|
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: 942.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 99 DTHWTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALRHCLDTSKARALI 178
Cdd:cd05939 1 DRHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 179 FgsemasaiceihasleptlslfcsgswepstvpvstEHLDPLLEDAPKHLPSHPDKGFTDKLFYIYTSGTTGLPKAAIV 258
Cdd:cd05939 81 F------------------------------------NLLDPLLTQSSTEPPSQDDVNFRDKLFYIYTSGTTGLPKAAVI 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 259 VHSRYYRMASLVYYGFRMRPDDIVYDCLPLYHSAGNIVGIGQCLLHGMTVVIRKKFSASRFWDDCIKYNCTIVQYIGELC 338
Cdd:cd05939 125 VHSRYYRIAAGAYYAFGMRPEDVVYDCLPLYHSAGGIMGVGQALLHGSTVVIRKKFSASNFWDDCVKYNCTIVQYIGEIC 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 339 RYLLNQPPREAESRHKVRMALGNGLRQSIWTDFSSRFHIPQVAEFYGATECNCSLGNFDSRVGACGFNSRILSFVYPIRL 418
Cdd:cd05939 205 RYLLAQPPSEEEQKHNVRLAVGNGLRPQIWEQFVRRFGIPQIGEFYGATEGNSSLVNIDNHVGACGFNSRILPSVYPIRL 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 419 VRVNEDTMELIRGPDGVCIPCQPGQPGQLVGRIIQQDPLRRFDGYLNQGANNKKIANDVFKKGDQAYLTGDVLVMDELGY 498
Cdd:cd05939 285 IKVDEDTGELIRDSDGLCIPCQPGEPGLLVGKIIQNDPLRRFDGYVNEGATNKKIARDVFKKGDSAFLSGDVLVMDELGY 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 499 LYFRDRTGDTFRWKGENVSTTEVEGTLSRLLHMADVAVYGVEVPGTEGRAGMAAVASPISNCDLESFAQTLKKELPLYAR 578
Cdd:cd05939 365 LYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVYGVEVPGVEGRAGMAAIVDPERKVDLDRFSAVLAKSLPPYAR 444
|
490 500 510
....*....|....*....|....*....|
gi 45597453 579 PIFLRFLPELHKTGTFKFQKTELRKEGFDP 608
Cdd:cd05939 445 PQFIRLLPEVDKTGTFKLQKTDLQKEGYDP 474
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
75-643 |
0e+00 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 715.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 75 TVPLLFASMVQRHPDKTALIFEgtDTHWTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKLGVEAA 154
Cdd:PRK08279 38 SLGDVFEEAAARHPDRPALLFE--DQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 155 LINTNLRRDALRHCLDTSKARALIFGSEMASAICEIHASLEPTLSLFCSGSwEPSTVPVSTEHLDPLLEDAPKHLP-SHP 233
Cdd:PRK08279 116 LLNTQQRGAVLAHSLNLVDAKHLIVGEELVEAFEEARADLARPPRLWVAGG-DTLDDPEGYEDLAAAAAGAPTTNPaSRS 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 234 DKGFTDKLFYIYTSGTTGLPKAAIVVHSRYYRMASlvyyGF----RMRPDDIVYDCLPLYHSAGNIVGIGQCLLHGMTVV 309
Cdd:PRK08279 195 GVTAKDTAFYIYTSGTTGLPKAAVMSHMRWLKAMG----GFggllRLTPDDVLYCCLPLYHNTGGTVAWSSVLAAGATLA 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 310 IRKKFSASRFWDDCIKYNCTIVQYIGELCRYLLNQPPREAESRHKVRMALGNGLRQSIWTDFSSRFHIPQVAEFYGATEC 389
Cdd:PRK08279 271 LRRKFSASRFWDDVRRYRATAFQYIGELCRYLLNQPPKPTDRDHRLRLMIGNGLRPDIWDEFQQRFGIPRILEFYAASEG 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 390 NCSLGNFDSRVGACGFNSRILSfvYPIRLVRVNEDTMELIRGPDGVCIPCQPGQPGQLVGRIiqqDPLRRFDGYLNQGAN 469
Cdd:PRK08279 351 NVGFINVFNFDGTVGRVPLWLA--HPYAIVKYDVDTGEPVRDADGRCIKVKPGEVGLLIGRI---TDRGPFDGYTDPEAS 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 470 NKKIANDVFKKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLHMADVAVYGVEVPGTEGRAG 549
Cdd:PRK08279 426 EKKILRDVFKKGDAWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVATTEVENALSGFPGVEEAVVYGVEVPGTDGRAG 505
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 550 MAA-VASPISNCDLESFAQTLKKELPLYARPIFLRFLPELHKTGTFKFQKTELRKEGFDPSVVKDPLFYLDARKGCYVAL 628
Cdd:PRK08279 506 MAAiVLADGAEFDLAALAAHLYERLPAYAVPLFVRLVPELETTGTFKYRKVDLRKEGFDPSKVDDPLYVLDPGSGGYVPL 585
|
570
....*....|....*
gi 45597453 629 DQEAYTRIQAGEEKL 643
Cdd:PRK08279 586 TAELYAEIAAGKFRL 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: 699.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 99 DTHWTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALRHCLDTSKARALI 178
Cdd:cd05940 1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 179 FgsemasaiceihasleptlslfcsgswepstvpvstehldplledapkhlpshpdkgftDKLFYIYTSGTTGLPKAAIV 258
Cdd:cd05940 81 V-----------------------------------------------------------DAALYIYTSGTTGLPKAAII 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 259 VHSRYYRMASLVYYGFRMRPDDIVYDCLPLYHSAGNIVGIGQCLLHGMTVVIRKKFSASRFWDDCIKYNCTIVQYIGELC 338
Cdd:cd05940 102 SHRRAWRGGAFFAGSGGALPSDVLYTCLPLYHSTALIVGWSACLASGATLVIRKKFSASNFWDDIRKYQATIFQYIGELC 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 339 RYLLNQPPREAESRHKVRMALGNGLRQSIWTDFSSRFHIPQVAEFYGATECNCSLGNFDSRVGACGFNSRILSFVYPIRL 418
Cdd:cd05940 182 RYLLNQPPKPTERKHKVRMIFGNGLRPDIWEEFKERFGVPRIAEFYAATEGNSGFINFFGKPGAIGRNPSLLRKVAPLAL 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 419 VRVNEDTMELIRGPDGVCIPCQPGQPGQLVGRIIqqdPLRRFDGYLNQGANNKKIANDVFKKGDQAYLTGDVLVMDELGY 498
Cdd:cd05940 262 VKYDLESGEPIRDAEGRCIKVPRGEPGLLISRIN---PLEPFDGYTDPAATEKKILRDVFKKGDAWFNTGDLMRLDGEGF 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 499 LYFRDRTGDTFRWKGENVSTTEVEGTLSRLLHMADVAVYGVEVPGTEGRAGMAAVASPIS-NCDLESFAQTLKKELPLYA 577
Cdd:cd05940 339 WYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQVPGTDGRAGMAAIVLQPNeEFDLSALAAHLEKNLPGYA 418
|
490 500 510
....*....|....*....|....*....|.
gi 45597453 578 RPIFLRFLPELHKTGTFKFQKTELRKEGFDP 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: 578.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 103 TFRQLDEYSSSVAN-FLQARGLASGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALRHCLDTSKARALIFGS 181
Cdd:cd05938 7 TYRDVDRRSNQAARaLLAHAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAKVLVVAP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 182 EMASAICEIHASL-EPTLSLFCSGswePSTVPVSTEHLDPLLEDA-----PKHLPSHPDkgFTDKLFYIYTSGTTGLPKA 255
Cdd:cd05938 87 ELQEAVEEVLPALrADGVSVWYLS---HTSNTEGVISLLDKVDAAsdepvPASLRAHVT--IKSPALYIYTSGTTGLPKA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 256 AIVVHSRYYRMaSLVYYGFRMRPDDIVYDCLPLYHSAGNIVGIGQCLLHGMTVVIRKKFSASRFWDDCIKYNCTIVQYIG 335
Cdd:cd05938 162 ARISHLRVLQC-SGFLSLCGVTADDVIYITLPLYHSSGFLLGIGGCIELGATCVLKPKFSASQFWDDCRKHNVTVIQYIG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 336 ELCRYLLNQPPREAESRHKVRMALGNGLRQSIWTDFSSRFHIPQVAEFYGATECNCSLGNFDSRVGACGFNSRILSFVYP 415
Cdd:cd05938 241 ELLRYLCNQPQSPNDRDHKVRLAIGNGLRADVWREFLRRFGPIRIREFYGSTEGNIGFFNYTGKIGAVGRVSYLYKLLFP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 416 IRLVRVNEDTMELIRGPDGVCIPCQPGQPGQLVGRIIQQDPlrrFDGYL-NQGANNKKIANDVFKKGDQAYLTGDVLVMD 494
Cdd:cd05938 321 FELIKFDVEKEEPVRDAQGFCIPVAKGEPGLLVAKITQQSP---FLGYAgDKEQTEKKLLRDVFKKGDVYFNTGDLLVQD 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 495 ELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLHMADVAVYGVEVPGTEGRAGMAAVA-SPISNCDLESFAQTLKKEL 573
Cdd:cd05938 398 QQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVYGVTVPGHEGRIGMAAVKlKPGHEFDGKKLYQHVREYL 477
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 574 PLYARPIFLRFLPELHKTGTFKFQKTELRKEGFDPSVVKDPLFYLDARKGCYVALDQEAY 633
Cdd:cd05938 478 PAYARPRFLRIQDSLEITGTFKQQKVRLVEEGFNPSIISDPLYFLDETQKTYVPLTPDIY 537
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
102-608 |
9.12e-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: 446.49 E-value: 9.12e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 102 WTFRQLDEYSSSVANFLQ-ARGLASGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALRHCLDTSKARALIfg 180
Cdd:cd05937 6 WTYSETYDLVLRYAHWLHdDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLSGSRFVI-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 181 semasaiceihasleptlslfcsgswepstvpvstehLDPlleDAPKHLpshpdkgftdklfyIYTSGTTGLPKAAIVVH 260
Cdd:cd05937 84 -------------------------------------VDP---DDPAIL--------------IYTSGTTGLPKAAAISW 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 261 SRYYRMASLVYYGFRMRPDDIVYDCLPLYHSAGNIVGIGQCLLHGMTVVIRKKFSASRFWDDCIKYNCTIVQYIGELCRY 340
Cdd:cd05937 110 RRTLVTSNLLSHDLNLKNGDRTYTCMPLYHGTAAFLGACNCLMSGGTLALSRKFSASQFWKDVRDSGATIIQYVGELCRY 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 341 LLNQPPREAESRHKVRMALGNGLRQSIWTDFSSRFHIPQVAEFYGATECNCSLGNFDS---RVGACGFNSRILSFVY--P 415
Cdd:cd05937 190 LLSTPPSPYDRDHKVRVAWGNGLRPDIWERFRERFNVPEIGEFYAATEGVFALTNHNVgdfGAGAIGHHGLIRRWKFenQ 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 416 IRLVRVNEDTMELIRGP-DGVCIPCQPGQPGQLVGRiIQQDPLRRFDGYL-NQGANNKKIANDVFKKGDQAYLTGDVLVM 493
Cdd:cd05937 270 VVLVKMDPETDDPIRDPkTGFCVRAPVGEPGEMLGR-VPFKNREAFQGYLhNEDATESKLVRDVFRKGDIYFRTGDLLRQ 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 494 DELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLHMADVAVYGVEVPGTEGRAGMAAV-----ASPISNCDLESFAQT 568
Cdd:cd05937 349 DADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGVKVPGHDGRAGCAAItleesSAVPTEFTKSLLASL 428
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 45597453 569 LKKELPLYARPIFLRFLPELHKTGTFKFQKTELRKEGFDP 608
Cdd:cd05937 429 ARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVLRDEGVDP 468
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
76-604 |
2.30e-95 |
|
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: 300.57 E-value: 2.30e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 76 VPLLFASMVQRHPDKTALIFEGTdtHWTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKLGVEAAL 155
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGR--RLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 156 INTNLRRDALRHCLDTSKARALIFgsemasaiceihasleptlslfcsgswepstvpvstehldplledapkhlpshpdk 235
Cdd:COG0318 79 LNPRLTAEELAYILEDSGARALVT-------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 236 gftdkLFYIYTSGTTGLPKAAIVVHSRYYRMASLVYYGFRMRPDDIVYDCLPLYHSAGNIVGIGQCLLHGMTVVIRKKFS 315
Cdd:COG0318 103 -----ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLPRFD 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 316 ASRFWDDCIKYNCTIVQYIGELCRYLLNQPPREAESRHKVRMAL--GNGLRQSIWTDFSSRFHIPqVAEFYGATECNCS- 392
Cdd:COG0318 178 PERVLELIERERVTVLFGVPTMLARLLRHPEFARYDLSSLRLVVsgGAPLPPELLERFEERFGVR-IVEGYGLTETSPVv 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 393 ----LGNFDSRVGACGFnsrilsfvyPIRLVRVnedtmeLIRGPDGvcIPCQPGQPGQLVGR---IiqqdplrrFDGYLN 465
Cdd:COG0318 257 tvnpEDPGERRPGSVGR---------PLPGVEV------RIVDEDG--RELPPGEVGEIVVRgpnV--------MKGYWN 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 466 QGANNKKiandVFKKGdqAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLHMADVAVYGVEVPGTe 545
Cdd:COG0318 312 DPEATAE----AFRDG--WLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKW- 384
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 546 GRAGMAAV-ASPISNCDLESFAQTLKKELPLYARPIFLRFLPELHKTGTFKFQKTELRKE 604
Cdd:COG0318 385 GERVVAFVvLRPGAELDAEELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRER 444
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
74-608 |
1.48e-88 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 285.88 E-value: 1.48e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 74 KTVPLLFASMVQRHPDKTALIFEGTdtHWTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKLGVEA 153
Cdd:PRK06155 21 RTLPAMLARQAERYPDRPLLVFGGT--RWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 154 ALINTNLRRDALRHCLDTSKARALIFGSEMASAICEIHASLEPTLSLFCSGSWEPSTVP--VSTEHLDPLLEDAPkhlPS 231
Cdd:PRK06155 99 VPINTALRGPQLEHILRNSGARLLVVEAALLAALEAADPGDLPLPAVWLLDAPASVSVPagWSTAPLPPLDAPAP---AA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 232 HPDKGftDKLFYIYTSGTTGLPKAAIVVHSRYYRMASLVYYGFRMRPDDIVYDCLPLYHS-AGNivGIGQCLLHGMTVVI 310
Cdd:PRK06155 176 AVQPG--DTAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADDVLYTTLPLFHTnALN--AFFQALLAGATYVL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 311 RKKFSASRFWDDCIKYNCTIVQYIGELCRYLLNQPPREAESRHKVRMALGNGLRQSIWTDFSSRFHIPqVAEFYGATECN 390
Cdd:PRK06155 252 EPRFSASGFWPAVRRHGATVTYLLGAMVSILLSQPARESDRAHRVRVALGPGVPAALHAAFRERFGVD-LLDGYGSTETN 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 391 --CSLGNFDSRVG-----ACGFNSRIlsfvypirlvrVNEDTMELirgpdgvcipcQPGQPGQLVGRiiQQDPLRRFDGY 463
Cdd:PRK06155 331 fvIAVTHGSQRPGsmgrlAPGFEARV-----------VDEHDQEL-----------PDGEPGELLLR--ADEPFAFATGY 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 464 LNQGANNKKIANDVFkkgdqaYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLHMADVAVYGVEVPG 543
Cdd:PRK06155 387 FGMPEKTVEAWRNLW------FHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSEL 460
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45597453 544 TEGRAGMAAVASPISNCDLESFAQTLKKELPLYARPIFLRFLPELHKTGTFKFQKTELRKEGFDP 608
Cdd:PRK06155 461 GEDEVMAAVVLRDGTALEPVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVLREQGVTA 525
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
99-602 |
1.53e-84 |
|
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: 271.47 E-value: 1.53e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 99 DTHWTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALRHCLDTSKARALI 178
Cdd:cd05934 1 GRRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 179 fgsemaSAICEIhasleptlslfcsgswepstvpvstehldplledapkhlpshpdkgftdklfyIYTSGTTGLPKAAIV 258
Cdd:cd05934 81 ------VDPASI-----------------------------------------------------LYTSGTTGPPKGVVI 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 259 VHSRYYRMASLVYYGFRMRPDDIVYDCLPLYHSAGNIVGIGQCLLHGMTVVIRKKFSASRFWDDCIKYNCTIVQYIGELC 338
Cdd:cd05934 102 THANLTFAGYYSARRFGLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLLPRFSASRFWSDVRRYGATVTNYLGAML 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 339 RYLLNQPPREAESRHKVRMALGNGLRQSIWTDFSSRFHIPqVAEFYGATE-CNCSLGNFDS--RVGACGfnsrilsfvYP 415
Cdd:cd05934 182 SYLLAQPPSPDDRAHRLRAAYGAPNPPELHEEFEERFGVR-LLEGYGMTEtIVGVIGPRDEprRPGSIG---------RP 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 416 IRLVRVnedtmeLIRGPDGVciPCQPGQPGQLVGRIIQqdPLRRFDGYLNQ-GANNKKIANDVFkkgdqayLTGDVLVMD 494
Cdd:cd05934 252 APGYEV------RIVDDDGQ--ELPAGEPGELVIRGLR--GWGFFKGYYNMpEATAEAMRNGWF-------HTGDLGYRD 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 495 ELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLHMADVAVYGVEVPGTEGRAGMAAVASPISNCDLESFAQTLKKELP 574
Cdd:cd05934 315 ADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLDPEELFAFCEGQLA 394
|
490 500
....*....|....*....|....*...
gi 45597453 575 LYARPIFLRFLPELHKTGTFKFQKTELR 602
Cdd:cd05934 395 YFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
84-512 |
3.75e-67 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 225.65 E-value: 3.75e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 84 VQRHPDKTALIFeGTDTHWTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRD 163
Cdd:pfam00501 5 AARTPDKTALEV-GEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 164 ALRHCLDTSKARALIFGSE-MASAICEIHASLEPTLSLFCSGSWEPSTVPVSTEHLDPLLEDAPKHLPSHPDkgftDKLF 242
Cdd:pfam00501 84 ELAYILEDSGAKVLITDDAlKLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVPPPPPPPPDPD----DLAY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 243 YIYTSGTTGLPKAAIVVH----SRYYRMASLVYYGFRMRPDDIVYDCLPLYHSAGNIVGIGQCLLHGMTVVIRKKFSA-- 316
Cdd:pfam00501 160 IIYTSGTTGKPKGVMLTHrnlvANVLSIKRVRPRGFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVVLPPGFPAld 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 317 -SRFWDDCIKYNCTIVQYIGELCRYLLNQPPREAESRHKVRMAL--GNGLRQSIWTDFSSRFhIPQVAEFYGATECNC-- 391
Cdd:pfam00501 240 pAALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSSLRLVLsgGAPLPPELARRFRELF-GGALVNGYGLTETTGvv 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 392 ----SLGNFDSRVGACGFnsrilsfvyPIRLVR---VNEDTMElirgpdgvciPCQPGQPGQLV--GRIIqqdplrrFDG 462
Cdd:pfam00501 319 ttplPLDEDLRSLGSVGR---------PLPGTEvkiVDDETGE----------PVPPGEPGELCvrGPGV-------MKG 372
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 45597453 463 YLNQ-GANNKKIANDVFkkgdqaYLTGDVLVMDELGYLYFRDRTGDTFRWK 512
Cdd:pfam00501 373 YLNDpELTAEAFDEDGW------YRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
241-597 |
7.66e-63 |
|
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341228 [Multi-domain] Cd Length: 336 Bit Score: 211.37 E-value: 7.66e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 241 LFYIYTSGTTGLPKAAIVVHSRYYRMASLVYYGFRMRPDDIVYDCLPLYHSAGnIVGIGQCLLHGMTVVIRKKFSASRFW 320
Cdd:cd04433 3 ALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGG-LFGLLGALLAGGTVVLLPKFDPEAAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 321 DDCIKYNCTIVQYIGELCRYLLNQPPREAESRHKVRMALGNG--LRQSIWTDFSSRFHIPqVAEFYGATECNCSL----- 393
Cdd:cd04433 82 ELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGapLPPELLERFEEAPGIK-LVNGYGLTETGGTVatgpp 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 394 GNFDSRVGACGFnsrilsfvyPIRLVRVNedtmelIRGPDGvcIPCQPGQPGQLVGRIIQqdplrRFDGYLNQGANNKki 473
Cdd:cd04433 161 DDDARKPGSVGR---------PVPGVEVR------IVDPDG--GELPPGEIGELVVRGPS-----VMKGYWNNPEATA-- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 474 andvFKKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLHMADVAVYGVEVPgTEGRAGMAAV 553
Cdd:cd04433 217 ----AVDEDGWYRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDP-EWGERVVAVV 291
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 45597453 554 -ASPISNCDLESFAQTLKKELPLYARPIFLRFLPELHKTGTFKFQ 597
Cdd:cd04433 292 vLRPGADLDAEELRAHVRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
89-618 |
4.36e-57 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 201.45 E-value: 4.36e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 89 DKTALIFEgtDTHWTFRQLDEYSSSVANFLQARGLASGNV-VALFMENRNEFvGLWLGMAKL-GVEAALINTNLRRDALR 166
Cdd:PRK07867 18 DDRGLYFE--DSFTSWREHIRGSAARAAALRARLDPTRPPhVGVLLDNTPEF-SLLLGAAALsGIVPVGLNPTRRGAALA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 167 HCLDTSKARALIFGSEMASAIceihASLEPTLSLFCSGSwepstvPVSTEHLDPLLEDAPKHLPSHPDkgftDKLFYIYT 246
Cdd:PRK07867 95 RDIAHADCQLVLTESAHAELL----DGLDPGVRVINVDS------PAWADELAAHRDAEPPFRVADPD----DLFMLIFT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 247 SGTTGLPKAAIVVHSRYYRMASLVYYGFRMRPDDIVYDCLPLYHSAGNIVGIGQCLLHGMTVVIRKKFSASRFWDDCIKY 326
Cdd:PRK07867 161 SGTSGDPKAVRCTHRKVASAGVMLAQRFGLGPDDVCYVSMPLFHSNAVMAGWAVALAAGASIALRRKFSASGFLPDVRRY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 327 NCTIVQYIGELCRYLLNQPPREAESRHKVRMALGNGLRQSIWTDFSSRFHIpQVAEFYGATECNCSLGNF-DSRVGACGf 405
Cdd:PRK07867 241 GATYANYVGKPLSYVLATPERPDDADNPLRIVYGNEGAPGDIARFARRFGC-VVVDGFGSTEGGVAITRTpDTPPGALG- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 406 nsrilsfvypirlvrvnedtmeliRGPDGVCI-------PCQPGQPG--------QLVGRIIQQDPLRRFDGYLN-QGAN 469
Cdd:PRK07867 319 ------------------------PLPPGVAIvdpdtgtECPPAEDAdgrllnadEAIGELVNTAGPGGFEGYYNdPEAD 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 470 NKKIANDVFKKGDQAYltgdvlvMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLHMADVAVYGVEVPgTEGRAG 549
Cdd:PRK07867 375 AERMRGGVYWSGDLAY-------RDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDP-VVGDQV 446
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45597453 550 MAAVA-SPISNCDLESFAQTL--KKELPLYARPIFLRFLPELHKTGTFKFQKTELRKEGFDPSvvkDPLFYL 618
Cdd:PRK07867 447 MAALVlAPGAKFDPDAFAEFLaaQPDLGPKQWPSYVRVCAELPRTATFKVLKRQLSAEGVDCA---DPVWWI 515
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
75-602 |
7.95e-56 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 197.72 E-value: 7.95e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 75 TVPLLFASM----VQRHPDKTALIFEGTDthWTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKLG 150
Cdd:PRK06187 3 DYPLTIGRIlrhgARKHPDKEAVYFDGRR--TTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 151 VEAALINTNLRRDALRHCLDTSKARALIFGSEMASAICEIHASLEPTLSLFCSGSWEPSTVPVSTEHLDPLLEDAPKHLP 230
Cdd:PRK06187 81 AVLHPINIRLKPEEIAYILNDAEDRVVLVDSEFVPLLAAILPQLPTVRTVIVEGDGPAAPLAPEVGEYEELLAAASDTFD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 231 sHPDKGFTDKLFYIYTSGTTGLPKAAIVVHSRYYRMASLVYYGFRMRPDDIVYDCLPLYHSAGniVGIG-QCLLHGMTVV 309
Cdd:PRK06187 161 -FPDIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVPMFHVHA--WGLPyLALMAGAKQV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 310 IRKKFSASRFWDDCIKYNCTIVQYIGELCRYLLNQPPREAESRHKVRMAL--GNGLRQSIWTDFSSRFHIpQVAEFYGAT 387
Cdd:PRK06187 238 IPRRFDPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYFVDFSSLRLVIygGAALPPALLREFKEKFGI-DLVQGYGMT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 388 ECncslgnfdSRVGAC--------GFNSRILSFVYPIRLVRVNedtmelIRGPDGVCIPCQPGQPGQLVGR---IIQqdp 456
Cdd:PRK06187 317 ET--------SPVVSVlppedqlpGQWTKRRSAGRPLPGVEAR------IVDDDGDELPPDGGEVGEIIVRgpwLMQ--- 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 457 lrrfdGYLNQ-GANNKKIANDvfkkgdqAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLHMADVA 535
Cdd:PRK06187 380 -----GYWNRpEATAETIDGG-------WLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVA 447
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45597453 536 VYGV------EVPGT--EGRAGMAAVASpisncDLESFaqtLKKELPLYARPIFLRFLPELHKTGTFKFQKTELR 602
Cdd:PRK06187 448 VIGVpdekwgERPVAvvVLKPGATLDAK-----ELRAF---LRGRLAKFKLPKRIAFVDELPRTSVGKILKRVLR 514
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
80-607 |
2.53e-51 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 186.00 E-value: 2.53e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 80 FASMV--QRHPDKTALIFEGTDthWTFRQLDEYSSSVANFLQARGLASGNV-VALFMENRNEFVgLWLGMAKLGvEAAL- 155
Cdd:PRK13388 5 IAQLLrdRAGDDTIAVRYGDRT--WTWREVLAEAAARAAALIALADPDRPLhVGVLLGNTPEML-FWLAAAALG-GYVLv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 156 -INTNLRRDALrhcldtskaralifGSEMASAICEI------HASLEPTLSLfcsgswepSTVPV----STEHLDpLLED 224
Cdd:PRK13388 81 gLNTTRRGAAL--------------AADIRRADCQLlvtdaeHRPLLDGLDL--------PGVRVldvdTPAYAE-LVAA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 225 APKHLPsHPDKGFTDKLFYIYTSGTTGLPKAAIVVHSRYYRMASLVYYGFRMRPDDIVYDCLPLYHSAGNIVGIGQCLLH 304
Cdd:PRK13388 138 AGALTP-HREVDAMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLTRDDVCYVSMPLFHSNAVMAGWAPAVAS 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 305 GMTVVIRKKFSASRFWDDCIKYNCTIVQYIGELCRYLLNQPPREAESRHKVRMALGNGLRQSIWTDFSSRFHIpQVAEFY 384
Cdd:PRK13388 217 GAAVALPAKFSASGFLDDVRRYGATYFNYVGKPLAYILATPERPDDADNPLRVAFGNEASPRDIAEFSRRFGC-QVEDGY 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 385 GATEcncslgnfdsrvGACgfnsrilsfvypiRLVRVnEDTME--LIRGPDGVCI-------PCQPGQ---------PGQ 446
Cdd:PRK13388 296 GSSE------------GAV-------------IVVRE-PGTPPgsIGRGAPGVAIynpetltECAVARfdahgallnADE 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 447 LVGRIIQQDPLRRFDGYLN-QGANNKKIANDVFKKGDQAYLtgdvlvmDELGYLYFRDRTGDTFRWKGENVSTTEVEGTL 525
Cdd:PRK13388 350 AIGELVNTAGAGFFEGYYNnPEATAERMRHGMYWSGDLAYR-------DADGWIYFAGRTADWMRVDGENLSAAPIERIL 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 526 SRLLHMADVAVYGVEVPGTeGRAGMAA-VASPISNCDLESFAQTL--KKELPLYARPIFLRFLPELHKTGTFKFQKTELR 602
Cdd:PRK13388 423 LRHPAINRVAVYAVPDERV-GDQVMAAlVLRDGATFDPDAFAAFLaaQPDLGTKAWPRYVRIAADLPSTATNKVLKRELI 501
|
....*
gi 45597453 603 KEGFD 607
Cdd:PRK13388 502 AQGWA 506
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
84-598 |
2.69e-51 |
|
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: 183.20 E-value: 2.69e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 84 VQRHPDKTALIFEGTDthWTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRD 163
Cdd:cd17631 5 ARRHPDRTALVFGGRS--LTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 164 ALRHCLDTSKARALIfgsemasaiceihasleptlslfcsgswepstvpvstehldplledapkhlpshpdkgftDKLFY 243
Cdd:cd17631 83 EVAYILADSGAKVLF------------------------------------------------------------DDLAL 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 244 I-YTSGTTGLPKAAIVVHSRYYRMASLVYYGFRMRPDDIVYDCLPLYHSAGNIVGIGQCLLHGMTVVIRKKFSASRFWDD 322
Cdd:cd17631 103 LmYTSGTTGRPKGAMLTHRNLLWNAVNALAALDLGPDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVILRKFDPETVLDL 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 323 CIKYNCTIVQYIGELCRYLLNQPPREAESRHKVRMALGNG------LRQsIWTDFSSRFHipqvaEFYGATECN---CSL 393
Cdd:cd17631 183 IERHRVTSFFLVPTMIQALLQHPRFATTDLSSLRAVIYGGapmperLLR-ALQARGVKFV-----QGYGMTETSpgvTFL 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 394 GNFD--SRVGACGfnsrilsfvYPIRLVRVNedtmelIRGPDGVciPCQPGQPGQLVGRIIQQdplrrFDGYLNQGANNK 471
Cdd:cd17631 257 SPEDhrRKLGSAG---------RPVFFVEVR------IVDPDGR--EVPPGEVGEIVVRGPHV-----MAGYWNRPEATA 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 472 KiandVFKKGdqAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLHMADVAVYGVEVPgTEGRAGMA 551
Cdd:cd17631 315 A----AFRDG--WFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDE-KWGEAVVA 387
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 45597453 552 AVA-SPISNCDLESFAQTLKKELPLYARPIFLRFLPELHKTGTFKFQK 598
Cdd:cd17631 388 VVVpRPGAELDEDELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
79-602 |
8.07e-51 |
|
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341259 [Multi-domain] Cd Length: 468 Bit Score: 182.76 E-value: 8.07e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 79 LFASMVQRHPDKTALIFEGTdtHWTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKLGVEAALINT 158
Cdd:cd05936 4 LLEEAARRFPDKTALIFMGR--KLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 159 NLRRDALRHCLDTSKARALIfgsemasaiceihasleptlslfcsgswepstVPVSTEHLdplLEDAPKHLPSHPDKGfT 238
Cdd:cd05936 82 LYTPRELEHILNDSGAKALI--------------------------------VAVSFTDL---LAAGAPLGERVALTP-E 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 239 DKLFYIYTSGTTGLPKAAIVVHSRYYRMASLV--YYGFRMRPDDIVYDCLPLYHSAGNIVGIGQCLLHGMTVVIRKKFSA 316
Cdd:cd05936 126 DVAVLQYTSGTTGVPKGAMLTHRNLVANALQIkaWLEDLLEGDDVVLAALPLFHVFGLTVALLLPLALGATIVLIPRFRP 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 317 SRFWDDCIKYNCTIV-----QYIGelcryLLNQPPREAESRHKVRMALGNG--LRQSIWTDFSSRFHIPqVAEFYGATEC 389
Cdd:cd05936 206 IGVLKEIRKHRVTIFpgvptMYIA-----LLNAPEFKKRDFSSLRLCISGGapLPVEVAERFEELTGVP-IVEGYGLTET 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 390 N----CSLGNFDSRVGACGfnsrilsfvYPIRlvrvneDTMELIRGPDGVCIPcqPGQPGQLVGRIIQqdplrRFDGYLN 465
Cdd:cd05936 280 SpvvaVNPLDGPRKPGSIG---------IPLP------GTEVKIVDDDGEELP--PGEVGELWVRGPQ-----VMKGYWN 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 466 QGANNKKiandVFKKGdqAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLHMADVAVYGV--EVPG 543
Cdd:cd05936 338 RPEETAE----AFVDG--WLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVpdPYSG 411
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 45597453 544 TEGRAgmAAVASPISNCDLESFAQTLKKELPLYARPIFLRFLPELHKTGTFKFQKTELR 602
Cdd:cd05936 412 EAVKA--FVVLKEGASLTEEEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
84-614 |
1.66e-47 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 175.69 E-value: 1.66e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 84 VQRHPDKTALIFE---GTDTHWTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNL 160
Cdd:COG0365 19 AEGRGDKVALIWEgedGEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPVFPGF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 161 RRDALRHCLDTSKARALI---------FGSEMASAICEIHASLEPTLSLFCSGSWEPSTVPVSTEHLDPLLEDAPKHLPS 231
Cdd:COG0365 99 GAEALADRIEDAEAKVLItadgglrggKVIDLKEKVDEALEELPSLEHVIVVGRTGADVPMEGDLDWDELLAAASAEFEP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 232 HPdKGFTDKLFYIYTSGTTGLPKAaiVVHS-RYYrMASLVYYG---FRMRPDDIVY---DClplyhsaGNIVGIGQC--- 301
Cdd:COG0365 179 EP-TDADDPLFILYTSGTTGKPKG--VVHThGGY-LVHAATTAkyvLDLKPGDVFWctaDI-------GWATGHSYIvyg 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 302 -LLHGMTVVI---RKKF-SASRFWDDCIKYNCTIvqyigeLC------RYLLNQPPREAESRH--KVRMALGNG--LRQS 366
Cdd:COG0365 248 pLLNGATVVLyegRPDFpDPGRLWELIEKYGVTV------FFtaptaiRALMKAGDEPLKKYDlsSLRLLGSAGepLNPE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 367 IWTDFSSRFHIPqVAEFYGATECNCSLGNF----DSRVGACGFnsrilsfvyPIRLVRVnedtmeLIRGPDGVciPCQPG 442
Cdd:COG0365 322 VWEWWYEAVGVP-IVDGWGQTETGGIFISNlpglPVKPGSMGK---------PVPGYDV------AVVDEDGN--PVPPG 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 443 QPGQLVgriIQQDPLRRFDGYLNqgaNNKKIANDVFKKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVE 522
Cdd:COG0365 384 EEGELV---IKGPWPGMFRGYWN---DPERYRETYFGRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIE 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 523 GTLSRLLHMADVAVYGVE--------------VPGTEGRAGMAAvaspisncDLesfAQTLKKELPLYARPIFLRFLPEL 588
Cdd:COG0365 458 SALVSHPAVAEAAVVGVPdeirgqvvkafvvlKPGVEPSDELAK--------EL---QAHVREELGPYAYPREIEFVDEL 526
|
570 580 590
....*....|....*....|....*....|.
gi 45597453 589 HKTGTFKFQKTELRK-----EGFDPSVVKDP 614
Cdd:COG0365 527 PKTRSGKIMRRLLRKiaegrPLGDTSTLEDP 557
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
88-603 |
1.24e-46 |
|
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: 171.73 E-value: 1.24e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 88 PDKTALIFEGTDTHWTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALRH 167
Cdd:cd05926 1 PDAPALVVPGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 168 CLDTSKARALI-----FGSEMASAICEIHASLEPTLSLFcSGSWEPSTVPVSTehLDPLLEDAPKHLPSHPDkgftDKLF 242
Cdd:cd05926 81 YLADLGSKLVLtpkgeLGPASRAASKLGLAILELALDVG-VLIRAPSAESLSN--LLADKKNAKSEGVPLPD----DLAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 243 YIYTSGTTGLPKAAIVVHSRYYRMASLVYYGFRMRPDDIVYDCLPLYHSAGNIVGIGQCLLHGMTVVIRKKFSASRFWDD 322
Cdd:cd05926 154 ILHTSGTTGRPKGVPLTHRNLAASATNITNTYKLTPDDRTLVVMPLFHVHGLVASLLSTLAAGGSVVLPPRFSASTFWPD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 323 CIKYNCTIVQYIGELCRYLLNQPPREAESR-HKVRMA--LGNGLRQSIWTDFSSRFHIPqVAEFYGATE------CNcsl 393
Cdd:cd05926 234 VRDYNATWYTAVPTIHQILLNRPEPNPESPpPKLRFIrsCSASLPPAVLEALEATFGAP-VLEAYGMTEaahqmtSN--- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 394 gNFDSRV---GACGfnsriLSFVYPIRLVrvnedtmelirGPDGvcipcQPGQPGQlVGRIIQQDPlRRFDGYLNQGANN 470
Cdd:cd05926 310 -PLPPGPrkpGSVG-----KPVGVEVRIL-----------DEDG-----EILPPGV-VGEICLRGP-NVTRGYLNNPEAN 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 471 KKIA--NDVFKKGDQAYLtgdvlvmDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLHMADVAVYGV--EVPGTEg 546
Cdd:cd05926 366 AEAAfkDGWFRTGDLGYL-------DADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVpdEKYGEE- 437
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 45597453 547 rAGMAAVASPISNCDLESFAQTLKKELPLYARPIFLRFLPELHKTGTFKFQKTELRK 603
Cdd:cd05926 438 -VAAAVVLREGASVTEEELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKVAE 493
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
98-595 |
2.27e-46 |
|
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: 170.86 E-value: 2.27e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 98 TDTHWTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALRHCLDTSKARAL 177
Cdd:cd05911 7 TGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 178 IFGSEMASAICEIHASLEPTLSLFCSGSWEPSTVPVSTEhLDPLLEDAPKHLPSHPDKGFTDKLFYIYTSGTTGLPKAAI 257
Cdd:cd05911 87 FTDPDGLEKVKEAAKELGPKDKIIVLDDKPDGVLSIEDL-LSPTLGEEDEDLPPPLKDGKDDTAAILYSSGTTGLPKGVC 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 258 VVHSRYYRMASLVYYGFR--MRPDDIVYDCLPLYHSAGnIVGIGQCLLHGMTVVIRKKFSASRFWDDCIKYNCTIVQYIG 335
Cdd:cd05911 166 LSHRNLIANLSQVQTFLYgnDGSNDVILGFLPLYHIYG-LFTTLASLLNGATVIIMPKFDSELFLDLIEKYKITFLYLVP 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 336 ELCRYLLNQPPREAESRHKVRMAL--GNGLRQSIWTDFSSRFHIPQVAEFYGATECNCSLG---NFDSRVGACGfnsRIL 410
Cdd:cd05911 245 PIAAALAKSPLLDKYDLSSLRVILsgGAPLSKELQELLAKRFPNATIKQGYGMTETGGILTvnpDGDDKPGSVG---RLL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 411 SFVypirLVR-VNEDTMELirgpdgvcipCQPGQPGQLVGRIIQQdplrrFDGYL-NQGANNKKIANDVFkkgdqaYLTG 488
Cdd:cd05911 322 PNV----EAKiVDDDGKDS----------LGPNEPGEICVRGPQV-----MKGYYnNPEATKETFDEDGW------LHTG 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 489 DVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLHMADVAVYGVEVP-GTEgRAGMAAVASPISNCDLESFAQ 567
Cdd:cd05911 377 DIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEvSGE-LPRAYVVRKPGEKLTEKEVKD 455
|
490 500 510
....*....|....*....|....*....|..
