPLLKDAPKHLPSCPDKG 236
Cdd:PRK07470 91 QtpDEVAYLAEASGARAMICHAdfpEHAAAVRAASPDLTHVVAI--------GG-ARAGLDYEALVARHLGARVANAAVD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 237 FTDKLFYIYTSGTTGLPKAAIVVHSryyRMAALV--YYGFRMrPNDIVYDC----LPLYHSAGnivgigqclLHGMTVVI 310
Cdd:PRK07470 162 HDDPCWFFFTSGTTGRPKAAVLTHG---QMAFVItnHLADLM-PGTTEQDAslvvAPLSHGAG---------IHQLCQVA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 311 R---------KKFSASRFWDDCIKYNC-------TIVQYIGE----------LCRYLLNQ-PPREAENQHQVRMALGNGL 363
Cdd:PRK07470 229 RgaatvllpsERFDPAEVWALVERHRVtnlftvpTILKMLVEhpavdrydhsSLRYVIYAgAPMYRADQKRALAKLGKVL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 364 RQsiwtnfssrfhipqvaeFYGATECNcslGNF--------------DSQVGACGFnsrilsfvypirlvrvnEDT-MEL 428
Cdd:PRK07470 309 VQ-----------------YFGLGEVT---GNItvlppalhdaedgpDARIGTCGF-----------------ERTgMEV 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 429 -IRGPDGVciPCQPGEpgqlVGRIIQKDPlRRFDGYL-NQGANNKKIAKDVFKkgdqaylTGDVLVMDELGYLYFRDRTG 506
Cdd:PRK07470 352 qIQDDEGR--ELPPGE----TGEICVIGP-AVFAGYYnNPEANAKAFRDGWFR-------TGDLGHLDARGFLYITGRAS 417
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 507 DTFRWKGENVSTTEVEGTLSRLLDMADVAVYGVEVPgTEGRAGMAA-VASPTGNCDLERFAQVLEKELPLYARPIFLRLL 585
Cdd:PRK07470 418 DMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDP-VWGEVGVAVcVARDGAPVDEAELLAWLDGKVARYKLPKRFFFW 496
|
570
....*....|....*....
gi 40807357 586 PELHKTGTYKFQKTELRKE 604
Cdd:PRK07470 497 DALPKSGYGKITKKMVREE 515
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
60-602 |
1.69e-25 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 111.00 E-value: 1.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 60 LKVKAKVRQclqERRTVPILFASTVRRHPDKTALIFE-GTdthWTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNE 138
Cdd:PRK13382 32 LRIVAAMRR---EGMGPTSGFAIAAQRCPDRPGLIDElGT---LTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 139 FVGLWLGMAKLGVEAALINTNLRRDALLHCLTTSRARALVFGSEMAsaicevhASLDPSLSLFC----SGSWepgavpPS 214
Cdd:PRK13382 106 FVEALLAANRIGADILLLNTSFAGPALAEVVTREGVDTVIYDEEFS-------ATVDRALADCPqatrIVAW------TD 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 215 TEHLDPLLKDAPKHL----PSCPDKGFTdklfYIYTSGTTGLPKAAIVVHSRYYRMAALVYYGFRMRPNDIVYDCLPLYH 290
Cdd:PRK13382 173 EDHDLTVEVLIAAHAgqrpEPTGRKGRV----ILLTSGTTGTPKGARRSGPGGIGTLKAILDRTPWRAEEPTVIVAPMFH 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 291 SAgnivGIGQCLLHGM---TVVIRKKFSASRFWDDCIKYNCTIVQYIGELCRYLLNQPPrEAENQHQVR-----MALGNG 362
Cdd:PRK13382 249 AW----GFSQLVLAASlacTIVTRRRFDPEATLDLIDRHRATGLAVVPVMFDRIMDLPA-EVRNRYSGRslrfaAASGSR 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 363 LRQSIWTNFSSRFHiPQVAEFYGATEcncslgnfdsqVGacgfnsrILSFVYPIRLvRVNEDTMEliRGPDGVCI----- 437
Cdd:PRK13382 324 MRPDVVIAFMDQFG-DVIYNNYNATE-----------AG-------MIATATPADL-RAAPDTAG--RPAEGTEIrildq 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 438 ---PCQPGEpgqlVGRIIQKDPLrRFDGYlNQGANnkkiaKDvFKKGDQAylTGDVLVMDELGYLYFRDRTGDTFRWKGE 514
Cdd:PRK13382 382 dfrEVPTGE----VGTIFVRNDT-QFDGY-TSGST-----KD-FHDGFMA--SGDVGYLDENGRLFVVGRDDEMIVSGGE 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 515 NVSTTEVEGTLSRLLDMADVAVYGVEVPGTEGRAGMAAVASPTGNCDLERFAQVLEKELPLYARPIFLRLLPELHKTGTY 594
Cdd:PRK13382 448 NVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPGASATPETLKQHVRDNLANYKVPRDIVVLDELPRGATG 527
|
....*...
gi 40807357 595 KFQKTELR 602
Cdd:PRK13382 528 KILRRELQ 535
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
75-539 |
3.07e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 109.97 E-value: 3.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 75 TVPILFASTVRRHPDKTALIFegTDTHWTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGveAA 154
Cdd:PRK07798 4 NIADLFEAVADAVPDRVALVC--GDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKAR--AV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 155 LINTNLR--RDALLHCLTTSRARALVFGSEMASAICEVHASLdPSLSLFCS---GS---WEPGAVPpstehLDPLLKDAP 226
Cdd:PRK07798 80 PVNVNYRyvEDELRYLLDDSDAVALVYEREFAPRVAEVLPRL-PKLRTLVVvedGSgndLLPGAVD-----YEDALAAGS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 227 khlpscPDKGFT----DKLFYIYTSGTTGLPK--------------------AAIVVHSrYYRMAALVYYGFRMRpndiV 282
Cdd:PRK07798 154 ------PERDFGerspDDLYLLYTGGTTGMPKgvmwrqedifrvllggrdfaTGEPIED-EEELAKRAAAGPGMR----R 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 283 YDCLPLYHSAGNIVGIGqCLLHGMTVVI--RKKFSASRFWDDCIKYNCTIVQYIGE-LCRYLLnqppREAENQHQVRM-- 357
Cdd:PRK07798 223 FPAPPLMHGAGQWAAFA-ALFSGQTVVLlpDVRFDADEVWRTIEREKVNVITIVGDaMARPLL----DALEARGPYDLss 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 358 --ALGNG---LRQSIwtnfSSRF--HIPQVA--EFYGATEcncslgnfdsqVGACGFnsrilSFVYPirlVRVNEDTMEL 428
Cdd:PRK07798 298 lfAIASGgalFSPSV----KEALleLLPNVVltDSIGSSE-----------TGFGGS-----GTVAK---GAVHTGGPRF 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 429 IRGPDGVCI-----PCQPGEPGqlVGRIIQKD--PLrrfdGYLNqgaNNKKIAKDVFKKGDQAY-LTGDVLVMDELGY-- 498
Cdd:PRK07798 355 TIGPRTVVLdedgnPVEPGSGE--IGWIARRGhiPL----GYYK---DPEKTAETFPTIDGVRYaIPGDRARVEADGTit 425
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 40807357 499 LYFRD----RTGdtfrwkGENVSTTEVEGTLSRLLDMADVAVYGV 539
Cdd:PRK07798 426 LLGRGsvciNTG------GEKVFPEEVEEALKAHPDVADALVVGV 464
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
76-542 |
3.12e-25 |
|
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: 109.63 E-value: 3.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 76 VPILFAStvrRHPDKTALIFEGTDTHWTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGVEAAL 155
Cdd:cd05904 10 VSFLFAS---AHPSRPALIDAATGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 156 INTNLRRDALLHCLTTSRARaLVFgsemaSAICEVHASLDPSLSLFCSGSWEPGAVppsteHLDPLLKDAPKHLPSCPDK 235
Cdd:cd05904 87 ANPLSTPAEIAKQVKDSGAK-LAF-----TTAELAEKLASLALPVVLLDSAEFDSL-----SFSDLLFEADEAEPPVVVI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 236 GFTDKLFYIYTSGTTGLPKAAIVVHSRYYRMAALVYYGFRMRPN-DIVYDC-LPLYHSAGnIVGIGQCLLH-GMTVVIRK 312
Cdd:cd05904 156 KQDDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQFVAGEGSNSDsEDVFLCvLPMFHIYG-LSSFALGLLRlGATVVVMP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 313 KFSASRFWDDCIKYNCTivqyigelcrYLLNQPP-------REAENQHQVR-----MALGNGLRQSIWTNFSSRFHIPQV 380
Cdd:cd05904 235 RFDLEELLAAIERYKVT----------HLPVVPPivlalvkSPIVDKYDLSslrqiMSGAAPLGKELIEAFRAKFPNVDL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 381 AEFYGATECNCSL------GNFDSQVGACGfnsrilsfvypiRLVR------VNEDTmelirgpdGVCIPcqPGEPGQLV 448
Cdd:cd05904 305 GQGYGMTESTGVVamcfapEKDRAKYGSVG------------RLVPnveakiVDPET--------GESLP--PNQTGELW 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 449 --GRIIQKdplrrfdGYLNqgaNNKKIAKDVFKKGdqaYL-TGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTL 525
Cdd:cd05904 363 irGPSIMK-------GYLN---NPEATAATIDKEG---WLhTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALL 429
|
490 500
....*....|....*....|...
gi 40807357 526 SRLLDMADVAVYGV------EVP 542
Cdd:cd05904 430 LSHPEILDAAVIPYpdeeagEVP 452
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
79-543 |
3.46e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 109.83 E-value: 3.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 79 LFASTVRRHPDKTALIFEGTDThwTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGVEAALINT 158
Cdd:PRK06164 15 LLDAHARARPDAVALIDEDRPL--SRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 159 NLRRDALLHCLTTSRARALVF-----GSEMASAICEVHASLDPSL---SLFCSGSWEPGAVPPSTEHLDPLLKDAPKHLP 230
Cdd:PRK06164 93 RYRSHEVAHILGRGRARWLVVwpgfkGIDFAAILAAVPPDALPPLraiAVVDDAADATPAPAPGARVQLFALPDPAPPAA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 231 SCPDKGFTDKLFYIY-TSGTTGLPKaaIVVHS-----RYYRMAALVYygfRMRPNDIVYDCLPLYHSAGnIVGIGQCLLH 304
Cdd:PRK06164 173 AGERAADPDAGALLFtTSGTTSGPK--LVLHRqatllRHARAIARAY---GYDPGAVLLAALPFCGVFG-FSTLLGALAG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 305 GMTVVIRKKFSASRFWDDCIKYNCTIVQYIGELCRYLLNQPPREAENQHqvrmalgngLRQSIWTNFSSRFH-IPQVAE- 382
Cdd:PRK06164 247 GAPLVCEPVFDAARTARALRRHRVTHTFGNDEMLRRILDTAGERADFPS---------ARLFGFASFAPALGeLAALARa 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 383 -------FYGATECncsLGNFDSQVGACGFNSRILS---FVYPIRLVRvnedtmelIRGPDGVCIpCQPGEPGQlvgriI 452
Cdd:PRK06164 318 rgvpltgLYGSSEV---QALVALQPATDPVSVRIEGggrPASPEARVR--------ARDPQDGAL-LPDGESGE-----I 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 453 QKDPLRRFDGYL-NQGANNKKIAKD-VFKKGDQAYLTGDvlvmdelGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLD 530
Cdd:PRK06164 381 EIRAPSLMRGYLdNPDATARALTDDgYFRTGDLGYTRGD-------GQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPG 453
|
490
....*....|...
gi 40807357 531 MADVAVYGVEVPG 543
Cdd:PRK06164 454 VAAAQVVGATRDG 466
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
102-603 |
3.49e-25 |
|
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: 108.59 E-value: 3.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 102 WTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGVEAALINTNLRRdallhclttsraralvfgS 181
Cdd:cd05912 2 YTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTP------------------N 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 182 EMASAICEVHASLDPSLSLfcsgswepgavppstehldpllkdapkhlpscpdkgftdklfyIYTSGTTGLPKAAIVVHS 261
Cdd:cd05912 64 ELAFQLKDSDVKLDDIATI-------------------------------------------MYTSGTTGKPKGVQQTFG 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 262 RYYRMAALVYYGFRMRPNDIVYDCLPLYHSAGNIVgIGQCLLHGMTVVIRKKFSASRFWDDCIKYNCTIVQYIGELCRYL 341
Cdd:cd05912 101 NHWWSAIGSALNLGLTEDDNWLCALPLFHISGLSI-LMRSVIYGMTVYLVDKFDAEQVLHLINSGKVTIISVVPTMLQRL 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 342 LNQPPrEAENQHQVRMALGNG------LRQSIWTNfssrfhIPqVAEFYGATEcNCSlgnfdsQVGAcgfnsriLSFvyp 415
Cdd:cd05912 180 LEILG-EGYPNNLRCILLGGGpapkplLEQCKEKG------IP-VYQSYGMTE-TCS------QIVT-------LSP--- 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 416 irlvrvnEDTMELIRGPDGVCIPCQ-----PGEPGQLVGRIIQKDPlRRFDGYLNQ-GANNKKIAKDVFKKGDQAYLtgd 489
Cdd:cd05912 235 -------EDALNKIGSAGKPLFPVElkiedDGQPPYEVGEILLKGP-NVTKGYLNRpDATEESFENGWFKTGDIGYL--- 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 490 vlvmDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLDMADVAVYGVEVPgTEGRAGMAAVASpTGNCDLERFAQVL 569
Cdd:cd05912 304 ----DEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDD-KWGQVPVAFVVS-ERPISEEELIAYC 377
|
490 500 510
....*....|....*....|....*....|....
gi 40807357 570 EKELPLYARPIFLRLLPELHKTGTYKFQKTELRK 603
Cdd:cd05912 378 SEKLAKYKVPKKIYFVDELPRTASGKLLRHELKQ 411
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
85-602 |
7.13e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 108.36 E-value: 7.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 85 RRHPDKTALIFEGTDTHWTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGVEAALINTNLRRDA 164
Cdd:PRK09088 6 RLQPQRLAAVDLALGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 165 LLHCLTTSRARALVFGSEMASAICEVHAsldpsLSLFCSGSwePGAVPPSTEHLDPllkDAPKhlpscpdkgftdklFYI 244
Cdd:PRK09088 86 LDALLQDAEPRLLLGDDAVAAGRTDVED-----LAAFIASA--DALEPADTPSIPP---ERVS--------------LIL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 245 YTSGTTGLPKAAIVvhSRYYRMAALVYYGFRMR-PNDIVYDC-LPLYHSAGNIVGIGQCLLHGMTVVIRKKFSASRFWDD 322
Cdd:PRK09088 142 FTSGTSGQPKGVML--SERNLQQTAHNFGVLGRvDAHSSFLCdAPMFHIIGLITSVRPVLAVGGSILVSNGFEPKRTLGR 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 323 CIKYNCTIVQYIG--ELCRYLLNQPpreaenqhqvrmalgnGLRQSIWTNFSSRFH-----------------IPqVAEF 383
Cdd:PRK09088 220 LGDPALGITHYFCvpQMAQAFRAQP----------------GFDAAALRHLTALFTggaphaaedilgwlddgIP-MVDG 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 384 YGATECNCSLGN------FDSQVGACGFNSrilsfvyPIRLVRVNEDtmeliRGPDgvcipCQPGEPGQLvgrIIQKDPL 457
Cdd:PRK09088 283 FGMSEAGTVFGMsvdcdvIRAKAGAAGIPT-------PTVQTRVVDD-----QGND-----CPAGVPGEL---LLRGPNL 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 458 rrFDGYLNQgannKKIAKDVFKkGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLDMADVAVY 537
Cdd:PRK09088 343 --SPGYWRR----PQATARAFT-GDGWFRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVV 415
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 40807357 538 GVEVP--GTEGRAgmAAVASPTGNCDLERFAQVLEKELPLYARPIFLRLLPELHKTGTYKFQKTELR 602
Cdd:PRK09088 416 GMADAqwGEVGYL--AIVPADGAPLDLERIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARLR 480
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
74-604 |
4.75e-24 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 106.68 E-value: 4.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 74 RTVPILFASTVRRHPDKTALI----FEGTDTHWTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKL 149
Cdd:PRK13295 24 RTINDDLDACVASCPDKTAVTavrlGTGAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 150 GVEAALINTNLRRDALLHCLTTSRARALVF-----GSEMASAICEVHASLdPSLS--LFCSG----SWEPGAVPPSTEhL 218
Cdd:PRK13295 104 GAVLNPLMPIFRERELSFMLKHAESKVLVVpktfrGFDHAAMARRLRPEL-PALRhvVVVGGdgadSFEALLITPAWE-Q 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 219 DPllkDAPKHLPS-CPDKgfTDKLFYIYTSGTTGLPKAaiVVHSRYYRMAALVYYGFRMR--PNDIVYDCLPLYHSAGNI 295
Cdd:PRK13295 182 EP---DAPAILARlRPGP--DDVTQLIYTSGTTGEPKG--VMHTANTLMANIVPYAERLGlgADDVILMASPMAHQTGFM 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 296 VGIGQCLLHGMTVVIRKKFSASRFWD----DCIKYNCTIVQYIGELCRyllnQPPREAENQHQVRMALGNG------LRQ 365
Cdd:PRK13295 255 YGLMMPVMLGATAVLQDIWDPARAAElirtEGVTFTMASTPFLTDLTR----AVKESGRPVSSLRTFLCAGapipgaLVE 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 366 SIWTNFSSRfhipqVAEFYGATECNC----SLGNFDSQVGAcgfnsrilSFVYPIRLVRVNedtmelIRGPDGVCIPcqP 441
Cdd:PRK13295 331 RARAALGAK-----IVSAWGMTENGAvtltKLDDPDERAST--------TDGCPLPGVEVR------VVDADGAPLP--A 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 442 GEPGQLVGRiiqkdPLRRFDGYLNQGANNKKIAKDVFKKGDQAYLTGDvlvmdelGYLYFRDRTGDTFRWKGENVSTTEV 521
Cdd:PRK13295 390 GQIGRLQVR-----GCSNFGGYLKRPQLNGTDADGWFDTGDLARIDAD-------GYIRISGRSKDVIIRGGENIPVVEI 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 522 EGTLSRLLDMADVAVYGVEVPGTEGRAGMAAVASPTGNCDLERFAQVL-EKELPLYARPIFLRLLPELHKTGTYKFQKTE 600
Cdd:PRK13295 458 EALLYRHPAIAQVAIVAYPDERLGERACAFVVPRPGQSLDFEEMVEFLkAQKVAKQYIPERLVVRDALPRTPSGKIQKFR 537
|
....
gi 40807357 601 LRKE 604
Cdd:PRK13295 538 LREM 541
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
89-603 |
2.43e-23 |
|
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: 103.14 E-value: 2.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 89 DKTALIFEGTDThwTFRQLDEYSSSVANFLQARG-LASGDVAAIFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALLH 167
Cdd:cd05941 1 DRIAIVDDGDSI--TYADLVARAARLANRLLALGkDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 168 CLTTSraralvfgsemasaicevhaslDPSLslfcsgswepgavppstehldpLLKDApkhlpscpdkgftdklFYIYTS 247
Cdd:cd05941 79 VITDS----------------------EPSL----------------------VLDPA----------------LILYTS 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 248 GTTGLPKAAIVVHSRYYRMA-ALVYYgFRMRPNDIVYDCLPLYHSAGNIVGIGQCLLHGMTVVIRKKFSASRFWDDCIKY 326
Cdd:cd05941 99 GTTGRPKGVVLTHANLAANVrALVDA-WRWTEDDVLLHVLPLHHVHGLVNALLCPLFAGASVEFLPKFDPKEVAISRLMP 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 327 NCTIVQYIGELCRYLLNQPPREAENQHQVRMALGNGLRQSI-------------WTNFSSRFhipqVAEFYGATECNCSL 393
Cdd:cd05941 178 SITVFMGVPTIYTRLLQYYEAHFTDPQFARAAAAERLRLMVsgsaalpvptleeWEAITGHT----LLERYGMTEIGMAL 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 394 GN---FDSQVGACGFNsriLSFVYpirlVRVNEDTmelirgpdgvciPCQPGEPGQlVGRIIQKDPlRRFDGYLNqganN 470
Cdd:cd05941 254 SNpldGERRPGTVGMP---LPGVQ----ARIVDEE------------TGEPLPRGE-VGEIQVRGP-SVFKEYWN----K 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 471 KKIAKDVFKkGDQAYLTGDVLVMDELGYLYFRDRTG-DTFRWKGENVSTTEVEGTLSRLLDMADVAVYGVEVPgTEGRAG 549
Cdd:cd05941 309 PEATKEEFT-DDGWFKTGDLGVVDEDGYYWILGRSSvDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDP-DWGERV 386
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 40807357 550 MAAVA--SPTGNCDLERFAQVLEKELPLYARPIFLRLLPELHKTGTYKFQKTELRK 603
Cdd:cd05941 387 VAVVVlrAGAAALSLEELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
72-538 |
3.30e-23 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 104.03 E-value: 3.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 72 ERRTVPILFASTVRRHPDKTALIF--EGTDTHWTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKL 149
Cdd:COG1022 9 PADTLPDLLRRRAARFPDRVALREkeDGIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 150 GVEAALINTNLRRDALLHCLTTSRARALVFGS-EMASAICEVHASLdPSLS-LFCsgsWEPGAVP--PSTEHLDPLLK-- 223
Cdd:COG1022 89 GAVTVPIYPTSSAEEVAYILNDSGAKVLFVEDqEQLDKLLEVRDEL-PSLRhIVV---LDPRGLRddPRLLSLDELLAlg 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 224 ---DAPKHLPSCPDKGFTDKLF-YIYTSGTTGLPKAAIVVHSRYYRMAALVYYGFRMRPNDIVYDCLPLYHSAGNIVGIG 299
Cdd:COG1022 165 revADPAELEARRAAVKPDDLAtIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFLPLAHVFERTVSYY 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 300 qCLLHGMTVV---------------------------------IRKKFSASRFW---------DDCIKYNCTIVQyiGEl 337
Cdd:COG1022 245 -ALAAGATVAfaespdtlaedlrevkptfmlavprvwekvyagIQAKAEEAGGLkrklfrwalAVGRRYARARLA--GK- 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 338 cryllnQPPREAENQHQ---------VRMALGNGLRQSIwT----------NFssrFH---IPqVAEFYGATE------C 389
Cdd:COG1022 321 ------SPSLLLRLKHAladklvfskLREALGGRLRFAV-SggaalgpelaRF---FRalgIP-VLEGYGLTEtspvitV 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 390 NcSLGNFDsqVGACGfnsRILSFVYpirlVRVNEDTmE-LIRGPdGVcipcqpgepgqlvgriiqkdplrrFDGYLNqga 468
Cdd:COG1022 390 N-RPGDNR--IGTVG---PPLPGVE----VKIAEDG-EiLVRGP-NV------------------------MKGYYK--- 430
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 40807357 469 NNKKIAKDVFKKGdqaYL-TGDVLVMDELGYLYFRDRTGDTFrwK---GENVSTTEVEGTL--SRLLDmaDVAVYG 538
Cdd:COG1022 431 NPEATAEAFDADG---WLhTGDIGELDEDGFLRITGRKKDLI--VtsgGKNVAPQPIENALkaSPLIE--QAVVVG 499
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
77-603 |
1.00e-22 |
|
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: 101.99 E-value: 1.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 77 PILF---ASTVrrHPDKTALIFEgtDTHWTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGVEA 153
Cdd:cd12118 6 PLSFlerAAAV--YPDRTSIVYG--DRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 154 ALINTNLRRDALLHCLTTSRARALVFGSEMASAicEVHASLDPSlslfcsgswePGAVPPSTEHldpllkdapkhlpscp 233
Cdd:cd12118 82 NALNTRLDAEEIAFILRHSEAKVLFVDREFEYE--DLLAEGDPD----------FEWIPPADEW---------------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 234 dkgftDKLFYIYTSGTTGLPKAAIVVHSRYYRMAALVYYGFRMRPNDiVYDC-LPLYHSAGnivgigQCLLHGM-----T 307
Cdd:cd12118 134 -----DPIALNYTSGTTGRPKGVVYHHRGAYLNALANILEWEMKQHP-VYLWtLPMFHCNG------WCFPWTVaavggT 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 308 VVIRKKFSASRFWDDCIKYNCTivqyigELC------RYLLNQPPREAEN-QHQVRMALGN--------GLRQSIwtnfs 372
Cdd:cd12118 202 NVCLRKVDAKAIYDLIEKHKVT------HFCgaptvlNMLANAPPSDARPlPHRVHVMTAGapppaavlAKMEEL----- 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 373 sRFHIPQV---AEFYG-ATEC------------NCSLGNFDSQVGACGFNsrilsfvyPIRLVrvNEDTMELIRGpDGVC 436
Cdd:cd12118 271 -GFDVTHVyglTETYGpATVCawkpewdelpteERARLKARQGVRYVGLE--------EVDVL--DPETMKPVPR-DGKT 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 437 IpcqpgepGQLV--GRIIQKdplrrfdGYLNqganNKKIAKDVFKKGdqAYLTGDVLVMDELGYLYFRDRTGDTFRWKGE 514
Cdd:cd12118 339 I-------GEIVfrGNIVMK-------GYLK----NPEATAEAFRGG--WFHSGDLAVIHPDGYIEIKDRSKDIIISGGE 398
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 515 NVSTTEVEGTLSRLLDMADVAVYGV------EVPgtegragMAAVAsptgncdLERFAQVLEKELPLYARpiflRLLP-- 586
Cdd:cd12118 399 NISSVEVEGVLYKHPAVLEAAVVARpdekwgEVP-------CAFVE-------LKEGAKVTEEEIIAFCR----EHLAgf 460
|
570 580
....*....|....*....|....*.
