|
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: 941.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 99 NTHWTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALRHCLDTSKARALI 178
Cdd:cd05939 1 DRHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 179 FgsemasavyeiqaildptltlfcsgswepstvpantEHLDPLLEDAPKHLPSIPDKGFTDKLFYIYTSGTTGLPKAAIV 258
Cdd:cd05939 81 F------------------------------------NLLDPLLTQSSTEPPSQDDVNFRDKLFYIYTSGTTGLPKAAVI 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 259 VHSRYYRMAALVYYGFRMRPDDIVYDCLPLYHSAGNIVGIGQCVLHGMTVVIRKKFSASRFWDDCIKYNCTIVQYIGELC 338
Cdd:cd05939 125 VHSRYYRIAAGAYYAFGMRPEDVVYDCLPLYHSAGGIMGVGQALLHGSTVVIRKKFSASNFWDDCVKYNCTIVQYIGEIC 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 339 RYLLNQPPREAESRHKVRMALGNGLRQSIWTDFSSRFHIPQVAEFYGATECNCSLGNFDSQVGACGFNSRILSFVYPIRL 418
Cdd:cd05939 205 RYLLAQPPSEEEQKHNVRLAVGNGLRPQIWEQFVRRFGIPQIGEFYGATEGNSSLVNIDNHVGACGFNSRILPSVYPIRL 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 419 VRVNEDTMELIRGPDGVCIPCQPGQPGQLVGRIIQQDPLRRFDGYLNQGANNKKIASDVFKKGDQAYLTGDVLVMDELGY 498
Cdd:cd05939 285 IKVDEDTGELIRDSDGLCIPCQPGEPGLLVGKIIQNDPLRRFDGYVNEGATNKKIARDVFKKGDSAFLSGDVLVMDELGY 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 499 LYFRDRTGDTFRWKGENVSTTEVEGTLSRLLQMADVAVYGVEVPGAEGRAGMAAVASPTSNCDLESFAQTLKKELPLYAR 578
Cdd:cd05939 365 LYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVYGVEVPGVEGRAGMAAIVDPERKVDLDRFSAVLAKSLPPYAR 444
|
490 500 510
....*....|....*....|....*....|
gi 291084711 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: 707.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 75 TVPLLFASVVRRHPDKTALIFEGTntHWTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKLGVEAA 154
Cdd:PRK08279 38 SLGDVFEEAAARHPDRPALLFEDQ--SISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 155 LINTNLRRDALRHCLDTSKARALIFGSEMASAVYEIQAILDPTLTLFCSGSWEPSTVPANTEhLDPLLEDAPKHLPSIPD 234
Cdd:PRK08279 116 LLNTQQRGAVLAHSLNLVDAKHLIVGEELVEAFEEARADLARPPRLWVAGGDTLDDPEGYED-LAAAAAGAPTTNPASRS 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 235 KGFT-DKLFYIYTSGTTGLPKAAIVVHSRYYRMAAlvyyGF----RMRPDDIVYDCLPLYHSAGNIVGIGQCVLHGMTVV 309
Cdd:PRK08279 195 GVTAkDTAFYIYTSGTTGLPKAAVMSHMRWLKAMG----GFggllRLTPDDVLYCCLPLYHNTGGTVAWSSVLAAGATLA 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 310 IRKKFSASRFWDDCIKYNCTIVQYIGELCRYLLNQPPREAESRHKVRMALGNGLRQSIWTDFSSRFHIPQVAEFYGATEC 389
Cdd:PRK08279 271 LRRKFSASRFWDDVRRYRATAFQYIGELCRYLLNQPPKPTDRDHRLRLMIGNGLRPDIWDEFQQRFGIPRILEFYAASEG 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 390 NCSLGNFDSQVGACGFNSRILSfvYPIRLVRVNEDTMELIRGPDGVCIPCQPGQPGQLVGRIiqqDPLRRFDGYLNQGAN 469
Cdd:PRK08279 351 NVGFINVFNFDGTVGRVPLWLA--HPYAIVKYDVDTGEPVRDADGRCIKVKPGEVGLLIGRI---TDRGPFDGYTDPEAS 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 470 NKKIASDVFKKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLQMADVAVYGVEVPGAEGRAG 549
Cdd:PRK08279 426 EKKILRDVFKKGDAWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVATTEVENALSGFPGVEEAVVYGVEVPGTDGRAG 505
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 550 MAA-VASPTSNCDLESFAQTLKKELPLYARPIFLRFLPELHKTGTFKFQKTELRKEGFDPSVVKDPLFYLDARTGCYVAL 628
Cdd:PRK08279 506 MAAiVLADGAEFDLAALAAHLYERLPAYAVPLFVRLVPELETTGTFKYRKVDLRKEGFDPSKVDDPLYVLDPGSGGYVPL 585
|
570
....*....|....*
gi 291084711 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 ... |
102-608 |
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: 695.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 102 WTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALRHCLDTSKARALIFgs 181
Cdd:cd05940 4 LTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLVV-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 182 emasavyeiqaildptltlfcsgswepstvpantehldplledapkhlpsipdkgftDKLFYIYTSGTTGLPKAAIVVHS 261
Cdd:cd05940 82 ---------------------------------------------------------DAALYIYTSGTTGLPKAAIISHR 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 262 RYYRMAALVYYGFRMRPDDIVYDCLPLYHSAGNIVGIGQCVLHGMTVVIRKKFSASRFWDDCIKYNCTIVQYIGELCRYL 341
Cdd:cd05940 105 RAWRGGAFFAGSGGALPSDVLYTCLPLYHSTALIVGWSACLASGATLVIRKKFSASNFWDDIRKYQATIFQYIGELCRYL 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 342 LNQPPREAESRHKVRMALGNGLRQSIWTDFSSRFHIPQVAEFYGATECNCSLGNFDSQVGACGFNSRILSFVYPIRLVRV 421
Cdd:cd05940 185 LNQPPKPTERKHKVRMIFGNGLRPDIWEEFKERFGVPRIAEFYAATEGNSGFINFFGKPGAIGRNPSLLRKVAPLALVKY 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 422 NEDTMELIRGPDGVCIPCQPGQPGQLVGRIIqqdPLRRFDGYLNQGANNKKIASDVFKKGDQAYLTGDVLVMDELGYLYF 501
Cdd:cd05940 265 DLESGEPIRDAEGRCIKVPRGEPGLLISRIN---PLEPFDGYTDPAATEKKILRDVFKKGDAWFNTGDLMRLDGEGFWYF 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 502 RDRTGDTFRWKGENVSTTEVEGTLSRLLQMADVAVYGVEVPGAEGRAGMAAVA-SPTSNCDLESFAQTLKKELPLYARPI 580
Cdd:cd05940 342 VDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQVPGTDGRAGMAAIVlQPNEEFDLSALAAHLEKNLPGYARPL 421
|
490 500
....*....|....*....|....*...
gi 291084711 581 FLRFLPELHKTGTFKFQKTELRKEGFDP 608
Cdd:cd05940 422 FLRLQPEMEITGTFKQQKVDLRNEGFDP 449
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
95-633 |
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: 575.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 95 FEGTNthWTFRQLDDYSSSVAN-FLQARGLVSGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALRHCLDTSK 173
Cdd:cd05938 1 FEGET--YTYRDVDRRSNQAARaLLAHAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 174 ARALIFGSEMASAVYEI-QAILDPTLTLFCSGswePSTVPANTEHLDPLLEDAPKHLPSIPDKG---FTDKLFYIYTSGT 249
Cdd:cd05938 79 AKVLVVAPELQEAVEEVlPALRADGVSVWYLS---HTSNTEGVISLLDKVDAASDEPVPASLRAhvtIKSPALYIYTSGT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 250 TGLPKAAIVVHSRYYRMAAlVYYGFRMRPDDIVYDCLPLYHSAGNIVGIGQCVLHGMTVVIRKKFSASRFWDDCIKYNCT 329
Cdd:cd05938 156 TGLPKAARISHLRVLQCSG-FLSLCGVTADDVIYITLPLYHSSGFLLGIGGCIELGATCVLKPKFSASQFWDDCRKHNVT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 330 IVQYIGELCRYLLNQPPREAESRHKVRMALGNGLRQSIWTDFSSRFHIPQVAEFYGATECNCSLGNFDSQVGACGFNSRI 409
Cdd:cd05938 235 VIQYIGELLRYLCNQPQSPNDRDHKVRLAIGNGLRADVWREFLRRFGPIRIREFYGSTEGNIGFFNYTGKIGAVGRVSYL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 410 LSFVYPIRLVRVNEDTMELIRGPDGVCIPCQPGQPGQLVGRIIQQDPlrrFDGYL-NQGANNKKIASDVFKKGDQAYLTG 488
Cdd:cd05938 315 YKLLFPFELIKFDVEKEEPVRDAQGFCIPVAKGEPGLLVAKITQQSP---FLGYAgDKEQTEKKLLRDVFKKGDVYFNTG 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 489 DVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLQMADVAVYGVEVPGAEGRAGMAAVA-SPTSNCDLESFAQ 567
Cdd:cd05938 392 DLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVYGVTVPGHEGRIGMAAVKlKPGHEFDGKKLYQ 471
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 291084711 568 TLKKELPLYARPIFLRFLPELHKTGTFKFQKTELRKEGFDPSVVKDPLFYLDARTGCYVALDQEAY 633
Cdd:cd05938 472 HVREYLPAYARPRFLRIQDSLEITGTFKQQKVRLVEEGFNPSIISDPLYFLDETQKTYVPLTPDIY 537
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
102-608 |
1.01e-151 |
|
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: 1.01e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 102 WTFRQLDDYSSSVANFLQ-ARGLVSGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALRHCLDTSKARalifg 180
Cdd:cd05937 6 WTYSETYDLVLRYAHWLHdDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLSGSR----- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 181 semasavyeiQAILDPtltlfcsgswepstvpantehldplleDAPKHLpsipdkgftdklfyIYTSGTTGLPKAAIVVH 260
Cdd:cd05937 81 ----------FVIVDP---------------------------DDPAIL--------------IYTSGTTGLPKAAAISW 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 261 SRYYRMAALVYYGFRMRPDDIVYDCLPLYHSAGNIVGIGQCVLHGMTVVIRKKFSASRFWDDCIKYNCTIVQYIGELCRY 340
Cdd:cd05937 110 RRTLVTSNLLSHDLNLKNGDRTYTCMPLYHGTAAFLGACNCLMSGGTLALSRKFSASQFWKDVRDSGATIIQYVGELCRY 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 341 LLNQPPREAESRHKVRMALGNGLRQSIWTDFSSRFHIPQVAEFYGATECNCSLGNFDS---QVGACGFNSRILSFVY--P 415
Cdd:cd05937 190 LLSTPPSPYDRDHKVRVAWGNGLRPDIWERFRERFNVPEIGEFYAATEGVFALTNHNVgdfGAGAIGHHGLIRRWKFenQ 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 416 IRLVRVNEDTMELIRGP-DGVCIPCQPGQPGQLVGRiIQQDPLRRFDGYL-NQGANNKKIASDVFKKGDQAYLTGDVLVM 493
Cdd:cd05937 270 VVLVKMDPETDDPIRDPkTGFCVRAPVGEPGEMLGR-VPFKNREAFQGYLhNEDATESKLVRDVFRKGDIYFRTGDLLRQ 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 494 DELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLQMADVAVYGVEVPGAEGRAGMAAV-----ASPTSNCDLESFAQT 568
Cdd:cd05937 349 DADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGVKVPGHDGRAGCAAItleesSAVPTEFTKSLLASL 428
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 291084711 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 |
3.00e-94 |
|
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: 297.88 E-value: 3.00e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 76 VPLLFASVVRRHPDKTALIFEGTntHWTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKLGVEAAL 155
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGR--RLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 156 INTNLRRDALRHCLDTSKARALIFgsemasavyeiqaildptltlfcsgswepstvpantehldplledapkhlpsipdk 235
Cdd:COG0318 79 LNPRLTAEELAYILEDSGARALVT-------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 236 gftdkLFYIYTSGTTGLPKAAIVVHSRYYRMAALVYYGFRMRPDDIVYDCLPLYHSAGNIVGIGQCVLHGMTVVIRKKFS 315
Cdd:COG0318 103 -----ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLPRFD 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 316 ASRFWDDCIKYNCTIVQYIGELCRYLLNQPPREAESRHKVRMAL--GNGLRQSIWTDFSSRFHIPqVAEFYGATECN--C 391
Cdd:COG0318 178 PERVLELIERERVTVLFGVPTMLARLLRHPEFARYDLSSLRLVVsgGAPLPPELLERFEERFGVR-IVEGYGLTETSpvV 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 392 SLGNFDSQ---VGACGFnsrilsfvyPIRLVRVnedtmeLIRGPDGvcIPCQPGQPGQLVGR---IiqqdplrrFDGYLN 465
Cdd:COG0318 257 TVNPEDPGerrPGSVGR---------PLPGVEV------RIVDEDG--RELPPGEVGEIVVRgpnV--------MKGYWN 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 466 QGANNKKiasdVFKKGdqAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLQMADVAVYGVEVPGAe 545
Cdd:COG0318 312 DPEATAE----AFRDG--WLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKW- 384
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 546 GRAGMAAV-ASPTSNCDLESFAQTLKKELPLYARPIFLRFLPELHKTGTFKFQKTELRKE 604
Cdd:COG0318 385 GERVVAFVvLRPGAELDAEELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRER 444
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
74-608 |
2.17e-85 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 277.41 E-value: 2.17e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 74 KTVPLLFASVVRRHPDKTALIFEGTntHWTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKLGVEA 153
Cdd:PRK06155 21 RTLPAMLARQAERYPDRPLLVFGGT--RWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 154 ALINTNLRRDALRHCLDTSKARALIFGSEMASAVYEIQAILDPTLTLFCSGSWEPSTVPA--NTEHLDPLLEDAPkhlPS 231
Cdd:PRK06155 99 VPINTALRGPQLEHILRNSGARLLVVEAALLAALEAADPGDLPLPAVWLLDAPASVSVPAgwSTAPLPPLDAPAP---AA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 232 IPDKGftDKLFYIYTSGTTGLPKAAIVVHSRYYRMAALVYYGFRMRPDDIVYDCLPLYHS-AGNivGIGQCVLHGMTVVI 310
Cdd:PRK06155 176 AVQPG--DTAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADDVLYTTLPLFHTnALN--AFFQALLAGATYVL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 311 RKKFSASRFWDDCIKYNCTIVQYIGELCRYLLNQPPREAESRHKVRMALGNGLRQSIWTDFSSRFHIPqVAEFYGATECN 390
Cdd:PRK06155 252 EPRFSASGFWPAVRRHGATVTYLLGAMVSILLSQPARESDRAHRVRVALGPGVPAALHAAFRERFGVD-LLDGYGSTETN 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 391 CSLG-NFDSQVG------ACGFNSRIlsfvypirlvrVNEDTMELirgpdgvcipcQPGQPGQLVGRiiQQDPLRRFDGY 463
Cdd:PRK06155 331 FVIAvTHGSQRPgsmgrlAPGFEARV-----------VDEHDQEL-----------PDGEPGELLLR--ADEPFAFATGY 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 464 LNQGANNKKIASDVFkkgdqaYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLQMADVAVYGVEVPG 543
Cdd:PRK06155 387 FGMPEKTVEAWRNLW------FHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSEL 460
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 291084711 544 AEGRAGMAAVASPTSNCDLESFAQTLKKELPLYARPIFLRFLPELHKTGTFKFQKTELRKEGFDP 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 |
1.86e-83 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 268.78 E-value: 1.86e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 99 NTHWTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALRHCLDTSKARALI 178
Cdd:cd05934 1 GRRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 179 fgsemasavyeiqaildptltlfcsgswepstvpantehldplledapkhlpsipdkgfTDKLFYIYTSGTTGLPKAAIV 258
Cdd:cd05934 81 -----------------------------------------------------------VDPASILYTSGTTGPPKGVVI 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 259 VHSRYYRMAALVYYGFRMRPDDIVYDCLPLYHSAGNIVGIGQCVLHGMTVVIRKKFSASRFWDDCIKYNCTIVQYIGELC 338
Cdd:cd05934 102 THANLTFAGYYSARRFGLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLLPRFSASRFWSDVRRYGATVTNYLGAML 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 339 RYLLNQPPREAESRHKVRMALGNGLRQSIWTDFSSRFHIPqVAEFYGATECNCSLgnfdsqVGACGFNSRILSFVYPIRL 418
Cdd:cd05934 182 SYLLAQPPSPDDRAHRLRAAYGAPNPPELHEEFEERFGVR-LLEGYGMTETIVGV------IGPRDEPRRPGSIGRPAPG 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 419 VRVnedtmeLIRGPDGVciPCQPGQPGQLVGRIIQqdPLRRFDGYLNQGANNKKiasdVFKKGdqAYLTGDVLVMDELGY 498
Cdd:cd05934 255 YEV------RIVDDDGQ--ELPAGEPGELVIRGLR--GWGFFKGYYNMPEATAE----AMRNG--WFHTGDLGYRDADGF 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 499 LYFRDRTGDTFRWKGENVSTTEVEGTLSRLLQMADVAVYGV--EVPGAEGRAgmAAVASPTSNCDLESFAQTLKKELPLY 576
Cdd:cd05934 319 FYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVpdEVGEDEVKA--VVVLRPGETLDPEELFAFCEGQLAYF 396
|
490 500
....*....|....*....|....*.
gi 291084711 577 ARPIFLRFLPELHKTGTFKFQKTELR 602
Cdd:cd05934 397 KVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
80-512 |
5.53e-63 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 214.48 E-value: 5.53e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 80 FASVVRRHPDKTALIFeGTNTHWTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKLGVEAALINTN 159
Cdd:pfam00501 1 LERQAARTPDKTALEV-GEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 160 LRRDALRHCLDTSKARALIFGSE-MASAVYEIQAILDPTLTLFCSGSWEPStvPANTEHLDPLLEDAPKHLPSIPDKgfT 238
Cdd:pfam00501 80 LPAEELAYILEDSGAKVLITDDAlKLEELLEALGKLEVVKLVLVLDRDPVL--KEEPLPEEAKPADVPPPPPPPPDP--D 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 239 DKLFYIYTSGTTGLPKAAIVVH----SRYYRMAALVYYGFRMRPDDIVYDCLPLYHSAGNIVGIGQCVLHGMTVVIRKKF 314
Cdd:pfam00501 156 DLAYIIYTSGTTGKPKGVMLTHrnlvANVLSIKRVRPRGFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVVLPPGF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 315 SA---SRFWDDCIKYNCTIVQYIGELCRYLLNQPPREAESRHKVRMAL--GNGLRQSIWTDFSSRFhIPQVAEFYGATEC 389
Cdd:pfam00501 236 PAldpAALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSSLRLVLsgGAPLPPELARRFRELF-GGALVNGYGLTET 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 390 NC------SLGNFDSQVGACGFnsrilsfvyPIRLVR---VNEDTMElirgpdgvciPCQPGQPGQLV--GRIIqqdplr 458
Cdd:pfam00501 315 TGvvttplPLDEDLRSLGSVGR---------PLPGTEvkiVDDETGE----------PVPPGEPGELCvrGPGV------ 369
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 291084711 459 rFDGYLNQ-GANNKKIASDVFkkgdqaYLTGDVLVMDELGYLYFRDRTGDTFRWK 512
Cdd:pfam00501 370 -MKGYLNDpELTAEAFDEDGW------YRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
241-597 |
9.73e-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: 9.73e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 241 LFYIYTSGTTGLPKAAIVVHSRYYRMAALVYYGFRMRPDDIVYDCLPLYHSAGnIVGIGQCVLHGMTVVIRKKFSASRFW 320
Cdd:cd04433 3 ALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGG-LFGLLGALLAGGTVVLLPKFDPEAAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 321 DDCIKYNCTIVQYIGELCRYLLNQPPREAESRHKVRMALGNG--LRQSIWTDFSSRFHIPqVAEFYGATECNCSL----- 393
Cdd:cd04433 82 ELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGapLPPELLERFEEAPGIK-LVNGYGLTETGGTVatgpp 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 394 GNFDSQVGACGFnsrilsfvyPIRLVRVNedtmelIRGPDGvcIPCQPGQPGQLVGRIIQqdplrRFDGYLNQGANNKki 473
Cdd:cd04433 161 DDDARKPGSVGR---------PVPGVEVR------IVDPDG--GELPPGEIGELVVRGPS-----VMKGYWNNPEATA-- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 474 asdvFKKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLQMADVAVYGVEVPGAEGRAGMAAV 553
Cdd:cd04433 217 ----AVDEDGWYRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVV 292
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 291084711 554 ASPTSNCDLESFAQTLKKELPLYARPIFLRFLPELHKTGTFKFQ 597
Cdd:cd04433 293 LRPGADLDAEELRAHVRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
75-602 |
6.30e-56 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 198.10 E-value: 6.30e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 75 TVPLLFASVVRRHPDKTALIFEGTNthWTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKLGVEAA 154
Cdd:PRK06187 7 TIGRILRHGARKHPDKEAVYFDGRR--TTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 155 LINTNLRRDALRHCLDTSKARALIFGSEMASAVYEIQAILDPTLTLFCSGSWEPSTVPANTEHLDPLLEDAPKHLPSiPD 234
Cdd:PRK06187 85 PINIRLKPEEIAYILNDAEDRVVLVDSEFVPLLAAILPQLPTVRTVIVEGDGPAAPLAPEVGEYEELLAAASDTFDF-PD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 235 KGFTDKLFYIYTSGTTGLPKAAIVVHSRYYRMAALVYYGFRMRPDDIVYDCLPLYHSAgnivGIGQCVL---HGMTVVIR 311
Cdd:PRK06187 164 IDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVPMFHVH----AWGLPYLalmAGAKQVIP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 312 KKFSASRFWDDCIKYNCTIVQYIGELCRYLLNQPPREAESRHKVRMAL--GNGLRQSIWTDFSSRFHIpQVAEFYGATEC 389
Cdd:PRK06187 240 RRFDPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYFVDFSSLRLVIygGAALPPALLREFKEKFGI-DLVQGYGMTET 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 390 nCSLGNF---DSQVGacGFNSRILSFVYPIRLVRVNedtmelIRGPDGVCIPCQPGQPGQLVGR---IIQqdplrrfdGY 463
Cdd:PRK06187 319 -SPVVSVlppEDQLP--GQWTKRRSAGRPLPGVEAR------IVDDDGDELPPDGGEVGEIIVRgpwLMQ--------GY 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 464 LNQ-GANNKKIASDvfkkgdqAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLQMADVAVYGV--- 539
Cdd:PRK06187 382 WNRpEATAETIDGG-------WLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVpde 454
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 291084711 540 ---EVPGA--EGRAGMAAVASptsncDLESFaqtLKKELPLYARPIFLRFLPELHKTGTFKFQKTELR 602
Cdd:PRK06187 455 kwgERPVAvvVLKPGATLDAK-----ELRAF---LRGRLAKFKLPKRIAFVDELPRTSVGKILKRVLR 514
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
73-623 |
6.81e-56 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 198.37 E-value: 6.81e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 73 RKTVPLLFASvvRRHPDKTALIFEGTNTHWtfRQLDDYSSSVANFLQARgLVSGNV--VALFMENRNEFvGLWLGMAKLG 150
Cdd:PRK07867 4 APTVAELLLP--LAEDDDRGLYFEDSFTSW--REHIRGSAARAAALRAR-LDPTRPphVGVLLDNTPEF-SLLLGAAALS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 151 --VEAALINTN----LRRDALR-HC---LDTSKARALIFGSEMASAVYEIQAildptltlfcsgswepstvPANTEHLDP 220
Cdd:PRK07867 78 giVPVGLNPTRrgaaLARDIAHaDCqlvLTESAHAELLDGLDPGVRVINVDS-------------------PAWADELAA 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 221 LLEDAPKHLPSIPDkgftDKLFYIYTSGTTGLPKAAIVVHSRYYRMAALVYYGFRMRPDDIVYDCLPLYHSAGNIVGIGQ 300
Cdd:PRK07867 139 HRDAEPPFRVADPD----DLFMLIFTSGTSGDPKAVRCTHRKVASAGVMLAQRFGLGPDDVCYVSMPLFHSNAVMAGWAV 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 301 CVLHGMTVVIRKKFSASRFWDDCIKYNCTIVQYIGELCRYLLNQPPREAESRHKVRMALGNGLRQSIWTDFSSRFHIpQV 380
Cdd:PRK07867 215 ALAAGASIALRRKFSASGFLPDVRRYGATYANYVGKPLSYVLATPERPDDADNPLRIVYGNEGAPGDIARFARRFGC-VV 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 381 AEFYGATECNCSLGNF-DSQVGACGfnsrilsfvypirlvrvnedtmeliRGPDGVCI-------PCQPGQPG------- 445
Cdd:PRK07867 294 VDGFGSTEGGVAITRTpDTPPGALG-------------------------PLPPGVAIvdpdtgtECPPAEDAdgrllna 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 446 -QLVGRIIQQDPLRRFDGYLN-QGANNKKIASDVFKKGDQAYltgdvlvMDELGYLYFRDRTGDTFRWKGENVSTTEVEG 523
Cdd:PRK07867 349 dEAIGELVNTAGPGGFEGYYNdPEADAERMRGGVYWSGDLAY-------RDADGYAYFAGRLGDWMRVDGENLGTAPIER 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 524 TLSRLLQMADVAVYGVEVPgAEGRAGMAAVA-SPTSNCDLESFAQTL--KKELPLYARPIFLRFLPELHKTGTFKFQKTE 600
Cdd:PRK07867 422 ILLRYPDATEVAVYAVPDP-VVGDQVMAALVlAPGAKFDPDAFAEFLaaQPDLGPKQWPSYVRVCAELPRTATFKVLKRQ 500
|
570 580
....*....|....*....|...
gi 291084711 601 LRKEGFDPSvvkDPLFYLDARTG 623
Cdd:PRK07867 501 LSAEGVDCA---DPVWWIRRLTP 520
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
84-598 |
8.12e-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: 182.04 E-value: 8.12e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 84 VRRHPDKTALIFEGTNthWTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRD 163
Cdd:cd17631 5 ARRHPDRTALVFGGRS--LTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 164 ALRHCLDTSKARALIfgsemasavyeiqaildptltlfcsgswepstvpantehldplledapkhlpsipdkgftDKLFY 243
Cdd:cd17631 83 EVAYILADSGAKVLF------------------------------------------------------------DDLAL 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 244 I-YTSGTTGLPKAAIVVHSRYYRMAALVYYGFRMRPDDIVYDCLPLYHSAGNIVGIGQCVLHGMTVVIRKKFSASRFWDD 322
Cdd:cd17631 103 LmYTSGTTGRPKGAMLTHRNLLWNAVNALAALDLGPDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVILRKFDPETVLDL 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 323 CIKYNCTIVQYIGELCRYLLNQPPREAESRHKVRMALGNG------LRQsIWTDFSSRFHipqvaEFYGATECN---CSL 393
Cdd:cd17631 183 IERHRVTSFFLVPTMIQALLQHPRFATTDLSSLRAVIYGGapmperLLR-ALQARGVKFV-----QGYGMTETSpgvTFL 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 394 GNFDSQ--VGACGfnsrilsfvYPIRLVRVNedtmelIRGPDGVciPCQPGQPGQLVGRIIQQdplrrFDGYLNQGANNK 471
Cdd:cd17631 257 SPEDHRrkLGSAG---------RPVFFVEVR------IVDPDGR--EVPPGEVGEIVVRGPHV-----MAGYWNRPEATA 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 472 KiasdVFKKGdqAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLQMADVAVYGveVPGAE-GRAGM 550
Cdd:cd17631 315 A----AFRDG--WFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIG--VPDEKwGEAVV 386
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 291084711 551 AAVA-SPTSNCDLESFAQTLKKELPLYARPIFLRFLPELHKTGTFKFQK 598
Cdd:cd17631 387 AVVVpRPGAELDEDELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
84-607 |
6.62e-50 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 182.15 E-value: 6.62e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 84 VRRHPDKTALIFEGTNthWTFRQLDDYSSSVANFLQARGLVSGNV-VALFMENRNEFVgLWLGMAKLGvEAAL--INTNL 160
Cdd:PRK13388 11 DRAGDDTIAVRYGDRT--WTWREVLAEAAARAAALIALADPDRPLhVGVLLGNTPEML-FWLAAAALG-GYVLvgLNTTR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 161 RRDAL----RH--C--LDTSKA-RALIFGsemasavyeiqaiLD-PTLTLFCSGSwepstvPANTEHLDPLLEDAPkhlp 230
Cdd:PRK13388 87 RGAALaadiRRadCqlLVTDAEhRPLLDG-------------LDlPGVRVLDVDT------PAYAELVAAAGALTP---- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 231 sIPDKGFTDKLFYIYTSGTTGLPKAAIVVHSRYYRMAALVYYGFRMRPDDIVYDCLPLYHSAGNIVGIGQCVLHGMTVVI 310
Cdd:PRK13388 144 -HREVDAMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLTRDDVCYVSMPLFHSNAVMAGWAPAVASGAAVAL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 311 RKKFSASRFWDDCIKYNCTIVQYIGELCRYLLNQPPREAESRHKVRMALGNGLRQSIWTDFSSRFHIpQVAEFYGATEcn 390
Cdd:PRK13388 223 PAKFSASGFLDDVRRYGATYFNYVGKPLAYILATPERPDDADNPLRVAFGNEASPRDIAEFSRRFGC-QVEDGYGSSE-- 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 391 cslgnfdsqvGACgfnsrilsfvypiRLVRVnEDTME--LIRGPDGVCI-------PCQPGQ---------PGQLVGRII 452
Cdd:PRK13388 300 ----------GAV-------------IVVRE-PGTPPgsIGRGAPGVAIynpetltECAVARfdahgallnADEAIGELV 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 453 QQDPLRRFDGYLN-QGANNKKIASDVFKKGDQAYLtgdvlvmDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLQM 531
Cdd:PRK13388 356 NTAGAGFFEGYYNnPEATAERMRHGMYWSGDLAYR-------DADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAI 428
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 291084711 532 ADVAVYGVEVPGAeGRAGMAA-VASPTSNCDLESFAQTL--KKELPLYARPIFLRFLPELHKTGTFKFQKTELRKEGFD 607
Cdd:PRK13388 429 NRVAVYAVPDERV-GDQVMAAlVLRDGATFDPDAFAAFLaaQPDLGTKAWPRYVRIAADLPSTATNKVLKRELIAQGWA 506
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
79-602 |
2.63e-49 |
|
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: 178.53 E-value: 2.63e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 79 LFASVVRRHPDKTALIFEGTNthWTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKLGVEAALINT 158
Cdd:cd05936 4 LLEEAARRFPDKTALIFMGRK--LTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 159 NLRRDALRHCLDTSKARALIfgsemasavyeiqaildpTLTLFCSgswepstvpantehldpLLEDAPKHLPSIPDKGfT 238
Cdd:cd05936 82 LYTPRELEHILNDSGAKALI------------------VAVSFTD-----------------LLAAGAPLGERVALTP-E 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 239 DKLFYIYTSGTTGLPKAAIVVHSRYYR--MAALVYYGFRMRPDDIVYDCLPLYHSAGNIVGIGQCVLHGMTVVIRKKFSA 316
Cdd:cd05936 126 DVAVLQYTSGTTGVPKGAMLTHRNLVAnaLQIKAWLEDLLEGDDVVLAALPLFHVFGLTVALLLPLALGATIVLIPRFRP 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 317 SRFWDDCIKYNCTIVQ-----YIGelcryLLNQPPREAESRHKVRMALGNG--LRQSIWTDFSSRFHIPqVAEFYGATEC 389
Cdd:cd05936 206 IGVLKEIRKHRVTIFPgvptmYIA-----LLNAPEFKKRDFSSLRLCISGGapLPVEVAERFEELTGVP-IVEGYGLTET 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 390 ncslgnfdSQVGAC---GFNSRILSFVYPIRlvrvneDTMELIRGPDGVCIPcqPGQPGQLVGRIIQqdplrRFDGYLNQ 466
Cdd:cd05936 280 --------SPVVAVnplDGPRKPGSIGIPLP------GTEVKIVDDDGEELP--PGEVGELWVRGPQ-----VMKGYWNR 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 467 GANNKKiasdVFKKGdqAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLQMADVAVYGV--EVPGA 544
Cdd:cd05936 339 PEETAE----AFVDG--WLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVpdPYSGE 412
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 291084711 545 EGRAgmAAVASPTSNCDLESFAQTLKKELPLYARPIFLRFLPELHKTGTFKFQKTELR 602
Cdd:cd05936 413 AVKA--FVVLKEGASLTEEEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
83-614 |
5.80e-49 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 179.92 E-value: 5.80e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 83 VVRRH----PDKTALIFE---GTNTHWTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKLGVEAAL 155
Cdd:COG0365 14 CLDRHaegrGDKVALIWEgedGEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 156 INTNLRRDALRHCLDTSKARALIFGSEMASA--VYEIQAILD------PTL-TLFCSGSWEPSTVPANTEHLDPLLEDAP 226
Cdd:COG0365 94 VFPGFGAEALADRIEDAEAKVLITADGGLRGgkVIDLKEKVDealeelPSLeHVIVVGRTGADVPMEGDLDWDELLAAAS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 227 KHLPSIPdKGFTDKLFYIYTSGTTGLPKAaiVVHS-RYYRMAALVY--YGFRMRPDDIVY---DClplyhsaGNIVGIGQ 300
Cdd:COG0365 174 AEFEPEP-TDADDPLFILYTSGTTGKPKG--VVHThGGYLVHAATTakYVLDLKPGDVFWctaDI-------GWATGHSY 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 301 CV----LHGMTVVI---RKKF-SASRFWDDCIKYNCTIvqyigeLC------RYLLNQPPREAESRH--KVRMALGNG-- 362
Cdd:COG0365 244 IVygplLNGATVVLyegRPDFpDPGRLWELIEKYGVTV------FFtaptaiRALMKAGDEPLKKYDlsSLRLLGSAGep 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 363 LRQSIWTDFSSRFHIPqVAEFYGATECNCSLGNF----DSQVGACGFnsrilsfvyPIRLVRVnedtmeLIRGPDGVciP 438
Cdd:COG0365 318 LNPEVWEWWYEAVGVP-IVDGWGQTETGGIFISNlpglPVKPGSMGK---------PVPGYDV------AVVDEDGN--P 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 439 CQPGQPGQLVgriIQQDPLRRFDGYLNqgaNNKKIASDVFKKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVST 518
Cdd:COG0365 380 VPPGEEGELV---IKGPWPGMFRGYWN---DPERYRETYFGRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGT 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 519 TEVEGTLSRLLQMADVAVygVEVPGAEGRAGMAAVASPTSNCDL-----ESFAQTLKKELPLYARPIFLRFLPELHKTGT 593
Cdd:COG0365 454 AEIESALVSHPAVAEAAV--VGVPDEIRGQVVKAFVVLKPGVEPsdelaKELQAHVREELGPYAYPREIEFVDELPKTRS 531
|
570 580
....*....|....*....|....*.