gi 45597453 568 TLKKELPLYARpifLR----FLPELHKTGTFK 595
Cdd:cd05911 456 YVAKKVASYKQ---LRggvvFVDEIPKSASGK 484
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
73-604 |
3.57e-43 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 162.79 E-value: 3.57e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 73 RKTVPLLFASMVQRHPDKTALIFEgtDTHWTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKLGVE 152
Cdd:PRK08316 10 RQTIGDILRRSARRYPDKTALVFG--DRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 153 AALINTNLRRDALRHCLDTSKARALIFGSEMASAIcEIHASLEPTLSLFCSGSWEPSTVPVSTEHLDPLLEDAPKHLPSh 232
Cdd:PRK08316 88 HVPVNFMLTGEELAYILDHSGARAFLVDPALAPTA-EAALALLPVDTLILSLVLGGREAPGGWLDFADWAEAGSVAEPD- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 233 PDKGFTDKLFYIYTSGTTGLPKAAIVVHSryyrmaSLV--YYG----FRMRPDDIVYDCLPLYHSAGNIVGIGQCLLHGM 306
Cdd:PRK08316 166 VELADDDLAQILYTSGTESLPKGAMLTHR------ALIaeYVScivaGDMSADDIPLHALPLYHCAQLDVFLGPYLYVGA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 307 TVVIRKKFSASRFWDDCIKYNCTI------VqYIGelcryLLNQP---PREAESRHK-------VRMALGNGLRQsiwtd 370
Cdd:PRK08316 240 TNVILDAPDPELILRTIEAERITSffapptV-WIS-----LLRHPdfdTRDLSSLRKgyygasiMPVEVLKELRE----- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 371 fssrfHIPQVA--EFYGATEC---NCSLG--NFDSRVGACGfnsRILSFVYpirlVRVNEDTMElirgpdgvciPCQPGQ 443
Cdd:PRK08316 309 -----RLPGLRfyNCYGQTEIaplATVLGpeEHLRRPGSAG---RPVLNVE----TRVVDDDGN----------DVAPGE 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 444 PGQLVGRIIQQdplrrFDGYLNQGAnnkKIAnDVFKKGdqAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEG 523
Cdd:PRK08316 367 VGEIVHRSPQL-----MLGYWDDPE---KTA-EAFRGG--WFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEE 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 524 TLSRLLHMADVAVYGVEVPgtegRAGMA--AVASPISNCDL--ESFAQTLKKELPLYARPIFLRFLPELHKTGTFKFQKT 599
Cdd:PRK08316 436 ALYTHPAVAEVAVIGLPDP----KWIEAvtAVVVPKAGATVteDELIAHCRARLAGFKVPKRVIFVDELPRNPSGKILKR 511
|
....*
gi 45597453 600 ELRKE 604
Cdd:PRK08316 512 ELRER 516
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
73-602 |
1.70e-42 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 160.62 E-value: 1.70e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 73 RKTVPLLFASMVQRHPDKTALIFE---GTDTHWTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKL 149
Cdd:PRK08008 6 GQHLRQMWDDLADVYGHKTALIFEssgGVVRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 150 GVEAALINTNLRRDALRHCLDTSKARALIFGSEMASAICEIHASLEPTLS-LFCSGSWEPSTVPVSteHLDPLLEDAPKH 228
Cdd:PRK08008 86 GAIMVPINARLLREESAWILQNSQASLLVTSAQFYPMYRQIQQEDATPLRhICLTRVALPADDGVS--SFTQLKAQQPAT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 229 LPSHPDKGFTDKLFYIYTSGTTGLPKAAIVVHsryyrmASLVYYGF------RMRPDDIVYDCLPLYHSAGNIVGIGQCL 302
Cdd:PRK08008 164 LCYAPPLSTDDTAEILFTSGTTSRPKGVVITH------YNLRFAGYysawqcALRDDDVYLTVMPAFHIDCQCTAAMAAF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 303 LHGMTVVIRKKFSASRFWDDCIKYNCTIVQYIGELCRYLLNQPPREAESRHKVR-----MALGNGLRQsiwtDFSSRFHI 377
Cdd:PRK08008 238 SAGATFVLLEKYSARAFWGQVCKYRATITECIPMMIRTLMVQPPSANDRQHCLRevmfyLNLSDQEKD----AFEERFGV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 378 pQVAEFYGATECNCSL-GNF--DSR----VGACGFNsrilsfvYPIRLvrVNEDTMELIRGPDG-VCIPCQPgqpgqlvG 449
Cdd:PRK08008 314 -RLLTSYGMTETIVGIiGDRpgDKRrwpsIGRPGFC-------YEAEI--RDDHNRPLPAGEIGeICIKGVP-------G 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 450 RIIqqdplrrFDGYLNQGANNKKI--ANDVFKKGDQAYltgdvlvMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSR 527
Cdd:PRK08008 377 KTI-------FKEYYLDPKATAKVleADGWLHTGDTGY-------VDEEGFFYFVDRRCNMIKRGGENVSCVELENIIAT 442
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45597453 528 LLHMADVAVYGVEVPGTEGRAGMAAVASPISNCDLESFAQTLKKELPLYARPIFLRFLPELHKTGTFKFQKTELR 602
Cdd:PRK08008 443 HPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
75-604 |
1.20e-41 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 158.14 E-value: 1.20e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 75 TVPLLFASMVQRHPDKTALIFEGTDThwTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKLGveAA 154
Cdd:PRK07656 6 TLPELLARAARRFGDKEAYVFGDQRL--TYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAG--AV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 155 LI--NTNLRRDALRHCLDTSKARALIFGSEMASAICEIHASLePTLSLF--CSGSwEPSTVPVSTEHLDPLLEDAPK--- 227
Cdd:PRK07656 82 VVplNTRYTADEAAYILARGDAKALFVLGLFLGVDYSATTRL-PALEHVviCETE-EDDPHTEKMKTFTDFLAAGDPaer 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 228 HLPSHPDkgftDKLFYIYTSGTTGLPKAAIVVHSRYYRMASLVYYGFRMRPDDIVYDCLPLYHSAGNIVGIGQCLLHGMT 307
Cdd:PRK07656 160 APEVDPD----DVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLAANPFFHVFGYKAGVNAPLMRGAT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 308 VVIRKKFSASRFWDDCIKYNCTIVQYIGELCRYLLNQPPREAESRHKVRMALGNG------LRQSiwtdFSSRFHIPQVA 381
Cdd:PRK07656 236 ILPLPVFDPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSAEDLSSLRLAVTGAasmpvaLLER----FESELGVDIVL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 382 EFYGATECN-----CSLGnfDSRV---GACGfnsrilsfvYPIRLVRVNedtmelIRGPDGVCIPcqPGQPGQLVGR--- 450
Cdd:PRK07656 312 TGYGLSEASgvttfNRLD--DDRKtvaGTIG---------TAIAGVENK------IVNELGEEVP--VGEVGELLVRgpn 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 451 IIQ---QDPLR-----RFDGYLNqgannkkiandvfkkgdqaylTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVE 522
Cdd:PRK07656 373 VMKgyyDDPEAtaaaiDADGWLH---------------------TGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVE 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 523 GTLSRLLHMADVAVYGVEVPGTeGRAGMA-AVASPISNCDLESFAQTLKKELPLYARPIFLRFLPELHKTGTFKFQKTEL 601
Cdd:PRK07656 432 EVLYEHPAVAEAAVIGVPDERL-GEVGKAyVVLKPGAELTEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRAL 510
|
...
gi 45597453 602 RKE 604
Cdd:PRK07656 511 REK 513
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
102-603 |
2.80e-36 |
|
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: 141.32 E-value: 2.80e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 102 WTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALRHCLDTSKARALIFGS 181
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 182 EmasaiceihasleptlslfcsgswepstvpvstehldplledapkhlpshpdkgftDKLFYIYTSGTTGLPKAAIVVHS 261
Cdd:cd05972 81 E--------------------------------------------------------DPALIYFTSGTTGLPKGVLHTHS 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 262 ryYRMASLVYYGF--RMRPDDIVY---DCLPLYHSAGNIVGIgqcLLHGMTVVI--RKKFSASRFWDDCIKYNCTIVQYI 334
Cdd:cd05972 105 --YPLGHIPTAAYwlGLRPDDIHWniaDPGWAKGAWSSFFGP---WLLGATVFVyeGPRFDAERILELLERYGVTSFCGP 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 335 GELCRYLLNQ-PPREAESRHKVRMALGNGLRQSIWTDFSSRFHIPqVAEFYGATECNCSLGNF---DSRVGACGfnsril 410
Cdd:cd05972 180 PTAYRMLIKQdLSSYKFSHLRLVVSAGEPLNPEVIEWWRAATGLP-IRDGYGQTETGLTVGNFpdmPVKPGSMG------ 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 411 sfvYPIRLVRVnedtmELIRGpDGVciPCQPGQPGQLVgriIQQDPLRRFDGYLNQGANNKKiandvfKKGDQAYLTGDV 490
Cdd:cd05972 253 ---RPTPGYDV-----AIIDD-DGR--ELPPGEEGDIA---IKLPPPGLFLGYVGDPEKTEA------SIRGDYYLTGDR 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 491 LVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLHMADVAVYGV--EVPGTEGRAGMAAVAS-PISNCDLESFAQ 567
Cdd:cd05972 313 AYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSpdPVRGEVVKAFVVLTSGyEPSEELAEELQG 392
|
490 500 510
....*....|....*....|....*....|....*.
gi 45597453 568 TLKKELPLYARPIFLRFLPELHKTGTFKFQKTELRK 603
Cdd:cd05972 393 HVKKVLAPYKYPREIEFVEELPKTISGKIRRVELRD 428
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
80-611 |
1.27e-35 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 141.45 E-value: 1.27e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 80 FASMVQRH----PDKTALIFEGTDTHWtfRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKLGVEAAL 155
Cdd:PRK07786 19 WVNQLARHalmqPDAPALRFLGNTTTW--RELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 156 INTNLRRDALRHCLDTSKARALIFGSEMASAICEIHAsLEPTLSLFCSGSWEPSTVPVSTEhlDPLLEDAPKHLPSH-PD 234
Cdd:PRK07786 97 VNFRLTPPEIAFLVSDCGAHVVVTEAALAPVATAVRD-IVPLLSTVVVAGGSSDDSVLGYE--DLLAEAGPAHAPVDiPN 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 235 KgfTDKLFyIYTSGTTGLPKAAIVVHSRYYRMASLVYYGFRM-RPDDIVYDCLPLYHSAGnIVGIGQCLLHGMTVVIR-- 311
Cdd:PRK07786 174 D--SPALI-MYTSGTTGRPKGAVLTHANLTGQAMTCLRTNGAdINSDVGFVGVPLFHIAG-IGSMLPGLLLGAPTVIYpl 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 312 KKFSASRFWDDCIKYNCTIVQYIGELCRYLLNQPprEAESRH-KVRMaLGNGL---RQSIWTDFSSRFHIPQVAEFYGAT 387
Cdd:PRK07786 250 GAFDPGQLLDVLEAEKVTGIFLVPAQWQAVCAEQ--QARPRDlALRV-LSWGAapaSDTLLRQMAATFPEAQILAAFGQT 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 388 ECN---CSLGNFDS--RVGACGfnsrilsFVYPIRLVRVNEDTMELIrgpdgvcipcQPGQpgqlVGRIIQQDPlRRFDG 462
Cdd:PRK07786 327 EMSpvtCMLLGEDAirKLGSVG-------KVIPTVAARVVDENMNDV----------PVGE----VGEIVYRAP-TLMSG 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 463 YLnqgaNNKKIANDVFKKGdqAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLHMADVAVYG---- 538
Cdd:PRK07786 385 YW----NNPEATAEAFAGG--WFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGrade 458
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45597453 539 --VEVPgtegrAGMAAVASPISNCDLESFAQTLKKELPLYARPIFLRFLPELHKTGTFKFQKTELRKEGFDPSVV 611
Cdd:PRK07786 459 kwGEVP-----VAVAAVRNDDAALTLEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKVLKTELRERYGACVNV 528
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
88-602 |
1.32e-35 |
|
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: 140.97 E-value: 1.32e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 88 PDKTALIfeGTDTHWTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALRH 167
Cdd:cd05959 18 GDKTAFI--DDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 168 CLDTSKARALIFGSEMASAICEIHASLEPTL-SLFCSGSWEPSTVPVSTEHLDPLLEDAPKHLPSHPDkgftDKLFYIYT 246
Cdd:cd05959 96 YLEDSRARVVVVSGELAPVLAAALTKSEHTLvVLIVSGGAGPEAGALLLAELVAAEAEQLKPAATHAD----DPAFWLYS 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 247 SGTTGLPKAAIVVHSRYYRMASLvyYG---FRMRPDDIVYDCLPLYHSagniVGIGQCLLH----GMTVVIRKKF-SASR 318
Cdd:cd05959 172 SGSTGRPKGVVHLHADIYWTAEL--YArnvLGIREDDVCFSAAKLFFA----YGLGNSLTFplsvGATTVLMPERpTPAA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 319 FWDDCIKYNCTIVQYIGELCRYLLNQPPREAESRHKVRMAL--GNGLRQSIWTDFSSRFHIpQVAEFYGATEC-NCSLGN 395
Cdd:cd05959 246 VFKRIRRYRPTVFFGVPTLYAAMLAAPNLPSRDLSSLRLCVsaGEALPAEVGERWKARFGL-DILDGIGSTEMlHIFLSN 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 396 F--DSRVGACGFNsrilsfV--YPIRLvrvnedtmeliRGPDGVCIPcqPGQPGQLVGRIIQQDPlrrfdGYLNQGANNK 471
Cdd:cd05959 325 RpgRVRYGTTGKP------VpgYEVEL-----------RDEDGGDVA--DGEPGELYVRGPSSAT-----MYWNNRDKTR 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 472 KiandVFKKGdqAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLHMADVAVYGVEVPgtEGRAGMA 551
Cdd:cd05959 381 D----TFQGE--WTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDE--DGLTKPK 452
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 45597453 552 AVASPISNCDLESFAQT-----LKKELPLYARPIFLRFLPELHKTGTFKFQKTELR 602
Cdd:cd05959 453 AFVVLRPGYEDSEALEEelkefVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
84-602 |
8.80e-35 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 138.29 E-value: 8.80e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 84 VQRHPDKTALIFEGTDTHWTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRD 163
Cdd:PRK13391 7 AQTTPDKPAVIMASTGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 164 ALRHCLDTSKARALIfGSEMASAICEIHASLEPTLslfcsgswEPSTVPVSTEHLDPL--LEDAPKHLPSHP--DKGFTD 239
Cdd:PRK13391 87 EAAYIVDDSGARALI-TSAAKLDVARALLKQCPGV--------RHRLVLDGDGELEGFvgYAEAVAGLPATPiaDESLGT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 240 KLFyiYTSGTTGLPKAAI-------VVHSRYYRMASLVYYGFRmrpDDIVYDC-LPLYHSAGN-IVGIGQCLlhGMTVVI 310
Cdd:PRK13391 158 DML--YSSGTTGRPKGIKrplpeqpPDTPLPLTAFLQRLWGFR---SDMVYLSpAPLYHSAPQrAVMLVIRL--GGTVIV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 311 RKKFSASRFWDDCIKYNCTIVQYIGELCRYLLnQPPREAESRHKVrmalgNGLRQSI-----------------WTdfss 373
Cdd:PRK13391 231 MEHFDAEQYLALIEEYGVTHTQLVPTMFSRML-KLPEEVRDKYDL-----SSLEVAIhaaapcppqvkeqmidwWG---- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 374 rfhiPQVAEFYGATECNcslgnfdsrvGACGFNSRiLSFVYPIRLVRVNEDTMElIRGPDGVciPCQPGQPGQlvgriIQ 453
Cdd:PRK13391 301 ----PIIHEYYAATEGL----------GFTACDSE-EWLAHPGTVGRAMFGDLH-ILDDDGA--ELPPGEPGT-----IW 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 454 QDPLRRFDgYLNQGANNKKIANDvfkkgDQAYLT-GDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLsrLLH-- 530
Cdd:PRK13391 358 FEGGRPFE-YLNDPAKTAEARHP-----DGTWSTvGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLL--ITHpk 429
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45597453 531 MADVAVYGveVPGTEGRAGMAAVASPISNCDL-ESFAQTL----KKELPLYARPIFLRFLPELHKTGTFKFQKTELR 602
Cdd:PRK13391 430 VADAAVFG--VPNEDLGEEVKAVVQPVDGVDPgPALAAELiafcRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLLR 504
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
84-604 |
5.20e-34 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 135.86 E-value: 5.20e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 84 VQRHPDKTALIFEGTDthWTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRD 163
Cdd:PRK03640 12 AFLTPDRTAIEFEEKK--VTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSRE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 164 ALRHCLDTSKARALIfgsemasaiceihasleptlslfCSGSWEPSTVPVSTEHLDPLLEDAPKHLPSHPDKGFTDKLFY 243
Cdd:PRK03640 90 ELLWQLDDAEVKCLI-----------------------TDDDFEAKLIPGISVKFAELMNGPKEEAEIQEEFDLDEVATI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 244 IYTSGTTGLPKAAIVVHSRYY--RMASLVYYGfrMRPDDIVYDCLPLYHSAG-NIvgIGQCLLHGMTVVIRKKFSASRFW 320
Cdd:PRK03640 147 MYTSGTTGKPKGVIQTYGNHWwsAVGSALNLG--LTEDDCWLAAVPIFHISGlSI--LMRSVIYGMRVVLVEKFDAEKIN 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 321 DDCIKYNCTIVQYIGELCRYLLNQPPREAESRHKVRMALGNG------LRQsiwtdfSSRFHIPqVAEFYGATE-CN--C 391
Cdd:PRK03640 223 KLLQTGGVTIISVVSTMLQRLLERLGEGTYPSSFRCMLLGGGpapkplLEQ------CKEKGIP-VYQSYGMTEtASqiV 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 392 SLGNFDS--RVGACG---FNSRIlsfvypirlvRVNEDTmelirgpdgvcipcQPGQPGQlVGRIIQQDPlRRFDGYLNQ 466
Cdd:PRK03640 296 TLSPEDAltKLGSAGkplFPCEL----------KIEKDG--------------VVVPPFE-EGEIVVKGP-NVTKGYLNR 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 467 -GANNKKIANDVFKKGDQAYLtgdvlvmDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLHMADVAVYGVEvpgtE 545
Cdd:PRK03640 350 eDATRETFQDGWFKTGDIGYL-------DEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVP----D 418
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45597453 546 GRAGMAAVA-----SPISNCDLESFAQTlkkELPLYARPIFLRFLPELHKTGTFKFQKTELRKE 604
Cdd:PRK03640 419 DKWGQVPVAfvvksGEVTEEELRHFCEE---KLAKYKVPKRFYFVEELPRNASGKLLRHELKQL 479
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
90-602 |
8.85e-34 |
|
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: 134.13 E-value: 8.85e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 90 KTALIfeGTDTHWTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALRHCL 169
Cdd:cd05919 1 KTAFY--AADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 170 DTSKARALIFGsemASAICeihasleptlslfcsgswepstvpvstehldplledapkhlpshpdkgftdklFYIYTSGT 249
Cdd:cd05919 79 RDCEARLVVTS---ADDIA-----------------------------------------------------YLLYSSGT 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 250 TGLPKAAIVVHSRYYRMASLvyYG---FRMRPDDIVYDCLPLY--HSAGNIVGIGqcLLHGMTVVIRKKF-SASRFWDDC 323
Cdd:cd05919 103 TGPPKGVMHAHRDPLLFADA--MAreaLGLTPGDRVFSSAKMFfgYGLGNSLWFP--LAVGASAVLNPGWpTAERVLATL 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 324 IKYNCTIVQYIGELCRYLLNQPPREAESRHKVRMAL--GNGLRQSIWTDFSSRFHIPqVAEFYGATEC-NCSLGNF--DS 398
Cdd:cd05919 179 ARFRPTVLYGVPTFYANLLDSCAGSPDALRSLRLCVsaGEALPRGLGERWMEHFGGP-ILDGIGATEVgHIFLSNRpgAW 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 399 RVGACGfnsRILSFvYPIRLVrvnedtmelirGPDGVCIPcqPGQPGQLVGRIIQQDPlrrfdGYLNQGANNKKIANDVF 478
Cdd:cd05919 258 RLGSTG---RPVPG-YEIRLV-----------DEEGHTIP--PGEEGDLLVRGPSAAV-----GYWNNPEKSRATFNGGW 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 479 kkgdqaYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLHMADVAVygVEVPGTEGRAGMAA---VAS 555
Cdd:cd05919 316 ------YRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAV--VAVPESTGLSRLTAfvvLKS 387
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 45597453 556 PISNCDL--ESFAQTLKKELPLYARPIFLRFLPELHKTGTFKFQKTELR 602
Cdd:cd05919 388 PAAPQESlaRDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKLR 436
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
74-595 |
3.93e-33 |
|
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: 133.40 E-value: 3.93e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 74 KTVPLLFASMVQRHPDKTALIFEGTDTHWTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKLGVEA 153
Cdd:cd05923 1 QTVFEMLRRAASRAPDACAIADPARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 154 ALINTNLRRDALRHCLDTSKARALIF--GSEMASAI-----CEIHASLEPTLSLFCSGSwepstvpvstehldPLLEDap 226
Cdd:cd05923 81 ALINPRLKAAELAELIERGEMTAAVIavDAQVMDAIfqsgvRVLALSDLVGLGEPESAG--------------PLIED-- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 227 khlpshPDKGFTDKLFYIYTSGTTGLPKAAIVVH----SRYYRMASLVyyGFRMRPDDIVYDCLPLYHSAGNIVGIGQCL 302
Cdd:cd05923 145 ------PPREPEQPAFVFYTSGTTGLPKGAVIPQraaeSRVLFMSTQA--GLRHGRHNVVLGLMPLYHVIGFFAVLVAAL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 303 LHGMTVVIRKKFSASRfwddcikynctIVQYIGEL---CRYL-----------LNQPPREAESRHKVRMAlGNGLRQSIW 368
Cdd:cd05923 217 ALDGTYVVVEEFDPAD-----------ALKLIEQErvtSLFAtpthldalaaaAEFAGLKLSSLRHVTFA-GATMPDAVL 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 369 TDFSSRFHIPQVaEFYGATECNCSLGNFDSRVGAC---GFNSRilsfvypIRLVRVNEDTMELIrgpdgvcipcQPGQPG 445
Cdd:cd05923 285 ERVNQHLPGEKV-NIYGTTEAMNSLYMRDARTGTEmrpGFFSE-------VRIVRIGGSPDEAL----------ANGEEG 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 446 QLvgrIIQQDPLRRFDGYLNQGANNKKiandvfKKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTL 525
Cdd:cd05923 347 EL---IVAAAADAAFTGYLNQPEATAK------KLQDGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVL 417
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45597453 526 SRLLHMADVAVYGVevpgTEGRAGMAAVA------SPISNCDLESFAQTlkKELPLYARPIFLRFLPELHKTGTFK 595
Cdd:cd05923 418 SRHPGVTEVVVIGV----ADERWGQSVTAcvvpreGTLSADELDQFCRA--SELADFKRPRRYFFLDELPKNAMNK 487
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
83-602 |
6.81e-33 |
|
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: 133.39 E-value: 6.81e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 83 MVQRHPDKTALIF---EGTDTHWTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKLGVEAALINTN 159
Cdd:cd05970 26 MAKEYPDKLALVWcddAGEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 160 LRRDALRHCLDTSKARALIFGSE--MASAICEIHASL-EPTLSLFCSGSwepstVPVSTEHLDPLLEDAPKHL--PSHPD 234
Cdd:cd05970 106 LTAKDIVYRIESADIKMIVAIAEdnIPEEIEKAAPECpSKPKLVWVGDP-----VPEGWIDFRKLIKNASPDFerPTANS 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 235 KGFTDKLFYIY-TSGTTGLPKaaIVVHSRYYRMASLV--YYGFRMRPDDIvydclplyHSAGNIVGIGQCL--------L 303
Cdd:cd05970 181 YPCGEDILLVYfSSGTTGMPK--MVEHDFTYPLGHIVtaKYWQNVREGGL--------HLTVADTGWGKAVwgkiygqwI 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 304 HGMTVVI--RKKFSASRFWDDCIKYNCTIVQYIGELCRYLLnqppREAESRH---KVRMAL--GNGLRQSIWTDFSSRFH 376
Cdd:cd05970 251 AGAAVFVydYDKFDPKALLEKLSKYGVTTFCAPPTIYRFLI----REDLSRYdlsSLRYCTtaGEALNPEVFNTFKEKTG 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 377 IpQVAEFYGATECNCSLGNF---DSRVGACGFNSRilsfVYPIRLVRvnedtmelirgPDGVciPCQPGQPGQLVGRIIQ 453
Cdd:cd05970 327 I-KLMEGFGQTETTLTIATFpwmEPKPGSMGKPAP----GYEIDLID-----------REGR--SCEAGEEGEIVIRTSK 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 454 QDPLRRFDGYlnqGANNKKIAnDVFKKGdqAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLsrLLHMA- 532
Cdd:cd05970 389 GKPVGLFGGY---YKDAEKTA-EVWHDG--YYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESAL--IQHPAv 460
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45597453 533 -DVAVYGVEVPgtegRAGMAAVASPISNCDLESfAQTLKKEL--------PLYARPIFLRFLPELHKTGTFKFQKTELR 602
Cdd:cd05970 461 lECAVTGVPDP----IRGQVVKATIVLAKGYEP-SEELKKELqdhvkkvtAPYKYPRIVEFVDELPKTISGKIRRVEIR 534
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
92-602 |
1.83e-31 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 128.48 E-value: 1.83e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 92 ALIFEGTDTHWTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALRHCLDT 171
Cdd:PRK08276 2 AVIMAPSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 172 SKARALIFGSEMASAICEIHASLEPTLSLFCSGSWEPSTVpvstEHLDPLLEDAPKHLPSHPDKGfTDKLfyiYTSGTTG 251
Cdd:PRK08276 82 SGAKVLIVSAALADTAAELAAELPAGVPLLLVVAGPVPGF----RSYEEALAAQPDTPIADETAG-ADML---YSSGTTG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 252 LPKA------AIVVHSRYYRMASLVYYGFRMRPDDIVYDCLPLYHSAgNIVGIGQCLLHGMTVVIRKKFSASRFWDDCIK 325
Cdd:PRK08276 154 RPKGikrplpGLDPDEAPGMMLALLGFGMYGGPDSVYLSPAPLYHTA-PLRFGMSALALGGTVVVMEKFDAEEALALIER 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 326 YNCTIVQYIGELCRYLLNQPPrEAESRHkvrmalgnglrqsiwtDFSS-RFHI-------------------PQVAEFYG 385
Cdd:PRK08276 233 YRVTHSQLVPTMFVRMLKLPE-EVRARY----------------DVSSlRVAIhaaapcpvevkramidwwgPIIHEYYA 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 386 ATECN----CSLGNFDSRVGACGfnSRILSFVypirlvrvnedtmeLIRGPDGVciPCQPGQPGQlvgrIIQQDPLRRFD 461
Cdd:PRK08276 296 SSEGGgvtvITSEDWLAHPGSVG--KAVLGEV--------------RILDEDGN--ELPPGEIGT----VYFEMDGYPFE 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 462 gYLNQGANNKKIANdvfkkgDQAYLT-GDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLHMADVAVYGve 540
Cdd:PRK08276 354 -YHNDPEKTAAARN------PHGWVTvGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFG-- 424
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 541 VPGTE-GRAGMAAV-------ASPISNCDLESFaqtLKKELPLYARPIFLRFLPELHKTGTFKFQKTELR 602
Cdd:PRK08276 425 VPDEEmGERVKAVVqpadgadAGDALAAELIAW---LRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLR 491
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
85-603 |
4.55e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 127.74 E-value: 4.55e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 85 QRHPDKTALIFE-GTdthWTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRD 163
Cdd:PRK07788 60 RRAPDRAALIDErGT---LTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGP 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 164 ALRHCLDTSKARALIFGSEMASAICEIHASLEPTLSLFCSGSWEPSTVPvSTEHLDPLLE-DAPKHLPSHPDKGFtdklF 242
Cdd:PRK07788 137 QLAEVAAREGVKALVYDDEFTDLLSALPPDLGRLRAWGGNPDDDEPSGS-TDETLDDLIAgSSTAPLPKPPKPGG----I 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 243 YIYTSGTTGLPKAAivVHSRYYRMASLVYYGFRM--RPDDIVYDCLPLYHSagniVGIGQCLL---HGMTVVIRKKFSAS 317
Cdd:PRK07788 212 VILTSGTTGTPKGA--PRPEPSPLAPLAGLLSRVpfRAGETTLLPAPMFHA----TGWAHLTLamaLGSTVVLRRRFDPE 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 318 RFWDDCIKYNCTIVQYIGELCRYLLNQPPREAE----SRHKVRMALGNGLRQSIWTDFSSRFHiPQVAEFYGATECN-CS 392
Cdd:PRK07788 286 ATLEDIAKHKATALVVVPVMLSRILDLGPEVLAkydtSSLKIIFVSGSALSPELATRALEAFG-PVLYNLYGSTEVAfAT 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 393 LGNFDSRVGACGFNSRilsfvyPIRLVRVNedtmelIRGPDGVCIPcqPGQpgqlVGRIIQQDPLrRFDGYLNQGanNKK 472
Cdd:PRK07788 365 IATPEDLAEAPGTVGR------PPKGVTVK------ILDENGNEVP--RGV----VGRIFVGNGF-PFEGYTDGR--DKQ 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 473 IANDVFKKGDQAYLtgdvlvmDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLHMADVAVYGVEVPGTEGRAGMAA 552
Cdd:PRK07788 424 IIDGLLSSGDVGYF-------DEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFV 496
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 45597453 553 VASPISNCDLESFAQTLKKELPLYARPIFLRFLPELHKTGTFKFQKTELRK 603
Cdd:PRK07788 497 VKAPGAALDEDAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELRE 547
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
111-595 |
5.69e-31 |
|
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: 126.40 E-value: 5.69e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 111 SSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKLGVEAALI----NTNLRRDALRHCLDTSKARAlifgsemasA 186
Cdd:cd05922 3 VSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRLGLVfvplNPTLKESVLRYLVADAGGRI---------V 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 187 ICEihASLEPTLSLFCSGSWEPSTVpVSTEHLDPLLEDAPKHLPSHPDKGFtdklfYIYTSGTTGLPKAAIVVHSRYYRM 266
Cdd:cd05922 74 LAD--AGAADRLRDALPASPDPGTV-LDADGIRAARASAPAHEVSHEDLAL-----LLYTSGSTGSPKLVRLSHQNLLAN 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 267 ASLVYYGFRMRPDDIVYDCLPLYHSAGNIVgIGQCLLHGMTVVIRKKFSASR-FWDDCIKYNCT---IVQYIGELCRYLl 342
Cdd:cd05922 146 ARSIAEYLGITADDRALTVLPLSYDYGLSV-LNTHLLRGATLVLTNDGVLDDaFWEDLREHGATglaGVPSTYAMLTRL- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 343 NQPPREAESRHKVRMAlGNGLRQSIWTDFSSRFHIPQVAEFYGATECncslgnfdsrvgacgfnSRILSFVYPIRLVRVN 422
Cdd:cd05922 224 GFDPAKLPSLRYLTQA-GGRLPQETIARLRELLPGAQVYVMYGQTEA-----------------TRRMTYLPPERILEKP 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 423 E-------DTMELIRGPDGVciPCQPGQPGQLVGRiiqqDPLRrFDGYLNQGANNKKIAndvfKKGDQAYlTGDVLVMDE 495
Cdd:cd05922 286 GsiglaipGGEFEILDDDGT--PTPPGEPGEIVHR----GPNV-MKGYWNDPPYRRKEG----RGGGVLH-TGDLARRDE 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 496 LGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLHMADVAVYGVEVPGTEgraGMAAVASPISNCDLESFAQTLKKELPL 575
Cdd:cd05922 354 DGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDPLGE---KLALFVTAPDKIDPKDVLRSLAERLPP 430
|
490 500
....*....|....*....|
gi 45597453 576 YARPIFLRFLPELHKTGTFK 595
Cdd:cd05922 431 YKVPATVRVVDELPLTASGK 450
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
96-602 |
5.80e-30 |
|
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: 122.93 E-value: 5.80e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 96 EGTDTHWTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALRHCLDTSKAR 175
Cdd:cd05971 1 KGTPEKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 176 ALIfgsemasaiceihasleptlslfCSGSWEPSTVpvstehldplledapkhlpshpdkgftdklfyIYTSGTTGLPKA 255
Cdd:cd05971 81 ALV-----------------------TDGSDDPALI--------------------------------IYTSGTTGPPKG 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 256 AIVVHSRYYRMASLVYYGFRM--RPDDIVYDCLPLYHSAGNIVGIGQCLLHGMTVVIRK--KFSASRFWDDCIKYNCTIV 331
Cdd:cd05971 106 ALHAHRVLLGHLPGVQFPFNLfpRDGDLYWTPADWAWIGGLLDVLLPSLYFGVPVLAHRmtKFDPKAALDLMSRYGVTTA 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 332 QYIGELCRYLLNQPPREAESRHKVRM------ALGNGLRQsiWTdfSSRFHIPqVAEFYGATECNCSLGN----FDSRVG 401
Cdd:cd05971 186 FLPPTALKMMRQQGEQLKHAQVKLRAiatggeSLGEELLG--WA--REQFGVE-VNEFYGQTECNLVIGNcsalFPIKPG 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 402 ACGFnsrilsfVYPIRLVRVNEDTMElirgpdgvciPCQPGQPGQLVgrIIQQDPLRrFDGYL-NQGANNKKIANDVFkk 480
Cdd:cd05971 261 SMGK-------PIPGHRVAIVDDNGT----------PLPPGEVGEIA--VELPDPVA-FLGYWnNPSATEKKMAGDWL-- 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 481 gdqayLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLHMADVAVYGV--EVPGT---------EGRAG 549
Cdd:cd05971 319 -----LTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIpdPIRGEivkafvvlnPGETP 393
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 45597453 550 MAAVASPISNcdlesfaqTLKKELPLYARPIFLRFLPELHKTGTFKFQKTELR 602
Cdd:cd05971 394 SDALAREIQE--------LVKTRLAAHEYPREIEFVNELPRTATGKIRRRELR 438
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
103-603 |
7.36e-29 |
|
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: 119.79 E-value: 7.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 103 TFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALRHCLDTSKARALIfgse 182
Cdd:cd05903 3 TYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFV---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 183 masaiceihasleptlslfcsgswepstVPVSTEHLDPL-LEDAPKHLpshpdkgftdklfyIYTSGTTGLPKAaiVVHS 261
Cdd:cd05903 79 ----------------------------VPERFRQFDPAaMPDAVALL--------------LFTSGTTGEPKG--VMHS 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 262 RYYRMASLVYYGFRM--RPDDIVYDCLPLYHSAGNIVGIGQCLLHGMTVVIRKKFSASRFWDDCIKYNCTIVQ----YIG 335
Cdd:cd05903 115 HNTLSASIRQYAERLglGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQDIWDPDKALALMREHGVTFMMgatpFLT 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 336 ELCRYLLNQPPREaeSRHKVRMALGNGLRQSIWTDFSSRFhIPQVAEFYGATECNCSLGNFDSrvGACGFNSRILSFVYP 415
Cdd:cd05903 195 DLLNAVEEAGEPL--SRLRTFVCGGATVPRSLARRAAELL-GAKVCSAYGSTECPGAVTSITP--APEDRRLYTDGRPLP 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 416 IRLVRVNEDtmelirgpDGVCIPcqPGQPGQLVGRIIQQdplrrFDGYLNQGANNKKIANDVFkkgdqaYLTGDVLVMDE 495
Cdd:cd05903 270 GVEIKVVDD--------TGATLA--PGVEGELLSRGPSV-----FLGYLDRPDLTADAAPEGW------FRTGDLARLDE 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 496 LGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLHMADVAVYGVEVPGTEGRAgmAAVASPISNC--DLESFAQTLKKE- 572
Cdd:cd05903 329 DGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERA--CAVVVTKSGAllTFDELVAYLDRQg 406
|
490 500 510
....*....|....*....|....*....|.
gi 45597453 573 LPLYARPIFLRFLPELHKTGTFKFQKTELRK 603
Cdd:cd05903 407 VAKQYWPERLVHVDDLPRTPSGKVQKFRLRE 437
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
76-542 |
1.66e-28 |
|
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.
Pssm-ID: 341230 [Multi-domain] Cd Length: 505 Bit Score: 119.65 E-value: 1.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 76 VPLLFASmvqRHPDKTALIFEGTDTHWTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKLGVEAAL 155
Cdd:cd05904 10 VSFLFAS---AHPSRPALIDAATGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 156 INTNLRRDALRHCLDTSKARALIFGSEMASAICEIHA-----------SLEPTLSLFCSGSWEPSTVPVSTEHLDPLLed 224
Cdd:cd05904 87 ANPLSTPAEIAKQVKDSGAKLAFTTAELAEKLASLALpvvlldsaefdSLSFSDLLFEADEAEPPVVVIKQDDVAALL-- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 225 apkhlpshpdkgftdklfyiYTSGTTGLPKAAIVVHSRYYRMASLVYYGFRMRPD-DIVYDC-LPLYHSAGnIVGIGQCL 302
Cdd:cd05904 165 --------------------YSSGTTGRSKGVMLTHRNLIAMVAQFVAGEGSNSDsEDVFLCvLPMFHIYG-LSSFALGL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 303 LH-GMTVVIRKKFSASRFWDDCIKYNCTIVQYIGELCRYLLNQPPREAESRHKVRMALGNG--LRQSIWTDFSSRFHIPQ 379
Cdd:cd05904 224 LRlGATVVVMPRFDLEELLAAIERYKVTHLPVVPPIVLALVKSPIVDKYDLSSLRQIMSGAapLGKELIEAFRAKFPNVD 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 380 VAEFYGATECNCSL------GNFDSRVGACGfnsrilsfvypiRLVR------VNEDTmelirgpdGVCIPcqPGQPGQL 447
Cdd:cd05904 304 LGQGYGMTESTGVVamcfapEKDRAKYGSVG------------RLVPnveakiVDPET--------GESLP--PNQTGEL 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 448 VGR---IIQqdplrrfdGYLNqgaNNKKIANDVFKKGdqaYL-TGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEG 523
Cdd:cd05904 362 WIRgpsIMK--------GYLN---NPEATAATIDKEG---WLhTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEA 427
|
490 500
....*....|....*....|....*..
gi 45597453 524 TLsrLLH--MADVAVYGV------EVP 542
Cdd:cd05904 428 LL--LSHpeILDAAVIPYpdeeagEVP 452
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
74-602 |
2.00e-28 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 119.88 E-value: 2.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 74 KTVPLLFASMVQRHPDKTALIFEGTDTHWTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKLGVEA 153
Cdd:PRK12583 18 QTIGDAFDATVARFPDREALVVRHQALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAIL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 154 ALINTNLRRDALRHCLDTSKARALIFGSEM-ASAICEIHASLEPTLSLFCSGSWEPSTVP-----VStehLDPlleDAPK 227
Cdd:PRK12583 98 VNINPAYRASELEYALGQSGVRWVICADAFkTSDYHAMLQELLPGLAEGQPGALACERLPelrgvVS---LAP---APPP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 228 HLPSHPD-----KGFTDK-LFYI-------------YTSGTTGLPKAAIVVHSRYYRMASLVYYGFRMRPDDIVYDCLPL 288
Cdd:PRK12583 172 GFLAWHElqargETVSREaLAERqasldrddpiniqYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCVPVPL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 289 YHSAGNIVGIGQCLLHGMTVVI-RKKFSASRFWDDCIKYNCTIVQ-----YIGElcrylLNQPPREAESRHKVRMALGNG 362
Cdd:PRK12583 252 YHCFGMVLANLGCMTVGACLVYpNEAFDPLATLQAVEEERCTALYgvptmFIAE-----LDHPQRGNFDLSSLRTGIMAG 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 363 -------LRQSIwtdfsSRFHIPQVAEFYGATECNcslgnfdsrvgacgfnsrilsfvyPIRLVRVNEDTMEL------- 428
Cdd:PRK12583 327 apcpievMRRVM-----DEMHMAEVQIAYGMTETS------------------------PVSLQTTAADDLERrvetvgr 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 429 --------IRGPDGVCIPcqPGQPGQLVGR---IIQqdplrrfdGYLNqgaNNKKIANDVFKKGdqaYL-TGDVLVMDEL 496
Cdd:PRK12583 378 tqphlevkVVDPDGATVP--RGEIGELCTRgysVMK--------GYWN---NPEATAESIDEDG---WMhTGDLATMDEQ 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 497 GYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLHMADVAVYGveVPGTE-GRAGMAAVA-SPISNCDLESFAQTLKKELP 574
Cdd:PRK12583 442 GYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFG--VPDEKyGEEIVAWVRlHPGHAASEEELREFCKARIA 519
|
570 580
....*....|....*....|....*...
gi 45597453 575 LYARPIFLRFLPELHKTGTFKFQKTELR 602
Cdd:PRK12583 520 HFKVPRYFRFVDEFPMTVTGKVQKFRMR 547
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
86-603 |
3.11e-28 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 120.06 E-value: 3.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 86 RHPDKTALIF--EGTDTH----WTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNE-FVGLWLGMAKlGVeAALINT 158
Cdd:PRK07529 37 RHPDAPALSFllDADPLDrpetWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPEtHFALWGGEAA-GI-ANPINP 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 159 NLRRDALRHCLDTSKARALI-----FGSEMASAICEIHASLEPTLSLFCSGS------WEPSTVPVSTEHLDPLLEDAPK 227
Cdd:PRK07529 115 LLEPEQIAELLRAAGAKVLVtlgpfPGTDIWQKVAEVLAALPELRTVVEVDLarylpgPKRLAVPLIRRKAHARILDFDA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 228 HLPSHP-DKGFTDKLF-------YIYTSGTTGLPKAAIVVHSRYYRMASLVYYGFRMRPDDIVYDCLPLYHSAGNIVGIG 299
Cdd:PRK07529 195 ELARQPgDRLFSGRPIgpddvaaYFHTGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPGDTVFCGLPLFHVNALLVTGL 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 300 QCLLHGMTVVI------RKKFSASRFWDDCIKYNCTIVQYIGELCRYLLNQPPrEAESRHKVRMALGNG--LRQSIWTDF 371
Cdd:PRK07529 275 APLARGAHVVLatpqgyRGPGVIANFWKIVERYRINFLSGVPTVYAALLQVPV-DGHDISSLRYALCGAapLPVEVFRRF 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 372 SSRFHIPqVAEFYGATECNC-SLGNF---DSRVGACGfnsriLSFVYP-IRLVRVNEDtmelirGPDGVciPCQPGQpgq 446
Cdd:PRK07529 354 EAATGVR-IVEGYGLTEATCvSSVNPpdgERRIGSVG-----LRLPYQrVRVVILDDA------GRYLR--DCAVDE--- 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 447 lVGRIIQQDPlRRFDGYLNqGANNKKIandvfkKGDQAYL-TGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTL 525
Cdd:PRK07529 417 -VGVLCIAGP-NVFSGYLE-AAHNKGL------WLEDGWLnTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEAL 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 526 SRLLHMADVAVYGV------EVPG--TEGRAGMAAVASpisncDLESFAQTLKKELPlyARPIFLRFLPELHKTGTFKFQ 597
Cdd:PRK07529 488 LRHPAVALAAAVGRpdahagELPVayVQLKPGASATEA-----ELLAFARDHIAERA--AVPKHVRILDALPKTAVGKIF 560
|
....*.