gi 40807357 587 ---------ELHKTGTYKFQKTELRK 603
Cdd:cd12118 461 mvpktvvfgELPKTSTGKIQKFVLRD 486
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
84-539 |
4.25e-22 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 100.35 E-value: 4.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 84 VRRHPDKTALIFEGTDTHWTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGVEAALINTnlrrd 163
Cdd:PRK05852 26 ATRLPEAPALVVTADRIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDP----- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 164 ALLHCLTTSRARAlvfgsemASAICEVHASLDPSLSLFCSGSWEPGAV------PPSTEHLDPLLKD--APKHLPSCPDK 235
Cdd:PRK05852 101 ALPIAEQRVRSQA-------AGARVVLIDADGPHDRAEPTTRWWPLTVnvggdsGPSGGTLSVHLDAatEPTPATSTPEG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 236 GFTDKLFYIYTSGTTGLPKAAIVVHSRYYRMAALVYYGFRMRPNDIVYDCLPLYHSAGNIVGIGQCLLHGMTVVI--RKK 313
Cdd:PRK05852 174 LRPDDAMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHGHGLIAALLATLASGGAVLLpaRGR 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 314 FSASRFWDDCIKYNCTIVQYIGELCRYLLNQPPREA--ENQHQVRM--ALGNGLRQSIWTNFSSRFHIPqVAEFYGATEC 389
Cdd:PRK05852 254 FSAHTFWDDIKAVGATWYTAVPTIHQILLERAATEPsgRKPAALRFirSCSAPLTAETAQALQTEFAAP-VVCAFGMTEA 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 390 NCSLGNFDSQVGACGFNSRILSFVypirlvrVNEDTMELIR--GPDGvcIPCQPGEPGQ--LVGRIIQKdplrrfdGYLn 465
Cdd:PRK05852 333 THQVTTTQIEGIGQTENPVVSTGL-------VGRSTGAQIRivGSDG--LPLPAGAVGEvwLRGTTVVR-------GYL- 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 40807357 466 qgaNNKKIAKDVFKKGdqAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLDMADVAVYGV 539
Cdd:PRK05852 396 ---GDPTITAANFTDG--WLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGV 464
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
80-588 |
5.79e-22 |
|
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: 99.73 E-value: 5.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 80 FASTVRRHPDKTALIFEGTdtHWTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGVEAALINTN 159
Cdd:cd17651 1 FERQAARTPDAPALVAEGR--RLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 160 LRRDALLHCLTTSRARALVfgsemasaiceVHASLDPSLSLfcsgswEPGAVPPSTEHLDPLLKDAPKHLPSCPDkgftD 239
Cdd:cd17651 79 YPAERLAFMLADAGPVLVL-----------THPALAGELAV------ELVAVTLLDQPGAAAGADAEPDPALDAD----D 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 240 KLFYIYTSGTTGLPKAAIVVHsryyRMAA-LVYYGFRmrpndiVYDCLPLYHSAgNIVGIG---------QCLLHGMTVV 309
Cdd:cd17651 138 LAYVIYTSGSTGRPKGVVMPH----RSLAnLVAWQAR------ASSLGPGARTL-QFAGLGfdvsvqeifSTLCAGATLV 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 310 IRK---KFSASRFWDDCIKYNCTIVQYIGELCRYLLNQPPReaenqHQVRMAlgnGLRQSIWTNFSSRFHiPQVAEF--- 383
Cdd:cd17651 207 LPPeevRTDPPALAAWLDEQRISRVFLPTVALRALAEHGRP-----LGVRLA---ALRYLLTGGEQLVLT-EDLREFcag 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 384 ---------YGATECN-CSLGNFDSQVGACGfnsRILSFVYPIRLVRVnedtmeliRGPDGVCIPCQPGEPGQLvgrIIQ 453
Cdd:cd17651 278 lpglrlhnhYGPTETHvVTALSLPGDPAAWP---APPPIGRPIDNTRV--------YVLDAALRPVPPGVPGEL---YIG 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 454 KDPLRRfdGYLNQ-GANNKKIAKDVFKKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLDMA 532
Cdd:cd17651 344 GAGLAR--GYLNRpELTAERFVPDPFVPGARMYRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVR 421
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 40807357 533 DVAVYGVEVPGTEGRAGMAAVASPTGNCDLERFAQVLEKELPLYARPIFLRLLPEL 588
Cdd:cd17651 422 EAVVLAREDRPGEKRLVAYVVGDPEAPVDAAELRAALATHLPEYMVPSAFVLLDAL 477
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
85-604 |
7.57e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 99.73 E-value: 7.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 85 RRHPDKTALIFEGTDThwTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGVEAALINTNLRRDA 164
Cdd:PRK06178 44 RERPQRPAIIFYGHVI--TYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 165 LLHCLTTSRARALVFG---SEMASAICE-------VHASL------DPSLSLFCSGSwEPGAVPPSTEHLDPLLKDAPKH 228
Cdd:PRK06178 122 LSYELNDAGAEVLLALdqlAPVVEQVRAetslrhvIVTSLadvlpaEPTLPLPDSLR-APRLAAAGAIDLLPALRACTAP 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 229 LPSCPdkGFTDKLFYI-YTSGTTGLPKAaiVVHSR---YYRMAALVYYGFRMRPNDIVYDCLPLYHSAGNIVGIGQCLLH 304
Cdd:PRK06178 201 VPLPP--PALDALAALnYTGGTTGMPKG--CEHTQrdmVYTAAAAYAVAVVGGEDSVFLSFLPEFWIAGENFGLLFPLFS 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 305 GMTVVIRKKFSASRFWDDCIKYNCTIVQYIGELCRYLLNQP---PREAENQHQVRMA-----LGNGLRQSiWTNFSSRFh 376
Cdd:PRK06178 277 GATLVLLARWDAVAFMAAVERYRVTRTVMLVDNAVELMDHPrfaEYDLSSLRQVRVVsfvkkLNPDYRQR-WRALTGSV- 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 377 ipqVAEF-YGATECNCSlgnfDSQvgACGFnsrilsfvypirlvrvNEDTMELIRGPDGVCIPCqPG--------EPGQL 447
Cdd:PRK06178 355 ---LAEAaWGMTETHTC----DTF--TAGF----------------QDDDFDLLSQPVFVGLPV-PGtefkicdfETGEL 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 448 V-----GRIIQKDPlRRFDGYLNQGANNkkiaKDVFKKGdqAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVE 522
Cdd:PRK06178 409 LplgaeGEIVVRTP-SLLKGYWNKPEAT----AEALRDG--WLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVE 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 523 GTLSRLLDMADVAVygveVPGTEGRAGMAAVA----SPTGNCDLERFAQVLEKELPLYARPIfLRLLPELHKTGTYKFQK 598
Cdd:PRK06178 482 ALLGQHPAVLGSAV----VGRPDPDKGQVPVAfvqlKPGADLTAAALQAWCRENMAVYKVPE-IRIVDALPMTATGKVRK 556
|
....*.
gi 40807357 599 TELRKE 604
Cdd:PRK06178 557 QDLQAL 562
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
99-602 |
8.57e-22 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 99.39 E-value: 8.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 99 DTHWTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALLHCLTTSRARALV 178
Cdd:PRK12406 9 DRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 179 FGSEMASAICEVhasLDPSLSLFCSG-----------SWEPGAVPPSTEHLDPLLKD-APKHLPSCPDKGFTdklfyIYT 246
Cdd:PRK12406 89 AHADLLHGLASA---LPAGVTVLSVPtppeiaaayriSPALLTPPAGAIDWEGWLAQqEPYDGPPVPQPQSM-----IYT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 247 SGTTGLPK-----AAIVVHSRYY-RMAALVyYGFrmRPNDIVYDCLPLYHSAGNIVGIgQCLLHGMTVVIRKKFSASRFW 320
Cdd:PRK12406 161 SGTTGHPKgvrraAPTPEQAAAAeQMRALI-YGL--KPGIRALLTGPLYHSAPNAYGL-RAGRLGGVLVLQPRFDPEELL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 321 DDCIKYNCTIVQYIGELCRYLLNQPP--REAENQHQVRMALGNGL-------RQSI--WTnfssrfhiPQVAEFYGATEc 389
Cdd:PRK12406 237 QLIERHRITHMHMVPTMFIRLLKLPEevRAKYDVSSLRHVIHAAApcpadvkRAMIewWG--------PVIYEYYGSTE- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 390 ncslgnfdsqVGACGFNSRILSFVYPIRLVRVNEDTMELIRGPDGVCIPcqPGEPGQLVGRIIQKDPLRrfdgYLNQGAN 469
Cdd:PRK12406 308 ----------SGAVTFATSEDALSHPGTVGKAAPGAELRFVDEDGRPLP--QGEIGEIYSRIAGNPDFT----YHNKPEK 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 470 NKKIAKDVFkkgdqaYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLDMADVAVYGveVPGTE-GRA 548
Cdd:PRK12406 372 RAEIDRGGF------ITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFG--IPDAEfGEA 443
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 40807357 549 GMAAV-ASPTGNCDLERFAQVLEKELPLYARPIFLRLLPELHKTGTYKFQKTELR 602
Cdd:PRK12406 444 LMAVVePQPGATLDEADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLR 498
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
72-595 |
3.74e-21 |
|
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: 98.78 E-value: 3.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 72 ERRTVPILFASTVRRHPDKTALIFEgtDTHWTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEF-VGLwLGMAKLG 150
Cdd:COG1020 474 ADATLHELFEAQAARTPDAVAVVFG--DQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMvVAL-LAVLKAG 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 151 veAAL--INTNLRRDALLHCLTTSRARALVfgsemasaiceVHASLDPSLSlfcsgswePGAVPpsTEHLD-PLLKDAPK 227
Cdd:COG1020 551 --AAYvpLDPAYPAERLAYMLEDAGARLVL-----------TQSALAARLP--------ELGVP--VLALDaLALAAEPA 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 228 HLPSCPDKGftDKLFY-IYTSGTTGLPKAAIVVHsryyrmAALVYY------GFRMRPNDIVydclPLYH------SAGN 294
Cdd:COG1020 608 TNPPVPVTP--DDLAYvIYTSGSTGRPKGVMVEH------RALVNLlawmqrRYGLGPGDRV----LQFAslsfdaSVWE 675
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 295 IVGigqCLLHGMTVVIRKK---FSASRFWDDCIKYNCTIVQYIGELCRYLLNQPPreaENQHQVRMAL--GNGLRQSIWT 369
Cdd:COG1020 676 IFG---ALLSGATLVLAPPearRDPAALAELLARHRVTVLNLTPSLLRALLDAAP---EALPSLRLVLvgGEALPPELVR 749
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 370 NFSSRFHIPQVAEFYGATECncslgnfdsQVGACgfnsrilsfVYPIRLVRVNEDTMELIRGPDGVCI--------PCQP 441
Cdd:COG1020 750 RWRARLPGARLVNLYGPTET---------TVDST---------YYEVTPPDADGGSVPIGRPIANTRVyvldahlqPVPV 811
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 442 GEPGQL------VGRiiqkdplrrfdGYLNQ-GANNKK-IAKDVFKKGDQAYLTGDVLVMDELGYLYFRDRTgDT----- 508
Cdd:COG1020 812 GVPGELyiggagLAR-----------GYLNRpELTAERfVADPFGFPGARLYRTGDLARWLPDGNLEFLGRA-DDqvkir 879
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 509 -FRwkgenVSTTEVEGTLSRLLDMADVAVYGVEVPGTEGRAGMAAVASPTGNCDLERFAQVLEKELPLYARPIFLRLLPE 587
Cdd:COG1020 880 gFR-----IELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAALLRLALALLLPPYMVPAAVVLLLP 954
|
....*...
gi 40807357 588 LHKTGTYK 595
Cdd:COG1020 955 LPLTGNGK 962
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
245-602 |
3.88e-21 |
|
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: 95.42 E-value: 3.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 245 YTSGTTGLPKAAIVVHSRYYRMAALVyyGFRMR--PNDIVYDCLPLYHSAGNIVGIGQCLLHGMTVVI-RKKFSASRFWD 321
Cdd:cd05917 9 FTSGTTGSPKGATLTHHNIVNNGYFI--GERLGltEQDRLCIPVPLFHCFGSVLGVLACLTHGATMVFpSPSFDPLAVLE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 322 DCIKYNCTIVQ-----YIGElcrylLNQPPREAENQHQVRMALGNG-------LRQSIwtnfsSRFHIPQVAEFYGATEc 389
Cdd:cd05917 87 AIEKEKCTALHgvptmFIAE-----LEHPDFDKFDLSSLRTGIMAGapcppelMKRVI-----EVMNMKDVTIAYGMTE- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 390 nCSLGNFDSQVGAcGFNSRILSfvypirLVRVNEDTMELIRGPDGVCIPcQPGEPGQLV--GRIIQKdplrrfdGYLNqg 467
Cdd:cd05917 156 -TSPVSTQTRTDD-SIEKRVNT------VGRIMPHTEAKIVDPEGGIVP-PVGVPGELCirGYSVMK-------GYWN-- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 468 aNNKKIAKDVfkKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLDMADVAVYGVEVPgTEGR 547
Cdd:cd05917 218 -DPEKTAEAI--DGDGWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDE-RYGE 293
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 40807357 548 AGMAAVAsptgncdLERFAQVLEKELPLYAR--------PIFLRLLPELHKTGTYKFQKTELR 602
Cdd:cd05917 294 EVCAWIR-------LKEGAELTEEDIKAYCKgkiahykvPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
84-544 |
4.84e-21 |
|
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: 97.26 E-value: 4.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 84 VRRHPDKTALIFEGTDT----HWTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGVEAALINTN 159
Cdd:cd17634 63 LRENGDRTAIIYEGDDTsqsrTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGG 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 160 LRRDALLHCLTTSRARALVFGSE------------MASAICEVHA-SLDPSLSLFCSGS---WEPGAvppSTEHLDPLLK 223
Cdd:cd17634 143 FAPEAVAGRIIDSSSRLLITADGgvragrsvplkkNVDDALNPNVtSVEHVIVLKRTGSdidWQEGR---DLWWRDLIAK 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 224 DAPKHLPSCPDKgfTDKLFYIYTSGTTGLPKAAIVVHSRYYRMAALVY-YGFRMRPNDIVYDCLPLYHSAGNIVGIGQCL 302
Cdd:cd17634 220 ASPEHQPEAMNA--EDPLFILYTSGTTGKPKGVLHTTGGYLVYAATTMkYVFDYGPGDIYWCTADVGWVTGHSYLLYGPL 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 303 LHGMTVVIRKKF----SASRFWDDCIKYNCTIVQYIGELCRYLLNQPPREAENQH----QVRMALGNGLRQSIWTNFSSR 374
Cdd:cd17634 298 ACGATTLLYEGVpnwpTPARMWQVVDKHGVNILYTAPTAIRALMAAGDDAIEGTDrsslRILGSVGEPINPEAYEWYWKK 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 375 FHIPQ--VAEFYGATE----CNCSLGNFDSQVGACGFNSrilsfVYPIRLVRVNEdtmeliRGpdgvcipcQPGEPGQlV 448
Cdd:cd17634 378 IGKEKcpVVDTWWQTEtggfMITPLPGAIELKAGSATRP-----VFGVQPAVVDN------EG--------HPQPGGT-E 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 449 GRIIQKDP--------LRRFDGYLnqgannkkiaKDVFKKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTE 520
Cdd:cd17634 438 GNLVITDPwpgqtrtlFGDHERFE----------QTYFSTFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAE 507
|
490 500
....*....|....*....|....*.
gi 40807357 521 VEGTLSRLLDMADVAVYGV--EVPGT 544
Cdd:cd17634 508 IESVLVAHPKVAEAAVVGIphAIKGQ 533
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
85-527 |
4.91e-21 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 96.95 E-value: 4.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 85 RRHPDKTALIFEGTDThwTFRQLDEYSSSVANFLQAR-GLASGDVAAIFMENRNEFVGLWLGMAKLGVEAALINTNLRRD 163
Cdd:PRK08314 21 RRYPDKTAIVFYGRAI--SYRELLEEAERLAGYLQQEcGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 164 ALLHCLTTSRARALVFGSEMASAICEVHASLdpSLSLFCSGSWEpGAVPPSTEHLDPLLKDAPKHLPSCPDKGFT----- 238
Cdd:PRK08314 99 ELAHYVTDSGARVAIVGSELAPKVAPAVGNL--RLRHVIVAQYS-DYLPAEPEIAVPAWLRAEPPLQALAPGGVVawkea 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 239 --------------DKLFYI-YTSGTTGLPKAAIVVHSRYYRMAALVYYGFRMRPNDIVYDCLPLYHSAGNIVGIGQCLL 303
Cdd:PRK08314 176 laaglappphtagpDDLAVLpYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVLPLFHVTGMVHSMNAPIY 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 304 HGMTVVIrkkfsASRfWD-----DCI-KYNCTIVQYIGELCRYLLNQPPREAENQHQVRMALGNG--LRQSIWTNFSSRF 375
Cdd:PRK08314 256 AGATVVL-----MPR-WDreaaaRLIeRYRVTHWTNIPTMVVDFLASPGLAERDLSSLRYIGGGGaaMPEAVAERLKELT 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 376 HIPQVaEFYGATEC--------------NCsLGnfdsqVGACGFNSRIlsfvypirlvrVNEDTMElirgpdgvciPCQP 441
Cdd:PRK08314 330 GLDYV-EGYGLTETmaqthsnppdrpklQC-LG-----IPTFGVDARV-----------IDPETLE----------ELPP 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 442 GEpgqlVGRIIQKDPlRRFDGYLNQGANNKK--IAKDvfkkGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTT 519
Cdd:PRK08314 382 GE----VGEIVVHGP-QVFKGYWNRPEATAEafIEID----GKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPA 452
|
....*...
gi 40807357 520 EVEGTLSR 527
Cdd:PRK08314 453 EVENLLYK 460
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
85-602 |
1.00e-20 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 95.85 E-value: 1.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 85 RRHPDKTALIFEGTDTHWTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNE-FVGLWLGMaKLGVEAALINTNLRRD 163
Cdd:PRK13390 8 QIAPDRPAVIVAETGEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEaLVVLWAAL-RSGLYITAINHHLTAP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 164 ALLHCLTTSRARALVFGSEMASAICEVHASLDPSLSLFCS----GSWE---PGAVPPSTEHldpllkdapkhlpSCpdkg 236
Cdd:PRK13390 87 EADYIVGDSGARVLVASAALDGLAAKVGADLPLRLSFGGEidgfGSFEaalAGAGPRLTEQ-------------PC---- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 237 ftdKLFYIYTSGTTGLPKA------AIVVHSRYYRMAALVYYGFRMRPNDIVYDCLPLYHSAgnivGIGQC-LLH--GMT 307
Cdd:PRK13390 150 ---GAVMLYSSGTTGFPKGiqpdlpGRDVDAPGDPIVAIARAFYDISESDIYYSSAPIYHAA----PLRWCsMVHalGGT 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 308 VVIRKKFSASRFWDDCIKYNCTIVQYIGEL-CRYL-LNQPPREAENQHQVRMALGNG------LRQSI--WTNfssrfhi 377
Cdd:PRK13390 223 VVLAKRFDAQATLGHVERYRITVTQMVPTMfVRLLkLDADVRTRYDVSSLRAVIHAAapcpvdVKHAMidWLG------- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 378 PQVAEFYGATECN----CSLGNFDSQVGACGfnSRILSFVYpirlvrvnedtmelIRGPDGVCIPCqpGEPGQLVgriIQ 453
Cdd:PRK13390 296 PIVYEYYSSTEAHgmtfIDSPDWLAHPGSVG--RSVLGDLH--------------ICDDDGNELPA--GRIGTVY---FE 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 454 KD--PLRrfdgYLNqgaNNKKIAKDVFKKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLDM 531
Cdd:PRK13390 355 RDrlPFR----YLN---DPEKTAAAQHPAHPFWTTVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAV 427
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 40807357 532 ADVAVYGVEVP--GTEGRAGMAAVASPTGNCDLER-FAQVLEKELPLYARPIFLRLLPELHKTGTYKFQKTELR 602
Cdd:PRK13390 428 HDVAVIGVPDPemGEQVKAVIQLVEGIRGSDELAReLIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
103-595 |
1.07e-20 |
|
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: 95.24 E-value: 1.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 103 TFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALLHCLTTSRARALVFGSE 182
Cdd:cd05935 3 TYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGSE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 183 MasaicevhasldpslslfcsgswepgavppstehldpllkdapkhlpscpdkgftDKLFYI-YTSGTTGLPKAAIVVHS 261
Cdd:cd05935 83 L-------------------------------------------------------DDLALIpYTSGTTGLPKGCMHTHF 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 262 RYYRMAALVYYGFRMRPNDIVYDCLPLYHSAGNIVGIGQCLLHGMTVVIRKKFSASRFWDDCIKYNCTIVQYIGELCRYL 341
Cdd:cd05935 108 SAAANALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMARWDRETALELIEKYKVTFWTNIPTMLVDL 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 342 LNQPPREAENQHQVRMALGNG--LRQSIWTNFSSRFHIPQVaEFYGATEcNCS------LGNFDSQ---VGACGFNSRIL 410
Cdd:cd05935 188 LATPEFKTRDLSSLKVLTGGGapMPPAVAEKLLKLTGLRFV-EGYGLTE-TMSqthtnpPLRPKLQclgIP*FGVDARVI 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 411 SFvypirlvrvnEDTMELirgPDGVcipcqpgepgqlVGRIIQKDPlRRFDGYLNQGANNKKIAKDVfkKGDQAYLTGDV 490
Cdd:cd05935 266 DI----------ETGREL---PPNE------------VGEIVVRGP-QIFKGYWNRPEETEESFIEI--KGRRFFRTGDL 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 491 LVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLDMADVAVYGV--EVPGTEGRAGMAAVASPTGNCDLERFAQV 568
Cdd:cd05935 318 GYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVpdERVGEEVKAFIVLRPEYRGKVTEEDIIEW 397
|
490 500
....*....|....*....|....*..
gi 40807357 569 LEKELPLYARPIFLRLLPELHKTGTYK 595
Cdd:cd05935 398 AREQMAAYKYPREVEFVDELPRSASGK 424
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
79-601 |
1.72e-20 |
|
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: 94.96 E-value: 1.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 79 LFASTVRRHPDKTALIFEGTDthWTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGVEAALINT 158
Cdd:cd12117 2 LFEEQAARTPDAVAVVYGDRS--LTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 159 NLRRDALLHCLTTSRARALVfgsemasaiceVHASLDPSLSlfcsgswEPGAVPPSTEHLDPLLKDAPKHlPSCPDkgft 238
Cdd:cd12117 80 ELPAERLAFMLADAGAKVLL-----------TDRSLAGRAG-------GLEVAVVIDEALDAGPAGNPAV-PVSPD---- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 239 DKLFYIYTSGTTGLPKAAIVVHSRYYRMAALVYYGfRMRPNDIVYDCLPLYHSAG--NIVGigqCLLHGMTVVIRKK--- 313
Cdd:cd12117 137 DLAYVMYTSGSTGRPKGVAVTHRGVVRLVKNTNYV-TLGPDDRVLQTSPLAFDAStfEIWG---ALLNGARLVLAPKgtl 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 314 FSASRFWDDCIKYNCTIVQYIGELCRYLLNQPPR------------EAENQHQVRMALGNGLRQSIW--------TNFSS 373
Cdd:cd12117 213 LDPDALGALIAEEGVTVLWLTAALFNQLADEDPEcfaglrelltggEVVSPPHVRRVLAACPGLRLVngygptenTTFTT 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 374 RFHIPQVAEFYGATECNCSLGNfdSQVgacgfnsRILsfvypirlvrvnedtmelirgpDGVCIPCQPGEPGQLVgriIQ 453
Cdd:cd12117 293 SHVVTELDEVAGSIPIGRPIAN--TRV-------YVL----------------------DEDGRPVPPGVPGELY---VG 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 454 KDPLRRfdGYLNQGA-NNKKIAKDVFKKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLDMA 532
Cdd:cd12117 339 GDGLAL--GYLNRPAlTAERFVADPFGPGERLYRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVR 416
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 40807357 533 DVAVygVEVPGTEGRAGMAAVASPTGNCDLERFAQVLEKELPLYARPIFLRLLPELHKTGTYKFQKTEL 601
Cdd:cd12117 417 EAVV--VVREDAGGDKRLVAYVVAEGALDAAELRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
241-587 |
4.26e-20 |
|
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: 91.70 E-value: 4.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 241 LFYI-YTSGTTGLPKAaivvhsrYYR-----MAALVY--YGFRMRPNDIVYDCLPLYHSaGNIVGIGQCLLHGMTVVIRK 312
Cdd:cd17633 2 PFYIgFTSGTTGLPKA-------YYRserswIESFVCneDLFNISGEDAILAPGPLSHS-LFLYGAISALYLGGTFIGQR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 313 KFSASRFWDDCIKYNCTIVQYIGELCRYLLnqppREAENQHQVRMAL--GNGLRQSIWTNFSSRFHIPQVAEFYGATEcn 390
Cdd:cd17633 74 KFNPKSWIRKINQYNATVIYLVPTMLQALA----RTLEPESKIKSIFssGQKLFESTKKKLKNIFPKANLIEFYGTSE-- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 391 cslgnfdsqvgacgfnsriLSFVypirLVRVNEDTmeliRGPDGVCIPCqPG-------EPGQLVGRIIQKDPLRrFDGY 463
Cdd:cd17633 148 -------------------LSFI----TYNFNQES----RPPNSVGRPF-PNveieirnADGGEIGKIFVKSEMV-FSGY 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 464 LNQGANNKkiakdvfkkgDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLDMADVAVYGVEvpg 543
Cdd:cd17633 199 VRGGFSNP----------DGWMSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIP--- 265
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 40807357 544 tEGRAGMAAVASPTGNC----DLERFaqvLEKELPLYARP---IFLRLLPE 587
Cdd:cd17633 266 -DARFGEIAVALYSGDKltykQLKRF---LKQKLSRYEIPkkiIFVDSLPY 312
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
103-601 |
6.24e-20 |
|
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 162605 [Multi-domain] Cd Length: 436 Bit Score: 92.90 E-value: 6.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 103 TFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGVEAALINTNLrrdallhcltTSRARALVFgse 182
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRL----------TENERTNQL--- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 183 masaicevhASLDPSLsLFCSGSWEPGAVppSTEHLDPLLKDAPKHLPSCPDKGFTDKLFYIYTSGTTGLPKAAIVVHSR 262
Cdd:TIGR01923 68 ---------EDLDVQL-LLTDSLLEEKDF--QADSLDRIEAAGRYETSLSASFNMDQIATLMFTSGTTGKPKAVPHTFRN 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 263 YYRMAALVYYGFRMRPNDIVYDCLPLYHSAGNIVgIGQCLLHGMTVVIRKKFSAsrFWDDCIKYNCTIVQYIGELCRYLL 342
Cdd:TIGR01923 136 HYASAVGSKENLGFTEDDNWLLSLPLYHISGLSI-LFRWLIEGATLRIVDKFNQ--LLEMIANERVTHISLVPTQLNRLL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 343 NQPPREaENQHQVRmaLGNG------LRQSIWTNFSsrfhipqVAEFYGATECNcslgnfdSQVgaCGFNsrilsfvypi 416
Cdd:TIGR01923 213 DEGGHN-ENLRKIL--LGGSaipaplIEEAQQYGLP-------IYLSYGMTETC-------SQV--TTAT---------- 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 417 rlvrvNEDTMEliRGPDGVCIP------CQPGEPGqlVGRIIQKDPLRrFDGYLNQGANNKKIAKD-VFKKGDQAYLTGD 489
Cdd:TIGR01923 264 -----PEMLHA--RPDVGRPLAgreikiKVDNKEG--HGEIMVKGANL-MKGYLYQGELTPAFEQQgWFNTGDIGELDGE 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 490 vlvmdelGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLDMADVAVygveVPGTEGRAGMAAVASPTGNCDL--ERFAQ 567
Cdd:TIGR01923 334 -------GFLYVLGRRDDLIISGGENIYPEEIETVLYQHPGIQEAVV----VPKPDAEWGQVPVAYIVSESDIsqAKLIA 402
|
490 500 510
....*....|....*....|....*....|....
gi 40807357 568 VLEKELPLYARPIFLRLLPELHKTGTYKFQKTEL 601
Cdd:TIGR01923 403 YLTEKLAKYKVPIAFEKLDELPYNASGKILRNQL 436
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
112-602 |
7.31e-20 |
|
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: 92.83 E-value: 7.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 112 SSVANFLQAR--GLASGDVAAIFMENRNEFVGLWLGmakLGVEAALINTNLRRDALLHCLTTSRARALVfgsEMASAICE 189
Cdd:cd05929 7 DRAQVFHQRRllLLDVYSIALNRNARAAAAEGVWIA---DGVYIYLINSILTVFAAAAAWKCGACPAYK---SSRAPRAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 190 VHASLDP-SLSLFCSGSWEPGAvPPSTEHLDPLLKDAPKHLPscPDKGFTDKLFYiyTSGTTGLPKA------AIVVHSR 262
Cdd:cd05929 81 ACAIIEIkAAALVCGLFTGGGA-LDGLEDYEAAEGGSPETPI--EDEAAGWKMLY--SGGTTGRPKGikrglpGGPPDND 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 263 YYRMAALvyyGFRMRPNDIVYDCLPLYHSAGNIVGIGqCLLHGMTVVIRKKFSASRFWDDCIKYNCTIVQYIGELCRYLL 342
Cdd:cd05929 156 TLMAAAL---GFGPGADSVYLSPAPLYHAAPFRWSMT-ALFMGGTLVLMEKFDPEEFLRLIERYRVTFAQFVPTMFVRLL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 343 NQP--PREAENQHQVRMALGNGLRQSIWTNfssRFHI----PQVAEFYGATECN----CSLGNFDSQVGACGfnsrilsf 412
Cdd:cd05929 232 KLPeaVRNAYDLSSLKRVIHAAAPCPPWVK---EQWIdwggPIIWEYYGGTEGQgltiINGEEWLTHPGSVG-------- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 413 vypirlvRVNEDTMElIRGPDGVciPCQPGEPGQlvgrIIQKDPlrrfDGYLNQGANNKKIAKdvFKKGDQAYLtGDVLV 492
Cdd:cd05929 301 -------RAVLGKVH-ILDEDGN--EVPPGEIGE----VYFANG----PGFEYTNDPEKTAAA--RNEGGWSTL-GDVGY 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 493 MDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLDMADVAVYGveVPGTE-GRAGMAAVASptgnCDLERFAQVLEK 571
Cdd:cd05929 360 LDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVG--VPDEElGQRVHAVVQP----APGADAGTALAE 433
|
490 500 510
....*....|....*....|....*....|....*....