gi 291084711 594 FKFQKTELRK-----EGFDPSVVKDP 614
Cdd:COG0365 532 GKIMRRLLRKiaegrPLGDTSTLEDP 557
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
98-595 |
6.90e-49 |
|
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: 178.18 E-value: 6.90e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 98 TNTHWTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALRHCLDTSKARAL 177
Cdd:cd05911 7 TGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 178 IFGSEMASAVYEIQAILDPTLTLFCSGSwEPSTVPANTEHLDPLLEDAPKHLPSIPDKGFTDKLFYIYTSGTTGLPKAAI 257
Cdd:cd05911 87 FTDPDGLEKVKEAAKELGPKDKIIVLDD-KPDGVLSIEDLLSPTLGEEDEDLPPPLKDGKDDTAAILYSSGTTGLPKGVC 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 258 VVHSRYYRMAALVYYGFR--MRPDDIVYDCLPLYHSAGnIVGIGQCVLHGMTVVIRKKFSASRFWDDCIKYNCTIVQYIG 335
Cdd:cd05911 166 LSHRNLIANLSQVQTFLYgnDGSNDVILGFLPLYHIYG-LFTTLASLLNGATVIIMPKFDSELFLDLIEKYKITFLYLVP 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 336 ELCRYLLNQPPREAESRHKVRMAL--GNGLRQSIWTDFSSRFHIPQVAEFYGATECNCSLG---NFDSQVGACGfnsRIL 410
Cdd:cd05911 245 PIAAALAKSPLLDKYDLSSLRVILsgGAPLSKELQELLAKRFPNATIKQGYGMTETGGILTvnpDGDDKPGSVG---RLL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 411 SFVypirLVR-VNEDTMELirgpdgvcipCQPGQPGQLVGRIIQQdplrrFDGYL-NQGANNKKIASDVFkkgdqaYLTG 488
Cdd:cd05911 322 PNV----EAKiVDDDGKDS----------LGPNEPGEICVRGPQV-----MKGYYnNPEATKETFDEDGW------LHTG 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 489 DVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLQMADVAVYGV------EVPGAegragmAAVASPTSNCDL 562
Cdd:cd05911 377 DIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIpdevsgELPRA------YVVRKPGEKLTE 450
|
490 500 510
....*....|....*....|....*....|....*..
gi 291084711 563 ESFAQTLKKELPLYARpifLR----FLPELHKTGTFK 595
Cdd:cd05911 451 KEVKDYVAKKVASYKQ---LRggvvFVDEIPKSASGK 484
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
88-603 |
1.20e-44 |
|
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: 166.33 E-value: 1.20e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 88 PDKTALIFEGTNTHWTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALRH 167
Cdd:cd05926 1 PDAPALVVPGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 168 CLDTSKARALI-----FGSEMASAVYEIQAILDPTLTLFCSGSWEPSTVPANTEHLDPLLEDAPKHLPSipdkgftDKLF 242
Cdd:cd05926 81 YLADLGSKLVLtpkgeLGPASRAASKLGLAILELALDVGVLIRAPSAESLSNLLADKKNAKSEGVPLPD-------DLAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 243 YIYTSGTTGLPKAAIVVHSRYYRMAALVYYGFRMRPDDIVYDCLPLYHSAGNIVGIGQCVLHGMTVVIRKKFSASRFWDD 322
Cdd:cd05926 154 ILHTSGTTGRPKGVPLTHRNLAASATNITNTYKLTPDDRTLVVMPLFHVHGLVASLLSTLAAGGSVVLPPRFSASTFWPD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 323 CIKYNCTIVQYIGELCRYLLNQPPREAESR-HKVRMA--LGNGLRQSIWTDFSSRFHIPqVAEFYGATECNcslgnfdSQ 399
Cdd:cd05926 234 VRDYNATWYTAVPTIHQILLNRPEPNPESPpPKLRFIrsCSASLPPAVLEALEATFGAP-VLEAYGMTEAA-------HQ 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 400 VgacgFNSRILSFVYPIRLVRVNEDTMELIRGPDGvcipcQPGQPGQlVGRIIQQDPlRRFDGYLNQGANNKKIAS--DV 477
Cdd:cd05926 306 M----TSNPLPPGPRKPGSVGKPVGVEVRILDEDG-----EILPPGV-VGEICLRGP-NVTRGYLNNPEANAEAAFkdGW 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 478 FKKGDQAYLtgdvlvmDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLQMADVAVYGV--EVPGAEgrAGMAAVAS 555
Cdd:cd05926 375 FRTGDLGYL-------DADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVpdEKYGEE--VAAAVVLR 445
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 291084711 556 PTSNCDLESFAQTLKKELPLYARPIFLRFLPELHKTGTFKFQKTELRK 603
Cdd:cd05926 446 EGASVTEEELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKVAE 493
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
73-604 |
2.14e-44 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 166.26 E-value: 2.14e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 73 RKTVPLLFASVVRRHPDKTALIFEGTNthWTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKLGVE 152
Cdd:PRK08316 10 RQTIGDILRRSARRYPDKTALVFGDRS--WTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 153 AALINTNLRRDALRHCLDTSKARALIFGSEMASAVyEIQAILDPTLTLFCSGSWEPSTVPANTEHLDPLLEDAPKHLPSI 232
Cdd:PRK08316 88 HVPVNFMLTGEELAYILDHSGARAFLVDPALAPTA-EAALALLPVDTLILSLVLGGREAPGGWLDFADWAEAGSVAEPDV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 233 PDKGfTDKLFYIYTSGTTGLPKAAIVVHSryyrmaALV--YYG----FRMRPDDIVYDCLPLYHSAGNIVGIGQCVLHGM 306
Cdd:PRK08316 167 ELAD-DDLAQILYTSGTESLPKGAMLTHR------ALIaeYVScivaGDMSADDIPLHALPLYHCAQLDVFLGPYLYVGA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 307 TVVIRKKFSASRFWDDCIKYNCTI------VqYIGelcryLLNQP---PREAESRHK-------VRMALGNGLRQsiwtd 370
Cdd:PRK08316 240 TNVILDAPDPELILRTIEAERITSffapptV-WIS-----LLRHPdfdTRDLSSLRKgyygasiMPVEVLKELRE----- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 371 fssrfHIPQVA--EFYGATEC---NCSLG--NFDSQVGACGfnsRILSFVYpirlVRVNEDTMElirgpdgvciPCQPGQ 443
Cdd:PRK08316 309 -----RLPGLRfyNCYGQTEIaplATVLGpeEHLRRPGSAG---RPVLNVE----TRVVDDDGN----------DVAPGE 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 444 PGQLVGRIIQQdplrrFDGYLNQGAnnkKIAsDVFKKGdqAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEG 523
Cdd:PRK08316 367 VGEIVHRSPQL-----MLGYWDDPE---KTA-EAFRGG--WFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEE 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 524 TLSRLLQMADVAVYGVEVPgaegRAGMA--AVASPTSNCDL--ESFAQTLKKELPLYARPIFLRFLPELHKTGTFKFQKT 599
Cdd:PRK08316 436 ALYTHPAVAEVAVIGLPDP----KWIEAvtAVVVPKAGATVteDELIAHCRARLAGFKVPKRVIFVDELPRNPSGKILKR 511
|
....*
gi 291084711 600 ELRKE 604
Cdd:PRK08316 512 ELRER 516
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
73-602 |
1.42e-41 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 158.31 E-value: 1.42e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 73 RKTVPLLFASVVRRHPDKTALIFE---GTNTHWTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKL 149
Cdd:PRK08008 6 GQHLRQMWDDLADVYGHKTALIFEssgGVVRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 150 GVEAALINTNLRRDALRHCLDTSKARALIFGSEMASAVYEIQAILDPTLT-LFCSGSWEPSTvpANTEHLDPLLEDAPKH 228
Cdd:PRK08008 86 GAIMVPINARLLREESAWILQNSQASLLVTSAQFYPMYRQIQQEDATPLRhICLTRVALPAD--DGVSSFTQLKAQQPAT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 229 LPSIPDKGFTDKLFYIYTSGTTGLPKAAIVVHsryYRMAALVYYG---FRMRPDDIVYDCLPLYHSAGNIVGIGQCVLHG 305
Cdd:PRK08008 164 LCYAPPLSTDDTAEILFTSGTTSRPKGVVITH---YNLRFAGYYSawqCALRDDDVYLTVMPAFHIDCQCTAAMAAFSAG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 306 MTVVIRKKFSASRFWDDCIKYNCTIVQYIGELCRYLLNQPPREAESRHKVR-----MALGNGLRQsiwtDFSSRFHIpQV 380
Cdd:PRK08008 241 ATFVLLEKYSARAFWGQVCKYRATITECIPMMIRTLMVQPPSANDRQHCLRevmfyLNLSDQEKD----AFEERFGV-RL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 381 AEFYGATECNCSL-GNFDSQ------VGACGFNsrilsfvYPIRLvrVNEDTMELIRGPDG-VCIpcqPGQPGQLVGRII 452
Cdd:PRK08008 316 LTSYGMTETIVGIiGDRPGDkrrwpsIGRPGFC-------YEAEI--RDDHNRPLPAGEIGeICI---KGVPGKTIFKEY 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 453 QQDP------LRRfDGYLnqgannkkiasdvfKKGDQAYltgdvlvMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLS 526
Cdd:PRK08008 384 YLDPkatakvLEA-DGWL--------------HTGDTGY-------VDEEGFFYFVDRRCNMIKRGGENVSCVELENIIA 441
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 291084711 527 RLLQMADVAVYGVEVPGAEGRAGMAAVASPTSNCDLESFAQTLKKELPLYARPIFLRFLPELHKTGTFKFQKTELR 602
Cdd:PRK08008 442 THPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
75-604 |
2.77e-41 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 157.37 E-value: 2.77e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 75 TVPLLFASVVRRHPDKTALIFEGTNThwTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKLGveAA 154
Cdd:PRK07656 6 TLPELLARAARRFGDKEAYVFGDQRL--TYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAG--AV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 155 LI--NTNLRRDALRHCLDTSKARALIFGSEMASAVYEIQAILdPTLTLF--CSGSwEPSTVPANTEHLDPLLEDAPKHLP 230
Cdd:PRK07656 82 VVplNTRYTADEAAYILARGDAKALFVLGLFLGVDYSATTRL-PALEHVviCETE-EDDPHTEKMKTFTDFLAAGDPAER 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 231 SIPDKGfTDKLFYIYTSGTTGLPKAAIVVHSRYYRMAALVYYGFRMRPDDIVYDCLPLYHSAGNIVGIGQCVLHGMTVVI 310
Cdd:PRK07656 160 APEVDP-DDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLAANPFFHVFGYKAGVNAPLMRGATILP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 311 RKKFSASRFWDDCIKYNCTIVQYIGELCRYLLNQPPREAESRHKVRMALGNG------LRQSiwtdFSSRFHIPQVAEFY 384
Cdd:PRK07656 239 LPVFDPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSAEDLSSLRLAVTGAasmpvaLLER----FESELGVDIVLTGY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 385 GATECN-----CSLGN-FDSQVGACGfnsrilsfvYPIRLVRVNedtmelIRGPDGVCIPcqPGQPGQLVGR---IIQ-- 453
Cdd:PRK07656 315 GLSEASgvttfNRLDDdRKTVAGTIG---------TAIAGVENK------IVNELGEEVP--VGEVGELLVRgpnVMKgy 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 454 -QDPLR-----RFDGYLNqgannkkiasdvfkkgdqaylTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSR 527
Cdd:PRK07656 378 yDDPEAtaaaiDADGWLH---------------------TGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYE 436
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 291084711 528 LLQMADVAVYGveVPGAE-GRAGMA-AVASPTSNCDLESFAQTLKKELPLYARPIFLRFLPELHKTGTFKFQKTELRKE 604
Cdd:PRK07656 437 HPAVAEAAVIG--VPDERlGEVGKAyVVLKPGAELTEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRALREK 513
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
84-611 |
6.68e-37 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 145.31 E-value: 6.68e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 84 VRRH----PDKTALIFEGTNTHWtfRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKLGVEAALINTN 159
Cdd:PRK07786 23 LARHalmqPDAPALRFLGNTTTW--RELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 160 LRRDALRHCLDTSKARALIFGSEMASAVYEIQAIlDPTLTLFCSGSWEPSTVPANTEhlDPLLEDAPKHLP-SIPDKgfT 238
Cdd:PRK07786 101 LTPPEIAFLVSDCGAHVVVTEAALAPVATAVRDI-VPLLSTVVVAGGSSDDSVLGYE--DLLAEAGPAHAPvDIPND--S 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 239 DKLFyIYTSGTTGLPKAAIVVHSRYYRMAALVYYGFRM-RPDDIVYDCLPLYHSAGnIVGIGQCVLHGMTVVIR--KKFS 315
Cdd:PRK07786 176 PALI-MYTSGTTGRPKGAVLTHANLTGQAMTCLRTNGAdINSDVGFVGVPLFHIAG-IGSMLPGLLLGAPTVIYplGAFD 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 316 ASRFWDDCIKYNCTIVQYIGELCRYLLNQPprEAESRH-KVRMaLGNGL---RQSIWTDFSSRFHIPQVAEFYGATECN- 390
Cdd:PRK07786 254 PGQLLDVLEAEKVTGIFLVPAQWQAVCAEQ--QARPRDlALRV-LSWGAapaSDTLLRQMAATFPEAQILAAFGQTEMSp 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 391 --CSLGNFDS--QVGACGfnsrilsFVYPIRLVRVNEDTMELIrgpdgvcipcQPGQpgqlVGRIIQQDPlRRFDGYLnq 466
Cdd:PRK07786 331 vtCMLLGEDAirKLGSVG-------KVIPTVAARVVDENMNDV----------PVGE----VGEIVYRAP-TLMSGYW-- 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 467 gaNNKKIASDVFKKGdqAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLQMADVAVYG------VE 540
Cdd:PRK07786 387 --NNPEATAEAFAGG--WFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGradekwGE 462
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 291084711 541 VPGAegragMAAVASPTSNCDLESFAQTLKKELPLYARPIFLRFLPELHKTGTFKFQKTELRKEGFDPSVV 611
Cdd:PRK07786 463 VPVA-----VAAVRNDDAALTLEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKVLKTELRERYGACVNV 528
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
102-603 |
3.68e-35 |
|
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: 137.85 E-value: 3.68e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 102 WTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALRHCLDTSKARALIFGS 181
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 182 EmasavyeiqaildptltlfcsgswepstvpantehldplledapkhlpsipdkgftDKLFYIYTSGTTGLPKAAIVVHS 261
Cdd:cd05972 81 E--------------------------------------------------------DPALIYFTSGTTGLPKGVLHTHS 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 262 ryYRMAALVYYGF--RMRPDDIVY---DCLPLYHSAGNIVGIgqcVLHGMTVVI--RKKFSASRFWDDCIKYNCTIVQYI 334
Cdd:cd05972 105 --YPLGHIPTAAYwlGLRPDDIHWniaDPGWAKGAWSSFFGP---WLLGATVFVyeGPRFDAERILELLERYGVTSFCGP 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 335 GELCRYLLNQ-PPREAESRHKVRMALGNGLRQSIWTDFSSRFHIPqVAEFYGATECNCSLGNF---DSQVGACGfnsril 410
Cdd:cd05972 180 PTAYRMLIKQdLSSYKFSHLRLVVSAGEPLNPEVIEWWRAATGLP-IRDGYGQTETGLTVGNFpdmPVKPGSMG------ 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 411 sfvYPIRLVRVnedtmELIRGpDGVciPCQPGQPGQLVgriIQQDPLRRFDGYLNqgaNNKKIASdvfKKGDQAYLTGDV 490
Cdd:cd05972 253 ---RPTPGYDV-----AIIDD-DGR--ELPPGEEGDIA---IKLPPPGLFLGYVG---DPEKTEA---SIRGDYYLTGDR 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 491 LVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLQMADVAVYGV--EVPGAEGRAGMAAVAS-PTSNCDLESFAQ 567
Cdd:cd05972 313 AYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSpdPVRGEVVKAFVVLTSGyEPSEELAEELQG 392
|
490 500 510
....*....|....*....|....*....|....*.
gi 291084711 568 TLKKELPLYARPIFLRFLPELHKTGTFKFQKTELRK 603
Cdd:cd05972 393 HVKKVLAPYKYPREIEFVEELPKTISGKIRRVELRD 428
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
84-604 |
1.76e-33 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 134.32 E-value: 1.76e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 84 VRRHPDKTALIFEgtNTHWTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRD 163
Cdd:PRK03640 12 AFLTPDRTAIEFE--EKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSRE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 164 ALRHCLDTSKARALIFGSEMASAVYEIQAILDPTLtlfcSGSWEPSTVPANTEHLDplledapkHLPSIpdkgftdklfy 243
Cdd:PRK03640 90 ELLWQLDDAEVKCLITDDDFEAKLIPGISVKFAEL----MNGPKEEAEIQEEFDLD--------EVATI----------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 244 IYTSGTTGLPKAAIVVHSRYYRMA---ALvyyGFRMRPDDIVYDCLPLYHSAG-NIvgIGQCVLHGMTVVIRKKFSASRF 319
Cdd:PRK03640 147 MYTSGTTGKPKGVIQTYGNHWWSAvgsAL---NLGLTEDDCWLAAVPIFHISGlSI--LMRSVIYGMRVVLVEKFDAEKI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 320 WDDCIKYNCTIVQYIGELCRYLLNQPPREAESRHKVRMALGNG------LRQsiwtdfSSRFHIPqVAEFYGATECNcsl 393
Cdd:PRK03640 222 NKLLQTGGVTIISVVSTMLQRLLERLGEGTYPSSFRCMLLGGGpapkplLEQ------CKEKGIP-VYQSYGMTETA--- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 394 gnfdSQVGAcgfnsriLSFvypirlvrvnEDTMELIrG-------PDGVCIP--CQPGQPGQlVGRIIQQDPlRRFDGYL 464
Cdd:PRK03640 292 ----SQIVT-------LSP----------EDALTKL-GsagkplfPCELKIEkdGVVVPPFE-EGEIVVKGP-NVTKGYL 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 465 NQ-GANNKKIASDVFKKGDQAYLtgdvlvmDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLQMADVAVYGVE--- 540
Cdd:PRK03640 348 NReDATRETFQDGWFKTGDIGYL-------DEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPddk 420
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 291084711 541 ---VPGAEGRAGmaavasptSNCDLESFAQTLKKELPLYARPIFLRFLPELHKTGTFKFQKTELRKE 604
Cdd:PRK03640 421 wgqVPVAFVVKS--------GEVTEEELRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHELKQL 479
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
84-602 |
1.92e-33 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 134.43 E-value: 1.92e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 84 VRRHPDKTALIFEGTNTHWTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRD 163
Cdd:PRK13391 7 AQTTPDKPAVIMASTGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 164 ALRHCLDTSKARALIfGSEMASAVYEIQAILDPTLTLfcsgsWEPSTVPANTEHLDPlLEDAPKHLPS--IPDKGFTDKL 241
Cdd:PRK13391 87 EAAYIVDDSGARALI-TSAAKLDVARALLKQCPGVRH-----RLVLDGDGELEGFVG-YAEAVAGLPAtpIADESLGTDM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 242 FyiYTSGTTGLPKAAI-------VVHSRYYRMAALVYYGFRmrpDDIVYDC-LPLYHSAGN-IVGIGQCVlhGMTVVIRK 312
Cdd:PRK13391 160 L--YSSGTTGRPKGIKrplpeqpPDTPLPLTAFLQRLWGFR---SDMVYLSpAPLYHSAPQrAVMLVIRL--GGTVIVME 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 313 KFSASRFWDDCIKYNCTIVQYIGELCRYLLnQPPREAESRHKVrmalgNGLRQSI-----------------WTdfssrf 375
Cdd:PRK13391 233 HFDAEQYLALIEEYGVTHTQLVPTMFSRML-KLPEEVRDKYDL-----SSLEVAIhaaapcppqvkeqmidwWG------ 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 376 hiPQVAEFYGATECNcslgnfdsqvGACGFNSRiLSFVYPIRLVRVNEDTMElIRGPDGVciPCQPGQPGQlvgriIQQD 455
Cdd:PRK13391 301 --PIIHEYYAATEGL----------GFTACDSE-EWLAHPGTVGRAMFGDLH-ILDDDGA--ELPPGEPGT-----IWFE 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 456 PLRRFDgYLNQGANNKKIASDvfkkgDQAYLT-GDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLQMADV 534
Cdd:PRK13391 360 GGRPFE-YLNDPAKTAEARHP-----DGTWSTvGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADA 433
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 291084711 535 AVYGveVPGAEGRAGMAAVASPTSNCDL-ESFAQTL----KKELPLYARPIFLRFLPELHKTGTFKFQKTELR 602
Cdd:PRK13391 434 AVFG--VPNEDLGEEVKAVVQPVDGVDPgPALAAELiafcRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLLR 504
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
78-602 |
9.36e-33 |
|
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: 132.49 E-value: 9.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 78 LLFASVVRRHPDKTALIfeGTNTHWTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKLGVEAALIN 157
Cdd:cd05959 8 LVDLNLNEGRGDKTAFI--DDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 158 TNLRRDALRHCLDTSKARALIFGSEMASAVYEIQAILDPTL-TLFCSGSWEPSTVPANTEHLDPLLEDAPKHLPSIPDkg 236
Cdd:cd05959 86 TLLTPDDYAYYLEDSRARVVVVSGELAPVLAAALTKSEHTLvVLIVSGGAGPEAGALLLAELVAAEAEQLKPAATHAD-- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 237 ftDKLFYIYTSGTTGLPKAAIVVHSRYYRMAALvyYG---FRMRPDDIVYDCLPLYHSagniVGIGQCVLH----GMTVV 309
Cdd:cd05959 164 --DPAFWLYSSGSTGRPKGVVHLHADIYWTAEL--YArnvLGIREDDVCFSAAKLFFA----YGLGNSLTFplsvGATTV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 310 IRKKF-SASRFWDDCIKYNCTIVQYIGELCRYLLNQPPREAESRHKVRMAL--GNGLRQSIWTDFSSRFHIpQVAEFYGA 386
Cdd:cd05959 236 LMPERpTPAAVFKRIRRYRPTVFFGVPTLYAAMLAAPNLPSRDLSSLRLCVsaGEALPAEVGERWKARFGL-DILDGIGS 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 387 TEC-NCSLGNF--DSQVGACGFNsrilsfV--YPIRLvrvnedtmeliRGPDGVCIPcqPGQPGQLVGRIIQQDPlrrfd 461
Cdd:cd05959 315 TEMlHIFLSNRpgRVRYGTTGKP------VpgYEVEL-----------RDEDGGDVA--DGEPGELYVRGPSSAT----- 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 462 GYLNQGANNKKiasdVFKKGdqAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEgtlSRLLQMADV---AVYG 538
Cdd:cd05959 371 MYWNNRDKTRD----TFQGE--WTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVE---SALVQHPAVleaAVVG 441
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 291084711 539 VEVPgaEGRAGMAAVASPTSNCDLESFAQT-----LKKELPLYARPIFLRFLPELHKTGTFKFQKTELR 602
Cdd:cd05959 442 VEDE--DGLTKPKAFVVLRPGYEDSEALEEelkefVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
85-603 |
2.93e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 131.59 E-value: 2.93e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 85 RRHPDKTALIFE-GTnthWTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRD 163
Cdd:PRK07788 60 RRAPDRAALIDErGT---LTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGP 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 164 ALRHCLDTSKARALIFGSEMASAVYEIQAILDPTLTLFCSGSWEPSTVPAnTEHLDPLLE-DAPKHLPSIPDKGFtdklF 242
Cdd:PRK07788 137 QLAEVAAREGVKALVYDDEFTDLLSALPPDLGRLRAWGGNPDDDEPSGST-DETLDDLIAgSSTAPLPKPPKPGG----I 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 243 YIYTSGTTGLPKAAIVVHSRYYRMAALVYYGFRMRPDDIVYDCLPLYHSagniVGIGQCVL---HGMTVVIRKKFSASRF 319
Cdd:PRK07788 212 VILTSGTTGTPKGAPRPEPSPLAPLAGLLSRVPFRAGETTLLPAPMFHA----TGWAHLTLamaLGSTVVLRRRFDPEAT 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 320 WDDCIKYNCTIVQYIGELCRYLLNQPPREAE----SRHKVRMALGNGLRQSIWTDFSSRFHiPQVAEFYGATECN-CSLG 394
Cdd:PRK07788 288 LEDIAKHKATALVVVPVMLSRILDLGPEVLAkydtSSLKIIFVSGSALSPELATRALEAFG-PVLYNLYGSTEVAfATIA 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 395 NFDSQVGACGFNSRilsfvyPIRLVRVNedtmelIRGPDGVCIPcqPGQpgqlVGRIIQQDPLrRFDGYLNQGanNKKIA 474
Cdd:PRK07788 367 TPEDLAEAPGTVGR------PPKGVTVK------ILDENGNEVP--RGV----VGRIFVGNGF-PFEGYTDGR--DKQII 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 475 SDVFKKGDQAYLtgdvlvmDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLQMADVAVYGVEVP--GAEGRAgmAA 552
Cdd:PRK07788 426 DGLLSSGDVGYF-------DEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEefGQRLRA--FV 496
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 291084711 553 VASPTSNCDLESFAQTLKKELPLYARPIFLRFLPELHKTGTFKFQKTELRK 603
Cdd:PRK07788 497 VKAPGAALDEDAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELRE 547
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
85-602 |
3.20e-32 |
|
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: 131.08 E-value: 3.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 85 RRHPDKTALIF---EGTNTHWTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLR 161
Cdd:cd05970 28 KEYPDKLALVWcddAGEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQLT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 162 RDALRHCLDTSKARALIFGSEmASAVYEIQAIL----DPTLTLFCSGSwepstVPANTEHLDPLLEDAPKHL--PSIPDK 235
Cdd:cd05970 108 AKDIVYRIESADIKMIVAIAE-DNIPEEIEKAApecpSKPKLVWVGDP-----VPEGWIDFRKLIKNASPDFerPTANSY 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 236 GFTDKLFYIY-TSGTTGLPKaaIVVHSRYYRMAALVY--YGFRMRPDDIvydclplyHSAGNIVGIGQCV--------LH 304
Cdd:cd05970 182 PCGEDILLVYfSSGTTGMPK--MVEHDFTYPLGHIVTakYWQNVREGGL--------HLTVADTGWGKAVwgkiygqwIA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 305 GMTVVI--RKKFSASRFWDDCIKYNCTIVQYIGELCRYLLnqppREAESRH---KVRMAL--GNGLRQSIWTDFSSRFHI 377
Cdd:cd05970 252 GAAVFVydYDKFDPKALLEKLSKYGVTTFCAPPTIYRFLI----REDLSRYdlsSLRYCTtaGEALNPEVFNTFKEKTGI 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 378 pQVAEFYGATECNCSLGNF---DSQVGACGFNSRilsfVYPIRLVRvnedtmelirgPDGVciPCQPGQPGQLVGRIIQQ 454
Cdd:cd05970 328 -KLMEGFGQTETTLTIATFpwmEPKPGSMGKPAP----GYEIDLID-----------REGR--SCEAGEEGEIVIRTSKG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 455 DPLRRFDGYlnqGANNKKIASdVFKKGdqAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLQMADV 534
Cdd:cd05970 390 KPVGLFGGY---YKDAEKTAE-VWHDG--YYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLEC 463
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 291084711 535 AVYGVEVPgaegRAGMAAVASPTSNCDLESfAQTLKKEL--------PLYARPIFLRFLPELHKTGTFKFQKTELR 602
Cdd:cd05970 464 AVTGVPDP----IRGQVVKATIVLAKGYEP-SEELKKELqdhvkkvtAPYKYPRIVEFVDELPKTISGKIRRVEIR 534
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
103-602 |
5.77e-32 |
|
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.
Pssm-ID: 341243 [Multi-domain] Cd Length: 436 Bit Score: 128.73 E-value: 5.77e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 103 TFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALRHCLDTSKARALIFGSE 182
Cdd:cd05919 12 TYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVVTSAD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 183 masavyeiqaildptltlfcsgswepstvpantehldplledapkhlpsipdkgftDKLFYIYTSGTTGLPKAAIVVHSR 262
Cdd:cd05919 92 --------------------------------------------------------DIAYLLYSSGTTGPPKGVMHAHRD 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 263 YYRMA-ALVYYGFRMRPDDIVYDCLPLY--HSAGNIVGIGQCVlhGMTVVIRKKF-SASRFWDDCIKYNCTIVQYIGELC 338
Cdd:cd05919 116 PLLFAdAMAREALGLTPGDRVFSSAKMFfgYGLGNSLWFPLAV--GASAVLNPGWpTAERVLATLARFRPTVLYGVPTFY 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 339 RYLLNQPPREAESRHKVRMAL--GNGLRQSIWTDFSSRFHIPqVAEFYGATEC-NCSLGNFDSQV--GACGfnsRILSFv 413
Cdd:cd05919 194 ANLLDSCAGSPDALRSLRLCVsaGEALPRGLGERWMEHFGGP-ILDGIGATEVgHIFLSNRPGAWrlGSTG---RPVPG- 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 414 YPIRLVrvnedtmelirGPDGVCIPcqPGQPGQLVGRIIQQDPlrrfdGYLNqganNKKIASDVFKKGdqAYLTGDVLVM 493
Cdd:cd05919 269 YEIRLV-----------DEEGHTIP--PGEEGDLLVRGPSAAV-----GYWN----NPEKSRATFNGG--WYRTGDKFCR 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 494 DELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLQMADVAVygVEVPGAEGRAGMAAVASPTSNCD-----LESFAQT 568
Cdd:cd05919 325 DADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAV--VAVPESTGLSRLTAFVVLKSPAApqeslARDIHRH 402
|
490 500 510
....*....|....*....|....*....|....
gi 291084711 569 LKKELPLYARPIFLRFLPELHKTGTFKFQKTELR 602
Cdd:cd05919 403 LLERLSAHKVPRRIAFVDELPRTATGKLQRFKLR 436
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
74-595 |
8.33e-32 |
|
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: 129.55 E-value: 8.33e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 74 KTVPLLFASVVRRHPDKTALIFEGTNTHWTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKLGVEA 153
Cdd:cd05923 1 QTVFEMLRRAASRAPDACAIADPARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 154 ALINTNLRRDALRHCLDTSKARALIfgseMASAVYEIQAILDPTLTLFCSGSWEPSTVPantEHLDPLLEDapkhlpsiP 233
Cdd:cd05923 81 ALINPRLKAAELAELIERGEMTAAV----IAVDAQVMDAIFQSGVRVLALSDLVGLGEP---ESAGPLIED--------P 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 234 DKGFTDKLFYIYTSGTTGLPKAAIVVH----SRYYRMAALVyyGFRMRPDDIVYDCLPLYHSAGNI-VGIGQCVLHGMTV 308
Cdd:cd05923 146 PREPEQPAFVFYTSGTTGLPKGAVIPQraaeSRVLFMSTQA--GLRHGRHNVVLGLMPLYHVIGFFaVLVAALALDGTYV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 309 VIRkKFSASRfwddcikynctIVQYIGEL---CRYL-----------LNQPPREAESRHKVRMAlGNGLRQSIWTDFSSR 374
Cdd:cd05923 224 VVE-EFDPAD-----------ALKLIEQErvtSLFAtpthldalaaaAEFAGLKLSSLRHVTFA-GATMPDAVLERVNQH 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 375 FHIPQVaEFYGATECNCSLGNFDSQVGAC---GFNSRilsfvypIRLVRVNEDTMELIrgpdgvcipcQPGQPGQLvgrI 451
Cdd:cd05923 291 LPGEKV-NIYGTTEAMNSLYMRDARTGTEmrpGFFSE-------VRIVRIGGSPDEAL----------ANGEEGEL---I 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 452 IQQDPLRRFDGYLNQGANNKKiasdvfKKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLQM 531
Cdd:cd05923 350 VAAAADAAFTGYLNQPEATAK------KLQDGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGV 423
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 532 ADVAVYGVevpgAEGRAGMAAVA------SPTSNCDLESFAQTlkKELPLYARPIFLRFLPELHKTGTFK 595
Cdd:cd05923 424 TEVVVIGV----ADERWGQSVTAcvvpreGTLSADELDQFCRA--SELADFKRPRRYFFLDELPKNAMNK 487
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
92-602 |
8.59e-31 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 126.56 E-value: 8.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 92 ALIFEGTNTHWTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALRHCLDT 171
Cdd:PRK08276 2 AVIMAPSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 172 SKARALIFGSEMASAVYEIQAILDPTLTLFCSGSWEPSTVpantEHLDPLLEDAPKhlPSIPDKGFTDKLfyIYTSGTTG 251
Cdd:PRK08276 82 SGAKVLIVSAALADTAAELAAELPAGVPLLLVVAGPVPGF----RSYEEALAAQPD--TPIADETAGADM--LYSSGTTG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 252 LPKA------AIVVHSRYYRMAALVYYGFRMRPDDIVYDCLPLYHSAgnIVGIGQCVLH-GMTVVIRKKFSASRFWDDCI 324
Cdd:PRK08276 154 RPKGikrplpGLDPDEAPGMMLALLGFGMYGGPDSVYLSPAPLYHTA--PLRFGMSALAlGGTVVVMEKFDAEEALALIE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 325 KYNCTIVQYIGELCRYLLNQPPrEAESRHkvrmalgnglrqsiwtDFSS-RFHI-------------------PQVAEFY 384
Cdd:PRK08276 232 RYRVTHSQLVPTMFVRMLKLPE-EVRARY----------------DVSSlRVAIhaaapcpvevkramidwwgPIIHEYY 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 385 GATECNcslgnfdsqvGACGFNSR------------ILSFVypirlvrvnedtmeLIRGPDGVciPCQPGQPGQlvgrII 452
Cdd:PRK08276 295 ASSEGG----------GVTVITSEdwlahpgsvgkaVLGEV--------------RILDEDGN--ELPPGEIGT----VY 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 453 QQDPLRRFDgYLNQGAnnKKIASDVfkkgDQAYLT-GDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLQM 531
Cdd:PRK08276 345 FEMDGYPFE-YHNDPE--KTAAARN----PHGWVTvGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKV 417
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 291084711 532 ADVAVYGveVPGAE-GRAGMAAV-------ASPTSNCDLESFaqtLKKELPLYARPIFLRFLPELHKTGTFKFQKTELR 602
Cdd:PRK08276 418 ADVAVFG--VPDEEmGERVKAVVqpadgadAGDALAAELIAW---LRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLR 491
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
74-602 |
2.34e-30 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 126.04 E-value: 2.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 74 KTVPLLFASVVRRHPDKTALIFEGTNTHWTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKLGVEA 153
Cdd:PRK12583 18 QTIGDAFDATVARFPDREALVVRHQALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAIL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 154 ALINTNLRRDALRHCLDTSKARALIFGSEMASAVYE--IQAILdPTLTLFCSGSWEPSTVP--ANTEHLDPlleDAPKHL 229
Cdd:PRK12583 98 VNINPAYRASELEYALGQSGVRWVICADAFKTSDYHamLQELL-PGLAEGQPGALACERLPelRGVVSLAP---APPPGF 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 230 PSIPD-----KGFTDK-LFYI-------------YTSGTTGLPKAAIVVHSRYYRMAALVYYGFRMRPDDIVYDCLPLYH 290
Cdd:PRK12583 174 LAWHElqargETVSREaLAERqasldrddpiniqYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCVPVPLYH 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 291 SAGNIVGIGQCVLHGMTVVI-RKKFSASRFWDDCIKYNCTIVQ-----YIGElcrylLNQPPREAESRHKVRMALGNG-- 362
Cdd:PRK12583 254 CFGMVLANLGCMTVGACLVYpNEAFDPLATLQAVEEERCTALYgvptmFIAE-----LDHPQRGNFDLSSLRTGIMAGap 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 363 -----LRQSIwtdfsSRFHIPQVAEFYGATECNcslgnfdsqvgacgfnsrilsfvyPIRLVRVNEDTMEL--------- 428
Cdd:PRK12583 329 cpievMRRVM-----DEMHMAEVQIAYGMTETS------------------------PVSLQTTAADDLERrvetvgrtq 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 429 ------IRGPDGVCIPcqPGQPGQLVGR---IIQqdplrrfdGYLNqgaNNKKIASDVFKKGdqaYL-TGDVLVMDELGY 498
Cdd:PRK12583 380 phlevkVVDPDGATVP--RGEIGELCTRgysVMK--------GYWN---NPEATAESIDEDG---WMhTGDLATMDEQGY 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 499 LYFRDRTGDTFRWKGENVSTTEVEGTLSRLLQMADVAVYGveVPGAE-GRAGMAAVA-SPTSNCDLESFAQTLKKELPLY 576
Cdd:PRK12583 444 VRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFG--VPDEKyGEEIVAWVRlHPGHAASEEELREFCKARIAHF 521
|
570 580
....*....|....*....|....*.