gi 45597453 598 KTELRK 603
Cdd:PRK07529 561 KPALRR 566
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
102-603 |
7.24e-28 |
|
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: 116.29 E-value: 7.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 102 WTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRdalrhcldtskaralifgS 181
Cdd:cd05912 2 YTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTP------------------N 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 182 EMASAICEIHASLEPTLSLfcsgswepstvpvstehldplledapkhlpshpdkgftdklfyIYTSGTTGLPKAAIVVHS 261
Cdd:cd05912 64 ELAFQLKDSDVKLDDIATI-------------------------------------------MYTSGTTGKPKGVQQTFG 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 262 RYYRMA--SLVYYGFRmrPDDIVYDCLPLYHSAGNIVgIGQCLLHGMTVVIRKKFSASRFWDDCIKYNCTIVQYIGELCR 339
Cdd:cd05912 101 NHWWSAigSALNLGLT--EDDNWLCALPLFHISGLSI-LMRSVIYGMTVYLVDKFDAEQVLHLINSGKVTIISVVPTMLQ 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 340 YLLNQPPrEAESRHKVRMALGNGLRQSIWTDFSSRFHIPqVAEFYGATEcncslgnfdsrvgACgfnSRILSFVYPIRLV 419
Cdd:cd05912 178 RLLEILG-EGYPNNLRCILLGGGPAPKPLLEQCKEKGIP-VYQSYGMTE-------------TC---SQIVTLSPEDALN 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 420 RVNEDTMELIrgpdgvciPCQ-----PGQPGQLVGRIIQQDPlRRFDGYLNQ-GANNKKIANDVFKKGDQAYLtgdvlvm 493
Cdd:cd05912 240 KIGSAGKPLF--------PVElkiedDGQPPYEVGEILLKGP-NVTKGYLNRpDATEESFENGWFKTGDIGYL------- 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 494 DELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLHMADVAVYGVEVPgTEGRAGMAAVAS--PISNCDLESFaqtLKK 571
Cdd:cd05912 304 DEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDD-KWGQVPVAFVVSerPISEEELIAY---CSE 379
|
490 500 510
....*....|....*....|....*....|..
gi 45597453 572 ELPLYARPIFLRFLPELHKTGTFKFQKTELRK 603
Cdd:cd05912 380 KLAKYKVPKKIYFVDELPRTASGKLLRHELKQ 411
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
87-601 |
1.29e-27 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 116.88 E-value: 1.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 87 HPDKTALIfeGTDTHWTFRQLDEYSSSVANFLQAR-GLASGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRDAL 165
Cdd:PRK06839 15 HPDRIAII--TEEEEMTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENEL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 166 RHCLDTSKARALIFGSEMASAICEIH--ASLEPtlslfcsgswepstvPVSTEHLDPLLEDAPKHLPshpDKGFTDKLFY 243
Cdd:PRK06839 93 IFQLKDSGTTVLFVEKTFQNMALSMQkvSYVQR---------------VISITSLKEIEDRKIDNFV---EKNESASFII 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 244 IYTSGTTGLPKAAIVVHSRYYRMASLVYYGFRMRPDDIVYDCLPLYHsagnIVGIG----QCLLHGMTVVIRKKFSASRF 319
Cdd:PRK06839 155 CYTSGTTGKPKGAVLTQENMFWNALNNTFAIDLTMHDRSIVLLPLFH----IGGIGlfafPTLFAGGVIIVPRKFEPTKA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 320 WDDCIKYNCTIVQYIGELCRYLLNQPPREAESRHKVRMALGNG--LRQSIWTDFSSRFHipQVAEFYGATECNCSL---- 393
Cdd:PRK06839 231 LSMIEKHKVTVVMGVPTIHQALINCSKFETTNLQSVRWFYNGGapCPEELMREFIDRGF--LFGQGFGMTETSPTVfmls 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 394 -GNFDSRVGACGfnsrilsfvYPIRLVRVnedtmELIrGPDGVCIPcqPGQpgqlVGRIIQQDPlRRFDGYLNqgaNNKK 472
Cdd:PRK06839 309 eEDARRKVGSIG---------KPVLFCDY-----ELI-DENKNKVE--VGE----VGELLIRGP-NVMKEYWN---RPDA 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 473 IANDVfkkGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLHMADVAVYGVEVPGTEGRAGMAA 552
Cdd:PRK06839 364 TEETI---QDGWLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFI 440
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 45597453 553 VASPISNCDLESFAQTLKKELPLYARPIFLRFLPELHKTGTFKFQKTEL 601
Cdd:PRK06839 441 VKKSSSVLIEKDVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQL 489
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
79-539 |
6.52e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 115.08 E-value: 6.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 79 LFASMVQRHPDKTALIFegTDTHWTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEfvgLWLGMAklgveAALInT 158
Cdd:PRK06188 17 LLVSALKRYPDRPALVL--GDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPE---VLMAIG-----AAQL-A 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 159 NLRRDAL---------RHCLDTSKARALIFGS----EMASAICEIHASLEPTLSLfcsgswepSTVPVSTEHLDPLLEDA 225
Cdd:PRK06188 86 GLRRTALhplgslddhAYVLEDAGISTLIVDPapfvERALALLARVPSLKHVLTL--------GPVPDGVDLLAAAAKFG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 226 PKHLpsHPDKGFTDKLFYIYTSGTTGLPKAAIVVHSRYYRMASLVYYGFRMrPDDIVY-DCLPLYHSAGNIVGIGqcLLH 304
Cdd:PRK06188 158 PAPL--VAAALPPDIAGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEW-PADPRFlMCTPLSHAGGAFFLPT--LLR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 305 GMTVVIRKKFSASRFWDDCIKYNCTIVQYIGELCRYLLNQPPREAESRHKVRMALGNG-------LRQSIwtdfsSRFHi 377
Cdd:PRK06188 233 GGTVIVLAKFDPAEVLRAIEEQRITATFLVPTMIYALLDHPDLRTRDLSSLETVYYGAspmspvrLAEAI-----ERFG- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 378 PQVAEFYGATECN---CSLGNFD------SRVGACGFnsrilsfvyPIRLVRVNedtmelIRGPDGVCIPcqPGQPGQLV 448
Cdd:PRK06188 307 PIFAQYYGQTEAPmviTYLRKRDhdpddpKRLTSCGR---------PTPGLRVA------LLDEDGREVA--QGEVGEIC 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 449 GRiiqqDPLrRFDGYLNQGANNKKiandVFKKGdqaYL-TGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSR 527
Cdd:PRK06188 370 VR----GPL-VMDGYWNRPEETAE----AFRDG---WLhTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAE 437
|
490
....*....|..
gi 45597453 528 LLHMADVAVYGV 539
Cdd:PRK06188 438 HPAVAQVAVIGV 449
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
71-602 |
1.13e-26 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 114.47 E-value: 1.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 71 QERKTVPLLFASMVQRHPDKTALIFE-GTdthWTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKL 149
Cdd:PRK13382 40 REGMGPTSGFAIAAQRCPDRPGLIDElGT---LTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 150 GVEAALINTNLRRDALRHCLDTSKARALIFGSEMASAICEIHASL-EPTLSLFCSGSWEPSTVPV-STEHldplLEDAPk 227
Cdd:PRK13382 117 GADILLLNTSFAGPALAEVVTREGVDTVIYDEEFSATVDRALADCpQATRIVAWTDEDHDLTVEVlIAAH----AGQRP- 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 228 hlPSHPDKGFTdklfYIYTSGTTGLPKAAIVVHSRYYRMASLVYYGFRMRPDDIVYDCLPLYHSAgnivGIGQCLLHGM- 306
Cdd:PRK13382 192 --EPTGRKGRV----ILLTSGTTGTPKGARRSGPGGIGTLKAILDRTPWRAEEPTVIVAPMFHAW----GFSQLVLAASl 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 307 --TVVIRKKFSASRFWDDCIKYNCTIVQYIGELCRYLLNQPPrEAESRHKVR-----MALGNGLRQSIWTDFSSRFHiPQ 379
Cdd:PRK13382 262 acTIVTRRRFDPEATLDLIDRHRATGLAVVPVMFDRIMDLPA-EVRNRYSGRslrfaAASGSRMRPDVVIAFMDQFG-DV 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 380 VAEFYGATEcncslgnfdsrVGacgfnsrILSFVYPIRLvRVNEDTMEliRGPDGVCI--------PCQPGQpgqlVGRI 451
Cdd:PRK13382 340 IYNNYNATE-----------AG-------MIATATPADL-RAAPDTAG--RPAEGTEIrildqdfrEVPTGE----VGTI 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 452 -IQQDPLrrFDGYlNQGANNKkiandvFKKGDQAylTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLH 530
Cdd:PRK13382 395 fVRNDTQ--FDGY-TSGSTKD------FHDGFMA--SGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPD 463
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45597453 531 MADVAVYGVEVPGTEGRAGMAAVASPISNCDLESFAQTLKKELPLYARPIFLRFLPELHKTGTFKFQKTELR 602
Cdd:PRK13382 464 VAEAAVIGVDDEQYGQRLAAFVVLKPGASATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQ 535
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
85-604 |
2.66e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 113.06 E-value: 2.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 85 QRHPDKTALIFEGTDThwTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRDA 164
Cdd:PRK06145 13 RRTPDRAALVYRDQEI--SYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 165 LRHCLDTSKARALIFGSEMasaicEIHASLEPTLSLFCSGSWEPSTVPVStehldPLLEDAPKHlPSHPDkgftDKLFYI 244
Cdd:PRK06145 91 VAYILGDAGAKLLLVDEEF-----DAIVALETPKIVIDAAAQADSRRLAQ-----GGLEIPPQA-AVAPT----DLVRLM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 245 YTSGTTGLPKAAIVVHSRYYRMASLVYYGFRMRPDDIVYDCLPLYH-SAGNIVGIGqCLLHGMTVVIRKKFSASRFWDDC 323
Cdd:PRK06145 156 YTSGTTDRPKGVMHSYGNLHWKSIDHVIALGLTASERLLVVGPLYHvGAFDLPGIA-VLWVGGTLRIHREFDPEAVLAAI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 324 IKYNCTIVQYIGELCRYLLNQPPREAESRHKVRMALGNGLR--QSIWTDFSSRFHIPQVAEFYGATEcNCS------LGN 395
Cdd:PRK06145 235 ERHRLTCAWMAPVMLSRVLTVPDRDRFDLDSLAWCIGGGEKtpESRIRDFTRVFTRARYIDAYGLTE-TCSgdtlmeAGR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 396 FDSRVGACGfnsRILSFVyPIRlvrvnedtmelIRGPDGVCIPcqPGQPGQ--LVGRIIQQdplrrfdGYLNqgaNNKKI 473
Cdd:PRK06145 314 EIEKIGSTG---RALAHV-EIR-----------IADGAGRWLP--PNMKGEicMRGPKVTK-------GYWK---DPEKT 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 474 ANDVFkkgDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLHMADVAVYGVEVPGTEGRAGMAAV 553
Cdd:PRK06145 367 AEAFY---GDWFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVV 443
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 45597453 554 ASPISNCDLESFAQTLKKELPLYARPIFLRFLPELHKTGTFKFQKTELRKE 604
Cdd:PRK06145 444 LNPGATLTLEALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVLRDE 494
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
57-604 |
1.05e-25 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 111.76 E-value: 1.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 57 MVLLKVKTKVRRYLQER-----KTVPLLFASMVQRHPDKTALIfEGTDTHWTFRQLDEYSSSVANFLQARGLASGNVVAL 131
Cdd:PRK06087 1 KVTLTFNEQRRAAYRQQgywgdASLADYWQQTARAMPDKIAVV-DNHGASYTYSALDHAASRLANWLLAKGIEPGDRVAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 132 FMENRNEFVGLWLGMAKLGVEAALINTNLRRDALRHCLDTSKARALifgsemasaICeihaslePTlsLFCSGSWEPSTV 211
Cdd:PRK06087 80 QLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMF---------FA-------PT--LFKQTRPVDLIL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 212 PVSTE--HLDPLL---EDAPKHLP-------------SHPDKGFTDKLFYI-YTSGTTGLPKAAIVVHSRYyrMASLVYY 272
Cdd:PRK06087 142 PLQNQlpQLQQIVgvdKLAPATSSlslsqiiadyeplTTAITTHGDELAAVlFTSGTEGLPKGVMLTHNNI--LASERAY 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 273 --GFRMRPDDIVYDCLPLYHSAGNIVGIGQCLLHGMTVVIRKKFSAsrfwDDCI----KYNCTIVQ----YIGELCRYLL 342
Cdd:PRK06087 220 caRLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVLLDIFTP----DACLalleQQRCTCMLgatpFIYDLLNLLE 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 343 NQPPREAesrhKVRMALGNG------LRQSIWtdfssRFHIpQVAEFYGATE-CNCSLGNFD---SRVGAcgFNSRILSF 412
Cdd:PRK06087 296 KQPADLS----ALRFFLCGGttipkkVARECQ-----QRGI-KLLSVYGSTEsSPHAVVNLDdplSRFMH--TDGYAAAG 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 413 VyPIRLVRVNEDTmelirgpdgvcIPCqpGQPGQLVGRIIQQdplrrFDGYLNQGANNKKIANDvfkkgDQAYLTGDVLV 492
Cdd:PRK06087 364 V-EIKVVDEARKT-----------LPP--GCEGEEASRGPNV-----FMGYLDEPELTARALDE-----EGWYYSGDLCR 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 493 MDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLHMADVAVYGVevpgTEGRAG--MAAVASPISNCDLESFAQTL- 569
Cdd:PRK06087 420 MDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAM----PDERLGerSCAYVVLKAPHHSLTLEEVVa 495
|
570 580 590
....*....|....*....|....*....|....*...
gi 45597453 570 ---KKELPLYARPIFLRFLPELHKTGTFKFQKTELRKE 604
Cdd:PRK06087 496 ffsRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRKD 533
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
85-604 |
3.19e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 110.13 E-value: 3.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 85 QRHPDKTALIFEGTDThwTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRDA 164
Cdd:PRK06178 44 RERPQRPAIIFYGHVI--TYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 165 LRHCLDTSKARALIFG---SEMASAICE-------IHASL------EPTLSLFCSGSwEPSTVPVSTEHLDPLLEDAPKH 228
Cdd:PRK06178 122 LSYELNDAGAEVLLALdqlAPVVEQVRAetslrhvIVTSLadvlpaEPTLPLPDSLR-APRLAAAGAIDLLPALRACTAP 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 229 LPSHPdkGFTDKLFYI-YTSGTTGLPKAaiVVHSR---YYRMASLVYYGFRMRPDDIVYDCLPLYHSAGNIVGIGQCLLH 304
Cdd:PRK06178 201 VPLPP--PALDALAALnYTGGTTGMPKG--CEHTQrdmVYTAAAAYAVAVVGGEDSVFLSFLPEFWIAGENFGLLFPLFS 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 305 GMTVVIRKKFSASRFWDDCIKYNCTIVQYIGELCRYLLNQP---PREAESRHKVRMA-----LGNGLRQSiWTDFSSRFh 376
Cdd:PRK06178 277 GATLVLLARWDAVAFMAAVERYRVTRTVMLVDNAVELMDHPrfaEYDLSSLRQVRVVsfvkkLNPDYRQR-WRALTGSV- 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 377 ipqVAEF-YGATECNCSlgnfDSRvgACGFnsrilsfvypirlvrvNEDTMELIRGPDGVCIPCqPG--------QPGQL 447
Cdd:PRK06178 355 ---LAEAaWGMTETHTC----DTF--TAGF----------------QDDDFDLLSQPVFVGLPV-PGtefkicdfETGEL 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 448 V-----GRIIQQDPlRRFDGYLNQGANNKkianDVFKKGdqAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVE 522
Cdd:PRK06178 409 LplgaeGEIVVRTP-SLLKGYWNKPEATA----EALRDG--WLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVE 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 523 GTLSRllHmADVAVYGVeVPGTEGRAGMAAVA----SPISNCDLESFAQTLKKELPLYARPIfLRFLPELHKTGTFKFQK 598
Cdd:PRK06178 482 ALLGQ--H-PAVLGSAV-VGRPDPDKGQVPVAfvqlKPGADLTAAALQAWCRENMAVYKVPE-IRIVDALPMTATGKVRK 556
|
....*.
gi 45597453 599 TELRKE 604
Cdd:PRK06178 557 QDLQAL 562
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
88-588 |
3.53e-25 |
|
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: 108.77 E-value: 3.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 88 PDKTALIFEgtDTHWTFRQLDEYSSSVANFLQARGLASGNVVALFMEnRNE--FVGLwLGMAKLGveAALIntnlrrdal 165
Cdd:cd05930 1 PDAVAVVDG--DQSLTYAELDARANRLARYLRERGVGPGDLVAVLLE-RSLemVVAI-LAVLKAG--AAYV--------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 166 rhcldtskaralifgsemasaiceihaSLEPTLslfcsgswePStvpvstEHLDPLLEDA-PKHLPSHPDKgftdkLFY- 243
Cdd:cd05930 66 ---------------------------PLDPSY---------PA------ERLAYILEDSgAKLVLTDPDD-----LAYv 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 244 IYTSGTTGLPKAAIVVHsryyrmASLVYY--GFRMRPDDIVYDCLPLYHSAGNIVGIGQ---CLLHGMTVVIRKK---FS 315
Cdd:cd05930 99 IYTSGSTGKPKGVMVEH------RGLVNLllWMQEAYPLTPGDRVLQFTSFSFDVSVWEifgALLAGATLVVLPEevrKD 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 316 ASRFWDDCIKYNCTIVQYIGELCRYLLNQPPREAesRHKVRMAL--GNGLRQSIWTDFSSRFHIPQVAEFYGATEC--NC 391
Cdd:cd05930 173 PEALADLLAEEGITVLHLTPSLLRLLLQELELAA--LPSLRLVLvgGEALPPDLVRRWRELLPGARLVNLYGPTEAtvDA 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 392 SLGnfdsRVGACGFNSRILSFVYPIRLVRVnedtmeLIRGPDGvcIPCQPGQPGQL------VGRiiqqdplrrfdGYLN 465
Cdd:cd05930 251 TYY----RVPPDDEEDGRVPIGRPIPNTRV------YVLDENL--RPVPPGVPGELyiggagLAR-----------GYLN 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 466 Q-GANNKKIANDVFKKGDQAYLTGDVLVMDELGYLYFRDRTgDT------FRwkgenVSTTEVEGTLSRLLHMADVAVyg 538
Cdd:cd05930 308 RpELTAERFVPNPFGPGERMYRTGDLVRWLPDGNLEFLGRI-DDqvkirgYR-----IELGEIEAALLAHPGVREAAV-- 379
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 45597453 539 VEVPGTEGRAGMAA--VASPISNCDLESFAQTLKKELPLYARPIFLRFLPEL 588
Cdd:cd05930 380 VAREDGDGEKRLVAyvVPDEGGELDEEELRAHLAERLPDYMVPSAFVVLDAL 431
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
103-601 |
3.61e-25 |
|
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: 108.69 E-value: 3.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 103 TFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLrrdalrhcldTSKARALIFG-S 181
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRL----------TENERTNQLEdL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 182 EMASAICEIHASLEPTLSLFCSGSWEPSTVPVSTEHLDPLleDAPKHLpshpdkgftdklfyIYTSGTTGLPKAAIVVHS 261
Cdd:TIGR01923 71 DVQLLLTDSLLEEKDFQADSLDRIEAAGRYETSLSASFNM--DQIATL--------------MFTSGTTGKPKAVPHTFR 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 262 RYYR--MASLVYYGFRmrPDDIVYDCLPLYHSAGNIVgIGQCLLHGMTVVIRKKFSAsrFWDDCIKYNCTIVQYIGELCR 339
Cdd:TIGR01923 135 NHYAsaVGSKENLGFT--EDDNWLLSLPLYHISGLSI-LFRWLIEGATLRIVDKFNQ--LLEMIANERVTHISLVPTQLN 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 340 YLLNQPPREAESRhkvRMALGNGlrqsiwtdfssrfHIPQ------------VAEFYGATEcncslgnfdsrvgACgfnS 407
Cdd:TIGR01923 210 RLLDEGGHNENLR---KILLGGS-------------AIPAplieeaqqyglpIYLSYGMTE-------------TC---S 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 408 RILSFVypirlvrvNEDTMEliRGPDGVCIP------CQPGQPGqlVGRIIQQDPLRrFDGYLNQG-ANNKKIANDVFKK 480
Cdd:TIGR01923 258 QVTTAT--------PEMLHA--RPDVGRPLAgreikiKVDNKEG--HGEIMVKGANL-MKGYLYQGeLTPAFEQQGWFNT 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 481 GDQAYLTGDvlvmdelGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLHMADVAVygveVPGTEGRAGMAAVA-----S 555
Cdd:TIGR01923 325 GDIGELDGE-------GFLYVLGRRDDLIISGGENIYPEEIETVLYQHPGIQEAVV----VPKPDAEWGQVPVAyivseS 393
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 45597453 556 PISNCDLESFaqtLKKELPLYARPIFLRFLPELHKTGTFKFQKTEL 601
Cdd:TIGR01923 394 DISQAKLIAY---LTEKLAKYKVPIAFEKLDELPYNASGKILRNQL 436
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
79-602 |
3.75e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 109.83 E-value: 3.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 79 LFASMVQRHPDKTALIFEGTDThwTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKLGVEAALINT 158
Cdd:PRK06164 15 LLDAHARARPDAVALIDEDRPL--SRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 159 NLRRDALRHCLDTSKARALIF-----GSEMASAICEIHASLEPTL---SLFCSGSWE-PSTVPVSTeHLDPLLEDAPKHL 229
Cdd:PRK06164 93 RYRSHEVAHILGRGRARWLVVwpgfkGIDFAAILAAVPPDALPPLraiAVVDDAADAtPAPAPGAR-VQLFALPDPAPPA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 230 PSHPDKGFTDKLFYIY-TSGTTGLPKaaIVVHsryyRMASLVYYGFR------MRPDDIVYDCLPLYHSAGnIVGIGQCL 302
Cdd:PRK06164 172 AAGERAADPDAGALLFtTSGTTSGPK--LVLH----RQATLLRHARAiaraygYDPGAVLLAALPFCGVFG-FSTLLGAL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 303 LHGMTVVIRKKFSASRFWDDCIKYNCTIVQYIGELCRYLLNQPPREAESRHkvrmalgngLRQSIWTDFSSRFH-IPQVA 381
Cdd:PRK06164 245 AGGAPLVCEPVFDAARTARALRRHRVTHTFGNDEMLRRILDTAGERADFPS---------ARLFGFASFAPALGeLAALA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 382 E--------FYGATECNC--SLGNFDSRVGAcgfnsRILS---FVYPIRLVRvnedtmelIRGPDGVCIpCQPGQPGQlv 448
Cdd:PRK06164 316 RargvpltgLYGSSEVQAlvALQPATDPVSV-----RIEGggrPASPEARVR--------ARDPQDGAL-LPDGESGE-- 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 449 griIQQDPLRRFDGYL-NQGANNKKIAND-VFKKGDQAYLTGDvlvmdelGYLYFRDRTGDTFRWKGENVSTTEVEGTLS 526
Cdd:PRK06164 380 ---IEIRAPSLMRGYLdNPDATARALTDDgYFRTGDLGYTRGD-------GQFVYQTRMGDSLRLGGFLVNPAEIEHALE 449
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45597453 527 RLLHMADVAVYGVEVPGtEGRAGMAAVASPISNCDLESFAQTLKKELPLY---ARPIFLRFLPELHKTGTFKFQKTELR 602
Cdd:PRK06164 450 ALPGVAAAQVVGATRDG-KTVPVAFVIPTDGASPDEAGLMAACREALAGFkvpARVQVVEAFPVTESANGAKIQKHRLR 527
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
85-604 |
1.52e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 107.82 E-value: 1.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 85 QRHPDKTALIfEGtDTHWTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNE-FVGLWlgmAKLGVEAALINTNLRR- 162
Cdd:PRK07470 18 RRFPDRIALV-WG-DRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQmFESMF---AAFRLGAVWVPTNFRQt 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 163 -DALRHCLDTSKARALIFGS---EMASAICEIHASLEPTLSLfCSGSWEPSTVPVSTEHLDPLLEDApkhlpshpDKGFT 238
Cdd:PRK07470 93 pDEVAYLAEASGARAMICHAdfpEHAAAVRAASPDLTHVVAI-GGARAGLDYEALVARHLGARVANA--------AVDHD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 239 DKLFYIYTSGTTGLPKAAIVVHSRYY-----RMASLVyygfrmrPDDIVYDC----LPLYHSAGnivgigqclLHGMTVV 309
Cdd:PRK07470 164 DPCWFFFTSGTTGRPKAAVLTHGQMAfvitnHLADLM-------PGTTEQDAslvvAPLSHGAG---------IHQLCQV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 310 IR---------KKFSASRFWDDCIKYNC-------TIVQYIGE----------LCRYLLNQ-PPREAESRHKVRMALGNG 362
Cdd:PRK07470 228 ARgaatvllpsERFDPAEVWALVERHRVtnlftvpTILKMLVEhpavdrydhsSLRYVIYAgAPMYRADQKRALAKLGKV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 363 LRQsiwtdfssrfhipqvaeFYGATECNcslGNF--------------DSRVGACGFnsrilsfvypirlvrvnEDT-ME 427
Cdd:PRK07470 308 LVQ-----------------YFGLGEVT---GNItvlppalhdaedgpDARIGTCGF-----------------ERTgME 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 428 L-IRGPDGvcipcQPGQPGQlVGRIIQQDPlRRFDGYL-NQGANNKKIANDVFKkgdqaylTGDVLVMDELGYLYFRDRT 505
Cdd:PRK07470 351 VqIQDDEG-----RELPPGE-TGEICVIGP-AVFAGYYnNPEANAKAFRDGWFR-------TGDLGHLDARGFLYITGRA 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 506 GDTFRWKGENVSTTEVEGTLsrLLH--MADVAVYGVEVPgTEGRAGMAA-VASPISNCDLESFAQTLKKELPLYARPIFL 582
Cdd:PRK07470 417 SDMYISGGSNVYPREIEEKL--LTHpaVSEVAVLGVPDP-VWGEVGVAVcVARDGAPVDEAELLAWLDGKVARYKLPKRF 493
|
570 580
....*....|....*....|..
gi 45597453 583 RFLPELHKTGTFKFQKTELRKE 604
Cdd:PRK07470 494 FFWDALPKSGYGKITKKMVREE 515
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
74-604 |
2.98e-24 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 107.06 E-value: 2.98e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 74 KTVPLLFASMVQRHPDKTALI----FEGTDTHWTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKL 149
Cdd:PRK13295 24 RTINDDLDACVASCPDKTAVTavrlGTGAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 150 GVEAALINTNLRRDALRHCLDTSKARALIF-----GSEMASAICEIHASLePTLS---------------LFCSGSWEps 209
Cdd:PRK13295 104 GAVLNPLMPIFRERELSFMLKHAESKVLVVpktfrGFDHAAMARRLRPEL-PALRhvvvvggdgadsfeaLLITPAWE-- 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 210 tvpvstehLDPlleDAPKHLPSH---PDkgftDKLFYIYTSGTTGLPKAaiVVHSRYYRMASLVYYGFRMR--PDDIVYD 284
Cdd:PRK13295 181 --------QEP---DAPAILARLrpgPD----DVTQLIYTSGTTGEPKG--VMHTANTLMANIVPYAERLGlgADDVILM 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 285 CLPLYHSAGNIVGIGQCLLHGMTVVIRKKFSASRFWD----DCIKYNCTIVQYIGELCRYLlnqppreAESRHKV---RM 357
Cdd:PRK13295 244 ASPMAHQTGFMYGLMMPVMLGATAVLQDIWDPARAAElirtEGVTFTMASTPFLTDLTRAV-------KESGRPVsslRT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 358 ALGNG------LRQSIWTDFSSRfhipqVAEFYGATECNC----SLGNFDSRVGAcgfnsrilSFVYPIRLVRVNedtme 427
Cdd:PRK13295 317 FLCAGapipgaLVERARAALGAK-----IVSAWGMTENGAvtltKLDDPDERAST--------TDGCPLPGVEVR----- 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 428 lIRGPDGVCIPcqPGQPGQLVGRiiqqdPLRRFDGYLNQGANNKKIANDVFKKGDQAYLTGDvlvmdelGYLYFRDRTGD 507
Cdd:PRK13295 379 -VVDADGAPLP--AGQIGRLQVR-----GCSNFGGYLKRPQLNGTDADGWFDTGDLARIDAD-------GYIRISGRSKD 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 508 TFRWKGENVSTTEVEGTLSRLLHMADVAVYGVEVPGTEGRAGMAAVASPISNCDLESFAQTLK-KELPLYARPIFLRFLP 586
Cdd:PRK13295 444 VIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPRPGQSLDFEEMVEFLKaQKVAKQYIPERLVVRD 523
|
570
....*....|....*...
gi 45597453 587 ELHKTGTFKFQKTELRKE 604
Cdd:PRK13295 524 ALPRTPSGKIQKFRLREM 541
|
|
| PRK07868 |
PRK07868 |
acyl-CoA synthetase; Validated |
79-639 |
3.21e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236121 [Multi-domain] Cd Length: 994 Bit Score: 108.27 E-value: 3.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 79 LFASMVQRHPDKTALIFEGTdTHwTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKLGVEAALint 158
Cdd:PRK07868 452 IIAEQARDAPKGEFLLFDGR-VH-TYEAVNRRINNVVRGLIAVGVRQGDRVGVLMETRPSALVAIAALSRLGAVAVL--- 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 159 nLRRDAlrhclDTSKARALIFGSEMASAICEIHASLEPTLSLFCSGSWEPSTVPVST-------EHLDPlleDAPKhLPS 231
Cdd:PRK07868 527 -MPPDT-----DLAAAVRLGGVTEIITDPTNLEAARQLPGRVLVLGGGESRDLDLPDdadvidmEKIDP---DAVE-LPG 596
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 232 --HPDKGFTDKLFYIYTSGTTGLPKAAIVVHSRYYRMASLVYYGFRMRPDDIVYDCLPLYHSAGNIVGIGQCLLHGMTVV 309
Cdd:PRK07868 597 wyRPNPGLARDLAFIAFSTAGGELVAKQITNYRWALSAFGTASAAALDRRDTVYCLTPLHHESGLLVSLGGAVVGGSRIA 676
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 310 IRKKFSASRFWDDCIKYNCTIVQYIGELCRYLLNQPPREAESRHKVRMALGNGLRQSIWTDFSSRFHIPQVAEFYGATEC 389
Cdd:PRK07868 677 LSRGLDPDRFVQEVRQYGVTVVSYTWAMLREVVDDPAFVLHGNHPVRLFIGSGMPTGLWERVVEAFAPAHVVEFFATTDG 756
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 390 NCSLGNFD-SRVGACGfnsRILSFVYPIRLVRVNEDTMELIRGPDGVCIPCQPGQPGQLVGRIiqqdplrrfDGYLNQGA 468
Cdd:PRK07868 757 QAVLANVSgAKIGSKG---RPLPGAGRVELAAYDPEHDLILEDDRGFVRRAEVNEVGVLLARA---------RGPIDPTA 824
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 469 NNKKianDVFKKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLHMADVAVYGVEVPGTEgrA 548
Cdd:PRK07868 825 SVKR---GVFAPADTWISTEYLFRRDDDGDYWLVDRRGSVIRTARGPVYTEPVTDALGRIGGVDLAVTYGVEVGGRQ--L 899
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 549 GMAAVA----SPISNCDL-ESFAqtlkkELPLYARPIFLRFLPELHKTGTFKFQKTELRKEGFdPSVVKDpLFYLDARKG 623
Cdd:PRK07868 900 AVAAVTlrpgAAITAADLtEALA-----SLPVGLGPDIVHVVPEIPLSATYRPTVSALRAAGI-PKPGRQ-AWYFDPETN 972
|
570
....*....|....*.
gi 45597453 624 CYVALDQEAYTRIQAG 639
Cdd:PRK07868 973 RYRRLTPAVRAELTGG 988
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
103-603 |
8.14e-24 |
|
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: 104.52 E-value: 8.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 103 TFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALRHCLDTSKARALIFGSE 182
Cdd:cd05973 2 TFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTDAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 183 MASAICEihasleptlslfcsgswepstvpvstehlDPLLEdapkhlpshpdkgftdklfyIYTSGTTGLPKAAIVVHSR 262
Cdd:cd05973 82 NRHKLDS-----------------------------DPFVM--------------------MFTSGTTGLPKGVPVPLRA 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 263 YYRMASLVYYGFRMRPDDIVYD------CLPLYHS--AGNIVGIGQCLLHGmtvvirkKFSASRFWDDCIKYNCTIVQYI 334
Cdd:cd05973 113 LAAFGAYLRDAVDLRPEDSFWNaadpgwAYGLYYAitGPLALGHPTILLEG-------GFSVESTWRVIERLGVTNLAGS 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 335 GELCRYLLNQPPrEAESRHKVRM----ALGNGLRQSIWTDFSSRFHIPqVAEFYGATECNCSLGNFDS-----RVGACGf 405
Cdd:cd05973 186 PTAYRLLMAAGA-EVPARPKGRLrrvsSAGEPLTPEVIRWFDAALGVP-IHDHYGQTELGMVLANHHAlehpvHAGSAG- 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 406 nsrilsFVYP-IRLVRVNEDTMELIrgpdgvcipcqPGQPGQLVgrI-IQQDPLRRFDGYlnQGANNKKIANDVfkkgdq 483
Cdd:cd05973 263 ------RAMPgWRVAVLDDDGDELG-----------PGEPGRLA--IdIANSPLMWFRGY--QLPDTPAIDGGY------ 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 484 aYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLHMADVAVYGV------EV--------PGTEGRAG 549
Cdd:cd05973 316 -YLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVpdpertEVvkafvvlrGGHEGTPA 394
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 45597453 550 MAavaspisncdlESFAQTLKKELPLYARPIFLRFLPELHKTGTFKFQKTELRK 603
Cdd:cd05973 395 LA-----------DELQLHVKKRLSAHAYPRTIHFVDELPKTPSGKIQRFLLRR 437
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
86-602 |
1.01e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 104.89 E-value: 1.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 86 RHPDKTALIFEGTDTHWTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRDAL 165
Cdd:PRK09088 7 LQPQRLAAVDLALGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASEL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 166 RHCLDTSKARALIFGSEMASAICEIHASLEPTLSLFCSGswepstvPVSTEHLDPlleDAPKhlpshpdkgftdklFYIY 245
Cdd:PRK09088 87 DALLQDAEPRLLLGDDAVAAGRTDVEDLAAFIASADALE-------PADTPSIPP---ERVS--------------LILF 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 246 TSGTTGLPKAAIVVHSRYYRMAslVYYGFRMRPD-DIVYDC-LPLYHSAGNIVGIGQCLLHGMTVVIRKKFSASRFWDDC 323
Cdd:PRK09088 143 TSGTSGQPKGVMLSERNLQQTA--HNFGVLGRVDaHSSFLCdAPMFHIIGLITSVRPVLAVGGSILVSNGFEPKRTLGRL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 324 IKYNCTIVQYIG--ELCRYLLNQPPREAES-RHKVRMALGNGLRQSI----WTDFSsrfhIPqVAEFYGATECNCSLGN- 395
Cdd:PRK09088 221 GDPALGITHYFCvpQMAQAFRAQPGFDAAAlRHLTALFTGGAPHAAEdilgWLDDG----IP-MVDGFGMSEAGTVFGMs 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 396 -----FDSRVGACGFNSrilsfvyPIRLVRVNEDtmeliRGPDgvcipCQPGQPGQLvgrIIQQDPLrrFDGYLNQGANN 470
Cdd:PRK09088 296 vdcdvIRAKAGAAGIPT-------PTVQTRVVDD-----QGND-----CPAGVPGEL---LLRGPNL--SPGYWRRPQAT 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 471 KkianDVFKkGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLHMADVAVYGVEVP--GTEGRA 548
Cdd:PRK09088 354 A----RAFT-GDGWFRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAqwGEVGYL 428
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 45597453 549 gmAAVASPISNCDLESFAQTLKKELPLYARPIFLRFLPELHKTGTFKFQKTELR 602
Cdd:PRK09088 429 --AIVPADGAPLDLERIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARLR 480
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
80-579 |
2.07e-23 |
|
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: 103.96 E-value: 2.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 80 FASMVQRHPDKTALIFEGTdtHWTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKLGVEAALINTN 159
Cdd:cd17651 1 FERQAARTPDAPALVAEGR--RLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 160 LRRDALRHCLDTSKARALIfgsemasaiceIHASLEPTLSLfcsgswEPSTVPVSTEHLDPLLEDAPKHLPSHPDkgftD 239
Cdd:cd17651 79 YPAERLAFMLADAGPVLVL-----------THPALAGELAV------ELVAVTLLDQPGAAAGADAEPDPALDAD----D 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 240 KLFYIYTSGTTGLPKAAIVVHSryyRMASLVYYGFRmrpddiVYDCLPLYHSAgNIVGIG---------QCLLHGMTVVI 310
Cdd:cd17651 138 LAYVIYTSGSTGRPKGVVMPHR---SLANLVAWQAR------ASSLGPGARTL-QFAGLGfdvsvqeifSTLCAGATLVL 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 311 RK---KFSASRFWDDCIKYNCTIV----QYIGELCRYLLNQPPREAESRHKV----RMALGNGLRQsiwtdFSSRFHIPQ 379
Cdd:cd17651 208 PPeevRTDPPALAAWLDEQRISRVflptVALRALAEHGRPLGVRLAALRYLLtggeQLVLTEDLRE-----FCAGLPGLR 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 380 VAEFYGATECN-CSLGNFDSRVGACGfnsRILSFVYPIRLVRVnedtmeliRGPDGVCIPCQPGQPGQLvgrIIQQDPLR 458
Cdd:cd17651 283 LHNHYGPTETHvVTALSLPGDPAAWP---APPPIGRPIDNTRV--------YVLDAALRPVPPGVPGEL---YIGGAGLA 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 459 RfdGYLNQ-GANNKKIANDVFKKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLHMADVAVY 537
Cdd:cd17651 349 R--GYLNRpELTAERFVPDPFVPGARMYRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVL 426
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 45597453 538 GVEVPGTEGRAGMAAVASPISNCDLESFAQTLKKELPLYARP 579
Cdd:cd17651 427 AREDRPGEKRLVAYVVGDPEAPVDAAELRAALATHLPEYMVP 468
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
99-602 |
3.97e-23 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 103.24 E-value: 3.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 99 DTHWTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALRHCLDTSKARALI 178
Cdd:PRK12406 9 DRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 179 FGSEMASAICEIhasLEPTLSLFCSG-----------SWEPSTVPVSTEHLDPLLED-APKHLPSHPDKGFTdklfyIYT 246
Cdd:PRK12406 89 AHADLLHGLASA---LPAGVTVLSVPtppeiaaayriSPALLTPPAGAIDWEGWLAQqEPYDGPPVPQPQSM-----IYT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 247 SGTTGLPK-----AAIVVHSRYY-RMASLVyYGFrmrPDDIVYDCL-PLYHSAGNIVGIgQCLLHGMTVVIRKKFSASRF 319
Cdd:PRK12406 161 SGTTGHPKgvrraAPTPEQAAAAeQMRALI-YGL---KPGIRALLTgPLYHSAPNAYGL-RAGRLGGVLVLQPRFDPEEL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 320 WDDCIKYNCTIVQYIGELCRYLLNQPPreaesrhKVRMALgnglrqsiwtDFSSRFHI--------------------PQ 379
Cdd:PRK12406 236 LQLIERHRITHMHMVPTMFIRLLKLPE-------EVRAKY----------DVSSLRHVihaaapcpadvkramiewwgPV 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 380 VAEFYGATEcncslgnfdsrVGACGFNSRILSFVYPIRLVRVNEDTMELIRGPDGVCIPcqPGQPGQLVGRIIQQDPLRr 459
Cdd:PRK12406 299 IYEYYGSTE-----------SGAVTFATSEDALSHPGTVGKAAPGAELRFVDEDGRPLP--QGEIGEIYSRIAGNPDFT- 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 460 fdgYLNQGANNKKIANDVFkkgdqaYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLHMADVAVYGv 539
Cdd:PRK12406 365 ---YHNKPEKRAEIDRGGF------ITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFG- 434
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45597453 540 eVPGTE-GRAGMAAV-ASPISNCDLESFAQTLKKELPLYARPIFLRFLPELHKTGTFKFQKTELR 602
Cdd:PRK12406 435 -IPDAEfGEALMAVVePQPGATLDEADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLR 498
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
75-335 |
4.81e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 103.43 E-value: 4.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 75 TVPLLFASMVQRHPDKTALIFegTDTHWTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKLGveAA 154
Cdd:PRK07798 4 NIADLFEAVADAVPDRVALVC--GDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKAR--AV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 155 LINTNLR--RDALRHCLDTSKARALIFGSEMASAICEIHASLePTLSLFCS----GSWEPSTVPVStehldplLEDAPKH 228
Cdd:PRK07798 80 PVNVNYRyvEDELRYLLDDSDAVALVYEREFAPRVAEVLPRL-PKLRTLVVvedgSGNDLLPGAVD-------YEDALAA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 229 lpSHPDKGFT----DKLFYIYTSGTTGLPKAAIVVHSRYYR--MASLVYYG--FRMRPDDIV-----------YDCLPLY 289
Cdd:PRK07798 152 --GSPERDFGerspDDLYLLYTGGTTGMPKGVMWRQEDIFRvlLGGRDFATgePIEDEEELAkraaagpgmrrFPAPPLM 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 45597453 290 HSAGNIVGIGqCLLHGMTVVI--RKKFSASRFWDDCIKYNCTIVQYIG 335
Cdd:PRK07798 230 HGAGQWAAFA-ALFSGQTVVLlpDVRFDADEVWRTIEREKVNVITIVG 276
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
84-568 |
5.39e-23 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 103.04 E-value: 5.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 84 VQRHPDKTALIFEGTDTHWTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRD 163
Cdd:PRK05852 26 ATRLPEAPALVVTADRIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 164 ALRHCLDTSKARALIFGSEmasAICEiHAslEPTLslfcsgSWEPSTVPVS----------TEHLDPLLEdaPKHLPSHP 233
Cdd:PRK05852 106 EQRVRSQAAGARVVLIDAD---GPHD-RA--EPTT------RWWPLTVNVGgdsgpsggtlSVHLDAATE--PTPATSTP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 234 DKGFTDKLFYIYTSGTTGLPKAAIVVHSRYYRMASLVYYGFRMRPDDIVYDCLPLYHSAGNIVGIGQCLLHGMTVVI--R 311
Cdd:PRK05852 172 EGLRPDDAMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHGHGLIAALLATLASGGAVLLpaR 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 312 KKFSASRFWDDCIKYNCTIVQYIGELCRYLLNQPPREA--ESRHKVRM--ALGNGLRQSIWTDFSSRFHIPqVAEFYGAT 387
Cdd:PRK05852 252 GRFSAHTFWDDIKAVGATWYTAVPTIHQILLERAATEPsgRKPAALRFirSCSAPLTAETAQALQTEFAAP-VVCAFGMT 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 388 ECNCSLGNFDSRVGACGFNSRILSFVypirlvrVNEDTMELIR--GPDGvcIPCQPGQPGQ--LVGRIIQQdplrrfdGY 463
Cdd:PRK05852 331 EATHQVTTTQIEGIGQTENPVVSTGL-------VGRSTGAQIRivGSDG--LPLPAGAVGEvwLRGTTVVR-------GY 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 464 LNQGANNKkiANdvFKKGdqAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLHMADVAVYGVEvPG 543
Cdd:PRK05852 395 LGDPTITA--AN--FTDG--WLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVP-DQ 467
|
490 500
....*....|....*....|....*....