gi 40807357 572 ELPLYAR--------PIFLRLLPELHKTGTYKFQKTELR 602
Cdd:cd05929 434 ELIAFLRdrlsrykcPRSIEFVAELPRDDTGKLYRRLLR 472
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
85-602 |
1.34e-19 |
|
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: 92.94 E-value: 1.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 85 RRHPDKTALIFEGTDTH---WTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGVEAALINTNLR 161
Cdd:cd05968 72 ADTRTRPALRWEGEDGTsrtLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFG 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 162 RDALLHCLTTSRARALVF--GSEMASAICEVHASLDpslslfcsgswEPGAVPPSTEHL---------------DPLLKD 224
Cdd:cd05968 152 KEAAATRLQDAEAKALITadGFTRRGREVNLKEEAD-----------KACAQCPTVEKVvvvrhlgndftpakgRDLSYD 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 225 APK--HLPSCPDKGFTDKLFYIYTSGTTGLPKAAIVVHSRYYRMAAL-VYYGFRMRPNDIVYDCLPLYHSAGNIVGIGQc 301
Cdd:cd05968 221 EEKetAGDGAERTESEDPLMIIYTSGTTGKPKGTVHVHAGFPLKAAQdMYFQFDLKPGDLLTWFTDLGWMMGPWLIFGG- 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 302 LLHGMTVVIRKKF----SASRFWDDCIKYNCTIVQYIGELCRYLL--NQPPREAENQHQVRMALGNGlrqSIWTNFSSRF 375
Cdd:cd05968 300 LILGATMVLYDGApdhpKADRLWRMVEDHEITHLGLSPTLIRALKprGDAPVNAHDLSSLRVLGSTG---EPWNPEPWNW 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 376 --------HIPqVAEFYGATECNCS-LGN-FDSQVGACGFNSrilsfVYPIRLVRVNEDTMELIRGPDGVCIPCQPGePG 445
Cdd:cd05968 377 lfetvgkgRNP-IINYSGGTEISGGiLGNvLIKPIKPSSFNG-----PVPGMKADVLDESGKPARPEVGELVLLAPW-PG 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 446 QLVGriIQKDPLRRFDGYlnqgannkkiakdvFKKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTL 525
Cdd:cd05968 450 MTRG--FWRDEDRYLETY--------------WSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVL 513
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 526 SRLLDMADVAVYGVEVPgTEGRAGMAAVASPTGncdlERFAQVLEKEL----------PLyaRPIFLRLLPELHKTGTYK 595
Cdd:cd05968 514 NAHPAVLESAAIGVPHP-VKGEAIVCFVVLKPG----VTPTEALAEELmervadelgkPL--SPERILFVKDLPKTRNAK 586
|
....*..
gi 40807357 596 FQKTELR 602
Cdd:cd05968 587 VMRRVIR 593
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
79-603 |
3.19e-19 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. 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: 91.15 E-value: 3.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 79 LFASTVRRHPDK---TALIfEGTDTHWTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGveAAL 155
Cdd:cd12119 1 LLEHAARLHGDReivSRTH-EGEVHRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMG--AVL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 156 --INTNLRRDALLHCLTTSRARALVFGSEMASAICEVHASLDPSLSLFCSGSWEPGAVP--PSTEHLDPLLKDAPkhlps 231
Cdd:cd12119 78 htINPRLFPEQIAYIINHAEDRVVFVDRDFLPLLEAIAPRLPTVEHVVVMTDDAAMPEPagVGVLAYEELLAAES----- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 232 cPDKGFTDK-------LFYiyTSGTTGLPKA------AIVVHSryyrMAALVYYGFRMRPNDIVYDCLPLYHsaGNIVGI 298
Cdd:cd12119 153 -PEYDWPDFdentaaaICY--TSGTTGNPKGvvyshrSLVLHA----MAALLTDGLGLSESDVVLPVVPMFH--VNAWGL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 299 G-QCLLHGMTVVIRKKFSASRFWDDCIK-YNCTIVQYIGELCRYLLNQPPREAENQHQVRMAL--GNGLRQSIWTNFSSR 374
Cdd:cd12119 224 PyAAAMVGAKLVLPGPYLDPASLAELIErEGVTFAAGVPTVWQGLLDHLEANGRDLSSLRRVVigGSAVPRSLIEAFEER 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 375 fHIPqVAEFYGATEcNCSLGNF----DSQVGACG---FNSRILSfVYPIRLVRVNedtmelIRGPDGVCIPCQPGEPGQL 447
Cdd:cd12119 304 -GVR-VIHAWGMTE-TSPLGTVarppSEHSNLSEdeqLALRAKQ-GRPVPGVELR------IVDDDGRELPWDGKAVGEL 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 448 VGR---IIQkdplrrfdGYLNQGANNKKIAKDVFKKgdqaylTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGT 524
Cdd:cd12119 374 QVRgpwVTK--------SYYKNDEESEALTEDGWLR------TGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENA 439
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 40807357 525 LSRLLDMADVAVYGVEVPGTEGRAGMAAVASPTGNCDLERFAQVLEKELPLYARPIFLRLLPELHKTGTYKFQKTELRK 603
Cdd:cd12119 440 IMAHPAVAEAAVIGVPHPKWGERPLAVVVLKEGATVTAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKALRE 518
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
79-543 |
3.52e-19 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 91.27 E-value: 3.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 79 LFASTVRRHPDKTALIFEGTDThwTFRQLDEYSSSVANFLQAR-GLASGDVAAIFMENRnefvgLWLGMAKLGV-EAALI 156
Cdd:PRK08974 28 MFEQAVARYADQPAFINMGEVM--TFRKLEERSRAFAAYLQNGlGLKKGDRVALMMPNL-----LQYPIALFGIlRAGMI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 157 NTNLR-----RDaLLHCLTTSRARALVFGSEMASAICEV-------H---ASLDPSLSlFCSGSWEPGAVppstEHLDPL 221
Cdd:PRK08974 101 VVNVNplytpRE-LEHQLNDSGAKAIVIVSNFAHTLEKVvfktpvkHvilTRMGDQLS-TAKGTLVNFVV----KYIKRL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 222 LkdaPK-HLPSC-----------------PDKGFTDKLFYIYTSGTTGLPKAAIVVHSRY---YRMAALVYYGFRMRPND 280
Cdd:PRK08974 175 V---PKyHLPDAisfrsalhkgrrmqyvkPELVPEDLAFLQYTGGTTGVAKGAMLTHRNMlanLEQAKAAYGPLLHPGKE 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 281 IVYDCLPLYHSAGNIVgigQCLLH----GMTVVIRKKFSASRFWDDCIKYNCTIVQYIGELCRYLLNQPPREAENQHQVR 356
Cdd:PRK08974 252 LVVTALPLYHIFALTV---NCLLFielgGQNLLITNPRDIPGFVKELKKYPFTAITGVNTLFNALLNNEEFQELDFSSLK 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 357 MALGNGL--RQSI---WTNFSSRFHIpqvaEFYGATECN----CSLGNFDSQVGACGFNSrilsfvyPIRLVRVNEDtme 427
Cdd:PRK08974 329 LSVGGGMavQQAVaerWVKLTGQYLL----EGYGLTECSplvsVNPYDLDYYSGSIGLPV-------PSTEIKLVDD--- 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 428 lirgpDGVCIPcqPGEPGQLVGRIIQKdplrrFDGYLNQGANNKKIAKDvfkkgdqAYL-TGDVLVMDELGYLYFRDRTG 506
Cdd:PRK08974 395 -----DGNEVP--PGEPGELWVKGPQV-----MLGYWQRPEATDEVIKD-------GWLaTGDIAVMDEEGFLRIVDRKK 455
|
490 500 510
....*....|....*....|....*....|....*....
gi 40807357 507 DTFRWKGENVSTTEVEGTLSRLLDMADVAVYGV--EVPG 543
Cdd:PRK08974 456 DMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVpsEVSG 494
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
103-603 |
5.58e-19 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 89.88 E-value: 5.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 103 TFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALLHCLTTSRARALVfgse 182
Cdd:cd05973 2 TFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVV---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 183 masaicevhasldpslslfcsgswepgavppstehldpllKDAPKHlpscpDKGFTDKLFYIYTSGTTGLPKAAIVVHSR 262
Cdd:cd05973 78 ----------------------------------------TDAANR-----HKLDSDPFVMMFTSGTTGLPKGVPVPLRA 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 263 YYRMAALVYYGFRMRPNDIVYD------CLPLYHS--AGNIVGIGQCLLHGmtvvirkKFSASRFWDDCIKYNCTIVQYI 334
Cdd:cd05973 113 LAAFGAYLRDAVDLRPEDSFWNaadpgwAYGLYYAitGPLALGHPTILLEG-------GFSVESTWRVIERLGVTNLAGS 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 335 GELCRYLLNQPPrEAENQHQVRM----ALGNGLRQSIWTNFSSRFHIPqVAEFYGATECNCSLGNFDS-----QVGACGf 405
Cdd:cd05973 186 PTAYRLLMAAGA-EVPARPKGRLrrvsSAGEPLTPEVIRWFDAALGVP-IHDHYGQTELGMVLANHHAlehpvHAGSAG- 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 406 nsrilsFVYP-IRLVRVNEDTMELIrgpdgvcipcqPGEPGQLVgrI-IQKDPLRRFDGYlnQGANNKKIAKDVfkkgdq 483
Cdd:cd05973 263 ------RAMPgWRVAVLDDDGDELG-----------PGEPGRLA--IdIANSPLMWFRGY--QLPDTPAIDGGY------ 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 484 aYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLDMADVAVYGV------EV--------PGTEGRAG 549
Cdd:cd05973 316 -YLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVpdpertEVvkafvvlrGGHEGTPA 394
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 40807357 550 MAavasptgncdlERFAQVLEKELPLYARPIFLRLLPELHKTGTYKFQKTELRK 603
Cdd:cd05973 395 LA-----------DELQLHVKKRLSAHAYPRTIHFVDELPKTPSGKIQRFLLRR 437
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
75-563 |
5.62e-19 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 90.83 E-value: 5.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 75 TVPILFASTVRRHPDKTALIFEGTDThwTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGVEAA 154
Cdd:PRK05605 33 TLVDLYDNAVARFGDRPALDFFGATT--TYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 155 LINTNLRRDALLHCLTTSRARALVFGSEMASAICEVHASLDP----SLSLfcsgswePGAVP------------------ 212
Cdd:PRK05605 111 EHNPLYTAHELEHPFEDHGARVAIVWDKVAPTVERLRRTTPLetivSVNM-------IAAMPllqrlalrlpipalrkar 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 213 -------PSTEHLDPLLKDAP---KHLPSCPDKGFTDKLFYIYTSGTTGLPKAAIVVHSRYY---RMAALVYYGFRMRPn 279
Cdd:PRK05605 184 aaltgpaPGTVPWETLVDAAIggdGSDVSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFanaAQGKAWVPGLGDGP- 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 280 DIVYDCLPLYHSAGNIVGIGQCLLHGMTVVIRKKFSASRFWDDCIKYNCTIVQYIGELCRYLLnqppREAENQ----HQV 355
Cdd:PRK05605 263 ERVLAALPMFHAYGLTLCLTLAVSIGGELVLLPAPDIDLILDAMKKHPPTWLPGVPPLYEKIA----EAAEERgvdlSGV 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 356 RMALGNG--LRQSI---WTNFSSRFHIpqvaEFYGATECN-CSLGN---FDSQVGACGfnsriLSFvyPIRLVRVNEdtm 426
Cdd:PRK05605 339 RNAFSGAmaLPVSTvelWEKLTGGLLV----EGYGLTETSpIIVGNpmsDDRRPGYVG-----VPF--PDTEVRIVD--- 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 427 elirgPDGVCIPCQPGEPGQLVGRIIQkdplrRFDGYLNQGANNKKiakdVFKkgDQAYLTGDVLVMDELGYLYFRDR-- 504
Cdd:PRK05605 405 -----PEDPDETMPDGEEGELLVRGPQ-----VFKGYWNRPEETAK----SFL--DGWFRTGDVVVMEEDGFIRIVDRik 468
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 40807357 505 ----TGdtfrwkGENVSTTEVEGTLSRLLDMADVAVYGveVPGTEGRAGMAAVASPTGNCDLE 563
Cdd:PRK05605 469 eliiTG------GFNVYPAEVEEVLREHPGVEDAAVVG--LPREDGSEEVVAAVVLEPGAALD 523
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
79-603 |
7.30e-19 |
|
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: 89.68 E-value: 7.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 79 LFASTVRRHPDKTALifEGTDTHWTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGVEAALINT 158
Cdd:cd17653 2 AFERIAAAHPDAVAV--ESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 159 NLRRDALLHCLTTSRARALVFgsemasaicevhasldpslslfcsgswepgavppstehldpllkdapkhlPSCPDkgft 238
Cdd:cd17653 80 KLPSARIQAILRTSGATLLLT--------------------------------------------------TDSPD---- 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 239 DKLFYIYTSGTTGLPKAAIVVHSRYYRMAALVYYGFRMRPND-------IVYDClplyhSAGNIVGigqCLLHGMTVVIR 311
Cdd:cd17653 106 DLAYIIFTSGSTGIPKGVMVPHRGVLNYVSQPPARLDVGPGSrvaqvlsIAFDA-----CIGEIFS---TLCNGGTLVLA 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 312 kkfSASRFWDDCIK----YNCT--IVQYIgelcryllnqPPREAENQHQVRMAlGNGLRQSIWTNFSSRfhiPQVAEFYG 385
Cdd:cd17653 178 ---DPSDPFAHVARtvdaLMSTpsILSTL----------SPQDFPNLKTIFLG-GEAVPPSLLDRWSPG---RRLYNAYG 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 386 ATECNCSlgnfdsqvgaCGFNS-RILSFV---YPIRLVRV---NEDTMELIRGPDG-VCIpcqpgePGQLVGRiiqkdpl 457
Cdd:cd17653 241 PTECTIS----------STMTElLPGQPVtigKPIPNSTCyilDADLQPVPEGVVGeICI------SGVQVAR------- 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 458 rrfdGYLNQGA-NNKKIAKDVFKKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLDMADVAV 536
Cdd:cd17653 298 ----GYLGNPAlTASKFVPDPFWPGSRMYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEVVLQSQPEVTQAA 373
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 40807357 537 YGVevpgTEGRagMAAVASPTGnCDLERFAQVLEKELPLYARPIFLRLLPELHKTGTYKFQKTELRK 603
Cdd:cd17653 374 AIV----VNGR--LVAFVTPET-VDVDGLRSELAKHLPSYAVPDRIIALDSFPLTANGKVDRKALRE 433
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
79-601 |
1.14e-18 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 89.67 E-value: 1.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 79 LFASTVRRHPDKTALIFEgtDTHWTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGVEAALINT 158
Cdd:PRK13383 40 LLAVTAARWPGRTAIIDD--DGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPIST 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 159 NLRRDALLHCLTTSRARALVFGSEMASAIC---EVHASLDPSlslfCSGSWEPGAVPpstehldpllKDAPkhlpscPDK 235
Cdd:PRK13383 118 EFRSDALAAALRAHHISTVVADNEFAERIAgadDAVAVIDPA----TAGAEESGGRP----------AVAA------PGR 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 236 gftdklFYIYTSGTTGLPKAaiVVHSRYYRMAALVYYGF----RMRPNDIVYDCLPLYHSagniVGIGQCLLH---GMTV 308
Cdd:PRK13383 178 ------IVLLTSGTTGKPKG--VPRAPQLRSAVGVWVTIldrtRLRTGSRISVAMPMFHG----LGLGMLMLTialGGTV 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 309 VIRKKFSASRFWDDCIKYNCTIVQYIGELCRYLLNQPPR-EAEN---QHQVRMALGNGLRQSIWTNFSSRFHiPQVAEFY 384
Cdd:PRK13383 246 LTHRHFDAEAALAQASLHRADAFTAVPVVLARILELPPRvRARNplpQLRVVMSSGDRLDPTLGQRFMDTYG-DILYNGY 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 385 GATEcncslgnfdsqVGacgfnsrILSFVYPIRLvrvnEDTMELIRGPDGVC---IPCQPGEP--GQLVGRIIQKDPLRR 459
Cdd:PRK13383 325 GSTE-----------VG-------IGALATPADL----RDAPETVGKPVAGCpvrILDRNNRPvgPRVTGRIFVGGELAG 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 460 fDGYlnQGANNKKIAKDVFKKGDQAYLtgdvlvmDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLDMADVAVYGV 539
Cdd:PRK13383 383 -TRY--TDGGGKAVVDGMTSTGDMGYL-------DNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGV 452
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 40807357 540 EVPGTEGRAGMAAVASPTGNCDLERFAQVLEKELPLYARPIFLRLLPELHKTGTYKFQKTEL 601
Cdd:PRK13383 453 PDERFGHRLAAFVVLHPGSGVDAAQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
102-542 |
1.75e-18 |
|
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: 88.33 E-value: 1.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 102 WTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALLHCLTTSRARALVFGS 181
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 182 EMAsaicevhasldpslslfcsgswepgavppstEHLDPllkdapkhlpscpdkgfTDKLFYIYTSGTTGLPKAAIVVHS 261
Cdd:cd05969 81 ELY-------------------------------ERTDP-----------------EDPTLLHYTSGTTGTPKGVLHVHD 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 262 RYYRMAALVYYGFRMRPNDIvYDCL--PLYhSAGNIVGIGQCLLHGMTVVIRK-KFSASRfWDDCIKYNCTIVQY----- 333
Cdd:cd05969 113 AMIFYYFTGKYVLDLHPDDI-YWCTadPGW-VTGTVYGIWAPWLNGVTNVVYEgRFDAES-WYGIIERVKVTVWYtapta 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 334 IGELCRYLLNQPPREAENQHQVRMALGNGLRQSI--WTN--FSSRFHipqvaEFYGATE------CNCSlgNFDSQVGAC 403
Cdd:cd05969 190 IRMLMKEGDELARKYDLSSLRFIHSVGEPLNPEAirWGMevFGVPIH-----DTWWQTEtgsimiANYP--CMPIKPGSM 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 404 GfnsrilsfvYPIRLVR---VNEDTMELirgpdgvcipcQPGEPGQLVgriIQKDPLRRFDGYLNQGANNKKiakdVFKK 480
Cdd:cd05969 263 G---------KPLPGVKaavVDENGNEL-----------PPGTKGILA---LKPGWPSMFRGIWNDEERYKN----SFID 315
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 40807357 481 GdqAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLDMADVAVYGVEVP 542
Cdd:cd05969 316 G--WYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDP 375
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
88-603 |
4.51e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 87.53 E-value: 4.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 88 PDKTALIFEgtDTHWTFRQLDEYSSSVANFLQARGLASGDVAaIFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALLH 167
Cdd:PRK07638 15 PNKIAIKEN--DRVLTYKDWFESVCKVANWLNEKESKNKTIA-ILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 168 CLTTSRARALV----FGSEMASAICEVhasldpslslfcsgsWEPGAVPPSTEhldpllKDAPKHLPSCpdkGFTDKLFY 243
Cdd:PRK07638 92 RLAISNADMIVteryKLNDLPDEEGRV---------------IEIDEWKRMIE------KYLPTYAPIE---NVQNAPFY 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 244 I-YTSGTTGLPKAAIVVHSRYYRMAALVYYGFRMRPNDIVYDCLPLYHSAgNIVGIGQCLLHGMTVVIRKKFSASRFWDD 322
Cdd:PRK07638 148 MgFTSGSTGKPKAFLRAQQSWLHSFDCNVHDFHMKREDSVLIAGTLVHSL-FLYGAISTLYVGQTVHLMRKFIPNQVLDK 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 323 CIKYNCTIVQYIGELCRYLLnqppREAENQHQVRMALGNGLRQSIWT--NFSSRFHIPQVAEFYGATECNcslgnFDSQV 400
Cdd:PRK07638 227 LETENISVMYTVPTMLESLY----KENRVIENKMKIISSGAKWEAEAkeKIKNIFPYAKLYEFYGASELS-----FVTAL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 401 GACGFNSRILSFVYPIRLVRVNedtmelIRGPDGVciPCQPGEpgqlVGRIIQKDPLRrFDGYLNQGANNKKIAKDvfkk 480
Cdd:PRK07638 298 VDEESERRPNSVGRPFHNVQVR------ICNEAGE--EVQKGE----IGTVYVKSPQF-FMGYIIGGVLARELNAD---- 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 481 gdqAYLT-GDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLDMADVAVYGVEVPgtegRAGMAAVASPTGN 559
Cdd:PRK07638 361 ---GWMTvRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDS----YWGEKPVAIIKGS 433
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 40807357 560 CDLERFAQVLEKELPLYARPIFLRLLPELHKTGTYKFQKTELRK 603
Cdd:PRK07638 434 ATKQQLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEAKS 477
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
74-604 |
5.54e-18 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 87.77 E-value: 5.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 74 RTVPILFASTVRRHPDKTALIFEGTDThwTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEF-VGLwlgMAKLGVE 152
Cdd:PRK07059 23 PSLADLLEESFRQYADRPAFICMGKAI--TYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYpVAI---AAVLRAG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 153 AALINTN---LRRDaLLHCLTTSRARALV----FGSEMASAICE------VHASLDPSLSLfcSG--------------- 204
Cdd:PRK07059 98 YVVVNVNplyTPRE-LEHQLKDSGAEAIVvlenFATTVQQVLAKtavkhvVVASMGDLLGF--KGhivnfvvrrvkkmvp 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 205 SWE-PGAVPPStehlDPLLKDAPKHLPScPDKGFTDKLFYIYTSGTTGLPKAAIVVH----SRYYRMAALVYYGFRMRPN 279
Cdd:PRK07059 175 AWSlPGHVRFN----DALAEGARQTFKP-VKLGPDDVAFLQYTGGTTGVSKGATLLHrnivANVLQMEAWLQPAFEKKPR 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 280 D--IVYDC-LPLYHsagnIVGIGQCLLHGM-----TVVIRKKFSASRFWDDCIKYNCTIVQYIGELCRYLLNQPPREAEN 351
Cdd:PRK07059 250 PdqLNFVCaLPLYH----IFALTVCGLLGMrtggrNILIPNPRDIPGFIKELKKYQVHIFPAVNTLYNALLNNPDFDKLD 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 352 QHQVRMALGNGL--RQSIWTNFSSRFHIPqVAEFYGATECN----CSLGNFDSQVGACGFnsrilsfvyPIRLVRVNedt 425
Cdd:PRK07059 326 FSKLIVANGGGMavQRPVAERWLEMTGCP-ITEGYGLSETSpvatCNPVDATEFSGTIGL---------PLPSTEVS--- 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 426 melIRGPDGVCIPcqPGEPGQLVGRIIQKDPlrrfdGYLNQGANNKK-IAKDVFKKgdqaylTGDVLVMDELGYLYFRDR 504
Cdd:PRK07059 393 ---IRDDDGNDLP--LGEPGEICIRGPQVMA-----GYWNRPDETAKvMTADGFFR------TGDVGVMDERGYTKIVDR 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 505 TGDTFRWKGENVSTTEVEGTLSRLLDMADVAVYGVEVPGTeGRAGMAAVASPTGNCDLERFAQVLEKELPLYARPIFLRL 584
Cdd:PRK07059 457 KKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHS-GEAVKLFVVKKDPALTEEDVKAFCKERLTNYKRPKFVEF 535
|
570 580
....*....|....*....|
gi 40807357 585 LPELHKTGTYKFQKTELRKE 604
Cdd:PRK07059 536 RTELPKTNVGKILRRELRDG 555
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
79-601 |
6.20e-18 |
|
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: 86.84 E-value: 6.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 79 LFASTVRRHPDKTALIFEGTDthWTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGVEAALINT 158
Cdd:cd17645 3 LFEEQVERTPDHVAVVDRGQS--LTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 159 NlrrdallhcLTTSRARALVFGSEMASaicevhasldpslslfcsgswepgavppstehldpLLKDApkhlpscpdkgfT 238
Cdd:cd17645 81 D---------YPGERIAYMLADSSAKI-----------------------------------LLTNP------------D 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 239 DKLFYIYTSGTTGLPKAAIVVHSRYYRMAALVYYGFRMRPND--IVYDCLPLyhsAGNIVGIGQCLLHGMTVVI---RKK 313
Cdd:cd17645 105 DLAYVIYTSGSTGLPKGVMIEHHNLVNLCEWHRPYFGVTPADksLVYASFSF---DASAWEIFPHLTAGAALHVvpsERR 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 314 FSASRFWDDCIKYNCTIVQYIGELCRYLLnqpprEAENqHQVRMAL--GNGLRQSIWTNFssrfhipQVAEFYGATECNC 391
Cdd:cd17645 182 LDLDALNDYFNQEGITISFLPTGAAEQFM-----QLDN-QSLRVLLtgGDKLKKIERKGY-------KLVNNYGPTENTV 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 392 SLGNF--DSQVGAcgfnsriLSFVYPIRLVRVnedtmeLIRGPDgvcIPCQP-GEPGQLvgrIIQKDPLRRfdGYLNQ-G 467
Cdd:cd17645 249 VATSFeiDKPYAN-------IPIGKPIDNTRV------YILDEA---LQLQPiGVAGEL---CIAGEGLAR--GYLNRpE 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 468 ANNKKIAKDVFKKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLDMADVAVYGVEVPGteGR 547
Cdd:cd17645 308 LTAEKFIVHPFVPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDAD--GR 385
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 40807357 548 AGMAAVASPTGNCDLERFAQVLEKELPLYARPIFLRLLPELHKTGTYKFQKTEL 601
Cdd:cd17645 386 KYLVAYVTAPEEIPHEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
239-542 |
1.07e-17 |
|
C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.