gi 291084711 577 ARPIFLRFLPELHKTGTFKFQKTELR 602
Cdd:PRK12583 522 KVPRYFRFVDEFPMTVTGKVQKFRMR 547
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
76-544 |
5.04e-30 |
|
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: 124.27 E-value: 5.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 76 VPLLFASvvrRHPDKTALIFEGTNTHWTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKLGVEAAL 155
Cdd:cd05904 10 VSFLFAS---AHPSRPALIDAATGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 156 INTNLRRDALRHCLDTSKARaLIFgseMASAVYE-IQAILDPTLTLfcsgswepSTVPANTEHLDPLLEDAPKHLPSIPD 234
Cdd:cd05904 87 ANPLSTPAEIAKQVKDSGAK-LAF---TTAELAEkLASLALPVVLL--------DSAEFDSLSFSDLLFEADEAEPPVVV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 235 KGFTDKLFYIYTSGTTGLPKAAIVVHSRYYRMAALVYYGFRMRPD-DIVYDC-LPLYHSAGnIVGIGQCVLH-GMTVVIR 311
Cdd:cd05904 155 IKQDDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQFVAGEGSNSDsEDVFLCvLPMFHIYG-LSSFALGLLRlGATVVVM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 312 KKFSASRFWDDCIKYNCTIVQYIGELCRYLLNQPPREAESRHKVRMALGNG--LRQSIWTDFSSRFHIPQVAEFYGATEC 389
Cdd:cd05904 234 PRFDLEELLAAIERYKVTHLPVVPPIVLALVKSPIVDKYDLSSLRQIMSGAapLGKELIEAFRAKFPNVDLGQGYGMTES 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 390 NCSL------GNFDSQVGACGfnsrilsfvypiRLVR------VNEDTmelirgpdGVCIPcqPGQPGQLVGR---IIQq 454
Cdd:cd05904 314 TGVVamcfapEKDRAKYGSVG------------RLVPnveakiVDPET--------GESLP--PNQTGELWIRgpsIMK- 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 455 dplrrfdGYLNqgaNNKKIASDVFKKGdqaYL-TGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLQMAD 533
Cdd:cd05904 371 -------GYLN---NPEATAATIDKEG---WLhTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILD 437
|
490
....*....|....*..
gi 291084711 534 VAVYGV------EVPGA 544
Cdd:cd05904 438 AAVIPYpdeeagEVPMA 454
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
111-595 |
2.17e-29 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 121.78 E-value: 2.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 111 SSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKLGVEAALI----NTNLRRDALRHCLDTSKARALIfgsemasa 186
Cdd:cd05922 3 VSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRLGLVfvplNPTLKESVLRYLVADAGGRIVL-------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 187 vyeIQAILDPTLTLFCSGSWEPSTVpANTEHLDPLLEDAPKHLPSIPDKGFtdklfYIYTSGTTGLPKAAIVVHSRYYRM 266
Cdd:cd05922 75 ---ADAGAADRLRDALPASPDPGTV-LDADGIRAARASAPAHEVSHEDLAL-----LLYTSGSTGSPKLVRLSHQNLLAN 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 267 AALVYYGFRMRPDDIVYDCLPLYHSAGNIVgIGQCVLHGMTVVIRKKFSASR-FWDDCIKYNCT---IVQYIGELCRYLl 342
Cdd:cd05922 146 ARSIAEYLGITADDRALTVLPLSYDYGLSV-LNTHLLRGATLVLTNDGVLDDaFWEDLREHGATglaGVPSTYAMLTRL- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 343 NQPPREAESRHKVRMAlGNGLRQSIWTDFSSRFHIPQVAEFYGATECncslgnfdsqvgacgfnSRILSFVYPIRLVRVN 422
Cdd:cd05922 224 GFDPAKLPSLRYLTQA-GGRLPQETIARLRELLPGAQVYVMYGQTEA-----------------TRRMTYLPPERILEKP 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 423 E-------DTMELIRGPDGVciPCQPGQPGQLVGRiiqqDPLRrFDGYLNQGANNKKIAsdvfKKGDQAYlTGDVLVMDE 495
Cdd:cd05922 286 GsiglaipGGEFEILDDDGT--PTPPGEPGEIVHR----GPNV-MKGYWNDPPYRRKEG----RGGGVLH-TGDLARRDE 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 496 LGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLQMADVAVYGVEVPGAEgraGMAAVASPTSNCDLESFAQTLKKELPL 575
Cdd:cd05922 354 DGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDPLGE---KLALFVTAPDKIDPKDVLRSLAERLPP 430
|
490 500
....*....|....*....|
gi 291084711 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 |
1.89e-28 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 118.69 E-value: 1.89e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 96 EGTNTHWTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALRHCLDTSKAR 175
Cdd:cd05971 1 KGTPEKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 176 ALIfgsemasavyeiqaildptltlfCSGSWEPSTVpantehldplledapkhlpsipdkgftdklfyIYTSGTTGLPKA 255
Cdd:cd05971 81 ALV-----------------------TDGSDDPALI--------------------------------IYTSGTTGPPKG 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 256 AIVVHSRYYRMAALVYYGFRM-RPDDIVYdclplYHSA--GNIVGIGQCVL----HGMTVVIRK--KFSASRFWDDCIKY 326
Cdd:cd05971 106 ALHAHRVLLGHLPGVQFPFNLfPRDGDLY-----WTPAdwAWIGGLLDVLLpslyFGVPVLAHRmtKFDPKAALDLMSRY 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 327 NCTIVQYIGELCRYLLNQPPREAESRHKVRM------ALGNGLRQsiWTdfSSRFHIPqVAEFYGATECNCSLGN----F 396
Cdd:cd05971 181 GVTTAFLPPTALKMMRQQGEQLKHAQVKLRAiatggeSLGEELLG--WA--REQFGVE-VNEFYGQTECNLVIGNcsalF 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 397 DSQVGACGFnsrilsfVYPIRLVRVNEDTMElirgpdgvciPCQPGQPGQLVgrIIQQDPLRrFDGYL-NQGANNKKIAS 475
Cdd:cd05971 256 PIKPGSMGK-------PIPGHRVAIVDDNGT----------PLPPGEVGEIA--VELPDPVA-FLGYWnNPSATEKKMAG 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 476 DVFkkgdqayLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLQMADVAVYGV--EVPGAEGRAGMAAV 553
Cdd:cd05971 316 DWL-------LTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIpdPIRGEIVKAFVVLN 388
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 291084711 554 ASPTSNCDLESFAQTL-KKELPLYARPIFLRFLPELHKTGTFKFQKTELR 602
Cdd:cd05971 389 PGETPSDALAREIQELvKTRLAAHEYPREIEFVNELPRTATGKIRRRELR 438
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
103-603 |
1.96e-28 |
|
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.
Pssm-ID: 341229 [Multi-domain] Cd Length: 437 Bit Score: 118.64 E-value: 1.96e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 103 TFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALRHCLDTSKARALIfgse 182
Cdd:cd05903 3 TYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFV---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 183 masavyeiqaildpTLTLFcsGSWEPSTVPANTEHLdplledapkhlpsipdkgftdklfyIYTSGTTGLPKAaiVVHSR 262
Cdd:cd05903 79 --------------VPERF--RQFDPAAMPDAVALL-------------------------LFTSGTTGEPKG--VMHSH 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 263 YYRMAALVYYGFRM--RPDDIVYDCLPLYHSAGNIVGIGQCVLHGMTVVIRKKFSASRFWDDCIKYNCTIVQ----YIGE 336
Cdd:cd05903 116 NTLSASIRQYAERLglGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQDIWDPDKALALMREHGVTFMMgatpFLTD 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 337 LCRYLLNQPPREaeSRHKVRMALGNGLRQSIWTDFSSRFhIPQVAEFYGATECNCSLGNFDSqvGACGFNSRILSFVYPI 416
Cdd:cd05903 196 LLNAVEEAGEPL--SRLRTFVCGGATVPRSLARRAAELL-GAKVCSAYGSTECPGAVTSITP--APEDRRLYTDGRPLPG 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 417 RLVRVNEDtmelirgpDGVCIPcqPGQPGQLVGRIIQQdplrrFDGYLNQGANNKKIASDVFkkgdqaYLTGDVLVMDEL 496
Cdd:cd05903 271 VEIKVVDD--------TGATLA--PGVEGELLSRGPSV-----FLGYLDRPDLTADAAPEGW------FRTGDLARLDED 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 497 GYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLQMADVAVygVEVPGAegRAG--MAAVASPTSNC--DLESFAQTLKKE 572
Cdd:cd05903 330 GYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAV--VALPDE--RLGerACAVVVTKSGAllTFDELVAYLDRQ 405
|
490 500 510
....*....|....*....|....*....|..
gi 291084711 573 -LPLYARPIFLRFLPELHKTGTFKFQKTELRK 603
Cdd:cd05903 406 gVAKQYWPERLVHVDDLPRTPSGKVQKFRLRE 437
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
85-604 |
8.67e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 117.29 E-value: 8.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 85 RRHPDKTALIFEGTNThwTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRDA 164
Cdd:PRK06145 13 RRTPDRAALVYRDQEI--SYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 165 LRHCLDTSKARALIFGSEMAS--AVYEIQAILDptltlfcsgswepSTVPANTEHLDPLLEDAPKHLPSIPDkgftDKLF 242
Cdd:PRK06145 91 VAYILGDAGAKLLLVDEEFDAivALETPKIVID-------------AAAQADSRRLAQGGLEIPPQAAVAPT----DLVR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 243 YIYTSGTTGLPKAAIVVHSRYYRMAALVYYGFRMRPDDIVYDCLPLYH-SAGNIVGIGqcVL-HGMTVVIRKKFSASRFW 320
Cdd:PRK06145 154 LMYTSGTTDRPKGVMHSYGNLHWKSIDHVIALGLTASERLLVVGPLYHvGAFDLPGIA--VLwVGGTLRIHREFDPEAVL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 321 DDCIKYNCTIVQYIGELCRYLLNQPPREAESRHKVRMALGNGLR--QSIWTDFSSRFHIPQVAEFYGATEcNCSLGNFDS 398
Cdd:PRK06145 232 AAIERHRLTCAWMAPVMLSRVLTVPDRDRFDLDSLAWCIGGGEKtpESRIRDFTRVFTRARYIDAYGLTE-TCSGDTLME 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 399 Q---VGACGFNSRILSFVyPIRlvrvnedtmelIRGPDGVCIPcqPGQPGQ--LVGRIIQQdplrrfdGYLNqgaNNKKI 473
Cdd:PRK06145 311 AgreIEKIGSTGRALAHV-EIR-----------IADGAGRWLP--PNMKGEicMRGPKVTK-------GYWK---DPEKT 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 474 ASDVFkkgDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLQMADVAVYGVEVPGAEGRAGMAAV 553
Cdd:PRK06145 367 AEAFY---GDWFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVV 443
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 291084711 554 ASPTSNCDLESFAQTLKKELPLYARPIFLRFLPELHKTGTFKFQKTELRKE 604
Cdd:PRK06145 444 LNPGATLTLEALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVLRDE 494
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
85-603 |
2.34e-27 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 117.36 E-value: 2.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 85 RRHPDKTALIF--EGTNTH----WTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNE-FVGLWLGMAKlGVeAALIN 157
Cdd:PRK07529 36 ARHPDAPALSFllDADPLDrpetWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPEtHFALWGGEAA-GI-ANPIN 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 158 TNLRRDALRHCLDTSKARALI-----FGSEMASAVYEIQAILDPTLTLFCSGS------WEPSTVPANTEH-------LD 219
Cdd:PRK07529 114 PLLEPEQIAELLRAAGAKVLVtlgpfPGTDIWQKVAEVLAALPELRTVVEVDLarylpgPKRLAVPLIRRKaharildFD 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 220 PLLEDAPK-HLPSIPDKGFTDKLFYIYTSGTTGLPKAAIVVHSRYYRMAALVYYGFRMRPDDIVYDCLPLYHSAGNIVGI 298
Cdd:PRK07529 194 AELARQPGdRLFSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPGDTVFCGLPLFHVNALLVTG 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 299 GQCVLHGMTVVI------RKKFSASRFWDDCIKYNCTIVQYIGELCRYLLNQPPrEAESRHKVRMALGNG--LRQSIWTD 370
Cdd:PRK07529 274 LAPLARGAHVVLatpqgyRGPGVIANFWKIVERYRINFLSGVPTVYAALLQVPV-DGHDISSLRYALCGAapLPVEVFRR 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 371 FSSRFHIPqVAEFYGATECNC-SLGNF---DSQVGACGfnsriLSFVYP-IRLVRVNEDtmelirGPDGVciPCQPGQpg 445
Cdd:PRK07529 353 FEAATGVR-IVEGYGLTEATCvSSVNPpdgERRIGSVG-----LRLPYQrVRVVILDDA------GRYLR--DCAVDE-- 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 446 qlVGRIIQQDPlRRFDGYLNqGANNKKIASdvfkkgDQAYL-TGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGT 524
Cdd:PRK07529 417 --VGVLCIAGP-NVFSGYLE-AAHNKGLWL------EDGWLnTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEA 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 525 LSRLLQMADVAVYGV------EVPGA--EGRAGMAAVASptsncDLESFAQTLKKELPlyARPIFLRFLPELHKTGTFKF 596
Cdd:PRK07529 487 LLRHPAVALAAAVGRpdahagELPVAyvQLKPGASATEA-----ELLAFARDHIAERA--AVPKHVRILDALPKTAVGKI 559
|
....*..
gi 291084711 597 QKTELRK 603
Cdd:PRK07529 560 FKPALRR 566
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
102-603 |
3.33e-27 |
|
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: 114.37 E-value: 3.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 102 WTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRdalrhcldtskaralifgS 181
Cdd:cd05912 2 YTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTP------------------N 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 182 EMASAVYEIQAILDPTLTLfcsgswepstvpantehldplledapkhlpsipdkgftdklfyIYTSGTTGLPKAAIVVHS 261
Cdd:cd05912 64 ELAFQLKDSDVKLDDIATI-------------------------------------------MYTSGTTGKPKGVQQTFG 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 262 RYYRMAALVYYGFRMRPDDIVYDCLPLYHSAGNIVgIGQCVLHGMTVVIRKKFSASRFWDDCIKYNCTIVQYIGELCRYL 341
Cdd:cd05912 101 NHWWSAIGSALNLGLTEDDNWLCALPLFHISGLSI-LMRSVIYGMTVYLVDKFDAEQVLHLINSGKVTIISVVPTMLQRL 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 342 LNQPPrEAESRHKVRMALGNGLRQSIWTDFSSRFHIPqVAEFYGATEcNCSlgnfdsQVGAcgfnsriLSFvypirlvrv 421
Cdd:cd05912 180 LEILG-EGYPNNLRCILLGGGPAPKPLLEQCKEKGIP-VYQSYGMTE-TCS------QIVT-------LSP--------- 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 422 nEDTMELIRGPDGVCIPCQ-----PGQPGQLVGRIIQQDPlRRFDGYLNQ-GANNKKIASDVFKKGDQAYLtgdvlvmDE 495
Cdd:cd05912 235 -EDALNKIGSAGKPLFPVElkiedDGQPPYEVGEILLKGP-NVTKGYLNRpDATEESFENGWFKTGDIGYL-------DE 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 496 LGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLQMADVAVYGveVPGAE-GRAGMAAVAS--PTSNCDLESFaqtLKKE 572
Cdd:cd05912 306 EGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVG--IPDDKwGQVPVAFVVSerPISEEELIAY---CSEK 380
|
490 500 510
....*....|....*....|....*....|.
gi 291084711 573 LPLYARPIFLRFLPELHKTGTFKFQKTELRK 603
Cdd:cd05912 381 LAKYKVPKKIYFVDELPRTASGKLLRHELKQ 411
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
79-602 |
1.08e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 114.46 E-value: 1.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 79 LFASVVRRHPDKTALIFEGTNThwTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKLGVEAALINT 158
Cdd:PRK06164 15 LLDAHARARPDAVALIDEDRPL--SRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 159 NLRRDALRHCLDTSKARALIF-----GSEMASAVYEIQAILDPTL---TLFCSGSWE-PSTVPANTeHLDPLLEDAPKHL 229
Cdd:PRK06164 93 RYRSHEVAHILGRGRARWLVVwpgfkGIDFAAILAAVPPDALPPLraiAVVDDAADAtPAPAPGAR-VQLFALPDPAPPA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 230 PSIPDKGFTDKLFYIY-TSGTTGLPKaaIVVHS-----RYYRMAALVYygfRMRPDDIVYDCLPL---YHSAGNIVGIGQ 300
Cdd:PRK06164 172 AAGERAADPDAGALLFtTSGTTSGPK--LVLHRqatllRHARAIARAY---GYDPGAVLLAALPFcgvFGFSTLLGALAG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 301 cvlhGMTVVIRKKFSASRFWDDCIKYNCTIVQYIGELCRYLLNQPPREAESRHkvrmalgngLRQSIWTDFSSRFH-IPQ 379
Cdd:PRK06164 247 ----GAPLVCEPVFDAARTARALRRHRVTHTFGNDEMLRRILDTAGERADFPS---------ARLFGFASFAPALGeLAA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 380 VAE--------FYGATECncsLGNFDSQVGACGFNSRILS---FVYPIRLVRvnedtmelIRGPDGVCIpCQPGQPGQlv 448
Cdd:PRK06164 314 LARargvpltgLYGSSEV---QALVALQPATDPVSVRIEGggrPASPEARVR--------ARDPQDGAL-LPDGESGE-- 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 449 griIQQDPLRRFDGYL-NQGANNKKIASD-VFKKGDQAYLTGDvlvmdelGYLYFRDRTGDTFRWKGENVSTTEVEGTLS 526
Cdd:PRK06164 380 ---IEIRAPSLMRGYLdNPDATARALTDDgYFRTGDLGYTRGD-------GQFVYQTRMGDSLRLGGFLVNPAEIEHALE 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 527 RLLQMADVAVYGVEVpgaEGRAGMAAVASPTSNC--DLESFAQTLKKELPLY---ARPIFLRFLPELHKTGTFKFQKTEL 601
Cdd:PRK06164 450 ALPGVAAAQVVGATR---DGKTVPVAFVIPTDGAspDEAGLMAACREALAGFkvpARVQVVEAFPVTESANGAKIQKHRL 526
|
.
gi 291084711 602 R 602
Cdd:PRK06164 527 R 527
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
57-604 |
1.92e-26 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 114.07 E-value: 1.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 57 MVLLKVKTKVRRYLQER-----KTVPLLFASVVRRHPDKTALIfEGTNTHWTFRQLDDYSSSVANFLQARGLVSGNVVAL 131
Cdd:PRK06087 1 KVTLTFNEQRRAAYRQQgywgdASLADYWQQTARAMPDKIAVV-DNHGASYTYSALDHAASRLANWLLAKGIEPGDRVAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 132 FMENRNEFVGLWLGMAKLGVEAALINTNLRRDALRHCLDTSKARALIFGSEMASAVYE--IQAILD--PTLT-LFCSGSW 206
Cdd:PRK06087 80 QLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFAPTLFKQTRPVdlILPLQNqlPQLQqIVGVDKL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 207 EPSTvpaNTEHLDPLLEDAPKHLPSIPDKGftDKLFYI-YTSGTTGLPKAAIVVHSRYyrMAALVYY--GFRMRPDDIVY 283
Cdd:PRK06087 160 APAT---SSLSLSQIIADYEPLTTAITTHG--DELAAVlFTSGTEGLPKGVMLTHNNI--LASERAYcaRLNLTWQDVFM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 284 DCLPLYHSAGNIVGIGQCVLHGMTVVIRKKFSAsrfwDDCI----KYNCTIVQ----YIGELCRYLLNQPPREAesrhKV 355
Cdd:PRK06087 233 MPAPLGHATGFLHGVTAPFLIGARSVLLDIFTP----DACLalleQQRCTCMLgatpFIYDLLNLLEKQPADLS----AL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 356 RMALGNG------LRQSIWtdfssRFHIpQVAEFYGATE-----------CNCSLGNFDSqVGACGFNSRIlsfvypirl 418
Cdd:PRK06087 305 RFFLCGGttipkkVARECQ-----QRGI-KLLSVYGSTEssphavvnlddPLSRFMHTDG-YAAAGVEIKV--------- 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 419 vrVNEDTMELirgpdgvcipcQPGQPGQLVGRIIQQdplrrFDGYLNQGANNKKIASDvfkkgDQAYLTGDVLVMDELGY 498
Cdd:PRK06087 369 --VDEARKTL-----------PPGCEGEEASRGPNV-----FMGYLDEPELTARALDE-----EGWYYSGDLCRMDEAGY 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 499 LYFRDRTGDTFRWKGENVSTTEVEGTLSRLLQMADVAVYGVevpgAEGRAG--MAAVASPTSNCDLESFAQTL----KKE 572
Cdd:PRK06087 426 IKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAM----PDERLGerSCAYVVLKAPHHSLTLEEVVaffsRKR 501
|
570 580 590
....*....|....*....|....*....|..
gi 291084711 573 LPLYARPIFLRFLPELHKTGTFKFQKTELRKE 604
Cdd:PRK06087 502 VAKYKYPEHIVVIDKLPRTASGKIQKFLLRKD 533
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
85-601 |
3.29e-26 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 112.65 E-value: 3.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 85 RRHPDKTALIfeGTNTHWTFRQLDDYSSSVANFLQAR-GLVSGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRD 163
Cdd:PRK06839 13 YLHPDRIAII--TEEEEMTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTEN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 164 ALRHCLDTSKARALIFGSEMASAVYEIQAILdptltlfcsgSWEPstvPANTEHLDPLLEDAPKHLPsipDKGFTDKLFY 243
Cdd:PRK06839 91 ELIFQLKDSGTTVLFVEKTFQNMALSMQKVS----------YVQR---VISITSLKEIEDRKIDNFV---EKNESASFII 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 244 IYTSGTTGLPKAAIVVHSRYYRMAALVYYGFRMRPDDIVYDCLPLYHsagnIVGIG----QCVLHGMTVVIRKKFSASRF 319
Cdd:PRK06839 155 CYTSGTTGKPKGAVLTQENMFWNALNNTFAIDLTMHDRSIVLLPLFH----IGGIGlfafPTLFAGGVIIVPRKFEPTKA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 320 WDDCIKYNCTIVQYIGELCRYLLNQPPREAESRHKVRMALGNG--LRQSIWTDFSSRFHipQVAEFYGATECNCSL---- 393
Cdd:PRK06839 231 LSMIEKHKVTVVMGVPTIHQALINCSKFETTNLQSVRWFYNGGapCPEELMREFIDRGF--LFGQGFGMTETSPTVfmls 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 394 -GNFDSQVGACGfnsrilsfvYPIRLVRVnedtmELIrGPDGVCIPcqPGQPGQLvgriiqqdpLRRFDGYLNQGANNKK 472
Cdd:PRK06839 309 eEDARRKVGSIG---------KPVLFCDY-----ELI-DENKNKVE--VGEVGEL---------LIRGPNVMKEYWNRPD 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 473 IASDVFKKGdqAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLQMADVAVYGV------EVPGAeg 546
Cdd:PRK06839 363 ATEETIQDG--WLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRqhvkwgEIPIA-- 438
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 291084711 547 ragmAAVASPTSNCDLESFAQTLKKELPLYARPIFLRFLPELHKTGTFKFQKTEL 601
Cdd:PRK06839 439 ----FIVKKSSSVLIEKDVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQL 489
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
71-602 |
1.06e-25 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 111.39 E-value: 1.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 71 QERKTVPLLFASVVRRHPDKTALIFE-GTnthWTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKL 149
Cdd:PRK13382 40 REGMGPTSGFAIAAQRCPDRPGLIDElGT---LTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 150 GVEAALINTNLRRDALRHCLDTSKARALIFGSEMASAV-YEIQAILDPTLTLfcsgSWePSTvPANTEHLDPLLEDAPKH 228
Cdd:PRK13382 117 GADILLLNTSFAGPALAEVVTREGVDTVIYDEEFSATVdRALADCPQATRIV----AW-TDE-DHDLTVEVLIAAHAGQR 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 229 LPSIPDKGFTdklfYIYTSGTTGLPKAAIVVHSRYYRMAALVYYGFRMRPDDIVYDCLPLYHSAgnivGIGQCVLHGM-- 306
Cdd:PRK13382 191 PEPTGRKGRV----ILLTSGTTGTPKGARRSGPGGIGTLKAILDRTPWRAEEPTVIVAPMFHAW----GFSQLVLAASla 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 307 -TVVIRKKFSASRFWDDCIKYNCTIVQYIGELCRYLLNQPPrEAESRHKVR-----MALGNGLRQSIWTDFSSRFHiPQV 380
Cdd:PRK13382 263 cTIVTRRRFDPEATLDLIDRHRATGLAVVPVMFDRIMDLPA-EVRNRYSGRslrfaAASGSRMRPDVVIAFMDQFG-DVI 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 381 AEFYGATEcncslgnfdsqVGacgfnsrILSFVYPIRLvRVNEDTMEliRGPDGVCI--------PCQPGQpgqlVGRI- 451
Cdd:PRK13382 341 YNNYNATE-----------AG-------MIATATPADL-RAAPDTAG--RPAEGTEIrildqdfrEVPTGE----VGTIf 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 452 IQQDPLrrFDGYlNQGANNKkiasdvFKKGDQAylTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLQM 531
Cdd:PRK13382 396 VRNDTQ--FDGY-TSGSTKD------FHDGFMA--SGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDV 464
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 291084711 532 ADVAVYGVEVPGAEGRAGMAAVASPTSNCDLESFAQTLKKELPLYARPIFLRFLPELHKTGTFKFQKTELR 602
Cdd:PRK13382 465 AEAAVIGVDDEQYGQRLAAFVVLKPGASATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQ 535
|
|
| PRK07868 |
PRK07868 |
acyl-CoA synthetase; Validated |
79-639 |
2.05e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236121 [Multi-domain] Cd Length: 994 Bit Score: 112.12 E-value: 2.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 79 LFASVVRRHPDKTALIFEGtNTHwTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKLGVEAALINT 158
Cdd:PRK07868 452 IIAEQARDAPKGEFLLFDG-RVH-TYEAVNRRINNVVRGLIAVGVRQGDRVGVLMETRPSALVAIAALSRLGAVAVLMPP 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 159 nlrrdalrhclDTSKARALIFGsemasAVYEIqaILDPT---------LTLFCSGSWEPSTVPA-------NTEHLDPll 222
Cdd:PRK07868 530 -----------DTDLAAAVRLG-----GVTEI--ITDPTnleaarqlpGRVLVLGGGESRDLDLpddadviDMEKIDP-- 589
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 223 eDAPKhLPSI--PDKGFTDKLFYIYTSGTTGLPKAAIVVHSRYyrmaALVYYGF----RMRPDDIVYDCLPLYHSAGNIV 296
Cdd:PRK07868 590 -DAVE-LPGWyrPNPGLARDLAFIAFSTAGGELVAKQITNYRW----ALSAFGTasaaALDRRDTVYCLTPLHHESGLLV 663
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 297 GIGQCVLHGMTVVIRKKFSASRFWDDCIKYNCTIVQYIGELCRYLLNQPPREAESRHKVRMALGNGLRQSIWTDFSSRFH 376
Cdd:PRK07868 664 SLGGAVVGGSRIALSRGLDPDRFVQEVRQYGVTVVSYTWAMLREVVDDPAFVLHGNHPVRLFIGSGMPTGLWERVVEAFA 743
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 377 IPQVAEFYGATECNCSLGNFD-SQVGACGfnsRILSFVYPIRLVRVNEDTMELIRGPDGVCIPCQPGQPGQLVGRIiqqd 455
Cdd:PRK07868 744 PAHVVEFFATTDGQAVLANVSgAKIGSKG---RPLPGAGRVELAAYDPEHDLILEDDRGFVRRAEVNEVGVLLARA---- 816
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 456 plrrfDGYLNQGANNKKiasDVFKKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLQMADVA 535
Cdd:PRK07868 817 -----RGPIDPTASVKR---GVFAPADTWISTEYLFRRDDDGDYWLVDRRGSVIRTARGPVYTEPVTDALGRIGGVDLAV 888
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 536 VYGVEVPGAEgrAGMAAV-----ASPTSNCDLESFAqtlkkELPLYARPIFLRFLPELHKTGTFKFQKTELRKEGFdPSV 610
Cdd:PRK07868 889 TYGVEVGGRQ--LAVAAVtlrpgAAITAADLTEALA-----SLPVGLGPDIVHVVPEIPLSATYRPTVSALRAAGI-PKP 960
|
570 580
....*....|....*....|....*....
gi 291084711 611 VKDpLFYLDARTGCYVALDQEAYTRIQAG 639
Cdd:PRK07868 961 GRQ-AWYFDPETNRYRRLTPAVRAELTGG 988
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
114-602 |
2.81e-25 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 109.79 E-value: 2.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 114 VANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALRHCLDTSKARALIFGSEMASAVYEiqaI 193
Cdd:PRK12406 24 AAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAHADLLHGLAS---A 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 194 LDPTLTLFCSG-----------SWEPSTVPANTEHLDPLLED-APKHLPSIPDKGFTdklfyIYTSGTTGLPK-----AA 256
Cdd:PRK12406 101 LPAGVTVLSVPtppeiaaayriSPALLTPPAGAIDWEGWLAQqEPYDGPPVPQPQSM-----IYTSGTTGHPKgvrraAP 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 257 IVVHSRYY-RMAALVyYGFrmrPDDIVYDCL-PLYHSAGNIVGIGQCVLhGMTVVIRKKFSASRFWDDCIKYNCTIVQYI 334
Cdd:PRK12406 176 TPEQAAAAeQMRALI-YGL---KPGIRALLTgPLYHSAPNAYGLRAGRL-GGVLVLQPRFDPEELLQLIERHRITHMHMV 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 335 GELCRYLLNQPPreaesrhKVRMALgnglrqsiwtDFSSRFHI--------------------PQVAEFYGATEcncslg 394
Cdd:PRK12406 251 PTMFIRLLKLPE-------EVRAKY----------DVSSLRHVihaaapcpadvkramiewwgPVIYEYYGSTE------ 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 395 nfdsqVGACGFNSRILSFVYPIRLVRVNEDTMELIRGPDGVCIPcqPGQPGQLVGRIIQQDPLRrfdgYLNQGANNKKIA 474
Cdd:PRK12406 308 -----SGAVTFATSEDALSHPGTVGKAAPGAELRFVDEDGRPLP--QGEIGEIYSRIAGNPDFT----YHNKPEKRAEID 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 475 SDVFkkgdqaYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLQMADVAVYGveVPGAE-GRAGMAAV 553
Cdd:PRK12406 377 RGGF------ITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFG--IPDAEfGEALMAVV 448
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 291084711 554 -ASPTSNCDLESFAQTLKKELPLYARPIFLRFLPELHKTGTFKFQKTELR 602
Cdd:PRK12406 449 ePQPGATLDEADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLR 498
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
85-604 |
2.00e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 107.82 E-value: 2.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 85 RRHPDKTALIFEGTNThwTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRDA 164
Cdd:PRK06178 44 RERPQRPAIIFYGHVI--TYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 165 LRHCLDTSKARALIFGSEMASAV------YEIQAIL----------DPTLTLFCSGSwEPSTVPANTEHLDPLLEDAPKH 228
Cdd:PRK06178 122 LSYELNDAGAEVLLALDQLAPVVeqvraeTSLRHVIvtsladvlpaEPTLPLPDSLR-APRLAAAGAIDLLPALRACTAP 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 229 LPS-IPDkgfTDKLFYI-YTSGTTGLPKAaiVVHSR---YYRMAALVYYGFRMRPDDIVYDCLPLYHSAGNIVGIGQCVL 303
Cdd:PRK06178 201 VPLpPPA---LDALAALnYTGGTTGMPKG--CEHTQrdmVYTAAAAYAVAVVGGEDSVFLSFLPEFWIAGENFGLLFPLF 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 304 HGMTVVIRKKFSASRFWDDCIKYNCTIVQYIGELCRYLLNQP---PREAESRHKVRMA-----LGNGLRQSiWTDFSSRF 375
Cdd:PRK06178 276 SGATLVLLARWDAVAFMAAVERYRVTRTVMLVDNAVELMDHPrfaEYDLSSLRQVRVVsfvkkLNPDYRQR-WRALTGSV 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 376 hipqVAEF-YGATECNCS--------LGNFD--SQVGACGFnsrilsfvyPI---RLVRVNEDTMELIrgpdgvcipcqP 441
Cdd:PRK06178 355 ----LAEAaWGMTETHTCdtftagfqDDDFDllSQPVFVGL---------PVpgtEFKICDFETGELL-----------P 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 442 -GQPGQLVGRiiqqDPlRRFDGYLNQGANNkkiaSDVFKKGdqAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTE 520
Cdd:PRK06178 411 lGAEGEIVVR----TP-SLLKGYWNKPEAT----AEALRDG--WLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSE 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 521 VEGTLSRLLQMADVAVygveVPGAEGRAGMAAVA----SPTSNCDLESFAQTLKKELPLYARPIfLRFLPELHKTGTFKF 596
Cdd:PRK06178 480 VEALLGQHPAVLGSAV----VGRPDPDKGQVPVAfvqlKPGADLTAAALQAWCRENMAVYKVPE-IRIVDALPMTATGKV 554
|
....*...