gi 45597453 544 TEGRAGMAAV----ASPISNCDLESFAQT 568
Cdd:PRK05852 468 LYGEAVAAVIvpreSAPPTAEELVQFCRE 496
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
72-593 |
1.25e-22 |
|
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 103.40 E-value: 1.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 72 ERKTVPLLFASMVQRHPDKTALIFEgtDTHWTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEF-VGLwLGMAKLG 150
Cdd:COG1020 474 ADATLHELFEAQAARTPDAVAVVFG--DQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMvVAL-LAVLKAG 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 151 veAAL--INTNLRRDALRHCLDTSKARALIfgsemasaiceIHASLEPTLSlfcsgSWEPSTVPVSTEHLDPLLEDAPKh 228
Cdd:COG1020 551 --AAYvpLDPAYPAERLAYMLEDAGARLVL-----------TQSALAARLP-----ELGVPVLALDALALAAEPATNPP- 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 229 LPSHPdkgftDKLFY-IYTSGTTGLPKAAIVVHsryyrmASLVYY------GFRMRPDDIVydclPLYH------SAGNI 295
Cdd:COG1020 612 VPVTP-----DDLAYvIYTSGSTGRPKGVMVEH------RALVNLlawmqrRYGLGPGDRV----LQFAslsfdaSVWEI 676
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 296 VGigqCLLHGMTVVIRKK---FSASRFWDDCIKYNCTIVQYIGELCRYLLNQPPreaESRHKVRMAL--GNGLRQSIWTD 370
Cdd:COG1020 677 FG---ALLSGATLVLAPPearRDPAALAELLARHRVTVLNLTPSLLRALLDAAP---EALPSLRLVLvgGEALPPELVRR 750
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 371 FSSRFHIPQVAEFYGATECncslgnfdsRVGACgfnsrilsfVYPIRLVRVNEDTMELIRGPDGVCI--------PCQPG 442
Cdd:COG1020 751 WRARLPGARLVNLYGPTET---------TVDST---------YYEVTPPDADGGSVPIGRPIANTRVyvldahlqPVPVG 812
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 443 QPGQL------VGRiiqqdplrrfdGYLNQ-GANNKK-IANDVFKKGDQAYLTGDVLVMDELGYLYFRDRTgDT------ 508
Cdd:COG1020 813 VPGELyiggagLAR-----------GYLNRpELTAERfVADPFGFPGARLYRTGDLARWLPDGNLEFLGRA-DDqvkirg 880
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 509 FRwkgenVSTTEVEGTLSRLLHMADVAVYGVEVPGTEGRAgmAAVASPISNCDLESFAQTLKKELPLYARPIFLRFLPEL 588
Cdd:COG1020 881 FR-----IELGEIEAALLQHPGVREAVVVAREDAPGDKRL--VAYVVPEAGAAAAAALLRLALALLLPPYMVPAAVVLLL 953
|
....*
gi 45597453 589 HKTGT 593
Cdd:COG1020 954 PLPLT 958
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
72-538 |
1.69e-22 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 102.10 E-value: 1.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 72 ERKTVPLLFASMVQRHPDKTALIF--EGTDTHWTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKL 149
Cdd:COG1022 9 PADTLPDLLRRRAARFPDRVALREkeDGIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 150 GVEAALINTNLRRDALRHCLDTSKARALIFGS-EMASAICEIHASLePTLS-LFC---SGSWEPSTVPvsteHLDPLLE- 223
Cdd:COG1022 89 GAVTVPIYPTSSAEEVAYILNDSGAKVLFVEDqEQLDKLLEVRDEL-PSLRhIVVldpRGLRDDPRLL----SLDELLAl 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 224 ----DAPKHLPSHPDKGFTDKLF-YIYTSGTTGLPKAAIVVHSRYYRMASLVYYGFRMRPDDIVYDCLPLYHSAGNIVGI 298
Cdd:COG1022 164 grevADPAELEARRAAVKPDDLAtIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFLPLAHVFERTVSY 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 299 GqCLLHGMTVV---------------------------------IRKKFSASRFW---------DDCIKYNCTIVQyiGE 336
Cdd:COG1022 244 Y-ALAAGATVAfaespdtlaedlrevkptfmlavprvwekvyagIQAKAEEAGGLkrklfrwalAVGRRYARARLA--GK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 337 lcryllnQPPREAESRH---------KVRMALGNGLRQSI------------WtdfssrFH---IPqVAEFYGATE---- 388
Cdd:COG1022 321 -------SPSLLLRLKHaladklvfsKLREALGGRLRFAVsggaalgpelarF------FRalgIP-VLEGYGLTEtspv 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 389 --CNcSLGNFdsRVGACGfnsRILSFVYpirlVRVNEDTmE-LIRGPdGVcipcqpgqpgqlvgriiqqdplrrFDGYLN 465
Cdd:COG1022 387 itVN-RPGDN--RIGTVG---PPLPGVE----VKIAEDG-EiLVRGP-NV------------------------MKGYYK 430
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45597453 466 qgaNNKKIANDVFKKGdqaYL-TGDVLVMDELGYLYFRDRTGDTFrwK---GENVSTTEVEGTLSRLLHMADVAVYG 538
Cdd:COG1022 431 ---NPEATAEAFDADG---WLhTGDIGELDEDGFLRITGRKKDLI--VtsgGKNVAPQPIENALKASPLIEQAVVVG 499
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
89-603 |
2.26e-22 |
|
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: 100.44 E-value: 2.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 89 DKTALIFEGTDThwTFRQLDEYSSSVANFLQARG-LASGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALRH 167
Cdd:cd05941 1 DRIAIVDDGDSI--TYADLVARAARLANRLLALGkDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 168 CLDTSKARALIFGSEMasaiceihasleptlslfcsgswepstvpvstehldplledapkhlpshpdkgftdklfyIYTS 247
Cdd:cd05941 79 VITDSEPSLVLDPALI------------------------------------------------------------LYTS 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 248 GTTGLPKAAIVVHSRYYRMA-SLVYYgFRMRPDDIVYDCLPLYHSAGNIVGIGQCLLHGMTVVIRKKFSASRFWDDCIKY 326
Cdd:cd05941 99 GTTGRPKGVVLTHANLAANVrALVDA-WRWTEDDVLLHVLPLHHVHGLVNALLCPLFAGASVEFLPKFDPKEVAISRLMP 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 327 NCTI---VQYIgelcrY--LLNQPPREAESRHKVRMALGNGLRqsIWTDFSSRFHIPQVAEF-----------YGATECN 390
Cdd:cd05941 178 SITVfmgVPTI-----YtrLLQYYEAHFTDPQFARAAAAERLR--LMVSGSAALPVPTLEEWeaitghtllerYGMTEIG 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 391 CSLGN---FDSRVGACGFNsriLSFVYpirlVRVNEDTmelirgpdgvciPCQPGQPGQlVGRI-IQQDPLrrFDGYLNQ 466
Cdd:cd05941 251 MALSNpldGERRPGTVGMP---LPGVQ----ARIVDEE------------TGEPLPRGE-VGEIqVRGPSV--FKEYWNK 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 467 GANNKKIANDvfkkgDQAYLTGDVLVMDELGYLYFRDRTG-DTFRWKGENVSTTEVEGTLSRLLHMADVAVYGVEVPgTE 545
Cdd:cd05941 309 PEATKEEFTD-----DGWFKTGDLGVVDEDGYYWILGRSSvDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDP-DW 382
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 546 GRAGMAAVA--SPISNCDLESFAQTLKKELPLYARPIFLRFLPELHKTGTFKFQKTELRK 603
Cdd:cd05941 383 GERVVAVVVlrAGAAALSLEELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
84-544 |
2.39e-22 |
|
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: 101.50 E-value: 2.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 84 VQRHPDKTALIFEGTDT----HWTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKLGVEAALINTN 159
Cdd:cd17634 63 LRENGDRTAIIYEGDDTsqsrTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGG 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 160 LRRDALRHCLDTSKARALIFGSE------------MASAICEIHA-SLEPTLSLFCSGS---WEPStvpvSTEHLDPLLE 223
Cdd:cd17634 143 FAPEAVAGRIIDSSSRLLITADGgvragrsvplkkNVDDALNPNVtSVEHVIVLKRTGSdidWQEG----RDLWWRDLIA 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 224 DA-PKHLPSHPDKgfTDKLFYIYTSGTTGLPKAAIVVHSRY-YRMASLVYYGFRMRPDDIVYDCLPLYHSAGNIVGIGQC 301
Cdd:cd17634 219 KAsPEHQPEAMNA--EDPLFILYTSGTTGKPKGVLHTTGGYlVYAATTMKYVFDYGPGDIYWCTADVGWVTGHSYLLYGP 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 302 LLHGMTVVIRKKF----SASRFWDDCIKYNCTIVQYIGELCRYLLNQPPREAE----SRHKVRMALGNGLRQSIWTDFSS 373
Cdd:cd17634 297 LACGATTLLYEGVpnwpTPARMWQVVDKHGVNILYTAPTAIRALMAAGDDAIEgtdrSSLRILGSVGEPINPEAYEWYWK 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 374 RFHIPQ--VAEFYGATE----CNCSLGNFDSRVGACGFNSrilsfVYPIRLVRVNEdtmeliRGPdgvciPCQPGQPGQL 447
Cdd:cd17634 377 KIGKEKcpVVDTWWQTEtggfMITPLPGAIELKAGSATRP-----VFGVQPAVVDN------EGH-----PQPGGTEGNL 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 448 V--------GRIIQQDPLRRFDGYlnqgannkkiandvFKKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTT 519
Cdd:cd17634 441 VitdpwpgqTRTLFGDHERFEQTY--------------FSTFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTA 506
|
490 500
....*....|....*....|....*..
gi 45597453 520 EVEGTLSRLLHMADVAVYGV--EVPGT 544
Cdd:cd17634 507 EIESVLVAHPKVAEAAVVGIphAIKGQ 533
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
245-602 |
2.66e-22 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 98.89 E-value: 2.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 245 YTSGTTGLPKAAIVVHSRYYRMASLVyyGFRMR--PDDIVYDCLPLYHSAGNIVGIGQCLLHGMTVVI-RKKFSASRFWD 321
Cdd:cd05917 9 FTSGTTGSPKGATLTHHNIVNNGYFI--GERLGltEQDRLCIPVPLFHCFGSVLGVLACLTHGATMVFpSPSFDPLAVLE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 322 DCIKYNCTIVQ-----YIGElcrylLNQPPREAESRHKVRMALGNG-------LRQSIwtdfsSRFHIPQVAEFYGATEc 389
Cdd:cd05917 87 AIEKEKCTALHgvptmFIAE-----LEHPDFDKFDLSSLRTGIMAGapcppelMKRVI-----EVMNMKDVTIAYGMTE- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 390 nCSLGNFDSRVGAcGFNSRILSfvypirLVRVNEDTMELIRGPDGVCIPcQPGQPGQLVGRiiqqdplrrfdGYL----- 464
Cdd:cd05917 156 -TSPVSTQTRTDD-SIEKRVNT------VGRIMPHTEAKIVDPEGGIVP-PVGVPGELCIR-----------GYSvmkgy 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 465 --NQGANNKKIANDVFkkgdqaYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLHMADVAVYGVEVP 542
Cdd:cd05917 216 wnDPEKTAEAIDGDGW------LHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDE 289
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45597453 543 gTEGRAGMAAVA----SPISNCDLESFAqtlKKELPLYARPIFLRFLPELHKTGTFKFQKTELR 602
Cdd:cd05917 290 -RYGEEVCAWIRlkegAELTEEDIKAYC---KGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
79-601 |
4.27e-21 |
|
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: 96.89 E-value: 4.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 79 LFASMVQRHPDKTALIFEGTDthWTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKLGVEAALINT 158
Cdd:cd12117 2 LFEEQAARTPDAVAVVYGDRS--LTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 159 NLRRDALRHCLDTSKARALIfgsemasaiceIHASLEPTLSlfcsgswEPSTVPVSTEHLDPLLEDAPKHlPSHPDkgft 238
Cdd:cd12117 80 ELPAERLAFMLADAGAKVLL-----------TDRSLAGRAG-------GLEVAVVIDEALDAGPAGNPAV-PVSPD---- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 239 DKLFYIYTSGTTGLPKAAIVVHSRYYRMASLVYYGfRMRPDDIVYDCLPLYHSAG--NIVGigqCLLHGMTVVIRKK--- 313
Cdd:cd12117 137 DLAYVMYTSGSTGRPKGVAVTHRGVVRLVKNTNYV-TLGPDDRVLQTSPLAFDAStfEIWG---ALLNGARLVLAPKgtl 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 314 FSASRFWDDCIKYNCTIVQYIGELCRYLLNQPPR------------EAESRHKVRMALGNGLRQSIW--------TDFSS 373
Cdd:cd12117 213 LDPDALGALIAEEGVTVLWLTAALFNQLADEDPEcfaglrelltggEVVSPPHVRRVLAACPGLRLVngygptenTTFTT 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 374 RFHIPQVAEFYGATECNCSLGNfdSRVgacgfnsRILsfvypirlvrvnedtmelirgpDGVCIPCQPGQPGQLVgriIQ 453
Cdd:cd12117 293 SHVVTELDEVAGSIPIGRPIAN--TRV-------YVL----------------------DEDGRPVPPGVPGELY---VG 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 454 QDPLRRfdGYLNQGA-NNKKIANDVFKKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLHMA 532
Cdd:cd12117 339 GDGLAL--GYLNRPAlTAERFVADPFGPGERLYRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVR 416
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45597453 533 DVAVygVEVPGTEGRAGMAAVASPISNCDLESFAQTLKKELPLYARPIFLRFLPELHKTGTFKFQKTEL 601
Cdd:cd12117 417 EAVV--VVREDAGGDKRLVAYVVAEGALDAAELRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
103-595 |
4.38e-21 |
|
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: 96.39 E-value: 4.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 103 TFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALRHCLDTSKARALIFGSE 182
Cdd:cd05935 3 TYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGSE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 183 masaiceihasleptlslfcsgswepstvpvstehldplLEDapkhlpshpdkgftdkLFYI-YTSGTTGLPKAAIVVHS 261
Cdd:cd05935 83 ---------------------------------------LDD----------------LALIpYTSGTTGLPKGCMHTHF 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 262 RYYRMASLVYYGFRMRPDDIVYDCLPLYHSAGNIVGIGQCLLHGMTVVIRKKFSASRFWDDCIKYNCTIVQYIGELCRYL 341
Cdd:cd05935 108 SAAANALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMARWDRETALELIEKYKVTFWTNIPTMLVDL 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 342 LNQPPREAESRHKVRMALGNG--LRQSIWTDFSSRFHIPQVaEFYGATE-CNCSLGNFDSR-------VGACGFNSRILS 411
Cdd:cd05935 188 LATPEFKTRDLSSLKVLTGGGapMPPAVAEKLLKLTGLRFV-EGYGLTEtMSQTHTNPPLRpklqclgIP*FGVDARVID 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 412 FvypirlvrvnEDTMELirgPDGVcipcqpgqpgqlVGRIIQQDPlRRFDGYLNQGANNKKIANDVfkKGDQAYLTGDVL 491
Cdd:cd05935 267 I----------ETGREL---PPNE------------VGEIVVRGP-QIFKGYWNRPEETEESFIEI--KGRRFFRTGDLG 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 492 VMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLHMADVAVYGV--EVPGTEGRAGMAAVASPISNCDLESFAQTL 569
Cdd:cd05935 319 YMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVpdERVGEEVKAFIVLRPEYRGKVTEEDIIEWA 398
|
490 500
....*....|....*....|....*.
gi 45597453 570 KKELPLYARPIFLRFLPELHKTGTFK 595
Cdd:cd05935 399 REQMAAYKYPREVEFVDELPRSASGK 424
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
96-603 |
8.75e-21 |
|
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: 96.16 E-value: 8.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 96 EGTDTHWTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKLGveAAL--INTNLRRDALRHCLDTSK 173
Cdd:cd12119 20 EGEVHRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMG--AVLhtINPRLFPEQIAYIINHAE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 174 ARALIFGSEMASAICEIHASLEP--TLSLFCSGSWEPSTVPVSTEHLDPLLEDAPkhlpshPDKGFTDK-------LFYi 244
Cdd:cd12119 98 DRVVFVDRDFLPLLEAIAPRLPTveHVVVMTDDAAMPEPAGVGVLAYEELLAAES------PEYDWPDFdentaaaICY- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 245 yTSGTTGLPKA------AIVVHSryyrMASLVYYGFRMRPDDIVYDCLPLYHsaGNIVGIG-QCLLHGMTVVIRKKFSAS 317
Cdd:cd12119 171 -TSGTTGNPKGvvyshrSLVLHA----MAALLTDGLGLSESDVVLPVVPMFH--VNAWGLPyAAAMVGAKLVLPGPYLDP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 318 RFWDDCIK-YNCTIVQYIGELCRYLLNQPPREAESRHKVRMAL--GNGLRQSIWTDFSSRfHIPqVAEFYGATE------ 388
Cdd:cd12119 244 ASLAELIErEGVTFAAGVPTVWQGLLDHLEANGRDLSSLRRVVigGSAVPRSLIEAFEER-GVR-VIHAWGMTEtsplgt 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 389 CNCSLGNFDSRVGACGFNSRILSfVYPIRLVRVNedtmelIRGPDGVCIPCQPGQPGQLVGR---IIQqdplrrfdGYLN 465
Cdd:cd12119 322 VARPPSEHSNLSEDEQLALRAKQ-GRPVPGVELR------IVDDDGRELPWDGKAVGELQVRgpwVTK--------SYYK 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 466 QGANNKKIANDVFKKgdqaylTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLHMADVAVYGVEVPGTE 545
Cdd:cd12119 387 NDEESEALTEDGWLR------TGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWG 460
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 45597453 546 GRAGMAAVASPISNCDLESFAQTLKKELPLYARPIFLRFLPELHKTGTFKFQKTELRK 603
Cdd:cd12119 461 ERPLAVVVLKEGATVTAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKALRE 518
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
88-614 |
8.80e-21 |
|
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: 96.79 E-value: 8.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 88 PDKTALIFEGTDTH---WTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRDA 164
Cdd:cd05968 75 RTRPALRWEGEDGTsrtLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEA 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 165 LRHCLDTSKARALIFG------------SEMASAICEIHASLEPTLSLFCSGSWEPSTvPVSTEHLDPLLEDAPKHLP-S 231
Cdd:cd05968 155 AATRLQDAEAKALITAdgftrrgrevnlKEEADKACAQCPTVEKVVVVRHLGNDFTPA-KGRDLSYDEEKETAGDGAErT 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 232 HPDkgftDKLFYIYTSGTTGLPKAAIVVHSRY-YRMASLVYYGFRMRPDDIVYDCLPLYHSAGNIVGIGQcLLHGMTVVI 310
Cdd:cd05968 234 ESE----DPLMIIYTSGTTGKPKGTVHVHAGFpLKAAQDMYFQFDLKPGDLLTWFTDLGWMMGPWLIFGG-LILGATMVL 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 311 RKKF----SASRFWDDCIKYNCTIVQYIGELCRYLL--NQPPREAESRHKVRMALGNGlrqSIWTDFSSRF--------H 376
Cdd:cd05968 309 YDGApdhpKADRLWRMVEDHEITHLGLSPTLIRALKprGDAPVNAHDLSSLRVLGSTG---EPWNPEPWNWlfetvgkgR 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 377 IPqVAEFYGATECNCS-LGNFDSR-VGACGFNSrilsfVYPIRLVRVNEDTMELIRGPDGVCIPCQPgQPGQLVGriIQQ 454
Cdd:cd05968 386 NP-IINYSGGTEISGGiLGNVLIKpIKPSSFNG-----PVPGMKADVLDESGKPARPEVGELVLLAP-WPGMTRG--FWR 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 455 DPLRRFDGYlnqgannkkiandvFKKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLHMADV 534
Cdd:cd05968 457 DEDRYLETY--------------WSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLES 522
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 535 AVYGVEVPgTEGRAGMAAVASPisncDLESFAQTLKKEL----------PLyaRPIFLRFLPELHKTGTFKFQKTELR-- 602
Cdd:cd05968 523 AAIGVPHP-VKGEAIVCFVVLK----PGVTPTEALAEELmervadelgkPL--SPERILFVKDLPKTRNAKVMRRVIRaa 595
|
570
....*....|....*
gi 45597453 603 ---KEGFDPSVVKDP 614
Cdd:cd05968 596 ylgKELGDLSSLENP 610
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
241-595 |
2.11e-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: 92.47 E-value: 2.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 241 LFYI-YTSGTTGLPKAaivvhsrYYR-----MASLVY--YGFRMRPDDIVYDCLPLYHSaGNIVGIGQCLLHGMTVVIRK 312
Cdd:cd17633 2 PFYIgFTSGTTGLPKA-------YYRserswIESFVCneDLFNISGEDAILAPGPLSHS-LFLYGAISALYLGGTFIGQR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 313 KFSASRFWDDCIKYNCTIVQYIGELCRYLLnqppREAESRHKVRMAL--GNGLRQSIWTDFSSRFHIPQVAEFYGATEcn 390
Cdd:cd17633 74 KFNPKSWIRKINQYNATVIYLVPTMLQALA----RTLEPESKIKSIFssGQKLFESTKKKLKNIFPKANLIEFYGTSE-- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 391 cslgnfdsrvgacgfnsriLSFVypirLVRVNEDTmeliRGPDGVCIPCqPG-------QPGQLVGRIIQQDPLRrFDGY 463
Cdd:cd17633 148 -------------------LSFI----TYNFNQES----RPPNSVGRPF-PNveieirnADGGEIGKIFVKSEMV-FSGY 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 464 LNQGANNKkiandvfkkgDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLHMADVAVYGVEvpg 543
Cdd:cd17633 199 VRGGFSNP----------DGWMSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIP--- 265
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 45597453 544 tEGRAGMAAVA----SPISNCDLESFaqtLKKELPLYARPIFLRFLPELHKTGTFK 595
Cdd:cd17633 266 -DARFGEIAVAlysgDKLTYKQLKRF---LKQKLSRYEIPKKIIFVDSLPYTSSGK 317
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
75-579 |
2.43e-20 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 95.07 E-value: 2.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 75 TVPLLFASMVQRHPDKTALIFEGTDThwTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKLGVEAA 154
Cdd:PRK05605 33 TLVDLYDNAVARFGDRPALDFFGATT--TYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 155 LINTNLRRDALRHCLDTSKARALIFGSEMASAICEIHA--SLE-----------PTLSLFC---------------SGSw 206
Cdd:PRK05605 111 EHNPLYTAHELEHPFEDHGARVAIVWDKVAPTVERLRRttPLEtivsvnmiaamPLLQRLAlrlpipalrkaraalTGP- 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 207 EPSTVPVSTehldpLLEDAP---KHLPSHPDKGFTDKLFYIYTSGTTGLPKAAIVVHSRYY---RMASLVYYGFRMRPDd 280
Cdd:PRK05605 190 APGTVPWET-----LVDAAIggdGSDVSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFanaAQGKAWVPGLGDGPE- 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 281 IVYDCLPLYHSAGNIVGIGQCLLHGMTVVIRKKFSASRFWDDCIKYNCTIVQYIGELCRYLLnqppREAESR----HKVR 356
Cdd:PRK05605 264 RVLAALPMFHAYGLTLCLTLAVSIGGELVLLPAPDIDLILDAMKKHPPTWLPGVPPLYEKIA----EAAEERgvdlSGVR 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 357 MALGNG--LRQSI---WTDFSSRFHIpqvaEFYGATECN-CSLGN---FDSRVGACGfnsriLSFvyPIRLVRVNEdtme 427
Cdd:PRK05605 340 NAFSGAmaLPVSTvelWEKLTGGLLV----EGYGLTETSpIIVGNpmsDDRRPGYVG-----VPF--PDTEVRIVD---- 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 428 lirgPDGVCIPCQPGQPGQLVGRIIQqdplrRFDGYLNQGANNKKiandVFKkgDQAYLTGDVLVMDELGYLYFRDR--- 504
Cdd:PRK05605 405 ----PEDPDETMPDGEEGELLVRGPQ-----VFKGYWNRPEETAK----SFL--DGWFRTGDVVVMEEDGFIRIVDRike 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 505 ---TGdtfrwkGENVSTTEVEGTLSRLLHMADVAVYGveVPGTEGRAGMAAVASPISNCDL--ESFAQTLKKELPLYARP 579
Cdd:PRK05605 470 liiTG------GFNVYPAEVEEVLREHPGVEDAAVVG--LPREDGSEEVVAAVVLEPGAALdpEGLRAYCREHLTRYKVP 541
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
85-527 |
2.45e-20 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 95.03 E-value: 2.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 85 QRHPDKTALIFEGTDThwTFRQLDEYSSSVANFLQAR-GLASGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRD 163
Cdd:PRK08314 21 RRYPDKTAIVFYGRAI--SYRELLEEAERLAGYLQQEcGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 164 ALRHCLDTSKARALIFGSEMASAICEIHAS--LEPTLSLFCSGswepsTVPVSTEHLDPLLEDAPKHLPSHPDKGFT--- 238
Cdd:PRK08314 99 ELAHYVTDSGARVAIVGSELAPKVAPAVGNlrLRHVIVAQYSD-----YLPAEPEIAVPAWLRAEPPLQALAPGGVVawk 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 239 ----------------DKLFYI-YTSGTTGLPKAAIvvHSRYYRMASLV--YYGFRMRPDDIVYDCLPLYHSAGNIVGIG 299
Cdd:PRK08314 174 ealaaglappphtagpDDLAVLpYTSGTTGVPKGCM--HTHRTVMANAVgsVLWSNSTPESVVLAVLPLFHVTGMVHSMN 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 300 QCLLHGMTVVIrkkfsASRfWD-----DCI-KYNCTIVQYIGELCRYLLNQPPREAESRHKVRMALGNG--LRQSIWTDF 371
Cdd:PRK08314 252 APIYAGATVVL-----MPR-WDreaaaRLIeRYRVTHWTNIPTMVVDFLASPGLAERDLSSLRYIGGGGaaMPEAVAERL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 372 SSRFHIPQVaEFYGATEC--------------NCsLG----NFDSRVgacgfnsrilsfvypirlvrVNEDTMELIrgPD 433
Cdd:PRK08314 326 KELTGLDYV-EGYGLTETmaqthsnppdrpklQC-LGiptfGVDARV--------------------IDPETLEEL--PP 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 434 GVcipcqpgqpgqlVGRIIQQDPlRRFDGYLNQGANNKKiandVFKKGD-QAYL-TGDVLVMDELGYLYFRDRTGDTFRW 511
Cdd:PRK08314 382 GE------------VGEIVVHGP-QVFKGYWNRPEATAE----AFIEIDgKRFFrTGDLGRMDEEGYFFITDRLKRMINA 444
|
490
....*....|....*.
gi 45597453 512 KGENVSTTEVEGTLSR 527
Cdd:PRK08314 445 SGFKVWPAEVENLLYK 460
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
102-602 |
3.60e-20 |
|
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: 93.72 E-value: 3.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 102 WTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALRHCLDTSKARALIFGS 181
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 182 EMAsaiceihasleptlslfcsgswepstvpvstEHLDPlledapkhlpshpdkgfTDKLFYIYTSGTTGLPKAAIVVHS 261
Cdd:cd05969 81 ELY-------------------------------ERTDP-----------------EDPTLLHYTSGTTGTPKGVLHVHD 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 262 RYYRMASLVYYGFRMRPDDIvYDCL--PLYhSAGNIVGIGQCLLHGMTVVIRK-KFSASRfWDDCIKYNCTIVQY----- 333
Cdd:cd05969 113 AMIFYYFTGKYVLDLHPDDI-YWCTadPGW-VTGTVYGIWAPWLNGVTNVVYEgRFDAES-WYGIIERVKVTVWYtapta 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 334 IGELCRYLLNQPPREAESRHKVRMALGNGLRQSI--WTD--FSSRFHipqvaEFYGATE------CNCSlgNFDSRVGAC 403
Cdd:cd05969 190 IRMLMKEGDELARKYDLSSLRFIHSVGEPLNPEAirWGMevFGVPIH-----DTWWQTEtgsimiANYP--CMPIKPGSM 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 404 GfnsrilsfvYPIRLVR---VNEDTMELIRGPDGVcIPCQPGQPGQlvgriiqqdplrrFDGYLNQGANNKKiandVFKK 480
Cdd:cd05969 263 G---------KPLPGVKaavVDENGNELPPGTKGI-LALKPGWPSM-------------FRGIWNDEERYKN----SFID 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 481 GdqAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLHMADVAVYGVEVPgtegRAGMAAVASPISNC 560
Cdd:cd05969 316 G--WYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDP----LRGEIIKAFISLKE 389
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 45597453 561 DLESfAQTLKKELPLYAR--------PIFLRFLPELHKTGTFKFQKTELR 602
Cdd:cd05969 390 GFEP-SDELKEEIINFVRqklgahvaPREIEFVDNLPKTRSGKIMRRVLK 438
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
90-602 |
7.17e-20 |
|
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: 92.54 E-value: 7.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 90 KTALIfeGTDTHWTFRQLDEYSSSVANFLQAR-GLASGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALRHC 168
Cdd:cd05958 1 RTCLR--SPEREWTYRDLLALANRIANVLVGElGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 169 LD-TSKARALIFGSEMASA-ICEIHasleptlslfcsgswepstvpvstehldplledapkhlpshpdkgftdklfyiYT 246
Cdd:cd05958 79 LDkARITVALCAHALTASDdICILA-----------------------------------------------------FT 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 247 SGTTGLPKAAIVVHSRYyrMASLVYYG---FRMRPDDIVYDCLPLYHSagniVGIGQCLLH----GMTVVIRKKFSASRF 319
Cdd:cd05958 106 SGTTGAPKATMHFHRDP--LASADRYAvnvLRLREDDRFVGSPPLAFT----FGLGGVLLFpfgvGASGVLLEEATPDLL 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 320 WDDCIKYNCTIVQYIGELCRYLLNQPPREAESRHKVRMAL--GNGLRQSIWTDFSSRFHIPqVAEFYGATE---CNCSLG 394
Cdd:cd05958 180 LSAIARYKPTVLFTAPTAYRAMLAHPDAAGPDLSSLRKCVsaGEALPAALHRAWKEATGIP-IIDGIGSTEmfhIFISAR 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 395 NFDSRVGACGfnsrilSFVYPIRLVRVNEDTMELirgPDGVcipcqpgqpgqlVGRIIQQDPlrrfDGYlnQGANNKKIA 474
Cdd:cd05958 259 PGDARPGATG------KPVPGYEAKVVDDEGNPV---PDGT------------IGRLAVRGP----TGC--RYLADKRQR 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 475 NDVfkkGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLHMADVAVYGVEVPG--------TEG 546
Cdd:cd05958 312 TYV---QGGWNITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESrgvvvkafVVL 388
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 45597453 547 RAGMAAVASPISncDLESFAqtlKKELPLYARPIFLRFLPELHKTGTFKFQKTELR 602
Cdd:cd05958 389 RPGVIPGPVLAR--ELQDHA---KAHIAPYKYPRAIEFVTELPRTATGKLQRFALR 439
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
77-603 |
8.12e-20 |
|
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: 93.13 E-value: 8.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 77 PLLF---ASMVqrHPDKTALIFEgtDTHWTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKLGveA 153
Cdd:cd12118 6 PLSFlerAAAV--YPDRTSIVYG--DRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAG--A 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 154 ALINTNLRRDA------LRHcldtSKARALIFGSEMAsaiceihaslepTLSLFCSGSWEPSTVPVSTEHldplledapk 227
Cdd:cd12118 80 VLNALNTRLDAeeiafiLRH----SEAKVLFVDREFE------------YEDLLAEGDPDFEWIPPADEW---------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 228 hlpshpdkgftDKLFYIYTSGTTGLPKAAIVVHSRYYRMASLVYYGFRMrPDDIVYDC-LPLYHSAGnivgigQCLLHGM 306
Cdd:cd12118 134 -----------DPIALNYTSGTTGRPKGVVYHHRGAYLNALANILEWEM-KQHPVYLWtLPMFHCNG------WCFPWTV 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 307 -----TVVIRKKFSASRFWDDCIKYNCTivqyigELC------RYLLNQPPREAESR-HKVRMALGN--------GLRQS 366
Cdd:cd12118 196 aavggTNVCLRKVDAKAIYDLIEKHKVT------HFCgaptvlNMLANAPPSDARPLpHRVHVMTAGapppaavlAKMEE 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 367 IwtdfssRFHIPQV---AEFYG-ATEC------------NCSLGNFDSRVGACGFNsrilsfvyPIRLVrvNEDTMELIR 430
Cdd:cd12118 270 L------GFDVTHVyglTETYGpATVCawkpewdelpteERARLKARQGVRYVGLE--------EVDVL--DPETMKPVP 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 431 GpDGVCIpcqpgqpGQLV--GRIIQQdplrrfdGYLNQGANNKKiandVFKKGdqAYLTGDVLVMDELGYLYFRDRTGDT 508
Cdd:cd12118 334 R-DGKTI-------GEIVfrGNIVMK-------GYLKNPEATAE----AFRGG--WFHSGDLAVIHPDGYIEIKDRSKDI 392
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 509 FRWKGENVSTTEVEGTLSRLLHMADVAVYGV------EVPGT--EGRAGMAAVASpisncDLESFAqtlKKELPLYARPI 580
Cdd:cd12118 393 IISGGENISSVEVEGVLYKHPAVLEAAVVARpdekwgEVPCAfvELKEGAKVTEE-----EIIAFC---REHLAGFMVPK 464
|
570 580
....*....|....*....|...
gi 45597453 581 FLRFLPeLHKTGTFKFQKTELRK 603
Cdd:cd12118 465 TVVFGE-LPKTSTGKIQKFVLRD 486
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
79-603 |
1.23e-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: 91.99 E-value: 1.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 79 LFASMVQRHPDKTALifEGTDTHWTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKLGVEAALINT 158
Cdd:cd17653 2 AFERIAAAHPDAVAV--ESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 159 NLRRDALRHCLDTSKARALIFgsemasaiceihasleptlslfcsgswepstvpvstehldplledapkhlPSHPDkgft 238
Cdd:cd17653 80 KLPSARIQAILRTSGATLLLT--------------------------------------------------TDSPD---- 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 239 DKLFYIYTSGTTGLPKAAIVVHSRYYRMASLVYYGFRMRPDD-------IVYDClplyhSAGNIVGigqCLLHGMTVVIR 311
Cdd:cd17653 106 DLAYIIFTSGSTGIPKGVMVPHRGVLNYVSQPPARLDVGPGSrvaqvlsIAFDA-----CIGEIFS---TLCNGGTLVLA 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 312 kkfSASRFWDDCIK----YNCT--IVQYIgelcryllnqPPREAESRHKVRMAlGNGLRQSIWTDFSSRfhiPQVAEFYG 385
Cdd:cd17653 178 ---DPSDPFAHVARtvdaLMSTpsILSTL----------SPQDFPNLKTIFLG-GEAVPPSLLDRWSPG---RRLYNAYG 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 386 ATECNCSlgnfdsrvgaCGFNS-RILSFV---YPIRLVRV---NEDTMELIRGPDG-VCIpcqpgqPGQLVGRiiqqdpl 457
Cdd:cd17653 241 PTECTIS----------STMTElLPGQPVtigKPIPNSTCyilDADLQPVPEGVVGeICI------SGVQVAR------- 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 458 rrfdGYLNQGA-NNKKIANDVFKKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLlhMADVA- 535
Cdd:cd17653 298 ----GYLGNPAlTASKFVPDPFWPGSRMYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEVVLQS--QPEVTq 371
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45597453 536 VYGVEVPGTegragMAAVASPISnCDLESFAQTLKKELPLYARPIFLRFLPELHKTGTFKFQKTELRK 603
Cdd:cd17653 372 AAAIVVNGR-----LVAFVTPET-VDVDGLRSELAKHLPSYAVPDRIIALDSFPLTANGKVDRKALRE 433
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
85-602 |
1.46e-19 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 92.38 E-value: 1.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 85 QRHPDKTALIFEGTDTHWTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNE-FVGLWLGMaKLGVEAALINTNLRRD 163
Cdd:PRK13390 8 QIAPDRPAVIVAETGEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEaLVVLWAAL-RSGLYITAINHHLTAP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 164 ALRHCLDTSKARALIFGSEMASAICEIHASLEPTLSLFCS----GSWEPStvpvstehldplLEDAPKHLPSHPDKGFTd 239
Cdd:PRK13390 87 EADYIVGDSGARVLVASAALDGLAAKVGADLPLRLSFGGEidgfGSFEAA------------LAGAGPRLTEQPCGAVM- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 240 klfyIYTSGTTGLPKA---------------AIVVHSRYYrmaslvyygFRMRPDDIVYDCLPLYHSAgnivGIGQC-LL 303
Cdd:PRK13390 154 ----LYSSGTTGFPKGiqpdlpgrdvdapgdPIVAIARAF---------YDISESDIYYSSAPIYHAA----PLRWCsMV 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 304 H--GMTVVIRKKFSASRFWDDCIKYNCTIVQYIGELCRYLLnQPPREAESRHKVrmalgNGLRQSIWTDFSSRFHI---- 377
Cdd:PRK13390 217 HalGGTVVLAKRFDAQATLGHVERYRITVTQMVPTMFVRLL-KLDADVRTRYDV-----SSLRAVIHAAAPCPVDVkham 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 378 -----PQVAEFYGATECN----CSLGNFDSRVGACGfnSRILSFVYPirlvrVNEDTMELirgpdgvcipcqpgqPGQLV 448
Cdd:PRK13390 291 idwlgPIVYEYYSSTEAHgmtfIDSPDWLAHPGSVG--RSVLGDLHI-----CDDDGNEL---------------PAGRI 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 449 GRI-IQQD--PLRrfdgYLNqgaNNKKIANDVFKKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTL 525
Cdd:PRK13390 349 GTVyFERDrlPFR----YLN---DPEKTAAAQHPAHPFWTTVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENAL 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 526 SrlLHMA--DVAVYGveVPGTEGRAGMAAVASPISNCD-LESFAQTL----KKELPLYARPIFLRFLPELHKTGTFKFQK 598
Cdd:PRK13390 422 T--MHPAvhDVAVIG--VPDPEMGEQVKAVIQLVEGIRgSDELARELidytRSRIAHYKAPRSVEFVDELPRTPTGKLVK 497
|
....