Pssm-ID: 341235 [Multi-domain] Cd Length: 490 Bit Score: 86.23 E-value: 1.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 239 DKLFYIYTSGTTGLPKAAIVVHSRYYRMAALVYYGFRMRPNDIVYDCLPLYHSAGNIVGIGQCLLHGMTVVirkkFSAS- 317
Cdd:cd05909 148 DPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPFFHSFGLTGCLWLPLLSGIKVV----FHPNp 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 318 -------RFWDDcikYNCTIVQYIGELCRYLLNQppREAENQHQVRMAL--GNGLRQSIWTNFSSRFHIPqVAEFYGATE 388
Cdd:cd05909 224 ldykkipELIYD---KKATILLGTPTFLRGYARA--AHPEDFSSLRLVVagAEKLKDTLRQEFQEKFGIR-ILEGYGTTE 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 389 CN----CSLGNFDSQVGACG-----FNSRILSfVYPIRLVRVNEDTMELIRGPDgvcipcqpgepgqlvgriiqkdplrR 459
Cdd:cd05909 298 CSpvisVNTPQSPNKEGTVGrplpgMEVKIVS-VETHEEVPIGEGGLLLVRGPN-------------------------V 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 460 FDGYLNqgannkKIAKDVFKKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLDMaDVAVYGV 539
Cdd:cd05909 352 MLGYLN------EPELTSFAFGDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEILPE-DNEVAVV 424
|
...
gi 40807357 540 EVP 542
Cdd:cd05909 425 SVP 427
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
74-604 |
2.42e-17 |
|
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: 85.58 E-value: 2.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 74 RTVPILFASTVRRHPDKTALIfeGTDTHWTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGVE- 152
Cdd:COG1021 25 ETLGDLLRRRAERHPDRIAVV--DGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAIp 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 153 -AALIntNLRRDALLHCLTTSRARALVFGS--------EMASAICEVHASLDPSLSLFCSGSWEPgavppstehLDPLLK 223
Cdd:COG1021 103 vFALP--AHRRAEISHFAEQSEAVAYIIPDrhrgfdyrALARELQAEVPSLRHVLVVGDAGEFTS---------LDALLA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 224 DAPKHLPSCPDKGftDKLFYIYTSGTTGLPKAAIVVHSRYyrmaalvYYGFRmRPNDI-------VYDC-LPLYHSAGNI 295
Cdd:COG1021 172 APADLSEPRPDPD--DVAFFQLSGGTTGLPKLIPRTHDDY-------LYSVR-ASAEIcgldadtVYLAaLPAAHNFPLS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 296 V-GIGQCLLHGMTVVIRKKFSAsrfwDDCI----KYNCTIVQYIGELCRYLLNQPPRE------------------AENQ 352
Cdd:COG1021 242 SpGVLGVLYAGGTVVLAPDPSP----DTAFplieRERVTVTALVPPLALLWLDAAERSrydlsslrvlqvggaklsPELA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 353 HQVRMALGNGLRQSiwtnfssrfhipqvaefYGATE--CNCS-LGnfDS---QVGACGfnsRILSfvyP---IRLVrvne 423
Cdd:COG1021 318 RRVRPALGCTLQQV-----------------FGMAEglVNYTrLD--DPeevILTTQG---RPIS---PddeVRIV---- 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 424 dtmelirGPDGVciPCQPGEPGQLVGR---IIQkdplrrfdGYLNQGANNKKiakdVFKKgDQAYLTGDVLVMDELGYLY 500
Cdd:COG1021 369 -------DEDGN--PVPPGEVGELLTRgpyTIR--------GYYRAPEHNAR----AFTP-DGFYRTGDLVRRTPDGYLV 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 501 FRDRTGDTFRWKGENVSTTEVEGTLSRLLDMADVAVygVEVPGTE-GRAGMAAV----ASPTGNcDLERFaqVLEKELPL 575
Cdd:COG1021 427 VEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAV--VAMPDEYlGERSCAFVvprgEPLTLA-ELRRF--LRERGLAA 501
|
570 580
....*....|....*....|....*....
gi 40807357 576 YARPIFLRLLPELHKTGTYKFQKTELRKE 604
Cdd:COG1021 502 FKLPDRLEFVDALPLTAVGKIDKKALRAA 530
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
244-598 |
3.75e-17 |
|
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: 82.93 E-value: 3.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 244 IYTSGTTGLPKAAIVVHSRYYRMAALVYYGFRMRPNDiVYDCL-PLYHSAGNIVGIGQCLLHGMTVVIRKKFSASRFWDD 322
Cdd:cd17638 6 MFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDD-RYLIInPFFHTFGYKAGIVACLLTGATVVPVAVFDVDAILEA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 323 CIKYNCTIVQYIGELCRYLLNQPPREAENQHQVRMALGNG--LRQSIWTNFSSRFHIPQVAEFYGATECNCSL-----GN 395
Cdd:cd17638 85 IERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVTGAatVPVELVRRMRSELGFETVLTAYGLTEAGVATmcrpgDD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 396 FDSQVGACGFnsrilsfVYPIRLVRVNEDTMELIRGPDgvcipcqpgepgqlvgrIIQkdplrrfdGYLNqgaNNKKIAK 475
Cdd:cd17638 165 AETVATTCGR-------ACPGFEVRIADDGEVLVRGYN-----------------VMQ--------GYLD---DPEATAE 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 476 DVFKKGdqaYL-TGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLDMADVAVYGV--EVPGTEGRAgmAA 552
Cdd:cd17638 210 AIDADG---WLhTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVpdERMGEVGKA--FV 284
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 40807357 553 VASPTGNCDLERFAQVLEKELPLYARPIFLRLLPELHKTGTYKFQK 598
Cdd:cd17638 285 VARPGVTLTEEDVIAWCRERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
243-603 |
4.03e-17 |
|
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: 83.30 E-value: 4.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 243 YIYTSGTTGLPKAAIVVHSRYYRMAALVYYGFRMRPNDIVYDCLPLYHSAGNIVGIGQCLLHGMTVVI------RKKFSA 316
Cdd:cd05944 7 YFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVVLagpagyRNPGLF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 317 SRFWDDCIKYNCTIVQYIGELCRYLLnQPPREAENQhQVRMALGNG--LRQSIWTNFSSRFHIPqVAEFYGATECNCSLG 394
Cdd:cd05944 87 DNFWKLVERYRITSLSTVPTVYAALL-QVPVNADIS-SLRFAMSGAapLPVELRARFEDATGLP-VVEGYGLTEATCLVA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 395 -NFDS---QVGACGfnsriLSFVYPIRLVRVNEDTMELIRgpdgvciPCQPGEpgqlVGRIIQKDPlRRFDGYLNQGANN 470
Cdd:cd05944 164 vNPPDgpkRPGSVG-----LRLPYARVRIKVLDGVGRLLR-------DCAPDE----VGEICVAGP-GVFGGYLYTEGNK 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 471 KKIAKDVFKKgdqaylTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLDMADVAVYGVEVPgtegRAGm 550
Cdd:cd05944 227 NAFVADGWLN------TGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDA----HAG- 295
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 40807357 551 aavASPTGNCDLERFAQVLEKELPLYAR---------PIFLRLLPELHKTGTYKFQKTELRK 603
Cdd:cd05944 296 ---ELPVAYVQLKPGAVVEEEELLAWARdhvperaavPKHIEVLEELPVTAVGKVFKPALRA 354
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
97-604 |
4.47e-17 |
|
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: 84.82 E-value: 4.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 97 GTDTHWTFRQLDEYSSSVANFL-QARGLASGDVAAIFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALLHCLTTSRAR 175
Cdd:cd05928 37 GDEVKWSFRELGSLSRKAANVLsGACGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 176 ALVFGSEMASAICEVhASLDPSLS--LFCSGSWEPGAVppsteHLDPLLKDA-PKHlpSCPDKGFTDKLFYIYTSGTTGL 252
Cdd:cd05928 117 CIVTSDELAPEVDSV-ASECPSLKtkLLVSEKSRDGWL-----NFKELLNEAsTEH--HCVETGSQEPMAIYFTSGTTGS 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 253 PKAAIVVHSRYYRMAALV-YYGFRMRPNDIVYDClplyHSAGNIVGIGQCL----LHGMTVVIRK--KFSASRFWDDCIK 325
Cdd:cd05928 189 PKMAEHSHSSLGLGLKVNgRYWLDLTASDIMWNT----SDTGWIKSAWSSLfepwIQGACVFVHHlpRFDPLVILKTLSS 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 326 YNCTIVQYIGELCRYLLNQPPREAENQH-QVRMALGNGLRQSIWTNFSSRFHIpQVAEFYGATECNCSLGNFDSQVGACG 404
Cdd:cd05928 265 YPITTFCGAPTVYRMLVQQDLSSYKFPSlQHCVTGGEPLNPEVLEKWKAQTGL-DIYEGYGQTETGLICANFKGMKIKPG 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 405 FNSRIlSFVYPIRLVRVNedtmelirgpdGVCIPcqPGEPGQLVGRIIQKDPLRRFDGYLNqgaNNKKIAKDVfkKGDqA 484
Cdd:cd05928 344 SMGKA-SPPYDVQIIDDN-----------GNVLP--PGTEGDIGIRVKPIRPFGLFSGYVD---NPEKTAATI--RGD-F 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 485 YLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLDMADVAVYGVEVPgTEGRAGMAAV--ASPTGNCDL 562
Cdd:cd05928 404 YLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDP-IRGEVVKAFVvlAPQFLSHDP 482
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 40807357 563 ERfaqvLEKEL---------PlYARPIFLRLLPELHKTGTYKFQKTELRKE 604
Cdd:cd05928 483 EQ----LTKELqqhvksvtaP-YKYPRKVEFVQELPKTVTGKIQRNELRDK 528
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
79-588 |
4.78e-17 |
|
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: 84.25 E-value: 4.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 79 LFASTVRRHPDKTALIFEGTdtHWTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGVEAALINT 158
Cdd:cd17646 3 LVAEQAARTPDAPAVVDEGR--TLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 159 NLRRDALLHCLTTSRARALVFGSEMASAICEVHASLDPslslfcsGSWEPGAvPPSTEHLDPLLKDAPKHLpscpdkgft 238
Cdd:cd17646 81 GYPADRLAYMLADAGPAVVLTTADLAARLPAGGDVALL-------GDEALAA-PPATPPLVPPRPDNLAYV--------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 239 dklfyIYTSGTTGLPKAAIVVHsryyrmAALVYY------GFRMRPNDIVYDCLPLyhsaGNIVGIGQCLL---HGMTVV 309
Cdd:cd17646 144 -----IYTSGSTGRPKGVMVTH------AGIVNRllwmqdEYPLGPGDRVLQKTPL----SFDVSVWELFWplvAGARLV 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 310 I------RKKFSASRFWDDcikYNCTIVQYIGELCRYLLNQP-PREAENQHQVrMALGNGLRQSIWTNFSSRFHIPQVaE 382
Cdd:cd17646 209 VarpgghRDPAYLAALIRE---HGVTTCHFVPSMLRVFLAEPaAGSCASLRRV-FCSGEALPPELAARFLALPGAELH-N 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 383 FYGATEcncslGNFDSQVGAC--GFNSRILSFVYPIRLVRVNEDTMELIRGPDGVcipcqPGE---PGQLVGRiiqkdpl 457
Cdd:cd17646 284 LYGPTE-----AAIDVTHWPVrgPAETPSVPIGRPVPNTRLYVLDDALRPVPVGV-----PGElylGGVQLAR------- 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 458 rrfdGYLNQGA-NNKKIAKDVFKKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLDMADVAV 536
Cdd:cd17646 347 ----GYLGRPAlTAERFVPDPFGPGSRMYRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVV 422
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 40807357 537 YGVEVPGTEGRAGMAAVASPTGNC-DLERFAQVLEKELPLYARPIFLRLLPEL 588
Cdd:cd17646 423 VARAAPAGAARLVGYVVPAAGAAGpDTAALRAHLAERLPEYMVPAAFVVLDAL 475
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
74-539 |
1.43e-16 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 83.32 E-value: 1.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 74 RTVPILFASTVRRHPDKTALIFEGTDTHWTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGVEA 153
Cdd:PRK08315 16 QTIGQLLDRTAARYPDREALVYRDQGLRWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAIL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 154 ALINTNLRRDALLHCLTTSRARALVF-----GSEMASAICEvhasLDPSLSlfcsgSWEPGAVppSTEHLdPLLK----- 223
Cdd:PRK08315 96 VTINPAYRLSELEYALNQSGCKALIAadgfkDSDYVAMLYE----LAPELA-----TCEPGQL--QSARL-PELRrvifl 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 224 DAPKH-----------LPSCPDKG----------FTDKLFYIYTSGTTGLPKAAIVVHSRYYRMAALVyyGFRMR--PND 280
Cdd:PRK08315 164 GDEKHpgmlnfdellaLGRAVDDAelaarqatldPDDPINIQYTSGTTGFPKGATLTHRNILNNGYFI--GEAMKltEED 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 281 IVYDCLPLYHSAGNIVGIGQCLLHGMTVVirkkFSASRFwdDCI-------KYNCTIVQ-----YIGElcrylLNQPPRE 348
Cdd:PRK08315 242 RLCIPVPLYHCFGMVLGNLACVTHGATMV----YPGEGF--DPLatlaaveEERCTALYgvptmFIAE-----LDHPDFA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 349 AENQHQVR---MAlgnG-------LRQSIwtnfsSRFHIPQVAEFYGATEcnCSLGNFDS--------QVGACGfnsRIL 410
Cdd:PRK08315 311 RFDLSSLRtgiMA---GspcpievMKRVI-----DKMHMSEVTIAYGMTE--TSPVSTQTrtddplekRVTTVG---RAL 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 411 SFVYpirlVR-VNEDTMElirgpdgvciPCQPGEPGQLVGR---IIQkdplrrfdGYLNqgaNNKKIAKDVFKKGdqaYL 486
Cdd:PRK08315 378 PHLE----VKiVDPETGE----------TVPRGEQGELCTRgysVMK--------GYWN---DPEKTAEAIDADG---WM 429
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 487 -TGDVLVMDELGYLYFrdrTGdtfRWK------GENVSTTEVEGTLSRLLDMADVAVYGV 539
Cdd:PRK08315 430 hTGDLAVMDEEGYVNI---VG---RIKdmiirgGENIYPREIEEFLYTHPKIQDVQVVGV 483
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
88-601 |
2.28e-16 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.
Pssm-ID: 341279 [Multi-domain] Cd Length: 477 Bit Score: 82.32 E-value: 2.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 88 PDKTALIfeGTDTHWTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGVEAALINTNL---RRDA 164
Cdd:cd12114 1 PDATAVI--CGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQpaaRREA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 165 LLHcltTSRARALVfgsemasaICEVHASLDpslslfcsgswepgaVPPSTEHLDPLLKDAPKHLPSCPDKGFTDKLFYI 244
Cdd:cd12114 79 ILA---DAGARLVL--------TDGPDAQLD---------------VAVFDVLILDLDALAAPAPPPPVDVAPDDLAYVI 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 245 YTSGTTGLPKAAIVVHSRYYRMAALVYYGFRMRPNDIVYDCLPLYH--SAGNIVGIgqcLLHGMTVVI----RKKFSASr 318
Cdd:cd12114 133 FTSGSTGTPKGVMISHRAALNTILDINRRFAVGPDDRVLALSSLSFdlSVYDIFGA---LSAGATLVLpdeaRRRDPAH- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 319 fWDDCI-KYNCTIVQYIGELCRYLLNQPPREAENQHQVRMALGNG------LRQSIWTNFSSrfhiPQVAEFYGATEcnc 391
Cdd:cd12114 209 -WAELIeRHGVTLWNSVPALLEMLLDVLEAAQALLPSLRLVLLSGdwipldLPARLRALAPD----ARLISLGGATE--- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 392 slgnfdsqvGAcgfnsrILSFVYPIRlvRVNEDT------MEL------IRGPDGVciPCQPGEPGQLvgrIIQKDPLRR 459
Cdd:cd12114 281 ---------AS------IWSIYHPID--EVPPDWrsipygRPLanqryrVLDPRGR--DCPDWVPGEL---WIGGRGVAL 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 460 fdGYLNQGAnnKKIAKDV--------FKKGDQAYLTGDvlvmdelGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLDM 531
Cdd:cd12114 339 --GYLGDPE--LTAARFVthpdgerlYRTGDLGRYRPD-------GTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGV 407
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 40807357 532 ADVAVygVEVPGTEGRAGMAAV-----ASPTGNCDLERFAQvleKELPLYARPIFLRLLPELHKTGTYKFQKTEL 601
Cdd:cd12114 408 ARAVV--VVLGDPGGKRLAAFVvpdndGTPIAPDALRAFLA---QTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
86-604 |
2.43e-16 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 82.39 E-value: 2.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 86 RHPDKTALIFEGTDThwTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGVEAALINTNLRRDAL 165
Cdd:PRK06710 36 RYPEKKALHFLGKDI--TFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTEREL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 166 LHCLTTSRARA-----LVF--------GSEMASAICEVHASLDPS----LSLFCSGSWEPGAVPPSTEHLDPLLKDAPKH 228
Cdd:PRK06710 114 EYQLHDSGAKVilcldLVFprvtnvqsATKIEHVIVTRIADFLPFpknlLYPFVQKKQSNLVVKVSESETIHLWNSVEKE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 229 ------LPSCPDkgfTDKLFYIYTSGTTGLPKAAIVVHSRYYRMAAL-VYYGFRMRP-NDIVYDCLPLYHSAGNIVGIGQ 300
Cdd:PRK06710 194 vntgveVPCDPE---NDLALLQYTGGTTGFPKGVMLTHKNLVSNTLMgVQWLYNCKEgEEVVLGVLPFFHVYGMTAVMNL 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 301 CLLHGMTVVIRKKFSASRFWDDCIKYNCTIVQYIGELCRYLLNQPPREAENQHQVRMALGNG--LRQSIWTNFSsRFHIP 378
Cdd:PRK06710 271 SIMQGYKMVLIPKFDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLLKEYDISSIRACISGSapLPVEVQEKFE-TVTGG 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 379 QVAEFYGATECN-CSLGNF--DSQV-GACGF-----NSRILSFvypirlvrvneDTMELIRgpdgvcipcqPGEpgqlVG 449
Cdd:PRK06710 350 KLVEGYGLTESSpVTHSNFlwEKRVpGSIGVpwpdtEAMIMSL-----------ETGEALP----------PGE----IG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 450 RIIQKDPlRRFDGYLNQGANNKKIAKDvfkkgdqAYL-TGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRL 528
Cdd:PRK06710 405 EIVVKGP-QIMKGYWNKPEETAAVLQD-------GWLhTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEH 476
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 40807357 529 LDMADVAVYGVEVPgTEGRAGMAAVASPTGN-CDLERFAQVLEKELPLYARPIFLRLLPELHKTGTYKFQKTELRKE 604
Cdd:PRK06710 477 EKVQEVVTIGVPDP-YRGETVKAFVVLKEGTeCSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVLIEE 552
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
79-591 |
6.46e-16 |
|
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341310 [Multi-domain] Cd Length: 490 Bit Score: 80.83 E-value: 6.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 79 LFASTVRRHPDKTALIFEgtDTHWTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNE-FVGLwLGMAKLGVEAALIN 157
Cdd:cd17655 2 LFEEQAEKTPDHTAVVFE--DQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEmIVGI-LGILKAGGAYLPID 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 158 TNLRRDALLHCLTTSRARALVfgsemasaiceVHASLDPSLSlfcsgswepgavppSTEHLDPLLKDAPKHLPSC---PD 234
Cdd:cd17655 79 PDYPEERIQYILEDSGADILL-----------TQSHLQPPIA--------------FIGLIDLLDEDTIYHEESEnlePV 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 235 KGFTDKLFYIYTSGTTGLPKAAIVVH-----------SRYY-----RMAALVYYGFRMRPNDIvydclplYHSagnivgi 298
Cdd:cd17655 134 SKSDDLAYVIYTSGSTGKPKGVMIEHrgvvnlvewanKVIYqgehlRVALFASISFDASVTEI-------FAS------- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 299 gqcLLHGMTVVIRKKFSASRFwddcikynCTIVQYIGELCRYLLNQPPRE----AENQHQVRMAL------GNGLRQSIW 368
Cdd:cd17655 200 ---LLSGNTLYIVRKETVLDG--------QALTQYIRQNRITIIDLTPAHlkllDAADDSEGLSLkhlivgGEALSTELA 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 369 TNFSSRFHI-PQVAEFYGATEC--NCSLGNFDSQ--------VGACGFNSRIlsfvYpirlvrVNEDTMELirgpdgvci 437
Cdd:cd17655 269 KKIIELFGTnPTITNAYGPTETtvDASIYQYEPEtdqqvsvpIGKPLGNTRI----Y------ILDQYGRP--------- 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 438 pcQP-GEPGQLVgriIQKDPLRRfdGYLNQGA-NNKKIAKDVFKKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGEN 515
Cdd:cd17655 330 --QPvGVAGELY---IGGEGVAR--GYLNRPElTAEKFVDDPFVPGERMYRTGDLARWLPDGNIEFLGRIDHQVKIRGYR 402
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 40807357 516 VSTTEVEGTLSRLLDMADVAVygVEVPGTEGRAGMAAVASPTGNCDLERFAQVLEKELPLYARPIFLRLLPELHKT 591
Cdd:cd17655 403 IELGEIEARLLQHPDIKEAVV--IARKDEQGQNYLCAYIVSEKELPVAQLREFLARELPDYMIPSYFIKLDEIPLT 476
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
88-591 |
2.06e-15 |
|
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: 78.95 E-value: 2.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 88 PDKTALIFEgtDTHWTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNE-FVGLwLGMAKLGveAALIntnlrrdall 166
Cdd:cd17649 1 PDAVALVFG--DQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEmVVAL-LAILKAG--GAYV---------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 167 hclttsraralvfgsemasaicevhaSLDPslslfcsgswepgAVPPstEHLDPLLKDAPKHLPSCPDKgftDKLFY-IY 245
Cdd:cd17649 66 --------------------------PLDP-------------EYPA--ERLRYMLEDSGAGLLLTHHP---RQLAYvIY 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 246 TSGTTGLPKAAIVVH---SRYYRMAALVYygfRMRPNDIVYDCLPLyhsagNIVGIGQCLLH----GMTVVIRKK---FS 315
Cdd:cd17649 102 TSGSTGTPKGVAVSHgplAAHCQATAERY---GLTPGDRELQFASF-----NFDGAHEQLLPplicGACVVLRPDelwAS 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 316 ASRFWDDCIKYNCTIVQ----YIGELCRYLLNQPPR------------EAENQHQVRMALGNGLRqsiWTNfssrfhipq 379
Cdd:cd17649 174 ADELAEMVRELGVTVLDlppaYLQQLAEEADRTGDGrppslrlyifggEALSPELLRRWLKAPVR---LFN--------- 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 380 vaeFYGATECNCSLGNFDSQVGA-CGFNSRILSFVYPIRLVRVNedtmelirgpDGVCIPCQPGEPGQLvgrIIQKDPLR 458
Cdd:cd17649 242 ---AYGPTEATVTPLVWKCEAGAaRAGASMPIGRPLGGRSAYIL----------DADLNPVPVGVTGEL---YIGGEGLA 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 459 RfdGYLNQ-GANNKKIAKDVF-KKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLDMADVAV 536
Cdd:cd17649 306 R--GYLGRpELTAERFVPDPFgAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAV 383
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 40807357 537 YGVEVPGTEGRAG-MAAVASPTGNCDLERFAQVLEKELPLYARPIFLRLLPELHKT 591
Cdd:cd17649 384 VALDGAGGKQLVAyVVLRAAAAQPELRAQLRTALRASLPDYMVPAHLVFLARLPLT 439
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
84-608 |
3.45e-15 |
|
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: 78.76 E-value: 3.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 84 VRRHPDKTALIFEGTDT----HWTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGVeaalintn 159
Cdd:cd05966 63 LKERGDKVAIIWEGDEPdqsrTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGA-------- 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 160 lrrdalLHclttsrarALVFGSEMASAICE--VHAslDPSLSLFCSGSWEPGAVPPSTEHLDPLLKDAP----------- 226
Cdd:cd05966 135 ------VH--------SVVFAGFSAESLADriNDA--QCKLVITADGGYRGGKVIPLKEIVDEALEKCPsvekvlvvkrt 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 227 -------------------KHLPSCPDKGFT--DKLFYIYTSGTTGLPKAaiVVHSR--YyrmaaLVY------YGFRMR 277
Cdd:cd05966 199 ggevpmtegrdlwwhdlmaKQSPECEPEWMDseDPLFILYTSGSTGKPKG--VVHTTggY-----LLYaattfkYVFDYH 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 278 PNDIVY---DClplyhsaGNIVG-----IGQcLLHGMTVVIrkkF-------SASRFWDDCIKYNCTIVqY-----IGEL 337
Cdd:cd05966 272 PDDIYWctaDI-------GWITGhsyivYGP-LANGATTVM---FegtptypDPGRYWDIVEKHKVTIF-YtaptaIRAL 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 338 CRYLLNQPPREAENQHQVRMALGNGLRQSIWTNFSS---RFHIPQVAEFYgATE----CNCSL-GNFDSQVGACGFnsri 409
Cdd:cd05966 340 MKFGDEWVKKHDLSSLRVLGSVGEPINPEAWMWYYEvigKERCPIVDTWW-QTEtggiMITPLpGATPLKPGSATR---- 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 410 lsfvyP---IRLVRVNEDTMELIRGPDGV-CIPcQPGePGQLvgRIIQKDPLRRFDGYlnqgannkkiakdvFKKGDQAY 485
Cdd:cd05966 415 -----PffgIEPAILDEEGNEVEGEVEGYlVIK-RPW-PGMA--RTIYGDHERYEDTY--------------FSKFPGYY 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 486 LTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLDMADVAVYGVEVPGTeGRAGMAAVASptgnCDLERF 565
Cdd:cd05966 472 FTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIK-GEAIYAFVTL----KDGEEP 546
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 40807357 566 AQVLEKELPL--------YARPIFLRLLPELHKTGTYKFQKTELRK--EGFDP 608
Cdd:cd05966 547 SDELRKELRKhvrkeigpIATPDKIQFVPGLPKTRSGKIMRRILRKiaAGEEE 599
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
90-602 |
6.58e-15 |
|
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: 77.52 E-value: 6.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 90 KTALIfeGTDTHWTFRQLDEYSSSVANFLQAR-GLASGDVAAIFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALLHC 168
Cdd:cd05958 1 RTCLR--SPEREWTYRDLLALANRIANVLVGElGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 169 L-TTSRARALVFGSEMASA-ICevhasldpslslfcsgswepgavppstehldpLLKdapkhlpscpdkgftdklfyiYT 246
Cdd:cd05958 79 LdKARITVALCAHALTASDdIC--------------------------------ILA---------------------FT 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 247 SGTTGLPKAAIVVHsRYYRMAALVY--YGFRMRPNDIVYDCLPLYHSagniVGIGQCLLH----GMTVVIRKKFSASRFW 320
Cdd:cd05958 106 SGTTGAPKATMHFH-RDPLASADRYavNVLRLREDDRFVGSPPLAFT----FGLGGVLLFpfgvGASGVLLEEATPDLLL 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 321 DDCIKYNCTIVQYIGELCRYLLNQPPREAENQHQVRMAL--GNGLRQSIWTNFSSRFHIPqVAEFYGATE---CNCSLGN 395
Cdd:cd05958 181 SAIARYKPTVLFTAPTAYRAMLAHPDAAGPDLSSLRKCVsaGEALPAALHRAWKEATGIP-IIDGIGSTEmfhIFISARP 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 396 FDSQVGACGFnsrilsfVYPIRLVRVNEDtmelirgpDGVCIPcqPGEPGQLVgriIQKDPLRRFDGylnqgannKKIAK 475
Cdd:cd05958 260 GDARPGATGK-------PVPGYEAKVVDD--------EGNPVP--DGTIGRLA---VRGPTGCRYLA--------DKRQR 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 476 DVFkkGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLDMADVAVYGVEVP--GTEGRAGMAAV 553
Cdd:cd05958 312 TYV--QGGWNITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDEsrGVVVKAFVVLR 389
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 40807357 554 ASPTGNCDLERFAQVLEKE-LPLYARPIFLRLLPELHKTGTYKFQKTELR 602
Cdd:cd05958 390 PGVIPGPVLARELQDHAKAhIAPYKYPRAIEFVTELPRTATGKLQRFALR 439
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
76-540 |
6.66e-15 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 77.96 E-value: 6.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 76 VPILFAStvRRHPDKTALIFEGTDTHWTFRQLDEYSSSVANFLQAR-GLASGDVAAIFMENRNEFVGLWLGMAKLGVEAA 154
Cdd:PLN02574 43 VSFIFSH--HNHNGDTALIDSSTGFSISYSELQPLVKSMAAGLYHVmGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 155 LINTnlrrdalLHCLTTSRAR------ALVFGSemASAICEVHASLDPSLSLFCSGSWEPGAVPPSTEHldPLLKDAPKH 228
Cdd:PLN02574 121 TMNP-------SSSLGEIKKRvvdcsvGLAFTS--PENVEKLSPLGVPVIGVPENYDFDSKRIEFPKFY--ELIKEDFDF 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 229 LPScPDKGFTDKLFYIYTSGTTGLPKAAIVVHSRYYRMAAL-VYYG---FRMRPNDIVY-DCLPLYHSAGNIVGIGQCLL 303
Cdd:PLN02574 190 VPK-PVIKQDDVAAIMYSSGTTGASKGVVLTHRNLIAMVELfVRFEasqYEYPGSDNVYlAALPMFHIYGLSLFVVGLLS 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 304 HGMTVVIRKKFSASRFWDDCIKYNCTIVQYIgelcryllnqPPREAENQHQVRMALGNGLR-------------QSIWTN 370
Cdd:PLN02574 269 LGSTIVVMRRFDASDMVKVIDRFKVTHFPVV----------PPILMALTKKAKGVCGEVLKslkqvscgaaplsGKFIQD 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 371 FSSRFHIPQVAEFYGATEcncslgnfDSQVGACGFNSRILSFVYPIRLVRVNEDTmELIRGPDGVCIPcqPGEPGQL--V 448
Cdd:PLN02574 339 FVQTLPHVDFIQGYGMTE--------STAVGTRGFNTEKLSKYSSVGLLAPNMQA-KVVDWSTGCLLP--PGNCGELwiQ 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 449 GRIIQKdplrrfdGYLNQG-ANNKKIAKDVFKKgdqaylTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSR 527
Cdd:PLN02574 408 GPGVMK-------GYLNNPkATQSTIDKDGWLR------TGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLIS 474
|
490
....*....|...