gi 291084711 597 QKTELRKE 604
Cdd:PRK06178 555 RKQDLQAL 562
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
85-602 |
2.50e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 106.81 E-value: 2.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 85 RRHPDKTALIFEGTNTHWTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRDA 164
Cdd:PRK09088 6 RLQPQRLAAVDLALGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 165 LRHCLDTSKARALIFGSEMASAVYEIQAILDPTLTLFCSGswepstvPANTEHLDPlleDAPKhlpsipdkgftdklFYI 244
Cdd:PRK09088 86 LDALLQDAEPRLLLGDDAVAAGRTDVEDLAAFIASADALE-------PADTPSIPP---ERVS--------------LIL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 245 YTSGTTGLPKAAIVvhSRYYRMAALVYYGFRMRPD-DIVYDC-LPLYHSAGNIVGIGQCVLHGMTVVIRKKFSASRFWDD 322
Cdd:PRK09088 142 FTSGTSGQPKGVML--SERNLQQTAHNFGVLGRVDaHSSFLCdAPMFHIIGLITSVRPVLAVGGSILVSNGFEPKRTLGR 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 323 CIKYNCTIVQYIG--ELCRYLLNQPPREAES-RHKVRMALGNGLRQSI----WTDFSsrfhIPqVAEFYGATECNCSLGN 395
Cdd:PRK09088 220 LGDPALGITHYFCvpQMAQAFRAQPGFDAAAlRHLTALFTGGAPHAAEdilgWLDDG----IP-MVDGFGMSEAGTVFGM 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 396 ------FDSQVGACGFNSrilsfvyPIRLVRVNEDtmeliRGPDgvcipCQPGQPGQLvgrIIQQDPLrrFDGYLNQgan 469
Cdd:PRK09088 295 svdcdvIRAKAGAAGIPT-------PTVQTRVVDD-----QGND-----CPAGVPGEL---LLRGPNL--SPGYWRR--- 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 470 nKKIASDVFKkGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLQMADVAVYGVEVP--GAEGR 547
Cdd:PRK09088 350 -PQATARAFT-GDGWFRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAqwGEVGY 427
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 291084711 548 AgmAAVASPTSNCDLESFAQTLKKELPLYARPIFLRFLPELHKTGTFKFQKTELR 602
Cdd:PRK09088 428 L--AIVPADGAPLDLERIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARLR 480
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
79-539 |
4.46e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 106.22 E-value: 4.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 79 LFASVVRRHPDKTALIFegTNTHWTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEfvgLWLGMAklgveAALInT 158
Cdd:PRK06188 17 LLVSALKRYPDRPALVL--GDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPE---VLMAIG-----AAQL-A 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 159 NLRRDAL---------RHCLDTSKARALIFGS----EMASAVYEIQAILDPTLTLfcsgswepSTVPANTEHLDPLLEDA 225
Cdd:PRK06188 86 GLRRTALhplgslddhAYVLEDAGISTLIVDPapfvERALALLARVPSLKHVLTL--------GPVPDGVDLLAAAAKFG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 226 PKHLpsIPDKGFTDKLFYIYTSGTTGLPKAAIVVHSRYYRMAALVYYGFRMrPDDIVY-DCLPLYHSAGNIVGIGqcVLH 304
Cdd:PRK06188 158 PAPL--VAAALPPDIAGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEW-PADPRFlMCTPLSHAGGAFFLPT--LLR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 305 GMTVVIRKKFSASRFWDDCIKYNCTIVQYIGELCRYLLNQPPREAESRHKVRMALGNG-------LRQSIwtdfsSRFHi 377
Cdd:PRK06188 233 GGTVIVLAKFDPAEVLRAIEEQRITATFLVPTMIYALLDHPDLRTRDLSSLETVYYGAspmspvrLAEAI-----ERFG- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 378 PQVAEFYGATECN---CSLGNFD------SQVGACGFnsrilsfvyPIRLVRVNedtmelIRGPDGVCIPcqPGQPGQLV 448
Cdd:PRK06188 307 PIFAQYYGQTEAPmviTYLRKRDhdpddpKRLTSCGR---------PTPGLRVA------LLDEDGREVA--QGEVGEIC 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 449 GRiiqqDPLRrFDGYLNQGAnnkkIASDVFKKGdqaYL-TGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSR 527
Cdd:PRK06188 370 VR----GPLV-MDGYWNRPE----ETAEAFRDG---WLhTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAE 437
|
490
....*....|..
gi 291084711 528 LLQMADVAVYGV 539
Cdd:PRK06188 438 HPAVAQVAVIGV 449
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
85-604 |
8.96e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 105.51 E-value: 8.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 85 RRHPDKTALIfEGTNThWTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNE-FVGLWlgmAKLGVEAALINTNLRR- 162
Cdd:PRK07470 18 RRFPDRIALV-WGDRS-WTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQmFESMF---AAFRLGAVWVPTNFRQt 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 163 -DALRHCLDTSKARALIFGS---EMASAVYEIQAILDPTLTLfCSGSWEPSTVPANTEHLDPLLEDApkhlpsipDKGFT 238
Cdd:PRK07470 93 pDEVAYLAEASGARAMICHAdfpEHAAAVRAASPDLTHVVAI-GGARAGLDYEALVARHLGARVANA--------AVDHD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 239 DKLFYIYTSGTTGLPKAAIVVHSryyRMAALV--YYGFRMrPDDIVYDC----LPLYHSAGnIVGIGQcVLHGMTVVI-- 310
Cdd:PRK07470 164 DPCWFFFTSGTTGRPKAAVLTHG---QMAFVItnHLADLM-PGTTEQDAslvvAPLSHGAG-IHQLCQ-VARGAATVLlp 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 311 RKKFSASRFWDDCIKYNC-------TIVQYIGE----------LCRYLLNQ-PPREAESRHKVRMALGNGLRQsiwtdfs 372
Cdd:PRK07470 238 SERFDPAEVWALVERHRVtnlftvpTILKMLVEhpavdrydhsSLRYVIYAgAPMYRADQKRALAKLGKVLVQ------- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 373 srfhipqvaeFYGATECNcslGNF--------------DSQVGACGFnsrilsfvypirlvrvnEDT-MEL-IRGPDGvc 436
Cdd:PRK07470 311 ----------YFGLGEVT---GNItvlppalhdaedgpDARIGTCGF-----------------ERTgMEVqIQDDEG-- 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 437 ipcQPGQPGQlVGRIIQQDPlRRFDGYL-NQGANNKKIASDVFKkgdqaylTGDVLVMDELGYLYFRDRTGDTFRWKGEN 515
Cdd:PRK07470 359 ---RELPPGE-TGEICVIGP-AVFAGYYnNPEANAKAFRDGWFR-------TGDLGHLDARGFLYITGRASDMYISGGSN 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 516 VSTTEVEGTLSRLLQMADVAVYGVEVPgAEGRAGMAA-VASPTSNCDLESFAQTLKKELPLYARPIFLRFLPELHKTGTF 594
Cdd:PRK07470 427 VYPREIEEKLLTHPAVSEVAVLGVPDP-VWGEVGVAVcVARDGAPVDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYG 505
|
570
....*....|
gi 291084711 595 KFQKTELRKE 604
Cdd:PRK07470 506 KITKKMVREE 515
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
74-604 |
1.01e-23 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 105.52 E-value: 1.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 74 KTVPLLFASVVRRHPDKTALI----FEGTNTHWTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKL 149
Cdd:PRK13295 24 RTINDDLDACVASCPDKTAVTavrlGTGAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 150 GVEAALINTNLRRDALRHCLDTSKARALIF-----GSEMASAVYEIQAILdPTL--TLFCSG----SWEpstvpantEHL 218
Cdd:PRK13295 104 GAVLNPLMPIFRERELSFMLKHAESKVLVVpktfrGFDHAAMARRLRPEL-PALrhVVVVGGdgadSFE--------ALL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 219 -DPLLEDAPkHLPSIPDK---GFTDKLFYIYTSGTTGLPKAaiVVHSRYYRMAALVYYGFRMR--PDDIVYDCLPLYHSA 292
Cdd:PRK13295 175 iTPAWEQEP-DAPAILARlrpGPDDVTQLIYTSGTTGEPKG--VMHTANTLMANIVPYAERLGlgADDVILMASPMAHQT 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 293 GNIVGIGQCVLHGMTVVIRKKFSASRFWD----DCIKYNCTIVQYIGELCRYLlnqppreAESRHKV---RMALGNG--- 362
Cdd:PRK13295 252 GFMYGLMMPVMLGATAVLQDIWDPARAAElirtEGVTFTMASTPFLTDLTRAV-------KESGRPVsslRTFLCAGapi 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 363 ---LRQSIWTDFSSRfhipqVAEFYGATECNC----SLGNFDSQVGAcgfnsrilSFVYPIRLVRVNedtmelIRGPDGV 435
Cdd:PRK13295 325 pgaLVERARAALGAK-----IVSAWGMTENGAvtltKLDDPDERAST--------TDGCPLPGVEVR------VVDADGA 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 436 CIPcqPGQPGQLVGRiiqqdPLRRFDGYLNQGANNKKIASDVFKKGDQAYLTGDvlvmdelGYLYFRDRTGDTFRWKGEN 515
Cdd:PRK13295 386 PLP--AGQIGRLQVR-----GCSNFGGYLKRPQLNGTDADGWFDTGDLARIDAD-------GYIRISGRSKDVIIRGGEN 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 516 VSTTEVEGTLSRLLQMADVAVYGVEVPGAEGRAGMAAVASPTSNCDLESFAQTLK-KELPLYARPIFLRFLPELHKTGTF 594
Cdd:PRK13295 452 IPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPRPGQSLDFEEMVEFLKaQKVAKQYIPERLVVRDALPRTPSG 531
|
570
....*....|
gi 291084711 595 KFQKTELRKE 604
Cdd:PRK13295 532 KIQKFRLREM 541
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
103-595 |
1.93e-23 |
|
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: 103.33 E-value: 1.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 103 TFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALRHCLDTSKARALIFGSE 182
Cdd:cd05935 3 TYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGSE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 183 masavyeiqaildptltlfcsgswepstvpantehldplLEDapkhLPSIPdkgftdklfyiYTSGTTGLPKAAIVVHSR 262
Cdd:cd05935 83 ---------------------------------------LDD----LALIP-----------YTSGTTGLPKGCMHTHFS 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 263 YYRMAALVYYGFRMRPDDIVYDCLPLYHSAGNIVGIGQCVLHGMTVVIRKKFSASRFWDDCIKYNCTIVQYIGELCRYLL 342
Cdd:cd05935 109 AAANALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMARWDRETALELIEKYKVTFWTNIPTMLVDLL 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 343 NQPPREAESRHKVRMALGNG--LRQSIWTDFSSRFHIPQVaEFYGATEcNCS------LGNFDSQ---VGACGFNSRILS 411
Cdd:cd05935 189 ATPEFKTRDLSSLKVLTGGGapMPPAVAEKLLKLTGLRFV-EGYGLTE-TMSqthtnpPLRPKLQclgIP*FGVDARVID 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 412 FvypirlvrvnEDTMELirgPDGVcipcqpgqpgqlVGRIIQQDPlRRFDGYLNQGANNKKiaSDVFKKGDQAYLTGDVL 491
Cdd:cd05935 267 I----------ETGREL---PPNE------------VGEIVVRGP-QIFKGYWNRPEETEE--SFIEIKGRRFFRTGDLG 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 492 VMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLQMADVAVYGV--EVPGAEGRA------GMAAVASPTsncDLE 563
Cdd:cd05935 319 YMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVpdERVGEEVKAfivlrpEYRGKVTEE---DII 395
|
490 500 510
....*....|....*....|....*....|..
gi 291084711 564 SFAqtlKKELPLYARPIFLRFLPELHKTGTFK 595
Cdd:cd05935 396 EWA---REQMAAYKYPREVEFVDELPRSASGK 424
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
88-588 |
3.07e-23 |
|
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: 102.99 E-value: 3.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 88 PDKTALIFEGTntHWTFRQLDDYSSSVANFLQARGLVSGNVVALFMEnRNE--FVGLwlgmakLGVeaalintnlrrdaL 165
Cdd:cd05930 1 PDAVAVVDGDQ--SLTYAELDARANRLARYLRERGVGPGDLVAVLLE-RSLemVVAI------LAV-------------L 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 166 RhcldtskaralifgsemASAVYeiqAILDPTLtlfcsgswepstvPAntEHLDPLLEDA-PKHLPSIPDKgftdkLFY- 243
Cdd:cd05930 59 K-----------------AGAAY---VPLDPSY-------------PA--ERLAYILEDSgAKLVLTDPDD-----LAYv 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 244 IYTSGTTGLPKAAIVVHsryyrmAALVYY--GFRMRPDDIVYDCLPLYHSAGNIVGIGQ---CVLHGMTVVIRKK---FS 315
Cdd:cd05930 99 IYTSGSTGKPKGVMVEH------RGLVNLllWMQEAYPLTPGDRVLQFTSFSFDVSVWEifgALLAGATLVVLPEevrKD 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 316 ASRFWDDCIKYNCTIVQYIGELCRYLLNQPPREAesRHKVRMAL--GNGLRQSIWTDFSSRFHIPQVAEFYGATECncsl 393
Cdd:cd05930 173 PEALADLLAEEGITVLHLTPSLLRLLLQELELAA--LPSLRLVLvgGEALPPDLVRRWRELLPGARLVNLYGPTEA---- 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 394 gNFDSQVGACGFNSRILSFV---YPIRLVRVnedtmeLIRGPDGvcIPCQPGQPGQL------VGRiiqqdplrrfdGYL 464
Cdd:cd05930 247 -TVDATYYRVPPDDEEDGRVpigRPIPNTRV------YVLDENL--RPVPPGVPGELyiggagLAR-----------GYL 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 465 NQ-GANNKKIASDVFKKGDQAYLTGDVLVMDELGYLYFRDRTgDT------FRwkgenVSTTEVEGTLSRLLQMADVAVy 537
Cdd:cd05930 307 NRpELTAERFVPNPFGPGERMYRTGDLVRWLPDGNLEFLGRI-DDqvkirgYR-----IELGEIEAALLAHPGVREAAV- 379
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 291084711 538 gVEVPGAEGRAGMAA--VASPTSNCDLESFAQTLKKELPLYARPIFLRFLPEL 588
Cdd:cd05930 380 -VAREDGDGEKRLVAyvVPDEGGELDEEELRAHLAERLPDYMVPSAFVVLDAL 431
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
103-603 |
3.42e-23 |
|
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: 102.98 E-value: 3.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 103 TFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALRHCLDTSKARALIfgse 182
Cdd:cd05973 2 TFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVV---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 183 masavyeiqaildptltlfcsgswepsTVPANTEHLDplledapkhlpsipdkgfTDKLFYIYTSGTTGLPKAAIVVHSR 262
Cdd:cd05973 78 ---------------------------TDAANRHKLD------------------SDPFVMMFTSGTTGLPKGVPVPLRA 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 263 YYRMAALVYYGFRMRPDDIVYD------CLPLYHS--AGNIVGIGQCVLHGmtvvirkKFSASRFWDDCIKYNCTIVQYI 334
Cdd:cd05973 113 LAAFGAYLRDAVDLRPEDSFWNaadpgwAYGLYYAitGPLALGHPTILLEG-------GFSVESTWRVIERLGVTNLAGS 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 335 GELCRYLLNQPPrEAESRHKVRM----ALGNGLRQSIWTDFSSRFHIPqVAEFYGATECNCSLGNFDS-----QVGACGf 405
Cdd:cd05973 186 PTAYRLLMAAGA-EVPARPKGRLrrvsSAGEPLTPEVIRWFDAALGVP-IHDHYGQTELGMVLANHHAlehpvHAGSAG- 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 406 nsrilsFVYP-IRLVRVNEDTMELIrgpdgvcipcqPGQPGQLVgrI-IQQDPLRRFDGYlnQGANNKKIASDVfkkgdq 483
Cdd:cd05973 263 ------RAMPgWRVAVLDDDGDELG-----------PGEPGRLA--IdIANSPLMWFRGY--QLPDTPAIDGGY------ 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 484 aYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLQMADVAVYGV------EVPGA-----EGRAGMAA 552
Cdd:cd05973 316 -YLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVpdpertEVVKAfvvlrGGHEGTPA 394
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 291084711 553 VAsptsncdlESFAQTLKKELPLYARPIFLRFLPELHKTGTFKFQKTELRK 603
Cdd:cd05973 395 LA--------DELQLHVKKRLSAHAYPRTIHFVDELPKTPSGKIQRFLLRR 437
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
89-603 |
1.17e-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: 101.21 E-value: 1.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 89 DKTALIFEGTNThwTFRQLDDYSSSVANFLQARG-LVSGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALRH 167
Cdd:cd05941 1 DRIAIVDDGDSI--TYADLVARAARLANRLLALGkDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 168 CLDTSkaralifgsemasavyEIQAILDPTLTlfcsgswepstvpantehldplledapkhlpsipdkgftdklfyIYTS 247
Cdd:cd05941 79 VITDS----------------EPSLVLDPALI--------------------------------------------LYTS 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 248 GTTGLPKAAIVVHSRYYRMA-ALVYYgFRMRPDDIVYDCLPLYHSAGNIVGIGQCVLHGMTVVIRKKFSASRFWDDCIKY 326
Cdd:cd05941 99 GTTGRPKGVVLTHANLAANVrALVDA-WRWTEDDVLLHVLPLHHVHGLVNALLCPLFAGASVEFLPKFDPKEVAISRLMP 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 327 NCTIVQYIGELCRYLLNQPPREAESRHKVRMALGNGLRqsIWTDFSSRFHIPQVAEF-----------YGATECNCSLGN 395
Cdd:cd05941 178 SITVFMGVPTIYTRLLQYYEAHFTDPQFARAAAAERLR--LMVSGSAALPVPTLEEWeaitghtllerYGMTEIGMALSN 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 396 ---FDSQVGACGFNsriLSFVYpirlVRVNEDTmelirgpdgvciPCQPGQPGQlVGRI-IQQDPLrrFDGYLNQGANNK 471
Cdd:cd05941 256 pldGERRPGTVGMP---LPGVQ----ARIVDEE------------TGEPLPRGE-VGEIqVRGPSV--FKEYWNKPEATK 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 472 KIASDvfkkgDQAYLTGDVLVMDELGYLYFRDRTG-DTFRWKGENVSTTEVEGTLSRLLQMADVAVYGveVPGAE-GRAG 549
Cdd:cd05941 314 EEFTD-----DGWFKTGDLGVVDEDGYYWILGRSSvDIIKSGGYKVSALEIERVLLAHPGVSECAVIG--VPDPDwGERV 386
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 291084711 550 MAAVA--SPTSNCDLESFAQTLKKELPLYARPIFLRFLPELHKTGTFKFQKTELRK 603
Cdd:cd05941 387 VAVVVlrAGAAALSLEELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
77-603 |
1.41e-22 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.
Pssm-ID: 341283 [Multi-domain] Cd Length: 486 Bit Score: 101.61 E-value: 1.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 77 PLLF---ASVVrrHPDKTALIFEGTntHWTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKLGveA 153
Cdd:cd12118 6 PLSFlerAAAV--YPDRTSIVYGDR--RYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAG--A 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 154 ALINTNLRRDA------LRHcldtSKARALIFGSEMAsavYEiqaildptlTLFCSGSWEPSTVPANTEHldplledapk 227
Cdd:cd12118 80 VLNALNTRLDAeeiafiLRH----SEAKVLFVDREFE---YE---------DLLAEGDPDFEWIPPADEW---------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 228 hlpsipdkgftDKLFYIYTSGTTGLPKAAIVVHSRYYRMAALVYYGFRMrPDDIVYDC-LPLYHSAG-----NIVGIGQc 301
Cdd:cd12118 134 -----------DPIALNYTSGTTGRPKGVVYHHRGAYLNALANILEWEM-KQHPVYLWtLPMFHCNGwcfpwTVAAVGG- 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 302 vlhgmTVVIRKKFSASRFWDDCIKYNCTivqyigELC------RYLLNQPPREAESR-HKVRMALGN--------GLRQS 366
Cdd:cd12118 201 -----TNVCLRKVDAKAIYDLIEKHKVT------HFCgaptvlNMLANAPPSDARPLpHRVHVMTAGapppaavlAKMEE 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 367 IwtdfssRFHIPQV---AEFYG-ATEC------------NCSLGNFDSQVGACGFNsrilsfvyPIRLVrvNEDTMELIR 430
Cdd:cd12118 270 L------GFDVTHVyglTETYGpATVCawkpewdelpteERARLKARQGVRYVGLE--------EVDVL--DPETMKPVP 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 431 GpDGVCIpcqpgqpGQLV--GRIIQQdplrrfdGYLNqganNKKIASDVFKKGdqAYLTGDVLVMDELGYLYFRDRTGDT 508
Cdd:cd12118 334 R-DGKTI-------GEIVfrGNIVMK-------GYLK----NPEATAEAFRGG--WFHSGDLAVIHPDGYIEIKDRSKDI 392
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 509 FRWKGENVSTTEVEGTLSRLLQMADVAVYGV------EVPGA--EGRAGMAAVASptsncDLESFAqtlKKELPLYARPI 580
Cdd:cd12118 393 IISGGENISSVEVEGVLYKHPAVLEAAVVARpdekwgEVPCAfvELKEGAKVTEE-----EIIAFC---REHLAGFMVPK 464
|
570 580
....*....|....*....|...
gi 291084711 581 FLRFLPeLHKTGTFKFQKTELRK 603
Cdd:cd12118 465 TVVFGE-LPKTSTGKIQKFVLRD 486
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
84-539 |
3.23e-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: 101.11 E-value: 3.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 84 VRRHPDKTALIFEGTNT----HWTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKLGVEAALINTN 159
Cdd:cd17634 63 LRENGDRTAIIYEGDDTsqsrTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGG 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 160 LRRDALRHCLDTSKARALIFGSEMASA--VYEIQAILDPTLTLfcSGSwEPSTV-------------PANTEHLDPLLED 224
Cdd:cd17634 143 FAPEAVAGRIIDSSSRLLITADGGVRAgrSVPLKKNVDDALNP--NVT-SVEHVivlkrtgsdidwqEGRDLWWRDLIAK 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 225 A-PKHLPSIPDKgfTDKLFYIYTSGTTGLPKAAIVVHSRYYRMAALVY-YGFRMRPDDIVYDCLPLYHSAGNIVGIGQCV 302
Cdd:cd17634 220 AsPEHQPEAMNA--EDPLFILYTSGTTGKPKGVLHTTGGYLVYAATTMkYVFDYGPGDIYWCTADVGWVTGHSYLLYGPL 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 303 LHGMTVVIRKKF----SASRFWDDCIKYNCTIVQYIGELCRYLLNQPPREAE----SRHKVRMALGNGLRQSIWTDFSSR 374
Cdd:cd17634 298 ACGATTLLYEGVpnwpTPARMWQVVDKHGVNILYTAPTAIRALMAAGDDAIEgtdrSSLRILGSVGEPINPEAYEWYWKK 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 375 FHIPQ--VAEFYGATE----CNCSLGNFDSQVGACGFNSrilsfVYPIRLVRVNEdtmeliRGPdgvciPCQPGQPGQLV 448
Cdd:cd17634 378 IGKEKcpVVDTWWQTEtggfMITPLPGAIELKAGSATRP-----VFGVQPAVVDN------EGH-----PQPGGTEGNLV 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 449 --------GRIIQQDPLRRFDGYlnqgannkkiasdvFKKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTE 520
Cdd:cd17634 442 itdpwpgqTRTLFGDHERFEQTY--------------FSTFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAE 507
|
490
....*....|....*....
gi 291084711 521 VEGTLSRLLQMADVAVYGV 539
Cdd:cd17634 508 IESVLVAHPKVAEAAVVGI 526
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
72-538 |
3.98e-22 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 100.95 E-value: 3.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 72 ERKTVPLLFASVVRRHPDKTALIF--EGTNTHWTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKL 149
Cdd:COG1022 9 PADTLPDLLRRRAARFPDRVALREkeDGIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 150 GVEAALINTNLRRDALRHCLDTSKARALIFGS-EMASAVYEIQAILdPTL-TLFCsgsWEPSTVPANTE--HLDPLLE-- 223
Cdd:COG1022 89 GAVTVPIYPTSSAEEVAYILNDSGAKVLFVEDqEQLDKLLEVRDEL-PSLrHIVV---LDPRGLRDDPRllSLDELLAlg 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 224 ---DAPKHLPSIPDKGFTDKLF-YIYTSGTTGLPKAAIVVHSRYYRMAALVYYGFRMRPDDIVYDCLPLYHSAGNIVGIG 299
Cdd:COG1022 165 revADPAELEARRAAVKPDDLAtIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFLPLAHVFERTVSYY 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 300 qCVLHGMTVV---------------------------------IRKKFSASRFW---------DDCIKYNCTIVQyiGEl 337
Cdd:COG1022 245 -ALAAGATVAfaespdtlaedlrevkptfmlavprvwekvyagIQAKAEEAGGLkrklfrwalAVGRRYARARLA--GK- 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 338 cryllnQPPREAESRH---------KVRMALGNGLRQSI------------WtdfssrFH---IPqVAEFYGATE----- 388
Cdd:COG1022 321 ------SPSLLLRLKHaladklvfsKLREALGGRLRFAVsggaalgpelarF------FRalgIP-VLEGYGLTEtspvi 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 389 -CNcSLGNFDsqVGACGfnsRILSFVYpirlVRVNEDTmE-LIRGPdGVcipcqpgqpgqlvgriiqqdplrrFDGYLNQ 466
Cdd:COG1022 388 tVN-RPGDNR--IGTVG---PPLPGVE----VKIAEDG-EiLVRGP-NV------------------------MKGYYKN 431
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 291084711 467 -GANNKKIASDvfkkGdqaYL-TGDVLVMDELGYLYFRDRTGDTFrwK---GENVSTTEVEGTLSRLLQMADVAVYG 538
Cdd:COG1022 432 pEATAEAFDAD----G---WLhTGDIGELDEDGFLRITGRKKDLI--VtsgGKNVAPQPIENALKASPLIEQAVVVG 499
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
84-568 |
6.24e-22 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 99.96 E-value: 6.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 84 VRRHPDKTALIFEGTNTHWTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRD 163
Cdd:PRK05852 26 ATRLPEAPALVVTADRIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 164 ALRHCLDTSKARALIFGSEMASAVYEIQAILDP-TLTLFCSGSWEPSTVpanTEHLDPLLEdaPKHLPSIPDKGFTDKLF 242
Cdd:PRK05852 106 EQRVRSQAAGARVVLIDADGPHDRAEPTTRWWPlTVNVGGDSGPSGGTL---SVHLDAATE--PTPATSTPEGLRPDDAM 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 243 YIYTSGTTGLPKAAIVVHSRYYRMAALVYYGFRMRPDDIVYDCLPLYHSAGNIVGIGQCVLHGMTVVI--RKKFSASRFW 320
Cdd:PRK05852 181 IMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHGHGLIAALLATLASGGAVLLpaRGRFSAHTFW 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 321 DDCIKYNCTIVQYIGELCRYLLNQPPREA--ESRHKVRM--ALGNGLRQSIWTDFSSRFHIPqVAEFYGATECNCSLGNF 396
Cdd:PRK05852 261 DDIKAVGATWYTAVPTIHQILLERAATEPsgRKPAALRFirSCSAPLTAETAQALQTEFAAP-VVCAFGMTEATHQVTTT 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 397 DSQVGACGFNSRILSFVypirlvrVNEDTMELIR--GPDGvcIPCQPGQPGQ--LVGRIIQQdplrrfdGYLnqgaNNKK 472
Cdd:PRK05852 340 QIEGIGQTENPVVSTGL-------VGRSTGAQIRivGSDG--LPLPAGAVGEvwLRGTTVVR-------GYL----GDPT 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 473 IASDVFKKGdqAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLQMADVAVYGveVPGAEGRAGMAA 552
Cdd:PRK05852 400 ITAANFTDG--WLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFG--VPDQLYGEAVAA 475
|
490 500
....*....|....*....|..
gi 291084711 553 V------ASPTSNcDLESFAQT 568
Cdd:PRK05852 476 VivpresAPPTAE-ELVQFCRE 496
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
82-614 |
6.81e-22 |
|
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: 100.26 E-value: 6.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 82 SVVRRHP----DKTALIFEGTNTH---WTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKLGVEAA 154
Cdd:cd05968 65 QLLDKWLadtrTRPALRWEGEDGTsrtLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVV 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 155 LINTNLRRDALRHCLDTSKARALIfgseMASAVYEIQAILDPTLTLFCSGSWEPST-------------VPANTEHLDPL 221
Cdd:cd05968 145 PIFSGFGKEAAATRLQDAEAKALI----TADGFTRRGREVNLKEEADKACAQCPTVekvvvvrhlgndfTPAKGRDLSYD 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 222 LEDApKHLPSIPDKGFTDKLFYIYTSGTTGLPKAAIVVHSRYYRMAAL-VYYGFRMRPDDIVYDCLPLYHSAGNIVGIGQ 300
Cdd:cd05968 221 EEKE-TAGDGAERTESEDPLMIIYTSGTTGKPKGTVHVHAGFPLKAAQdMYFQFDLKPGDLLTWFTDLGWMMGPWLIFGG 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 301 CVLhGMTVVIRKKF----SASRFWDDCIKYNCTIVQYIGELCRYLL--NQPPREAESRHKVRMALGNGlrqSIWTDFSSR 374
Cdd:cd05968 300 LIL-GATMVLYDGApdhpKADRLWRMVEDHEITHLGLSPTLIRALKprGDAPVNAHDLSSLRVLGSTG---EPWNPEPWN 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 375 F--------HIPqVAEFYGATECNCS-LGN-FDSQVGACGFNSrilsfVYPIRLVRVNEDTMELIRGPDGVCIPCQPgQP 444
Cdd:cd05968 376 WlfetvgkgRNP-IINYSGGTEISGGiLGNvLIKPIKPSSFNG-----PVPGMKADVLDESGKPARPEVGELVLLAP-WP 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 445 GQLVGriIQQDPLRRFDGYlnqgannkkiasdvFKKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGT 524
Cdd:cd05968 449 GMTRG--FWRDEDRYLETY--------------WSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESV 512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 525 LSRLLQMADVAVYGVEVPgAEGRAGMA-AVASPTSncdleSFAQTLKKEL----------PLyaRPIFLRFLPELHKTGT 593
Cdd:cd05968 513 LNAHPAVLESAAIGVPHP-VKGEAIVCfVVLKPGV-----TPTEALAEELmervadelgkPL--SPERILFVKDLPKTRN 584
|
570 580
....*....|....*....|....*.
gi 291084711 594 FKFQKTELR-----KEGFDPSVVKDP 614
Cdd:cd05968 585 AKVMRRVIRaaylgKELGDLSSLENP 610
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
103-601 |
7.17e-22 |
|
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: 98.68 E-value: 7.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 103 TFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALRHCLDTSKArALIFGSE 182
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDV-QLLLTDS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 183 MASAVYeIQAILDPTLtlfcsgsWEPSTVPANTEHLDPLleDAPKHLpsipdkgftdklfyIYTSGTTGLPKAAIVVHSR 262
Cdd:TIGR01923 80 LLEEKD-FQADSLDRI-------EAAGRYETSLSASFNM--DQIATL--------------MFTSGTTGKPKAVPHTFRN 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 263 YYRMAALVYYGFRMRPDDIVYDCLPLYHSAGNIVgIGQCVLHGMTVVIRKKFSAsrFWDDCIKYNCTIVQYIGELCRYLL 342
Cdd:TIGR01923 136 HYASAVGSKENLGFTEDDNWLLSLPLYHISGLSI-LFRWLIEGATLRIVDKFNQ--LLEMIANERVTHISLVPTQLNRLL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 343 NQPPREAESRhkvRMALGNGlrqsiwtdfssrfHIPQ------------VAEFYGATECNcslgnfdSQVgaCGFNsril 410
Cdd:TIGR01923 213 DEGGHNENLR---KILLGGS-------------AIPAplieeaqqyglpIYLSYGMTETC-------SQV--TTAT---- 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 411 sfvypirlvrvNEDTMEliRGPDGVCIP------CQPGQPGqlVGRIIQQDPLRrFDGYLNQG----ANNKKiasDVFKK 480
Cdd:TIGR01923 264 -----------PEMLHA--RPDVGRPLAgreikiKVDNKEG--HGEIMVKGANL-MKGYLYQGeltpAFEQQ---GWFNT 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 481 GDQAYLTGDvlvmdelGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLQMADVAVygveVPGAEGRAGMAAVA-----S 555
Cdd:TIGR01923 325 GDIGELDGE-------GFLYVLGRRDDLIISGGENIYPEEIETVLYQHPGIQEAVV----VPKPDAEWGQVPVAyivseS 393
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 291084711 556 PTSNCDLESFaqtLKKELPLYARPIFLRFLPELHKTGTFKFQKTEL 601
Cdd:TIGR01923 394 DISQAKLIAY---LTEKLAKYKVPIAFEKLDELPYNASGKILRNQL 436
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
72-593 |
1.09e-21 |
|
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 100.32 E-value: 1.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 72 ERKTVPLLFASVVRRHPDKTALIFEGTntHWTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEF-VGLwLGMAKLG 150
Cdd:COG1020 474 ADATLHELFEAQAARTPDAVAVVFGDQ--SLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMvVAL-LAVLKAG 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 151 veAAL--INTNLRRDALRHCLDTSKARALIFGSEMASAVYEIQAildPTLTLfcsgswepstvpantehLDPLLEDAPKH 228
Cdd:COG1020 551 --AAYvpLDPAYPAERLAYMLEDAGARLVLTQSALAARLPELGV---PVLAL-----------------DALALAAEPAT 608
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 229 LPSIPDKGftDKLFY-IYTSGTTGLPKAAIVVHsryyrmAALVYY------GFRMRPDDIVydclPLYH------SAGNI 295
Cdd:COG1020 609 NPPVPVTP--DDLAYvIYTSGSTGRPKGVMVEH------RALVNLlawmqrRYGLGPGDRV----LQFAslsfdaSVWEI 676
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 296 VGigqCVLHGMTVVIRKK---FSASRFWDDCIKYNCTIVQYIGELCRYLLNQPPreaESRHKVRMAL--GNGLRQSIWTD 370
Cdd:COG1020 677 FG---ALLSGATLVLAPPearRDPAALAELLARHRVTVLNLTPSLLRALLDAAP---EALPSLRLVLvgGEALPPELVRR 750
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 371 FSSRFHIPQVAEFYGATECncslgnfdsQVGACgfnsrilsfVYPIRLVRVNEDTMELIRGPDGVCI--------PCQPG 442
Cdd:COG1020 751 WRARLPGARLVNLYGPTET---------TVDST---------YYEVTPPDADGGSVPIGRPIANTRVyvldahlqPVPVG 812
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 443 QPGQL------VGRiiqqdplrrfdGYLNQ-GANNKK-IASDVFKKGDQAYLTGDVLVMDELGYLYFRDRTgDT------ 508
Cdd:COG1020 813 VPGELyiggagLAR-----------GYLNRpELTAERfVADPFGFPGARLYRTGDLARWLPDGNLEFLGRA-DDqvkirg 880
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 509 FRwkgenVSTTEVEGTLSRLLQMADVAVYGVEVPGAEGRAgmAAVASPTSNCDLESFAQTLKKELPLYARPIFLRFLPEL 588
Cdd:COG1020 881 FR-----IELGEIEAALLQHPGVREAVVVAREDAPGDKRL--VAYVVPEAGAAAAAALLRLALALLLPPYMVPAAVVLLL 953
|
....*
gi 291084711 589 HKTGT 593
Cdd:COG1020 954 PLPLT 958
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
245-602 |
1.19e-21 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 96.96 E-value: 1.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 245 YTSGTTGLPKAAIVVHSRYYRMAALVyyGFRMR--PDDIVYDCLPLYHSAGNIVGIGQCVLHGMTVVI-RKKFSASRFWD 321
Cdd:cd05917 9 FTSGTTGSPKGATLTHHNIVNNGYFI--GERLGltEQDRLCIPVPLFHCFGSVLGVLACLTHGATMVFpSPSFDPLAVLE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 322 DCIKYNCTIVQ-----YIGElcrylLNQPPREAESRHKVRMALGNG-------LRQSIwtdfsSRFHIPQVAEFYGATEc 389
Cdd:cd05917 87 AIEKEKCTALHgvptmFIAE-----LEHPDFDKFDLSSLRTGIMAGapcppelMKRVI-----EVMNMKDVTIAYGMTE- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 390 nCSLGNFDSQVGAcGFNSRILSfvypirLVRVNEDTMELIRGPDGVCIPcQPGQPGQLVGRiiqqdplrrfdGY-LNQG- 467
Cdd:cd05917 156 -TSPVSTQTRTDD-SIEKRVNT------VGRIMPHTEAKIVDPEGGIVP-PVGVPGELCIR-----------GYsVMKGy 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 468 -ANNKKIASDVfkKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLQMADVAVYGveVPGAE- 545
Cdd:cd05917 216 wNDPEKTAEAI--DGDGWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVG--VPDERy 291
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 291084711 546 GRAGMAAVA-SPTSNCDLESFAQTLKKELPLYARPIFLRFLPELHKTGTFKFQKTELR 602
Cdd:cd05917 292 GEEVCAWIRlKEGAELTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
75-335 |
1.83e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 98.42 E-value: 1.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 75 TVPLLFASVVRRHPDKTALIFeGTNTHwTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKLGveAA 154
Cdd:PRK07798 4 NIADLFEAVADAVPDRVALVC-GDRRL-TYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKAR--AV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 155 LINTNLR--RDALRHCLDTSKARALIFGSEMASAVYEIQAILdPTLTLFCS---GSWEPSTVPAntEHLDPLLEDAPKHL 229
Cdd:PRK07798 80 PVNVNYRyvEDELRYLLDDSDAVALVYEREFAPRVAEVLPRL-PKLRTLVVvedGSGNDLLPGA--VDYEDALAAGSPER 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 230 PSIPDKGftDKLFYIYTSGTTGLPKAAIVVHSRYYR--MAALVYYG--FRMRPDDIV-----------YDCLPLYHSAGN 294
Cdd:PRK07798 157 DFGERSP--DDLYLLYTGGTTGMPKGVMWRQEDIFRvlLGGRDFATgePIEDEEELAkraaagpgmrrFPAPPLMHGAGQ 234
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 291084711 295 IVGIGqCVLHGMTVVI--RKKFSASRFWDDCIKYNCTIVQYIG 335
Cdd:PRK07798 235 WAAFA-ALFSGQTVVLlpDVRFDADEVWRTIEREKVNVITIVG 276
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
85-527 |
3.01e-21 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 97.72 E-value: 3.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 85 RRHPDKTALIFEGTNThwTFRQLDDYSSSVANFLQAR-GLVSGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRD 163
Cdd:PRK08314 21 RRYPDKTAIVFYGRAI--SYRELLEEAERLAGYLQQEcGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 164 ALRHCLDTSKARALIFGSEMASAVyeIQAILDPTLTLFCSGSWEpSTVPANTEHLDPLLEDAPKHLPSIPDKGFT----- 238
Cdd:PRK08314 99 ELAHYVTDSGARVAIVGSELAPKV--APAVGNLRLRHVIVAQYS-DYLPAEPEIAVPAWLRAEPPLQALAPGGVVawkea 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 239 --------------DKLFYI-YTSGTTGLPKAAIVVHSRYYRMAALVYYGFRMRPDDIVYDCLPLYHSAGNIVGIGQCVL 303
Cdd:PRK08314 176 laaglappphtagpDDLAVLpYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVLPLFHVTGMVHSMNAPIY 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 304 HGMTVVIrkkfsASRfWD-----DCI-KYNCTIVQYIGELCRYLLNQPPREAESRHKVRMALGNG--LRQSIWTDFSSRF 375
Cdd:PRK08314 256 AGATVVL-----MPR-WDreaaaRLIeRYRVTHWTNIPTMVVDFLASPGLAERDLSSLRYIGGGGaaMPEAVAERLKELT 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 376 HIPQVaEFYGATEC-------------NCSLGnfdsqVGACGFNSRIlsfvypirlvrVNEDTMElirgpdgvciPCQPG 442
Cdd:PRK08314 330 GLDYV-EGYGLTETmaqthsnppdrpkLQCLG-----IPTFGVDARV-----------IDPETLE----------ELPPG 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 443 QpgqlVGRIIQQDPlRRFDGYLNQGANNKK--IASDvfkkGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTE 520
Cdd:PRK08314 383 E----VGEIVVHGP-QVFKGYWNRPEATAEafIEID----GKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAE 453
|
....*..