gi 45597453 599 TELR 602
Cdd:PRK13390 498 GLLR 501
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
105-602 |
2.39e-19 |
|
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: 91.28 E-value: 2.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 105 RQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLwlGMAKLGVEAALINTNLRRDALRHCLDTSKARALIfGSEMA 184
Cdd:cd05929 1 LEARDLDRAQVFHQRRLLLLDVYSIALNRNARAAAAEG--VWIADGVYIYLINSILTVFAAAAAWKCGACPAYK-SSRAP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 185 SAICEIHASLEPTlSLFCS--GSWEPSTVPVStehLDPLLEDAPKHLPshPDKGFTDKLFYiyTSGTTGLPKA------A 256
Cdd:cd05929 78 RAEACAIIEIKAA-ALVCGlfTGGGALDGLED---YEAAEGGSPETPI--EDEAAGWKMLY--SGGTTGRPKGikrglpG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 257 IVVHSRYYRMASLvyyGFRMRPDDIVYDCLPLYHSAGNIVGIGqCLLHGMTVVIRKKFSASRFWDDCIKYNCTIVQYIGE 336
Cdd:cd05929 150 GPPDNDTLMAAAL---GFGPGADSVYLSPAPLYHAAPFRWSMT-ALFMGGTLVLMEKFDPEEFLRLIERYRVTFAQFVPT 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 337 LCRYLLNQPprEAEsRHKVRMAlgnGLR-------------QSIWTDFSSrfhiPQVAEFYGATECN----CSLGNFDSR 399
Cdd:cd05929 226 MFVRLLKLP--EAV-RNAYDLS---SLKrvihaaapcppwvKEQWIDWGG----PIIWEYYGGTEGQgltiINGEEWLTH 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 400 VGACGfnsrilsfvypirlvRVNEDTMElIRGPDGVciPCQPGQPGQlvgriIQQDPLRRFDgYLNQGANNKKIANdvfk 479
Cdd:cd05929 296 PGSVG---------------RAVLGKVH-ILDEDGN--EVPPGEIGE-----VYFANGPGFE-YTNDPEKTAAARN---- 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 480 KGDQAYLtGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLHMADVAVYGveVPGTE-GRAGMAAVASPIS 558
Cdd:cd05929 348 EGGWSTL-GDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVG--VPDEElGQRVHAVVQPAPG 424
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 45597453 559 NCDLESFAQTL----KKELPLYARPIFLRFLPELHKTGTFKFQKTELR 602
Cdd:cd05929 425 ADAGTALAEELiaflRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLR 472
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
79-604 |
4.53e-19 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 90.71 E-value: 4.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 79 LFASMVQRHPDKTALIFEGTD-THWTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKLGVEAALIN 157
Cdd:PRK07514 5 LFDALRAAFADRDAPFIETPDgLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 158 TNLRRDALRHCLDTSKARALIFGSEMASAICEIHA-----SLEpTLSLFCSGSwepstvpvstehldpLLEDAPKHLPSH 232
Cdd:PRK07514 85 TAYTLAELDYFIGDAEPALVVCDPANFAWLSKIAAaagapHVE-TLDADGTGS---------------LLEAAAAAPDDF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 233 PD--KGFTDKLFYIYTSGTTGLPKAAIVVHSRYYRMA-SLV-YYGFRmrPDDIVYDCLPLYHSAGNIVGIGQCLLHGMTV 308
Cdd:PRK07514 149 ETvpRGADDLAAILYTSGTTGRSKGAMLSHGNLLSNAlTLVdYWRFT--PDDVLIHALPIFHTHGLFVATNVALLAGASM 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 309 VIRKKFSAsrfwDDCIKY--NCTIVQYIGELCRYLLNQP--PREAESrhkvRMAL---GNG-LRQSIWTDFSSRF-HipQ 379
Cdd:PRK07514 227 IFLPKFDP----DAVLALmpRATVMMGVPTFYTRLLQEPrlTREAAA----HMRLfisGSApLLAETHREFQERTgH--A 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 380 VAEFYGATECNCSLGN-FDS--RVGACGFnsrilsfvyPIRLVRVNedtmelIRGPD-GVciPCQPGQPGQlvgriIQ-Q 454
Cdd:PRK07514 297 ILERYGMTETNMNTSNpYDGerRAGTVGF---------PLPGVSLR------VTDPEtGA--ELPPGEIGM-----IEvK 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 455 DPlRRFDGYLNqgaNNKKIANDVfkKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLHMADV 534
Cdd:PRK07514 355 GP-NVFKGYWR---MPEKTAEEF--RADGFFITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVES 428
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45597453 535 AVYGVEVPGTeGRAGMAAV-ASPISNCDLESFAQTLKKELPLYARPIFLRFLPELHKTGTFKFQKTELRKE 604
Cdd:PRK07514 429 AVIGVPHPDF-GEGVTAVVvPKPGAALDEAAILAALKGRLARFKQPKRVFFVDELPRNTMGKVQKNLLREQ 498
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
83-604 |
7.55e-19 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 90.48 E-value: 7.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 83 MVQRHPDKTALIFEGTDThwTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRR 162
Cdd:PRK06710 33 MASRYPEKKALHFLGKDI--TFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 163 DALRHCLDTSKARA-----LIF--------GSEMASAICEIHASLEP----TLSLFCSGSWEPSTVPVSTEHLDPLLEDA 225
Cdd:PRK06710 111 RELEYQLHDSGAKVilcldLVFprvtnvqsATKIEHVIVTRIADFLPfpknLLYPFVQKKQSNLVVKVSESETIHLWNSV 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 226 PKH------LPSHPDkgfTDKLFYIYTSGTTGLPKAAIVVHSryyRMASLVYYGFR-----MRPDDIVYDCLPLYHSAGN 294
Cdd:PRK06710 191 EKEvntgveVPCDPE---NDLALLQYTGGTTGFPKGVMLTHK---NLVSNTLMGVQwlyncKEGEEVVLGVLPFFHVYGM 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 295 IVGIGQCLLHGMTVVIRKKFSASRFWDDCIKYNCTIVQYIGELCRYLLNQPPREAESRHKVRMALGNG--LRQSIWTDFs 372
Cdd:PRK06710 265 TAVMNLSIMQGYKMVLIPKFDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLLKEYDISSIRACISGSapLPVEVQEKF- 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 373 SRFHIPQVAEFYGATECN-CSLGNF--DSRV-GACGF-----NSRILSFvypirlvrvneDTMELIRgpdgvcipcqPGQ 443
Cdd:PRK06710 344 ETVTGGKLVEGYGLTESSpVTHSNFlwEKRVpGSIGVpwpdtEAMIMSL-----------ETGEALP----------PGE 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 444 pgqlVGRIIQQDPlRRFDGYLNQGANNKKIANDvfkkgdqAYL-TGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVE 522
Cdd:PRK06710 403 ----IGEIVVKGP-QIMKGYWNKPEETAAVLQD-------GWLhTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVE 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 523 GTLSRLLHMADVAVYGVEVPGTEGRAGMAAVASPISNCDLESFAQTLKKELPLYARPIFLRFLPELHKTGTFKFQKTELR 602
Cdd:PRK06710 471 EVLYEHEKVQEVVTIGVPDPYRGETVKAFVVLKEGTECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVLI 550
|
..
gi 45597453 603 KE 604
Cdd:PRK06710 551 EE 552
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
79-601 |
1.10e-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: 89.15 E-value: 1.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 79 LFASMVQRHPDKTALIFEGTDthWTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKLGVEAALINT 158
Cdd:cd17645 3 LFEEQVERTPDHVAVVDRGQS--LTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 159 NLRRDALRHCLDTSKARALIFGSEmasaiceihasleptlslfcsgswepstvpvstehldplledapkhlpshpdkgft 238
Cdd:cd17645 81 DYPGERIAYMLADSSAKILLTNPD-------------------------------------------------------- 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 239 DKLFYIYTSGTTGLPKAAIVVHSRYYRMASLVYYGFRMRPDD--IVYDCLPLyhsAGNIVGIGQCLLHGMTVVI---RKK 313
Cdd:cd17645 105 DLAYVIYTSGSTGLPKGVMIEHHNLVNLCEWHRPYFGVTPADksLVYASFSF---DASAWEIFPHLTAGAALHVvpsERR 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 314 FSASRFWDDCIKYNCTIVQYIGELCRYLLnqppreAESRHKVRMAL--GNGLRQSIWTDFssrfhipQVAEFYGATECNC 391
Cdd:cd17645 182 LDLDALNDYFNQEGITISFLPTGAAEQFM------QLDNQSLRVLLtgGDKLKKIERKGY-------KLVNNYGPTENTV 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 392 SLGNF--DSRVGAcgfnsriLSFVYPIRLVRVnedtmeLIRGPDgvcIPCQP-GQPGQLvgrIIQQDPLRRfdGYLNQ-G 467
Cdd:cd17645 249 VATSFeiDKPYAN-------IPIGKPIDNTRV------YILDEA---LQLQPiGVAGEL---CIAGEGLAR--GYLNRpE 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 468 ANNKKIANDVFKKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLHMADVAVYGVEVPGteGR 547
Cdd:cd17645 308 LTAEKFIVHPFVPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDAD--GR 385
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 45597453 548 AGMAAVASPISNCDLESFAQTLKKELPLYARPIFLRFLPELHKTGTFKFQKTEL 601
Cdd:cd17645 386 KYLVAYVTAPEEIPHEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
79-604 |
1.27e-18 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 89.73 E-value: 1.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 79 LFASMVQRHPDKTALIFEGTDThwTFRQLDEYSSSVANFLQAR-GLASGNVVALFMENRnefvgLWLGMAKLGV-EAALI 156
Cdd:PRK08974 28 MFEQAVARYADQPAFINMGEVM--TFRKLEERSRAFAAYLQNGlGLKKGDRVALMMPNL-----LQYPIALFGIlRAGMI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 157 NTNLR-----RDaLRHCLDTSKARALIFGSEMASAICE----------IHASLEPTLSlFCSGSwepsTVPVSTEHLDPL 221
Cdd:PRK08974 101 VVNVNplytpRE-LEHQLNDSGAKAIVIVSNFAHTLEKvvfktpvkhvILTRMGDQLS-TAKGT----LVNFVVKYIKRL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 222 LedaPK-HLPS-----------------HPDKGFTDKLFYIYTSGTTGLPKAAIVVHSRY---YRMASLVYYGFRMRPDD 280
Cdd:PRK08974 175 V---PKyHLPDaisfrsalhkgrrmqyvKPELVPEDLAFLQYTGGTTGVAKGAMLTHRNMlanLEQAKAAYGPLLHPGKE 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 281 IVYDCLPLYHSAGNIVgigQCLLH----GMTVVIRKKFSASRFWDDCIKYNCTIVQYIGELCRYLLNQPPREAESRHKVR 356
Cdd:PRK08974 252 LVVTALPLYHIFALTV---NCLLFielgGQNLLITNPRDIPGFVKELKKYPFTAITGVNTLFNALLNNEEFQELDFSSLK 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 357 MALGNGL--RQSI---WTDFSSRFHIpqvaEFYGATECN----CSLGNFDSRVGACGFNSrilsfvyPIRLVRVNEDtme 427
Cdd:PRK08974 329 LSVGGGMavQQAVaerWVKLTGQYLL----EGYGLTECSplvsVNPYDLDYYSGSIGLPV-------PSTEIKLVDD--- 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 428 lirgpDGVCIPcqPGQPGQLVGRIIQQdplrrFDGYLNQGANNKkianDVFKKGDQAylTGDVLVMDELGYLYFRDRTGD 507
Cdd:PRK08974 395 -----DGNEVP--PGEPGELWVKGPQV-----MLGYWQRPEATD----EVIKDGWLA--TGDIAVMDEEGFLRIVDRKKD 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 508 TFRWKGENVSTTEVEGTLSRLLHMADVAVYGV--EVPGTEGRAGMAAVASPISNCDLESFAqtlKKELPLYARPIFLRFL 585
Cdd:PRK08974 457 MILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVpsEVSGEAVKIFVVKKDPSLTEEELITHC---RRHLTGYKVPKLVEFR 533
|
570
....*....|....*....
gi 45597453 586 PELHKTGTFKFQKTELRKE 604
Cdd:PRK08974 534 DELPKSNVGKILRRELRDE 552
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
239-603 |
1.53e-18 |
|
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: 88.93 E-value: 1.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 239 DKLFYIYTSGTTGLPKAAIVVHSRYYRMASLVYYGFRMRPDDIVYDCLPLYHSAGNIVGIGQCLLHGMTVVirkkFSAS- 317
Cdd:cd05909 148 DPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPFFHSFGLTGCLWLPLLSGIKVV----FHPNp 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 318 -------RFWDDcikYNCTIVQYIGELCRYLLNQPPREAESRHKVRMALGNGLRQSIWTDFSSRFHIPqVAEFYGATECN 390
Cdd:cd05909 224 ldykkipELIYD---KKATILLGTPTFLRGYARAAHPEDFSSLRLVVAGAEKLKDTLRQEFQEKFGIR-ILEGYGTTECS 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 391 ----CSLGNFDSRVGACG-----FNSRILSfVYPIRLVRVNEDTMELIRGPDgvcipcqpgqpgqlvgriiqqdplrRFD 461
Cdd:cd05909 300 pvisVNTPQSPNKEGTVGrplpgMEVKIVS-VETHEEVPIGEGGLLLVRGPN-------------------------VML 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 462 GYLNqgaNNKKIandVFKKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLHMaDVAVYGVEV 541
Cdd:cd05909 354 GYLN---EPELT---SFAFGDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEILPE-DNEVAVVSV 426
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45597453 542 PgtEGRAGMAAVA-SPISNCDLESFAQTLKK-ELPLYARPIFLRFLPELHKTGTFKFQKTELRK 603
Cdd:cd05909 427 P--DGRKGEKIVLlTTTTDTDPSSLNDILKNaGISNLAKPSYIHQVEEIPLLGTGKPDYVTLKA 488
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
75-604 |
2.05e-18 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 88.92 E-value: 2.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 75 TVPLLFASMVQRHPDKTALIFEGTDThwTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEF-VGLwlgMAKLGVEA 153
Cdd:PRK07059 24 SLADLLEESFRQYADRPAFICMGKAI--TYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYpVAI---AAVLRAGY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 154 ALINTN---LRRDaLRHCLDTSKARALI----FGSEMASAICE------IHASLEPTLSLfcSG---------------S 205
Cdd:PRK07059 99 VVVNVNplyTPRE-LEHQLKDSGAEAIVvlenFATTVQQVLAKtavkhvVVASMGDLLGF--KGhivnfvvrrvkkmvpA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 206 WEpstVPVSTEHLDPLLEDAPKHLpSHPDKGFTDKLFYIYTSGTTGLPKAAIVVH----SRYYRMASLVYYGF--RMRPD 279
Cdd:PRK07059 176 WS---LPGHVRFNDALAEGARQTF-KPVKLGPDDVAFLQYTGGTTGVSKGATLLHrnivANVLQMEAWLQPAFekKPRPD 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 280 DIVYDC-LPLYHsagnIVGIGQCLLHGM-----TVVIRKKFSASRFWDDCIKYNCTIVQYIGELCRYLLNQPPREAESRH 353
Cdd:PRK07059 252 QLNFVCaLPLYH----IFALTVCGLLGMrtggrNILIPNPRDIPGFIKELKKYQVHIFPAVNTLYNALLNNPDFDKLDFS 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 354 KVRMALGNGL--RQSIWTDFSSRFHIPqVAEFYGATE------CNcslgnfdsRVGACGFNSRIlsfVYPIRLVRVNedt 425
Cdd:PRK07059 328 KLIVANGGGMavQRPVAERWLEMTGCP-ITEGYGLSEtspvatCN--------PVDATEFSGTI---GLPLPSTEVS--- 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 426 melIRGPDGVCIPcqPGQPGQLVGRIIQQDPlrrfdGYLNQGANNKKI--ANDVFKkgdqaylTGDVLVMDELGYLYFRD 503
Cdd:PRK07059 393 ---IRDDDGNDLP--LGEPGEICIRGPQVMA-----GYWNRPDETAKVmtADGFFR-------TGDVGVMDERGYTKIVD 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 504 RTGDTFRWKGENVSTTEVEGTLSRLLHMADVAVYGVEVPGTeGRAGMAAVASPISNCDLESFAQTLKKELPLYARPIFLR 583
Cdd:PRK07059 456 RKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHS-GEAVKLFVVKKDPALTEEDVKAFCKERLTNYKRPKFVE 534
|
570 580
....*....|....*....|.
gi 45597453 584 FLPELHKTGTFKFQKTELRKE 604
Cdd:PRK07059 535 FRTELPKTNVGKILRRELRDG 555
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
88-603 |
2.23e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 88.68 E-value: 2.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 88 PDKTALIFEgtDTHWTFRQLDEYSSSVANFLQARGlASGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALRH 167
Cdd:PRK07638 15 PNKIAIKEN--DRVLTYKDWFESVCKVANWLNEKE-SKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 168 CLDTSKARALI----FGSEMASAICEIhasleptlslfcsgsWEpstvpvstehLDPLLEDAPKHLPS-HPDKGFTDKLF 242
Cdd:PRK07638 92 RLAISNADMIVteryKLNDLPDEEGRV---------------IE----------IDEWKRMIEKYLPTyAPIENVQNAPF 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 243 YI-YTSGTTGLPKAAIVVHSRYYRMASLVYYGFRMRPDDIVYDCLPLYHSAgNIVGIGQCLLHGMTVVIRKKFSASRFWD 321
Cdd:PRK07638 147 YMgFTSGSTGKPKAFLRAQQSWLHSFDCNVHDFHMKREDSVLIAGTLVHSL-FLYGAISTLYVGQTVHLMRKFIPNQVLD 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 322 DCIKYNCTIVQYIGELCRYLLnqppREAESRHKVRMALGNGLRQSIWT--DFSSRFHIPQVAEFYGATEcncslgnfdsr 399
Cdd:PRK07638 226 KLETENISVMYTVPTMLESLY----KENRVIENKMKIISSGAKWEAEAkeKIKNIFPYAKLYEFYGASE----------- 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 400 vgacgfnsriLSFVYPIrlvrVNEDTMeliRGPDGVCIPCQPG------------QPGQlVGRIIQQDPLRrFDGYLNQG 467
Cdd:PRK07638 291 ----------LSFVTAL----VDEESE---RRPNSVGRPFHNVqvricneageevQKGE-IGTVYVKSPQF-FMGYIIGG 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 468 ANNKKIANDvfkkgdqAYLT-GDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLHMADVAVYGVEVPgteg 546
Cdd:PRK07638 352 VLARELNAD-------GWMTvRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDS---- 420
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 45597453 547 RAGMAAVASPISNCDLESFAQTLKKELPLYARPIFLRFLPELHKTGTFKFQKTELRK 603
Cdd:PRK07638 421 YWGEKPVAIIKGSATKQQLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEAKS 477
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
66-604 |
2.27e-18 |
|
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: 88.66 E-value: 2.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 66 VRRYLQER----KTVPLLFASMVQRHPDKTALIfeGTDTHWTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVG 141
Cdd:COG1021 13 AARYREAGywrgETLGDLLRRRAERHPDRIAVV--DGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 142 LWLGMAKLGVE--AALIntNLRRDALRHCLDTSKARALIFGS--------EMASAICEIHASLEPTLSLFCSGSWEPstv 211
Cdd:COG1021 91 VFFALFRAGAIpvFALP--AHRRAEISHFAEQSEAVAYIIPDrhrgfdyrALARELQAEVPSLRHVLVVGDAGEFTS--- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 212 pvstehLDPLLEDAPKHLPSHPDKGftDKLFYIYTSGTTGLPKAAIVVHSRYyrmaslvYYGFRMR-------PDDiVYD 284
Cdd:COG1021 166 ------LDALLAAPADLSEPRPDPD--DVAFFQLSGGTTGLPKLIPRTHDDY-------LYSVRASaeicgldADT-VYL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 285 C-LPLYHSAGNIV-GIGQCLLHGMTVVIRKKFSAsrfwDDCI----KYNCTIVQYIGELCRYLLNQPPRE---------- 348
Cdd:COG1021 230 AaLPAAHNFPLSSpGVLGVLYAGGTVVLAPDPSP----DTAFplieRERVTVTALVPPLALLWLDAAERSrydlsslrvl 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 349 --------AESRHKVRMALGNGLRQSiwtdfssrfhipqvaefYGATE--CNCS-LGnfDS---RVGACGfnsRILSfvy 414
Cdd:COG1021 306 qvggaklsPELARRVRPALGCTLQQV-----------------FGMAEglVNYTrLD--DPeevILTTQG---RPIS--- 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 415 P---IRLVrvnedtmelirGPDGVciPCQPGQPGQLVGR---IIQqdplrrfdGYLNQGANNKKiandVFKKgDQAYLTG 488
Cdd:COG1021 361 PddeVRIV-----------DEDGN--PVPPGEVGELLTRgpyTIR--------GYYRAPEHNAR----AFTP-DGFYRTG 414
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 489 DVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLHMADVAVYGV--EVPGTEGRAGMAAVASPISNCDLESFA 566
Cdd:COG1021 415 DLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMpdEYLGERSCAFVVPRGEPLTLAELRRFL 494
|
570 580 590
....*....|....*....|....*....|....*...
gi 45597453 567 QTlkKELPLYARPIFLRFLPELHKTGTFKFQKTELRKE 604
Cdd:COG1021 495 RE--RGLAAFKLPDRLEFVDALPLTAVGKIDKKALRAA 530
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
244-598 |
5.90e-18 |
|
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: 85.63 E-value: 5.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 244 IYTSGTTGLPKAAIVVHSRYYRMASLVYYGFRMRPDDiVYDCL-PLYHSAGNIVGIGQCLLHGMTVVIRKKFSASRFWDD 322
Cdd:cd17638 6 MFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDD-RYLIInPFFHTFGYKAGIVACLLTGATVVPVAVFDVDAILEA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 323 CIKYNCTIVQYIGELCRYLLNQPPREAESRHKVRMALGNG--LRQSIWTDFSSRFHIPQVAEFYGATECNCSL-----GN 395
Cdd:cd17638 85 IERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVTGAatVPVELVRRMRSELGFETVLTAYGLTEAGVATmcrpgDD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 396 FDSRVGACGFnsrilsfVYPIRLVRVNEDTMELIRGPDgvcipcqpgqpgqlvgrIIQqdplrrfdGYL-NQGANNKKIA 474
Cdd:cd17638 165 AETVATTCGR-------ACPGFEVRIADDGEVLVRGYN-----------------VMQ--------GYLdDPEATAEAID 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 475 NDvfkkgdqAYL-TGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLHMADVAVYGV--EVPGTEGRAgmA 551
Cdd:cd17638 213 AD-------GWLhTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVpdERMGEVGKA--F 283
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 45597453 552 AVASPISNCDLESFAQTLKKELPLYARPIFLRFLPELHKTGTFKFQK 598
Cdd:cd17638 284 VVARPGVTLTEEDVIAWCRERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
79-588 |
2.91e-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: 85.02 E-value: 2.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 79 LFASMVQRHPDKTALIFEGTdtHWTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKLGVEAALINT 158
Cdd:cd17646 3 LVAEQAARTPDAPAVVDEGR--TLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 159 NLRRDALRHCLDTSKARALIFGSEMAsaiceihASLEPTLSLFCSGSWEPSTVPvstehldplleDAPKHLPSHPDkgft 238
Cdd:cd17646 81 GYPADRLAYMLADAGPAVVLTTADLA-------ARLPAGGDVALLGDEALAAPP-----------ATPPLVPPRPD---- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 239 DKLFYIYTSGTTGLPKAAIVVHsryyrmASLVYY------GFRMRPDDIVYDCLPLyhsaGNIVGIGQCLL---HGMTVV 309
Cdd:cd17646 139 NLAYVIYTSGSTGRPKGVMVTH------AGIVNRllwmqdEYPLGPGDRVLQKTPL----SFDVSVWELFWplvAGARLV 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 310 I------RKKFSASRFWDDcikYNCTIVQYIGELCRYLLNQPprEAESRHKVRMAL--GNGLRQSIWTDFSSRFHIPQVa 381
Cdd:cd17646 209 VarpgghRDPAYLAALIRE---HGVTTCHFVPSMLRVFLAEP--AAGSCASLRRVFcsGEALPPELAARFLALPGAELH- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 382 EFYGATE-------CNCSLGNFDSRV--GACGFNSRilsfvypirlVRVNEDTMElirgpdgvciPCQPGQPGQLVgriI 452
Cdd:cd17646 283 NLYGPTEaaidvthWPVRGPAETPSVpiGRPVPNTR----------LYVLDDALR----------PVPVGVPGELY---L 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 453 QQDPLRRfdGYLNQGA-NNKKIANDVFKKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLHM 531
Cdd:cd17646 340 GGVQLAR--GYLGRPAlTAERFVPDPFGPGSRMYRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAV 417
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 45597453 532 ADVAVYGVEVPGTEGR-AGMAAVASPISNCDLESFAQTLKKELPLYARPIFLRFLPEL 588
Cdd:cd17646 418 THAVVVARAAPAGAARlVGYVVPAAGAAGPDTAALRAHLAERLPEYMVPAAFVVLDAL 475
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
79-613 |
3.89e-17 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 86.37 E-value: 3.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 79 LFASMVQRHPDKTALIFEGTdtHWTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKLGVEAALINT 158
Cdd:PRK12467 517 LIEAQARQHPERPALVFGEQ--VLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDP 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 159 NLRRDALRHCLDTSKARALIFGSEMAsAICEIHASLePTLSLfcsgswepstvpvstEHLDPLLEDAPKHlpsHPDKGFT 238
Cdd:PRK12467 595 EYPQDRLAYMLDDSGVRLLLTQSHLL-AQLPVPAGL-RSLCL---------------DEPADLLCGYSGH---NPEVALD 654
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 239 -DKLFY-IYTSGTTGLPKAAIVVHSRYYRMASLVYYGFRMRPDDIVYDCLPLYHSAGNIVGIGQcLLHGMTVVIRKK--- 313
Cdd:PRK12467 655 pDNLAYvIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGA-LASGATLHLLPPdca 733
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 314 FSASRFWDDCIKYNCTIVQYIGELCRYLLnQPPREAESRHKVRMALG------NGLRQsiWTDFSsrfhiPQVAEF--YG 385
Cdd:PRK12467 734 RDAEAFAALMADQGVTVLKIVPSHLQALL-QASRVALPRPQRALVCGgealqvDLLAR--VRALG-----PGARLInhYG 805
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 386 ATECncslgNFDSRVGACGFNSRILSFVyPIRLVRVNEDTMELirgpDGVCIPCQPGQPGQLvgrIIQQDPLRRfdGYLN 465
Cdd:PRK12467 806 PTET-----TVGVSTYELSDEERDFGNV-PIGQPLANLGLYIL----DHYLNPVPVGVVGEL---YIGGAGLAR--GYHR 870
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 466 QGA-NNKKIANDVF-KKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEgtlSRLLHMADVAVYGVEVPG 543
Cdd:PRK12467 871 RPAlTAERFVPDPFgADGGRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIE---ARLLAQPGVREAVVLAQP 947
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45597453 544 TEGRAGMAAVASPISNCD-------LESFAQTLKKELPLYARPIFLRFLPELHKTGTFKFQKTELRKegFDPSVVKD 613
Cdd:PRK12467 948 GDAGLQLVAYLVPAAVADgaehqatRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALPK--PDASAVQA 1022
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
79-591 |
6.88e-17 |
|
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: 83.92 E-value: 6.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 79 LFASMVQRHPDKTALIFEgtDTHWTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNE-FVGLwLGMAKLGVEAALIN 157
Cdd:cd17655 2 LFEEQAEKTPDHTAVVFE--DQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEmIVGI-LGILKAGGAYLPID 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 158 TNLRRDALRHCLDTSKARALIfgSEMASAICEIHAsleptlslfcsgswepstvpvstEHLDPLLEDAPKHLPS---HPD 234
Cdd:cd17655 79 PDYPEERIQYILEDSGADILL--TQSHLQPPIAFI-----------------------GLIDLLDEDTIYHEESenlEPV 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 235 KGFTDKLFYIYTSGTTGLPKAAIVVH-----------SRYY-----RMASLVYYGFrmrpDDIVYDclpLYHSagnivgi 298
Cdd:cd17655 134 SKSDDLAYVIYTSGSTGKPKGVMIEHrgvvnlvewanKVIYqgehlRVALFASISF----DASVTE---IFAS------- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 299 gqcLLHGMTVVIRKKFSASR---FWDDCIKYNCTIVqyigELCRYLLNQ-PPREAESRHKVRMAL--GNGLRQSIWTDFS 372
Cdd:cd17655 200 ---LLSGNTLYIVRKETVLDgqaLTQYIRQNRITII----DLTPAHLKLlDAADDSEGLSLKHLIvgGEALSTELAKKII 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 373 SRFHI-PQVAEFYGATEC--NCSLGNFDSR--------VGACGFNSRIlsfvYpirlvrVNEDTMELirgpdgvcipcQP 441
Cdd:cd17655 273 ELFGTnPTITNAYGPTETtvDASIYQYEPEtdqqvsvpIGKPLGNTRI----Y------ILDQYGRP-----------QP 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 442 -GQPGQLVgriIQQDPLRRfdGYLNQGA-NNKKIANDVFKKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTT 519
Cdd:cd17655 332 vGVAGELY---IGGEGVAR--GYLNRPElTAEKFVDDPFVPGERMYRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELG 406
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45597453 520 EVEGTLSRLLHMADVAVygVEVPGTEGRAGMAAVASPISNCDLESFAQTLKKELPLYARPIFLRFLPELHKT 591
Cdd:cd17655 407 EIEARLLQHPDIKEAVV--IARKDEQGQNYLCAYIVSEKELPVAQLREFLARELPDYMIPSYFIKLDEIPLT 476
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
79-601 |
9.39e-17 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 83.51 E-value: 9.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 79 LFASMVQRHPDKTALIFEgtDTHWTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKLGVEAALINT 158
Cdd:PRK13383 40 LLAVTAARWPGRTAIIDD--DGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPIST 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 159 NLRRDALRHCLDTSKARALIFGSEMASaicEIHASLEPTLSLfcsgswEPSTVPVSTEHLDPLLEdAPKHLpshpdkgft 238
Cdd:PRK13383 118 EFRSDALAAALRAHHISTVVADNEFAE---RIAGADDAVAVI------DPATAGAEESGGRPAVA-APGRI--------- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 239 dklfYIYTSGTTGLPKAaiVVHSRYYRMASLVYYGF----RMRPDDIVYDCLPLYHSagniVGIGQCLLH---GMTVVIR 311
Cdd:PRK13383 179 ----VLLTSGTTGKPKG--VPRAPQLRSAVGVWVTIldrtRLRTGSRISVAMPMFHG----LGLGMLMLTialGGTVLTH 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 312 KKFSASRFWDDCIKYNCTIVQYIGELCRYLLNQPPReAESRH-----KVRMALGNGLRQSIWTDFSSRFHiPQVAEFYGA 386
Cdd:PRK13383 249 RHFDAEAALAQASLHRADAFTAVPVVLARILELPPR-VRARNplpqlRVVMSSGDRLDPTLGQRFMDTYG-DILYNGYGS 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 387 TEcncslgnfdsrVGacgfnsrILSFVYPIRLvrvnEDTMELIRGPDGVC---IPCQPGQP--GQLVGRIIQQDPLRRfD 461
Cdd:PRK13383 327 TE-----------VG-------IGALATPADL----RDAPETVGKPVAGCpvrILDRNNRPvgPRVTGRIFVGGELAG-T 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 462 GYlnQGANNKKIANDVFKKGDQAYLtgdvlvmDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLHMADVAVYGVEV 541
Cdd:PRK13383 384 RY--TDGGGKAVVDGMTSTGDMGYL-------DNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPD 454
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 542 PGTEGRAGMAAVASPISNCDLESFAQTLKKELPLYARPIFLRFLPELHKTGTFKFQKTEL 601
Cdd:PRK13383 455 ERFGHRLAAFVVLHPGSGVDAAQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
243-603 |
9.78e-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: 82.14 E-value: 9.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 243 YIYTSGTTGLPKAAIVVHSRYYRMASLVYYGFRMRPDDIVYDCLPLYHSAGNIVGIGQCLLHGMTVVI------RKKFSA 316
Cdd:cd05944 7 YFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVVLagpagyRNPGLF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 317 SRFWDDCIKYNCTIVQYIGELCRYLLNQPPREAESRHKVRMALGNGLRQSIWTDFSSRFHIPqVAEFYGATECNCSLG-N 395
Cdd:cd05944 87 DNFWKLVERYRITSLSTVPTVYAALLQVPVNADISSLRFAMSGAAPLPVELRARFEDATGLP-VVEGYGLTEATCLVAvN 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 396 FDS---RVGACGfnsriLSFVYPIRLVRVNEDTMELIRgpdgvciPCQPGQpgqlVGRIIQQDPlRRFDGYLNQGANNKK 472
Cdd:cd05944 166 PPDgpkRPGSVG-----LRLPYARVRIKVLDGVGRLLR-------DCAPDE----VGEICVAGP-GVFGGYLYTEGNKNA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 473 IANDVFKKgdqaylTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRllHMAdvavygVEVPGTEGRAGMAA 552
Cdd:cd05944 229 FVADGWLN------TGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLR--HPA------VAFAGAVGQPDAHA 294
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 553 VASPISNCDLESFAQTLKKELPLYAR---------PIFLRFLPELHKTGTFKFQKTELRK 603
Cdd:cd05944 295 GELPVAYVQLKPGAVVEEEELLAWARdhvperaavPKHIEVLEELPVTAVGKVFKPALRA 354
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
103-536 |
1.45e-16 |
|
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: 82.31 E-value: 1.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 103 TFRQLDEYSSSVANFLQAR-GLASGNVVALFMENrnefvGLWLGMAKLGVEAA-----LINTNLRRDALRHCLDTSKARA 176
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLER-----SAELVVAILAVLKAgaayvPLDPAYPAERLAFILEDAGARL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 177 LIFGSEMASAiceihASLEPTLSLFCSGSWEPSTvpvstehlDPLLEDAPKHLPSHPDkgftDKLFYIYTSGTTGLPKAA 256
Cdd:TIGR01733 76 LLTDSALASR-----LAGLVLPVILLDPLELAAL--------DDAPAPPPPDAPSGPD----DLAYVIYTSGSTGRPKGV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 257 IVVHsryyrmASLVYYG------FRMRPDDIVYDCLPLYH--SAGNIVGigqCLLHGMTVVI------RKKFSASRFWDD 322
Cdd:TIGR01733 139 VVTH------RSLVNLLawlarrYGLDPDDRVLQFASLSFdaSVEEIFG---ALLAGATLVVppedeeRDDAALLAALIA 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 323 ciKYNCTIVQyigeLCRYLLNQ-PPREAESRHKVRMALGNG--LRQSIWTDFSSRFHIPQVAEFYGATECNCSLGNFD-S 398
Cdd:TIGR01733 210 --EHPVTVLN----LTPSLLALlAAALPPALASLRLVILGGeaLTPALVDRWRARGPGARLINLYGPTETTVWSTATLvD 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 399 RVGACGFNSRILSfvYPIRLVRVnedtmeLIRGPDGVciPCQPGQPGQLVgriIQQDPLRRfdGYLNQ-GANNKKIANDV 477
Cdd:TIGR01733 284 PDDAPRESPVPIG--RPLANTRL------YVLDDDLR--PVPVGVVGELY---IGGPGVAR--GYLNRpELTAERFVPDP 348
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45597453 478 FKKGDQA--YLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLHMADVAV 536
Cdd:TIGR01733 349 FAGGDGArlYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
88-591 |
1.70e-16 |
|
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: 82.42 E-value: 1.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 88 PDKTALIFEgtDTHWTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNE-FVGLwLGMAKLGVEAALINTNLRRDALR 166
Cdd:cd17649 1 PDAVALVFG--DQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEmVVAL-LAILKAGGAYVPLDPEYPAERLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 167 HCLDTSKARALIfgsemasaiceihasleptlslfcsgswepstvpvsTEHldplledaPKHLPshpdkgftdklFYIYT 246
Cdd:cd17649 78 YMLEDSGAGLLL------------------------------------THH--------PRQLA-----------YVIYT 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 247 SGTTGLPKAAIVVH---SRYYRMASLVYygfRMRPDDIVYDCLPLyhsagNIVGIGQCLLH----GMTVVIRKK---FSA 316
Cdd:cd17649 103 SGSTGTPKGVAVSHgplAAHCQATAERY---GLTPGDRELQFASF-----NFDGAHEQLLPplicGACVVLRPDelwASA 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 317 SRFWDDCIKYNCTIVQ----YIGELCRYLLNQPPREAESrhkVRMALGNGlrQSIWTDFSSRFHIPQVAEF--YGATECN 390
Cdd:cd17649 175 DELAEMVRELGVTVLDlppaYLQQLAEEADRTGDGRPPS---LRLYIFGG--EALSPELLRRWLKAPVRLFnaYGPTEAT 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 391 CSLGNFDSRVGA-CGFNSRILSFVYPIRLVRVNedtmelirgpDGVCIPCQPGQPGQLvgrIIQQDPLRRfdGYLNQGAN 469
Cdd:cd17649 250 VTPLVWKCEAGAaRAGASMPIGRPLGGRSAYIL----------DADLNPVPVGVTGEL---YIGGEGLAR--GYLGRPEL 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 470 NKK--IANDVFKKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLHMADVAVYGVEVPGTEGR 547
Cdd:cd17649 315 TAErfVPDPFGAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAGGKQL 394
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 45597453 548 AG-MAAVASPISNCDLESFAQTLKKELPLYARPIFLRFLPELHKT 591
Cdd:cd17649 395 VAyVVLRAAAAQPELRAQLRTALRASLPDYMVPAHLVFLARLPLT 439
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
88-601 |
4.31e-16 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.