gi 40807357 528 LLDMADVAVYGVE 540
Cdd:PLN02574 475 HPEIIDAAVTAVP 487
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
79-604 |
7.11e-15 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 77.61 E-value: 7.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 79 LFASTVRRHPDKTALIFEGTD-THWTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGVEAALIN 157
Cdd:PRK07514 5 LFDALRAAFADRDAPFIETPDgLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 158 TNLRRDALLHCLTTSRARALVFGSEMASAICEVhASLDPSLSLFCSGSWEPGAVPPSTEHLDPLLKDAPKHlpscpdkgf 237
Cdd:PRK07514 85 TAYTLAELDYFIGDAEPALVVCDPANFAWLSKI-AAAAGAPHVETLDADGTGSLLEAAAAAPDDFETVPRG--------- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 238 TDKLFYI-YTSGTTGLPKAAIVVHSRYYRMA-ALV-YYGFrmRPNDIVYDCLPLYHSAGNIVGIGQCLLHGMTVVIRKKF 314
Cdd:PRK07514 155 ADDLAAIlYTSGTTGRSKGAMLSHGNLLSNAlTLVdYWRF--TPDDVLIHALPIFHTHGLFVATNVALLAGASMIFLPKF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 315 SAsrfwDDCIKY--NCTIVQYIGELCRYLLNQP--PREAENqhqvRMAL---GNG-LRQSIWTNFSSRF-HipQVAEFYG 385
Cdd:PRK07514 233 DP----DAVLALmpRATVMMGVPTFYTRLLQEPrlTREAAA----HMRLfisGSApLLAETHREFQERTgH--AILERYG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 386 ATECNCSLGN-FDSQ--VGACGFnsrilsfvyPIRLVRVNedtmelIRGPD-GVciPCQPGEPGQlvgriIQ-KDPlRRF 460
Cdd:PRK07514 303 MTETNMNTSNpYDGErrAGTVGF---------PLPGVSLR------VTDPEtGA--ELPPGEIGM-----IEvKGP-NVF 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 461 DGYLNqgaNNKKIAKDVfkKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLDMADVAVYGVE 540
Cdd:PRK07514 360 KGYWR---MPEKTAEEF--RADGFFITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVP 434
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 40807357 541 VPGTeGRAGMAA-VASPTGNCDLERFAQVLEKELPLYARPIFLRLLPELHKTGTYKFQKTELRKE 604
Cdd:PRK07514 435 HPDF-GEGVTAVvVPKPGAALDEAAILAALKGRLARFKQPKRVFFVDELPRNTMGKVQKNLLREQ 498
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
103-536 |
1.01e-14 |
|
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: 76.54 E-value: 1.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 103 TFRQLDEYSSSVANFLQAR-GLASGDVAAIFMENrnefvGLWLGMAKLGVEAA-----LINTNL---RRDALLhclTTSR 173
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLER-----SAELVVAILAVLKAgaayvPLDPAYpaeRLAFIL---EDAG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 174 ARALVFGSEMASAICEVhasldPSLSLFCSGSWEPgavppsteHLDPLLKDAPKHLPSCPDkgftDKLFYIYTSGTTGLP 253
Cdd:TIGR01733 73 ARLLLTDSALASRLAGL-----VLPVILLDPLELA--------ALDDAPAPPPPDAPSGPD----DLAYVIYTSGSTGRP 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 254 KAAIVVHSryyRMAALV-----YYGFrmRPNDIVYDCLPLYH--SAGNIVGigqCLLHGMTVVI------RKKFSASRFW 320
Cdd:TIGR01733 136 KGVVVTHR---SLVNLLawlarRYGL--DPDDRVLQFASLSFdaSVEEIFG---ALLAGATLVVppedeeRDDAALLAAL 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 321 DDciKYNCTIVQyigeLCRYLLNQ-PPREAENQHQVRMALGNG--LRQSIWTNFSSRFHIPQVAEFYGATECNCSLGNFD 397
Cdd:TIGR01733 208 IA--EHPVTVLN----LTPSLLALlAAALPPALASLRLVILGGeaLTPALVDRWRARGPGARLINLYGPTETTVWSTATL 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 398 SQVGACGFNSRIlsfvyPI-------RLVRVNEDTMELirgPDGVcipcqPGE---PGQLVGRiiqkdplrrfdGYLNQ- 466
Cdd:TIGR01733 282 VDPDDAPRESPV-----PIgrplantRLYVLDDDLRPV---PVGV-----VGElyiGGPGVAR-----------GYLNRp 337
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 40807357 467 GANNKKIAKDVFKKGDQA--YLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLDMADVAV 536
Cdd:TIGR01733 338 ELTAERFVPDPFAGGDGArlYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
73-586 |
1.25e-14 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 77.89 E-value: 1.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 73 RRTVPILFASTVRRHPDKTALIFEGTdtHWTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGVE 152
Cdd:PRK12467 511 PDCVHQLIEAQARQHPERPALVFGEQ--VLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGA 588
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 153 AALINTNLRRDALLHCLTTSRARALVFGSEMAsAICEVHASLdPSLSLfcsgswepgavppstEHLDPLLKDAPKHLPSC 232
Cdd:PRK12467 589 YVPLDPEYPQDRLAYMLDDSGVRLLLTQSHLL-AQLPVPAGL-RSLCL---------------DEPADLLCGYSGHNPEV 651
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 233 PDKgfTDKLFY-IYTSGTTGLPKAAIVVHSRYYRMAALVYYGFRMRPNDIVYDCLPLYHSAGNIVGIGQcLLHGMTVVIR 311
Cdd:PRK12467 652 ALD--PDNLAYvIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGA-LASGATLHLL 728
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 312 KK---FSASRFWDDCIKYNCTIVQYIGELCRYLLnQPPREAENQHQVRMALG------NGLRQsiWTNFSsrfhiPQVAE 382
Cdd:PRK12467 729 PPdcaRDAEAFAALMADQGVTVLKIVPSHLQALL-QASRVALPRPQRALVCGgealqvDLLAR--VRALG-----PGARL 800
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 383 F--YGATECncslgNFDSQVGACGFNSRILSFVyPIRLVRVNEDTMELirgpDGVCIPCQPGEPGQLvgrIIQKDPLRRf 460
Cdd:PRK12467 801 InhYGPTET-----TVGVSTYELSDEERDFGNV-PIGQPLANLGLYIL----DHYLNPVPVGVVGEL---YIGGAGLAR- 866
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 461 dGYLNQGA-NNKKIAKDVF-KKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEgtlSRLLDMADVAVYG 538
Cdd:PRK12467 867 -GYHRRPAlTAERFVPDPFgADGGRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIE---ARLLAQPGVREAV 942
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 40807357 539 VEVPGTEGRAGMAAVASPTGNCD-------LERFAQVLEKELPLYARP---IFLRLLP 586
Cdd:PRK12467 943 VLAQPGDAGLQLVAYLVPAAVADgaehqatRDELKAQLRQVLPDYMVPahlLLLDSLP 1000
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
74-601 |
1.48e-14 |
|
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: 76.60 E-value: 1.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 74 RTVPILFASTVRRHPDKTALIfeGTDTHWTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGVEA 153
Cdd:cd05920 15 EPLGDLLARSAARHPDRIAVV--DGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAVP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 154 ALINTNLRRDALLHCLTTSRARALVfgsemasaICEVHASLDPslslfcsgswepgavppstehldplLKDAPKHLPSCP 233
Cdd:cd05920 93 VLALPSHRRSELSAFCAHAEAVAYI--------VPDRHAGFDH-------------------------RALARELAESIP 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 234 DKGftdklFYIYTSGTTGLPKAAIVVHSRYYRM--AALVYYGFRmrpNDIVYDC-LPLYHS-AGNIVGIGQCLLHGMTVV 309
Cdd:cd05920 140 EVA-----LFLLSGGTTGTPKLIPRTHNDYAYNvrASAEVCGLD---QDTVYLAvLPAAHNfPLACPGVLGTLLAGGRVV 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 310 irkkFSASRFWDDCI------KYNCTIV------QYIGELCRY-------LLNQ---PPREAENQHQVRMALGNGLRQsi 367
Cdd:cd05920 212 ----LAPDPSPDAAFpliereGVTVTALvpalvsLWLDAAASRradlsslRLLQvggARLSPALARRVPPVLGCTLQQ-- 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 368 wtnfssrfhipqvaeFYGATE---CNCSLGNFDSQVgaCGFNSRILSFVYPIRLVrvnedtmelirgpDGVCIPCQPGEP 444
Cdd:cd05920 286 ---------------VFGMAEgllNYTRLDDPDEVI--IHTQGRPMSPDDEIRVV-------------DEEGNPVPPGEE 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 445 GQLVGRiiqkDPLrRFDGYLNQGANNKKiakdVFKKgDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGT 524
Cdd:cd05920 336 GELLTR----GPY-TIRGYYRAPEHNAR----AFTP-DGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENL 405
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 40807357 525 LSRLLDMADVAVYGVEVPGTEGRAGMAAVASPTGNCDLERFAQVLEKELPLYARPIFLRLLPELHKTGTYKFQKTEL 601
Cdd:cd05920 406 LLRHPAVHDAAVVAMPDELLGERSCAFVVLRDPPPSAAQLRRFLRERGLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
79-603 |
2.43e-14 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 77.30 E-value: 2.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 79 LFASTVRRHPDKTALIFEgtDTHWTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGVEAALINT 158
Cdd:PRK12316 2008 RIAEQAARAPEAIAVVFG--DQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDP 2085
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 159 NLRRDALLHCLTTSRARALVFGSEMASAIcEVHASLdPSLSLFCSGSWEPGavpPSTehlDPLLKDAPKHLPscpdkgft 238
Cdd:PRK12316 2086 NYPAERLAYMLEDSGAALLLTQRHLLERL-PLPAGV-ARLPLDRDAEWADY---PDT---APAVQLAGENLA-------- 2149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 239 dklFYIYTSGTTGLPKAAIVVHsryyrmAALVYY------GFRMRPNDIVYDCLPLYHSaGNIVGIGQCLLHGMTVVIR- 311
Cdd:PRK12316 2150 ---YVIYTSGSTGLPKGVAVSH------GALVAHcqaageRYELSPADCELQFMSFSFD-GAHEQWFHPLLNGARVLIRd 2219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 312 -KKFSASRFWDDCIKYNCTIV-------QYIGELCRYLLNQPP-------REAENQHQVRMALgNGLRQSIWTNfssrfh 376
Cdd:PRK12316 2220 dELWDPEQLYDEMERHGVTILdfppvylQQLAEHAERDGRPPAvrvycfgGEAVPAASLRLAW-EALRPVYLFN------ 2292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 377 ipqvaeFYGATECNCSLGNFDSQ-VGACGfnsrilSFVYPIRLVRVNEDTMELirgpDGVCIPCQPGEPGQLVgriIQKD 455
Cdd:PRK12316 2293 ------GYGPTEAVVTPLLWKCRpQDPCG------AAYVPIGRALGNRRAYIL----DADLNLLAPGMAGELY---LGGE 2353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 456 PLRRfdGYLNQ-GANNKKIAKDVF-KKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLDMAD 533
Cdd:PRK12316 2354 GLAR--GYLNRpGLTAERFVPDPFsASGERLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVRE 2431
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 40807357 534 VAVygVEVPGTEGRAGMAAVASPTGNCDL-ERFAQVLEKELPLYARPIFLRLLPELHKTGTYKFQKTELRK 603
Cdd:PRK12316 2432 AVV--VAQDGASGKQLVAYVVPDDAAEDLlAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPK 2500
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
88-554 |
2.95e-14 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 75.79 E-value: 2.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 88 PDKTALIFEGTDTHWTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGVEAALIN-----TNLRR 162
Cdd:PLN02246 37 SDRPCLIDGATGRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANpfytpAEIAK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 163 DAllhclTTSRARALVFGSEMASAICEVHAslDPSLSLFCSGSWEPGAVppsteHLDPLLKDAPKHLPSC---PDkgftD 239
Cdd:PLN02246 117 QA-----KASGAKLIITQSCYVDKLKGLAE--DDGVTVVTIDDPPEGCL-----HFSELTQADENELPEVeisPD----D 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 240 KLFYIYTSGTTGLPKAAIVVH-SRYYRMAALV---YYGFRMRPNDIVYDCLPLYHsagnIVGIGQCLLHGM----TVVIR 311
Cdd:PLN02246 181 VVALPYSSGTTGLPKGVMLTHkGLVTSVAQQVdgeNPNLYFHSDDVILCVLPMFH----IYSLNSVLLCGLrvgaAILIM 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 312 KKFSASRFWDDCIKYNCTIVQYIGELCRYLLNQPPREAENQHQVRMALGNG--LRQSIWTNFSSRFHIPQVAEFYGATEC 389
Cdd:PLN02246 257 PKFEIGALLELIQRHKVTIAPFVPPIVLAIAKSPVVEKYDLSSIRMVLSGAapLGKELEDAFRAKLPNAVLGQGYGMTEA 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 390 ----NCSLG----NFDSQVGACGfnsrilSFVYPIRLVRVNEDT-MELIRGpdgvcipcQPGEPGqLVGRIIQKdplrrf 460
Cdd:PLN02246 337 gpvlAMCLAfakePFPVKSGSCG------TVVRNAELKIVDPETgASLPRN--------QPGEIC-IRGPQIMK------ 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 461 dGYLNQ-GANNKKIAKDvfkkgdqAYL-TGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLDMADVAVyg 538
Cdd:PLN02246 396 -GYLNDpEATANTIDKD-------GWLhTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAV-- 465
|
490
....*....|....*.
gi 40807357 539 veVPGTEGRAGMAAVA 554
Cdd:PLN02246 466 --VPMKDEVAGEVPVA 479
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
70-602 |
4.97e-14 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 75.30 E-value: 4.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 70 LQERRTVPILFASTVRRHPDKTALIFEGTDThwTFRQLDEYSSSVANFLQAR-GLASGDVAAIFMENRNEFVGLWLGMAK 148
Cdd:PRK08751 21 LEQFRTVAEVFATSVAKFADRPAYHSFGKTI--TYREADQLVEQFAAYLLGElQLKKGDRVALMMPNCLQYPIATFGVLR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 149 LGVEAALINTNLRRDALLHCLTTSRARALV----FGSEMASAICEVhasldPSLSLFCSGSWEPGAVPPST------EHL 218
Cdd:PRK08751 99 AGLTVVNVNPLYTPRELKHQLIDSGASVLVvidnFGTTVQQVIADT-----PVKQVITTGLGDMLGFPKAAlvnfvvKYV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 219 DPLLKD---------------APKHLPSCPDKGFTDKLFYIYTSGTTGLPKAAIVVHSryyRMAA--------LVYYGFR 275
Cdd:PRK08751 174 KKLVPEyringairfrealalGRKHSMPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHR---NLVAnmqqahqwLAGTGKL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 276 MRPNDIVYDCLPLYH----SAGNIV--GIGQCllhgmTVVIRKKFSASRFWDDCIKYNCTIVQYIGELCRYLLNQPPREA 349
Cdd:PRK08751 251 EEGCEVVITALPLYHifalTANGLVfmKIGGC-----NHLISNPRDMPGFVKELKKTRFTAFTGVNTLFNGLLNTPGFDQ 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 350 ENQHQVRMALGNGL--RQSIWTNFSSRFHIPQVaEFYGATEcncslgnfdSQVGACgfnsrilsfVYPIRLVRVNedtme 427
Cdd:PRK08751 326 IDFSSLKMTLGGGMavQRSVAERWKQVTGLTLV-EAYGLTE---------TSPAAC---------INPLTLKEYN----- 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 428 lirGPDGVCIP----CQPGEPGQL-----VGRIIQKDPlRRFDGYLNQGANNKKIAkdvfkKGDQAYLTGDVLVMDELGY 498
Cdd:PRK08751 382 ---GSIGLPIPstdaCIKDDAGTVlaigeIGELCIKGP-QVMKGYWKRPEETAKVM-----DADGWLHTGDIARMDEQGF 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 499 LYFRDRTGDTFRWKGENVSTTEVEGTLSRLLDMADVAVYGveVPGTE-GRAGMAAVASPTGNCDLERFAQVLEKELPLYA 577
Cdd:PRK08751 453 VYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVG--VPDEKsGEIVKVVIVKKDPALTAEDVKAHARANLTGYK 530
|
570 580
....*....|....*....|....*
gi 40807357 578 RPIFLRLLPELHKTGTYKFQKTELR 602
Cdd:PRK08751 531 QPRIIEFRKELPKTNVGKILRRELR 555
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
89-539 |
1.15e-13 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 74.16 E-value: 1.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 89 DKTALIFEGTDTH--WTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALL 166
Cdd:PRK04319 59 DKVALRYLDASRKekYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVR 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 167 HCLTTSRARALVFGSEMASAIceVHASLdPSL-SLFCSGswEPGAVPPSTEHLDPLLKDAPKHLPsCPDKGFTDKLFYIY 245
Cdd:PRK04319 139 DRLEDSEAKVLITTPALLERK--PADDL-PSLkHVLLVG--EDVEEGPGTLDFNALMEQASDEFD-IEWTDREDGAILHY 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 246 TSGTTGLPKAAIVVHSRYYRMAALVYYGFRMRPNDIvYDClplyhSA------GNIVGIGQCLLHGMTVVIRK-KFSASR 318
Cdd:PRK04319 213 TSGSTGKPKGVLHVHNAMLQHYQTGKYVLDLHEDDV-YWC-----TAdpgwvtGTSYGIFAPWLNGATNVIDGgRFSPER 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 319 FWDDCIKYNCTiVQYigelcryllnqpprEAENQHQVRMALGNGLRQSIwtNFSSRFHIPQVAE------------FYG- 385
Cdd:PRK04319 287 WYRILEDYKVT-VWY--------------TAPTAIRMLMGAGDDLVKKY--DLSSLRHILSVGEplnpevvrwgmkVFGl 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 386 -------ATE------CNcsLGNFDSQVGACGfnsrilsfvYPI-----RLVRvnedtmeliRGPDGVcipcQPGEPGQL 447
Cdd:PRK04319 350 pihdnwwMTEtggimiAN--YPAMDIKPGSMG---------KPLpgieaAIVD---------DQGNEL----PPNRMGNL 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 448 VgriiqkdpLRR-----FDGYLNQGANNKKiakdVFKKGdqAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVE 522
Cdd:PRK04319 406 A--------IKKgwpsmMRGIWNNPEKYES----YFAGD--WYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVE 471
|
490
....*....|....*..
gi 40807357 523 gtlSRLLDMADVAVYGV 539
Cdd:PRK04319 472 ---SKLMEHPAVAEAGV 485
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
84-540 |
1.93e-13 |
|
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: 73.50 E-value: 1.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 84 VRRH-----PDKTALIFE----GTDTHWTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGVeaa 154
Cdd:cd05967 56 LDRHveagrGDQIALIYDspvtGTERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGA--- 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 155 lintnlrrdalLHclttsrarALVFG----SEMASAICEVhaslDPSLSLFCSGSWEPGAVPPSTEHLDPLLKDA---PK 227
Cdd:cd05967 133 -----------IH--------SVVFGgfaaKELASRIDDA----KPKLIVTASCGIEPGKVVPYKPLLDKALELSghkPH 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 228 HL-----PSCP----DKGF---------------------TDKLFYIYTSGTTGLPKAaiVVHSRYYRMAALVYygfRMR 277
Cdd:cd05967 190 HVlvlnrPQVPadltKPGRdldwsellakaepvdcvpvaaTDPLYILYTSGTTGKPKG--VVRDNGGHAVALNW---SMR 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 278 pndIVYDCLP--LYHSA---GNIVG----IGQCLLHGMTVVIRKKF-----SASRFWDDCIKYNCTIVQYIGELCRYLLN 343
Cdd:cd05967 265 ---NIYGIKPgdVWWAAsdvGWVVGhsyiVYGPLLHGATTVLYEGKpvgtpDPGAFWRVIEKYQVNALFTAPTAIRAIRK 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 344 QPPREAENQHQVRMALGN----GLRQSIWT-NFSSR-FHIPqVAEFYGATE------CNCS-LGNFDSQVGAC-----GF 405
Cdd:cd05967 342 EDPDGKYIKKYDLSSLRTlflaGERLDPPTlEWAENtLGVP-VIDHWWQTEtgwpitANPVgLEPLPIKAGSPgkpvpGY 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 406 NSRILSfvypirlvrvneDTMElirgpdgvciPCQPGEpgqlVGRIIQKDPLRrfDGYLNQGANNKKIAKDV-FKKGDQA 484
Cdd:cd05967 421 QVQVLD------------EDGE----------PVGPNE----LGNIVIKLPLP--PGCLLTLWKNDERFKKLyLSKFPGY 472
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 40807357 485 YLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLDMADVAVYGVE 540
Cdd:cd05967 473 YDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVR 528
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
84-588 |
1.99e-13 |
|
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: 72.66 E-value: 1.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 84 VRRHPDKTALIFEGTDthWTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGveAALINTNLRrd 163
Cdd:cd05945 1 AAANPDRPAVVEGGRT--LTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAG--HAYVPLDAS-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 164 allhcLTTSRARALVfgsEMASaicevhasldPSLsLFCSGswepgavppstehldpllkdapkhlpscpdkgftDKLFY 243
Cdd:cd05945 75 -----SPAERIREIL---DAAK----------PAL-LIADG----------------------------------DDNAY 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 244 I-YTSGTTGLPKAaiVVHSRyyrmAALVYYG------FRMRPNDiVYDCLPLYHSAGNIVGIGQCLLHGMTVVIRKKfsa 316
Cdd:cd05945 102 IiFTSGSTGRPKG--VQISH----DNLVSFTnwmlsdFPLGPGD-VFLNQAPFSFDLSVMDLYPALASGATLVPVPR--- 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 317 srfwddcikyncTIVQYIGELCRYLlnqppreaeNQHQV----------RMALGNG---------LRQSIwtnFS----- 372
Cdd:cd05945 172 ------------DATADPKQLFRFL---------AEHGItvwvstpsfaAMCLLSPtftpeslpsLRHFL---FCgevlp 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 373 --------SRFhiPQVAEF--YGATECN--CSLGNFDSQVGACgfNSRIlsfvyPIRlvRVNEDTMELIRGPDGVCIPcq 440
Cdd:cd05945 228 hktaralqQRF--PDARIYntYGPTEATvaVTYIEVTPEVLDG--YDRL-----PIG--YAKPGAKLVILDEDGRPVP-- 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 441 PGEPGQLVGRIIQkdplrRFDGYLNqgaNNKKIAKDVFK-KGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTT 519
Cdd:cd05945 295 PGEKGELVISGPS-----VSKGYLN---NPEKTAAAFFPdEGQRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELE 366
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 40807357 520 EVEGTLSRLLDMADVAVygVEVPGTEGRAGMAAVASPTGNCDLE---RFAQVLEKELPLYARPIFLRLLPEL 588
Cdd:cd05945 367 EIEAALRQVPGVKEAVV--VPKYKGEKVTELIAFVVPKPGAEAGltkAIKAELAERLPPYMIPRRFVYLDEL 436
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
102-525 |
2.86e-13 |
|
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: 72.24 E-value: 2.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 102 WTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALLHCLTTSRARALVfgs 181
Cdd:cd05907 6 ITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALF--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 182 emasaicevhasldpslslfcsgswepgavppsTEHLDPLLKdapkhlpscpdkgftdklfYIYTSGTTGLPKAAIVVHS 261
Cdd:cd05907 83 ---------------------------------VEDPDDLAT-------------------IIYTSGTTGRPKGVMLSHR 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 262 RYYRMAALVYYGFRMRPNDIVYDCLPLYHSAGNIVGIGQCLLHGMTVVIrkkFSASRfwddcikyncTIVQYIGELCRYL 341
Cdd:cd05907 111 NILSNALALAERLPATEGDRHLSFLPLAHVFERRAGLYVPLLAGARIYF---ASSAE----------TLLDDLSEVRPTV 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 342 LNQPPREAENQHQ-VRMALGNGLRQSI--WTNFSS-RFHI-------PQVAEF-----------YGATEC----NCSLGN 395
Cdd:cd05907 178 FLAVPRVWEKVYAaIKVKAVPGLKRKLfdLAVGGRlRFAAsggaplpAELLHFfralgipvyegYGLTETsavvTLNPPG 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 396 fDSQVGACGfnsrilSFVYPIRlVRVNEDTMELIRGPdGVcipcqpgepgqlvgriiqkdplrrFDGYLNqgaNNKKIAK 475
Cdd:cd05907 258 -DNRIGTVG------KPLPGVE-VRIADDGEILVRGP-NV------------------------MLGYYK---NPEATAE 301
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 40807357 476 DVFKkgDQAYLTGDVLVMDELGYLYFRDRTGDTFRW-KGENVSTTEVEGTL 525
Cdd:cd05907 302 ALDA--DGWLHTGDLGEIDEDGFLHITGRKKDLIITsGGKNISPEPIENAL 350
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
88-601 |
3.26e-13 |
|
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341311 [Multi-domain] Cd Length: 479 Bit Score: 72.12 E-value: 3.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 88 PDKTALIFEgtDTHWTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALLH 167
Cdd:cd17656 2 PDAVAVVFE--NQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 168 CLTTSRARALVFGSEMASAIC---EVHASLDPSLSlfcsgswepgavPPSTEHLDplLKDAPKHLpscpdkgftdkLFYI 244
Cdd:cd17656 80 IMLDSGVRVVLTQRHLKSKLSfnkSTILLEDPSIS------------QEDTSNID--YINNSDDL-----------LYII 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 245 YTSGTTGLPKAAIVVHSryyRMAALVYYGFRMRPNDIVYDCLPL--------YHSagnivgIGQCLLHGMTV-VIRK--K 313
Cdd:cd17656 135 YTSGTTGKPKGVQLEHK---NMVNLLHFEREKTNINFSDKVLQFatcsfdvcYQE------IFSTLLSGGTLyIIREetK 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 314 FSASRFWDDCIKYNCTIVQYIGELCRYLLNQppREAENQ--HQVRMALGNGLRQSIWTNFSSRFHIPQVA--EFYGATEC 389
Cdd:cd17656 206 RDVEQLFDLVKRHNIEVVFLPVAFLKFIFSE--REFINRfpTCVKHIITAGEQLVITNEFKEMLHEHNVHlhNHYGPSET 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 390 NCslgnfdsqVGACGFNSRILSFVY-PIRLVRVNEDTmeLIRGPDGVCIPCqpGEPGQLVgriIQKDPLRRfdGYLN-QG 467
Cdd:cd17656 284 HV--------VTTYTINPEAEIPELpPIGKPISNTWI--YILDQEQQLQPQ--GIVGELY---ISGASVAR--GYLNrQE 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 468 ANNKKIAKDVFKKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLDMADVAVYGVEvpGTEGR 547
Cdd:cd17656 347 LTAEKFFPDPFDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKA--DDKGE 424
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 40807357 548 AGMAAVASPTGNCDLERFAQVLEKELPLYARPIFLRLLPELHKTGTYKFQKTEL 601
Cdd:cd17656 425 KYLCAYFVMEQELNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
239-573 |
9.44e-13 |
|
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: 69.61 E-value: 9.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 239 DKLFYIYTSGTTGLPKAAIVVHSRYYRMAALVYYGFRMRPNDIVYDCLPLYHSAGniVGIGQCLLH--GMTVVIRKkFSA 316
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPLFHIAG--LNLALATFHagGANVVMEK-FDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 317 SRFWDDCIKYNCTivqYIGELCRYLLNQPPREAENQHQV---RMALGNGLRQSIwtnfsSRFHIPQVAEF---YGATECN 390
Cdd:cd17637 78 AEALELIEEEKVT---LMGSFPPILSNLLDAAEKSGVDLsslRHVLGLDAPETI-----QRFEETTGATFwslYGQTETS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 391 C--SLGNFDSQVGACGfnsRILsfvyPIRLVR-VNEDTMELirgPDGvcipcQPGEpgqlvgrIIQKDPLRrFDGYLNQG 467
Cdd:cd17637 150 GlvTLSPYRERPGSAG---RPG----PLVRVRiVDDNDRPV---PAG-----ETGE-------IVVRGPLV-FQGYWNLP 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 468 ANNKKiakdVFKKGdqAYLTGDVLVMDELGYLYFRDRTGDTFRWK--GENVSTTEVEGTLSRLLDMADVAVYGveVPGTE 545
Cdd:cd17637 207 ELTAY----TFRNG--WHHTGDLGRFDEDGYLWYAGRKPEKELIKpgGENVYPAEVEKVILEHPAIAEVCVIG--VPDPK 278
|
330 340
....*....|....*....|....*...