gi 291084711 521 VEGTLSR 527
Cdd:PRK08314 454 VENLLYK 460
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
80-579 |
3.49e-21 |
|
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341306 [Multi-domain] Cd Length: 491 Bit Score: 97.03 E-value: 3.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 80 FASVVRRHPDKTALIFEGTNthWTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKLGVEAALINTN 159
Cdd:cd17651 1 FERQAARTPDAPALVAEGRR--LTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 160 LRRDALRHCLDTSKARALIFGSEMASAVyeIQAILDPTLTLfcsgsWEPSTVPANTEHLDPLledAPKHLpsipdkgftd 239
Cdd:cd17651 79 YPAERLAFMLADAGPVLVLTHPALAGEL--AVELVAVTLLD-----QPGAAAGADAEPDPAL---DADDL---------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 240 kLFYIYTSGTTGLPKAAIVVHsryyRMAA-LVYYGFRmrpddiVYDCLPLYHSAgNIVGIG---------QCVLHGMTVV 309
Cdd:cd17651 139 -AYVIYTSGSTGRPKGVVMPH----RSLAnLVAWQAR------ASSLGPGARTL-QFAGLGfdvsvqeifSTLCAGATLV 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 310 IRK---KFSASRFWDDCIKYNCTIV----QYIGELCRYLLNQPPREAESRHKV----RMALGNGLRQsiwtdFSSRFHIP 378
Cdd:cd17651 207 LPPeevRTDPPALAAWLDEQRISRVflptVALRALAEHGRPLGVRLAALRYLLtggeQLVLTEDLRE-----FCAGLPGL 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 379 QVAEFYGATECN-CSLGNFDSQVGACGfnsRILSFVYPIRLVRVnedtmeliRGPDGVCIPCQPGQPGQLvgrIIQQDPL 457
Cdd:cd17651 282 RLHNHYGPTETHvVTALSLPGDPAAWP---APPPIGRPIDNTRV--------YVLDAALRPVPPGVPGEL---YIGGAGL 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 458 RRfdGYLNQ-GANNKKIASDVFKKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLQMADVAV 536
Cdd:cd17651 348 AR--GYLNRpELTAERFVPDPFVPGARMYRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVV 425
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 291084711 537 YGVEVPGAEGRAGMAAVASPTSNCDLESFAQTLKKELPLYARP 579
Cdd:cd17651 426 LAREDRPGEKRLVAYVVGDPEAPVDAAELRAALATHLPEYMVP 468
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
79-603 |
5.55e-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: 96.93 E-value: 5.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 79 LFASVVRRHPDK---TALIfEGTNTHWTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKLGveAAL 155
Cdd:cd12119 1 LLEHAARLHGDReivSRTH-EGEVHRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMG--AVL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 156 --INTNLRRDALRHCLDTSKARALIFGSEMASAVYEIQAILDPTLTLFCSGSWEPSTVPA--NTEHLDPLLEDAPkhlps 231
Cdd:cd12119 78 htINPRLFPEQIAYIINHAEDRVVFVDRDFLPLLEAIAPRLPTVEHVVVMTDDAAMPEPAgvGVLAYEELLAAES----- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 232 iPDKGFTDK-------LFYiyTSGTTGLPKA------AIVVHSryyrMAALVYYGFRMRPDDIVYDCLPLYHsaGNIVGI 298
Cdd:cd12119 153 -PEYDWPDFdentaaaICY--TSGTTGNPKGvvyshrSLVLHA----MAALLTDGLGLSESDVVLPVVPMFH--VNAWGL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 299 G-QCVLHGMTVVIRKKFSASRFWDDCIK-YNCTIVQYIGELCRYLLNQPPREAESRHKVRMAL--GNGLRQSIWTDFSSR 374
Cdd:cd12119 224 PyAAAMVGAKLVLPGPYLDPASLAELIErEGVTFAAGVPTVWQGLLDHLEANGRDLSSLRRVVigGSAVPRSLIEAFEER 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 375 fHIPqVAEFYGATEcNCSLGNF----DSQVGACG---FNSRILSfVYPIRLVRVNedtmelIRGPDGVCIPCQPGQPGQL 447
Cdd:cd12119 304 -GVR-VIHAWGMTE-TSPLGTVarppSEHSNLSEdeqLALRAKQ-GRPVPGVELR------IVDDDGRELPWDGKAVGEL 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 448 VGR---IIQqdplrrfdGYLNQGANNKKIASDVFKKgdqaylTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGT 524
Cdd:cd12119 374 QVRgpwVTK--------SYYKNDEESEALTEDGWLR------TGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENA 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 525 LSRLLQMADVAVYGV------EVPGAegragmAAVASPTSNCDLESFAQTLKKELPLYARPIFLRFLPELHKTGTFKFQK 598
Cdd:cd12119 440 IMAHPAVAEAAVIGVphpkwgERPLA------VVVLKEGATVTAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDK 513
|
....*
gi 291084711 599 TELRK 603
Cdd:cd12119 514 KALRE 518
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
102-602 |
3.80e-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: 3.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 102 WTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALRHCLDTSKARALIFGS 181
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 182 EMasavYEIQAILDPTLTLfcsgswepstvpantehldplledapkhlpsipdkgftdklfyiYTSGTTGLPKAAIVVHS 261
Cdd:cd05969 81 EL----YERTDPEDPTLLH--------------------------------------------YTSGTTGTPKGVLHVHD 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 262 RYYRMAALVYYGFRMRPDDIvYDCL--PLYhSAGNIVGIGQCVLHGMTVVIRK-KFSASRfWDDCIKYNCTIVQY----- 333
Cdd:cd05969 113 AMIFYYFTGKYVLDLHPDDI-YWCTadPGW-VTGTVYGIWAPWLNGVTNVVYEgRFDAES-WYGIIERVKVTVWYtapta 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 334 IGELCRYLLNQPPREAESRHKVRMALGNGLRQSI--WTD--FSSRFHipqvaEFYGATE------CNCSlgNFDSQVGAC 403
Cdd:cd05969 190 IRMLMKEGDELARKYDLSSLRFIHSVGEPLNPEAirWGMevFGVPIH-----DTWWQTEtgsimiANYP--CMPIKPGSM 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 404 GfnsrilsfvYPIRLVR---VNEDTMELIRGPDGVcIPCQPGQPGQlvgriiqqdplrrFDGYLNQGANNKKiasdVFKK 480
Cdd:cd05969 263 G---------KPLPGVKaavVDENGNELPPGTKGI-LALKPGWPSM-------------FRGIWNDEERYKN----SFID 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 481 GdqAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLQMADVAVYGVEVPgaegRAGMAAVASPTSNC 560
Cdd:cd05969 316 G--WYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDP----LRGEIIKAFISLKE 389
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 291084711 561 DLESfAQTLKKELPLYAR--------PIFLRFLPELHKTGTFKFQKTELR 602
Cdd:cd05969 390 GFEP-SDELKEEIINFVRqklgahvaPREIEFVDNLPKTRSGKIMRRVLK 438
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
105-602 |
6.33e-20 |
|
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.
Pssm-ID: 341252 [Multi-domain] Cd Length: 473 Bit Score: 93.21 E-value: 6.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 105 RQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLwlGMAKLGVEAALINTNLRRDALRHCLDTSKARALIfGSEMA 184
Cdd:cd05929 1 LEARDLDRAQVFHQRRLLLLDVYSIALNRNARAAAAEG--VWIADGVYIYLINSILTVFAAAAAWKCGACPAYK-SSRAP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 185 SAvyEIQAILDPT-LTLFCS--GSWEPSTVPANtehLDPLLEDAPKhlPSIPDKGFTDKLFYiyTSGTTGLPKA------ 255
Cdd:cd05929 78 RA--EACAIIEIKaAALVCGlfTGGGALDGLED---YEAAEGGSPE--TPIEDEAAGWKMLY--SGGTTGRPKGikrglp 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 256 AIVVHSRYYRMAALvyyGFRMRPDDIVYDCLPLYHSAGNIVGIGQCVLhGMTVVIRKKFSASRFWDDCIKYNCTIVQYIG 335
Cdd:cd05929 149 GGPPDNDTLMAAAL---GFGPGADSVYLSPAPLYHAAPFRWSMTALFM-GGTLVLMEKFDPEEFLRLIERYRVTFAQFVP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 336 ELCRYLLNQPprEAEsRHKVRMAlgnGLR-------------QSIWTDFSSrfhiPQVAEFYGATECN----CSLGNFDS 398
Cdd:cd05929 225 TMFVRLLKLP--EAV-RNAYDLS---SLKrvihaaapcppwvKEQWIDWGG----PIIWEYYGGTEGQgltiINGEEWLT 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 399 QVGACGfnsrilsfvypirlvRVNEDTMElIRGPDGVciPCQPGQPGQlvgrIIQQDPlrrfDGYLNQGANNKKIASdvF 478
Cdd:cd05929 295 HPGSVG---------------RAVLGKVH-ILDEDGN--EVPPGEIGE----VYFANG----PGFEYTNDPEKTAAA--R 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 479 KKGDQAYLtGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLQMADVAVYGveVPGAE-GRAGMAAVASPT 557
Cdd:cd05929 347 NEGGWSTL-GDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVG--VPDEElGQRVHAVVQPAP 423
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 291084711 558 SNCDLESFAQTL----KKELPLYARPIFLRFLPELHKTGTFKFQKTELR 602
Cdd:cd05929 424 GADAGTALAEELiaflRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLR 472
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
75-579 |
7.40e-20 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 93.53 E-value: 7.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 75 TVPLLFASVVRRHPDKTALIFEGTNThwTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKLGVEAA 154
Cdd:PRK05605 33 TLVDLYDNAVARFGDRPALDFFGATT--TYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 155 LINTNLRRDALRHCLDTSKARALIFGSEMAS---------------AVYEIQAIldPTLTLFC--------SGSWEPSTV 211
Cdd:PRK05605 111 EHNPLYTAHELEHPFEDHGARVAIVWDKVAPtverlrrttpletivSVNMIAAM--PLLQRLAlrlpipalRKARAALTG 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 212 PA-NTEHLDPLLEDAP---KHLPSIPDKGFTDKLFYIYTSGTTGLPKAAIVVHSRYY---RMAALVYYGFRMRPDdIVYD 284
Cdd:PRK05605 189 PApGTVPWETLVDAAIggdGSDVSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFanaAQGKAWVPGLGDGPE-RVLA 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 285 CLPLYHSAGNIVGIGQCVLHGMTVVIRKKFSASRFWDDCIKYNCTIVQYIGELCRYLLnqppREAESR----HKVRMALG 360
Cdd:PRK05605 268 ALPMFHAYGLTLCLTLAVSIGGELVLLPAPDIDLILDAMKKHPPTWLPGVPPLYEKIA----EAAEERgvdlSGVRNAFS 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 361 NG--LRQSI---WTDFSSRFHIpqvaEFYGATECN-CSLGN---FDSQVGACGfnsriLSFvyPIRLVRVNEdtmelirg 431
Cdd:PRK05605 344 GAmaLPVSTvelWEKLTGGLLV----EGYGLTETSpIIVGNpmsDDRRPGYVG-----VPF--PDTEVRIVD-------- 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 432 PDGVCIPCQPGQPGQLVGRIIQqdplrRFDGYLNQGANNKKiasdVFKkgDQAYLTGDVLVMDELGYLYFRDR------T 505
Cdd:PRK05605 405 PEDPDETMPDGEEGELLVRGPQ-----VFKGYWNRPEETAK----SFL--DGWFRTGDVVVMEEDGFIRIVDRikeliiT 473
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 291084711 506 GdtfrwkGENVSTTEVEGTLSRLLQMADVAVYGveVPGAEGRAGMAA--VASPTSNCDLESFAQTLKKELPLYARP 579
Cdd:PRK05605 474 G------GFNVYPAEVEEVLREHPGVEDAAVVG--LPREDGSEEVVAavVLEPGAALDPEGLRAYCREHLTRYKVP 541
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
85-602 |
8.41e-20 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 93.15 E-value: 8.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 85 RRHPDKTALIFEGTNTHWTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNE-FVGLWLGMaKLGVEAALINTNLRRD 163
Cdd:PRK13390 8 QIAPDRPAVIVAETGEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEaLVVLWAAL-RSGLYITAINHHLTAP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 164 ALRHCLDTSKARALIFGSEMASAVYEIQAILDPTLTLFCS----GSWEPSTVPANtehldPLLEDAPKhlpsipdkgftd 239
Cdd:PRK13390 87 EADYIVGDSGARVLVASAALDGLAAKVGADLPLRLSFGGEidgfGSFEAALAGAG-----PRLTEQPC------------ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 240 KLFYIYTSGTTGLPKA------AIVVHSRYYRMAALVYYGFRMRPDDIVYDCLPLYHSAgnivGIGQC-VLH--GMTVVI 310
Cdd:PRK13390 150 GAVMLYSSGTTGFPKGiqpdlpGRDVDAPGDPIVAIARAFYDISESDIYYSSAPIYHAA----PLRWCsMVHalGGTVVL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 311 RKKFSASRFWDDCIKYNCTIVQYIGELCRYLLnQPPREAESRHKVrmalgNGLRQSIWTDFSSRFHI---------PQVA 381
Cdd:PRK13390 226 AKRFDAQATLGHVERYRITVTQMVPTMFVRLL-KLDADVRTRYDV-----SSLRAVIHAAAPCPVDVkhamidwlgPIVY 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 382 EFYGATECN----CSLGNFDSQVGACGfnSRILSFVYPirlvrVNEDTMELirgpdgvcipcqpgqPGQLVGRI-IQQD- 455
Cdd:PRK13390 300 EYYSSTEAHgmtfIDSPDWLAHPGSVG--RSVLGDLHI-----CDDDGNEL---------------PAGRIGTVyFERDr 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 456 -PLRrfdgYLNqgaNNKKIASDVFKKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLQMADV 534
Cdd:PRK13390 358 lPFR----YLN---DPEKTAAAQHPAHPFWTTVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDV 430
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 291084711 535 AVYGveVPGAEGRAGMAAVASPTSNCD-LESFAQTL----KKELPLYARPIFLRFLPELHKTGTFKFQKTELR 602
Cdd:PRK13390 431 AVIG--VPDPEMGEQVKAVIQLVEGIRgSDELARELidytRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
75-604 |
1.53e-19 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 92.39 E-value: 1.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 75 TVPLLFASVVRRHPDKTALIFEGTNThwTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEF-VGLwlgMAKLGVEA 153
Cdd:PRK07059 24 SLADLLEESFRQYADRPAFICMGKAI--TYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYpVAI---AAVLRAGY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 154 ALINTN---LRRDaLRHCLDTSKARALIFGSEMASAVyeiQAILDPTLT-----------LFCSG--------------- 204
Cdd:PRK07059 99 VVVNVNplyTPRE-LEHQLKDSGAEAIVVLENFATTV---QQVLAKTAVkhvvvasmgdlLGFKGhivnfvvrrvkkmvp 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 205 SWE-PSTVPANtehlDPLLEDAPKHLPSiPDKGFTDKLFYIYTSGTTGLPKAAIVVH----SRYYRMAALVYYGF--RMR 277
Cdd:PRK07059 175 AWSlPGHVRFN----DALAEGARQTFKP-VKLGPDDVAFLQYTGGTTGVSKGATLLHrnivANVLQMEAWLQPAFekKPR 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 278 PDDIVYDC-LPLYHsagnIVGIGQCVLHGM-----TVVIRKKFSASRFWDDCIKYNCTIVQYIGELCRYLLNQPPREAES 351
Cdd:PRK07059 250 PDQLNFVCaLPLYH----IFALTVCGLLGMrtggrNILIPNPRDIPGFIKELKKYQVHIFPAVNTLYNALLNNPDFDKLD 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 352 RHKVRMALGNGL--RQSIWTDFSSRFHIPqVAEFYGATECN----CSLGNFDSQVGACGFnsrilsfvyPIRLVRVNedt 425
Cdd:PRK07059 326 FSKLIVANGGGMavQRPVAERWLEMTGCP-ITEGYGLSETSpvatCNPVDATEFSGTIGL---------PLPSTEVS--- 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 426 melIRGPDGVCIPcqPGQPGQLVGRIIQQDPlrrfdGYLNQGANNKKIASDvfkkgDQAYLTGDVLVMDELGYLYFRDRT 505
Cdd:PRK07059 393 ---IRDDDGNDLP--LGEPGEICIRGPQVMA-----GYWNRPDETAKVMTA-----DGFFRTGDVGVMDERGYTKIVDRK 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 506 GDTFRWKGENVSTTEVEGTLSRLLQMADVAVYGVEVPGAeGRAGMAAVASPTSNCDLESFAQTLKKELPLYARPIFLRFL 585
Cdd:PRK07059 458 KDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHS-GEAVKLFVVKKDPALTEEDVKAFCKERLTNYKRPKFVEFR 536
|
570
....*....|....*....
gi 291084711 586 PELHKTGTFKFQKTELRKE 604
Cdd:PRK07059 537 TELPKTNVGKILRRELRDG 555
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
241-595 |
2.04e-19 |
|
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain
Pssm-ID: 341288 [Multi-domain] Cd Length: 320 Bit Score: 89.77 E-value: 2.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 241 LFYI-YTSGTTGLPKAaivvhsrYYR-----MAALVY--YGFRMRPDDIVYDCLPLYHSaGNIVGIGQCVLHGMTVVIRK 312
Cdd:cd17633 2 PFYIgFTSGTTGLPKA-------YYRserswIESFVCneDLFNISGEDAILAPGPLSHS-LFLYGAISALYLGGTFIGQR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 313 KFSASRFWDDCIKYNCTIVQYIGELCRYLLnqppREAESRHKVRMAL--GNGLRQSIWTDFSSRFHIPQVAEFYGATEcn 390
Cdd:cd17633 74 KFNPKSWIRKINQYNATVIYLVPTMLQALA----RTLEPESKIKSIFssGQKLFESTKKKLKNIFPKANLIEFYGTSE-- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 391 cslgnfdsqvgacgfnsriLSFVypirLVRVNEDTmeliRGPDGVCIPCqPG-------QPGQLVGRIIQQDPLRrFDGY 463
Cdd:cd17633 148 -------------------LSFI----TYNFNQES----RPPNSVGRPF-PNveieirnADGGEIGKIFVKSEMV-FSGY 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 464 LNQGANNKkiasdvfkkgDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLQMADVAVYGVEvpg 543
Cdd:cd17633 199 VRGGFSNP----------DGWMSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIP--- 265
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 291084711 544 aEGRAGMAAVASPTSNC----DLESFaqtLKKELPLYARPIFLRFLPELHKTGTFK 595
Cdd:cd17633 266 -DARFGEIAVALYSGDKltykQLKRF---LKQKLSRYEIPKKIIFVDSLPYTSSGK 317
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
102-602 |
4.48e-19 |
|
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: 90.23 E-value: 4.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 102 WTFRQLDDYSSSVANFLQAR-GLVSGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALRHCLD-TSKARALIF 179
Cdd:cd05958 11 WTYRDLLALANRIANVLVGElGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDkARITVALCA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 180 GSEMASavyeiqailDPTltlfcsGSWEpstvpantehldplledapkhlpsipdkgftdklfyiYTSGTTGLPKAAIVV 259
Cdd:cd05958 91 HALTAS---------DDI------CILA-------------------------------------FTSGTTGAPKATMHF 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 260 HsRYYRMAALVY--YGFRMRPDDIVYDCLPLYHSagniVGIGQCVLH----GMTVVIRKKFSASRFWDDCIKYNCTIVQY 333
Cdd:cd05958 119 H-RDPLASADRYavNVLRLREDDRFVGSPPLAFT----FGLGGVLLFpfgvGASGVLLEEATPDLLLSAIARYKPTVLFT 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 334 IGELCRYLLNQPPREAESRHKVRMAL--GNGLRQSIWTDFSSRFHIPqVAEFYGATEcncslgNFDSQVGACGFNSRILS 411
Cdd:cd05958 194 APTAYRAMLAHPDAAGPDLSSLRKCVsaGEALPAALHRAWKEATGIP-IIDGIGSTE------MFHIFISARPGDARPGA 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 412 FVYPI---RLVRVNEDTMELirgPDGVcipcqpgqpgqlVGRIIQQDPlrrfDGYLNqgaNNKKIASDVFkkGDQAYLTG 488
Cdd:cd05958 267 TGKPVpgyEAKVVDDEGNPV---PDGT------------IGRLAVRGP----TGCRY---LADKRQRTYV--QGGWNITG 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 489 DVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLQMADVAVYGVEVP--GAEGRAGMAAVASPTSNCDL-ESF 565
Cdd:cd05958 323 DTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDEsrGVVVKAFVVLRPGVIPGPVLaREL 402
|
490 500 510
....*....|....*....|....*....|....*..
gi 291084711 566 AQTLKKELPLYARPIFLRFLPELHKTGTFKFQKTELR 602
Cdd:cd05958 403 QDHAKAHIAPYKYPRAIEFVTELPRTATGKLQRFALR 439
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
244-598 |
2.36e-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: 86.79 E-value: 2.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 244 IYTSGTTGLPKAAIVVHSRYYRMAALVYYGFRMRPDDiVYDCL-PLYHSAGNIVGIGQCVLHGMTVVIRKKFSASRFWDD 322
Cdd:cd17638 6 MFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDD-RYLIInPFFHTFGYKAGIVACLLTGATVVPVAVFDVDAILEA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 323 CIKYNCTIVQYIGELCRYLLNQPPREAESRHKVRMALGNG--LRQSIWTDFSSRFHIPQVAEFYGATECNCSL-----GN 395
Cdd:cd17638 85 IERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVTGAatVPVELVRRMRSELGFETVLTAYGLTEAGVATmcrpgDD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 396 FDSQVGACGFnsrilsfVYPIRLVRVNEDTMELIRGPDgvcipcqpgqpgqlvgrIIQqdplrrfdGYL-NQGANNKKIA 474
Cdd:cd17638 165 AETVATTCGR-------ACPGFEVRIADDGEVLVRGYN-----------------VMQ--------GYLdDPEATAEAID 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 475 SDvfkkgdqAYL-TGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLQMADVAVYGV--EVPGAEGRAgmA 551
Cdd:cd17638 213 AD-------GWLhTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVpdERMGEVGKA--F 283
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 291084711 552 AVASPTSNCDLESFAQTLKKELPLYARPIFLRFLPELHKTGTFKFQK 598
Cdd:cd17638 284 VVARPGVTLTEEDVIAWCRERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
239-603 |
3.09e-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: 88.16 E-value: 3.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 239 DKLFYIYTSGTTGLPKAAIVVHSRYYRMAALVYYGFRMRPDDIVYDCLPLYHSAGNIVGIGQCVLHGMTVVirkkFSAS- 317
Cdd:cd05909 148 DPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPFFHSFGLTGCLWLPLLSGIKVV----FHPNp 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 318 -------RFWDDcikYNCTIVQYIGELCRYLLNQPPREAESRHKVRMALGNGLRQSIWTDFSSRFHIPqVAEFYGATECN 390
Cdd:cd05909 224 ldykkipELIYD---KKATILLGTPTFLRGYARAAHPEDFSSLRLVVAGAEKLKDTLRQEFQEKFGIR-ILEGYGTTECS 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 391 ----CSLGNFDSQVGACG-----FNSRILSfVYPIRLVRVNEDTMELIRGPDgvcipcqpgqpgqlvgriiqqdplrRFD 461
Cdd:cd05909 300 pvisVNTPQSPNKEGTVGrplpgMEVKIVS-VETHEEVPIGEGGLLLVRGPN-------------------------VML 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 462 GYLNqgaNNKKIasdVFKKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLQMaDVAVYGVEV 541
Cdd:cd05909 354 GYLN---EPELT---SFAFGDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEILPE-DNEVAVVSV 426
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 291084711 542 PgaEGRAGMAAVASPT-SNCDLESFAQTLKK-ELPLYARPIFLRFLPELHKTGTFKFQKTELRK 603
Cdd:cd05909 427 P--DGRKGEKIVLLTTtTDTDPSSLNDILKNaGISNLAKPSYIHQVEEIPLLGTGKPDYVTLKA 488
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
79-601 |
4.63e-18 |
|
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: 87.64 E-value: 4.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 79 LFASVVRRHPDKTALIFEGTNthWTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKLGVEAALINT 158
Cdd:cd12117 2 LFEEQAARTPDAVAVVYGDRS--LTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 159 NLRRDALRHCLDTSKARALIFGSEMASAVYEIQAILDptltlfcsgswepstvpantehLDPLLEDAPKHLPSIPDKGft 238
Cdd:cd12117 80 ELPAERLAFMLADAGAKVLLTDRSLAGRAGGLEVAVV----------------------IDEALDAGPAGNPAVPVSP-- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 239 DKLFYI-YTSGTTGLPKAAIVVHSRYYRMAALVYYGfRMRPDDIVYDCLPLYHSAG--NIVGigqCVLHGMTVVIRKK-- 313
Cdd:cd12117 136 DDLAYVmYTSGSTGRPKGVAVTHRGVVRLVKNTNYV-TLGPDDRVLQTSPLAFDAStfEIWG---ALLNGARLVLAPKgt 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 314 -FSASRFWDDCIKYNCTIVQYIGELCRYLLNQPPR------------EAESRHKVRMALGNGLRQSIW--------TDFS 372
Cdd:cd12117 212 lLDPDALGALIAEEGVTVLWLTAALFNQLADEDPEcfaglrelltggEVVSPPHVRRVLAACPGLRLVngygptenTTFT 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 373 SRFHIPQVAEFYGATECNCSLGNfdSQVgacgfnsRILsfvypirlvrvnedtmelirgpDGVCIPCQPGQPGQLVgriI 452
Cdd:cd12117 292 TSHVVTELDEVAGSIPIGRPIAN--TRV-------YVL----------------------DEDGRPVPPGVPGELY---V 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 453 QQDPLRRfdGYLNQGA-NNKKIASDVFKKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLQM 531
Cdd:cd12117 338 GGDGLAL--GYLNRPAlTAERFVADPFGPGERLYRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGV 415
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 532 ADVAVygVEVPGAEGRAGMAAVASPTSNCDLESFAQTLKKELPLYARPIFLRFLPELHKTGTFKFQKTEL 601
Cdd:cd12117 416 REAVV--VVREDAGGDKRLVAYVVAEGALDAAELRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
79-603 |
5.07e-18 |
|
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: 86.98 E-value: 5.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 79 LFASVVRRHPDKTALIFEGTNThwTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKLGVEAALINT 158
Cdd:cd17653 2 AFERIAAAHPDAVAVESLGGSL--TYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 159 NLRRDALRHCLDTSKARALIFgsemasavyeiqaildptltlfcsgswepstvpantehldplledapkhlPSIPDkgft 238
Cdd:cd17653 80 KLPSARIQAILRTSGATLLLT--------------------------------------------------TDSPD---- 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 239 DKLFYIYTSGTTGLPKAAIVVHSRYYRMAALVYYGFRMRPDD-------IVYDClplyhSAGNIVGigqCVLHGMTVVIR 311
Cdd:cd17653 106 DLAYIIFTSGSTGIPKGVMVPHRGVLNYVSQPPARLDVGPGSrvaqvlsIAFDA-----CIGEIFS---TLCNGGTLVLA 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 312 kkfSASRFWDDCIK----YNCT--IVQYIgelcryllnqPPREAESRHKVRMAlGNGLRQSIWTDFSSRfhiPQVAEFYG 385
Cdd:cd17653 178 ---DPSDPFAHVARtvdaLMSTpsILSTL----------SPQDFPNLKTIFLG-GEAVPPSLLDRWSPG---RRLYNAYG 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 386 ATECNCSlgnfdsqvgaCGFNS-RILSFV---YPIRLVRV---NEDTMELIRGPDG-VCIpcqpgqPGQLVGRiiqqdpl 457
Cdd:cd17653 241 PTECTIS----------STMTElLPGQPVtigKPIPNSTCyilDADLQPVPEGVVGeICI------SGVQVAR------- 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 458 rrfdGYLNQGA-NNKKIASDVFKKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLQMADVAV 536
Cdd:cd17653 298 ----GYLGNPAlTASKFVPDPFWPGSRMYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEVVLQSQPEVTQAA 373
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 291084711 537 YGVevpgAEGRagMAAVASPTSnCDLESFAQTLKKELPLYARPIFLRFLPELHKTGTFKFQKTELRK 603
Cdd:cd17653 374 AIV----VNGR--LVAFVTPET-VDVDGLRSELAKHLPSYAVPDRIIALDSFPLTANGKVDRKALRE 433
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
79-613 |
5.98e-18 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 88.68 E-value: 5.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 79 LFASVVRRHPDKTALIFEgtNTHWTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKLGVEAALINT 158
Cdd:PRK12467 517 LIEAQARQHPERPALVFG--EQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDP 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 159 NLRRDALRHCLDTSKARALIFGSEMAsavyeiqAILDptltlfcsgswEPSTVPA-NTEHLDPLLEDAPKHLPSIPDKgf 237
Cdd:PRK12467 595 EYPQDRLAYMLDDSGVRLLLTQSHLL-------AQLP-----------VPAGLRSlCLDEPADLLCGYSGHNPEVALD-- 654
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 238 TDKLFY-IYTSGTTGLPKAAIVVHSRYYRMAALVYYGFRMRPDDIVYDCLPLYHSAGNIVGIGQcVLHGMTVVIRKK--- 313
Cdd:PRK12467 655 PDNLAYvIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGA-LASGATLHLLPPdca 733
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 314 FSASRFWDDCIKYNCTIVQYIGELCRYLLnQPPREAESRHKVRMALG------NGLRQsiWTDFSsrfhiPQVAEF--YG 385
Cdd:PRK12467 734 RDAEAFAALMADQGVTVLKIVPSHLQALL-QASRVALPRPQRALVCGgealqvDLLAR--VRALG-----PGARLInhYG 805
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 386 ATECncslgNFDSQVGACGFNSRILSFVyPIRLVRVNEDTMELirgpDGVCIPCQPGQPGQLvgrIIQQDPLRRfdGYLN 465
Cdd:PRK12467 806 PTET-----TVGVSTYELSDEERDFGNV-PIGQPLANLGLYIL----DHYLNPVPVGVVGEL---YIGGAGLAR--GYHR 870
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 466 QGA-NNKKIASDVF-KKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEgtlSRLLQMADVAVYGVEVPG 543
Cdd:PRK12467 871 RPAlTAERFVPDPFgADGGRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIE---ARLLAQPGVREAVVLAQP 947
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 291084711 544 AEGRAGMAAVASPTSNCD-------LESFAQTLKKELPLYARPIFLRFLPELHKTGTFKFQKTELRKegFDPSVVKD 613
Cdd:PRK12467 948 GDAGLQLVAYLVPAAVADgaehqatRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALPK--PDASAVQA 1022
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
79-601 |
6.60e-18 |
|
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.