Pssm-ID: 341279 [Multi-domain] Cd Length: 477 Bit Score: 81.16 E-value: 4.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 88 PDKTALIfeGTDTHWTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKLGveAALINTNLRRDALRh 167
Cdd:cd12114 1 PDATAVI--CGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAG--AAYVPVDIDQPAAR- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 168 cldtskaralifgsemasaICEIHASLEPTLSLFCSGSWEPStVPVSTEHLDPLLEDAPKHLPSHPDKGFTDKLFYIYTS 247
Cdd:cd12114 76 -------------------REAILADAGARLVLTDGPDAQLD-VAVFDVLILDLDALAAPAPPPPVDVAPDDLAYVIFTS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 248 GTTGLPKAAIVVHSRYYRMASLVYYGFRMRPDDIVYDCLPLYH--SAGNIVGIgqcLLHGMTVVI----RKKFSASrfWD 321
Cdd:cd12114 136 GSTGTPKGVMISHRAALNTILDINRRFAVGPDDRVLALSSLSFdlSVYDIFGA---LSAGATLVLpdeaRRRDPAH--WA 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 322 DCI-KYNCTIVQYIGELCRYLLNQPPREAESRHKVRMALGNG------LRQSIWTDFSSrfhiPQVAEFYGATEcncslg 394
Cdd:cd12114 211 ELIeRHGVTLWNSVPALLEMLLDVLEAAQALLPSLRLVLLSGdwipldLPARLRALAPD----ARLISLGGATE------ 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 395 nfdsrvGAcgfnsrILSFVYPIRlvRVNEDT------MEL------IRGPDGVciPCQPGQPGQLV--GRIIQQdplrrf 460
Cdd:cd12114 281 ------AS------IWSIYHPID--EVPPDWrsipygRPLanqryrVLDPRGR--DCPDWVPGELWigGRGVAL------ 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 461 dGYLNQGAnnkKIAND---------VFKKGDQAYLTGDvlvmdelGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLHM 531
Cdd:cd12114 339 -GYLGDPE---LTAARfvthpdgerLYRTGDLGRYRPD-------GTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGV 407
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45597453 532 ADVAVygVEVPGTEGRAGMAAV-----ASPISNCDLESFaqtLKKELPLYARPIFLRFLPELHKTGTFKFQKTEL 601
Cdd:cd12114 408 ARAVV--VVLGDPGGKRLAAFVvpdndGTPIAPDALRAF---LAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
74-602 |
5.02e-16 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 81.40 E-value: 5.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 74 KTVPLLFASMVQRHPDKTALIFEGTDTHWTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKLGVEA 153
Cdd:PRK08315 16 QTIGQLLDRTAARYPDREALVYRDQGLRWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAIL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 154 ALINTNLRRDALRHCLDTSKARALIF-GSEMASAICEIHASLEPTLSLFCSGSWEPSTVPvsteHLDPLLE-DAPKH--- 228
Cdd:PRK08315 96 VTINPAYRLSELEYALNQSGCKALIAaDGFKDSDYVAMLYELAPELATCEPGQLQSARLP----ELRRVIFlGDEKHpgm 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 229 --------LPSHPDKG----------FTDKLFYIYTSGTTGLPKAAIVVHSRYYRMASLVyyGFRMR--PDDIVYDCLPL 288
Cdd:PRK08315 172 lnfdellaLGRAVDDAelaarqatldPDDPINIQYTSGTTGFPKGATLTHRNILNNGYFI--GEAMKltEEDRLCIPVPL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 289 YHSAGNIVGIGQCLLHGMTVVirkkFSASRFwdDCI-------KYNCTIVQ-----YIGElcrylLNQPPREAESRHKVR 356
Cdd:PRK08315 250 YHCFGMVLGNLACVTHGATMV----YPGEGF--DPLatlaaveEERCTALYgvptmFIAE-----LDHPDFARFDLSSLR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 357 ---MAlgnG-------LRQSIwtdfsSRFHIPQVAEFYGATEcnCSLGNFDS--------RVGACGfnsRILSFVYpirl 418
Cdd:PRK08315 319 tgiMA---GspcpievMKRVI-----DKMHMSEVTIAYGMTE--TSPVSTQTrtddplekRVTTVG---RALPHLE---- 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 419 VR-VNEDTMElirgpdgvciPCQPGQPGQLVGR---IIQqdplrrfdGYLNqgaNNKKIANDVFKKGdqaYL-TGDVLVM 493
Cdd:PRK08315 382 VKiVDPETGE----------TVPRGEQGELCTRgysVMK--------GYWN---DPEKTAEAIDADG---WMhTGDLAVM 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 494 DELGYLYFrdrTGdtfRWK------GENVSTTEVEGTLSRLLHMADVAVYGV-------EVpgtegragMAAV----ASP 556
Cdd:PRK08315 438 DEEGYVNI---VG---RIKdmiirgGENIYPREIEEFLYTHPKIQDVQVVGVpdekygeEV--------CAWIilrpGAT 503
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 45597453 557 ISNCDLESFAQTlkkELPLYARPIFLRFLPELHKTGTFKFQKTELR 602
Cdd:PRK08315 504 LTEEDVRDFCRG---KIAHYKIPRYIRFVDEFPMTVTGKIQKFKMR 546
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
76-604 |
5.98e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 81.15 E-value: 5.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 76 VPLLFASMVQR----HPDKTALIFEgtDTHWTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKLGv 151
Cdd:PRK08162 16 VPLTPLSFLERaaevYPDRPAVIHG--DRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAG- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 152 eaALINT-NLRRDA------LRHCldtsKARALIFGSEMASAIceihaslEPTLSLFcsgswePSTVPVSTEHLDPLLED 224
Cdd:PRK08162 93 --AVLNTlNTRLDAasiafmLRHG----EAKVLIVDTEFAEVA-------REALALL------PGPKPLVIDVDDPEYPG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 225 AP-------KHLPSHPDKGFT--------DKLFYIYTSGTTGLPKAaIVVHSR-YYRMA--SLVYYGFRMRPddiVYD-C 285
Cdd:PRK08162 154 GRfigaldyEAFLASGDPDFAwtlpadewDAIALNYTSGTTGNPKG-VVYHHRgAYLNAlsNILAWGMPKHP---VYLwT 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 286 LPLYH------------SAGNIVgigqCLlhgmtvvirKKFSASRFWDDCIKYNCT------IVQYIgelcryLLNQPPR 347
Cdd:PRK08162 230 LPMFHcngwcfpwtvaaRAGTNV----CL---------RKVDPKLIFDLIREHGVThycgapIVLSA------LINAPAE 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 348 EAES-RHKVR-MALGNGLRQSIWTDFSSR-FHIPQVaefYGATEcncslgnfdsrvgacgfnsrilsfVY-PIRLVRVNE 423
Cdd:PRK08162 291 WRAGiDHPVHaMVAGAAPPAAVIAKMEEIgFDLTHV---YGLTE------------------------TYgPATVCAWQP 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 424 DTMEL-------IRGPDGVCIPCQPG---------QP----GQLVGRIIqqdplrrF------DGYLNqganNKKIANDV 477
Cdd:PRK08162 344 EWDALplderaqLKARQGVRYPLQEGvtvldpdtmQPvpadGETIGEIM-------FrgnivmKGYLK----NPKATEEA 412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 478 FKKGdqAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRllHMAdVAVYGV---------EVPGT--EG 546
Cdd:PRK08162 413 FAGG--WFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYR--HPA-VLVAAVvakpdpkwgEVPCAfvEL 487
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 45597453 547 RAGMAAVASPI-SNCdlesfaqtlKKELPLYARPIFLRFlPELHKTGTFKFQKTELRKE 604
Cdd:PRK08162 488 KDGASATEEEIiAHC---------REHLAGFKVPKAVVF-GELPKTSTGKIQKFVLREQ 536
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
79-603 |
1.25e-15 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 81.16 E-value: 1.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 79 LFASMVQRHPDKTALIFEgtDTHWTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKLGVEAALINT 158
Cdd:PRK12316 2008 RIAEQAARAPEAIAVVFG--DQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDP 2085
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 159 NLRRDALRHCLDTSKARALIFGSEMASAIcEIHASLePTLSLFCSGSWE--PSTvpvstehlDPLLEDAPKHLPshpdkg 236
Cdd:PRK12316 2086 NYPAERLAYMLEDSGAALLLTQRHLLERL-PLPAGV-ARLPLDRDAEWAdyPDT--------APAVQLAGENLA------ 2149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 237 ftdklFYIYTSGTTGLPKAAIVVHSRYYRMASLVYYGFRMRPDDIVYDCLPLYHSaGNIVGIGQCLLHGMTVVIR--KKF 314
Cdd:PRK12316 2150 -----YVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPADCELQFMSFSFD-GAHEQWFHPLLNGARVLIRddELW 2223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 315 SASRFWDDCIKYNCTIVQYIGELCRYLLNQPPREAeSRHKVRMAL--GNGLRQSIWTDFSSRFHIPQVAEFYGATECNCS 392
Cdd:PRK12316 2224 DPEQLYDEMERHGVTILDFPPVYLQQLAEHAERDG-RPPAVRVYCfgGEAVPAASLRLAWEALRPVYLFNGYGPTEAVVT 2302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 393 LGNFDSR-VGACGfnsrilSFVYPIRLVRVNEDTMELirgpDGVCIPCQPGQPGQLVgriIQQDPLRRfdGYLNQ-GANN 470
Cdd:PRK12316 2303 PLLWKCRpQDPCG------AAYVPIGRALGNRRAYIL----DADLNLLAPGMAGELY---LGGEGLAR--GYLNRpGLTA 2367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 471 KKIANDVF-KKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLHMADVAVygVEVPGTEGRAG 549
Cdd:PRK12316 2368 ERFVPDPFsASGERLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVV--VAQDGASGKQL 2445
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 45597453 550 MA-AVASPISNCDLESFAQTLKKELPLYARPIFLRFLPELHKTGTFKFQKTELRK 603
Cdd:PRK12316 2446 VAyVVPDDAAEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPK 2500
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
88-591 |
1.68e-15 |
|
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: 79.27 E-value: 1.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 88 PDKTALIFEgtDTHWTFRQLDEYSSSVANFLQARGLASGNVVALFMENrnefvglwlgmaklgveaalintnlrrdalrh 167
Cdd:cd17643 1 PEAVAVVDE--DRRLTYGELDARANRLARTLRAEGVGPGDRVALALPR-------------------------------- 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 168 cldtskaralifGSEMASAICEIhasleptlsLFCSGSWepstVPVSTEH----LDPLLEDA-PKHLPSHPDkgftDKLF 242
Cdd:cd17643 47 ------------SAELIVALLAI---------LKAGGAY----VPIDPAYpverIAFILADSgPSLLLTDPD----DLAY 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 243 YIYTSGTTGLPKAAIVVHSRYYRMASLVYYGFRMRPDDIVYdclpLYHSAG------NIVGigqCLLHGMTVVIRKKF-- 314
Cdd:cd17643 98 VIYTSGSTGRPKGVVVSHANVLALFAATQRWFGFNEDDVWT----LFHSYAfdfsvwEIWG---ALLHGGRLVVVPYEva 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 315 -SASRFWDDCIKYNCTIvqyigelcrylLNQPP-------REAESRHKVRMAL------GNGLRQSIWTDFSSRF--HIP 378
Cdd:cd17643 171 rSPEDFARLLRDEGVTV-----------LNQTPsafyqlvEAADRDGRDPLALryvifgGEALEAAMLRPWAGRFglDRP 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 379 QVAEFYGATEcncslgnfdsrvgACGFNSrilsfVYPIRLVRVNEDTMELIRGP-----------DGVCIPcqPGQPGQL 447
Cdd:cd17643 240 QLVNMYGITE-------------TTVHVT-----FRPLDAADLPAAAASPIGRPlpglrvyvldaDGRPVP--PGVVGEL 299
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 448 VgriIQQDPLRRfdGYLNQGA--NNKKIANDVFKKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTL 525
Cdd:cd17643 300 Y---VSGAGVAR--GYLGRPEltAERFVANPFGGPGSRMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAAL 374
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45597453 526 SRLLHMADVAVYGVEvpGTEGRAGMAA--VASPISNCDLESFAQTLKKELPLYARPIFLRFLPELHKT 591
Cdd:cd17643 375 ATHPSVRDAAVIVRE--DEPGDTRLVAyvVADDGAAADIAELRALLKELLPDYMVPARYVPLDALPLT 440
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
97-604 |
2.20e-15 |
|
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: 79.43 E-value: 2.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 97 GTDTHWTFRQLDEYSSSVANFL-QARGLASGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALRHCLDTSKAR 175
Cdd:cd05928 37 GDEVKWSFRELGSLSRKAANVLsGACGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 176 ALIFGSEMASAICEIhASLEPTLS---LFCSGSWE-------------PSTVPVSTEHLDPLLedapkhlpshpdkgftd 239
Cdd:cd05928 117 CIVTSDELAPEVDSV-ASECPSLKtklLVSEKSRDgwlnfkellneasTEHHCVETGSQEPMA----------------- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 240 klfyIY-TSGTTGLPKAAIVVHSRYYRMASLV-YYGFRMRPDDIVYDClplyHSAGNIVGIGQCL----LHGMTVVIRK- 312
Cdd:cd05928 179 ----IYfTSGTTGSPKMAEHSHSSLGLGLKVNgRYWLDLTASDIMWNT----SDTGWIKSAWSSLfepwIQGACVFVHHl 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 313 -KFSASRFWDDCIKYNCTIVQYIGELCRYLLNQPPreaeSRHKVR-----MALGNGLRQSIWTDFSSRFHIpQVAEFYGA 386
Cdd:cd05928 251 pRFDPLVILKTLSSYPITTFCGAPTVYRMLVQQDL----SSYKFPslqhcVTGGEPLNPEVLEKWKAQTGL-DIYEGYGQ 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 387 TECNCSLGNFDSRVGACGFNSRIlSFVYPIRLVRVNedtmelirgpdGVCIPcqPGQPGQLVGRIIQQDPLRRFDGYLNq 466
Cdd:cd05928 326 TETGLICANFKGMKIKPGSMGKA-SPPYDVQIIDDN-----------GNVLP--PGTEGDIGIRVKPIRPFGLFSGYVD- 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 467 gaNNKKIANDVfkKGDqAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLHMADVAVYGVEVPgTEG 546
Cdd:cd05928 391 --NPEKTAATI--RGD-FYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDP-IRG 464
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45597453 547 RAGMAAV--ASPISNCDLESFAQTL----KKELPLYARPIFLRFLPELHKTGTFKFQKTELRKE 604
Cdd:cd05928 465 EVVKAFVvlAPQFLSHDPEQLTKELqqhvKSVTAPYKYPRKVEFVQELPKTVTGKIQRNELRDK 528
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
102-590 |
2.50e-15 |
|
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: 78.79 E-value: 2.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 102 WTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALRHCLDTSKARALifgs 181
Cdd:cd05907 6 ITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKAL---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 182 emasaiceihasleptlslFCSGSWEPSTVpvstehldplledapkhlpshpdkgftdklfyIYTSGTTGLPKAaiVVHS 261
Cdd:cd05907 82 -------------------FVEDPDDLATI--------------------------------IYTSGTTGRPKG--VMLS 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 262 rYYRMASLVYYGFRM---RPDDIVYDCLPLYHSAGNIVGIGQCLLHGMTVVIrkkFSASRfwddcikyncTIVQYIGELC 338
Cdd:cd05907 109 -HRNILSNALALAERlpaTEGDRHLSFLPLAHVFERRAGLYVPLLAGARIYF---ASSAE----------TLLDDLSEVR 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 339 RYLLNQPPREAE-SRHKVRMALGNGLRQSI--W-----------------TDFSSRFH---IPqVAEFYGATEC----NC 391
Cdd:cd05907 175 PTVFLAVPRVWEkVYAAIKVKAVPGLKRKLfdLavggrlrfaasggaplpAELLHFFRalgIP-VYEGYGLTETsavvTL 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 392 SLGNfDSRVGACGfnsrilSFVYPIRlVRVNEDTMELIRGPdGVcipcqpgqpgqlvgriiqqdplrrFDGYLNqgaNNK 471
Cdd:cd05907 254 NPPG-DNRIGTVG------KPLPGVE-VRIADDGEILVRGP-NV------------------------MLGYYK---NPE 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 472 KIANDVFKkgDQAYLTGDVLVMDELGYLYFRDRTGDTFRW-KGENVSTTEVEGTLSRLLHMADVAVYGvevpgtEGRAGM 550
Cdd:cd05907 298 ATAEALDA--DGWLHTGDLGEIDEDGFLHITGRKKDLIITsGGKNISPEPIENALKASPLISQAVVIG------DGRPFL 369
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 45597453 551 AAVASPisncDLESFAQTLKKELPLYARPIFLRFLPELHK 590
Cdd:cd05907 370 VALIVP----DPEALEAWAEEHGIAYTDVAELAANPAVRA 405
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
84-539 |
4.53e-15 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 78.40 E-value: 4.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 84 VQRHP-----DKTALIFEGTDTH--WTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKLGVEAALI 156
Cdd:PRK04319 49 IDRHAdggrkDKVALRYLDASRKekYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 157 NTNLRRDALRHCLDTSKARALIFGSEMASAIceIHASLePTL-SLFCSGswEPSTVPVSTEHLDPLLEDAPKHL---PSH 232
Cdd:PRK04319 129 FEAFMEEAVRDRLEDSEAKVLITTPALLERK--PADDL-PSLkHVLLVG--EDVEEGPGTLDFNALMEQASDEFdieWTD 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 233 PDkgftDKLFYIYTSGTTGLPKAAIVVHS---RYYRMAslvYYGFRMRPDDIvYDClplyhSA------GNIVGIGQCLL 303
Cdd:PRK04319 204 RE----DGAILHYTSGSTGKPKGVLHVHNamlQHYQTG---KYVLDLHEDDV-YWC-----TAdpgwvtGTSYGIFAPWL 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 304 HGMTVVIRK-KFSASRFWDDCIKYNCTiVQYigelcryllnqpprEAESRHKVRMALGNGLRQSIwtDFSSRFHIPQVAE 382
Cdd:PRK04319 271 NGATNVIDGgRFSPERWYRILEDYKVT-VWY--------------TAPTAIRMLMGAGDDLVKKY--DLSSLRHILSVGE 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 383 ------------FYG--------ATE------CNcsLGNFDSRVGACGfnsrilsfvYPI-----RLVRvnedtmeliRG 431
Cdd:PRK04319 334 plnpevvrwgmkVFGlpihdnwwMTEtggimiAN--YPAMDIKPGSMG---------KPLpgieaAIVD---------DQ 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 432 PDGVcipcQPGQPGQLVgriiqqdpLRR-----FDGYLNQGANNKKiandVFKKGdqAYLTGDVLVMDELGYLYFRDRTG 506
Cdd:PRK04319 394 GNEL----PPNRMGNLA--------IKKgwpsmMRGIWNNPEKYES----YFAGD--WYVSGDSAYMDEDGYFWFQGRVD 455
|
490 500 510
....*....|....*....|....*....|...
gi 45597453 507 DTFRWKGENVSTTEVEgtlSRLLHMADVAVYGV 539
Cdd:PRK04319 456 DVIKTSGERVGPFEVE---SKLMEHPAVAEAGV 485
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
88-578 |
5.12e-15 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 78.10 E-value: 5.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 88 PDKTALIFEGTDTHWTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALRH 167
Cdd:PLN02246 37 SDRPCLIDGATGRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 168 CLDTSKARALIFGSEMASAICEIHAslEPTLSLFCSGSWEPSTVPVSTehldpLLEDAPKHLPS---HPDkgftDKLFYI 244
Cdd:PLN02246 117 QAKASGAKLIITQSCYVDKLKGLAE--DDGVTVVTIDDPPEGCLHFSE-----LTQADENELPEveiSPD----DVVALP 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 245 YTSGTTGLPKAAIVVH-SRYYRMASLV---YYGFRMRPDDIVYDCLPLYHsagnIVGIGQCLLHGM----TVVIRKKFSA 316
Cdd:PLN02246 186 YSSGTTGLPKGVMLTHkGLVTSVAQQVdgeNPNLYFHSDDVILCVLPMFH----IYSLNSVLLCGLrvgaAILIMPKFEI 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 317 SRFWDDCIKYNCTIVQYIGELCRYLLNQPPREAESRHKVRMALGNG--LRQSIWTDFSSRFHIPQVAEFYGATEC----N 390
Cdd:PLN02246 262 GALLELIQRHKVTIAPFVPPIVLAIAKSPVVEKYDLSSIRMVLSGAapLGKELEDAFRAKLPNAVLGQGYGMTEAgpvlA 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 391 CSLG----NFDSRVGACGfnsrilsfvypiRLVRVNEdtMELIRGPDGVCIPcqPGQPGQLVGRIIQQdplrrFDGYLNq 466
Cdd:PLN02246 342 MCLAfakePFPVKSGSCG------------TVVRNAE--LKIVDPETGASLP--RNQPGEICIRGPQI-----MKGYLN- 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 467 gaNNKKIANDVFKKGdqaYL-TGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLHMADVAVygveVPGTE 545
Cdd:PLN02246 400 --DPEATANTIDKDG---WLhTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAV----VPMKD 470
|
490 500 510
....*....|....*....|....*....|....*..
gi 45597453 546 GRAGMAAVA----SPISNCDLESFAQTLKKELPLYAR 578
Cdd:PLN02246 471 EVAGEVPVAfvvrSNGSEITEDEIKQFVAKQVVFYKR 507
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
76-540 |
6.90e-15 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 77.96 E-value: 6.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 76 VPLLFASmvQRHPDKTALIFEGTDTHWTFRQLDEYSSSVANFLQAR-GLASGNVVALFMENRNEFVGLWLGMAKLGVEAA 154
Cdd:PLN02574 43 VSFIFSH--HNHNGDTALIDSSTGFSISYSELQPLVKSMAAGLYHVmGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 155 LINTNLRRDALR-HCLDTSKAraLIFGSemASAICEIHASLEPTLSLFCSGSWEPSTVPVSTEHldPLLEDAPKHLPShP 233
Cdd:PLN02574 121 TMNPSSSLGEIKkRVVDCSVG--LAFTS--PENVEKLSPLGVPVIGVPENYDFDSKRIEFPKFY--ELIKEDFDFVPK-P 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 234 DKGFTDKLFYIYTSGTTGLPKAAIVVHSRYYRM--------ASLVYYGfrmRPDDIVYDCLPLYHSAGNIVGIGQCLLHG 305
Cdd:PLN02574 194 VIKQDDVAAIMYSSGTTGASKGVVLTHRNLIAMvelfvrfeASQYEYP---GSDNVYLAALPMFHIYGLSLFVVGLLSLG 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 306 MTVVIRKKFSASRFWDDCIKYNCTIVQYIgelcryllnqPPREAESRHKVRMALGNGLR-------------QSIWTDFS 372
Cdd:PLN02574 271 STIVVMRRFDASDMVKVIDRFKVTHFPVV----------PPILMALTKKAKGVCGEVLKslkqvscgaaplsGKFIQDFV 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 373 SRFHIPQVAEFYGATEcncslgnfDSRVGACGFNSRILSFVYPIRLVRVNEDTmELIRGPDGVCIPcqPGQPGQLvgrII 452
Cdd:PLN02574 341 QTLPHVDFIQGYGMTE--------STAVGTRGFNTEKLSKYSSVGLLAPNMQA-KVVDWSTGCLLP--PGNCGEL---WI 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 453 QQDPLRRfdGYLNQG-ANNKKIANDVFKKgdqaylTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLHM 531
Cdd:PLN02574 407 QGPGVMK--GYLNNPkATQSTIDKDGWLR------TGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEI 478
|
....*....
gi 45597453 532 ADVAVYGVE 540
Cdd:PLN02574 479 IDAAVTAVP 487
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
70-602 |
1.19e-14 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 77.22 E-value: 1.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 70 LQERKTVPLLFASMVQRHPDKTALIFEGTDThwTFRQLDEYSSSVANFLQAR-GLASGNVVALFMENRNEFVGLWLGMAK 148
Cdd:PRK08751 21 LEQFRTVAEVFATSVAKFADRPAYHSFGKTI--TYREADQLVEQFAAYLLGElQLKKGDRVALMMPNCLQYPIATFGVLR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 149 LGVEAALINTNLRRDALRHCLDTSKARALI----FGSEMASAICEIHASLEPTLSLF-CSGSWEPSTVPVSTEHLDPLLE 223
Cdd:PRK08751 99 AGLTVVNVNPLYTPRELKHQLIDSGASVLVvidnFGTTVQQVIADTPVKQVITTGLGdMLGFPKAALVNFVVKYVKKLVP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 224 D---------------APKHLPSHPDKGFTDKLFYIYTSGTTGLPKAAIVVHSRY---YRMAS--LVYYGFRMRPDDIVY 283
Cdd:PRK08751 179 EyringairfrealalGRKHSMPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLvanMQQAHqwLAGTGKLEEGCEVVI 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 284 DCLPLYH----SAGNIV--GIGQCllhgmTVVIRKKFSASRFWDDCIKYNCTIVQYIGELCRYLLNQPPREAESRHKVRM 357
Cdd:PRK08751 259 TALPLYHifalTANGLVfmKIGGC-----NHLISNPRDMPGFVKELKKTRFTAFTGVNTLFNGLLNTPGFDQIDFSSLKM 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 358 ALGNGL--RQSIWTDFSSRFHIPQVaEFYGATEcncslgnfdSRVGACgfnsrilsfVYPIRLVRVNEDTMELIRGPDgV 435
Cdd:PRK08751 334 TLGGGMavQRSVAERWKQVTGLTLV-EAYGLTE---------TSPAAC---------INPLTLKEYNGSIGLPIPSTD-A 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 436 CIPCQPGQ--PGQLVGRIIQQDPlRRFDGYLNQGANNKKIANdvfkkGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKG 513
Cdd:PRK08751 394 CIKDDAGTvlAIGEIGELCIKGP-QVMKGYWKRPEETAKVMD-----ADGWLHTGDIARMDEQGFVYIVDRKKDMILVSG 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 514 ENVSTTEVEGTLSRLLHMADVAVYGveVPGTE-GRAGMAAVASPISNCDLESFAQTLKKELPLYARPIFLRFLPELHKTG 592
Cdd:PRK08751 468 FNVYPNEIEDVIAMMPGVLEVAAVG--VPDEKsGEIVKVVIVKKDPALTAEDVKAHARANLTGYKQPRIIEFRKELPKTN 545
|
570
....*....|
gi 45597453 593 TFKFQKTELR 602
Cdd:PRK08751 546 VGKILRRELR 555
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
88-601 |
1.42e-14 |
|
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: 76.74 E-value: 1.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 88 PDKTALIFEgtDTHWTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALRH 167
Cdd:cd17656 2 PDAVAVVFE--NQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 168 CLDTSKARALIFGSEMASAICE--IHASLEptlslfcsgswEPSTVPVSTEHLDplLEDAPKHLpshpdkgftdkLFYIY 245
Cdd:cd17656 80 IMLDSGVRVVLTQRHLKSKLSFnkSTILLE-----------DPSISQEDTSNID--YINNSDDL-----------LYIIY 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 246 TSGTTGLPKAAIVVHSryyRMASLVYYGFRMRPDDIVYDCLPL--------YHSagnivgIGQCLLHGMTV-VIRK--KF 314
Cdd:cd17656 136 TSGTTGKPKGVQLEHK---NMVNLLHFEREKTNINFSDKVLQFatcsfdvcYQE------IFSTLLSGGTLyIIREetKR 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 315 SASRFWDDCIKYNCTIVQYIGELCRYLLNQppREAESR--HKVRMALGNGLRQSIWTDFSSRFHIPQVA--EFYGATECN 390
Cdd:cd17656 207 DVEQLFDLVKRHNIEVVFLPVAFLKFIFSE--REFINRfpTCVKHIITAGEQLVITNEFKEMLHEHNVHlhNHYGPSETH 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 391 CslgnfdsrVGACGFNSRILSFVY-PIRLVRVNEDTmeLIRGPDGVCIPCqpGQPGQLVgriIQQDPLRRfdGYLN-QGA 468
Cdd:cd17656 285 V--------VTTYTINPEAEIPELpPIGKPISNTWI--YILDQEQQLQPQ--GIVGELY---ISGASVAR--GYLNrQEL 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 469 NNKKIANDVFKKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLHMADVAVYGVEvpGTEGRA 548
Cdd:cd17656 348 TAEKFFPDPFDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKA--DDKGEK 425
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 45597453 549 GMAAVASPISNCDLESFAQTLKKELPLYARPIFLRFLPELHKTGTFKFQKTEL 601
Cdd:cd17656 426 YLCAYFVMEQELNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
84-608 |
4.02e-14 |
|
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: 75.68 E-value: 4.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 84 VQRHPDKTALIFEGTDT----HWTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKLGVEAALINTN 159
Cdd:cd05966 63 LKERGDKVAIIWEGDEPdqsrTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFAG 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 160 LRRDALRHCLDTSKARALIFGSE------------MASAICEIHASLEPTLslfcsgSWEPSTVPVS-TEHLDPLLEDA- 225
Cdd:cd05966 143 FSAESLADRINDAQCKLVITADGgyrggkviplkeIVDEALEKCPSVEKVL------VVKRTGGEVPmTEGRDLWWHDLm 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 226 PKHLPSHPDKGFT--DKLFYIYTSGTTGLPKAaiVVHSR--YyrmasLVY------YGFRMRPDDIVY---DClplyhsa 292
Cdd:cd05966 217 AKQSPECEPEWMDseDPLFILYTSGSTGKPKG--VVHTTggY-----LLYaattfkYVFDYHPDDIYWctaDI------- 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 293 GNIVG-----IGQcLLHGMTVVIrkkF-------SASRFWDDCIKYNCTIVqY-----IGELCRYLLNQPPREAESRHKV 355
Cdd:cd05966 283 GWITGhsyivYGP-LANGATTVM---FegtptypDPGRYWDIVEKHKVTIF-YtaptaIRALMKFGDEWVKKHDLSSLRV 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 356 RMALGNGLRQSIWTDFSS---RFHIPQVAEFYgATE----CNCSL-GNFDSRVGACGFnsrilsfvyP---IRLVRVNED 424
Cdd:cd05966 358 LGSVGEPINPEAWMWYYEvigKERCPIVDTWW-QTEtggiMITPLpGATPLKPGSATR---------PffgIEPAILDEE 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 425 TMELIRGPDGV-CIPcQPgQPGQLvgRIIQQDPLRRFDGYlnqgannkkiandvFKKGDQAYLTGDVLVMDELGYLYFRD 503
Cdd:cd05966 428 GNEVEGEVEGYlVIK-RP-WPGMA--RTIYGDHERYEDTY--------------FSKFPGYYFTGDGARRDEDGYYWITG 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 504 RTGDTFRWKGENVSTTEVEGTLsrLLH--MADVAVYGVEVPGTeGRAGMAAVASpisnCDLESFAQTLKKELPL------ 575
Cdd:cd05966 490 RVDDVINVSGHRLGTAEVESAL--VAHpaVAEAAVVGRPHDIK-GEAIYAFVTL----KDGEEPSDELRKELRKhvrkei 562
|
570 580 590
....*....|....*....|....*....|....*..
gi 45597453 576 --YARPIFLRFLPELHKTGTFKFQKTELRK--EGFDP 608
Cdd:cd05966 563 gpIATPDKIQFVPGLPKTRSGKIMRRILRKiaAGEEE 599
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
244-603 |
4.74e-14 |
|
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.
Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 73.52 E-value: 4.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 244 IYTSGTTGLPKAaiVVHSRY----YRMASLVYYGFRMRPDDIVydCLPLYHSAGNIVgIGQCLLHGMTVVIRKKFSASRf 319
Cdd:cd17630 6 ILTSGSTGTPKA--VVHTAAnllaSAAGLHSRLGFGGGDSWLL--SLPLYHVGGLAI-LVRSLLAGAELVLLERNQALA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 320 wDDCIKYNCTIVQYIGELCRYLLnQPPREAESRHKVRMALGNGlrQSIWTDFSSRF---HIPqVAEFYGATEcncslgnF 396
Cdd:cd17630 80 -EDLAPPGVTHVSLVPTQLQRLL-DSGQGPAALKSLRAVLLGG--APIPPELLERAadrGIP-LYTTYGMTE-------T 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 397 DSRVGACGFNSRILSFVYPI---RLVRVNEDTMELIRGPdgvcipcqpgqpgqlvgriiqqdplRRFDGYLNQGannkkI 473
Cdd:cd17630 148 ASQVATKRPDGFGRGGVGVLlpgRELRIVEDGEIWVGGA-------------------------SLAMGYLRGQ-----L 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 474 ANDVFKkgDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLHMADVAVYGVEVPgtegRAGMAAV 553
Cdd:cd17630 198 VPEFNE--DGWFTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDE----ELGQRPV 271
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 45597453 554 ASPISNC--DLESFAQTLKKELPLYARPIFLRFLPELHKTGTFKFQKTELRK 603
Cdd:cd17630 272 AVIVGRGpaDPAELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRA 323
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
77-552 |
8.58e-14 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 75.20 E-value: 8.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 77 PLLFASMVQRH----PDKTALIF----EGTDTHWTFRQLDEYSSSVANFLQARGLASGNVVALFmENRNEFVGLWLGMAK 148
Cdd:PRK05691 8 PLTLVQALQRRaaqtPDRLALRFladdPGEGVVLSYRDLDLRARTIAAALQARASFGDRAVLLF-PSGPDYVAAFFGCLY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 149 LGVEA--ALINTNLRRDALRHCL---DTSKARALIFGSEMASAICEIHASLEPTLslfcsgswePSTVPVSTehLDPLLE 223
Cdd:PRK05691 87 AGVIAvpAYPPESARRHHQERLLsiiADAEPRLLLTVADLRDSLLQMEELAAANA---------PELLCVDT--LDPALA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 224 DAPKHLPSHPDkgftDKLFYIYTSGTTGLPKAAIVVHSRYYRMASLVYYGFRMR--PDDIVYDCLPLYHSAGNIVGIGQC 301
Cdd:PRK05691 156 EAWQEPALQPD----DIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGIDlnPDDVIVSWLPLYHDMGLIGGLLQP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 302 LLHGMTVVIrkkFSASRFWDDCIKYNCTIVQYIG----------ELCRyllnqpPREAESrhkvrmALgNGLRQSIW-TD 370
Cdd:PRK05691 232 IFSGVPCVL---MSPAYFLERPLRWLEAISEYGGtisggpdfayRLCS------ERVSES------AL-ERLDLSRWrVA 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 371 FSSRFHIPQVaefygatecncSLGNFDSRVGACGFNSRILSFVY----------------PIRLVRVNEDTMELIRGPDG 434
Cdd:PRK05691 296 YSGSEPIRQD-----------SLERFAEKFAACGFDPDSFFASYglaeatlfvsggrrgqGIPALELDAEALARNRAEPG 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 435 ---VCIPCQPGQPGQLVgRIIQQDPLRRFD----------------GYLNqgaNNKKIANDVFKKGDQAYL-TGDVLVMD 494
Cdd:PRK05691 365 tgsVLMSCGRSQPGHAV-LIVDPQSLEVLGdnrvgeiwasgpsiahGYWR---NPEASAKTFVEHDGRTWLrTGDLGFLR 440
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45597453 495 ElGYLYFRDRTGDTFRWKGENVSTTEVEGTLSR---LLHMADVAVYGVEVPGTEGrAGMAA 552
Cdd:PRK05691 441 D-GELFVTGRLKDMLIVRGHNLYPQDIEKTVEReveVVRKGRVAAFAVNHQGEEG-IGIAA 499
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
84-588 |
9.96e-14 |
|
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: 73.82 E-value: 9.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 84 VQRHPDKTALIFEGTDthWTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKLGveAALINTNlrrd 163
Cdd:cd05945 1 AAANPDRPAVVEGGRT--LTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAG--HAYVPLD---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 164 alrhcLDTSKARalifgsemasaICEIHASLEPTLsLFCSGswepstvpvstehldplledapkhlpshpdkgftDKLFY 243
Cdd:cd05945 73 -----ASSPAER-----------IREILDAAKPAL-LIADG----------------------------------DDNAY 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 244 I-YTSGTTGLPKAaiVVHSRyyrmASLVYYGFRMRPD-----DIVYDCLPLYHSAGNIVGIGQCLLHGMTVVIRKKfsas 317
Cdd:cd05945 102 IiFTSGSTGRPKG--VQISH----DNLVSFTNWMLSDfplgpGDVFLNQAPFSFDLSVMDLYPALASGATLVPVPR---- 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 318 rfwddcikyncTIVQYIGELCRYLlnqppreaeSRHKV----------RMALGNG---------LRQSIwtdFS------ 372
Cdd:cd05945 172 -----------DATADPKQLFRFL---------AEHGItvwvstpsfaAMCLLSPtftpeslpsLRHFL---FCgevlph 228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 373 -------SRFhiPQVAEF--YGATECN--CSLGNFDSRVGACgfNSRIlsfvyPIRlvRVNEDTMELIRGPDGVCIPcqP 441
Cdd:cd05945 229 ktaralqQRF--PDARIYntYGPTEATvaVTYIEVTPEVLDG--YDRL-----PIG--YAKPGAKLVILDEDGRPVP--P 295
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 442 GQPGQLVGRIIQqdplrRFDGYLNqgaNNKKIANDVFK-KGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTE 520
Cdd:cd05945 296 GEKGELVISGPS-----VSKGYLN---NPEKTAAAFFPdEGQRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEE 367
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45597453 521 VEGTLSRLLHMADVAVygVEVPGTEGRAGMAAVASPISNCDLE---SFAQTLKKELPLYARPIFLRFLPEL 588
Cdd:cd05945 368 IEAALRQVPGVKEAVV--VPKYKGEKVTELIAFVVPKPGAEAGltkAIKAELAERLPPYMIPRRFVYLDEL 436
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
88-543 |
3.32e-13 |
|
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: 72.56 E-value: 3.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 88 PDKTALIFEGTDTHWTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALRH 167
Cdd:cd17642 31 PGTIAFTDAHTGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDH 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 168 CLDTSKARaLIFGSEMA-SAICEIHASLEPTLSLFCSGSWEP-----STVPVSTEHLDPLLeDAPKHLPSHPDKGfTDKL 241
Cdd:cd17642 111 SLNISKPT-IVFCSKKGlQKVLNVQKKLKIIKTIIILDSKEDykgyqCLYTFITQNLPPGF-NEYDFKPPSFDRD-EQVA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 242 FYIYTSGTTGLPKAAIVVHSRYY-RMASLV--YYGFRMRPDDIVYDCLPLYHSAGNIVGIGQcLLHGMTVVIRKKFSASR 318
Cdd:cd17642 188 LIMNSSGSTGLPKGVQLTHKNIVaRFSHARdpIFGNQIIPDTAILTVIPFHHGFGMFTTLGY-LICGFRVVLMYKFEEEL 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 319 FWDDCIKYNCTIVQYIGELCRYLLNQPPREA-ESRHKVRMALGNG-LRQSIWTDFSSRFHIPQVAEFYGATECNCSL--- 393
Cdd:cd17642 267 FLRSLQDYKVQSALLVPTLFAFFAKSTLVDKyDLSNLHEIASGGApLSKEVGEAVAKRFKLPGIRQGYGLTETTSAIlit 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 394 GNFDSRVGACGfnsRILSFVYpirlVRVNEDTMELIRGPDgvcipcqpgQPGQLV--GRIIQQdplrrfdGYLNqganNK 471
Cdd:cd17642 347 PEGDDKPGAVG---KVVPFFY----AKVVDLDTGKTLGPN---------ERGELCvkGPMIMK-------GYVN----NP 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45597453 472 KIANDVFKKgDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLHMADVAVYGV------EVPG 543
Cdd:cd17642 400 EATKALIDK-DGWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIpdedagELPA 476
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
89-614 |
4.27e-13 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 72.24 E-value: 4.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 89 DKTALIFEGT----DTHWTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRDA 164
Cdd:PLN02654 104 DKIAIYWEGNepgfDASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAES 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 165 LRHCLDTSKARALIFGSEMASAICEIH------ASLEPT----LSLFCSGSWEPSTVPVS-----TEHLDPLLEDAPKHL 229
Cdd:PLN02654 184 LAQRIVDCKPKVVITCNAVKRGPKTINlkdivdAALDESakngVSVGICLTYENQLAMKRedtkwQEGRDVWWQDVVPNY 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 230 PSHPDKGFTDK---LFYIYTSGTTGLPKAaiVVHSRYYRM---ASLVYYGFRMRPDDIVY---DClplyhsaGNIVGIGQ 300
Cdd:PLN02654 264 PTKCEVEWVDAedpLFLLYTSGSTGKPKG--VLHTTGGYMvytATTFKYAFDYKPTDVYWctaDC-------GWITGHSY 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 301 C----LLHGMTVVIRKKF----SASRFWDDCIKYNCTIVQYIGELCRYLL--NQPPREAESRHKVRM--ALGNGLRQSIW 368
Cdd:PLN02654 335 VtygpMLNGATVLVFEGApnypDSGRCWDIVDKYKVTIFYTAPTLVRSLMrdGDEYVTRHSRKSLRVlgSVGEPINPSAW 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 369 TDFssrFHIpqvaefYGATECNCSLGNFDSRVGacGFNSRILSFVYP------------IRLVRVNEDTMELirgpDGVC 436
Cdd:PLN02654 415 RWF---FNV------VGDSRCPISDTWWQTETG--GFMITPLPGAWPqkpgsatfpffgVQPVIVDEKGKEI----EGEC 479
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 437 ---IPCQPGQPGQLvgRIIQQDPLRRFDGYlnqgannkkiandvFKKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKG 513
Cdd:PLN02654 480 sgyLCVKKSWPGAF--RTLYGDHERYETTY--------------FKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSG 543
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 514 ENVSTTEVEGTLSRLLHMADVAVYGV--EVPGTEGRAGMAAV-ASPISNCDLESFAQTLKKELPLYARPIFLRFLPELHK 590
Cdd:PLN02654 544 HRIGTAEVESALVSHPQCAEAAVVGIehEVKGQGIYAFVTLVeGVPYSEELRKSLILTVRNQIGAFAAPDKIHWAPGLPK 623
|
570 580 590
....*....|....*....|....*....|.
gi 45597453 591 TGTFKFQKTELRK-------EGFDPSVVKDP 614
Cdd:PLN02654 624 TRSGKIMRRILRKiasrqldELGDTSTLADP 654
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
89-603 |
6.39e-13 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.