gi 40807357 546 GRAGMAAVasptgnCDLERFAQVLEKEL 573
Cdd:cd17637 279 WGEGIKAV------CVLKPGATLTADEL 300
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
77-604 |
1.01e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 70.75 E-value: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 77 PILF-ASTVRRHPDKTALIFEgtDTHWTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGveaAL 155
Cdd:PRK08162 20 PLSFlERAAEVYPDRPAVIHG--DRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAG---AV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 156 INT-NLRRDA--LLHCLTTSRARALVFGSEMASAICEVhASLDPSLSLFC----SGSWEPGAVPPSTEHLDPLLKDAPKH 228
Cdd:PRK08162 95 LNTlNTRLDAasIAFMLRHGEAKVLIVDTEFAEVAREA-LALLPGPKPLVidvdDPEYPGGRFIGALDYEAFLASGDPDF 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 229 LPSCPDKGFtDKLFYIYTSGTTGLPKAaIVVHSR-YYRMAA--LVYYGFRMRPndiVYD-CLPLYH------------SA 292
Cdd:PRK08162 174 AWTLPADEW-DAIALNYTSGTTGNPKG-VVYHHRgAYLNALsnILAWGMPKHP---VYLwTLPMFHcngwcfpwtvaaRA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 293 GNIVgigqCLlhgmtvvirKKFSASRFWDDCIKYNCT------IVQYIgelcryLLNQPPREAEN-QHQVR--------- 356
Cdd:PRK08162 249 GTNV----CL---------RKVDPKLIFDLIREHGVThycgapIVLSA------LINAPAEWRAGiDHPVHamvagaapp 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 357 MALGNGLRQSiwtnfssRFHIPQV---AEFYG-ATECNCSLG----NFDSQVGacgFNSRiLSFVYPIR-LVRV-NEDTM 426
Cdd:PRK08162 310 AAVIAKMEEI-------GFDLTHVyglTETYGpATVCAWQPEwdalPLDERAQ---LKAR-QGVRYPLQeGVTVlDPDTM 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 427 ELIrgP-DGVCIpcqpgepGQLV--GRIIQKdplrrfdGYLNqganNKKIAKDVFKKGdqAYLTGDVLVMDELGYLYFRD 503
Cdd:PRK08162 379 QPV--PaDGETI-------GEIMfrGNIVMK-------GYLK----NPKATEEAFAGG--WFHTGDLAVLHPDGYIKIKD 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 504 RTGDTFRWKGENVSTTEVEGTLSRLLDMADVAV-------YGvEVPGT--EGRAGMAAVASptgncDLERFAQvleKELP 574
Cdd:PRK08162 437 RSKDIIISGGENISSIEVEDVLYRHPAVLVAAVvakpdpkWG-EVPCAfvELKDGASATEE-----EIIAHCR---EHLA 507
|
570 580 590
....*....|....*....|....*....|
gi 40807357 575 LYARPIFLRlLPELHKTGTYKFQKTELRKE 604
Cdd:PRK08162 508 GFKVPKAVV-FGELPKTSTGKIQKFVLREQ 536
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
84-309 |
1.43e-12 |
|
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: 70.35 E-value: 1.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 84 VRRHPDKTALIF----EGTDTHWTFRQLDEYSSSVANFLQARGLAsGDVAAIFMENRNEFVGLWLG--MAKL-GVEAALI 156
Cdd:cd05931 3 AAARPDRPAYTFlddeGGREETLTYAELDRRARAIAARLQAVGKP-GDRVLLLAPPGLDFVAAFLGclYAGAiAVPLPPP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 157 NTNLRRDALLHCLTTSRARALVFGSEMASAICEVHASLdpslslfcsgswePGAVPPSTEHLDPLLKDAPKHLPsCPDKG 236
Cdd:cd05931 82 TPGRHAERLAAILADAGPRVVLTTAAALAAVRAFAASR-------------PAAGTPRLLVVDLLPDTSAADWP-PPSPD 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 40807357 237 FTDKLFYIYTSGTTGLPKAAIVVHsryyrmAALVY------YGFRMRPNDIVYDCLPLYHSAGNIVGIGQCLLHGMTVV 309
Cdd:cd05931 148 PDDIAYLQYTSGSTGTPKGVVVTH------RNLLAnvrqirRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGPSV 220
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
88-543 |
2.72e-12 |
|
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: 69.48 E-value: 2.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 88 PDKTALIFEGTDTHWTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALLH 167
Cdd:cd17642 31 PGTIAFTDAHTGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDH 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 168 CLTTSRARaLVFGSEMA-SAICEVHASLDPSLSLFCSGSWEPGAVPPS-----TEHLDPLLkDAPKHLPSCPDKGfTDKL 241
Cdd:cd17642 111 SLNISKPT-IVFCSKKGlQKVLNVQKKLKIIKTIIILDSKEDYKGYQClytfiTQNLPPGF-NEYDFKPPSFDRD-EQVA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 242 FYIYTSGTTGLPKAAIVVHsryyrMAALV--------YYGFRMRPNDIVYDCLPLYHSAGNIVGIGQcLLHGMTVVIRKK 313
Cdd:cd17642 188 LIMNSSGSTGLPKGVQLTH-----KNIVArfshardpIFGNQIIPDTAILTVIPFHHGFGMFTTLGY-LICGFRVVLMYK 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 314 FSASRFWDDCIKYNCTIVQYIGELCRYLLNQPPREAEN-QHQVRMALGNG-LRQSIWTNFSSRFHIPQVAEFYGATECNC 391
Cdd:cd17642 262 FEEELFLRSLQDYKVQSALLVPTLFAFFAKSTLVDKYDlSNLHEIASGGApLSKEVGEAVAKRFKLPGIRQGYGLTETTS 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 392 SL---GNFDSQVGACGfnsRILSFVYpirlVRVNEDTMELIRGPDgvcipcqpgEPGQLV--GRIIQKdplrrfdGYLNq 466
Cdd:cd17642 342 AIlitPEGDDKPGAVG---KVVPFFY----AKVVDLDTGKTLGPN---------ERGELCvkGPMIMK-------GYVN- 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 467 ganNKKIAKDVFKKgDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLDMADVAVYGV------E 540
Cdd:cd17642 398 ---NPEATKALIDK-DGWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIpdedagE 473
|
...
gi 40807357 541 VPG 543
Cdd:cd17642 474 LPA 476
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
88-552 |
2.72e-12 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 70.58 E-value: 2.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 88 PDKTALIF----EGTDTHWTFRQLDEYSSSVANFLQARGlASGDVAAIFMENRNEFVGLWLGMAKLGVEA--ALINTNLR 161
Cdd:PRK05691 23 PDRLALRFladdPGEGVVLSYRDLDLRARTIAAALQARA-SFGDRAVLLFPSGPDYVAAFFGCLYAGVIAvpAYPPESAR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 162 R---DALLHCLTTSRARALVFGSEMASAICEVHASLDPSL-SLFCsgswepgavppsTEHLDPLLKDAPKHLPSCPDkgf 237
Cdd:PRK05691 102 RhhqERLLSIIADAEPRLLLTVADLRDSLLQMEELAAANApELLC------------VDTLDPALAEAWQEPALQPD--- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 238 tDKLFYIYTSGTTGLPKAAIVVHSRYYRMAALVYYGFRMR--PNDIVYDCLPLYHSAGNIVGIGQCLLHGMTVVIrkkFS 315
Cdd:PRK05691 167 -DIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGIDlnPDDVIVSWLPLYHDMGLIGGLLQPIFSGVPCVL---MS 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 316 ASRFWDDCIKYNCTIVQYIGElcrylLNQPPREAENQHQVRMALGN--GLRQSIW-TNFSSRFHIPQVaefygatecncS 392
Cdd:PRK05691 243 PAYFLERPLRWLEAISEYGGT-----ISGGPDFAYRLCSERVSESAleRLDLSRWrVAYSGSEPIRQD-----------S 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 393 LGNFDSQVGACGFNSRILSFVY----------------PIRLVRVNEDTMELIRGPDG---VCIPCQPGEPGQLVgRIIQ 453
Cdd:PRK05691 307 LERFAEKFAACGFDPDSFFASYglaeatlfvsggrrgqGIPALELDAEALARNRAEPGtgsVLMSCGRSQPGHAV-LIVD 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 454 KDPLRRFD----------------GYLNqgaNNKKIAKDVFKKGDQAYL-TGDVLVMDElGYLYFRDRTGDTFRWKGENV 516
Cdd:PRK05691 386 PQSLEVLGdnrvgeiwasgpsiahGYWR---NPEASAKTFVEHDGRTWLrTGDLGFLRD-GELFVTGRLKDMLIVRGHNL 461
|
490 500 510
....*....|....*....|....*....|....*....
gi 40807357 517 STTEVEGTLSRLLDMA---DVAVYGVEVPGTEGrAGMAA 552
Cdd:PRK05691 462 YPQDIEKTVEREVEVVrkgRVAAFAVNHQGEEG-IGIAA 499
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
89-603 |
3.55e-12 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 69.54 E-value: 3.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 89 DKTALIFEGT----DTHWTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGVEAALINTNLRRDA 164
Cdd:PLN02654 104 DKIAIYWEGNepgfDASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAES 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 165 L------------LHCLTTSRARALVFGSEMasaiceVHASLDPS----LSLFCSGSWEPGAV-----PPSTEHLDPLLK 223
Cdd:PLN02654 184 LaqrivdckpkvvITCNAVKRGPKTINLKDI------VDAALDESakngVSVGICLTYENQLAmkredTKWQEGRDVWWQ 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 224 D-APKHLPSCPDKGF--TDKLFYIYTSGTTGLPKAAIVVHSRYYRMAALVY-YGFRMRPNDIVY---DClplyhsaGNIV 296
Cdd:PLN02654 258 DvVPNYPTKCEVEWVdaEDPLFLLYTSGSTGKPKGVLHTTGGYMVYTATTFkYAFDYKPTDVYWctaDC-------GWIT 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 297 GIGQC----LLHGMTVVIRKKF----SASRFWDDCIKYNCTIVQYIGELCRYLLNQPP----REAENQHQVRMALGNGLR 364
Cdd:PLN02654 331 GHSYVtygpMLNGATVLVFEGApnypDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGDeyvtRHSRKSLRVLGSVGEPIN 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 365 QSIWTNFssrFHIpqvaefYGATECNCSLGNFDSQVGacGFNSRILSFVYP------------IRLVRVNEDTMELirgp 432
Cdd:PLN02654 411 PSAWRWF---FNV------VGDSRCPISDTWWQTETG--GFMITPLPGAWPqkpgsatfpffgVQPVIVDEKGKEI---- 475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 433 DGVC---IPCQPGEPGQLvgRIIQKDPLRRFDGYlnqgannkkiakdvFKKGDQAYLTGDVLVMDELGYLYFRDRTGDTF 509
Cdd:PLN02654 476 EGECsgyLCVKKSWPGAF--RTLYGDHERYETTY--------------FKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVI 539
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 510 RWKGENVSTTEVEGTLSRLLDMADVAVYGV--EVPGTEGRAGMAAVASPTGNCDLER-FAQVLEKELPLYARPIFLRLLP 586
Cdd:PLN02654 540 NVSGHRIGTAEVESALVSHPQCAEAAVVGIehEVKGQGIYAFVTLVEGVPYSEELRKsLILTVRNQIGAFAAPDKIHWAP 619
|
570
....*....|....*..
gi 40807357 587 ELHKTGTYKFQKTELRK 603
Cdd:PLN02654 620 GLPKTRSGKIMRRILRK 636
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
88-591 |
3.74e-12 |
|
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: 68.87 E-value: 3.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 88 PDKTALIFEgtDTHWTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGveAALIntnlrrdallh 167
Cdd:cd17643 1 PEAVAVVDE--DRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAG--GAYV----------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 168 clttsraralvfgsemasaicevhaSLDPslslfcsgswepgAVPPstEHLDPLLKDA-PKHLPSCPDkgftDKLFYIYT 246
Cdd:cd17643 66 -------------------------PIDP-------------AYPV--ERIAFILADSgPSLLLTDPD----DLAYVIYT 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 247 SGTTGLPKAAIVVHSRYYRMAALVYYGFRMRPNDIVYdclpLYHSAG------NIVGigqCLLHGMTVVIRKKF---SAS 317
Cdd:cd17643 102 SGSTGRPKGVVVSHANVLALFAATQRWFGFNEDDVWT----LFHSYAfdfsvwEIWG---ALLHGGRLVVVPYEvarSPE 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 318 RFWDDCIKYNCTIvqyigelcrylLNQPP-----------REAENQHQVRMAL--GNGLRQSIWTNFSSRF--HIPQVAE 382
Cdd:cd17643 175 DFARLLRDEGVTV-----------LNQTPsafyqlveaadRDGRDPLALRYVIfgGEALEAAMLRPWAGRFglDRPQLVN 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 383 FYGATEcncslgnfdsqvgACGFNSrilsfVYPIRLVRVNEDTMELIRGP-----------DGVCIPcqPGEPGQLVgri 451
Cdd:cd17643 244 MYGITE-------------TTVHVT-----FRPLDAADLPAAAASPIGRPlpglrvyvldaDGRPVP--PGVVGELY--- 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 452 IQKDPLRRfdGYLNQ-GANNKKIAKDVFKK-GDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLL 529
Cdd:cd17643 301 VSGAGVAR--GYLGRpELTAERFVANPFGGpGSRMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHP 378
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 530 DMADVAVYGVE-VPGTE-------GRAGMAAVASptgncDLERFAQVLekeLPLYARPIFLRLLPELHKT 591
Cdd:cd17643 379 SVRDAAVIVREdEPGDTrlvayvvADDGAAADIA-----ELRALLKEL---LPDYMVPARYVPLDALPLT 440
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
70-602 |
5.95e-12 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 68.51 E-value: 5.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 70 LQERRTVPILFASTVRR----HPDKTALIFegTDTHWTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLG 145
Cdd:PLN03102 6 LCEANNVPLTPITFLKRasecYPNRTSIIY--GKTRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 146 MAKLGVEAALINTNLRRDALLHCLTTSRARALVFGSEMASAICEVhasldpsLSLFCSGSWEPG-----------AVPPS 214
Cdd:PLN03102 84 VPMAGAVLNPINTRLDATSIAAILRHAKPKILFVDRSFEPLAREV-------LHLLSSEDSNLNlpvifiheidfPKRPS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 215 TEHLD---PLLKDAPKhlPSCPDKGFT-----DKLFYIYTSGTTGLPKAAIVVHSRYYRMAALVYYGFRMRPNDIVYDCL 286
Cdd:PLN03102 157 SEELDyecLIQRGEPT--PSLVARMFRiqdehDPISLNYTSGTTADPKGVVISHRGAYLSTLSAIIGWEMGTCPVYLWTL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 287 PLYHSAGNIVGIGQCLLHGMTVVIRKkFSASRFWDDCIKYNCTIVQYIGELCRYLL-----NQPPREAEnqhqVRMALGN 361
Cdd:PLN03102 235 PMFHCNGWTFTWGTAARGGTSVCMRH-VTAPEIYKNIEMHNVTHMCCVPTVFNILLkgnslDLSPRSGP----VHVLTGG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 362 GLRQSIWTNFSSRFHIpQVAEFYGATEcncslgnfdsqvgACGfnsRILSFVYPIRLVRVNEDTMELIRGPDGVCI---- 437
Cdd:PLN03102 310 SPPPAALVKKVQRLGF-QVMHAYGLTE-------------ATG---PVLFCEWQDEWNRLPENQQMELKARQGVSIlgla 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 438 -------PCQPGEP--GQLVGRIIQKDPLRrFDGYLNqganNKKIAKDVFKKGdqaYL-TGDVLVMDELGYLYFRDRTGD 507
Cdd:PLN03102 373 dvdvknkETQESVPrdGKTMGEIVIKGSSI-MKGYLK----NPKATSEAFKHG---WLnTGDVGVIHPDGHVEIKDRSKD 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 508 TFRWKGENVSTTEVEGTLSRLLDMADVAVYGVEVPgTEGRAGMAAVA---SPTGNCDLERFAQVLEKELPLYAR---PIF 581
Cdd:PLN03102 445 IIISGGENISSVEVENVLYKYPKVLETAVVAMPHP-TWGETPCAFVVlekGETTKEDRVDKLVTRERDLIEYCRenlPHF 523
|
570 580
....*....|....*....|....*.
gi 40807357 582 L-----RLLPELHKTGTYKFQKTELR 602
Cdd:PLN03102 524 McprkvVFLQELPKNGNGKILKPKLR 549
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
74-586 |
7.14e-12 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 69.22 E-value: 7.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 74 RTVPILFASTVRRHPDKTALIFEGTDThwTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGVEA 153
Cdd:PRK12316 4551 RCVHQLVAERARMTPDAVAVVFDEEKL--TYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAY 4628
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 154 ALINTNLRRDALLHCLTTSRArALVFGSEMASAICEVHASLDpSLSLFCSGSWEPgavppSTEHlDPLLKDAPKHLPscp 233
Cdd:PRK12316 4629 VPLDPEYPRERLAYMMEDSGA-ALLLTQSHLLQRLPIPDGLA-SLALDRDEDWEG-----FPAH-DPAVRLHPDNLA--- 4697
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 234 dkgftdklFYIYTSGTTGLPKAAIVVHSRYYRMAALVYYGFRMRPNDIVYDCLPlYHSAGNIVGIGQCLLHGMTVVIRKk 313
Cdd:PRK12316 4698 --------YVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMS-FSFDGSHEGLYHPLINGASVVIRD- 4767
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 314 fsaSRFWD------DCIKYNCTIVQYIGELCRYLLNQPPREAENQhQVRMAL--GNGLRQSIWTNFSSRFHIPQVAEFYG 385
Cdd:PRK12316 4768 ---DSLWDperlyaEIHEHRVTVLVFPPVYLQQLAEHAERDGEPP-SLRVYCfgGEAVAQASYDLAWRALKPVYLFNGYG 4843
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 386 ATECNCSLGNFDSQVG-ACGFNSRILSFVYPIRLVRVNEDTMELIrgPDGVCipcqpGE---PGQLVGRiiqkdplrrfd 461
Cdd:PRK12316 4844 PTETTVTVLLWKARDGdACGAAYMPIGTPLGNRSGYVLDGQLNPL--PVGVA-----GElylGGEGVAR----------- 4905
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 462 GYLNQGA-NNKKIAKDVF-KKGDQAYLTGDVL------VMDELGylyfrdRTGDTFRWKGENVSTTEVEGTLSRLLDMAD 533
Cdd:PRK12316 4906 GYLERPAlTAERFVPDPFgAPGGRLYRTGDLAryradgVIDYLG------RVDHQVKIRGFRIELGEIEARLREHPAVRE 4979
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 40807357 534 VAVYGVEVPGTEGRAGM------AAVASPTGNCDL-ERFAQVLEKELPLYARP---IFLRLLP 586
Cdd:PRK12316 4980 AVVIAQEGAVGKQLVGYvvpqdpALADADEAQAELrDELKAALRERLPEYMVPahlVFLARMP 5042
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
85-389 |
1.81e-11 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 66.85 E-value: 1.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 85 RRHPDKTALIFEGT---------DTHwTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGVEAAL 155
Cdd:PRK09274 17 QERPDQLAVAVPGGrgadgklayDEL-SFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGAVPVL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 156 INTNLRRDALLHCLTTSRARALVfgsemasAICEVH----------ASLDPSLSlfCSGSWEPGAVppsteHLDPLLKDA 225
Cdd:PRK09274 96 VDPGMGIKNLKQCLAEAQPDAFI-------GIPKAHlarrlfgwgkPSVRRLVT--VGGRLLWGGT-----TLATLLRDG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 226 PKHLPSCPDKGFTDKLFYIYTSGTTGLPKAAIVVHSRYYRMAALVYYGFRMRPNDIVYDCLPLYhsagniVGIGQCLlhG 305
Cdd:PRK09274 162 AAAPFPMADLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEIDLPTFPLF------ALFGPAL--G 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 306 MTVVI-------------RKKFSASRfwddciKYNCTIV----QYIGELCRYLLNqppreaeNQHQ---VRMALGNG--L 363
Cdd:PRK09274 234 MTSVIpdmdptrpatvdpAKLFAAIE------RYGVTNLfgspALLERLGRYGEA-------NGIKlpsLRRVISAGapV 300
|
330 340
....*....|....*....|....*....