Pssm-ID: 341300 [Multi-domain] Cd Length: 440 Bit Score: 86.84 E-value: 6.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 79 LFASVVRRHPDKTALIFEGTNthWTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKLGVEAALINT 158
Cdd:cd17645 3 LFEEQVERTPDHVAVVDRGQS--LTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 159 NLRRDALRHCLDTSKARALIFGSEmasavyeiqaildptltlfcsgswepstvpantehldplledapkhlpsipdkgft 238
Cdd:cd17645 81 DYPGERIAYMLADSSAKILLTNPD-------------------------------------------------------- 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 239 DKLFYIYTSGTTGLPKAAIVVHSR------YYRMA--------ALVYYGFRMrpDDIVYDCLPlYHSAGnivgigqCVLH 304
Cdd:cd17645 105 DLAYVIYTSGSTGLPKGVMIEHHNlvnlceWHRPYfgvtpadkSLVYASFSF--DASAWEIFP-HLTAG-------AALH 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 305 GMTVVIRkkFSASRFWDDCIKYNCTIVQYIGELCRYLLnqppreAESRHKVRMAL--GNGLRQSIWTDFssrfhipQVAE 382
Cdd:cd17645 175 VVPSERR--LDLDALNDYFNQEGITISFLPTGAAEQFM------QLDNQSLRVLLtgGDKLKKIERKGY-------KLVN 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 383 FYGATECNCSLGNF--DSQVGAcgfnsriLSFVYPIRLVRVnedtmeLIRGPDgvcIPCQP-GQPGQLVgriIQQDPLRR 459
Cdd:cd17645 240 NYGPTENTVVATSFeiDKPYAN-------IPIGKPIDNTRV------YILDEA---LQLQPiGVAGELC---IAGEGLAR 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 460 fdGYLNQ-GANNKKIASDVFKKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLQMADVAVYG 538
Cdd:cd17645 301 --GYLNRpELTAEKFIVHPFVPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLA 378
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 291084711 539 VEvpGAEGRAGMAAVASPTSNCDLESFAQTLKKELPLYARPIFLRFLPELHKTGTFKFQKTEL 601
Cdd:cd17645 379 KE--DADGRKYLVAYVTAPEEIPHEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
79-604 |
1.36e-17 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 86.08 E-value: 1.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 79 LFASVVRRHPDKTALIFE-GTNTHWTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKLGVEAALIN 157
Cdd:PRK07514 5 LFDALRAAFADRDAPFIEtPDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 158 TNLRRDALRHCLDTSKARALIFGSEMASAVYEIQ----AILDPTLTLFCSGSwepstVPANTEHLDPLLEDAPKH---LP 230
Cdd:PRK07514 85 TAYTLAELDYFIGDAEPALVVCDPANFAWLSKIAaaagAPHVETLDADGTGS-----LLEAAAAAPDDFETVPRGaddLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 231 SIpdkgftdklfyIYTSGTTGLPKAAIVVHSRYYRMA-ALV-YYGFrmRPDDIVYDCLPLYHSAGNIVGIGQCVLHGMTV 308
Cdd:PRK07514 160 AI-----------LYTSGTTGRSKGAMLSHGNLLSNAlTLVdYWRF--TPDDVLIHALPIFHTHGLFVATNVALLAGASM 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 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 291084711 380 VAEFYGATECNCSLGN-FDSQ--VGACGFnsrilsfvyPIRLVRVNedtmelIRGPD-GVciPCQPGQPGQlvgriIQ-Q 454
Cdd:PRK07514 297 ILERYGMTETNMNTSNpYDGErrAGTVGF---------PLPGVSLR------VTDPEtGA--ELPPGEIGM-----IEvK 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 455 DPlRRFDGYLNqgaNNKKIASDVfkKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLQMADV 534
Cdd:PRK07514 355 GP-NVFKGYWR---MPEKTAEEF--RADGFFITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVES 428
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 291084711 535 AVYGveVPGAE-GRAGMAA-VASPTSNCDLESFAQTLKKELPLYARPIFLRFLPELHKTGTFKFQKTELRKE 604
Cdd:PRK07514 429 AVIG--VPHPDfGEGVTAVvVPKPGAALDEAAILAALKGRLARFKQPKRVFFVDELPRNTMGKVQKNLLREQ 498
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
79-604 |
1.95e-17 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 85.88 E-value: 1.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 79 LFASVVRRHPDKTALIFEGTNThwTFRQLDDYSSSVANFLQAR-GLVSGNVVALFMENRnefvgLWLGMAKLGV-EAALI 156
Cdd:PRK08974 28 MFEQAVARYADQPAFINMGEVM--TFRKLEERSRAFAAYLQNGlGLKKGDRVALMMPNL-----LQYPIALFGIlRAGMI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 157 NTNLR-----RDaLRHCLDTSKARALIFGSEMASAVYEI-------QAILD--------PTLTLfcsgswepstVPANTE 216
Cdd:PRK08974 101 VVNVNplytpRE-LEHQLNDSGAKAIVIVSNFAHTLEKVvfktpvkHVILTrmgdqlstAKGTL----------VNFVVK 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 217 HLDPLLedaPK-HLPSI-----------------PDKGFTDKLFYIYTSGTTGLPKAAIVVHSRY---YRMAALVYYGFR 275
Cdd:PRK08974 170 YIKRLV---PKyHLPDAisfrsalhkgrrmqyvkPELVPEDLAFLQYTGGTTGVAKGAMLTHRNMlanLEQAKAAYGPLL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 276 MRPDDIVYDCLPLYHSAGNIVgigQCVLH----GMTVVIRKKFSASRFWDDCIKYNCTIVQYIGELCRYLLNQPPREAES 351
Cdd:PRK08974 247 HPGKELVVTALPLYHIFALTV---NCLLFielgGQNLLITNPRDIPGFVKELKKYPFTAITGVNTLFNALLNNEEFQELD 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 352 RHKVRMALGNGL--RQSI---WTDFSSRFHIpqvaEFYGATECN----CSLGNFDSQVGACGFNSrilsfvyPIRLVRVN 422
Cdd:PRK08974 324 FSSLKLSVGGGMavQQAVaerWVKLTGQYLL----EGYGLTECSplvsVNPYDLDYYSGSIGLPV-------PSTEIKLV 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 423 EDtmelirgpDGVCIPcqPGQPGQLVGRIIQQdplrrFDGYLNQGANNKKIASDvfkkgdqAYL-TGDVLVMDELGYLYF 501
Cdd:PRK08974 393 DD--------DGNEVP--PGEPGELWVKGPQV-----MLGYWQRPEATDEVIKD-------GWLaTGDIAVMDEEGFLRI 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 502 RDRTGDTFRWKGENVSTTEVEGTLSRLLQMADVAVYGVEvPGAEGRAGMAAVASPTSNCDLESFAQTLKKELPLYARPIF 581
Cdd:PRK08974 451 VDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVP-SEVSGEAVKIFVVKKDPSLTEEELITHCRRHLTGYKVPKL 529
|
570 580
....*....|....*....|...
gi 291084711 582 LRFLPELHKTGTFKFQKTELRKE 604
Cdd:PRK08974 530 VEFRDELPKSNVGKILRRELRDE 552
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
88-603 |
3.27e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 84.83 E-value: 3.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 88 PDKTALIFEgtNTHWTFRQLDDYSSSVANFLQARGLVSgNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALRH 167
Cdd:PRK07638 15 PNKIAIKEN--DRVLTYKDWFESVCKVANWLNEKESKN-KTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 168 CLDTSKArALIFGSEmasavYEIQAILDPTLTLFCSGSWEP-----STVPANTEHldplLEDAPkhlpsipdkgftdklF 242
Cdd:PRK07638 92 RLAISNA-DMIVTER-----YKLNDLPDEEGRVIEIDEWKRmiekyLPTYAPIEN----VQNAP---------------F 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 243 YI-YTSGTTGLPKAAIVVHSRYYRMAALVYYGFRMRPDDIVYDCLPLYHS-----AGNIVGIGQcvlhgmTVVIRKKFSA 316
Cdd:PRK07638 147 YMgFTSGSTGKPKAFLRAQQSWLHSFDCNVHDFHMKREDSVLIAGTLVHSlflygAISTLYVGQ------TVHLMRKFIP 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 317 SRFWDDCIKYNCTIVQYIGELCRYLLnqppREAESRHKVRMALGNGLRQSIWT--DFSSRFHIPQVAEFYGATEcncslg 394
Cdd:PRK07638 221 NQVLDKLETENISVMYTVPTMLESLY----KENRVIENKMKIISSGAKWEAEAkeKIKNIFPYAKLYEFYGASE------ 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 395 nfdsqvgacgfnsriLSFVYPIrlvrVNEDTMeliRGPDGVCIPCQPG------------QPGQlVGRIIQQDPLrRFDG 462
Cdd:PRK07638 291 ---------------LSFVTAL----VDEESE---RRPNSVGRPFHNVqvricneageevQKGE-IGTVYVKSPQ-FFMG 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 463 YLNQGANNKKIASDvfkkgdqAYLT-GDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLQMADVAVYGVEV 541
Cdd:PRK07638 347 YIIGGVLARELNAD-------GWMTvRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPD 419
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 291084711 542 PgaegRAGMAAVASPTSNCDLESFAQTLKKELPLYARPIFLRFLPELHKTGTFKFQKTELRK 603
Cdd:PRK07638 420 S----YWGEKPVAIIKGSATKQQLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEAKS 477
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
243-603 |
3.99e-17 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 83.30 E-value: 3.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 243 YIYTSGTTGLPKAAIVVHSRYYRMAALVYYGFRMRPDDIVYDCLPLYHSAGNIVGIGQCVLHGMTVVI------RKKFSA 316
Cdd:cd05944 7 YFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVVLagpagyRNPGLF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 317 SRFWDDCIKYNCTIVQYIGELCRYLLNQPPREAESRHKVRMALGNGLRQSIWTDFSSRFHIPqVAEFYGATECNCSLG-N 395
Cdd:cd05944 87 DNFWKLVERYRITSLSTVPTVYAALLQVPVNADISSLRFAMSGAAPLPVELRARFEDATGLP-VVEGYGLTEATCLVAvN 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 396 FDS---QVGACGfnsriLSFVYPIRLVRVNEDTMELIRgpdgvciPCQPGQpgqlVGRIIQQDPlRRFDGYLNQGANNKK 472
Cdd:cd05944 166 PPDgpkRPGSVG-----LRLPYARVRIKVLDGVGRLLR-------DCAPDE----VGEICVAGP-GVFGGYLYTEGNKNA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 473 IASDVFKKgdqaylTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLQMADVAVYGV------EVPGAEG 546
Cdd:cd05944 229 FVADGWLN------TGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQpdahagELPVAYV 302
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 291084711 547 RAGMAAVASPTsncDLESFAQTLKKELPlyARPIFLRFLPELHKTGTFKFQKTELRK 603
Cdd:cd05944 303 QLKPGAVVEEE---ELLAWARDHVPERA--AVPKHIEVLEELPVTAVGKVFKPALRA 354
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
79-601 |
5.29e-17 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 84.28 E-value: 5.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 79 LFASVVRRHPDKTALIFEgtNTHWTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKLGVEAALINT 158
Cdd:PRK13383 40 LLAVTAARWPGRTAIIDD--DGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPIST 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 159 NLRRDALRHCLDTSKARALIFGSEMASavyEIQAILDPTLTLfcsgswEPSTVPAntehldpllEDAPKHlPSIPDKGft 238
Cdd:PRK13383 118 EFRSDALAAALRAHHISTVVADNEFAE---RIAGADDAVAVI------DPATAGA---------EESGGR-PAVAAPG-- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 239 dkLFYIYTSGTTGLPKAaiVVHSRYYRMAALVYYGF----RMRPDDIVYDCLPLYHSagniVGIGQCVLH---GMTVVIR 311
Cdd:PRK13383 177 --RIVLLTSGTTGKPKG--VPRAPQLRSAVGVWVTIldrtRLRTGSRISVAMPMFHG----LGLGMLMLTialGGTVLTH 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 312 KKFSASRFWDDCIKYNCTIVQYIGELCRYLLNQPPReAESRH-----KVRMALGNGLRQSIWTDFSSRFHiPQVAEFYGA 386
Cdd:PRK13383 249 RHFDAEAALAQASLHRADAFTAVPVVLARILELPPR-VRARNplpqlRVVMSSGDRLDPTLGQRFMDTYG-DILYNGYGS 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 387 TEcncslgnfdsqVGacgfnsrILSFVYPIRLvrvnEDTMELIRGPDGVC---IPCQPGQP--GQLVGRIIQQDPLRRfD 461
Cdd:PRK13383 327 TE-----------VG-------IGALATPADL----RDAPETVGKPVAGCpvrILDRNNRPvgPRVTGRIFVGGELAG-T 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 462 GYlnQGANNKKIASDVFKKGDQAYLtgdvlvmDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLQMADVAVYGVEV 541
Cdd:PRK13383 384 RY--TDGGGKAVVDGMTSTGDMGYL-------DNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPD 454
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 542 PGAEGRAGMAAVASPTSNCDLESFAQTLKKELPLYARPIFLRFLPELHKTGTFKFQKTEL 601
Cdd:PRK13383 455 ERFGHRLAAFVVLHPGSGVDAAQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
86-604 |
9.02e-17 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 83.93 E-value: 9.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 86 RHPDKTALIFEGTNThwTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRDAL 165
Cdd:PRK06710 36 RYPEKKALHFLGKDI--TFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTEREL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 166 RHCLDTSKARALIFGSEMASAVYEIQA-----------ILD----PT--LTLFCSGSWEPSTVPANTEHLDPLLEDAPKH 228
Cdd:PRK06710 114 EYQLHDSGAKVILCLDLVFPRVTNVQSatkiehvivtrIADflpfPKnlLYPFVQKKQSNLVVKVSESETIHLWNSVEKE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 229 LPS---IPDKGFTDKLFYIYTSGTTGLPKAAIVVHSRYYRMAAL-VYYGFRMRP-DDIVYDCLPLYHSAGNIVGIGQCVL 303
Cdd:PRK06710 194 VNTgveVPCDPENDLALLQYTGGTTGFPKGVMLTHKNLVSNTLMgVQWLYNCKEgEEVVLGVLPFFHVYGMTAVMNLSIM 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 304 HGMTVVIRKKFSASRFWDDCIKYNCTIVQYIGELCRYLLNQPPREAESRHKVRMALGNG--LRQSIWTDFSsRFHIPQVA 381
Cdd:PRK06710 274 QGYKMVLIPKFDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLLKEYDISSIRACISGSapLPVEVQEKFE-TVTGGKLV 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 382 EFYGATECN-CSLGNF--DSQV-GACGF-----NSRILSFvypirlvrvneDTMELIRgpdgvcipcqpgqPGQlVGRII 452
Cdd:PRK06710 353 EGYGLTESSpVTHSNFlwEKRVpGSIGVpwpdtEAMIMSL-----------ETGEALP-------------PGE-IGEIV 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 453 QQDPlRRFDGYLNQGANNKKIASDvfkkgdqAYL-TGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLQM 531
Cdd:PRK06710 408 VKGP-QIMKGYWNKPEETAAVLQD-------GWLhTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKV 479
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 291084711 532 ADVAVYGVEVPGAEGRAGMAAVASPTSNCDLESFAQTLKKELPLYARPIFLRFLPELHKTGTFKFQKTELRKE 604
Cdd:PRK06710 480 QEVVTIGVPDPYRGETVKAFVVLKEGTECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVLIEE 552
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
79-603 |
1.20e-16 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 84.62 E-value: 1.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 79 LFASVVRRHPDKTALIFEGTntHWTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKLGVEAALINT 158
Cdd:PRK12316 2008 RIAEQAARAPEAIAVVFGDQ--HLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDP 2085
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 159 NLRRDALRHCLDTSKARALIFGSEMASAVYEIQAIldPTLTLFCSGSWE--PSTVPANTEHLDPLledapkhlpsipdkg 236
Cdd:PRK12316 2086 NYPAERLAYMLEDSGAALLLTQRHLLERLPLPAGV--ARLPLDRDAEWAdyPDTAPAVQLAGENL--------------- 2148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 237 ftdkLFYIYTSGTTGLPKAAIVVHsryyrmAALVYY------GFRMRPDDIVYDCLPLYHSaGNIVGIGQCVLHGMTVVI 310
Cdd:PRK12316 2149 ----AYVIYTSGSTGLPKGVAVSH------GALVAHcqaageRYELSPADCELQFMSFSFD-GAHEQWFHPLLNGARVLI 2217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 311 R--KKFSASRFWDDCIKYNCTIVQYIGELCRYLLNQPPREAeSRHKVRMAL--GNGLRQSIWTDFSSRFHIPQVAEFYGA 386
Cdd:PRK12316 2218 RddELWDPEQLYDEMERHGVTILDFPPVYLQQLAEHAERDG-RPPAVRVYCfgGEAVPAASLRLAWEALRPVYLFNGYGP 2296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 387 TECNCSLGNFDSQ-VGACGfnsrilSFVYPIRLVRVNEDTMELirgpDGVCIPCQPGQPGQLVgriIQQDPLRRfdGYLN 465
Cdd:PRK12316 2297 TEAVVTPLLWKCRpQDPCG------AAYVPIGRALGNRRAYIL----DADLNLLAPGMAGELY---LGGEGLAR--GYLN 2361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 466 Q-GANNKKIASDVF-KKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLQMADVAVygVEVPG 543
Cdd:PRK12316 2362 RpGLTAERFVPDPFsASGERLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVV--VAQDG 2439
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 291084711 544 AEGRAGMAAVASPTSNCDL-ESFAQTLKKELPLYARPIFLRFLPELHKTGTFKFQKTELRK 603
Cdd:PRK12316 2440 ASGKQLVAYVVPDDAAEDLlAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPK 2500
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
79-588 |
1.66e-16 |
|
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: 82.71 E-value: 1.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 79 LFASVVRRHPDKTALIFEGTntHWTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKLGVEAALINT 158
Cdd:cd17646 3 LVAEQAARTPDAPAVVDEGR--TLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 159 NLRRDALRHCLDTSKARALIFGSEMASAVYeiqAILDPTLTlfcsGSWEPSTVPAnTEHLDPLLEDAPKHLpsipdkgft 238
Cdd:cd17646 81 GYPADRLAYMLADAGPAVVLTTADLAARLP---AGGDVALL----GDEALAAPPA-TPPLVPPRPDNLAYV--------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 239 dklfyIYTSGTTGLPKAAIVVHsryyrmAALVYY------GFRMRPDDIV-------YDC------LPLyhSAGNIVGIG 299
Cdd:cd17646 144 -----IYTSGSTGRPKGVMVTH------AGIVNRllwmqdEYPLGPGDRVlqktplsFDVsvwelfWPL--VAGARLVVA 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 300 QCVLHG----MTVVIRkkfsasrfwddciKYNCTIVQYIGELCRYLLNQPprEAESRHKVRMAL--GNGLRQSIWTDFSS 373
Cdd:cd17646 211 RPGGHRdpayLAALIR-------------EHGVTTCHFVPSMLRVFLAEP--AAGSCASLRRVFcsGEALPPELAARFLA 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 374 RFHIPQVaEFYGATE-------CNCSLGNFDSQV--GACGFNSRilsfvypirlVRVNEDTMElirgpdgvciPCQPGQP 444
Cdd:cd17646 276 LPGAELH-NLYGPTEaaidvthWPVRGPAETPSVpiGRPVPNTR----------LYVLDDALR----------PVPVGVP 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 445 GQLVgriIQQDPLRRfdGYLNQGA-NNKKIASDVFKKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEG 523
Cdd:cd17646 335 GELY---LGGVQLAR--GYLGRPAlTAERFVPDPFGPGSRMYRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEA 409
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 291084711 524 TLSRLLQMADVAVYGVEVPGAEGRAGMAAVASPTSNC-DLESFAQTLKKELPLYARPIFLRFLPEL 588
Cdd:cd17646 410 ALAAHPAVTHAVVVARAAPAGAARLVGYVVPAAGAAGpDTAALRAHLAERLPEYMVPAAFVVLDAL 475
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
74-602 |
1.90e-16 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 82.94 E-value: 1.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 74 KTVPLLFASVVRRHPDKTALIFEGTNTHWTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKLGVEA 153
Cdd:PRK08315 16 QTIGQLLDRTAARYPDREALVYRDQGLRWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAIL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 154 ALINTNLRRDALRHCLDTSKARALIF-----GSEMASAVYEiqaiLDPTLTLFCSGSWEPSTVP-------------ANT 215
Cdd:PRK08315 96 VTINPAYRLSELEYALNQSGCKALIAadgfkDSDYVAMLYE----LAPELATCEPGQLQSARLPelrrviflgdekhPGM 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 216 EHLDPLLEDA----PKHLPSIPDK-GFTDKLFYIYTSGTTGLPKAAIVVHSRYYRMAALVyyGFRMR--PDDIVYDCLPL 288
Cdd:PRK08315 172 LNFDELLALGravdDAELAARQATlDPDDPINIQYTSGTTGFPKGATLTHRNILNNGYFI--GEAMKltEEDRLCIPVPL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 289 YHSAGNIVGIGQCVLHGMTVVirkkFSASRFwdDCI-------KYNCTIVQ-----YIGElcrylLNQPPREAESRHKVR 356
Cdd:PRK08315 250 YHCFGMVLGNLACVTHGATMV----YPGEGF--DPLatlaaveEERCTALYgvptmFIAE-----LDHPDFARFDLSSLR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 357 ---MAlgnG-------LRQSIwtdfsSRFHIPQVAEFYGATEcnCSLGNFDS--------QVGACGfnsRILSFVYpirl 418
Cdd:PRK08315 319 tgiMA---GspcpievMKRVI-----DKMHMSEVTIAYGMTE--TSPVSTQTrtddplekRVTTVG---RALPHLE---- 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 419 VR-VNEDTMElirgpdgvciPCQPGQPGQLVGRiiqqdplrrfdGYL-------NQGANNKKIASDvfkkgdqAYL-TGD 489
Cdd:PRK08315 382 VKiVDPETGE----------TVPRGEQGELCTR-----------GYSvmkgywnDPEKTAEAIDAD-------GWMhTGD 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 490 VLVMDELGYLYFrdrTGdtfRWK------GENVSTTEVEGTLSRLLQMADVAVYGveVPGAE-GRAGMAAV-----ASPT 557
Cdd:PRK08315 434 LAVMDEEGYVNI---VG---RIKdmiirgGENIYPREIEEFLYTHPKIQDVQVVG--VPDEKyGEEVCAWIilrpgATLT 505
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 291084711 558 SNcDLESFAQTlkkELPLYARPIFLRFLPELHKTGTFKFQKTELR 602
Cdd:PRK08315 506 EE-DVRDFCRG---KIAHYKIPRYIRFVDEFPMTVTGKIQKFKMR 546
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
79-591 |
2.97e-16 |
|
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341310 [Multi-domain] Cd Length: 490 Bit Score: 81.99 E-value: 2.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 79 LFASVVRRHPDKTALIFEgtNTHWTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNE-FVGLwLGMAKLGVEAALIN 157
Cdd:cd17655 2 LFEEQAEKTPDHTAVVFE--DQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEmIVGI-LGILKAGGAYLPID 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 158 TNLRRDALRHCLDTSKARALIfgsemasavyeIQAILDPTLtlfcsgswepstvpANTEHLDPLLEDAPKHLPSI---PD 234
Cdd:cd17655 79 PDYPEERIQYILEDSGADILL-----------TQSHLQPPI--------------AFIGLIDLLDEDTIYHEESEnlePV 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 235 KGFTDKLFYIYTSGTTGLPKAAIVVH-----------SRYY-----RMAALVYYGFrmrpDDIVYDclpLYHSagnivgi 298
Cdd:cd17655 134 SKSDDLAYVIYTSGSTGKPKGVMIEHrgvvnlvewanKVIYqgehlRVALFASISF----DASVTE---IFAS------- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 299 gqcVLHGMTVVIRKKFSASR---FWDDCIKYNCTIVqyigELCRYLLNQ-PPREAESRHKVRMAL--GNGLRQSIWTDFS 372
Cdd:cd17655 200 ---LLSGNTLYIVRKETVLDgqaLTQYIRQNRITII----DLTPAHLKLlDAADDSEGLSLKHLIvgGEALSTELAKKII 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 373 SRFHI-PQVAEFYGATEC--NCSLGNFDSQ--------VGACGFNSRIlsfvYpirlvrVNEDTMELirgpdgvcipcQP 441
Cdd:cd17655 273 ELFGTnPTITNAYGPTETtvDASIYQYEPEtdqqvsvpIGKPLGNTRI----Y------ILDQYGRP-----------QP 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 442 -GQPGQLVgriIQQDPLRRfdGYLNQGA-NNKKIASDVFKKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTT 519
Cdd:cd17655 332 vGVAGELY---IGGEGVAR--GYLNRPElTAEKFVDDPFVPGERMYRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELG 406
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 291084711 520 EVEgtlSRLLQMADVAVYGVEV-PGAEGRAGMAAVASPTSNCDLESFAQTLKKELPLYARPIFLRFLPELHKT 591
Cdd:cd17655 407 EIE---ARLLQHPDIKEAVVIArKDEQGQNYLCAYIVSEKELPVAQLREFLARELPDYMIPSYFIKLDEIPLT 476
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
103-536 |
3.51e-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: 81.16 E-value: 3.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 103 TFRQLDDYSSSVANFLQARGLVS-GNVVALFMENrnefvGLWLGMAKLGVEAA-----LINTNLRRDALRHCLDTSKARA 176
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAGGVGpGDRVAVLLER-----SAELVVAILAVLKAgaayvPLDPAYPAERLAFILEDAGARL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 177 LIFGSEMASAVYEIqaildPTLTLFCSGSWEPSTVPANTEhldplledAPKHLPSIPDkgftDKLFYIYTSGTTGLPKAA 256
Cdd:TIGR01733 76 LLTDSALASRLAGL-----VLPVILLDPLELAALDDAPAP--------PPPDAPSGPD----DLAYVIYTSGSTGRPKGV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 257 IVVH----------SRYY------RMAALVYYGFrmrpDDIVYD-CLPLYHsagnivgiGQCVLHGMTVVIRKKFSASRF 319
Cdd:TIGR01733 139 VVTHrslvnllawlARRYgldpddRVLQFASLSF----DASVEEiFGALLA--------GATLVVPPEDEERDDAALLAA 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 320 WDDciKYNCTIVQyigeLCRYLLNQ-PPREAESRHKVRMALGNG--LRQSIWTDFSSRFHIPQVAEFYGATECncslgnf 396
Cdd:TIGR01733 207 LIA--EHPVTVLN----LTPSLLALlAAALPPALASLRLVILGGeaLTPALVDRWRARGPGARLINLYGPTET------- 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 397 dsQVGACGFnsrILSFVYPIRLVRVN-----EDTMELIRGPDGVciPCQPGQPGQLVgriIQQDPLRRfdGYLNQ-GANN 470
Cdd:TIGR01733 274 --TVWSTAT---LVDPDDAPRESPVPigrplANTRLYVLDDDLR--PVPVGVVGELY---IGGPGVAR--GYLNRpELTA 341
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 291084711 471 KKIASDVFKKGDQA--YLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLQMADVAV 536
Cdd:TIGR01733 342 ERFVPDPFAGGDGArlYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
66-604 |
5.57e-16 |
|
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440644 [Multi-domain] Cd Length: 533 Bit Score: 81.35 E-value: 5.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 66 VRRYLQER----KTVPLLFASVVRRHPDKTALIfeGTNTHWTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVG 141
Cdd:COG1021 13 AARYREAGywrgETLGDLLRRRAERHPDRIAVV--DGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 142 LWLGMAKLGVE--AALIntNLRRDALRHCLDTSKARALIFGS--------EMASavyEIQAILdPTL-TLFCSGSwepst 210
Cdd:COG1021 91 VFFALFRAGAIpvFALP--AHRRAEISHFAEQSEAVAYIIPDrhrgfdyrALAR---ELQAEV-PSLrHVLVVGD----- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 211 vPANTEHLDPLLEDAPKHLPSIPDKGftDKLFYIYTSGTTGLPKAAIVVHSRYY----RMAALVyygfRMRPDDiVYDC- 285
Cdd:COG1021 160 -AGEFTSLDALLAAPADLSEPRPDPD--DVAFFQLSGGTTGLPKLIPRTHDDYLysvrASAEIC----GLDADT-VYLAa 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 286 LPLYHSAGNIV-GIGQCVLHGMTVVIRKKFSAsrfwDDCI----KYNCTIVQYIGELCRYLLNQPPRE------------ 348
Cdd:COG1021 232 LPAAHNFPLSSpGVLGVLYAGGTVVLAPDPSP----DTAFplieRERVTVTALVPPLALLWLDAAERSrydlsslrvlqv 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 349 ------AESRHKVRMALGNGLRQSiwtdfssrfhipqvaefYGATE--CNCS-LGnfDS---QVGACGfnsRILSfvyP- 415
Cdd:COG1021 308 ggaklsPELARRVRPALGCTLQQV-----------------FGMAEglVNYTrLD--DPeevILTTQG---RPIS---Pd 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 416 --IRLVrvnedtmelirGPDGVciPCQPGQPGQLVGR---IIQqdplrrfdGYLNQGANNKKiasdVFKKgDQAYLTGDV 490
Cdd:COG1021 363 deVRIV-----------DEDGN--PVPPGEVGELLTRgpyTIR--------GYYRAPEHNAR----AFTP-DGFYRTGDL 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 491 LVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLQMADVAVygVEVPGAE-GRAGMAAV----ASPTSNcDLESF 565
Cdd:COG1021 417 VRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAV--VAMPDEYlGERSCAFVvprgEPLTLA-ELRRF 493
|
570 580 590
....*....|....*....|....*....|....*....
gi 291084711 566 AQTlkKELPLYARPIFLRFLPELHKTGTFKFQKTELRKE 604
Cdd:COG1021 494 LRE--RGLAAFKLPDRLEFVDALPLTAVGKIDKKALRAA 530
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
88-591 |
6.38e-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: 80.49 E-value: 6.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 88 PDKTALIFEGTNthWTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNE-FVGLwLGMAKLGVEAALINTNLRRDALR 166
Cdd:cd17649 1 PDAVALVFGDQS--LSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEmVVAL-LAILKAGGAYVPLDPEYPAERLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 167 HCLDTSKARALIfgsemasavyeiqaildptltlfcsgswepstvpanTEHldplledaPKHLPSIpdkgftdklfyIYT 246
Cdd:cd17649 78 YMLEDSGAGLLL------------------------------------THH--------PRQLAYV-----------IYT 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 247 SGTTGLPKAAIVVH---SRYYRMAALVYygfRMRPDDIVYDCLPLyhsagNIVGIGQCVLH----GMTVVIRKK---FSA 316
Cdd:cd17649 103 SGSTGTPKGVAVSHgplAAHCQATAERY---GLTPGDRELQFASF-----NFDGAHEQLLPplicGACVVLRPDelwASA 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 317 SRFWDDCIKYNCTIVQ----YIGELCRYLLNQPPREAESrhkVRMALGNGlrQSIWTDFSSRFHIPQVAEF--YGATECN 390
Cdd:cd17649 175 DELAEMVRELGVTVLDlppaYLQQLAEEADRTGDGRPPS---LRLYIFGG--EALSPELLRRWLKAPVRLFnaYGPTEAT 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 391 CSLGNFDSQVGA-CGFNSRILSFVYPIRLVRVNedtmelirgpDGVCIPCQPGQPGQLvgrIIQQDPLRRfdGYLNQ-GA 468
Cdd:cd17649 250 VTPLVWKCEAGAaRAGASMPIGRPLGGRSAYIL----------DADLNPVPVGVTGEL---YIGGEGLAR--GYLGRpEL 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 469 NNKKIASDVF-KKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLQMADVAVYGVEVPGAEGR 547
Cdd:cd17649 315 TAERFVPDPFgAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAGGKQL 394
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 291084711 548 AG-MAAVASPTSNCDLESFAQTLKKELPLYARPIFLRFLPELHKT 591
Cdd:cd17649 395 VAyVVLRAAAAQPELRAQLRTALRASLPDYMVPAHLVFLARLPLT 439
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
97-604 |
7.81e-16 |
|
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: 80.59 E-value: 7.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 97 GTNTHWTFRQLDDYSSSVANFL-QARGLVSGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALRHCLDTSKAR 175
Cdd:cd05928 37 GDEVKWSFRELGSLSRKAANVLsGACGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 176 ALIFGSEMASAVYEIqAILDPTLT---LFCSGSWEpstvpaNTEHLDPLLEDA-PKHlpSIPDKGFTDKLFYIYTSGTTG 251
Cdd:cd05928 117 CIVTSDELAPEVDSV-ASECPSLKtklLVSEKSRD------GWLNFKELLNEAsTEH--HCVETGSQEPMAIYFTSGTTG 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 252 LPKAAIVVHSRYYRMAALV-YYGFRMRPDDIVYDClplyHSAGNIVGI----------GQCV-LHGM----TVVIRK--- 312
Cdd:cd05928 188 SPKMAEHSHSSLGLGLKVNgRYWLDLTASDIMWNT----SDTGWIKSAwsslfepwiqGACVfVHHLprfdPLVILKtls 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 313 KFSASRFWDDCIKYNCTIVQyigELCRY--------LLNQPPREAESRHKVRMALGNGLRQSiwtdfssrfhipqvaefY 384
Cdd:cd05928 264 SYPITTFCGAPTVYRMLVQQ---DLSSYkfpslqhcVTGGEPLNPEVLEKWKAQTGLDIYEG-----------------Y 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 385 GATECNCSLGNFDSQVGACGFNSRIlSFVYPIRLVRVNedtmelirgpdGVCIPcqPGQPGQLVGRIIQQDPLRRFDGYL 464
Cdd:cd05928 324 GQTETGLICANFKGMKIKPGSMGKA-SPPYDVQIIDDN-----------GNVLP--PGTEGDIGIRVKPIRPFGLFSGYV 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 465 NqgaNNKKIASDVfkKGDqAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLQMADVAVYGVEVPgA 544
Cdd:cd05928 390 D---NPEKTAATI--RGD-FYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDP-I 462
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 291084711 545 EGRAGMAAV--ASPTSNCDLESFAQTL----KKELPLYARPIFLRFLPELHKTGTFKFQKTELRKE 604
Cdd:cd05928 463 RGEVVKAFVvlAPQFLSHDPEQLTKELqqhvKSVTAPYKYPRKVEFVQELPKTVTGKIQRNELRDK 528
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
88-578 |
9.68e-16 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 80.41 E-value: 9.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 88 PDKTALIFEGTNTHWTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALRH 167
Cdd:PLN02246 37 SDRPCLIDGATGRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 168 CLDTSKARALIFGSEMASAVYEIQAilDPTLTLFCSGSwepstVPANTEHLDPLLEDAPKHLPSI---PDkgftDKLFYI 244
Cdd:PLN02246 117 QAKASGAKLIITQSCYVDKLKGLAE--DDGVTVVTIDD-----PPEGCLHFSELTQADENELPEVeisPD----DVVALP 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 245 YTSGTTGLPKAAIVVH-SRYYRMAALV---YYGFRMRPDDIVYDCLPLYHsagnIVGIGQCVLHGM----TVVIRKKFSA 316
Cdd:PLN02246 186 YSSGTTGLPKGVMLTHkGLVTSVAQQVdgeNPNLYFHSDDVILCVLPMFH----IYSLNSVLLCGLrvgaAILIMPKFEI 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 317 SRFWDDCIKYNCTIVQYIGELCRYLLNQPPREAESRHKVRMALGNG--LRQSIWTDFSSRFHIPQVAEFYGATEC----N 390
Cdd:PLN02246 262 GALLELIQRHKVTIAPFVPPIVLAIAKSPVVEKYDLSSIRMVLSGAapLGKELEDAFRAKLPNAVLGQGYGMTEAgpvlA 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 391 CSLG----NFDSQVGACGfnsrilsfvypiRLVRVNEdtMELIRGPDGVCIPcqPGQPGQLVGRIIQQdplrrFDGYLNq 466
Cdd:PLN02246 342 MCLAfakePFPVKSGSCG------------TVVRNAE--LKIVDPETGASLP--RNQPGEICIRGPQI-----MKGYLN- 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 467 gaNNKKIASDVFKKGdqaYL-TGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLQMADVAVygveVPGAE 545
Cdd:PLN02246 400 --DPEATANTIDKDG---WLhTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAV----VPMKD 470
|
490 500 510
....*....|....*....|....*....|....*..
gi 291084711 546 GRAGMAAVA----SPTSNCDLESFAQTLKKELPLYAR 578
Cdd:PLN02246 471 EVAGEVPVAfvvrSNGSEITEDEIKQFVAKQVVFYKR 507
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
88-591 |
1.19e-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: 79.66 E-value: 1.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 88 PDKTALIFEGTntHWTFRQLDDYSSSVANFLQARGLVSGNVVALFMENrnefvglwlgmaklgveaalintnlrrdalrh 167
Cdd:cd17643 1 PEAVAVVDEDR--RLTYGELDARANRLARTLRAEGVGPGDRVALALPR-------------------------------- 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 168 cldtskaralifGSEMASAVYEIqaildptltLFCSGSWEPSTVPANTEHLDPLLEDA-PKHLPSIPDkgftDKLFYIYT 246
Cdd:cd17643 47 ------------SAELIVALLAI---------LKAGGAYVPIDPAYPVERIAFILADSgPSLLLTDPD----DLAYVIYT 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 247 SGTTGLPKAAIVVHSRYYRMAALVYYGFRMRPDDIVYdclpLYHSAG------NIVGigqCVLHGMTVVIRKKF---SAS 317
Cdd:cd17643 102 SGSTGRPKGVVVSHANVLALFAATQRWFGFNEDDVWT----LFHSYAfdfsvwEIWG---ALLHGGRLVVVPYEvarSPE 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 318 RFWDDCIKYNCTIvqyigelcrylLNQPP-------REAESRHKVRMAL------GNGLRQSIWTDFSSRF--HIPQVAE 382
Cdd:cd17643 175 DFARLLRDEGVTV-----------LNQTPsafyqlvEAADRDGRDPLALryvifgGEALEAAMLRPWAGRFglDRPQLVN 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 383 FYGATEcncslgnfdsqvgACGFNSrilsfVYPIRLVRVNEDTMELIRGP-----------DGVCIPcqPGQPGQLVgri 451
Cdd:cd17643 244 MYGITE-------------TTVHVT-----FRPLDAADLPAAAASPIGRPlpglrvyvldaDGRPVP--PGVVGELY--- 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 452 IQQDPLRRfdGYLNQ-GANNKKIASDVFKK-GDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLL 529
Cdd:cd17643 301 VSGAGVAR--GYLGRpELTAERFVANPFGGpGSRMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHP 378
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 291084711 530 QMADVAVYGVEvpGAEGRAGMAA--VASPTSNCDLESFAQTLKKELPLYARPIFLRFLPELHKT 591
Cdd:cd17643 379 SVRDAAVIVRE--DEPGDTRLVAyvVADDGAAADIAELRALLKELLPDYMVPARYVPLDALPLT 440
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
84-608 |
3.13e-15 |
|
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.