Pssm-ID: 213283 [Multi-domain] Cd Length: 509 Bit Score: 71.31 E-value: 6.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 89 DKTALIFEGT---DTHWTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRDAL 165
Cdd:cd05915 9 GRKEVVSRLHtgeVHRTTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 166 RHCLDTSKARALIFGSEMASAIceihaslEPTLSLFCSGSWEPSTVPVSTEHLDPLLEDAPKHLPSHP-DKgfTDKLFYI 244
Cdd:cd05915 89 AYILNHAEDKVLLFDPNLLPLV-------EAIRGELKTVQHFVVMDEKAPEGYLAYEEALGEEADPVRvPE--RAACGMA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 245 YTSGTTGLPKAAIVVHSRYYRMASLVYYGFRMRPDDI-VYDC-LPLYHSAGNIVGIGQCLLHGMTVVIRKKFSASRFWDD 322
Cdd:cd05915 160 YTTGTTGLPKGVVYSHRALVLHSLAASLVDGTALSEKdVVLPvVPMFHVNAWCLPYAATLVGAKQVLPGPRLDPASLVEL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 323 CIKYNCTivQYIGElcRYLLNQPPREAESRHK-----VRMALGNGLRQSIWTDFsSRFHIPQVAEFYGATECNcSLGNfd 397
Cdd:cd05915 240 FDGEGVT--FTAGV--PTVWLALADYLESTGHrlktlRRLVVGGSAAPRSLIAR-FERMGVEVRQGYGLTETS-PVVV-- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 398 srvgACGFNSRILSFVYPIRLVRVNEDTMELIRGPDGVCIPCQPGQPGQlvGRIIQQDPLRR---FDGYLNQGANNKKIA 474
Cdd:cd05915 312 ----QNFVKSHLESLSEEEKLTLKAKTGLPIPLVRLRVADEEGRPVPKD--GKALGEVQLKGpwiTGGYYGNEEATRSAL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 475 ndvFKKGdqAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLsrllhMADVAVYGVEVPG----TEGRAGM 550
Cdd:cd05915 386 ---TPDG--FFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENAL-----MGHPKVKEAAVVAiphpKWQERPL 455
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 45597453 551 AAVASPISNCDLESFAQTLKKEL-PLYARPIFLRFLPELHKTGTFKFQKTELRK 603
Cdd:cd05915 456 AVVVPRGEKPTPEELNEHLLKAGfAKWQLPDAYVFAEEIPRTSAGKFLKRALRE 509
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
72-559 |
7.15e-13 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 71.55 E-value: 7.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 72 ERKTVPLLFASMVQRHPDKTALIFEGTDTHWTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLG-MAKLG 150
Cdd:PLN02330 26 DKLTLPDFVLQDAELYADKVAFVEAVTGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGiMAAGG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 151 VEAALINTNLRRDaLRHCLDTSKARALIFGSEMASAIceihASLEptLSLFCSGSWEPSTVPVSTEHLDPllEDAPKHLP 230
Cdd:PLN02330 106 VFSGANPTALESE-IKKQAEAAGAKLIVTNDTNYGKV----KGLG--LPVIVLGEEKIEGAVNWKELLEA--ADRAGDTS 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 231 SHPDKGFTDKLFYIYTSGTTGLPKAAIVVHSRYyrMASLVYYGFRMRPDDI----VYDCLPLYHSAGnIVGIGQCLLHGM 306
Cdd:PLN02330 177 DNEEILQTDLCALPFSSGTTGISKGVMLTHRNL--VANLCSSLFSVGPEMIgqvvTLGLIPFFHIYG-ITGICCATLRNK 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 307 -TVVIRKKFSASRFWDDCIKYNCTIVQYIGELCRYLLNQPPREAESRHKVR----MALGNGLRQSIWTDFSSRFHIPQVA 381
Cdd:PLN02330 254 gKVVVMSRFELRTFLNALITQEVSFAPIVPPIILNLVKNPIVEEFDLSKLKlqaiMTAAAPLAPELLTAFEAKFPGVQVQ 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 382 EFYGATECNC---SLGNFDSRVGACGFNSriLSFVYPIRLVR-VNEDTmelirgpdGVCIPcqPGQPGQLVGR---IIQq 454
Cdd:PLN02330 334 EAYGLTEHSCitlTHGDPEKGHGIAKKNS--VGFILPNLEVKfIDPDT--------GRSLP--KNTPGELCVRsqcVMQ- 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 455 dplrrfdGYLNqgaNNKKIANDVFKKGdqaYL-TGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLHMAD 533
Cdd:PLN02330 401 -------GYYN---NKEETDRTIDEDG---WLhTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVED 467
|
490 500
....*....|....*....|....*.
gi 45597453 534 VAVygveVPGTEGRAGMAAVASPISN 559
Cdd:PLN02330 468 AAV----VPLPDEEAGEIPAACVVIN 489
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
102-573 |
9.83e-13 |
|
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: 70.96 E-value: 9.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 102 WTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFV----GLWLGmaklGVEAALINTNLRRDALRHCLDTSKARAL 177
Cdd:cd05932 7 FTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFitdlAIWMA----GHISVPLYPTLNPDTIRYVLEHSESKAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 178 IFG-----SEMASAICE--IHASLEPTLSLFCSGSWEpstvpvSTEHLDPLLEDAPKHLPshpdkgftDKLF-YIYTSGT 249
Cdd:cd05932 83 FVGklddwKAMAPGVPEglISISLPPPSAANCQYQWD------DLIAQHPPLEERPTRFP--------EQLAtLIYTSGT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 250 TGLPKAAIVVHSRYYRMASLVYYGFRMRPDDIVYDCLPLYHSAGNIVGIGQCLLHGMTV------------VIRKK---- 313
Cdd:cd05932 149 TGQPKGVMLTFGSFAWAAQAGIEHIGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVafaesldtfvedVQRARptlf 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 314 FSASRFWddcIKYNCTIVQYIG--ELCRyLLNQPPREAESRHKVRMALG-NGLR---------QSIWTDFSSRFHIPqVA 381
Cdd:cd05932 229 FSVPRLW---TKFQQGVQDKIPqqKLNL-LLKIPVVNSLVKRKVLKGLGlDQCRlagcgsapvPPALLEWYRSLGLN-IL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 382 EFYGATEcNCSLGN----FDSRVGACGFNsrilsfvYPIRLVRVNEDTMELIRgpdgvcipcqpgQPGQLVGRiiqqdpl 457
Cdd:cd05932 304 EAYGMTE-NFAYSHlnypGRDKIGTVGNA-------GPGVEVRISEDGEILVR------------SPALMMGY------- 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 458 rrfdgYLNQGANNKKIANDVFKKgdqaylTGDVLVMDELGYLYFRDRTGDTFRW-KGENVSTTEVEGTLSRLLHMADVAV 536
Cdd:cd05932 357 -----YKDPEATAEAFTADGFLR------TGDKGELDADGNLTITGRVKDIFKTsKGKYVAPAPIENKLAEHDRVEMVCV 425
|
490 500 510
....*....|....*....|....*....|....*...
gi 45597453 537 YGVEVPGTEGRAGMAAVASPIS-NCDLESFAQTLKKEL 573
Cdd:cd05932 426 IGSGLPAPLALVVLSEEARLRAdAFARAELEASLRAHL 463
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
68-588 |
9.88e-13 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 71.91 E-value: 9.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 68 RYLQERkTVPLLFASMVQRHPDKTALIFegTDTHWTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMA 147
Cdd:PRK12316 3052 EYPLER-GVHRLFEEQVERTPDAVALAF--GEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAIL 3128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 148 KLGVEAALINTNLRRDALRHCLDTSKARALIFGSemasaiceiHASLeptlslfcsgswePSTVPVSTEHLDPLLEDAPK 227
Cdd:PRK12316 3129 KAGGAYVPLDPEYPEERLAYMLEDSGAQLLLSQS---------HLRL-------------PLAQGVQVLDLDRGDENYAE 3186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 228 HLPshPDKGFTDKLFY-IYTSGTTGLPKAAIVVHSRYYRMASLVYYGFRMRPDDIVydclpLYHSAGNIVGIGQCLLHGM 306
Cdd:PRK12316 3187 ANP--AIRTMPENLAYvIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRV-----LQFTTFSFDVFVEELFWPL 3259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 307 TVVIRKKFSASRFWDDCIKYNCTIVQ--------YIGELCRYLLNQPPREAESrhkVRMALGNGlrQSIWTDFSSRFHIP 378
Cdd:PRK12316 3260 MSGARVVLAGPEDWRDPALLVELINSegvdvlhaYPSMLQAFLEEEDAHRCTS---LKRIVCGG--EALPADLQQQVFAG 3334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 379 Q-VAEFYGATECNCSLGNFDSRVGACGFnsrilsfvYPIRLVRVNEDTMELirgpDGVCIPCQPGQPGQLvgrIIQQDPL 457
Cdd:PRK12316 3335 LpLYNLYGPTEATITVTHWQCVEEGKDA--------VPIGRPIANRACYIL----DGSLEPVPVGALGEL---YLGGEGL 3399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 458 RRfdGYLNQ-GANNKKIANDVFKKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEgtlSRLLHMAdvAV 536
Cdd:PRK12316 3400 AR--GYHNRpGLTAERFVPDPFVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIE---ARLLEHP--WV 3472
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 45597453 537 YGVEVPGTEGRAGMAAVASPISNCDL-ESFAQTLKKELPLYARPIFLRFLPEL 588
Cdd:PRK12316 3473 REAVVLAVDGRQLVAYVVPEDEAGDLrEALKAHLKASLPEYMVPAHLLFLERM 3525
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
239-591 |
1.11e-12 |
|
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: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 239 DKLFYIYTSGTTGLPKAAIVVHSRYYRMASLVYYGFRMRPDDIVYDCLPLYHSAGniVGIGQCLLH--GMTVVIRKkFSA 316
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPLFHIAG--LNLALATFHagGANVVMEK-FDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 317 SRFWDDCIKYNCTivqYIGE----LCRYL--LNQPPREAESrhkVRMALGNGLRQSIwtdfsSRFHIPQVAEF---YGAT 387
Cdd:cd17637 78 AEALELIEEEKVT---LMGSfppiLSNLLdaAEKSGVDLSS---LRHVLGLDAPETI-----QRFEETTGATFwslYGQT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 388 ECNC--SLGNFDSRVGACGfnsRILsfvyPIRLVR-VNEDTMELirgPDGVcipcqpgqpgqlVGRIIQQDPLRrFDGYL 464
Cdd:cd17637 147 ETSGlvTLSPYRERPGSAG---RPG----PLVRVRiVDDNDRPV---PAGE------------TGEIVVRGPLV-FQGYW 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 465 NQGANNkkiaNDVFKKGdqAYLTGDVLVMDELGYLYFRDRTGDTFRWK--GENVSTTEVEGTLSRLLHMADVAVYGveVP 542
Cdd:cd17637 204 NLPELT----AYTFRNG--WHHTGDLGRFDEDGYLWYAGRKPEKELIKpgGENVYPAEVEKVILEHPAIAEVCVIG--VP 275
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 45597453 543 GTEGRAGMAAVaspisnCDLESFAQTLKKEL--------PLYARPIFLRFLPELHKT 591
Cdd:cd17637 276 DPKWGEGIKAV------CVLKPGATLTADELiefvgsriARYKKPRYVVFVEALPKT 326
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
75-588 |
1.29e-12 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 71.23 E-value: 1.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 75 TVPLLFASMVQRHPDKTALIFEGTdtHWTFRQLDEYSSSVANFLQARGLASGNVVALFMEnRNEFVGLWLgMAKLGVEAA 154
Cdd:PRK10252 459 TLSALVAQQAAKTPDAPALADARY--QFSYREMREQVVALANLLRERGVKPGDSVAVALP-RSVFLTLAL-HAIVEAGAA 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 155 L--INTNLRRDALRHCLDTSKARALIFGSEMASAICEIhaslePTLSLFCSGSWEPstvpvstehlDPLLEDAPKHLPSH 232
Cdd:PRK10252 535 WlpLDTGYPDDRLKMMLEDARPSLLITTADQLPRFADV-----PDLTSLCYNAPLA----------PQGAAPLQLSQPHH 599
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 233 PdkgftdkLFYIYTSGTTGLPKAAIVVH----SRYYRMASlvYYGfrMRPDDIVYDCLPlyhsAGNIVGIGQC---LLHG 305
Cdd:PRK10252 600 T-------AYIIFTSGSTGRPKGVMVGQtaivNRLLWMQN--HYP--LTADDVVLQKTP----CSFDVSVWEFfwpFIAG 664
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 306 MTVVI------RKKFSASRFWDDcikYNCTIVQYIGELCRYLLNQPPREAESRHKVRM--------ALGNGLRQsiwtDF 371
Cdd:PRK10252 665 AKLVMaepeahRDPLAMQQFFAE---YGVTTTHFVPSMLAAFVASLTPEGARQSCASLrqvfcsgeALPADLCR----EW 737
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 372 SSRFHIPqVAEFYGATE----------CNCSLGNFDSRVGACGF---NSRIlsfvypirlvRVNEDTMElirgpdgvciP 438
Cdd:PRK10252 738 QQLTGAP-LHNLYGPTEaavdvswypaFGEELAAVRGSSVPIGYpvwNTGL----------RILDARMR----------P 796
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 439 CQPGQPGQLVGRIIQqdpLRRfdGYLNQ-GANNKKIANDVFKKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVS 517
Cdd:PRK10252 797 VPPGVAGDLYLTGIQ---LAQ--GYLGRpDLTASRFIADPFAPGERMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIE 871
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45597453 518 TTEVEGTLSRLLHMADVAVYGVEVPGTEGRAGMAA------VASPISNCDLESFAQTLKKELPLYARPIFLRFLPEL 588
Cdd:PRK10252 872 LGEIDRAMQALPDVEQAVTHACVINQAAATGGDARqlvgylVSQSGLPLDTSALQAQLRERLPPHMVPVVLLQLDQL 948
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
66-601 |
1.47e-12 |
|
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: 70.05 E-value: 1.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 66 VRRYLQ----ERKTVPLLFASMVQRHPDKTALIfeGTDTHWTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVG 141
Cdd:cd05920 3 ARRYRAagywQDEPLGDLLARSAARHPDRIAVV--DGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 142 LWLGMAKLGVEAALINTNLRRDALRHCLDTSKARALIfgsemasaiceihasleptlslfcsgswepstVPVSTEHLDPl 221
Cdd:cd05920 81 LFFALLRLGAVPVLALPSHRRSELSAFCAHAEAVAYI--------------------------------VPDRHAGFDH- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 222 LEDAPKHLPSHPDKGftdklFYIYTSGTTGLPKAAIVVHSRYYRM--ASLVYYGFRmrpDDIVYDC-LPLYHS-AGNIVG 297
Cdd:cd05920 128 RALARELAESIPEVA-----LFLLSGGTTGTPKLIPRTHNDYAYNvrASAEVCGLD---QDTVYLAvLPAAHNfPLACPG 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 298 IGQCLLHGMTVVIRKKFSASRFWDDCIKYNCTIVQYIGELCRYLLNqpprEAESRH----------------------KV 355
Cdd:cd05920 200 VLGTLLAGGRVVLAPDPSPDAAFPLIEREGVTVTALVPALVSLWLD----AAASRRadlsslrllqvggarlspalarRV 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 356 RMALGNGLRQsiwtdfssrfhipqvaeFYGATE---CNCSLGNFDSRVgaCGFNSRILSFVYPIRLVrvnedtmelirgp 432
Cdd:cd05920 276 PPVLGCTLQQ-----------------VFGMAEgllNYTRLDDPDEVI--IHTQGRPMSPDDEIRVV------------- 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 433 DGVCIPCQPGQPGQLVGRiiqqDPLrRFDGYLNQGANNKKIANDvfkkgDQAYLTGDVLVMDELGYLYFRDRTGDTFRWK 512
Cdd:cd05920 324 DEEGNPVPPGEEGELLTR----GPY-TIRGYYRAPEHNARAFTP-----DGFYRTGDLVRRTPDGYLVVEGRIKDQINRG 393
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 513 GENVSTTEVEGTLSRLLHMADVAVYGVEVPGTEGRAGMAAVASPISnCDLESFAQTLKK-ELPLYARPIFLRFLPELHKT 591
Cdd:cd05920 394 GEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVLRDPP-PSAAQLRRFLRErGLAAYKLPDRIEFVDSLPLT 472
|
570
....*....|
gi 45597453 592 GTFKFQKTEL 601
Cdd:cd05920 473 AVGKIDKKAL 482
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
68-609 |
1.49e-12 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 71.53 E-value: 1.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 68 RYLQERkTVPLLFASMVQRHPDKTALIFEGTDThwTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMA 147
Cdd:PRK12316 4546 GYPATR-CVHQLVAERARMTPDAVAVVFDEEKL--TYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVL 4622
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 148 KLGVEAALINTNLRRDALRHCLDTSKARALIFGSEMASAIcEIHASLEpTLSLFCSGSWE--PSTvpvstehlDPLLEDA 225
Cdd:PRK12316 4623 KAGGAYVPLDPEYPRERLAYMMEDSGAALLLTQSHLLQRL-PIPDGLA-SLALDRDEDWEgfPAH--------DPAVRLH 4692
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 226 PKHLPshpdkgftdklFYIYTSGTTGLPKAAIVVHSRYyrMASLVYYG--FRMRPDDIVYDCLPlYHSAGNIVGIGQCLL 303
Cdd:PRK12316 4693 PDNLA-----------YVIYTSGSTGRPKGVAVSHGSL--VNHLHATGerYELTPDDRVLQFMS-FSFDGSHEGLYHPLI 4758
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 304 HGMTVVIRKkfsaSRFWD------DCIKYNCTIVQYIGELCRYLLNQPPREAE-SRHKVRMALGNGLRQSIWTDFSSRFH 376
Cdd:PRK12316 4759 NGASVVIRD----DSLWDperlyaEIHEHRVTVLVFPPVYLQQLAEHAERDGEpPSLRVYCFGGEAVAQASYDLAWRALK 4834
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 377 IPQVAEFYGATECNCSLGNFDSRVG-ACGfnsrilSFVYPIRLVRVNEDTMELirgpDGVCIPCQPGQPGQLVgriIQQD 455
Cdd:PRK12316 4835 PVYLFNGYGPTETTVTVLLWKARDGdACG------AAYMPIGTPLGNRSGYVL----DGQLNPLPVGVAGELY---LGGE 4901
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 456 PLRRfdGYLNQGA-NNKKIANDVF-KKGDQAYLTGDVL------VMDELGylyfrdRTGDTFRWKGENVSTTEVEGTLSR 527
Cdd:PRK12316 4902 GVAR--GYLERPAlTAERFVPDPFgAPGGRLYRTGDLAryradgVIDYLG------RVDHQVKIRGFRIELGEIEARLRE 4973
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 528 LLHMADVAVYGVEVPGTEGRAGM------AAVASPISNCDL-ESFAQTLKKELPLYARPIFLRFLPELHKTGTFKFQKTE 600
Cdd:PRK12316 4974 HPAVREAVVIAQEGAVGKQLVGYvvpqdpALADADEAQAELrDELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRKA 5053
|
....*....
gi 45597453 601 LRKegFDPS 609
Cdd:PRK12316 5054 LPQ--PDAS 5060
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
113-539 |
5.58e-12 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 68.67 E-value: 5.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 113 SVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALRHCLDTSKARALIFgSEMASAICEIHA 192
Cdd:PLN02860 44 SLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWSFEEAKSAMLLVRPVMLVT-DETCSSWYEELQ 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 193 SLE-PTLSLFC-SGSWEPSTVP-----VSTEHL-DPLLEDAPKHLPSHPDkgftDKLFYIYTSGTTGLPKAAIVVHSRYY 264
Cdd:PLN02860 123 NDRlPSLMWQVfLESPSSSVFIflnsfLTTEMLkQRALGTTELDYAWAPD----DAVLICFTSGTTGRPKGVTISHSALI 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 265 --RMASLVYYGFRmrPDDIVYDCLPLYHsagnIVGIGQC---LLHGMTVVIRKKFSASRFWDdCIKYNC-----TIVQYI 334
Cdd:PLN02860 199 vqSLAKIAIVGYG--EDDVYLHTAPLCH----IGGLSSAlamLMVGACHVLLPKFDAKAALQ-AIKQHNvtsmiTVPAMM 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 335 GELCRYllNQPPREAESRHKVRMAL--GNGLRQSIWTDFSSRFHIPQVAEFYGATECNCSLGNFDSRVGACGFNSRILSF 412
Cdd:PLN02860 272 ADLISL--TRKSMTWKVFPSVRKILngGGSLSSRLLPDAKKLFPNAKLFSAYGMTEACSSLTFMTLHDPTLESPKQTLQT 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 413 VYPIRLVRVNEdtmelirgPDGVCIpcqpGQPGQLVGRIIQQDPLRRFDGYLNQG--------ANNKKIANDvfkKGDQA 484
Cdd:PLN02860 350 VNQTKSSSVHQ--------PQGVCV----GKPAPHVELKIGLDESSRVGRILTRGphvmlgywGQNSETASV---LSNDG 414
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 45597453 485 YL-TGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLHMADVAVYGV 539
Cdd:PLN02860 415 WLdTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGV 470
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
70-602 |
5.65e-12 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 68.51 E-value: 5.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 70 LQERKTVPLLFASMVQR----HPDKTALIFegTDTHWTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLG 145
Cdd:PLN03102 6 LCEANNVPLTPITFLKRasecYPNRTSIIY--GKTRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 146 MAKLGVEAALINTNLRRDALRHCLDTSKARALIFGSEMASAICEIhasleptLSLFCSGSWEP-----------STVPVS 214
Cdd:PLN03102 84 VPMAGAVLNPINTRLDATSIAAILRHAKPKILFVDRSFEPLAREV-------LHLLSSEDSNLnlpvifiheidFPKRPS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 215 TEHLD-PLLEDAPKHLPSHPDKGFT-----DKLFYIYTSGTTGLPKAAIVVHSRYYRMASLVYYGFRMRPDDIVYDCLPL 288
Cdd:PLN03102 157 SEELDyECLIQRGEPTPSLVARMFRiqdehDPISLNYTSGTTADPKGVVISHRGAYLSTLSAIIGWEMGTCPVYLWTLPM 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 289 YHSAGNIVGIGQCLLHGMTVVIRKkFSASRFWDDCIKYNCTIVQYIGELCRYLL-----NQPPREAesrhKVRMALGNGL 363
Cdd:PLN03102 237 FHCNGWTFTWGTAARGGTSVCMRH-VTAPEIYKNIEMHNVTHMCCVPTVFNILLkgnslDLSPRSG----PVHVLTGGSP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 364 RQSIWTDFSSRFHIpQVAEFYGATECN-----CSLGN------------FDSRVGAcgfnsRILSFVYpirlVRV-NEDT 425
Cdd:PLN03102 312 PPAALVKKVQRLGF-QVMHAYGLTEATgpvlfCEWQDewnrlpenqqmeLKARQGV-----SILGLAD----VDVkNKET 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 426 MElirgpdgvCIPcqpgQPGQLVGRIIQQDPLRrFDGYLNqganNKKIANDVFKKGdqaYL-TGDVLVMDELGYLYFRDR 504
Cdd:PLN03102 382 QE--------SVP----RDGKTMGEIVIKGSSI-MKGYLK----NPKATSEAFKHG---WLnTGDVGVIHPDGHVEIKDR 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 505 TGDTFRWKGENVSTTEVEGTLSRLLHMADVAVYGVEVPgTEGRAGMAAVA---SPISNCDLESFAQTLKKELPLYAR--- 578
Cdd:PLN03102 442 SKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHP-TWGETPCAFVVlekGETTKEDRVDKLVTRERDLIEYCRenl 520
|
570 580
....*....|....*....|....*....
gi 45597453 579 PIFL-----RFLPELHKTGTFKFQKTELR 602
Cdd:PLN03102 521 PHFMcprkvVFLQELPKNGNGKILKPKLR 549
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
239-598 |
1.25e-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: 66.52 E-value: 1.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 239 DKLFYIYTSGTTGLPKAAIVVH-SRYYRMASLVYYGFRMRPDDIVYDCLPLYHSaGNIVGIGQCLLHGMTVVIRKKFSAS 317
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANkTFFAVPDILQKEGLNWVVGDVTYLPLPATHI-GGLWWILTCLIHGGLCVTGGENTTY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 318 R-FWDDCIKYNCTIVQYIGELCRYLLNQPPREAESRHKVRMaLGNGLRQSIWTD--FSSRFHIPQVAEFYGATE----CN 390
Cdd:cd17635 81 KsLFKILTTNAVTTTCLVPTLLSKLVSELKSANATVPSLRL-IGYGGSRAIAADvrFIEATGLTNTAQVYGLSEtgtaLC 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 391 CSLGNFDSRVGACGfnsrilsfvYPIRLVRVNEDTMELIRGPDGVcipcqpgqpgqlVGRIIQQDPlRRFDGYLNqganN 470
Cdd:cd17635 160 LPTDDDSIEINAVG---------RPYPGVDVYLAATDGIAGPSAS------------FGTIWIKSP-ANMLGYWN----N 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 471 KKIANDVFKKGdqaYL-TGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLHMADVAVYGVEVPGTEGRAG 549
Cdd:cd17635 214 PERTAEVLIDG---WVnTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVG 290
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 45597453 550 MAAVASPIsncDLESFA----QTLKKELPLYARPIFLRFLPELHKTGTFKFQK 598
Cdd:cd17635 291 LAVVASAE---LDENAIralkHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
84-309 |
1.60e-11 |
|
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: 67.26 E-value: 1.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 84 VQRHPDKTALIF----EGTDTHWTFRQLDEYSSSVANFLQARGLAsGNVVALFMENRNEFVGLWLG--MAKL-GVEAALI 156
Cdd:cd05931 3 AAARPDRPAYTFlddeGGREETLTYAELDRRARAIAARLQAVGKP-GDRVLLLAPPGLDFVAAFLGclYAGAiAVPLPPP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 157 NTNLRRDALRHCLDTSKARALIFGSEMASAICEIHASLeptlslfcsgswePSTVPVSTEHLDPLLEDAPKHLPsHPDKG 236
Cdd:cd05931 82 TPGRHAERLAAILADAGPRVVLTTAAALAAVRAFAASR-------------PAAGTPRLLVVDLLPDTSAADWP-PPSPD 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45597453 237 FTDKLFYIYTSGTTGLPKAAIVVHsryyR--MASLVYY--GFRMRPDDIVYDCLPLYHSAGNIVGIGQCLLHGMTVV 309
Cdd:cd05931 148 PDDIAYLQYTSGSTGTPKGVVVTH----RnlLANVRQIrrAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGPSV 220
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
84-540 |
1.96e-11 |
|
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: 66.96 E-value: 1.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 84 VQRH-----PDKTALIFE----GTDTHWTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKLGVeaa 154
Cdd:cd05967 56 LDRHveagrGDQIALIYDspvtGTERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGA--- 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 155 lintnlrrdalrhcldtskARALIFG----SEMASAIceIHAslEPTLSLFCSGSWEPSTVPVSTEHLDPLLEDA---PK 227
Cdd:cd05967 133 -------------------IHSVVFGgfaaKELASRI--DDA--KPKLIVTASCGIEPGKVVPYKPLLDKALELSghkPH 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 228 HL-----------PSHPDKGF-------------------TDKLFYIYTSGTTGLPKAaiVV-----HS--RYYRMASLv 270
Cdd:cd05967 190 HVlvlnrpqvpadLTKPGRDLdwsellakaepvdcvpvaaTDPLYILYTSGTTGKPKG--VVrdnggHAvaLNWSMRNI- 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 271 yYGfrMRPDDIVYdclplyhsAGNIVG--IGQC------LLHGMTVVIRKKF-----SASRFWDDCIKYNCTIVQYIGEL 337
Cdd:cd05967 267 -YG--IKPGDVWW--------AASDVGwvVGHSyivygpLLHGATTVLYEGKpvgtpDPGAFWRVIEKYQVNALFTAPTA 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 338 CRYLLNQPPREAE------SRHKVRMALGNGLRQSIWTDFSSRFHIPqVAEFYGATE------CNCS-LGNFDSRVGAC- 403
Cdd:cd05967 336 IRAIRKEDPDGKYikkydlSSLRTLFLAGERLDPPTLEWAENTLGVP-VIDHWWQTEtgwpitANPVgLEPLPIKAGSPg 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 404 ----GFNSRILSfvypirlvrvneDTMElirgpdgvciPCQPGQPGQLVGRI---------IQQDPLRRFDGYLNqgann 470
Cdd:cd05967 415 kpvpGYQVQVLD------------EDGE----------PVGPNELGNIVIKLplppgclltLWKNDERFKKLYLS----- 467
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 471 kkiandvfkKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLHMADVAVYGVE 540
Cdd:cd05967 468 ---------KFPGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVR 528
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
77-602 |
2.67e-11 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 66.41 E-value: 2.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 77 PLLF---ASMVqrHPDKTALIFEgtDTHWTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKLGVEA 153
Cdd:PLN02479 22 PLWFlerAAVV--HPTRKSVVHG--SVRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 154 ALINTNLRRDALRHCLDTSKARALIFGSE---MASAICEIHA-----SLEPTLsLFCSGswEPSTVPVSTEH-------- 217
Cdd:PLN02479 98 NCVNIRLNAPTIAFLLEHSKSEVVMVDQEfftLAEEALKILAekkksSFKPPL-LIVIG--DPTCDPKSLQYalgkgaie 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 218 LDPLLEDAPKHLPSHPDKGFTDKLFYIYTSGTTGLPKAAIVVHSRYYRMA--SLVYYGFrmrPDDIVYD-CLPLYHSAGN 294
Cdd:PLN02479 175 YEKFLETGDPEFAWKPPADEWQSIALGYTSGTTASPKGVVLHHRGAYLMAlsNALIWGM---NEGAVYLwTLPMFHCNGW 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 295 IVGIGQCLLHGMTVVIRKkFSASRFWDDCIKYNCTIVQYIGELCRYLLNQPPREA--ESRHKVR-MALGNGLRQSIWTDF 371
Cdd:PLN02479 252 CFTWTLAALCGTNICLRQ-VTAKAIYSAIANYGVTHFCAAPVVLNTIVNAPKSETilPLPRVVHvMTAGAAPPPSVLFAM 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 372 SSR-FhipQVAEFYGATEcncSLGnfDSRVgaCGFNSRILSFVyPIRLVRVNE---------DTMELIRGPDGVCIPCQP 441
Cdd:PLN02479 331 SEKgF---RVTHTYGLSE---TYG--PSTV--CAWKPEWDSLP-PEEQARLNArqgvryiglEGLDVVDTKTMKPVPADG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 442 GQPGQLV--GRIIQQdplrrfdGYL-NQGANNKKIANDVFKKGDQAYLTGDvlvmdelGYLYFRDRTGDTFRWKGENVST 518
Cdd:PLN02479 400 KTMGEIVmrGNMVMK-------GYLkNPKANEEAFANGWFHSGDLGVKHPD-------GYIEIKDRSKDIIISGGENISS 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 519 TEVEGTLSRllHMADVAVYGVEVPGTEGRAGMAAVASPISNCDLESFAQTL-------KKELPLYARPIFLRFLPeLHKT 591
Cdd:PLN02479 466 LEVENVVYT--HPAVLEASVVARPDERWGESPCAFVTLKPGVDKSDEAALAedimkfcRERLPAYWVPKSVVFGP-LPKT 542
|
570
....*....|.
gi 45597453 592 GTFKFQKTELR 602
Cdd:PLN02479 543 ATGKIQKHVLR 553
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
83-389 |
4.76e-11 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 65.69 E-value: 4.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 83 MVQRHPDKTALIFEGT---------DTHwTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKLGVEA 153
Cdd:PRK09274 15 AAQERPDQLAVAVPGGrgadgklayDEL-SFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGAVP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 154 ALINTNLRRDALRHCLDTSKARALIfGSEMASAICEIHASLEPTL-SLFCSG---SWEPSTvpvstehLDPLLEDAPKHL 229
Cdd:PRK09274 94 VLVDPGMGIKNLKQCLAEAQPDAFI-GIPKAHLARRLFGWGKPSVrRLVTVGgrlLWGGTT-------LATLLRDGAAAP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 230 PSHPDKGFTDKLFYIYTSGTTGLPKAAIVVHSRYYRMASLVYYGFRMRPDDIVYDCLPLYhsagniVGIGQCLlhGMTVV 309
Cdd:PRK09274 166 FPMADLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEIDLPTFPLF------ALFGPAL--GMTSV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 310 I-------------RKKFSASRfwddciKYNCTIV----QYIGELCRYLLNQPpreaesrHK---VRMALGNGLRQSIWT 369
Cdd:PRK09274 238 IpdmdptrpatvdpAKLFAAIE------RYGVTNLfgspALLERLGRYGEANG-------IKlpsLRRVISAGAPVPIAV 304
|
330 340
....*....|....*....|....*
gi 45597453 370 dfSSRFH--IPQVAEF---YGATEC 389
Cdd:PRK09274 305 --IERFRamLPPDAEIltpYGATEA 327
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
103-603 |
5.98e-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: 5.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 103 TFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALRHCLDTSKAralifgsE 182
Cdd:cd05974 2 SFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRDRVDRGGA-------V 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 183 MASAICEIHASleptlslfcsgswepstvpvstehlDPLLedapkhlpshpdkgftdklFYiYTSGTTGLPKaaIVVHS- 261
Cdd:cd05974 75 YAAVDENTHAD-------------------------DPML-------------------LY-FTSGTTSKPK--LVEHTh 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 262 RYYRMASL-VYYGFRMRPDDIVYDClplyHSAGNIVGIGQCLLH----GMTVVI--RKKFSASRFWDDCIKYNCTIVQYI 334
Cdd:cd05974 108 RSYPVGHLsTMYWIGLKPGDVHWNI----SSPGWAKHAWSCFFApwnaGATVFLfnYARFDAKRVLAALVRYGVTTLCAP 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 335 GELCRYLLNQPPREAESRHKVRMALGNGLRQSIWTDFSSRFHIpQVAEFYGATECNCSLGNFDSRVGACGFNSRilsfvy 414
Cdd:cd05974 184 PTVWRMLIQQDLASFDVKLREVVGAGEPLNPEVIEQVRRAWGL-TIRDGYGQTETTALVGNSPGQPVKAGSMGR------ 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 415 PIRLVRVNedtmelIRGPDGvcipcQPGQPGQLVGRIIQQDPLRRFDGYLNqgaNNKKIANDVfkkGDQAYLTGDVLVMD 494
Cdd:cd05974 257 PLPGYRVA------LLDPDG-----APATEGEVALDLGDTRPVGLMKGYAG---DPDKTAHAM---RGGYYRTGDIAMRD 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 495 ELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLHMADVAVygVEVPGTEGRA------GMAAVASPISNCDLESFAQT 568
Cdd:cd05974 320 EDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAV--VPSPDPVRLSvpkafiVLRAGYEPSPETALEIFRFS 397
|
490 500 510
....*....|....*....|....*....|....*
gi 45597453 569 LKKELPlYARPIFLRFLpELHKTGTFKFQKTELRK 603
Cdd:cd05974 398 RERLAP-YKRIRRLEFA-ELPKTISGKIRRVELRR 430
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
79-601 |
8.43e-11 |
|
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: 64.65 E-value: 8.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 79 LFASMVQRHPDKTALIFEgtDTHWTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKLGVEAALINT 158
Cdd:cd12115 4 LVEAQAARTPDAIALVCG--DESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 159 NLRRDALRHCLDTSKARALIFGSemasaiceihasleptlslfcsgswepstvpvstehldplledapkhlpshpdkgfT 238
Cdd:cd12115 82 AYPPERLRFILEDAQARLVLTDP--------------------------------------------------------D 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 239 DKLFYIYTSGTTGLPKAAIVVHSR---YYRMASLVYYGFRMR----PDDIVYDcLPLYHSAGNivgigqcLLHGMTVVIR 311
Cdd:cd12115 106 DLAYVIYTSGSTGRPKGVAIEHRNaaaFLQWAAAAFSAEELAgvlaSTSICFD-LSVFELFGP-------LATGGKVVLA 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 312 KkfSASRFWDDCIKYNCTIVQYIGELCRYLLNQPPREAESRhKVRMAlGNGLRQSIWTDFSSRFHIPQVAEFYGATECN- 390
Cdd:cd12115 178 D--NVLALPDLPAAAEVTLINTVPSAAAELLRHDALPASVR-VVNLA-GEPLPRDLVQRLYARLQVERVVNLYGPSEDTt 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 391 ----CSLGNFDSRVGACGFNsrilsfVYPIRlVRVNEDTMElirgpdgvciPCQPGQPGQLvgrIIQQDPLRRfdGYLNQ 466
Cdd:cd12115 254 ystvAPVPPGASGEVSIGRP------LANTQ-AYVLDRALQ----------PVPLGVPGEL---YIGGAGVAR--GYLGR 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 467 -GANNKKIANDVFKKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLHMADVAVYGVEVPGTE 545
Cdd:cd12115 312 pGLTAERFLPDPFGPGARLYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGE 391
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 45597453 546 GRAGMAAVASPISNCDLESFAQTLKKELPLYARPIFLRFLPELHKTGTFKFQKTEL 601
Cdd:cd12115 392 RRLVAYIVAEPGAAGLVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
79-586 |
8.44e-11 |
|
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341242 [Multi-domain] Cd Length: 481 Bit Score: 64.49 E-value: 8.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 79 LFASMVQRHPDKTALifEGTDTHWTFRQLDEYSSSVANFLQARGLASGNVVALFMENrnefvGLWLGMAKLGVeaalint 158
Cdd:cd05918 4 LIEERARSQPDAPAV--CAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEK-----SKWAVVAMLAV------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 159 nlrrdalrhcldtSKARAlifgsemasAICeihaSLEPTLslfcsgswepstvPVstEHLDPLLED--APKHLPSHPDkg 236
Cdd:cd05918 70 -------------LKAGG---------AFV----PLDPSH-------------PL--QRLQEILQDtgAKVVLTSSPS-- 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 237 ftDKLFYIYTSGTTGLPKAAIVVHSRYyrMASLVYYG--FRMRPDDIVYDcLPLYH---SAGNIVGIgqcLLHGMTVVIr 311
Cdd:cd05918 107 --DAAYVIFTSGSTGKPKGVVIEHRAL--STSALAHGraLGLTSESRVLQ-FASYTfdvSILEIFTT---LAAGGCLCI- 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 312 kkfsASRfwDDCI--------KYNCTIVQYIGELCRyLLNqpPREAESrhkVR-MALGnG--LRQSIWTDFSSRfhiPQV 380
Cdd:cd05918 178 ----PSE--EDRLndlagfinRLRVTWAFLTPSVAR-LLD--PEDVPS---LRtLVLG-GeaLTQSDVDTWADR---VRL 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 381 AEFYGATEC--NCSLGNFDSrvgacGFNSRILSFVYPIRLVRVNEDTMElirgpdgvcIPCQPGQPGQLV--GRIIQQdp 456
Cdd:cd05918 242 INAYGPAECtiAATVSPVVP-----STDPRNIGRPLGATCWVVDPDNHD---------RLVPIGAVGELLieGPILAR-- 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 457 lrrfdGYLNqgaNNKKIA-----------NDVFKKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTL 525
Cdd:cd05918 306 -----GYLN---DPEKTAaafiedpawlkQEGSGRGRRLYRTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHL 377
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 526 SRLLHMADVAVYGVEVPGTEGRAGM--AAVASPISNC--------------DLESFAQTLKKE----LPLYARP---IFL 582
Cdd:cd05918 378 RQSLPGAKEVVVEVVKPKDGSSSPQlvAFVVLDGSSSgsgdgdslflepsdEFRALVAELRSKlrqrLPSYMVPsvfLPL 457
|
....
gi 45597453 583 RFLP 586
Cdd:cd05918 458 SHLP 461
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
79-280 |
1.37e-10 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 64.80 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 79 LFASMVQRHPDKTALIFEGTdtHWTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKLGVEAALINT 158
Cdd:PRK05691 2193 LFAAQAARTPQAPALTFAGQ--TLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDP 2270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 159 NLRRDALRHCLDTSKARALIFGSEMASAICEIHASLeptlSLFCSGSWEPSTVPVSTEHLDPLledapkHLPSHpdkgft 238
Cdd:PRK05691 2271 EYPLERLHYMIEDSGIGLLLSDRALFEALGELPAGV----ARWCLEDDAAALAAYSDAPLPFL------SLPQH------ 2334
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 45597453 239 dKLFYIYTSGTTGLPKAAIVVHSRYYRMASLVYYGFRMRPDD 280
Cdd:PRK05691 2335 -QAYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIERFGMRADD 2375
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
104-545 |
2.10e-10 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 63.49 E-value: 2.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 104 FRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKLG-VEAAL-INTNL-RRDA----LRHCLDTSKARA 176
Cdd:PRK09192 52 YQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGlVPVPLpLPMGFgGRESyiaqLRGMLASAQPAA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 177 LIFGSEMASAICEIHASLEPTLslfcSGSWepstvpvstEHLDpLLEDAPKHLPShPDKgftDKLFYI-YTSGTTGLPKA 255
Cdd:PRK09192 132 IITPDELLPWVNEATHGNPLLH----VLSH---------AWFK-ALPEADVALPR-PTP---DDIAYLqYSSGSTRFPRG 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 256 AIVVHSRYyrMASL---VYYGFRMRPDDIVYDCLPLYHSAGnIVGigqCLLHGMTVVIRKKFSASR-F------WDDCIK 325
Cdd:PRK09192 194 VIITHRAL--MANLraiSHDGLKVRPGDRCVSWLPFYHDMG-LVG---FLLTPVATQLSVDYLPTRdFarrplqWLDLIS 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 326 YN-CTIV--QYIG-ELCryllnqpPREAESRHKVRMAL------GNG---LRQSIWTDFSSRFhipQVAEF--------Y 384
Cdd:PRK09192 268 RNrGTISysPPFGyELC-------ARRVNSKDLAELDLscwrvaGIGadmIRPDVLHQFAEAF---APAGFddkafmpsY 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 385 GATEcncslgnfdsrvgacgfNSRILSFVYP---IRLVRVNEDTMEL------------------------------IRG 431
Cdd:PRK09192 338 GLAE-----------------ATLAVSFSPLgsgIVVEEVDRDRLEYqgkavapgaetrrvrtfvncgkalpgheieIRN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 432 PDGVCIpcqpgqPGQLVGRIIQQDP-LRRfdGYLNQGANNKKIANDvfkkgdqAYL-TGDVLVMDElGYLYFRDRTGDTF 509
Cdd:PRK09192 401 EAGMPL------PERVVGHICVRGPsLMS--GYFRDEESQDVLAAD-------GWLdTGDLGYLLD-GYLYITGRAKDLI 464
|
490 500 510
....*....|....*....|....*....|....*...