gi 40807357 364 RQSIWTNFSSRFhiPQVAEF---YGATEC 389
Cdd:PRK09274 301 PIAVIERFRAML--PPDAEIltpYGATEA 327
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
75-588 |
3.21e-11 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 66.61 E-value: 3.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 75 TVPILFASTVRRHPDKTALIFEGTdtHWTFRQLDEYSSSVANFLQARGLASGDVAAIFMEnRNEFVGLWLgMAKLGVEAA 154
Cdd:PRK10252 459 TLSALVAQQAAKTPDAPALADARY--QFSYREMREQVVALANLLRERGVKPGDSVAVALP-RSVFLTLAL-HAIVEAGAA 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 155 L--INTNLRRDALLHCLTTSRARALVFGSEMASAICEVhasldPSLSLFCSGSWEPGAVPPstehldPLLKDAPKHLPsc 232
Cdd:PRK10252 535 WlpLDTGYPDDRLKMMLEDARPSLLITTADQLPRFADV-----PDLTSLCYNAPLAPQGAA------PLQLSQPHHTA-- 601
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 233 pdkgftdklFYIYTSGTTGLPKAAIVVHsryyrmAALV--------YYGfrMRPNDIVYDCLPlyhsAGNIVGIGQC--- 301
Cdd:PRK10252 602 ---------YIIFTSGSTGRPKGVMVGQ------TAIVnrllwmqnHYP--LTADDVVLQKTP----CSFDVSVWEFfwp 660
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 302 LLHGMTVVI------RKKFSASRFWDDcikYNCTIVQYIGELCRYLLNQPprEAENQHQVRMAL------GNGLRQSIWT 369
Cdd:PRK10252 661 FIAGAKLVMaepeahRDPLAMQQFFAE---YGVTTTHFVPSMLAAFVASL--TPEGARQSCASLrqvfcsGEALPADLCR 735
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 370 NFSSRFHIPqVAEFYGATE----------CNCSLGNFDSQVGACGF---NSRIlsfvypirlvRVNEDTMElirgpdgvc 436
Cdd:PRK10252 736 EWQQLTGAP-LHNLYGPTEaavdvswypaFGEELAAVRGSSVPIGYpvwNTGL----------RILDARMR--------- 795
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 437 iPCQPGEPGQLVGRIIQkdpLRRfdGYLNQ-GANNKKIAKDVFKKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGEN 515
Cdd:PRK10252 796 -PVPPGVAGDLYLTGIQ---LAQ--GYLGRpDLTASRFIADPFAPGERMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQR 869
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 40807357 516 VSTTEVEGTLSRLLDMADVAVYGVEVPGTEGRAGMAA------VASPTGNCDLERFAQVLEKELPLYARPIFLRLLPEL 588
Cdd:PRK10252 870 IELGEIDRAMQALPDVEQAVTHACVINQAAATGGDARqlvgylVSQSGLPLDTSALQAQLRERLPPHMVPVVLLQLDQL 948
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
103-603 |
6.47e-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: 64.90 E-value: 6.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 103 TFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALlhclttsRARALVFGSE 182
Cdd:cd05974 2 SFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDL-------RDRVDRGGAV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 183 MASAICEVHASldpslslfcsgswepgavppstehlDPLLkdapkhlpscpdkgftdklFYiYTSGTTGLPKaaIVVHS- 261
Cdd:cd05974 75 YAAVDENTHAD-------------------------DPML-------------------LY-FTSGTTSKPK--LVEHTh 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 262 RYYRMAAL-VYYGFRMRPNDIVYDClplyHSAGNIVGIGQCLLH----GMTVVI--RKKFSASRFWDDCIKYNCTIVQYI 334
Cdd:cd05974 108 RSYPVGHLsTMYWIGLKPGDVHWNI----SSPGWAKHAWSCFFApwnaGATVFLfnYARFDAKRVLAALVRYGVTTLCAP 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 335 GELCRYLLNQP-------PREA---------ENQHQVRMALGNGLRQSiwtnfssrfhipqvaefYGATECNCSLGNFDS 398
Cdd:cd05974 184 PTVWRMLIQQDlasfdvkLREVvgageplnpEVIEQVRRAWGLTIRDG-----------------YGQTETTALVGNSPG 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 399 QVGACGFNSRilsfvyPIRLVRVNedtmelIRGPDGvcipcQPGEPGQLVGRIIQKDPLRRFDGYLNQGANNKKIAKDVF 478
Cdd:cd05974 247 QPVKAGSMGR------PLPGYRVA------LLDPDG-----APATEGEVALDLGDTRPVGLMKGYAGDPDKTAHAMRGGY 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 479 kkgdqaYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLDMADVAVygVEVPGTEGRA------GMAA 552
Cdd:cd05974 310 ------YRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAV--VPSPDPVRLSvpkafiVLRA 381
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 40807357 553 VASPTGNCDLERFAQVLEKELPlYARpifLRLLP--ELHKTGTYKFQKTELRK 603
Cdd:cd05974 382 GYEPSPETALEIFRFSRERLAP-YKR---IRRLEfaELPKTISGKIRRVELRR 430
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
239-598 |
8.40e-11 |
|
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: 63.82 E-value: 8.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 239 DKLFYIYTSGTTGLPKAAIVVH-SRYYRMAALVYYGFRMRPNDIVYDCLPLYHSaGNIVGIGQCLLHGMTVVIRKKFSAS 317
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANkTFFAVPDILQKEGLNWVVGDVTYLPLPATHI-GGLWWILTCLIHGGLCVTGGENTTY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 318 R-FWDDCIKYNCTIVQYIGELCRYLLNQPPREAENQHQVRMaLGNGLRQSIWTN--FSSRFHIPQVAEFYGATE----CN 390
Cdd:cd17635 81 KsLFKILTTNAVTTTCLVPTLLSKLVSELKSANATVPSLRL-IGYGGSRAIAADvrFIEATGLTNTAQVYGLSEtgtaLC 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 391 CSLGNFDSQVGACGfnsrilsfvYPIRLVRVNEDTMELIRGPDGvcipcqpGEpgqlvGRIIQKDPlRRFDGYLNqganN 470
Cdd:cd17635 160 LPTDDDSIEINAVG---------RPYPGVDVYLAATDGIAGPSA-------SF-----GTIWIKSP-ANMLGYWN----N 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 471 KKIAKDVFKKGdqaYL-TGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLDMADVAVYgvEVPGTEGRAG 549
Cdd:cd17635 214 PERTAEVLIDG---WVnTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACY--EISDEEFGEL 288
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 40807357 550 MAAVASPTGNCDLERFAQVLEK---ELPLYARPIFLRLLPELHKTGTYKFQK 598
Cdd:cd17635 289 VGLAVVASAELDENAIRALKHTirrELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
113-539 |
9.07e-11 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 64.82 E-value: 9.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 113 SVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALLHCLTTSRARALVFGSEMASAICEVHA 192
Cdd:PLN02860 44 SLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWSFEEAKSAMLLVRPVMLVTDETCSSWYEELQN 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 193 SLDPSLSLFC---SGSWEPGAVPPSTEHLDPLLKDA--PKHLPSC--PDkgftDKLFYIYTSGTTGLPKAAIVVHSRYYR 265
Cdd:PLN02860 124 DRLPSLMWQVfleSPSSSVFIFLNSFLTTEMLKQRAlgTTELDYAwaPD----DAVLICFTSGTTGRPKGVTISHSALIV 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 266 MA----ALVYYGfrmrpNDIVY-DCLPLYHsagnIVGIGQC---LLHGMTVVIRKKFSASRFWDDCIKYNCTIVQYIGEL 337
Cdd:PLN02860 200 QSlakiAIVGYG-----EDDVYlHTAPLCH----IGGLSSAlamLMVGACHVLLPKFDAKAALQAIKQHNVTSMITVPAM 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 338 CRYLLnQPPREAENQHQ---VRMAL--GNGLRQSIWTNFSSRFHIPQVAEFYGATECNCSLGNFDSQVGACGFNSRILSF 412
Cdd:PLN02860 271 MADLI-SLTRKSMTWKVfpsVRKILngGGSLSSRLLPDAKKLFPNAKLFSAYGMTEACSSLTFMTLHDPTLESPKQTLQT 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 413 VYPIRLVRVNEdtmelirgPDGVCIpcqpGEPG---QL---------VGRIIQKDPlRRFDGYLNQganNKKIAKDvfkK 480
Cdd:PLN02860 350 VNQTKSSSVHQ--------PQGVCV----GKPAphvELkigldessrVGRILTRGP-HVMLGYWGQ---NSETASV---L 410
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 481 GDQAYL-TGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLDMADVAVYGV 539
Cdd:PLN02860 411 SNDGWLdTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGV 470
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
244-603 |
1.23e-10 |
|
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: 63.12 E-value: 1.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 244 IYTSGTTGLPKAaiVVHSRY----YRMAALVYYGFRmrPNDIVYDCLPLYHSAGNIVgIGQCLLHGMTVVIRKKFSASRf 319
Cdd:cd17630 6 ILTSGSTGTPKA--VVHTAAnllaSAAGLHSRLGFG--GGDSWLLSLPLYHVGGLAI-LVRSLLAGAELVLLERNQALA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 320 wddcikynctiVQYIGELCRYLLNQPPreaenqhQVRMALGNGLRQS--------------IWTNFSSRF---HIPqVAE 382
Cdd:cd17630 80 -----------EDLAPPGVTHVSLVPT-------QLQRLLDSGQGPAalkslravllggapIPPELLERAadrGIP-LYT 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 383 FYGATEcncslgnFDSQVGACGFNSRILSFVYPI---RLVRVNEDTMELIRGPdgvcipcqpgepgqlvgriiqkdplRR 459
Cdd:cd17630 141 TYGMTE-------TASQVATKRPDGFGRGGVGVLlpgRELRIVEDGEIWVGGA-------------------------SL 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 460 FDGYLNQGannkkIAKDVFKkgDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLDMADVAVYGV 539
Cdd:cd17630 189 AMGYLRGQ-----LVPEFNE--DGWFTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGV 261
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 40807357 540 EVPgtegRAGMAAVASPTGNC--DLERFAQVLEKELPLYARPIFLRLLPELHKTGTYKFQKTELRK 603
Cdd:cd17630 262 PDE----ELGQRPVAVIVGRGpaDPAELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRA 323
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
89-603 |
2.43e-10 |
|
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: 63.22 E-value: 2.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 89 DKTALIFEGT---DTHWTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGVEAALINTNLRRDAL 165
Cdd:cd05915 9 GRKEVVSRLHtgeVHRTTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 166 LHCLTTSRARALVFGSEMASAICEvhasldpSLSLFCSGSWEPGAVPPSTEHLDPLLKDAPKHLPSCP-DKgfTDKLFYI 244
Cdd:cd05915 89 AYILNHAEDKVLLFDPNLLPLVEA-------IRGELKTVQHFVVMDEKAPEGYLAYEEALGEEADPVRvPE--RAACGMA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 245 YTSGTTGLPKAAIVVHSRYYRMAALVYYGFRMRPNDI-VYDC-LPLYHSAGNIVGIGQCLLHGMTVVIRKKFSASRFWDD 322
Cdd:cd05915 160 YTTGTTGLPKGVVYSHRALVLHSLAASLVDGTALSEKdVVLPvVPMFHVNAWCLPYAATLVGAKQVLPGPRLDPASLVEL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 323 CIKYNCTIVQYIGELCRYLLNQppREAENQH---QVRMALGNGLRQSIWTNFsSRFHIPQVAEFYGATECNcSLGNfdsq 399
Cdd:cd05915 240 FDGEGVTFTAGVPTVWLALADY--LESTGHRlktLRRLVVGGSAAPRSLIAR-FERMGVEVRQGYGLTETS-PVVV---- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 400 vgACGFNSRILSFVYPIRLVRVNEDTMELIRGPDGVCIPCQPGEPGQlvGRIIQKDPLRR---FDGYLNQGANNKKIAkd 476
Cdd:cd05915 312 --QNFVKSHLESLSEEEKLTLKAKTGLPIPLVRLRVADEEGRPVPKD--GKALGEVQLKGpwiTGGYYGNEEATRSAL-- 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 477 vFKKGdqAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLsrlldMADVAVYGVEVPG----TEGRAGMAA 552
Cdd:cd05915 386 -TPDG--FFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENAL-----MGHPKVKEAAVVAiphpKWQERPLAV 457
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 40807357 553 VASPTGNCDLERFAQVLEKEL-PLYARPIFLRLLPELHKTGTYKFQKTELRK 603
Cdd:cd05915 458 VVPRGEKPTPEELNEHLLKAGfAKWQLPDAYVFAEEIPRTSAGKFLKRALRE 509
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
79-261 |
2.49e-10 |
|
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341242 [Multi-domain] Cd Length: 481 Bit Score: 63.33 E-value: 2.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 79 LFASTVRRHPDKTALifEGTDTHWTFRQLDEYSSSVANFLQARGLASGDVAAIFMENrnefvGLWLGMAKLGVeaalint 158
Cdd:cd05918 4 LIEERARSQPDAPAV--CAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEK-----SKWAVVAMLAV------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 159 nLRrdallhclttsraralvfgsemASAICevhASLDPSLslfcsgswepgavPPstEHLDPLLKD--APKHLPSCPDkg 236
Cdd:cd05918 70 -LK----------------------AGGAF---VPLDPSH-------------PL--QRLQEILQDtgAKVVLTSSPS-- 106
|
170 180
....*....|....*....|....*
gi 40807357 237 ftDKLFYIYTSGTTGLPKAAIVVHS 261
Cdd:cd05918 107 --DAAYVIFTSGSTGKPKGVVIEHR 129
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
244-542 |
2.87e-10 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 63.79 E-value: 2.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 244 IYTSGTTGLPKAaiVVHSRYYRMA-----ALVyygFRMRPNDIVYDCLPLYHSAGNIVGIGQCLLHGMTVV--------- 309
Cdd:PRK08633 788 IFSSGSEGEPKG--VMLSHHNILSnieqiSDV---FNLRNDDVILSSLPFFHSFGLTVTLWLPLLEGIKVVyhpdptdal 862
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 310 -IRKKfsasrfwddCIKYNCTIVQYIGELCRYLLNQPPREAENQHQVRMALGNG--LRQSIWTNFSSRFHIPQVaEFYGA 386
Cdd:PRK08633 863 gIAKL---------VAKHRATILLGTPTFLRLYLRNKKLHPLMFASLRLVVAGAekLKPEVADAFEEKFGIRIL-EGYGA 932
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 387 TECN----CSLGN-----FDSQVGacgfnSRILSFVYPI--RLVR-VNEDTMElirgpdgvciPCQPGEPGQLVGRIIQk 454
Cdd:PRK08633 933 TETSpvasVNLPDvlaadFKRQTG-----SKEGSVGMPLpgVAVRiVDPETFE----------ELPPGEDGLILIGGPQ- 996
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 455 dplrRFDGYLNQGANNKKIAKDVFKKGdqAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLDMADV 534
Cdd:PRK08633 997 ----VMKGYLGDPEKTAEVIKDIDGIG--WYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAKALGGEEV 1070
|
....*...
gi 40807357 535 AVYGVEVP 542
Cdd:PRK08633 1071 VFAVTAVP 1078
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
245-545 |
4.74e-10 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 62.30 E-value: 4.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 245 YTSGTTGLPKAAIVVHSRYyrMAALVYYGFRMRPNDI----VYDCLPLYHSAGnIVGIGQCLLHGM-TVVIRKKFSASRF 319
Cdd:PLN02330 191 FSSGTTGISKGVMLTHRNL--VANLCSSLFSVGPEMIgqvvTLGLIPFFHIYG-ITGICCATLRNKgKVVVMSRFELRTF 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 320 WDDCIKYNCTIVQYIGELCRYLLNQPPREAENQHQVR----MALGNGLRQSIWTNFSSRFHIPQVAEFYGATECNC---S 392
Cdd:PLN02330 268 LNALITQEVSFAPIVPPIILNLVKNPIVEEFDLSKLKlqaiMTAAAPLAPELLTAFEAKFPGVQVQEAYGLTEHSCitlT 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 393 LGNFDSQVGACGFNSriLSFVYPIRLVR-VNEDTmelirgpdGVCIPcqPGEPGQLVGR---IIQkdplrrfdGYLNqga 468
Cdd:PLN02330 348 HGDPEKGHGIAKKNS--VGFILPNLEVKfIDPDT--------GRSLP--KNTPGELCVRsqcVMQ--------GYYN--- 404
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 40807357 469 NNKKIAKDVFKKGdqaYL-TGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLDMADVAVygVEVPGTE 545
Cdd:PLN02330 405 NKEETDRTIDEDG---WLhTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAV--VPLPDEE 477
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
79-601 |
2.12e-09 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.
Pssm-ID: 341280 [Multi-domain] Cd Length: 447 Bit Score: 60.02 E-value: 2.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 79 LFASTVRRHPDKTALIFEgtDTHWTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGveAAlint 158
Cdd:cd12115 4 LVEAQAARTPDAIALVCG--DESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAG--AA---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 159 nlrrdallhclttsraralvfgsemasaicevHASLDPslslfcsgswepgAVPPstEHLDPLLKDA-PKHLPSCPDkgf 237
Cdd:cd12115 76 --------------------------------YVPLDP-------------AYPP--ERLRFILEDAqARLVLTDPD--- 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 238 tDKLFYIYTSGTTGLPKAAIVVHSR---YYRMAALVYYGFRMR----PNDIVYDcLPLYHSAGNivgigqcLLHGMTVVI 310
Cdd:cd12115 106 -DLAYVIYTSGSTGRPKGVAIEHRNaaaFLQWAAAAFSAEELAgvlaSTSICFD-LSVFELFGP-------LATGGKVVL 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 311 RKkfSASRFWDDCIKYNCTIVQYIGELCRYLLNQ---PPreaenqhQVRM------ALGNGLRQSIWtnfsSRFHIPQVA 381
Cdd:cd12115 177 AD--NVLALPDLPAAAEVTLINTVPSAAAELLRHdalPA-------SVRVvnlagePLPRDLVQRLY----ARLQVERVV 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 382 EFYGATECN-----CSLGNFDSQVGACGFNsrilsfVYPIRlVRVNEDTMElirgpdgvciPCQPGEPGQLvgrIIQKDP 456
Cdd:cd12115 244 NLYGPSEDTtystvAPVPPGASGEVSIGRP------LANTQ-AYVLDRALQ----------PVPLGVPGEL---YIGGAG 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 457 LRRfdGYLNQ-GANNKKIAKDVFKKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLDMADVA 535
Cdd:cd12115 304 VAR--GYLGRpGLTAERFLPDPFGPGARLYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAV 381
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 40807357 536 VYGVEVPGTEGRAGMAAVASPTGNCDLERFAQVLEKELPLYARPIFLRLLPELHKTGTYKFQKTEL 601
Cdd:cd12115 382 VVAIGDAAGERRLVAYIVAEPGAAGLVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
74-586 |
2.22e-09 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 61.13 E-value: 2.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 74 RTVPILFASTVRRHPDKTALIFegTDTHWTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGVEA 153
Cdd:PRK12316 3057 RGVHRLFEEQVERTPDAVALAF--GEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAY 3134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 154 ALINTNLRRDALLHCLTTSRARALVFGSemasaicevHASLdpslslfcsgswePGAVPPSTEHLDPLLKDAPKHLPscP 233
Cdd:PRK12316 3135 VPLDPEYPEERLAYMLEDSGAQLLLSQS---------HLRL-------------PLAQGVQVLDLDRGDENYAEANP--A 3190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 234 DKGFTDKLFY-IYTSGTTGLPKAAIVVHSRYYRMAALVYYGFRMRPNDIVydclpLYHSAGNIVGIGQCLLHGMTVVIRK 312
Cdd:PRK12316 3191 IRTMPENLAYvIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRV-----LQFTTFSFDVFVEELFWPLMSGARV 3265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 313 KFSASRFWDDCIKYNCTIVQ--------YIGELCRYLLNQPPREAENQHQVRM---ALGNGLRQSIwtnfssrFHIPQVA 381
Cdd:PRK12316 3266 VLAGPEDWRDPALLVELINSegvdvlhaYPSMLQAFLEEEDAHRCTSLKRIVCggeALPADLQQQV-------FAGLPLY 3338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 382 EFYGATECNCSLGNFDSQVGACGFnsrilsfvYPIRLVRVNEDTMELirgpDGVCIPCQPGEPGQLvgrIIQKDPLRRfd 461
Cdd:PRK12316 3339 NLYGPTEATITVTHWQCVEEGKDA--------VPIGRPIANRACYIL----DGSLEPVPVGALGEL---YLGGEGLAR-- 3401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 462 GYLNQ-GANNKKIAKDVFKKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEgtlSRLLDMAdvAVYGVE 540
Cdd:PRK12316 3402 GYHNRpGLTAERFVPDPFVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIE---ARLLEHP--WVREAV 3476
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 40807357 541 VPGTEGRAGMAAVASPTGNCDLER-FAQVLEKELPLYARP---IFLRLLP 586
Cdd:PRK12316 3477 VLAVDGRQLVAYVVPEDEAGDLREaLKAHLKASLPEYMVPahlLFLERMP 3526
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
88-601 |
3.69e-09 |
|
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: 59.40 E-value: 3.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 88 PDKTALIFEgtDTHWTFRQLDEYSSSVANFLQARGLASGDVAAIfmenrnefvglwlgMAKLGVEAALintnlrrdALLH 167
Cdd:cd17650 1 PDAIAVSDA--TRQLTYRELNERANQLARTLRGLGVAPGSVVGV--------------CADRSLDAIV--------GLLA 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 168 CLTTSRAralvfgsemasaicevHASLDPSLSLfcsgswepgavppstEHLDPLLKDA-PKHLPSCPDkgftDKLFYIYT 246
Cdd:cd17650 57 VLKAGGA----------------YVPIDPDYPA---------------ERLQYMLEDSgAKLLLTQPE----DLAYVIYT 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 247 SGTTGLPKAAIVVHSRYYRMaalvYYGFRMRpndivY--DCLPLYH----------SAGNIVgigQCLLHGMTVVI---R 311
Cdd:cd17650 102 SGTTGKPKGVMVEHRNVAHA----AHAWRRE-----YelDSFPVRLlqmasfsfdvFAGDFA---RSLLNGGTLVIcpdE 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 312 KKFSASRFWDDCIKYNCTIVQYIGELCRYLLNQPPREAENQHQVR-MALGNGLRQSIW-TNFSSRF-HIPQVAEFYGATE 388
Cdd:cd17650 170 VKLDPAALYDLILKSRITLMESTPALIRPVMAYVYRNGLDLSAMRlLIVGSDGCKAQDfKTLAARFgQGMRIINSYGVTE 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 389 CNCSLGNFD-SQVGACGfnSRILSFVYPIRLVR--VNEDTMELIrgPDGVCIPCQPGEPGqlVGRiiqkdplrrfdGYLN 465
Cdd:cd17650 250 ATIDSTYYEeGRDPLGD--SANVPIGRPLPNTAmyVLDERLQPQ--PVGVAGELYIGGAG--VAR-----------GYLN 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 466 QGANNK-KIAKDVFKKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLDMADVAVYGVEVPGt 544
Cdd:cd17650 313 RPELTAeRFVENPFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVREDKG- 391
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 40807357 545 eGRAGMAAVASPTGNCDLERFAQVLEKELPLYARPIFLRLLPELHKTGTYKFQKTEL 601
Cdd:cd17650 392 -GEARLCAYVVAAATLNTAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
102-525 |
1.81e-08 |
|
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: 57.48 E-value: 1.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 102 WTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFV----GLWLGmaklGVEAALINTNLRRDALLHCLTTSRARAL 177
Cdd:cd05932 7 FTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFitdlAIWMA----GHISVPLYPTLNPDTIRYVLEHSESKAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 178 VFG-----SEMASAICE--VHASLDPSLSLFCSGSWEpgavppSTEHLDPLLKDAPKHLPscpdkgftDKLF-YIYTSGT 249
Cdd:cd05932 83 FVGklddwKAMAPGVPEglISISLPPPSAANCQYQWD------DLIAQHPPLEERPTRFP--------EQLAtLIYTSGT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 250 TGLPKAAIVVHSRYYRMAALVYYGFRMRPNDIVYDCLPLYHSAGNIVGIGQCLLHGMTV------------VIRKK---- 313
Cdd:cd05932 149 TGQPKGVMLTFGSFAWAAQAGIEHIGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVafaesldtfvedVQRARptlf 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 314 FSASRFWddcIKYNCTIVQYIG--ELCRyLLNQPPREAENQHQVRMALG-NGLRQSIwtnfSSRFHIP------------ 378
Cdd:cd05932 229 FSVPRLW---TKFQQGVQDKIPqqKLNL-LLKIPVVNSLVKRKVLKGLGlDQCRLAG----CGSAPVPpallewyrslgl 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 379 QVAEFYGATEcNCSLGN----FDSQVGACGFNsrilsfvYPIRLVRVNEDTMELIRgpdgvcipcqpgEPGQLVGRiiqk 454
Cdd:cd05932 301 NILEAYGMTE-NFAYSHlnypGRDKIGTVGNA-------GPGVEVRISEDGEILVR------------SPALMMGY---- 356
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 40807357 455 dplrrfdgYLNQGANNKKIAKDVFKKgdqaylTGDVLVMDELGYLYFRDRTGDTFRW-KGENVSTTEVEGTL 525
Cdd:cd05932 357 --------YKDPEATAEAFTADGFLR------TGDKGELDADGNLTITGRVKDIFKTsKGKYVAPAPIENKL 414
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
70-604 |
1.95e-08 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 57.47 E-value: 1.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 70 LQERRTVPILFASTVRRHPDKTAliFEGTDTHWTFRQLDEYSSSVANFLQAR-GLASGDVAAIFMENRNEFVGLWLGMAK 148
Cdd:PRK05677 20 PDEYPNIQAVLKQSCQRFADKPA--FSNLGKTLTYGELYKLSGAFAAWLQQHtDLKPGDRIAVQLPNVLQYPVAVFGAMR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 149 LGVeaALINTNLRRDA--LLHCLTTSRARALVFGSEMASAICEVHASLDPSLSLFCsgswEPGAVPPSTEHLdpLLKDAP 226
Cdd:PRK05677 98 AGL--IVVNTNPLYTAreMEHQFNDSGAKALVCLANMAHLAEKVLPKTGVKHVIVT----EVADMLPPLKRL--LINAVV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 227 KHLP------SCPDK-GFTDKL-------------------FYIYTSGTTGLPKAAIVVHSRYYR--------MAALVYY 272
Cdd:PRK05677 170 KHVKkmvpayHLPQAvKFNDALakgagqpvteanpqaddvaVLQYTGGTTGVAKGAMLTHRNLVAnmlqcralMGSNLNE 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 273 GfrmrpNDIVYDCLPLYH--------SAGNIVGIGQCL------LHGMTVVIRK-KFSAsrFwddcIKYNCTIVQyigeL 337
Cdd:PRK05677 250 G-----CEILIAPLPLYHiyaftfhcMAMMLIGNHNILisnprdLPAMVKELGKwKFSG--F----VGLNTLFVA----L 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 338 CRyllNQPPREAE-NQHQVRMALGNGLRQSI---WTNFSSrfhiPQVAEFYGATECN--CSLGNFDS-QVGACGFnsril 410
Cdd:PRK05677 315 CN---NEAFRKLDfSALKLTLSGGMALQLATaerWKEVTG----CAICEGYGMTETSpvVSVNPSQAiQVGTIGI----- 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 411 sfvyPIrlvrvnEDTMELIRGPDGVCIPCqpGEPGQLVgriiQKDPlRRFDGYL-NQGANNKKIAKDVFKKgdqaylTGD 489
Cdd:PRK05677 383 ----PV------PSTLCKVIDDDGNELPL--GEVGELC----VKGP-QVMKGYWqRPEATDEILDSDGWLK------TGD 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 490 VLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLDMADVAVYGVEVPGTEGRAGMAAVASPTGNCDLERFAQVL 569
Cdd:PRK05677 440 IALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIKVFVVVKPGETLTKEQVMEHM 519
|
570 580 590
....*....|....*....|....*....|....*
gi 40807357 570 EKELPLYARPIFLRLLPELHKTGTYKFQKTELRKE 604
Cdd:PRK05677 520 RANLTGYKVPKAVEFRDELPTTNVGKILRRELRDE 554
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
75-290 |
2.42e-08 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 57.05 E-value: 2.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 75 TVPILFASTVRRHPDKTALifeGT-----------------------DTHW-TFRQLDEYSSSVANFLQARGLASGDVAA 130
Cdd:PLN02387 59 TLAALFEQSCKKYSDKRLL---GTrklisrefetssdgrkfeklhlgEYEWiTYGQVFERVCNFASGLVALGHNKEERVA 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 131 IFMENRNEfvglWL----GMAKLGVEAALINTNLRRDALLHCLTTSRARALVFGS-------EMAS-------AICEVHA 192
Cdd:PLN02387 136 IFADTRAE----WLialqGCFRQNITVVTIYASLGEEALCHSLNETEVTTVICDSkqlkkliDISSqletvkrVIYMDDE 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 193 SLDPSLSLFCSGSWepgaVPPSTEHLDPLLKDAPKHlPSCPDKgfTDKLFYIYTSGTTGLPKAAIVVHSRYYRMAALVYY 272
Cdd:PLN02387 212 GVDSDSSLSGSSNW----TVSSFSEVEKLGKENPVD-PDLPSP--NDIAVIMYTSGSTGLPKGVMMTHGNIVATVAGVMT 284
|
250
....*....|....*....
gi 40807357 273 GF-RMRPNDIVYDCLPLYH 290
Cdd:PLN02387 285 VVpKLGKNDVYLAYLPLAH 303
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
77-602 |
2.75e-08 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 56.78 E-value: 2.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 77 PILF---ASTVrrHPDKTALIFEgtDTHWTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGVEA 153
Cdd:PLN02479 22 PLWFlerAAVV--HPTRKSVVHG--SVRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 154 ALINTNLRRDALLHCLTTSRARALVFGSEMASAICE--------VHASLDPSLsLFCSGswEPGAVPPSTEH-------- 217
Cdd:PLN02479 98 NCVNIRLNAPTIAFLLEHSKSEVVMVDQEFFTLAEEalkilaekKKSSFKPPL-LIVIG--DPTCDPKSLQYalgkgaie 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 218 LDPLLKDAPKHLPSCPDKGFTDKLFYIYTSGTTGLPKAAIVVHSRYYRMAALVYYGFRMRPNDIVYDCLPLYHSAGNIVG 297
Cdd:PLN02479 175 YEKFLETGDPEFAWKPPADEWQSIALGYTSGTTASPKGVVLHHRGAYLMALSNALIWGMNEGAVYLWTLPMFHCNGWCFT 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 298 IGQCLLHGMTVVIRKkFSASRFWDDCIKYNCTIVQYIGELCRYLLNQPPREA--ENQHQVR-MALGNGLRQSIWTNFSSR 374
Cdd:PLN02479 255 WTLAALCGTNICLRQ-VTAKAIYSAIANYGVTHFCAAPVVLNTIVNAPKSETilPLPRVVHvMTAGAAPPPSVLFAMSEK 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 375 ----FHIPQVAEFYGATECNCSLGNFDSQ--VGACGFNSRilsfvypiRLVR-VNEDTMELIRGPDGVCIPCQPGEPGQL 447
Cdd:PLN02479 334 gfrvTHTYGLSETYGPSTVCAWKPEWDSLppEEQARLNAR--------QGVRyIGLEGLDVVDTKTMKPVPADGKTMGEI 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 448 V--GRIIQKdplrrfdGYLNqganNKKIAKDVFKKGdqAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTL 525
Cdd:PLN02479 406 VmrGNMVMK-------GYLK----NPKANEEAFANG--WFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVV 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 526 SR---LLDMADVA-----------VYGVEVPGTEgRAGMAAVASptgncDLERFAQvleKELPLYARPIFLRLLPeLHKT 591
Cdd:PLN02479 473 YThpaVLEASVVArpderwgespcAFVTLKPGVD-KSDEAALAE-----DIMKFCR---ERLPAYWVPKSVVFGP-LPKT 542
|
570
....*....|.