Pssm-ID: 341270 [Multi-domain] Cd Length: 608 Bit Score: 79.14 E-value: 3.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 84 VRRHPDKTALIFEG----TNTHWTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKLGVEAALINTN 159
Cdd:cd05966 63 LKERGDKVAIIWEGdepdQSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFAG 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 160 LRRDALRHCLDTSKARALIF--GSEMASAVYEIQAILDPTLTLfcSGSWEPSTVPANTEH-----------LDPLLEDAP 226
Cdd:cd05966 143 FSAESLADRINDAQCKLVITadGGYRGGKVIPLKEIVDEALEK--CPSVEKVLVVKRTGGevpmtegrdlwWHDLMAKQS 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 227 KHLPSIPDKGfTDKLFYIYTSGTTGLPKAaiVVHSR--YyrmaaLVY------YGFRMRPDDIVY---DClplyhsaGNI 295
Cdd:cd05966 221 PECEPEWMDS-EDPLFILYTSGSTGKPKG--VVHTTggY-----LLYaattfkYVFDYHPDDIYWctaDI-------GWI 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 296 VGIGQCV----LHGMTVVIrkkF-------SASRFWDDCIKYNCTIVqY-----IGELCRYLLNQPPREAESRHKVRMAL 359
Cdd:cd05966 286 TGHSYIVygplANGATTVM---FegtptypDPGRYWDIVEKHKVTIF-YtaptaIRALMKFGDEWVKKHDLSSLRVLGSV 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 360 GNGLRQSIWTDFSS---RFHIPQVAEFYgATE----CNCSL-GNFDSQVGACGFnsrilsfvyP---IRLVRVNEDTMEL 428
Cdd:cd05966 362 GEPINPEAWMWYYEvigKERCPIVDTWW-QTEtggiMITPLpGATPLKPGSATR---------PffgIEPAILDEEGNEV 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 429 IRGPDGV-CIPcQPgQPGQLvgRIIQQDPLRRFDGYlnqgannkkiasdvFKKGDQAYLTGDVLVMDELGYLYFRDRTGD 507
Cdd:cd05966 432 EGEVEGYlVIK-RP-WPGMA--RTIYGDHERYEDTY--------------FSKFPGYYFTGDGARRDEDGYYWITGRVDD 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 508 TFRWKGENVSTTEVEGTLSRLLQMADVAVYGV--EVpgaEGRAGMAAVASptsnCDLESFAQTLKKELPL--------YA 577
Cdd:cd05966 494 VINVSGHRLGTAEVESALVAHPAVAEAAVVGRphDI---KGEAIYAFVTL----KDGEEPSDELRKELRKhvrkeigpIA 566
|
570 580 590
....*....|....*....|....*....|...
gi 291084711 578 RPIFLRFLPELHKTGTFKFQKTELRK--EGFDP 608
Cdd:cd05966 567 TPDKIQFVPGLPKTRSGKIMRRILRKiaAGEEE 599
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
89-539 |
3.58e-15 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 78.78 E-value: 3.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 89 DKTALIFEGTNTH--WTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALR 166
Cdd:PRK04319 59 DKVALRYLDASRKekYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVR 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 167 HCLDTSKARALIFGSEMASAVyeIQAILdPTL-TLFCSGswEPSTVPANTEHLDPLLEDAPKHLPsIPDKGFTDKLFYIY 245
Cdd:PRK04319 139 DRLEDSEAKVLITTPALLERK--PADDL-PSLkHVLLVG--EDVEEGPGTLDFNALMEQASDEFD-IEWTDREDGAILHY 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 246 TSGTTGLPKAAIVVHSRYYRMAALVYYGFRMRPDDIvYDClplyhSA------GNIVGIGQCVLHGMTVVIRK-KFSASR 318
Cdd:PRK04319 213 TSGSTGKPKGVLHVHNAMLQHYQTGKYVLDLHEDDV-YWC-----TAdpgwvtGTSYGIFAPWLNGATNVIDGgRFSPER 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 319 FWDDCIKYNCTiVQYigelcryllnqpprEAESRHKVRMALGNGLRQSIwtDFSSRFHIPQVAE------------FYG- 385
Cdd:PRK04319 287 WYRILEDYKVT-VWY--------------TAPTAIRMLMGAGDDLVKKY--DLSSLRHILSVGEplnpevvrwgmkVFGl 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 386 -------ATE------CNcsLGNFDSQVGACGfnsrilsfvYPI-----RLVRvnedtmeliRGPDGVcipcQPGQPGQL 447
Cdd:PRK04319 350 pihdnwwMTEtggimiAN--YPAMDIKPGSMG---------KPLpgieaAIVD---------DQGNEL----PPNRMGNL 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 448 VgriiqqdpLRR-----FDGYLNQGANNKKiasdVFKKGdqAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVE 522
Cdd:PRK04319 406 A--------IKKgwpsmMRGIWNNPEKYES----YFAGD--WYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVE 471
|
490
....*....|....*..
gi 291084711 523 gtlSRLLQMADVAVYGV 539
Cdd:PRK04319 472 ---SKLMEHPAVAEAGV 485
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
88-601 |
3.81e-15 |
|
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: 78.47 E-value: 3.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 88 PDKTALIfeGTNTHWTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKLGveAALINTNLRRDALRh 167
Cdd:cd12114 1 PDATAVI--CGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAG--AAYVPVDIDQPAAR- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 168 cldtskaRALIFGSEMASAVyeiqaildptltLFCSGSWEPStVPANTEHLDPLLEDAPKHLPSIPDKGFTDKLFYIYTS 247
Cdd:cd12114 76 -------REAILADAGARLV------------LTDGPDAQLD-VAVFDVLILDLDALAAPAPPPPVDVAPDDLAYVIFTS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 248 GTTGLPKAAIVVHSRYYRMAALVYYGFRMRPDDIVYDCLPLYH--SAGNIVGigqcVLH-GMTVVI----RKKFSASrfW 320
Cdd:cd12114 136 GSTGTPKGVMISHRAALNTILDINRRFAVGPDDRVLALSSLSFdlSVYDIFG----ALSaGATLVLpdeaRRRDPAH--W 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 321 DDCI-KYNCTIVQYIGELCRYLLNQPPREAESRHKVRMALGNG------LRQSIWTDFSSrfhiPQVAEFYGATEcncsl 393
Cdd:cd12114 210 AELIeRHGVTLWNSVPALLEMLLDVLEAAQALLPSLRLVLLSGdwipldLPARLRALAPD----ARLISLGGATE----- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 394 gnfdsqvGAcgfnsrILSFVYPIRlvRVNEDT------MEL------IRGPDGVciPCQPGQPGQLV--GRIIQQdplrr 459
Cdd:cd12114 281 -------AS------IWSIYHPID--EVPPDWrsipygRPLanqryrVLDPRGR--DCPDWVPGELWigGRGVAL----- 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 460 fdGYLNQGAnnKKIASDV--------FKKGDQAYLTGDvlvmdelGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLQM 531
Cdd:cd12114 339 --GYLGDPE--LTAARFVthpdgerlYRTGDLGRYRPD-------GTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGV 407
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 291084711 532 ADVAVygVEVPGAEGRAgMAAVASPTSNC---DLESFAQTLKKELPLYARPIFLRFLPELHKTGTFKFQKTEL 601
Cdd:cd12114 408 ARAVV--VVLGDPGGKR-LAAFVVPDNDGtpiAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
76-604 |
7.21e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 77.68 E-value: 7.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 76 VPLLFASVVRR----HPDKTALIFEGTntHWTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKLGv 151
Cdd:PRK08162 16 VPLTPLSFLERaaevYPDRPAVIHGDR--RRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAG- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 152 eaALINT-NLRRDA------LRHCldtsKARALIFGSEMASAVYEIQAILD---PTLTLFCSGSWEPSTVPANTEHLDPL 221
Cdd:PRK08162 93 --AVLNTlNTRLDAasiafmLRHG----EAKVLIVDTEFAEVAREALALLPgpkPLVIDVDDPEYPGGRFIGALDYEAFL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 222 LEDAPKHLPSIPDKGFtDKLFYIYTSGTTGLPKAaIVVHSR-YYRMAA--LVYYGFRMRPddiVYD-CLPLYHSagNivg 297
Cdd:PRK08162 167 ASGDPDFAWTLPADEW-DAIALNYTSGTTGNPKG-VVYHHRgAYLNALsnILAWGMPKHP---VYLwTLPMFHC--N--- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 298 iGQC------VLHGMTVVIRKkFSASRFWDDCIKYNCT------IVQYIgelcryLLNQPPREAES-RHKVR-MALGNGL 363
Cdd:PRK08162 237 -GWCfpwtvaARAGTNVCLRK-VDPKLIFDLIREHGVThycgapIVLSA------LINAPAEWRAGiDHPVHaMVAGAAP 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 364 RQSIWTDFSSR-FHIPQVaefYGATEcncslgnfdsqvgacgfnsrilsfVY-PIRLVRVNEDTMEL-------IRGPDG 434
Cdd:PRK08162 309 PAAVIAKMEEIgFDLTHV---YGLTE------------------------TYgPATVCAWQPEWDALplderaqLKARQG 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 435 VCIPCQPG---------QP----GQLVGRIIqqdplrrF------DGYLNqganNKKIASDVFKKGdqAYLTGDVLVMDE 495
Cdd:PRK08162 362 VRYPLQEGvtvldpdtmQPvpadGETIGEIM-------FrgnivmKGYLK----NPKATEEAFAGG--WFHTGDLAVLHP 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 496 LGYLYFRDRTGDTFRWKGENVSTTEVEGTLSR---LLQMADVAV----YGvEVPGA--EGRAGMAAVASptsncDLESFA 566
Cdd:PRK08162 429 DGYIKIKDRSKDIIISGGENISSIEVEDVLYRhpaVLVAAVVAKpdpkWG-EVPCAfvELKDGASATEE-----EIIAHC 502
|
570 580 590
....*....|....*....|....*....|....*...
gi 291084711 567 qtlKKELPLYARPIFLRFlPELHKTGTFKFQKTELRKE 604
Cdd:PRK08162 503 ---REHLAGFKVPKAVVF-GELPKTSTGKIQKFVLREQ 536
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
76-540 |
8.43e-15 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 77.57 E-value: 8.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 76 VPLLFASvvRRHPDKTALIFEGTNTHWTFRQLDDYSSSVANFLQAR-GLVSGNVVALFMENRNEFVGLWLGMAKLGVEAA 154
Cdd:PLN02574 43 VSFIFSH--HNHNGDTALIDSSTGFSISYSELQPLVKSMAAGLYHVmGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 155 LINTNLRRDALR-HCLDTSKAraLIFGSemASAVYEIQAILDPTLTlfcsgswepstVPANTEHLDPLLEDAPKHLPSIP 233
Cdd:PLN02574 121 TMNPSSSLGEIKkRVVDCSVG--LAFTS--PENVEKLSPLGVPVIG-----------VPENYDFDSKRIEFPKFYELIKE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 234 DKGFT--------DKLFYIYTSGTTGLPKAAIVVHSRYYRMAALvYYGFRMR------PDDIVYDCLPLYHSAG-NIVGI 298
Cdd:PLN02574 186 DFDFVpkpvikqdDVAAIMYSSGTTGASKGVVLTHRNLIAMVEL-FVRFEASqyeypgSDNVYLAALPMFHIYGlSLFVV 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 299 GQCVLhGMTVVIRKKFSASRFWDDCIKYNCTIVQYIgelcryllnqPPREAESRHKVRMALGNGLR-------------Q 365
Cdd:PLN02574 265 GLLSL-GSTIVVMRRFDASDMVKVIDRFKVTHFPVV----------PPILMALTKKAKGVCGEVLKslkqvscgaaplsG 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 366 SIWTDFSSRFHIPQVAEFYGATEcncslgnfDSQVGACGFNSRILSFVYPIRLVRVNEDTmELIRGPDGVCIPcqPGQPG 445
Cdd:PLN02574 334 KFIQDFVQTLPHVDFIQGYGMTE--------STAVGTRGFNTEKLSKYSSVGLLAPNMQA-KVVDWSTGCLLP--PGNCG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 446 QLvgrIIQQDPLRRfdGYLNqgaNNKKIASDVFKKGdqaYL-TGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGT 524
Cdd:PLN02574 403 EL---WIQGPGVMK--GYLN---NPKATQSTIDKDG---WLrTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAV 471
|
490
....*....|....*.
gi 291084711 525 LSRLLQMADVAVYGVE 540
Cdd:PLN02574 472 LISHPEIIDAAVTAVP 487
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
70-602 |
1.37e-14 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 76.84 E-value: 1.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 70 LQERKTVPLLFASVVRRHPDKTALIFEGTNThwTFRQLDDYSSSVANFLQAR-GLVSGNVVALFMENRNEFVGLWLGMAK 148
Cdd:PRK08751 21 LEQFRTVAEVFATSVAKFADRPAYHSFGKTI--TYREADQLVEQFAAYLLGElQLKKGDRVALMMPNCLQYPIATFGVLR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 149 LGVEAALINTNLRRDALRHCLDTSKARALIFGSEMASAVYeiQAILD-PTLTLFCSGSWEPSTVPANT------EHLDPL 221
Cdd:PRK08751 99 AGLTVVNVNPLYTPRELKHQLIDSGASVLVVIDNFGTTVQ--QVIADtPVKQVITTGLGDMLGFPKAAlvnfvvKYVKKL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 222 LED---------------APKH-LPSI---PDkgftDKLFYIYTSGTTGLPKAAIVVHSryyRMAA--------LVYYGF 274
Cdd:PRK08751 177 VPEyringairfrealalGRKHsMPTLqiePD----DIAFLQYTGGTTGVAKGAMLTHR---NLVAnmqqahqwLAGTGK 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 275 RMRPDDIVYDCLPLYH----SAGNIV--GIGQCvlhgmTVVIRKKFSASRFWDDCIKYNCTIVQYIGELCRYLLNQPPRE 348
Cdd:PRK08751 250 LEEGCEVVITALPLYHifalTANGLVfmKIGGC-----NHLISNPRDMPGFVKELKKTRFTAFTGVNTLFNGLLNTPGFD 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 349 AESRHKVRMALGNGL--RQSIWTDFSSRFHIPQVaEFYGATEcncslgnfdSQVGACgfnsrilsfVYPIRLVRVNEDTM 426
Cdd:PRK08751 325 QIDFSSLKMTLGGGMavQRSVAERWKQVTGLTLV-EAYGLTE---------TSPAAC---------INPLTLKEYNGSIG 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 427 ELIRGPDgVCIPCQPGQ--PGQLVGRIIQQDPlRRFDGYLNQGANNKKIASdvfkkGDQAYLTGDVLVMDELGYLYFRDR 504
Cdd:PRK08751 386 LPIPSTD-ACIKDDAGTvlAIGEIGELCIKGP-QVMKGYWKRPEETAKVMD-----ADGWLHTGDIARMDEQGFVYIVDR 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 505 TGDTFRWKGENVSTTEVEGTLSRLLQMADVAVYGveVPGAE-GRAGMAAVASPTSNCDLESFAQTLKKELPLYARPIFLR 583
Cdd:PRK08751 459 KKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVG--VPDEKsGEIVKVVIVKKDPALTAEDVKAHARANLTGYKQPRIIE 536
|
570
....*....|....*....
gi 291084711 584 FLPELHKTGTFKFQKTELR 602
Cdd:PRK08751 537 FRKELPKTNVGKILRRELR 555
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
102-590 |
2.26e-14 |
|
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: 75.71 E-value: 2.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 102 WTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALRHCLDTSKARALIfgs 181
Cdd:cd05907 6 ITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALF--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 182 emasavyeiqaildptltlfcsgswepstvpanTEHLDplledapkHLPSIpdkgftdklfyIYTSGTTGLPKAAIVVHS 261
Cdd:cd05907 83 ---------------------------------VEDPD--------DLATI-----------IYTSGTTGRPKGVMLSHR 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 262 RYYRMAALVYYGFRMRPDDIVYDCLPLYHSAGNIVGIGQCVLHGMTVVIrkkFSASRfwddcikyncTIVQYIGELCRYL 341
Cdd:cd05907 111 NILSNALALAERLPATEGDRHLSFLPLAHVFERRAGLYVPLLAGARIYF---ASSAE----------TLLDDLSEVRPTV 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 342 LNQPPREAE-SRHKVRMALGNGLRQSI--W-----------------TDFSSRFH---IPqVAEFYGATEC----NCSLG 394
Cdd:cd05907 178 FLAVPRVWEkVYAAIKVKAVPGLKRKLfdLavggrlrfaasggaplpAELLHFFRalgIP-VYEGYGLTETsavvTLNPP 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 395 NfDSQVGACGfnsrilSFVYPIRlVRVNEDTMELIRGPdGVcipcqpgqpgqlvgriiqqdplrrFDGYLNQGAnnkkiA 474
Cdd:cd05907 257 G-DNRIGTVG------KPLPGVE-VRIADDGEILVRGP-NV------------------------MLGYYKNPE-----A 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 475 SDVFKKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRW-KGENVSTTEVEGTLSRLLQMADVAVYGvevpgaEGRAGMAAV 553
Cdd:cd05907 299 TAEALDADGWLHTGDLGEIDEDGFLHITGRKKDLIITsGGKNISPEPIENALKASPLISQAVVIG------DGRPFLVAL 372
|
490 500 510
....*....|....*....|....*....|....*..
gi 291084711 554 ASPtsncDLESFAQTLKKELPLYARPIFLRFLPELHK 590
Cdd:cd05907 373 IVP----DPEALEAWAEEHGIAYTDVAELAANPAVRA 405
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
244-603 |
2.74e-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: 74.29 E-value: 2.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 244 IYTSGTTGLPKAaiVVHSRY----YRMAALVYYGFRMRPDDIVydCLPLYHSAGNIVgIGQCVLHGMTVVIRKKFSASRf 319
Cdd:cd17630 6 ILTSGSTGTPKA--VVHTAAnllaSAAGLHSRLGFGGGDSWLL--SLPLYHVGGLAI-LVRSLLAGAELVLLERNQALA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 320 wDDCIKYNCTIVQYIGELCRYLLnQPPREAESRHKVRMALGNGlrQSIWTDFSSRF---HIPqVAEFYGATEcncslgnF 396
Cdd:cd17630 80 -EDLAPPGVTHVSLVPTQLQRLL-DSGQGPAALKSLRAVLLGG--APIPPELLERAadrGIP-LYTTYGMTE-------T 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 397 DSQVGACGFNSRILSFVYPI---RLVRVNEDTMELIRGPdgvcipcqpgqpgqlvgriiqqdplRRFDGYLNQGANNKKI 473
Cdd:cd17630 148 ASQVATKRPDGFGRGGVGVLlpgRELRIVEDGEIWVGGA-------------------------SLAMGYLRGQLVPEFN 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 474 ASDVFKKGDQAYLTGDvlvmdelGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLQMADVAVYGVevpgAEGRAGMAAV 553
Cdd:cd17630 203 EDGWFTTKDLGELHAD-------GRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGV----PDEELGQRPV 271
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 291084711 554 ASPTSNC--DLESFAQTLKKELPLYARPIFLRFLPELHKTGTFKFQKTELRK 603
Cdd:cd17630 272 AVIVGRGpaDPAELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRA 323
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
70-602 |
3.19e-14 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 75.83 E-value: 3.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 70 LQERKTVPLLFASVVRR----HPDKTALIFegTNTHWTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLG 145
Cdd:PLN03102 6 LCEANNVPLTPITFLKRasecYPNRTSIIY--GKTRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 146 MAKLGVEAALINTNLRRDALRHCLDTSKARALIFGSEMASAVYEIQAIL-----DPTLTLFCSGSWEPSTVPANTEHLDP 220
Cdd:PLN03102 84 VPMAGAVLNPINTRLDATSIAAILRHAKPKILFVDRSFEPLAREVLHLLssedsNLNLPVIFIHEIDFPKRPSSEELDYE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 221 LLEDAPKHLPSIPDKGFT-----DKLFYIYTSGTTGLPKAAIVVHSRYYRMAALVYYGFRMRPDDIVYDCLPLYHSAGNI 295
Cdd:PLN03102 164 CLIQRGEPTPSLVARMFRiqdehDPISLNYTSGTTADPKGVVISHRGAYLSTLSAIIGWEMGTCPVYLWTLPMFHCNGWT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 296 VGIGQCVLHGMTVVIRKkFSASRFWDDCIKYNCTIVQYIGELCRYLL-----NQPPREAesrhKVRMALGNGLRQSIWTD 370
Cdd:PLN03102 244 FTWGTAARGGTSVCMRH-VTAPEIYKNIEMHNVTHMCCVPTVFNILLkgnslDLSPRSG----PVHVLTGGSPPPAALVK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 371 FSSRFHIpQVAEFYGATEcncslgnfdsqvgACGfnsRILSFVYPIRLVRVNEDTMELIRGPDGVCI-----------PC 439
Cdd:PLN03102 319 KVQRLGF-QVMHAYGLTE-------------ATG---PVLFCEWQDEWNRLPENQQMELKARQGVSIlgladvdvknkET 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 440 QPGQP--GQLVGRIIQQDPLRrFDGYLNqganNKKIASDVFKKGdqaYL-TGDVLVMDELGYLYFRDRTGDTFRWKGENV 516
Cdd:PLN03102 382 QESVPrdGKTMGEIVIKGSSI-MKGYLK----NPKATSEAFKHG---WLnTGDVGVIHPDGHVEIKDRSKDIIISGGENI 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 517 STTEVEGTLSRLLQMADVAVYGVEVP--GAEGRAGMAAVASPTSNCDLESFAQTLKKELPLYAR---PIFL-----RFLP 586
Cdd:PLN03102 454 SSVEVENVLYKYPKVLETAVVAMPHPtwGETPCAFVVLEKGETTKEDRVDKLVTRERDLIEYCRenlPHFMcprkvVFLQ 533
|
570
....*....|....*.
gi 291084711 587 ELHKTGTFKFQKTELR 602
Cdd:PLN03102 534 ELPKNGNGKILKPKLR 549
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
88-601 |
3.43e-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: 75.20 E-value: 3.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 88 PDKTALIFEgtNTHWTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALRH 167
Cdd:cd17656 2 PDAVAVVFE--NQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 168 CLDTSKARALIFGSEMASAV---YEIQAILDPTLTlfcSGSWEPSTVPANTEHLdplledapkhlpsipdkgftdkLFYI 244
Cdd:cd17656 80 IMLDSGVRVVLTQRHLKSKLsfnKSTILLEDPSIS---QEDTSNIDYINNSDDL----------------------LYII 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 245 YTSGTTGLPKAAIVVHSryyRMAALVYYGFRMRPDDIVYDCLPL--------YHSagnivgIGQCVLHGMTV-VIRK--K 313
Cdd:cd17656 135 YTSGTTGKPKGVQLEHK---NMVNLLHFEREKTNINFSDKVLQFatcsfdvcYQE------IFSTLLSGGTLyIIREetK 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 314 FSASRFWDDCIKYNCTIVQYIGELCRYLLNQppREAESR--HKVRMALGNGLRQSIWTDFSSRFHIPQVA--EFYGATEC 389
Cdd:cd17656 206 RDVEQLFDLVKRHNIEVVFLPVAFLKFIFSE--REFINRfpTCVKHIITAGEQLVITNEFKEMLHEHNVHlhNHYGPSET 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 390 NCslgnfdsqVGACGFNSRILSFVY-PIRLVRVNEDTmeLIRGPDGVCIPCqpGQPGQLVgriIQQDPLRRfdGYLN-QG 467
Cdd:cd17656 284 HV--------VTTYTINPEAEIPELpPIGKPISNTWI--YILDQEQQLQPQ--GIVGELY---ISGASVAR--GYLNrQE 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 468 ANNKKIASDVFKKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRL--LQMADVAVYGvevpGAE 545
Cdd:cd17656 347 LTAEKFFPDPFDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHpgVSEAVVLDKA----DDK 422
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 291084711 546 GRAGMAAVASPTSNCDLESFAQTLKKELPLYARPIFLRFLPELHKTGTFKFQKTEL 601
Cdd:cd17656 423 GEKYLCAYFVMEQELNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
88-544 |
8.34e-14 |
|
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: 74.49 E-value: 8.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 88 PDKTALIFEGTNTHWTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALRH 167
Cdd:cd17642 31 PGTIAFTDAHTGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDH 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 168 CLDTSKARaLIFGSE--------MASAVYEIQAILDPTLTLFCSGSWEPSTVpaNTEHLDPLLeDAPKHLPSIPDKGfTD 239
Cdd:cd17642 111 SLNISKPT-IVFCSKkglqkvlnVQKKLKIIKTIIILDSKEDYKGYQCLYTF--ITQNLPPGF-NEYDFKPPSFDRD-EQ 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 240 KLFYIYTSGTTGLPKAAIVVHsryyrMAALV--------YYGFRMRPDDIVYDCLPLYHSAGNIVGIGQCVLhGMTVVIR 311
Cdd:cd17642 186 VALIMNSSGSTGLPKGVQLTH-----KNIVArfshardpIFGNQIIPDTAILTVIPFHHGFGMFTTLGYLIC-GFRVVLM 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 312 KKFSASRFWDDCIKYNCTIVQYIGELCRYLLNQPPREA-ESRHKVRMALGNG-LRQSIWTDFSSRFHIPQVAEFYGATEC 389
Cdd:cd17642 260 YKFEEELFLRSLQDYKVQSALLVPTLFAFFAKSTLVDKyDLSNLHEIASGGApLSKEVGEAVAKRFKLPGIRQGYGLTET 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 390 NCSL---GNFDSQVGACGfnsRILSFVYpirlVRVNEDTMELIRGPDgvcipcqpgQPGQLV--GRIIQQdplrrfdGYL 464
Cdd:cd17642 340 TSAIlitPEGDDKPGAVG---KVVPFFY----AKVVDLDTGKTLGPN---------ERGELCvkGPMIMK-------GYV 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 465 NqgaNNKKIASDVFKKGdqaYL-TGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLQMADVAVYGV---- 539
Cdd:cd17642 397 N---NPEATKALIDKDG---WLhSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIpded 470
|
....*..
gi 291084711 540 --EVPGA 544
Cdd:cd17642 471 agELPAA 477
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
77-552 |
1.11e-13 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 74.82 E-value: 1.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 77 PLLFASVVRRH----PDKTALIF----EGTNTHWTFRQLDDYSSSVANFLQARGLVSGNVVALFmENRNEFVGLWLGMAK 148
Cdd:PRK05691 8 PLTLVQALQRRaaqtPDRLALRFladdPGEGVVLSYRDLDLRARTIAAALQARASFGDRAVLLF-PSGPDYVAAFFGCLY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 149 LGVEA--ALINTNLRRDALRHCL---DTSKARALIFGSEMASAVYEIQAILDPTL-TLFCsgswepstvpanTEHLDPLL 222
Cdd:PRK05691 87 AGVIAvpAYPPESARRHHQERLLsiiADAEPRLLLTVADLRDSLLQMEELAAANApELLC------------VDTLDPAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 223 EDAPKHlPSIPDKgftDKLFYIYTSGTTGLPKAAIVVHSRYYRMAALVYYGFRMR--PDDIVYDCLPLYHSAGNIVGIGQ 300
Cdd:PRK05691 155 AEAWQE-PALQPD---DIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGIDlnPDDVIVSWLPLYHDMGLIGGLLQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 301 CVLHGMTVVIrkkFSASRFWDDCIKYNCTIVQYIG----------ELCRyllnqpPREAESrhkvrmALgNGLRQSIW-T 369
Cdd:PRK05691 231 PIFSGVPCVL---MSPAYFLERPLRWLEAISEYGGtisggpdfayRLCS------ERVSES------AL-ERLDLSRWrV 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 370 DFSSRFHIPQVaefygatecncSLGNFDSQVGACGFNSRILSFVY----------------PIRLVRVNEDTMELIRGPD 433
Cdd:PRK05691 295 AYSGSEPIRQD-----------SLERFAEKFAACGFDPDSFFASYglaeatlfvsggrrgqGIPALELDAEALARNRAEP 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 434 G---VCIPCQPGQPGQLVgRIIQQDPLRRFD----------------GYLnqgaNNKKIASDVFKKGD-QAYL-TGDVLV 492
Cdd:PRK05691 364 GtgsVLMSCGRSQPGHAV-LIVDPQSLEVLGdnrvgeiwasgpsiahGYW----RNPEASAKTFVEHDgRTWLrTGDLGF 438
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 291084711 493 MDElGYLYFRDRTGDTFRWKGENVSTTEVEGTLSR---LLQMADVAVYGVEVPGAEGrAGMAA 552
Cdd:PRK05691 439 LRD-GELFVTGRLKDMLIVRGHNLYPQDIEKTVEReveVVRKGRVAAFAVNHQGEEG-IGIAA 499
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
89-614 |
1.36e-13 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 74.16 E-value: 1.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 89 DKTALIFEGT----NTHWTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRDA 164
Cdd:PLN02654 104 DKIAIYWEGNepgfDASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAES 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 165 LRHCLDTSKARALIF--GSEMASAVYEIQAILDPTLTL---------FCSGSWEPSTVPANT----EHLDPLLEDAPKHL 229
Cdd:PLN02654 184 LAQRIVDCKPKVVITcnAVKRGPKTINLKDIVDAALDEsakngvsvgICLTYENQLAMKREDtkwqEGRDVWWQDVVPNY 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 230 PSIPDKGFTDK---LFYIYTSGTTGLPKAAIVVHSRYYRMAALVY-YGFRMRPDDIVY---DClplyhsaGNIVGIGQC- 301
Cdd:PLN02654 264 PTKCEVEWVDAedpLFLLYTSGSTGKPKGVLHTTGGYMVYTATTFkYAFDYKPTDVYWctaDC-------GWITGHSYVt 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 302 ---VLHGMTVVIRKKF----SASRFWDDCIKYNCTIVQYIGELCRYLL--NQPPREAESRHKVRM--ALGNGLRQSIWTD 370
Cdd:PLN02654 337 ygpMLNGATVLVFEGApnypDSGRCWDIVDKYKVTIFYTAPTLVRSLMrdGDEYVTRHSRKSLRVlgSVGEPINPSAWRW 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 371 FssrFHIpqvaefYGATECNCSLGNFDSQVGacGFNSRILSFVYP------------IRLVRVNEDTMELirgpDGVC-- 436
Cdd:PLN02654 417 F---FNV------VGDSRCPISDTWWQTETG--GFMITPLPGAWPqkpgsatfpffgVQPVIVDEKGKEI----EGECsg 481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 437 -IPCQPGQPGQLvgRIIQQDPLRRFDGYlnqgannkkiasdvFKKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGEN 515
Cdd:PLN02654 482 yLCVKKSWPGAF--RTLYGDHERYETTY--------------FKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHR 545
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 516 VSTTEVEGTLSRLLQMADVAVYGV--EVPGAEGRAGMAAVASPTSNCDL-ESFAQTLKKELPLYARPIFLRFLPELHKTG 592
Cdd:PLN02654 546 IGTAEVESALVSHPQCAEAAVVGIehEVKGQGIYAFVTLVEGVPYSEELrKSLILTVRNQIGAFAAPDKIHWAPGLPKTR 625
|
570 580
....*....|....*....|....*....