gi 45597453 510 RWKGENVSTTEVEGTLSRL--LHMADVAVYGVEVPGTE 545
Cdd:PRK09192 465 IINGRNIWPQDIEWIAEQEpeLRSGDAAAFSIAQENGE 502
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
88-601 |
3.79e-10 |
|
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: 62.48 E-value: 3.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 88 PDKTALIFEgtDTHWTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKLGveaalintnlrrdalrh 167
Cdd:cd17650 1 PDAIAVSDA--TRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAG----------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 168 cldtskaralifgsemasaiceihasleptlslfcsGSWEPSTVPVSTEHLDPLLEDA-PKHLPSHPDkgftDKLFYIYT 246
Cdd:cd17650 62 ------------------------------------GAYVPIDPDYPAERLQYMLEDSgAKLLLTQPE----DLAYVIYT 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 247 SGTTGLPKAAIVVHSRYYRMaslvYYGFRmrpDDIVYDCLPLYH----------SAGNIVgigQCLLHGMTVVI---RKK 313
Cdd:cd17650 102 SGTTGKPKGVMVEHRNVAHA----AHAWR---REYELDSFPVRLlqmasfsfdvFAGDFA---RSLLNGGTLVIcpdEVK 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 314 FSASRFWDDCIKYNCTIVQYIGELCRYLLNQPPREAESRHKVR-MALGNGLRQSIW-TDFSSRF-HIPQVAEFYGATECN 390
Cdd:cd17650 172 LDPAALYDLILKSRITLMESTPALIRPVMAYVYRNGLDLSAMRlLIVGSDGCKAQDfKTLAARFgQGMRIINSYGVTEAT 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 391 CSLGNFD-SRVGACGfnSRILSFVYPIRLVR--VNEDTMELIrgPDGVCIPCQPGQPGqlVGRiiqqdplrrfdGYLNQG 467
Cdd:cd17650 252 IDSTYYEeGRDPLGD--SANVPIGRPLPNTAmyVLDERLQPQ--PVGVAGELYIGGAG--VAR-----------GYLNRP 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 468 ANNK-KIANDVFKKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLHMADVAVYGVEVPGteG 546
Cdd:cd17650 315 ELTAeRFVENPFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVREDKG--G 392
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 45597453 547 RAGMAAVASPISNCDLESFAQTLKKELPLYARPIFLRFLPELHKTGTFKFQKTEL 601
Cdd:cd17650 393 EARLCAYVVAAATLNTAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
244-542 |
2.85e-09 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 60.32 E-value: 2.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 244 IYTSGTTGLPKAaiVVHSRYYRMA-----SLVyygFRMRPDDIVYDCLPLYHSAGNIVGIGQCLLHGMTVV--------- 309
Cdd:PRK08633 788 IFSSGSEGEPKG--VMLSHHNILSnieqiSDV---FNLRNDDVILSSLPFFHSFGLTVTLWLPLLEGIKVVyhpdptdal 862
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 310 -IRKKfsasrfwddCIKYNCTIVQYIGELCRYLLNQPPREAESRHKVRMALGNG--LRQSIWTDFSSRFHIPQVaEFYGA 386
Cdd:PRK08633 863 gIAKL---------VAKHRATILLGTPTFLRLYLRNKKLHPLMFASLRLVVAGAekLKPEVADAFEEKFGIRIL-EGYGA 932
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 387 TECN----CSLGNF---------DSRVGACG-----FNSRIlsfvypirlvrVNEDTMElirgpdgvciPCQPGQPGQLV 448
Cdd:PRK08633 933 TETSpvasVNLPDVlaadfkrqtGSKEGSVGmplpgVAVRI-----------VDPETFE----------ELPPGEDGLIL 991
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 449 GRIIQqdplrRFDGYLNQGANNKKIANDVFKKGdqAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRL 528
Cdd:PRK08633 992 IGGPQ-----VMKGYLGDPEKTAEVIKDIDGIG--WYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAKA 1064
|
330
....*....|....
gi 45597453 529 LHMADVAVYGVEVP 542
Cdd:PRK08633 1065 LGGEEVVFAVTAVP 1078
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
88-595 |
4.13e-09 |
|
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: 59.23 E-value: 4.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 88 PDKTALIFEgtDTHWTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALRH 167
Cdd:cd12116 1 PDATAVRDD--DRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 168 CLDTSKARALIFGSEMASAIceihasleptlslfcsgswePSTVPVStehldPLLEDAPKHLPSHPDKGFT-DKLFY-IY 245
Cdd:cd12116 79 ILEDAEPALVLTDDALPDRL--------------------PAGLPVL-----LLALAAAAAAPAAPRTPVSpDDLAYvIY 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 246 TSGTTGLPKAAIVVHsryyrmASLVYY------GFRMRPDD-------IVYDC------LPlyhsagnivgigqcLLHGM 306
Cdd:cd12116 134 TSGSTGRPKGVVVSH------RNLVNFlhsmreRLGLGPGDrllavttYAFDIsllellLP--------------LLAGA 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 307 TVVIRKK---FSASRFWDDCIKYNCTIVQYIGELCRYLLNQPPREAESrhkVRMALGNglrQSIWTDFSSRF--HIPQVA 381
Cdd:cd12116 194 RVVIAPRetqRDPEALARLIEAHSITVMQATPATWRMLLDAGWQGRAG---LTALCGG---EALPPDLAARLlsRVGSLW 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 382 EFYGATEcncslgnfdSRVGACGfnSRILSFVYPIRLVRVNEDTMELIRGPDGVCIPcqPGQPGQLvgrIIQQDPLRRfd 461
Cdd:cd12116 268 NLYGPTE---------TTIWSTA--ARVTAAAGPIPIGRPLANTQVYVLDAALRPVP--PGVPGEL---YIGGDGVAQ-- 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 462 GYLNQGANNKK--IANDVFKKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLHMADVAVYGV 539
Cdd:cd12116 330 GYLGRPALTAErfVPDPFAGPGSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVR 409
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 45597453 540 EVPGTEGRAGMAAVASPISnCDLESFAQTLKKELPLYARPIFLRFLPELHKTGTFK 595
Cdd:cd12116 410 EDGGDRRLVAYVVLKAGAA-PDAAALRAHLRATLPAYMVPSAFVRLDALPLTANGK 464
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
70-604 |
5.60e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 59.01 E-value: 5.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 70 LQERKTVPLLFASMVQRHPDKTAliFEGTDTHWTFRQLDEYSSSVANFLQAR-GLASGNVVALFMENRNEFVGLWLGMAK 148
Cdd:PRK05677 20 PDEYPNIQAVLKQSCQRFADKPA--FSNLGKTLTYGELYKLSGAFAAWLQQHtDLKPGDRIAVQLPNVLQYPVAVFGAMR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 149 LGVeaALINTNLRRDA--LRHCLDTSKARALIFGSEMAS--------------AICEIHASLEPTLSLFCSGSWE----- 207
Cdd:PRK05677 98 AGL--IVVNTNPLYTAreMEHQFNDSGAKALVCLANMAHlaekvlpktgvkhvIVTEVADMLPPLKRLLINAVVKhvkkm 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 208 ------PSTVP----VSTEHLDPLLEDAPkhlpsHPDkgftDKLFYIYTSGTTGLPKAAIVVHSRYYR--------MASL 269
Cdd:PRK05677 176 vpayhlPQAVKfndaLAKGAGQPVTEANP-----QAD----DVAVLQYTGGTTGVAKGAMLTHRNLVAnmlqcralMGSN 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 270 VYYGFrmrpdDIVYDCLPLYH--------SAGNIVGIGQCL------LHGMTVVIRK-KFSAsrFwddcIKYNCTIVQyi 334
Cdd:PRK05677 247 LNEGC-----EILIAPLPLYHiyaftfhcMAMMLIGNHNILisnprdLPAMVKELGKwKFSG--F----VGLNTLFVA-- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 335 geLCRyllNQPPREAE-SRHKVRMALGNGLRQSI---WTDFSSrfhiPQVAEFYGATEcncslgnfdsrvgacgfNSRIL 410
Cdd:PRK05677 314 --LCN---NEAFRKLDfSALKLTLSGGMALQLATaerWKEVTG----CAICEGYGMTE-----------------TSPVV 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 411 SfVYPIRLVRVNE------DTMELIRGPDGVCIPCqpGQPGQLVGRIIQQdplrrFDGYL-NQGANNKKIANDVFKKgdq 483
Cdd:PRK05677 368 S-VNPSQAIQVGTigipvpSTLCKVIDDDGNELPL--GEVGELCVKGPQV-----MKGYWqRPEATDEILDSDGWLK--- 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 484 aylTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLHMADVAVYGVEVPGTEGRAGMAAVASPISNCDLE 563
Cdd:PRK05677 437 ---TGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIKVFVVVKPGETLTKE 513
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 45597453 564 SFAQTLKKELPLYARPIFLRFLPELHKTGTFKFQKTELRKE 604
Cdd:PRK05677 514 QVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRRELRDE 554
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
228-605 |
2.66e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 56.54 E-value: 2.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 228 HLPSHPDKGFTdkLFYIYTSGTTGLPKAaiVVHSRYYRMASL--VYYGFRMRPDDIVYDCLPLYHSAGNIVGIGQCLLHG 305
Cdd:PRK07787 120 HRYPEPDPDAP--ALIVYTSGTTGPPKG--VVLSRRAIAADLdaLAEAWQWTADDVLVHGLPLFHVHGLVLGVLGPLRIG 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 306 MTVVIRKKFSASRFWDDCiKYNCTIvqYIGELCRYL-LNQPPREAESRHKVRMaLGNGlrqsiwtdfSSRFHIP------ 378
Cdd:PRK07787 196 NRFVHTGRPTPEAYAQAL-SEGGTL--YFGVPTVWSrIAADPEAARALRGARL-LVSG---------SAALPVPvfdrla 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 379 -----QVAEFYGATEC--NCS-LGNFDSRVGACGFnsrilsfvyPIRLVRVNedtmelIRGPDGVCIPCQpgqpGQLVGR 450
Cdd:PRK07787 263 altghRPVERYGMTETliTLStRADGERRPGWVGL---------PLAGVETR------LVDEDGGPVPHD----GETVGE 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 451 IIQQDPLrRFDGYLNQGANNKkianDVFkKGDQAYLTGDVLVMDELGYLYF--RDRTgDTFRWKGENVSTTEVEGTLsrL 528
Cdd:PRK07787 324 LQVRGPT-LFDGYLNRPDATA----AAF-TADGWFRTGDVAVVDPDGMHRIvgREST-DLIKSGGYRIGAGEIETAL--L 394
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45597453 529 LH--MADVAVYGVEVPGTEGRagMAAVASPISNCDLESFAQTLKKELPLYARPIFLRFLPELHKTGTFKFQKTELRKEG 605
Cdd:PRK07787 395 GHpgVREAAVVGVPDDDLGQR--IVAYVVGADDVAADELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLLSEG 471
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
85-261 |
3.12e-08 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 56.42 E-value: 3.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 85 QRHPDKTALIFEGTDthWTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLrRDA 164
Cdd:PRK09029 14 QVRPQAIALRLNDEV--LTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQL-PQP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 165 LRHCLDTskaralifgsemasaiceihaSLEPTLSLFCSGSWEPSTVPvsteHLDPLLEDAPKHLPSHPDKGFTdklfYI 244
Cdd:PRK09029 91 LLEELLP---------------------SLTLDFALVLEGENTFSALT----SLHLQLVEGAHAVAWQPQRLAT----MT 141
|
170
....*....|....*..
gi 45597453 245 YTSGTTGLPKAaiVVHS 261
Cdd:PRK09029 142 LTSGSTGLPKA--AVHT 156
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
85-601 |
3.90e-08 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 56.17 E-value: 3.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 85 QRHPDKTALIFEGTDTHWTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRDA 164
Cdd:PRK05857 25 RQQPEAIALRRCDGTSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLPIAA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 165 LRHCLDTSKARALIFGSEmasaiCEIHASLEPTLsLFCSGSWEPSTVPVSTEHLDPLLEDAPKhlpSHPDKGFTDKLFYI 244
Cdd:PRK05857 105 IERFCQITDPAAALVAPG-----SKMASSAVPEA-LHSIPVIAVDIAAVTRESEHSLDAASLA---GNADQGSEDPLAMI 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 245 YTSGTTGLPKAAIVVHSRYYRMASLVY-YGFR---MRPDDIVYDCLPLYHsAGNIVGIGQCLLHGMTVVIRKKFSASR-- 318
Cdd:PRK05857 176 FTSGTTGEPKAVLLANRTFFAVPDILQkEGLNwvtWVVGETTYSPLPATH-IGGLWWILTCLMHGGLCVTGGENTTSLle 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 319 -FWDDCIKYNCTIVQYIGELCRYL----LNQPPreaesrhkVRMaLGNGLRQSIWTDFssRFhIP----QVAEFYGATEC 389
Cdd:PRK05857 255 iLTTNAVATTCLVPTLLSKLVSELksanATVPS--------LRL-VGYGGSRAIAADV--RF-IEatgvRTAQVYGLSET 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 390 NCSLGNFDSRVGACgfnSRI----LSFVYPirlvrvnedTMELIRGPDGVCIPCQP-GQPGQLVGRIIQQDPLRRFdGYL 464
Cdd:PRK05857 323 GCTALCLPTDDGSI---VKIeagaVGRPYP---------GVDVYLAATDGIGPTAPgAGPSASFGTLWIKSPANML-GYW 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 465 NQGANNKKIANDVFKKgdqaylTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLHMADVAVYgvEVPGT 544
Cdd:PRK05857 390 NNPERTAEVLIDGWVN------TGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACY--EIPDE 461
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45597453 545 EGRA--GMAAVASPISNcdlESFAQTLK--------KELPLYARPIFLRFLPELHKTGTFKFQKTEL 601
Cdd:PRK05857 462 EFGAlvGLAVVASAELD---ESAARALKhtiaarfrRESEPMARPSTIVIVTDIPRTQSGKVMRASL 525
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
103-604 |
4.15e-08 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 56.58 E-value: 4.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 103 TFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRD--ALRHcLDTSKARALIFG 180
Cdd:PRK06060 32 THGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDdhALAA-RNTEPALVVTSD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 181 SemasaICEihasleptlslfcsgSWEPSTVPVSTEhldpLLEDAPKHLPSHPDKGFTDKLFY-IYTSGTTGLPKAAIVV 259
Cdd:PRK06060 111 A-----LRD---------------RFQPSRVAEAAE----LMSEAARVAPGGYEPMGGDALAYaTYTSGTTGPPKAAIHR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 260 HSRYYRMA-SLVYYGFRMRPDDIVYDCLPLY--HSAGNIVGI-----GQCLLHGMTVVIRKKFSASRFWDDCIKYNC-TI 330
Cdd:PRK06060 167 HADPLTFVdAMCRKALRLTPEDTGLCSARMYfaYGLGNSVWFplatgGSAVINSAPVTPEAAAILSARFGPSVLYGVpNF 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 331 VQYIGELCryllnqpprEAESRHKVR--MALGNGLRQSIWTDFSSRFHIPQVAEFYGATECNCSLGNF---DSRVGACGf 405
Cdd:PRK06060 247 FARVIDSC---------SPDSFRSLRcvVSAGEALELGLAERLMEFFGGIPILDGIGSTEVGQTFVSNrvdEWRLGTLG- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 406 nsRILSfVYPIRLVrvnedtmelirGPDGVCipCQPGQPGQLVGR---IIQQ-----DPLRRFDGYLNqgannkkiandv 477
Cdd:PRK06060 317 --RVLP-PYEIRVV-----------APDGTT--AGPGVEGDLWVRgpaIAKGywnrpDSPVANEGWLD------------ 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 478 fkkgdqaylTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLHMADVAVYGV-EVPGTEGRAG--MAAVA 554
Cdd:PRK06060 369 ---------TRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVrESTGASTLQAflVATSG 439
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 45597453 555 SPISNCDLESFAQTLKKELPLYARPIFLRFLPELHKTGTFKFQKTELRKE 604
Cdd:PRK06060 440 ATIDGSVMRDLHRGLLNRLSAFKVPHRFAVVDRLPRTPNGKLVRGALRKQ 489
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
79-261 |
4.78e-08 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 56.50 E-value: 4.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 79 LFASMVQRHPDKTALIFegTDTHWTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKLGVEAALINT 158
Cdd:PRK12316 516 LFEEQVERTPEAPALAF--GEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDP 593
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 159 NLRRDALRHCLDTSKARALIFGSEmasaiceihasLEPTLSLfcsgswepstvPVSTEHLDplLEDAPKHLPSHPDKGFT 238
Cdd:PRK12316 594 EYPAERLAYMLEDSGVQLLLSQSH-----------LGRKLPL-----------AAGVQVLD--LDRPAAWLEGYSEENPG 649
|
170 180
....*....|....*....|....*....
gi 45597453 239 -----DKLFY-IYTSGTTGLPKAAIVVHS 261
Cdd:PRK12316 650 telnpENLAYvIYTSGSTGKPKGAGNRHR 678
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
84-330 |
9.86e-08 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 55.15 E-value: 9.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 84 VQRHPDKTALIFEG----TDTHWTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKLGVEAALINTN 159
Cdd:PRK00174 77 LKTRGDKVAIIWEGddpgDSRKITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVVFGG 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 160 LRRDALRHCLDTSKARALIFGSE---------------MASAICEihaSLEPTLSLFCSG---SWEPS--------TVPV 213
Cdd:PRK00174 157 FSAEALADRIIDAGAKLVITADEgvrggkpiplkanvdEALANCP---SVEKVIVVRRTGgdvDWVEGrdlwwhelVAGA 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 214 STEHldplledAPKHLPS-HPdkgftdkLFYIYTSGTTGLPKAaiVVHSR--YyrmasLVY------YGFRMRPDDiVYD 284
Cdd:PRK00174 234 SDEC-------EPEPMDAeDP-------LFILYTSGSTGKPKG--VLHTTggY-----LVYaamtmkYVFDYKDGD-VYW 291
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 285 ClplyhSA--GNIVG-----IGQcLLHGMTVVIrkkF-------SASRFWDDCIKYNCTI 330
Cdd:PRK00174 292 C-----TAdvGWVTGhsyivYGP-LANGATTLM---FegvpnypDPGRFWEVIDKHKVTI 342
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
87-310 |
1.38e-07 |
|
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.
Pssm-ID: 341245 [Multi-domain] Cd Length: 561 Bit Score: 54.75 E-value: 1.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 87 HPDKTALIFEGTDTHW---TFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKLGVEAA-------LI 156
Cdd:cd05921 8 APDRTWLAEREGNGGWrrvTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAApvspaysLM 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 157 NTNLRRdaLRHCLDTSKArALIFGSE---MASAICEIHASLEPTLSLFCSGSWEPSTVPVSTEHLDPLLEDAPKHLPSHP 233
Cdd:cd05921 88 SQDLAK--LKHLFELLKP-GLVFAQDaapFARALAAIFPLGTPLVVSRNAVAGRGAISFAELAATPPTAAVDAAFAAVGP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 234 DkgftDKLFYIYTSGTTGLPKAAIVVHsryyRMASLVY------YGFRMRPDDIVYDCLPLYHSAGNIVGIGQCLLHGMT 307
Cdd:cd05921 165 D----TVAKFLFTSGSTGLPKAVINTQ----RMLCANQamleqtYPFFGEEPPVLVDWLPWNHTFGGNHNFNLVLYNGGT 236
|
...
gi 45597453 308 VVI 310
Cdd:cd05921 237 LYI 239
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
69-296 |
1.51e-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: 54.60 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 69 YLQERKTVPLLFASMVQRHPDKTALIF------EGTDTHWTFRQLDEYSSSVANFLQARGLASGNVVAL-FMENRNEFVG 141
Cdd:cd05906 1 PLHRPEGAPRTLLELLLRAAERGPTKGityidaDGSEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILqFDDNEDFIPA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 142 LW---LGMAKLGVEAALINTNLRRDALRHCLDTSKaralIFGSEMASAICEIHASLEPTLSLFcsgSWEPSTVPVSTEHL 218
Cdd:cd05906 81 FWacvLAGFVPAPLTVPPTYDEPNARLRKLRHIWQ----LLGSPVVLTDAELVAEFAGLETLS---GLPGIRVLSIEELL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45597453 219 DPlleDAPKHLP-SHPDkgftDKLFYIYTSGTTGLPKAAIVVHSRYYRMASLVYYGFRMRPDDIVYDCLPLYHsAGNIV 296
Cdd:cd05906 154 DT---AADHDLPqSRPD----DLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVPLDH-VGGLV 224
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
102-308 |
1.74e-07 |
|
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: 54.35 E-value: 1.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 102 WTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKLGVeaalINTNLRRDALR----HCLDTSKARAL 177
Cdd:cd17641 12 FTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGA----LSLGIYQDSMAeevaYLLNYTGARVV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 178 IFG-SEMASAICEIHASLEPTLSLFcsgSWEPSTVpvsTEHLDPLLEDAPK-------HLPSHPDKG--------FTDKL 241
Cdd:cd17641 88 IAEdEEQVDKLLEIADRIPSVRYVI---YCDPRGM---RKYDDPRLISFEDvvalgraLDRRDPGLYerevaagkGEDVA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45597453 242 FYIYTSGTTGLPKAAIVVHSRYYRM-ASLVYYGFRmRPDDIVYDCLPLYHSAGNIVGIGQCLLHGMTV 308
Cdd:cd17641 162 VLCTTSGTTGKPKLAMLSHGNFLGHcAAYLAADPL-GPGDEYVSVLPLPWIGEQMYSVGQALVCGFIV 228
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
88-282 |
2.28e-07 |
|
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: 53.80 E-value: 2.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 88 PDKTALIFEgtDTHWTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKLGveAALintnlrrdalrh 167
Cdd:cd17652 1 PDAPAVVFG--DETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAG--AAY------------ 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 168 cldtskaralifgsemasaiceihasleptlslfcsgswepstVPVSTEHLDP----LLEDAPKHL----PSHPdkgftd 239
Cdd:cd17652 65 -------------------------------------------LPLDPAYPAEriayMLADARPALllttPDNL------ 95
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 45597453 240 kLFYIYTSGTTGLPKAAIVVHSRYYRMASLVYYGFRMRPDDIV 282
Cdd:cd17652 96 -AYVIYTSGSTGRPKGVVVTHRGLANLAAAQIAAFDVGPGSRV 137
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
520-595 |
2.64e-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: 2.64e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45597453 520 EVEGTLSRLLHMADVAVYGVEVPgTEGRAGMAAVASPISNCDL-ESFAQTLKKELPLYARPIFLRFLPELHKTGTFK 595
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDE-LKGEAPVAFVVLKPGVELLeEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
85-310 |
3.53e-07 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 53.34 E-value: 3.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 85 QRHPDKTALIFEGTDTHW---TFRQLDEYSSSVANFLQARGLASGNVVALFMENRNE-----FVGLWLGMAKLGVEAA-- 154
Cdd:PRK08180 50 QEAPDRVFLAERGADGGWrrlTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEhallaLAAMYAGVPYAPVSPAys 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 155 LINTNLRRdaLRHCLDTSKArALIF---GSEMASAIceiHASLEPTLSLFCSGSWEPSTVPVStehLDPLLEDAP----- 226
Cdd:PRK08180 130 LVSQDFGK--LRHVLELLTP-GLVFaddGAAFARAL---AAVVPADVEVVAVRGAVPGRAATP---FAALLATPPtaavd 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 227 -KHLPSHPD---KgftdklfYIYTSGTTGLPKAAIVVHsryyRM--ASLVYYG-----FRMRPDDIVyDCLPLYHSAGNI 295
Cdd:PRK08180 201 aAHAAVGPDtiaK-------FLFTSGSTGLPKAVINTH----RMlcANQQMLAqtfpfLAEEPPVLV-DWLPWNHTFGGN 268
|
250
....*....|....*
gi 45597453 296 VGIGQCLLHGMTVVI 310
Cdd:PRK08180 269 HNLGIVLYNGGTLYI 283
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
100-292 |
4.10e-07 |
|
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: 52.75 E-value: 4.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 100 THWTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFvgLWLGMAKLGVEAAlintnlrrDALRHCLDTSKARALIF 179
Cdd:cd17640 4 KRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRW--LIADQGIMALGAV--------DVVRGSDSSVEELLYIL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 180 GSEMASAIceihasleptlslfcsgswepstvpvstehldpLLEDAPKHLPShpdkgftdklfYIYTSGTTGLPKAAIVV 259
Cdd:cd17640 74 NHSESVAL---------------------------------VVENDSDDLAT-----------IIYTSGTTGNPKGVMLT 109
|
170 180 190
....*....|....*....|....*....|....
gi 45597453 260 H-SRYYRMASLvYYGFRMRPDDIVYDCLPLYHSA 292
Cdd:cd17640 110 HaNLLHQIRSL-SDIVPPQPGDRFLSILPIWHSY 142
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
75-260 |
6.58e-07 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 52.43 E-value: 6.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 75 TVPLLFASMVQRHPDKTALifeGT-----------------------DTHW-TFRQLDEYSSSVANFLQARGLASGNVVA 130
Cdd:PLN02387 59 TLAALFEQSCKKYSDKRLL---GTrklisrefetssdgrkfeklhlgEYEWiTYGQVFERVCNFASGLVALGHNKEERVA 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 131 LFMENRNEfvglWL----GMAKLGVEAALINTNLRRDALRHCLDTSKARALIFGSEMASAICEIHASLEP---------- 196
Cdd:PLN02387 136 IFADTRAE----WLialqGCFRQNITVVTIYASLGEEALCHSLNETEVTTVICDSKQLKKLIDISSQLETvkrviymdde 211
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45597453 197 ----TLSLFCSGSWEPStvpvSTEHLDPLLEDAPKHlPSHPDKgfTDKLFYIYTSGTTGLPKAAIVVH 260
Cdd:PLN02387 212 gvdsDSSLSGSSNWTVS----SFSEVEKLGKENPVD-PDLPSP--NDIAVIMYTSGSTGLPKGVMMTH 272
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
99-308 |
1.12e-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: 51.45 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 99 DTHW-TFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALRHCLDTSKARAL 177
Cdd:cd17639 2 EYKYmSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECSAI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 178 ifgsemasaiceihasleptlslFCSGSwepstvpvstehldplledapkhlpshPDkgftDKLFYIYTSGTTGLPKAai 257
Cdd:cd17639 82 -----------------------FTDGK---------------------------PD----DLACIMYTSGSTGNPKG-- 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 45597453 258 VVHSRYYRMASLVYYGFR----MRPDDIVYDCLPLYH----SAGNIvgigqCLLHGMTV 308
Cdd:cd17639 106 VMLTHGNLVAGIAGLGDRvpelLGPDDRYLAYLPLAHifelAAENV-----CLYRGGTI 159
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
74-310 |
2.54e-06 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 50.43 E-value: 2.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 74 KTVPLLFASMVQRHPDKTALI-FEGTDTHW---TFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKL 149
Cdd:PRK12582 49 RSIPHLLAKWAAEAPDRPWLAqREPGHGQWrkvTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 150 GVEAA-------LINTNLRRdaLRHCLDTSKARaLIF---GSEMASAICEIHASLEPTLSLFCSGSWEPSTvpvsteHLD 219
Cdd:PRK12582 129 GVPAApvspaysLMSHDHAK--LKHLFDLVKPR-VVFaqsGAPFARALAALDLLDVTVVHVTGPGEGIASI------AFA 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 220 PLLEDAP------KHLPSHPDKgfTDKlfYIYTSGTTGLPKAAIVVHSryyRMASLVYYGFRMRPDD------IVYDCLP 287
Cdd:PRK12582 200 DLAATPPtaavaaAIAAITPDT--VAK--YLFTSGSTGMPKAVINTQR---MMCANIAMQEQLRPREpdppppVSLDWMP 272
|
250 260
....*....|....*....|....
gi 45597453 288 LYH-SAGNIvGIGQCLLHGMTVVI 310
Cdd:PRK12582 273 WNHtMGGNA-NFNGLLWGGGTLYI 295
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
95-261 |
3.59e-06 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 49.97 E-value: 3.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 95 FEGTdTHWTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALRHCLDTSKA 174
Cdd:PTZ00216 116 FNET-RYITYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETEC 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 175 RALIF-GSEMASAICEIHASLEPTLSLFCSGSWEPStvpVSTEHLD-----PLLEDAPKHLPSHPDKGFTDK---LFYIY 245
Cdd:PTZ00216 195 KAIVCnGKNVPNLLRLMKSGGMPNTTIIYLDSLPAS---VDTEGCRlvawtDVVAKGHSAGSHHPLNIPENNddlALIMY 271
|
170
....*....|....*.
gi 45597453 246 TSGTTGLPKAaiVVHS 261
Cdd:PTZ00216 272 TSGTTGDPKG--VMHT 285
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
67-258 |
1.19e-05 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 49.01 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 67 RRYLQERKTVPLlFASMVQRHPDKTALifEGTDTHWTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGM 146
Cdd:PRK05691 3714 RDYPLEQSYVRL-FEAQVAAHPQRIAA--SCLDQQWSYAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLLGMIVGS 3790
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 147 AKLGVEAALINTNLRRDALRHCLDTSKARALIfgsemASAIC--EIHASLEptlSLFCSGS-----WEPSTVPVSTEHlD 219
Cdd:PRK05691 3791 FKAGAGYLPLDPGLPAQRLQRIIELSRTPVLV-----CSAACreQARALLD---ELGCANRprllvWEEVQAGEVASH-N 3861
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 45597453 220 PLLEDAPkhlpshpdkgftDKLFY-IYTSGTTGLPKAAIV 258
Cdd:PRK05691 3862 PGIYSGP------------DNLAYvIYTSGSTGLPKGVMV 3889
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
398-614 |
1.66e-05 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 48.02 E-value: 1.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 398 SRVGACGFNsrilsfVYPIRLVRVNEDTMElirgpdgvciPCQPGQPGQLVgriiqqdplrrFDGYLNQGA------NNK 471
Cdd:PRK10524 408 TRLGSPGVP------MYGYNVKLLNEVTGE----------PCGPNEKGVLV-----------IEGPLPPGCmqtvwgDDD 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 472 KIANDVFKK-GDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLHMADVAVYGVEVPgTEGRAGM 550
Cdd:PRK10524 461 RFVKTYWSLfGRQVYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDA-LKGQVAV 539
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 551 A--------AVASPISNCDLE-SFAQTLKKELPLYARPIFLRFLPELHKTGTFKFqkteLRK------EGFDP---SVVK 612
Cdd:PRK10524 540 AfvvpkdsdSLADREARLALEkEIMALVDSQLGAVARPARVWFVSALPKTRSGKL----LRRaiqaiaEGRDPgdlTTIE 615
|
..
gi 45597453 613 DP 614
Cdd:PRK10524 616 DP 617
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
487-604 |
2.10e-05 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 47.44 E-value: 2.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 487 TGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLHMADVAVYGVEVPGTEGRAGMAAVASPISNCDLESFA 566
Cdd:PRK06018 414 TGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQLKPGETATREEIL 493
|
90 100 110
....*....|....*....|....*....|....*...
gi 45597453 567 QTLKKELPLYARPIFLRFLPELHKTGTFKFQKTELRKE 604
Cdd:PRK06018 494 KYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALREQ 531
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
73-579 |
2.32e-05 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 47.86 E-value: 2.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 73 RKTVPLLFASMVQRHPDKTALIFEGTDThwTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEF-VGLwLGMAKLGV 151
Cdd:PRK05691 1130 QAWLPELLNEQARQTPERIALVWDGGSL--DYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLlVGL-LAILKAGG 1206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 152 EAALINTNLRRDALRHCLDTSKARALIfgsemasaiceIHASLEPTLslfcsgswePSTVPVSTEHLDPL-LEDAPKHLP 230
Cdd:PRK05691 1207 AYVPLDPDYPAERLAYMLADSGVELLL-----------TQSHLLERL---------PQAEGVSAIALDSLhLDSWPSQAP 1266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 231 SHPDKGftDKLFY-IYTSGTTGLPKAAIVVHSRYYRMASLVYYGFRMRPDDIVYDCLPLYHSagniVGIGQC---LLHGM 306
Cdd:PRK05691 1267 GLHLHG--DNLAYvIYTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKAPISFD----VSVWECfwpLITGC 1340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 307 TVVIR---KKFSASRFWDDCIKYNCTIVQYIGELCRYLLNQPprEAESRHKVRM------ALGNGLRQSIwtdfssRFHI 377
Cdd:PRK05691 1341 RLVLAgpgEHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDEP--LAAACTSLRRlfsggeALPAELRNRV------LQRL 1412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 378 PQVA--EFYGATE---------CNCSLGNFdSRVGacgfnsRILSFVypirLVRVNEDTMELIrgpdgvcipcQPGQPGQ 446
Cdd:PRK05691 1413 PQVQlhNRYGPTEtainvthwqCQAEDGER-SPIG------RPLGNV----LCRVLDAELNLL----------PPGVAGE 1471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 447 LVgriIQQDPLRRfdGYLNQGANNKK--IANDVFKKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEgt 524
Cdd:PRK05691 1472 LC---IGGAGLAR--GYLGRPALTAErfVPDPLGEDGARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQ-- 1544
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 45597453 525 lSRLLHMADVAVYGVEVpgTEGRAGMAAV----ASPISNCDLESFAQTLKKELPLYARP 579
Cdd:PRK05691 1545 -ARLLAQPGVAQAAVLV--REGAAGAQLVgyytGEAGQEAEAERLKAALAAELPEYMVP 1600
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
231-522 |
8.22e-05 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 45.89 E-value: 8.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 231 SHPdkgftdkLFYIYTSGTTGLPKAaiVVHSRYYRMASLVYYGFRMRPDDIVYdclpLYHSAGNIVGIG------QCLLH 304
Cdd:PTZ00237 254 SHP-------LYILYTSGTTGNSKA--VVRSNGPHLVGLKYYWRSIIEKDIPT----VVFSHSSIGWVSfhgflyGSLSL 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 305 GMTVV------IRKKFSASRFWDDCIKYNCTIVQYIGELCRYLLNQPPrEAE--------SRHKVRMALGNGLRQSIWTD 370
Cdd:PTZ00237 321 GNTFVmfeggiIKNKHIEDDLWNTIEKHKVTHTLTLPKTIRYLIKTDP-EATiirskydlSNLKEIWCGGEVIEESIPEY 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 371 FSSRFHIpQVAEFYGATECNCSL----GNFDSRVGACGFNSrilSFVYPIRLvrvNEDTMELirgpdgvcipcqpgqPGQ 446
Cdd:PTZ00237 400 IENKLKI-KSSRGYGQTEIGITYlycyGHINIPYNATGVPS---IFIKPSIL---SEDGKEL---------------NVN 457
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45597453 447 LVGRIIQQDPLRrfDGYLNQGANNKKIANDVFKKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVE 522
Cdd:PTZ00237 458 EIGEVAFKLPMP--PSFATTFYKNDEKFKQLFSKFPGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIE 531
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
83-264 |
1.91e-04 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 44.60 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 83 MVQRH--PDKTALIfEGtDTHWTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKLGVeaALINT-- 158
Cdd:PRK10946 30 ILTRHaaSDAIAVI-CG-ERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLGV--APVNAlf 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 159 NLRRDALRHCLDTSKARALI-------FGS-EMASAICEIHASLEPTLSLFCSGswepstvpvsTEHLDPLLEDAPKHLP 230
Cdd:PRK10946 106 SHQRSELNAYASQIEPALLIadrqhalFSDdDFLNTLVAEHSSLRVVLLLNDDG----------EHSLDDAINHPAEDFT 175
|
170 180 190
....*....|....*....|....*....|....*
gi 45597453 231 SHPDKgfTDKL-FYIYTSGTTGLPKAAIVVHSRYY 264
Cdd:PRK10946 176 ATPSP--ADEVaFFQLSGGSTGTPKLIPRTHNDYY 208
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
103-205 |
2.12e-04 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 44.37 E-value: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 103 TFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALRHCLDTSKARALIfgse 182
Cdd:cd05910 4 SFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEAEPDAFI---- 79
|
90 100
....*....|....*....|...
gi 45597453 183 masaicEIHASLEPTLSLFCSGS 205
Cdd:cd05910 80 ------GIPKADEPAAILFTSGS 96
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
238-308 |
2.91e-04 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 44.19 E-value: 2.91e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45597453 238 TDKLFYIYTSGTTGLPKAAIVVH----SRYYRMASLVYYGfrmrPDDIVYDCLPLYHSAGNIVGIGQCLLHGMTV 308
Cdd:PRK06814 793 DDPAVILFTSGSEGTPKGVVLSHrnllANRAQVAARIDFS----PEDKVFNALPVFHSFGLTGGLVLPLLSGVKV 863
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
487-614 |
2.95e-04 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 44.00 E-value: 2.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 487 TGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLHMADVAVYGVEVPGTEGRAGMAAVASPISNCDLESfA 566
Cdd:PRK05620 434 TGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLAVTVLAPGIEPTRET-A 512
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 45597453 567 QTLKKEL----PLYARPIFLRFLPELHKTGTFKFQKTELRK---EG-FDPSVVKDP 614
Cdd:PRK05620 513 ERLRDQLrdrlPNWMLPEYWTFVDEIDKTSVGKFDKKDLRQhlaDGdFEIIKLKGP 568
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
244-308 |
5.97e-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: 42.73 E-value: 5.97e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45597453 244 IYTSGTTGLPKAAIVVHSRYYRMASLVYYGFRMRPDD----IVYDCLPLYHSAGNIVGIGQCLLHGMTV 308
Cdd:cd05933 156 IYTSGTTGMPKGVMLSHDNITWTAKAASQHMDLRPATvgqeSVVSYLPLSHIAAQILDIWLPIKVGGQV 224
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
482-604 |
1.16e-03 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 42.00 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 482 DQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLHMADVAVYGVEVPGTEGRAGMAAVASPISNCD 561
Cdd:PRK07008 408 DGWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLVVVKRPGAEVT 487
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 45597453 562 LESFAQTLKKELPLYARPIFLRFLPELHKTGTFKFQKTELRKE 604
Cdd:PRK07008 488 REELLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKLREQ 530
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
438-536 |
1.27e-03 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 41.90 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 438 PCQPGQPGQLVGRiiqqDPLRrFDGYLNQGANNKKiandVFKKgDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVS 517
Cdd:PRK10946 374 PLPQGEVGRLMTR----GPYT-FRGYYKSPQHNAS----AFDA-NGFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIA 443
|
90 100
....*....|....*....|..
gi 45597453 518 TTEVEGTLSR---LLHMADVAV 536
Cdd:PRK10946 444 AEEIENLLLRhpaVIHAALVSM 465
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
87-205 |
1.54e-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: 41.35 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 87 HPDKTALIFEGT-----DTHWTFRQLDEYSSSVANFLQARGLASGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLR 161
Cdd:cd17647 1 FPERTCVVETPSlnsskTRSFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYP 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 45597453 162 RDALRHCLDTSKARALIfGSEMASAIceIHASLEPTLSlFCSGS 205
Cdd:cd17647 81 PARQNIYLGVAKPRGLI-VIRAAGVV--VGPDSNPTLS-FTSGS 120
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
477-605 |
2.63e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 40.79 E-value: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 477 VFKKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLHMADVAVYGVEVPGTEGRAGMAAVA-S 555
Cdd:PRK08308 285 VVKMGDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVIShE 364
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 45597453 556 PISNCDLESFAQtlkKELPLYARPIFLRFLPELHKTGTFKFQKTELRKEG 605
Cdd:PRK08308 365 EIDPVQLREWCI---QHLAPYQVPHEIESVTEIPKNANGKVSRKLLELGE 411
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
229-522 |
3.35e-03 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 40.46 E-value: 3.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 229 LPSHPDkgftDKLFYIYTSGTTGLPKAaiVVHSRyyrmASLVYYGFRMR------PDDIVYDCLPLYHSAGNIVGIGQCL 302
Cdd:PRK08043 360 VKQQPE----DAALILFTSGSEGHPKG--VVHSH----KSLLANVEQIKtiadftPNDRFMSALPLFHSFGLTVGLFTPL 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 303 LHGMTVVIRKKFSASRFWDDCIkY--NCTIV----QYIGELCRYLlnQPPREAESRHKVRMA--LGNGLRQsIWTDfssR 374
Cdd:PRK08043 430 LTGAEVFLYPSPLHYRIVPELV-YdrNCTVLfgtsTFLGNYARFA--NPYDFARLRYVVAGAekLQESTKQ-LWQD---K 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 375 FHIpQVAEFYGATEC------NCSLGnfdSRVGACGfnsRILSfvypirlvrvnedtmelirGPDGVCIPCqPG--QPG- 445
Cdd:PRK08043 503 FGL-RILEGYGVTECapvvsiNVPMA---AKPGTVG---RILP-------------------GMDARLLSV-PGieQGGr 555
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 446 -QLVGRIIQQdplrrfdGYL---NQGANNKKIANDVFKKGDQA-YLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTE 520
Cdd:PRK08043 556 lQLKGPNIMN-------GYLrveKPGVLEVPTAENARGEMERGwYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEM 628
|
..
gi 45597453 521 VE 522
Cdd:PRK08043 629 VE 630
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
239-538 |
4.01e-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: 40.28 E-value: 4.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 239 DKLFYI-YTSGTTGLPKAAIVVHSryyRMASLV-------YYGFRMRPDDIVYDCLPLYHSAGNIVgIGQCLLHGM---- 306
Cdd:cd05927 114 EDLATIcYTSGTTGNPKGVMLTHG---NIVSNVagvfkilEILNKINPTDVYISYLPLAHIFERVV-EALFLYHGAkigf 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 307 -----------------TVVIrkkfSASRFWD---DCIKYNctiVQYIGELCRYLLNqppreAESRHKV-RMALGNGLRQ 365
Cdd:cd05927 190 ysgdirlllddikalkpTVFP----GVPRVLNriyDKIFNK---VQAKGPLKRKLFN-----FALNYKLaELRSGVVRAS 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 366 SIWTD--FSS---------RFHI-------PQVAEF------------YGATECN--CSLGN-FDSRVGACGfnsRILSF 412
Cdd:cd05927 258 PFWDKlvFNKikqalggnvRLMLtgsaplsPEVLEFlrvalgcpvlegYGQTECTagATLTLpGDTSVGHVG---GPLPC 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45597453 413 VYpIRLVRVNEdtME-LIRGPDG---VCIpcqpgqPGQLVgriiqqdplrrFDGYLNqgaNNKKIANDVFKKGdqAYLTG 488
Cdd:cd05927 335 AE-VKLVDVPE--MNyDAKDPNPrgeVCI------RGPNV-----------FSGYYK---DPEKTAEALDEDG--WLHTG 389
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 45597453 489 DVLVMDELGYLYFRDRTGDTFRW-KGENVSTTEVEGTLSRLLHMADVAVYG 538
Cdd:cd05927 390 DIGEWLPNGTLKIIDRKKNIFKLsQGEYVAPEKIENIYARSPFVAQIFVYG 440
|
|
| |