gi 40807357 592 GTYKFQKTELR 602
Cdd:PLN02479 543 ATGKIQKHVLR 553
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
88-595 |
3.01e-08 |
|
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: 56.53 E-value: 3.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 88 PDKTALIFEgtDTHWTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALLH 167
Cdd:cd12116 1 PDATAVRDD--DRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 168 CLTTSRARALVFGSEMAsaicevhasldpslslfcsgswEPGAVPPSTEHLDPLLKDAPKHLPSCPDKGftDKLFY-IYT 246
Cdd:cd12116 79 ILEDAEPALVLTDDALP----------------------DRLPAGLPVLLLALAAAAAAPAAPRTPVSP--DDLAYvIYT 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 247 SGTTGLPKAAIVVH----------------SRYYRMAALVYYGFrmrpnDIvyDCLPLYHSagnivgigqcLLHGMTVVI 310
Cdd:cd12116 135 SGSTGRPKGVVVSHrnlvnflhsmrerlglGPGDRLLAVTTYAF-----DI--SLLELLLP----------LLAGARVVI 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 311 RKK---FSASRFWDDCIKYNCTIVQYIGELCRYLLNQPPREAENQHqvrmAL--GNGLRQSIWTNFSSRfhIPQVAEFYG 385
Cdd:cd12116 198 APRetqRDPEALARLIEAHSITVMQATPATWRMLLDAGWQGRAGLT----ALcgGEALPPDLAARLLSR--VGSLWNLYG 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 386 ATEcncslgnfdSQVGACGfnSRILSFVYPIRLVRVNEDTMELIRGPDGVCIPcqPGEPGQLvgrIIQKDPLRRfdGYLN 465
Cdd:cd12116 272 PTE---------TTIWSTA--ARVTAAAGPIPIGRPLANTQVYVLDAALRPVP--PGVPGEL---YIGGDGVAQ--GYLG 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 466 QGA-NNKKIAKDVFKK-GDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLDMADVAVYGVEVPG 543
Cdd:cd12116 334 RPAlTAERFVPDPFAGpGSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGG 413
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 40807357 544 TEGRAGMAAVASPTGnCDLERFAQVLEKELPLYARPIFLRLLPELHKTGTYK 595
Cdd:cd12116 414 DRRLVAYVVLKAGAA-PDAAALRAHLRATLPAYMVPSAFVRLDALPLTANGK 464
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
68-280 |
5.08e-08 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 56.72 E-value: 5.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 68 QCLQErrtvpiLFASTVRRHPDKTALIFEGTdtHWTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMA 147
Cdd:PRK05691 2188 QTLHG------LFAAQAARTPQAPALTFAGQ--TLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAIL 2259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 148 KLGVEAALINTNLRRDALLHCLTTSRARALVFGSEMASAICEVHASL------DPSLSLfcsgSWEPGAVPPSTehldpl 221
Cdd:PRK05691 2260 KAGGAYVPLDPEYPLERLHYMIEDSGIGLLLSDRALFEALGELPAGVarwcleDDAAAL----AAYSDAPLPFL------ 2329
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 40807357 222 lkDAPKHLPscpdkgftdklFYIYTSGTTGLPKAAIVVHSRYYRMAALVYYGFRMRPND 280
Cdd:PRK05691 2330 --SLPQHQA-----------YLIYTSGSTGKPKGVVVSHGEIAMHCQAVIERFGMRADD 2375
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
86-330 |
5.93e-08 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 55.92 E-value: 5.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 86 RH----PDKTALIFEG----TDTHWTFRQLDEYSSSVANFLQARGLASGDVAAIFMenrnefvglwlGMAklgVEAALin 157
Cdd:PRK00174 75 RHlktrGDKVAIIWEGddpgDSRKITYRELHREVCRFANALKSLGVKKGDRVAIYM-----------PMI---PEAAV-- 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 158 tnlrrdALLHClttsrAR-----ALVFGSEMASAICE----VHASLdpslsLFCS-GSWEPGAV-------------PPS 214
Cdd:PRK00174 139 ------AMLAC-----ARigavhSVVFGGFSAEALADriidAGAKL-----VITAdEGVRGGKPiplkanvdealanCPS 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 215 TEH--------------------LDPLLKDAPKHlpsCPDKGFT--DKLFYIYTSGTTGLPKAaiVVHSR--YyrmaaLV 270
Cdd:PRK00174 203 VEKvivvrrtggdvdwvegrdlwWHELVAGASDE---CEPEPMDaeDPLFILYTSGSTGKPKG--VLHTTggY-----LV 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 271 Y------YGFRMRPNDiVYDClplyhSA--GNIVG-----IGQcLLHGMTVVIrkkF-------SASRFWDDCIKYNCTI 330
Cdd:PRK00174 273 YaamtmkYVFDYKDGD-VYWC-----TAdvGWVTGhsyivYGP-LANGATTLM---FegvpnypDPGRFWEVIDKHKVTI 342
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
74-309 |
7.73e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 55.33 E-value: 7.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 74 RTVPILFASTVRRHPDKTALIFEGTDTHW-------TFRQLDEYSSSVANFLQARGlASGDVAAIFMENRNEFVGLWLGm 146
Cdd:PRK05850 1 SSVPSLLRERASLQPDDAAFTFIDYEQDPagvaetlTWSQLYRRTLNVAEELRRHG-STGDRAVILAPQGLEYIVAFLG- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 147 aklGVEAALINTNL----------RRDALLH------CLTTSraralvfgsemaSAICEVHASLDPSlslfcsgswePGA 210
Cdd:PRK05850 79 ---ALQAGLIAVPLsvpqggahdeRVSAVLRdtspsvVLTTS------------AVVDDVTEYVAPQ----------PGQ 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 211 VPPSTEHLDPLLKDAPKHLPSCPDkGFTDKLFYIYTSGTTGLPKAAIVVH-----------SRYYRmaalvYYGFRMRPN 279
Cdd:PRK05850 134 SAPPVIEVDLLDLDSPRGSDARPR-DLPSTAYLQYTSGSTRTPAGVMVSHrnvianfeqlmSDYFG-----DTGGVPPPD 207
|
250 260 270
....*....|....*....|....*....|
gi 40807357 280 DIVYDCLPLYHSAGNIVGIGQCLLHGMTVV 309
Cdd:PRK05850 208 TTVVSWLPFYHDMGLVLGVCAPILGGCPAV 237
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
80-261 |
8.12e-08 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 55.57 E-value: 8.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 80 FASTVRRH--PDKTALIFEGTDTH---WTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLG---- 150
Cdd:PRK03584 88 YAENLLRHrrDDRPAIIFRGEDGPrreLSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLATASLGaiws 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 151 -------VEAALintnlrrdallhclttSR-----ARALV------FGS---EMASAICEVHASLdPSLSLFCS----GS 205
Cdd:PRK03584 168 scspdfgVQGVL----------------DRfgqiePKVLIavdgyrYGGkafDRRAKVAELRAAL-PSLEHVVVvpylGP 230
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 40807357 206 WEPGAVPPSTEHLDPLLKDAPKHLPSCPDKGFTDKLFYIYTSGTTGLPKAaiVVHS 261
Cdd:PRK03584 231 AAAAAALPGALLWEDFLAPAEAAELEFEPVPFDHPLWILYSSGTTGLPKC--IVHG 284
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
85-601 |
2.07e-07 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 53.86 E-value: 2.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 85 RRHPDKTALIFEGTDTHWTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGVEAALINTNLRRDA 164
Cdd:PRK05857 25 RQQPEAIALRRCDGTSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLPIAA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 165 LLHCLTTSRARALVFGSEmasaiCEVHASLDPSLsLFCSGSWEPGAVPPSTEHLDPLLKDAPKhlpSCPDKGFTDKLFYI 244
Cdd:PRK05857 105 IERFCQITDPAAALVAPG-----SKMASSAVPEA-LHSIPVIAVDIAAVTRESEHSLDAASLA---GNADQGSEDPLAMI 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 245 YTSGTTGLPKAAIVVHSRYY------RMAALVYYGFRMrpNDIVYDCLPLYHsAGNIVGIGQCLLHGMTVVIRKKFSASR 318
Cdd:PRK05857 176 FTSGTTGEPKAVLLANRTFFavpdilQKEGLNWVTWVV--GETTYSPLPATH-IGGLWWILTCLMHGGLCVTGGENTTSL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 319 ---FWDDCIKYNCTIVQYIGELCRYL----LNQPPreaenqhqVRMaLGNGLRQSIWTNFssRFhIP----QVAEFYGAT 387
Cdd:PRK05857 253 leiLTTNAVATTCLVPTLLSKLVSELksanATVPS--------LRL-VGYGGSRAIAADV--RF-IEatgvRTAQVYGLS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 388 ECNCSLGNFDSQVGACgfnSRI----LSFVYPirlvrvnedTMELIRGPDGVCIPCQP-GEPGQLVGRIIQKDPLRRFdG 462
Cdd:PRK05857 321 ETGCTALCLPTDDGSI---VKIeagaVGRPYP---------GVDVYLAATDGIGPTAPgAGPSASFGTLWIKSPANML-G 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 463 YLNQGANNKKIAKDVFKKgdqaylTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLDMADVAVYgvEVP 542
Cdd:PRK05857 388 YWNNPERTAEVLIDGWVN------TGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACY--EIP 459
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 40807357 543 GTEGRA--GMAAVASP----TGNCDLE-RFAQVLEKELPLYARPIFLRLLPELHKTGTYKFQKTEL 601
Cdd:PRK05857 460 DEEFGAlvGLAVVASAeldeSAARALKhTIAARFRRESEPMARPSTIVIVTDIPRTQSGKVMRASL 525
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
520-595 |
2.31e-07 |
|
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: 48.31 E-value: 2.31e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 40807357 520 EVEGTLSRLLDMADVAVYGVEVPgTEGRAGMAAVASPTGNCDLER-FAQVLEKELPLYARPIFLRLLPELHKTGTYK 595
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDE-LKGEAPVAFVVLKPGVELLEEeLVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
241-522 |
4.93e-07 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 52.82 E-value: 4.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 241 LFYIYTSGTTGLPKAaiVVHSRYYRMAALVYYGFRMRPNDIVYdclpLYHSAGNIVGIG------QCLLHGMTVV----- 309
Cdd:PTZ00237 257 LYILYTSGTTGNSKA--VVRSNGPHLVGLKYYWRSIIEKDIPT----VVFSHSSIGWVSfhgflyGSLSLGNTFVmfegg 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 310 -IRKKFSASRFWDDCIKYNCTIVQYIGELCRYLLNQPPrEAENQHQvRMALGNglRQSIWtnFSSRFHIPQVAEF----- 383
Cdd:PTZ00237 331 iIKNKHIEDDLWNTIEKHKVTHTLTLPKTIRYLIKTDP-EATIIRS-KYDLSN--LKEIW--CGGEVIEESIPEYienkl 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 384 -------YGATECNCSL----GNFDSQVGACGFNSrilSFVYPIRLvrvNEDTMELirgpdgvcipcqpgePGQLVGRII 452
Cdd:PTZ00237 405 kikssrgYGQTEIGITYlycyGHINIPYNATGVPS---IFIKPSIL---SEDGKEL---------------NVNEIGEVA 463
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 453 QKDPLRrfDGYLNQGANNKKIAKDVFKKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVE 522
Cdd:PTZ00237 464 FKLPMP--PSFATTFYKNDEKFKQLFSKFPGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIE 531
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
74-296 |
8.51e-07 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 51.90 E-value: 8.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 74 RTVPILFASTVRRHPDKTaLIFE---GTDTHWTFRQLDEYSSSVANFLQARGLASGDVAaIFMENRNE--FVGLW---LG 145
Cdd:cd05906 10 RTLLELLLRAAERGPTKG-ITYIdadGSEEFQSYQDLLEDARRLAAGLRQLGLRPGDSV-ILQFDDNEdfIPAFWacvLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 146 ---MAKLGVEAALINTNLRRDALLHCLTTSRARALVFGSEMASAICEVHASLdpslslfcsgSWEPGAVPPSTEHLDPll 222
Cdd:cd05906 88 gfvPAPLTVPPTYDEPNARLRKLRHIWQLLGSPVVLTDAELVAEFAGLETLS----------GLPGIRVLSIEELLDT-- 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 40807357 223 kDAPKHLPSC-PDkgftDKLFYIYTSGTTGLPKAAIVVHSRYYRMAALVYYGFRMRPNDIVYDCLPLYHsAGNIV 296
Cdd:cd05906 156 -AADHDLPQSrPD----DLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVPLDH-VGGLV 224
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
86-261 |
9.48e-07 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 51.80 E-value: 9.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 86 RHPDKTALIFEGTDthWTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGVEAALINTnlrrdAL 165
Cdd:PRK09029 15 VRPQAIALRLNDEV--LTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNP-----QL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 166 LHCLTtsraralvfgsemasaicevhASLDPSLSLFCSGSWEPGAVPPSTEHLDPLLKDAPKHLPSCPDKGFTdklfYIY 245
Cdd:PRK09029 88 PQPLL---------------------EELLPSLTLDFALVLEGENTFSALTSLHLQLVEGAHAVAWQPQRLAT----MTL 142
|
170
....*....|....*.
gi 40807357 246 TSGTTGLPKAaiVVHS 261
Cdd:PRK09029 143 TSGSTGLPKA--AVHT 156
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
72-261 |
1.52e-06 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 51.88 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 72 ERRTVPILFASTVRRHPDKTALIFegTDTHWTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGV 151
Cdd:PRK12316 509 LQRGVHRLFEEQVERTPEAPALAF--GEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGG 586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 152 EAALINTNLRRDALLHCLTTSRARALVFGSEMASAIcEVHASLDpSLSLFCSGSWEPG--AVPPSTeHLDPllkdapkhl 229
Cdd:PRK12316 587 AYVPLDPEYPAERLAYMLEDSGVQLLLSQSHLGRKL-PLAAGVQ-VLDLDRPAAWLEGysEENPGT-ELNP--------- 654
|
170 180 190
....*....|....*....|....*....|...
gi 40807357 230 pscpdkgftDKLFY-IYTSGTTGLPKAAIVVHS 261
Cdd:PRK12316 655 ---------ENLAYvIYTSGSTGKPKGAGNRHR 678
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
99-308 |
6.12e-06 |
|
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: 49.14 E-value: 6.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 99 DTHW-TFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALLHCLTTSRARAL 177
Cdd:cd17639 2 EYKYmSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECSAI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 178 vfgsemasaicevhasldpslslFCSGSwepgavppstehldpllkdapkhlpscPDkgftDKLFYIYTSGTTGLPKAai 257
Cdd:cd17639 82 -----------------------FTDGK---------------------------PD----DLACIMYTSGSTGNPKG-- 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 40807357 258 VVHSRYYRMAALVYYGFR----MRPNDIVYDCLPLYH----SAGNIvgigqCLLHGMTV 308
Cdd:cd17639 106 VMLTHGNLVAGIAGLGDRvpelLGPDDRYLAYLPLAHifelAAENV-----CLYRGGTI 159
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
83-281 |
6.33e-06 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 49.22 E-value: 6.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 83 TVRRHPDKTALIfEGtDTHWTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGVeaALINT--NL 160
Cdd:PRK10946 32 TRHAASDAIAVI-CG-ERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLGV--APVNAlfSH 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 161 RRDALL--------HCLTTSRARALVFGSEMASAICEVHASLDPSLSLFCSGswepgavppsTEHLDPLLKDAPKHLPSC 232
Cdd:PRK10946 108 QRSELNayasqiepALLIADRQHALFSDDDFLNTLVAEHSSLRVVLLLNDDG----------EHSLDDAINHPAEDFTAT 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 40807357 233 PDKgfTDKL-FYIYTSGTTGLPKAAIVVHSRYyrmaalvYYGFRmRPNDI 281
Cdd:PRK10946 178 PSP--ADEVaFFQLSGGSTGTPKLIPRTHNDY-------YYSVR-RSVEI 217
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
73-272 |
8.80e-06 |
|
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.
Pssm-ID: 274582 [Multi-domain] Cd Length: 1389 Bit Score: 49.29 E-value: 8.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 73 RRTVPILFASTVRRHPDKTALI----FEGTDTH---WTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLG 145
Cdd:TIGR03443 235 RGAIHDIFADNAEKHPDRTCVVetpsFLDPSSKtrsFTYKQINEASNILAHYLLKTGIKRGDVVMIYAYRGVDLVVAVMG 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 146 MAKLGVEAALINTNLRRDALLHCLTTSRARALVfGSEMASAICE-----VHASLD-----PSLSLFCSGSWEPGAVP-PS 214
Cdd:TIGR03443 315 VLKAGATFSVIDPAYPPARQTIYLSVAKPRALI-VIEKAGTLDQlvrdyIDKELElrteiPALALQDDGSLVGGSLEgGE 393
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 215 TEHLDPL--LKDAPKHLPSCPDKGFTdklfYIYTSGTTGLPKAaivVHSRYYrmaALVYY 272
Cdd:TIGR03443 394 TDVLAPYqaLKDTPTGVVVGPDSNPT----LSFTSGSEGIPKG---VLGRHF---SLAYY 443
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
88-282 |
9.15e-06 |
|
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).
Pssm-ID: 341307 [Multi-domain] Cd Length: 436 Bit Score: 48.40 E-value: 9.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 88 PDKTALIFEgtDTHWTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGveAALIntnlrrdallh 167
Cdd:cd17652 1 PDAPAVVFG--DETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAG--AAYL----------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 168 clttsraralvfgsemasaicevhaSLDPSLslfcsgswepgavPPstEHLDPLLKDA-PKHLPSCPDkgftDKLFYIYT 246
Cdd:cd17652 66 -------------------------PLDPAY-------------PA--ERIAYMLADArPALLLTTPD----NLAYVIYT 101
|
170 180 190
....*....|....*....|....*....|....*.
gi 40807357 247 SGTTGLPKAAIVVHSRYYRMAALVYYGFRMRPNDIV 282
Cdd:cd17652 102 SGSTGRPKGVVVTHRGLANLAAAQIAAFDVGPGSRV 137
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
102-358 |
1.07e-05 |
|
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341296 [Multi-domain] Cd Length: 569 Bit Score: 48.57 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 102 WTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGVeaalINTNLRRDAL----LHCLTTSRARAL 177
Cdd:cd17641 12 FTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGA----LSLGIYQDSMaeevAYLLNYTGARVV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 178 VFG-SEMASAICEvHASLDPSLSLFCSgsWEPGAVppsTEHLDPLLKDAPK-------HLPSCPDKG--------FTDKL 241
Cdd:cd17641 88 IAEdEEQVDKLLE-IADRIPSVRYVIY--CDPRGM---RKYDDPRLISFEDvvalgraLDRRDPGLYerevaagkGEDVA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 242 FYIYTSGTTGLPKAAIVVHSRYYRM-AALVYYGFRmRPNDIVYDCLPLYHSAGNIVGIGQCLLHGMTVvirkkfsasrfw 320
Cdd:cd17641 162 VLCTTSGTTGKPKLAMLSHGNFLGHcAAYLAADPL-GPGDEYVSVLPLPWIGEQMYSVGQALVCGFIV------------ 228
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 40807357 321 dDCIKYNCTIVQYIGELCRYLLNQPPREAENQH---QVRMA 358
Cdd:cd17641 229 -NFPEEPETMMEDLREIGPTFVLLPPRVWEGIAadvRARMM 268
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
100-292 |
1.16e-05 |
|
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341295 [Multi-domain] Cd Length: 468 Bit Score: 48.12 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 100 THWTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALLHCLTTSRARALVf 179
Cdd:cd17640 4 KRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALV- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 180 gsemasaicevhasldpslslfcsgswepgavppstehldplLKDAPKHLPSCpdkgftdklfyIYTSGTTGLPKAAIVV 259
Cdd:cd17640 83 ------------------------------------------VENDSDDLATI-----------IYTSGTTGNPKGVMLT 109
|
170 180 190
....*....|....*....|....*....|....
gi 40807357 260 H-SRYYRMAALvYYGFRMRPNDIVYDCLPLYHSA 292
Cdd:cd17640 110 HaNLLHQIRSL-SDIVPPQPGDRFLSILPIWHSY 142
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
206-605 |
1.25e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 48.06 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 206 WEPGAVPpsteHLDPLLKDAPKHLPSCPDKGFTdkLFYIYTSGTTGLPKAaiVVHSRYYRMAAL--VYYGFRMRPNDIVY 283
Cdd:PRK07787 102 DDPAGLP----HVPVRLHARSWHRYPEPDPDAP--ALIVYTSGTTGPPKG--VVLSRRAIAADLdaLAEAWQWTADDVLV 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 284 DCLPLYHSAGNIVGIGQCLLHGMTVVIRKKFSASRFWDDCiKYNCTIvqYIGELCRYLlnqppREAENQHQVRmALGnGL 363
Cdd:PRK07787 174 HGLPLFHVHGLVLGVLGPLRIGNRFVHTGRPTPEAYAQAL-SEGGTL--YFGVPTVWS-----RIAADPEAAR-ALR-GA 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 364 RqsIWTNFSSRFHIP-----------QVAEFYGATEC--NCS-LGNFDSQVGACGFnsrilsfvyPIRLVRVNedtmelI 429
Cdd:PRK07787 244 R--LLVSGSAALPVPvfdrlaaltghRPVERYGMTETliTLStRADGERRPGWVGL---------PLAGVETR------L 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 430 RGPDGVCIPCQpgepGQLVGRIIQKDPLrRFDGYLnqgaNNKKIAKDVFkKGDQAYLTGDVLVMDELGYLYF--RDRTgD 507
Cdd:PRK07787 307 VDEDGGPVPHD----GETVGELQVRGPT-LFDGYL----NRPDATAAAF-TADGWFRTGDVAVVDPDGMHRIvgREST-D 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 508 TFRWKGENVSTTEVEGTLSRLLDMADVAVYGVEVPGTEGRagMAAVASPTGNCDLERFAQVLEKELPLYARPIFLRLLPE 587
Cdd:PRK07787 376 LIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQR--IVAYVVGADDVAADELIDFVAQQLSVHKRPREVRFVDA 453
|
410
....*....|....*...
gi 40807357 588 LHKTGTYKFQKTELRKEG 605
Cdd:PRK07787 454 LPRNAMGKVLKKQLLSEG 471
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
473-604 |
1.89e-05 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 47.82 E-value: 1.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 473 IAKDVFKKGDQA------YLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLDMADVAVYGVEVPGTEG 546
Cdd:PRK06018 394 VAAAYYRVDGEIldddgfFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDE 473
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 40807357 547 RAGMAAVASPTGNCDLERFAQVLEKELPLYARPIFLRLLPELHKTGTYKFQKTELRKE 604
Cdd:PRK06018 474 RPLLIVQLKPGETATREEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALREQ 531
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
413-608 |
3.17e-05 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 46.87 E-value: 3.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 413 VYPIRLVRVNEDTMElirgpdgvciPCQPGEPGQLVgriiqkdplrrFDGYLNQGA------NNKKIAKDVFKK-GDQAY 485
Cdd:PRK10524 417 MYGYNVKLLNEVTGE----------PCGPNEKGVLV-----------IEGPLPPGCmqtvwgDDDRFVKTYWSLfGRQVY 475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 486 LTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLDMADVAVYGVEVPgTEGRAGMA--------AVASPT 557
Cdd:PRK10524 476 STFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDA-LKGQVAVAfvvpkdsdSLADRE 554
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 40807357 558 GNCDLER-FAQVLEKELPLYARPIFLRLLPELHKTGTYKFqkteLRK------EGFDP 608
Cdd:PRK10524 555 ARLALEKeIMALVDSQLGAVARPARVWFVSALPKTRSGKL----LRRaiqaiaEGRDP 608
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
69-258 |
5.34e-05 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 46.70 E-value: 5.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 69 CLQERRTVPI------LFASTVRRHPDKTALifEGTDTHWTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGL 142
Cdd:PRK05691 3709 CNRSERDYPLeqsyvrLFEAQVAAHPQRIAA--SCLDQQWSYAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLLGM 3786
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 143 WLGMAKLGVEAALINTNLRRDALLHCLTTSRARALVfgsemASAIC--EVHASLDpslSLFCSGS-----WEPGAVPPST 215
Cdd:PRK05691 3787 IVGSFKAGAGYLPLDPGLPAQRLQRIIELSRTPVLV-----CSAACreQARALLD---ELGCANRprllvWEEVQAGEVA 3858
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 40807357 216 EHlDPLLKDAPkhlpscpdkgftDKLFY-IYTSGTTGLPKAAIV 258
Cdd:PRK05691 3859 SH-NPGIYSGP------------DNLAYvIYTSGSTGLPKGVMV 3889
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
238-308 |
5.80e-05 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 46.50 E-value: 5.80e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 40807357 238 TDKLFYIYTSGTTGLPKAAIVVH----SRYYRMAALVYYGfrmrPNDIVYDCLPLYHSAGNIVGIGQCLLHGMTV 308
Cdd:PRK06814 793 DDPAVILFTSGSEGTPKGVVLSHrnllANRAQVAARIDFS----PEDKVFNALPVFHSFGLTGGLVLPLLSGVKV 863
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
95-261 |
6.54e-05 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 46.12 E-value: 6.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 95 FEGTdTHWTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALLHCLTTSRA 174
Cdd:PTZ00216 116 FNET-RYITYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETEC 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 175 RALVF-GSEMASAICEVHASLDPSLSLFCSGSwepgaVPPST----------EHLDPLLKDAPKHLPsCPDKGFTDKLFY 243
Cdd:PTZ00216 195 KAIVCnGKNVPNLLRLMKSGGMPNTTIIYLDS-----LPASVdtegcrlvawTDVVAKGHSAGSHHP-LNIPENNDDLAL 268
|
170
....*....|....*....
gi 40807357 244 I-YTSGTTGLPKAaiVVHS 261
Cdd:PTZ00216 269 ImYTSGTTGDPKG--VMHT 285
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
234-529 |
1.95e-04 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 44.42 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 234 DKGFTDKLFYIYTSGTTGLPKAAIVVHSRYYRMAALVYYGFRMRPNDIVYDCLPLYHSagniVGIGQC----LLHGMTVV 309
Cdd:PRK06334 179 DKDPEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSFLPPFHA----YGFNSCtlfpLLSGVPVV 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 310 irkkFSASRFwddcikYNCTIVQYIGE-----------LCRYLLNQPPREAENQHQVRMAL--GNGLRQSIWTNFSSRFh 376
Cdd:PRK06334 255 ----FAYNPL------YPKKIVEMIDEakvtflgstpvFFDYILKTAKKQESCLPSLRFVVigGDAFKDSLYQEALKTF- 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 377 iPQVA--EFYGATECN--CSLGNFDSqvgacgfnSRILSFV-YPIR---LVRVNEDTMelirgpdgvcIPCQPGEPGQLV 448
Cdd:PRK06334 324 -PHIQlrQGYGTTECSpvITINTVNS--------PKHESCVgMPIRgmdVLIVSEETK----------VPVSSGETGLVL 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 449 GRiiqkdPLRRFDGYLNQGANNKKIAKDvfkkGDQAYLTGDvlvmdeLGYLyfrDRTGDTFrwkgenvstteVEGTLSRL 528
Cdd:PRK06334 385 TR-----GTSLFSGYLGEDFGQGFVELG----GETWYVTGD------LGYV---DRHGELF-----------LKGRLSRF 435
|
.
gi 40807357 529 L 529
Cdd:PRK06334 436 V 436
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
244-308 |
2.34e-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: 44.27 E-value: 2.34e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 40807357 244 IYTSGTTGLPKAAIVVHSRYYRMAALVYYGFRMRPND----IVYDCLPLYHSAGNIVGIGQCLLHGMTV 308
Cdd:cd05933 156 IYTSGTTGMPKGVMLSHDNITWTAKAASQHMDLRPATvgqeSVVSYLPLSHIAAQILDIWLPIKVGGQV 224
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
103-299 |
8.38e-04 |
|
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.
Pssm-ID: 341287 [Multi-domain] Cd Length: 588 Bit Score: 42.44 E-value: 8.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 103 TFRQLDEYSSSVANFLQA-RGLASGDVAAIFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALLHCLTTSRARALVFGS 181
Cdd:cd17632 69 TYAELWERVGAVAAAHDPeQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLAVSA 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 182 EMASAICEVHAS--LDPSLSLF------------CSGSWEPGAVPPSTEHLDPLL----KDAPKHLPSCPDKGfTDKL-F 242
Cdd:cd17632 149 EHLDLAVEAVLEggTPPRLVVFdhrpevdahraaLESARERLAAVGIPVTTLTLIavrgRDLPPAPLFRPEPD-DDPLaL 227
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 40807357 243 YIYTSGTTGLPKAAIVVHsRYYRMAALVYYGFRMR--PNDIVYDCLPLYHSAGNIVGIG 299
Cdd:cd17632 228 LIYTSGSTGTPKGAMYTE-RLVATFWLKVSSIQDIrpPASITLNFMPMSHIAGRISLYG 285
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
482-604 |
1.98e-03 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 41.23 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 482 DQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLDMADVAVYGVEVPGTEGRAGMAAVASPTGNCD 561
Cdd:PRK07008 408 DGWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLVVVKRPGAEVT 487
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 40807357 562 LERFAQVLEKELPLYARPIFLRLLPELHKTGTYKFQKTELRKE 604
Cdd:PRK07008 488 REELLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKLREQ 530
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
487-614 |
2.09e-03 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 41.31 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 487 TGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLDMADVAVYGVEVPGTEGRAGMAAVASPTGNCDLE--- 563
Cdd:PRK05620 434 TGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLAVTVLAPGIEPTREtae 513
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 40807357 564 RFAQVLEKELPLYARPIFLRLLPELHKTGTYKFQKTELRK---EG-FDPAIVKDP 614
Cdd:PRK05620 514 RLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDLRQhlaDGdFEIIKLKGP 568
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
87-205 |
4.88e-03 |
|
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Pssm-ID: 341302 [Multi-domain] Cd Length: 520 Bit Score: 39.81 E-value: 4.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 87 HPDKTALIFEGT-----DTHWTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGVEAALINTNLR 161
Cdd:cd17647 1 FPERTCVVETPSlnsskTRSFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYP 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 40807357 162 RDALLHCLTTSRARALVfGSEMASAIceVHASLDPSLSlFCSGS 205
Cdd:cd17647 81 PARQNIYLGVAKPRGLI-VIRAAGVV--VGPDSNPTLS-FTSGS 120
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
239-290 |
9.99e-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: 38.74 E-value: 9.99e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807357 239 DKLFYI-YTSGTTGLPKAAIVVHSryyRMAALV-------YYGFRMRPNDIVYDCLPLYH 290
Cdd:cd05927 114 EDLATIcYTSGTTGNPKGVMLTHG---NIVSNVagvfkilEILNKINPTDVYISYLPLAH 170
|
|
| |