gi 291084711 593 TFKFQKTELRK-------EGFDPSVVKDP 614
Cdd:PLN02654 626 SGKIMRRILRKiasrqldELGDTSTLADP 654
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
84-588 |
1.55e-13 |
|
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341267 [Multi-domain] Cd Length: 449 Bit Score: 73.05 E-value: 1.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 84 VRRHPDKTALIFEGTNthWTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKLGveAALINTNLrrd 163
Cdd:cd05945 1 AAANPDRPAVVEGGRT--LTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAG--HAYVPLDA--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 164 alrhclDTSKARalifgsemasaVYEIQAILDPTLtLFCSGswepstvpantehldplledapkhlpsipdkgftDKLFY 243
Cdd:cd05945 74 ------SSPAER-----------IREILDAAKPAL-LIADG----------------------------------DDNAY 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 244 I-YTSGTTGLPKAaiVVHSRyyrmAALVYYGFRMRPD-----DIVYDCLPLYHSAGNIVGIGQCVLHGMTVVIRKKfsas 317
Cdd:cd05945 102 IiFTSGSTGRPKG--VQISH----DNLVSFTNWMLSDfplgpGDVFLNQAPFSFDLSVMDLYPALASGATLVPVPR---- 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 318 rfwddcikyncTIVQYIGELCRYLlnqppreaeSRHKV----------RMALGNG---------LRQSIWT--------- 369
Cdd:cd05945 172 -----------DATADPKQLFRFL---------AEHGItvwvstpsfaAMCLLSPtftpeslpsLRHFLFCgevlphkta 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 370 -DFSSRFhiPQVAEF--YGATECN--CSLGNFDSQVGACgfNSRIlsfvyPIRlvRVNEDTMELIRGPDGVCIPcqPGQP 444
Cdd:cd05945 232 rALQQRF--PDARIYntYGPTEATvaVTYIEVTPEVLDG--YDRL-----PIG--YAKPGAKLVILDEDGRPVP--PGEK 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 445 GQLVGRIIQqdplrRFDGYLNqgaNNKKIASDVFK-KGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEG 523
Cdd:cd05945 299 GELVISGPS-----VSKGYLN---NPEKTAAAFFPdEGQRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEA 370
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 291084711 524 TLSRLLQMADVAVygVEVPGAEGRAGMAAVASPTSNCDLE---SFAQTLKKELPLYARPIFLRFLPEL 588
Cdd:cd05945 371 ALRQVPGVKEAVV--VPKYKGEKVTELIAFVVPKPGAEAGltkAIKAELAERLPPYMIPRRFVYLDEL 436
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
72-604 |
5.09e-13 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 71.93 E-value: 5.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 72 ERKTVPLLFASVVRRHPDKTALIFEGTNTHWTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLG-MAKLG 150
Cdd:PLN02330 26 DKLTLPDFVLQDAELYADKVAFVEAVTGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGiMAAGG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 151 VEAALINTNLRRDaLRHCLDTSKARALIfgseMASAVYE-IQAILDPTLTLfcsgswePSTVPANTEHLDPLLEDAPKHL 229
Cdd:PLN02330 106 VFSGANPTALESE-IKKQAEAAGAKLIV----TNDTNYGkVKGLGLPVIVL-------GEEKIEGAVNWKELLEAADRAG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 230 PSIPDKGF--TDKLFYIYTSGTTGLPKAAIVVHSRYyrMAALVYYGFRMRPDDI----VYDCLPLYHSAGnIVGIGQCVL 303
Cdd:PLN02330 174 DTSDNEEIlqTDLCALPFSSGTTGISKGVMLTHRNL--VANLCSSLFSVGPEMIgqvvTLGLIPFFHIYG-ITGICCATL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 304 HGM-TVVIRKKFSASRFWDDCIKYNCTIVQYIGELCRYLLNQPPREAESRHKVR----MALGNGLRQSIWTDFSSRFHIP 378
Cdd:PLN02330 251 RNKgKVVVMSRFELRTFLNALITQEVSFAPIVPPIILNLVKNPIVEEFDLSKLKlqaiMTAAAPLAPELLTAFEAKFPGV 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 379 QVAEFYGATECNC---SLGNFDSQVGACGFNSriLSFVYPIRLVR-VNEDTmelirgpdGVCIPcqPGQPGQLVGR---I 451
Cdd:PLN02330 331 QVQEAYGLTEHSCitlTHGDPEKGHGIAKKNS--VGFILPNLEVKfIDPDT--------GRSLP--KNTPGELCVRsqcV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 452 IQqdplrrfdGYLNqganNKKIASDVFKKgdQAYL-TGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLQ 530
Cdd:PLN02330 399 MQ--------GYYN----NKEETDRTIDE--DGWLhTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPS 464
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 291084711 531 MADVAVygVEVPGAEGRAGMAA--VASPTSNCDLESFAQTLKKELPLYARPIFLRFLPELHKTGTFKFQKTELRKE 604
Cdd:PLN02330 465 VEDAAV--VPLPDEEAGEIPAAcvVINPKAKESEEDILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLKEK 538
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
239-591 |
7.80e-13 |
|
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341292 [Multi-domain] Cd Length: 333 Bit Score: 69.99 E-value: 7.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 239 DKLFYIYTSGTTGLPKAAIVVHSRYYRMAALVYYGFRMRPDDIVYDCLPLYHSAGniVGIGQCVLH--GMTVVIRKkFSA 316
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPLFHIAG--LNLALATFHagGANVVMEK-FDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 317 SRFWDDCIKYNCTivqYIGE----LCRYL--LNQPPREAESrhkVRMALGNGLRQSIwtdfsSRFHIPQVAEF---YGAT 387
Cdd:cd17637 78 AEALELIEEEKVT---LMGSfppiLSNLLdaAEKSGVDLSS---LRHVLGLDAPETI-----QRFEETTGATFwslYGQT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 388 ECNC--SLGNFDSQVGACGfnsRILsfvyPIRLVR-VNEDTMELirgPDGVcipcqpgqpgqlVGRIIQQDPLRrFDGYL 464
Cdd:cd17637 147 ETSGlvTLSPYRERPGSAG---RPG----PLVRVRiVDDNDRPV---PAGE------------TGEIVVRGPLV-FQGYW 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 465 NQGANNKKiasdVFKKGdqAYLTGDVLVMDELGYLYFRDRTGDTFRWK--GENVSTTEVEGTLSRLLQMADVAVYGveVP 542
Cdd:cd17637 204 NLPELTAY----TFRNG--WHHTGDLGRFDEDGYLWYAGRKPEKELIKpgGENVYPAEVEKVILEHPAIAEVCVIG--VP 275
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 291084711 543 GAEGRAGMAAV------ASPTSNcDLESFAQTLkkeLPLYARPIFLRFLPELHKT 591
Cdd:cd17637 276 DPKWGEGIKAVcvlkpgATLTAD-ELIEFVGSR---IARYKKPRYVVFVEALPKT 326
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
102-573 |
8.62e-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: 8.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 102 WTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFV----GLWLGmaklGVEAALINTNLRRDALRHCLDTSKARAL 177
Cdd:cd05932 7 FTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFitdlAIWMA----GHISVPLYPTLNPDTIRYVLEHSESKAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 178 IFG-----SEMASAVYE--IQAILDPTLTLFCSGSWEpstvpaNTEHLDPLLEDAPKHLPsipdkgftDKLF-YIYTSGT 249
Cdd:cd05932 83 FVGklddwKAMAPGVPEglISISLPPPSAANCQYQWD------DLIAQHPPLEERPTRFP--------EQLAtLIYTSGT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 250 TGLPKAAIVVHSRYYRMAALVYYGFRMRPDDIVYDCLPLYHSAGNIVGIGQCVLHGMTV------------VIRKK---- 313
Cdd:cd05932 149 TGQPKGVMLTFGSFAWAAQAGIEHIGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVafaesldtfvedVQRARptlf 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 314 FSASRFWddcIKYNCTIVQYIG--ELCRyLLNQPPREAESRHKVRMALG-NGLR---------QSIWTDFSSRFHIPqVA 381
Cdd:cd05932 229 FSVPRLW---TKFQQGVQDKIPqqKLNL-LLKIPVVNSLVKRKVLKGLGlDQCRlagcgsapvPPALLEWYRSLGLN-IL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 382 EFYGATEcNCSLGN----FDSQVGACGFNsrilsfvYPIRLVRVNEDTMELIRgpdgvcipcqpgQPGQLVGRiiqqdpl 457
Cdd:cd05932 304 EAYGMTE-NFAYSHlnypGRDKIGTVGNA-------GPGVEVRISEDGEILVR------------SPALMMGY------- 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 458 rrfdgYLNQGANNKKIASDVFKKgdqaylTGDVLVMDELGYLYFRDRTGDTFRW-KGENVSTTEVEGTLSRLLQMADVAV 536
Cdd:cd05932 357 -----YKDPEATAEAFTADGFLR------TGDKGELDADGNLTITGRVKDIFKTsKGKYVAPAPIENKLAEHDRVEMVCV 425
|
490 500 510
....*....|....*....|....*....|....*...
gi 291084711 537 YGVEVPGAEGRAGMAAVASPTS-NCDLESFAQTLKKEL 573
Cdd:cd05932 426 IGSGLPAPLALVVLSEEARLRAdAFARAELEASLRAHL 463
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
103-539 |
9.37e-13 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 70.98 E-value: 9.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 103 TFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALRHCLDTSKARALIFGSE 182
Cdd:PLN02860 34 TGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWSFEEAKSAMLLVRPVMLVTDET 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 183 MASAVYEIQAILDPTL---TLFCSGSWEPSTVPANTEHLDPLLEDAPKhlPSIPDKGFT--DKLFYIYTSGTTGLPKAAI 257
Cdd:PLN02860 114 CSSWYEELQNDRLPSLmwqVFLESPSSSVFIFLNSFLTTEMLKQRALG--TTELDYAWApdDAVLICFTSGTTGRPKGVT 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 258 VVHSRYYRMA----ALVYYGfrmrPDDIVYDCLPLYH-----SAGNIVGIGQCvlHgmtvVIRKKFSASRFWDdCIKYNC 328
Cdd:PLN02860 192 ISHSALIVQSlakiAIVGYG----EDDVYLHTAPLCHigglsSALAMLMVGAC--H----VLLPKFDAKAALQ-AIKQHN 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 329 -----TIVQYIGELCRYllNQPPREAESRHKVRMAL--GNGLRQSIWTDFSSRFHIPQVAEFYGATECNCSLGNFDSQVG 401
Cdd:PLN02860 261 vtsmiTVPAMMADLISL--TRKSMTWKVFPSVRKILngGGSLSSRLLPDAKKLFPNAKLFSAYGMTEACSSLTFMTLHDP 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 402 ACGFNSRILSFVYPIRLVRVNEdtmelirgPDGVCIpcqpGQPGQLVGRIIQQDPLRRFDGYLNQG--------ANNKKI 473
Cdd:PLN02860 339 TLESPKQTLQTVNQTKSSSVHQ--------PQGVCV----GKPAPHVELKIGLDESSRVGRILTRGphvmlgywGQNSET 406
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 291084711 474 ASDvfkKGDQAYL-TGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLQMADVAVYGV 539
Cdd:PLN02860 407 ASV---LSNDGWLdTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGV 470
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
239-598 |
1.54e-12 |
|
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: 69.21 E-value: 1.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 239 DKLFYIYTSGTTGLPKAAIVVH-SRYYRMAALVYYGFRMRPDDIVYDCLPLYHSaGNIVGIGQCVLHGMTVVIRKKFSAS 317
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANkTFFAVPDILQKEGLNWVVGDVTYLPLPATHI-GGLWWILTCLIHGGLCVTGGENTTY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 318 R-FWDDCIKYNCTIVQYIGELCRYLLNQPPREAESRHKVRMaLGNGLRQSIWTD--FSSRFHIPQVAEFYGATE----CN 390
Cdd:cd17635 81 KsLFKILTTNAVTTTCLVPTLLSKLVSELKSANATVPSLRL-IGYGGSRAIAADvrFIEATGLTNTAQVYGLSEtgtaLC 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 391 CSLGNFDSQVGACGfnsrilsfvYPIRLVRVNEDTMELIRGPDGVcipcqpgqpgqlVGRIIQQDPlRRFDGYLNqganN 470
Cdd:cd17635 160 LPTDDDSIEINAVG---------RPYPGVDVYLAATDGIAGPSAS------------FGTIWIKSP-ANMLGYWN----N 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 471 KKIASDVFKKGdqaYL-TGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLQMADVAVYgvEVPGAE-GRA 548
Cdd:cd17635 214 PERTAEVLIDG---WVnTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACY--EISDEEfGEL 288
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 291084711 549 GMAAVASPTSNCD--LESFAQTLKKELPLYARPIFLRFLPELHKTGTFKFQK 598
Cdd:cd17635 289 VGLAVVASAELDEnaIRALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
84-601 |
1.97e-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: 69.66 E-value: 1.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 84 VRRHPDKTALIfeGTNTHWTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRD 163
Cdd:cd05920 25 AARHPDRIAVV--DGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPVLALPSHRRS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 164 ALRHCLDTSKARALIfgsemasavyeiqaildptltlfcsgswepstVPANTEHLDPlLEDAPKHLPSIPDKGftdklFY 243
Cdd:cd05920 103 ELSAFCAHAEAVAYI--------------------------------VPDRHAGFDH-RALARELAESIPEVA-----LF 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 244 IYTSGTTGLPKAAIVVHSRYYRM--AALVYYGFRmrpDDIVYDC-LPLYHSA--------GNIVGIGQCVL--------- 303
Cdd:cd05920 145 LLSGGTTGTPKLIPRTHNDYAYNvrASAEVCGLD---QDTVYLAvLPAAHNFplacpgvlGTLLAGGRVVLapdpspdaa 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 304 ------HGMTVVIRKKFSASRFWDDCIKY-----NCTIVQYIGElcryllnqpPREAESRHKVRMALGNGLRQsiwtdfs 372
Cdd:cd05920 222 fplierEGVTVTALVPALVSLWLDAAASRradlsSLRLLQVGGA---------RLSPALARRVPPVLGCTLQQ------- 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 373 srfhipqvaeFYGATE---CNCSLGNFDSQVgaCGFNSRILSFVYPIRLVrvnedtmelirgpDGVCIPCQPGQPGQLVG 449
Cdd:cd05920 286 ----------VFGMAEgllNYTRLDDPDEVI--IHTQGRPMSPDDEIRVV-------------DEEGNPVPPGEEGELLT 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 450 RiiqqDPLrRFDGYLNQGANNKKIASDvfkkgDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLL 529
Cdd:cd05920 341 R----GPY-TIRGYYRAPEHNARAFTP-----DGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHP 410
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 291084711 530 QMADVAVYGVEVPGAEGRAGMAAVASPTSnCDLESFAQTLKK-ELPLYARPIFLRFLPELHKTGTFKFQKTEL 601
Cdd:cd05920 411 AVHDAAVVAMPDELLGERSCAFVVLRDPP-PSAAQLRRFLRErGLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
89-603 |
2.12e-12 |
|
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: 69.77 E-value: 2.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 89 DKTALIFeGTNTH----WTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRDA 164
Cdd:cd05915 9 GRKEVVS-RLHTGevhrTTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 165 LRHCLDTSKARALIFGSEMASAVYEiqaildpTLTLFCSGSWEPSTVPANTEHLDPLLEDAPKHLPSIP-DKgfTDKLFY 243
Cdd:cd05915 88 IAYILNHAEDKVLLFDPNLLPLVEA-------IRGELKTVQHFVVMDEKAPEGYLAYEEALGEEADPVRvPE--RAACGM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 244 IYTSGTTGLPKAAIVVHSRYYRMAALVYYGFRMRPDDI-VYDC-LPLYHSAGNIVGIGQCVLHGMTVVIRKKFSASRFWD 321
Cdd:cd05915 159 AYTTGTTGLPKGVVYSHRALVLHSLAASLVDGTALSEKdVVLPvVPMFHVNAWCLPYAATLVGAKQVLPGPRLDPASLVE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 322 DCIKYNCTivQYIGElcRYLLNQPPREAESRHK-----VRMALGNGLRQSIWTDFsSRFHIPQVAEFYGATECNcSLGNf 396
Cdd:cd05915 239 LFDGEGVT--FTAGV--PTVWLALADYLESTGHrlktlRRLVVGGSAAPRSLIAR-FERMGVEVRQGYGLTETS-PVVV- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 397 dsqvgACGFNSRILSFVYPIRLVRVNEDTMELIRGPDGVCIPCQPGQPGQlvGRIIQQDPLRR---FDGYLNqgaNNKKI 473
Cdd:cd05915 312 -----QNFVKSHLESLSEEEKLTLKAKTGLPIPLVRLRVADEEGRPVPKD--GKALGEVQLKGpwiTGGYYG---NEEAT 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 474 ASDVFKKGdqAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLQMADVAVYGvEVPGAEGRAGMAAV 553
Cdd:cd05915 382 RSALTPDG--FFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVA-IPHPKWQERPLAVV 458
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 291084711 554 ASPTSNCDLESFAQTLKKEL-PLYARPIFLRFLPELHKTGTFKFQKTELRK 603
Cdd:cd05915 459 VPRGEKPTPEELNEHLLKAGfAKWQLPDAYVFAEEIPRTSAGKFLKRALRE 509
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
68-609 |
2.36e-12 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 70.76 E-value: 2.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 68 RYLQERkTVPLLFASVVRRHPDKTALIFEGTNThwTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMA 147
Cdd:PRK12316 4546 GYPATR-CVHQLVAERARMTPDAVAVVFDEEKL--TYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVL 4622
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 148 KLGVEAALINTNLRRDALRHCLDTSKARALIFGSEmASAVYEIQAILDpTLTLFCSGSWE--PSTVPANteHLDPlleda 225
Cdd:PRK12316 4623 KAGGAYVPLDPEYPRERLAYMMEDSGAALLLTQSH-LLQRLPIPDGLA-SLALDRDEDWEgfPAHDPAV--RLHP----- 4693
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 226 pkhlpsipdkgftDKLFY-IYTSGTTGLPKAAIVVHSRYYRMAALVYYGFRMRPDDIVYDCLPlYHSAGNIVGIGQCVLH 304
Cdd:PRK12316 4694 -------------DNLAYvIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMS-FSFDGSHEGLYHPLIN 4759
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 305 GMTVVIRKkfsaSRFWD------DCIKYNCTIVQYIGELCRYLLNQPPREAE-SRHKVRMALGNGLRQSIWTDFSSRFHI 377
Cdd:PRK12316 4760 GASVVIRD----DSLWDperlyaEIHEHRVTVLVFPPVYLQQLAEHAERDGEpPSLRVYCFGGEAVAQASYDLAWRALKP 4835
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 378 PQVAEFYGATECNCSLGNFDSQVG-ACGfnsrilSFVYPIRLVRVNEDTMELirgpDGVCIPCQPGQPGQLVgriIQQDP 456
Cdd:PRK12316 4836 VYLFNGYGPTETTVTVLLWKARDGdACG------AAYMPIGTPLGNRSGYVL----DGQLNPLPVGVAGELY---LGGEG 4902
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 457 LRRfdGYLNQGA-NNKKIASDVF-KKGDQAYLTGDVL------VMDELGylyfrdRTGDTFRWKGENVSTTEVEgtlSRL 528
Cdd:PRK12316 4903 VAR--GYLERPAlTAERFVPDPFgAPGGRLYRTGDLAryradgVIDYLG------RVDHQVKIRGFRIELGEIE---ARL 4971
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 529 LQMADV--AVYgVEVPGAEGRAGMAAVA--------SPTSNCDL-ESFAQTLKKELPLYARPIFLRFLPELHKTGTFKFQ 597
Cdd:PRK12316 4972 REHPAVreAVV-IAQEGAVGKQLVGYVVpqdpaladADEAQAELrDELKAALRERLPEYMVPAHLVFLARMPLTPNGKLD 5050
|
570
....*....|..
gi 291084711 598 KTELRKegFDPS 609
Cdd:PRK12316 5051 RKALPQ--PDAS 5060
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
103-603 |
3.59e-12 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 68.75 E-value: 3.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 103 TFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALRHCLDTSKAralifgse 182
Cdd:cd05974 2 SFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRDRVDRGGA-------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 183 MASAVYEIQAILDPTLTLFcsgswepstvpantehldplledapkhlpsipdkgftdklfyiyTSGTTGLPKaaIVVHS- 261
Cdd:cd05974 74 VYAAVDENTHADDPMLLYF--------------------------------------------TSGTTSKPK--LVEHTh 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 262 RYYRMAAL-VYYGFRMRPDDIVYD-CLPLY--HSAGNIVG---IGQCVLhgmtVVIRKKFSASRFWDDCIKYNCTIVQYI 334
Cdd:cd05974 108 RSYPVGHLsTMYWIGLKPGDVHWNiSSPGWakHAWSCFFApwnAGATVF----LFNYARFDAKRVLAALVRYGVTTLCAP 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 335 GELCRYLLNQPPREAESRHKVRMALGNGLRQSIWTDFSSRFHIpQVAEFYGATECNCSLGNFDSQVGACGFNSRilsfvy 414
Cdd:cd05974 184 PTVWRMLIQQDLASFDVKLREVVGAGEPLNPEVIEQVRRAWGL-TIRDGYGQTETTALVGNSPGQPVKAGSMGR------ 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 415 PIRLVRVNedtmelIRGPDGvcipcQPGQPGQLVGRIIQQDPLRRFDGYlnqgANNKKIASDVFkkGDQAYLTGDVLVMD 494
Cdd:cd05974 257 PLPGYRVA------LLDPDG-----APATEGEVALDLGDTRPVGLMKGY----AGDPDKTAHAM--RGGYYRTGDIAMRD 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 495 ELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLQMADVAVygVEVPGAEGRA------GMAAVASPTSNCDLESFAQT 568
Cdd:cd05974 320 EDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAV--VPSPDPVRLSvpkafiVLRAGYEPSPETALEIFRFS 397
|
490 500 510
....*....|....*....|....*....|....*
gi 291084711 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 |
3.81e-12 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.
Pssm-ID: 341280 [Multi-domain] Cd Length: 447 Bit Score: 68.88 E-value: 3.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 79 LFASVVRRHPDKTALIFEgtNTHWTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKLGVEAALINT 158
Cdd:cd12115 4 LVEAQAARTPDAIALVCG--DESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 159 NLRRDALRHCLDTSKARALIfgsemasavyeiqaildptltlfcsgswepsTVPANTEHLdplledapkhlpsipdkgft 238
Cdd:cd12115 82 AYPPERLRFILEDAQARLVL-------------------------------TDPDDLAYV-------------------- 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 239 dklfyIYTSGTTGLPKAAIVVHSR---YYRMAALVYYGFRMR----PDDIVYDC------LPLyhSAGNIVGIGQCVLHG 305
Cdd:cd12115 111 -----IYTSGSTGRPKGVAIEHRNaaaFLQWAAAAFSAEELAgvlaSTSICFDLsvfelfGPL--ATGGKVVLADNVLAL 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 306 MTVVIRKKfsasrfwddcikynCTIVQYIGELCRYLLNQPPREAESRhKVRMAlGNGLRQSIWTDFSSRFHIPQVAEFYG 385
Cdd:cd12115 184 PDLPAAAE--------------VTLINTVPSAAAELLRHDALPASVR-VVNLA-GEPLPRDLVQRLYARLQVERVVNLYG 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 386 ATECN-----CSLGNFDSQVGACGFNsrilsfVYPIRlVRVNEDTMElirgpdgvciPCQPGQPGQLvgrIIQQDPLRRf 460
Cdd:cd12115 248 PSEDTtystvAPVPPGASGEVSIGRP------LANTQ-AYVLDRALQ----------PVPLGVPGEL---YIGGAGVAR- 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 461 dGYLNQ-GANNKKIASDVFKKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLQMADVAVYGV 539
Cdd:cd12115 307 -GYLGRpGLTAERFLPDPFGPGARLYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAI 385
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 291084711 540 EVPGAEGRAGMAAVASPTSNCDLESFAQTLKKELPLYARPIFLRFLPELHKTGTFKFQKTEL 601
Cdd:cd12115 386 GDAAGERRLVAYIVAEPGAAGLVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
75-588 |
4.80e-12 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 69.30 E-value: 4.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 75 TVPLLFASVVRRHPDKTALIFEGTntHWTFRQLDDYSSSVANFLQARGLVSGNVVALFMEnRNEFVGLWLgMAKLGVEAA 154
Cdd:PRK10252 459 TLSALVAQQAAKTPDAPALADARY--QFSYREMREQVVALANLLRERGVKPGDSVAVALP-RSVFLTLAL-HAIVEAGAA 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 155 L--INTNLRRDALRHCLDTSKARALIFGSEMASAVYEIqaildPTLTLFCSGSWEPSTVPAntehldPLLEDAPKHLPSI 232
Cdd:PRK10252 535 WlpLDTGYPDDRLKMMLEDARPSLLITTADQLPRFADV-----PDLTSLCYNAPLAPQGAA------PLQLSQPHHTAYI 603
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 233 pdkgftdklfyIYTSGTTGLPKAAIVVHsryyrmAALV--------YYGfrMRPDDIV-------YDC------LPLyhs 291
Cdd:PRK10252 604 -----------IFTSGSTGRPKGVMVGQ------TAIVnrllwmqnHYP--LTADDVVlqktpcsFDVsvweffWPF--- 661
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 292 agnivgigqcvLHGMTVVI------RKKFSASRFWDDcikYNCTIVQYIGELCRYLLNQPPREAESRHKVRM-------- 357
Cdd:PRK10252 662 -----------IAGAKLVMaepeahRDPLAMQQFFAE---YGVTTTHFVPSMLAAFVASLTPEGARQSCASLrqvfcsge 727
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 358 ALGNGLRQsiwtDFSSRFHIPqVAEFYGATE----------CNCSLGNFDSQVGACGF---NSRIlsfvypirlvRVNED 424
Cdd:PRK10252 728 ALPADLCR----EWQQLTGAP-LHNLYGPTEaavdvswypaFGEELAAVRGSSVPIGYpvwNTGL----------RILDA 792
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 425 TMElirgpdgvciPCQPGQPGQLVGRIIQqdpLRRfdGYLNQ-GANNKKIASDVFKKGDQAYLTGDVLVMDELGYLYFRD 503
Cdd:PRK10252 793 RMR----------PVPPGVAGDLYLTGIQ---LAQ--GYLGRpDLTASRFIADPFAPGERMYRTGDVARWLDDGAVEYLG 857
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 504 RTGDTFRWKGENVSTTEVEGTLSRLLQMADVAVYGVEVPGAEGRAGMAA------VASPTSNCDLESFAQTLKKELPLYA 577
Cdd:PRK10252 858 RSDDQLKIRGQRIELGEIDRAMQALPDVEQAVTHACVINQAAATGGDARqlvgylVSQSGLPLDTSALQAQLRERLPPHM 937
|
570
....*....|.
gi 291084711 578 RPIFLRFLPEL 588
Cdd:PRK10252 938 VPVVLLQLDQL 948
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
84-540 |
1.35e-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: 67.34 E-value: 1.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 84 VRRH-----PDKTALIFE----GTNTHWTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKLGVEAA 154
Cdd:cd05967 56 LDRHveagrGDQIALIYDspvtGTERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHS 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 155 LINTNLRRDALRHCLDTSKARALI---FGSEmASAVYEIQAILDPTLTLfcsGSWEPSTV--------------PANTEH 217
Cdd:cd05967 136 VVFGGFAAKELASRIDDAKPKLIVtasCGIE-PGKVVPYKPLLDKALEL---SGHKPHHVlvlnrpqvpadltkPGRDLD 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 218 LDPLLEDAPKHlPSIPDKGfTDKLFYIYTSGTTGLPKAaiVVHSRYYRMAALVYygfRMRpddIVYDCLP--LYHSA--- 292
Cdd:cd05967 212 WSELLAKAEPV-DCVPVAA-TDPLYILYTSGTTGKPKG--VVRDNGGHAVALNW---SMR---NIYGIKPgdVWWAAsdv 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 293 GNIVGIGQCV----LHGMTVVIRKKF-----SASRFWDDCIKYNCTIVQYIGELCRYLLNQPPREAE------SRHKVRM 357
Cdd:cd05967 282 GWVVGHSYIVygplLHGATTVLYEGKpvgtpDPGAFWRVIEKYQVNALFTAPTAIRAIRKEDPDGKYikkydlSSLRTLF 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 358 ALGNGLRQSIWTDFSSRFHIPqVAEFYGATE------CNCS-LGNFDSQVGAC-----GFNSRILSfvypirlvrvneDT 425
Cdd:cd05967 362 LAGERLDPPTLEWAENTLGVP-VIDHWWQTEtgwpitANPVgLEPLPIKAGSPgkpvpGYQVQVLD------------ED 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 426 MElirgpdgvciPCQPGQPGQLVGRI---------IQQDPLRRFDGYLNqgannkkiasdvfkKGDQAYLTGDVLVMDEL 496
Cdd:cd05967 429 GE----------PVGPNELGNIVIKLplppgclltLWKNDERFKKLYLS--------------KFPGYYDTGDAGYKDED 484
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 291084711 497 GYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLQMADVAVYGVE 540
Cdd:cd05967 485 GYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVR 528
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
85-389 |
2.20e-11 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 66.85 E-value: 2.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 85 RRHPDKTALIFEGTNT--------HWTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKLGVEAALI 156
Cdd:PRK09274 17 QERPDQLAVAVPGGRGadgklaydELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGAVPVLV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 157 NTNLRRDALRHCLDTSKARALIfGSEMASAVYEIQAILDPTL-TLFCSG---SWEPSTvpantehLDPLLEDAPKHLPSI 232
Cdd:PRK09274 97 DPGMGIKNLKQCLAEAQPDAFI-GIPKAHLARRLFGWGKPSVrRLVTVGgrlLWGGTT-------LATLLRDGAAAPFPM 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 233 PDKGFTDKLFYIYTSGTTGLPKAAIVVHSRYYRMAALVYYGFRMRPDDIVYDCLPLYhsagnivgigqcVLH----GMTV 308
Cdd:PRK09274 169 ADLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEIDLPTFPLF------------ALFgpalGMTS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 309 VI-------------RKKFSASRfwddciKYNCTIV----QYIGELCRYLLNQPpreaesrHK---VRMALGNGLRQSIW 368
Cdd:PRK09274 237 VIpdmdptrpatvdpAKLFAAIE------RYGVTNLfgspALLERLGRYGEANG-------IKlpsLRRVISAGAPVPIA 303
|
330 340
....*....|....*....|....*.
gi 291084711 369 TdfSSRFH--IPQVAEF---YGATEC 389
Cdd:PRK09274 304 V--IERFRamLPPDAEIltpYGATEA 327
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
84-309 |
5.12e-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: 65.34 E-value: 5.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 84 VRRHPDKTALIF----EGTNTHWTFRQLDDYSSSVANFLQARGLVsGNVVALFMENRNEFVGLWLG--MAKL-GVEAALI 156
Cdd:cd05931 3 AAARPDRPAYTFlddeGGREETLTYAELDRRARAIAARLQAVGKP-GDRVLLLAPPGLDFVAAFLGclYAGAiAVPLPPP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 157 NTNLRRDALRHCLDTSKARALIFGSEMASAVYEIQAILdptltlfcsgswePSTVPANTEHLDPLLEDAPKHLPsIPDKG 236
Cdd:cd05931 82 TPGRHAERLAAILADAGPRVVLTTAAALAAVRAFAASR-------------PAAGTPRLLVVDLLPDTSAADWP-PPSPD 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 291084711 237 FTDKLFYIYTSGTTGLPKAAIVVHsryyrmAALVY------YGFRMRPDDIVYDCLPLYHSAGNIVGIGQCVLHGMTVV 309
Cdd:cd05931 148 PDDIAYLQYTSGSTGTPKGVVVTH------RNLLAnvrqirRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGPSV 220
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
68-588 |
7.31e-11 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 65.75 E-value: 7.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 68 RYLQERkTVPLLFASVVRRHPDKTALIFEGTntHWTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMA 147
Cdd:PRK12316 3052 EYPLER-GVHRLFEEQVERTPDAVALAFGEQ--RLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAIL 3128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 148 KLGVEAALINTNLRRDALRHCLDTSKARALIFGSEMASavyeiqaildptltlfcsgswePSTVPANTEHLDPLLEDAPK 227
Cdd:PRK12316 3129 KAGGAYVPLDPEYPEERLAYMLEDSGAQLLLSQSHLRL----------------------PLAQGVQVLDLDRGDENYAE 3186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 228 HLPSIPDKGftDKLFY-IYTSGTTGLPKAAIVVHSRYYRMAALVYYGFRMRPDDIVydclpLYHSAGNIVGIGQCVLHGM 306
Cdd:PRK12316 3187 ANPAIRTMP--ENLAYvIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRV-----LQFTTFSFDVFVEELFWPL 3259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 307 TVVIRKKFSASRFWDDCIKYNCTIVQ--------YIGELCRYLLNQPPREAESrhkVRMALGNGlrQSIWTDFSSRFHIP 378
Cdd:PRK12316 3260 MSGARVVLAGPEDWRDPALLVELINSegvdvlhaYPSMLQAFLEEEDAHRCTS---LKRIVCGG--EALPADLQQQVFAG 3334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 379 Q-VAEFYGATECNCSLGNFDSQVGACGFnsrilsfvYPIRLVRVNEDTMELirgpDGVCIPCQPGQPGQLvgrIIQQDPL 457
Cdd:PRK12316 3335 LpLYNLYGPTEATITVTHWQCVEEGKDA--------VPIGRPIANRACYIL----DGSLEPVPVGALGEL---YLGGEGL 3399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 458 RRfdGYLNQ-GANNKKIASDVFKKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEgtlSRLLQMAdvAV 536
Cdd:PRK12316 3400 AR--GYHNRpGLTAERFVPDPFVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIE---ARLLEHP--WV 3472
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 291084711 537 YGVEVPGAEGRAGMAAVASPTSNCDL-ESFAQTLKKELPLYARPIFLRFLPEL 588
Cdd:PRK12316 3473 REAVVLAVDGRQLVAYVVPEDEAGDLrEALKAHLKASLPEYMVPAHLLFLERM 3525
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
77-602 |
8.76e-11 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 64.87 E-value: 8.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 77 PLLF---ASVVrrHPDKTALIFEgtNTHWTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKLGVEA 153
Cdd:PLN02479 22 PLWFlerAAVV--HPTRKSVVHG--SVRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 154 ALINTNLRRDALRHCLDTSKARALIFGSEMASAVYEIQAIL--------DPTLTLFCSgswEPSTVPANTEH-------- 217
Cdd:PLN02479 98 NCVNIRLNAPTIAFLLEHSKSEVVMVDQEFFTLAEEALKILaekkkssfKPPLLIVIG---DPTCDPKSLQYalgkgaie 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 218 LDPLLEDAPKHLPSIPDKGFTDKLFYIYTSGTTGLPKAAIVVHSRYYRMAALVYYGFRMrPDDIVYD-CLPLYHSAGNIV 296
Cdd:PLN02479 175 YEKFLETGDPEFAWKPPADEWQSIALGYTSGTTASPKGVVLHHRGAYLMALSNALIWGM-NEGAVYLwTLPMFHCNGWCF 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 297 GIGQCVLHGMTVVIRKkFSASRFWDDCIKYNCTIVQYIGELCRYLLNQPPREA--ESRHKVR-MALGNGLRQSIWTDFSS 373
Cdd:PLN02479 254 TWTLAALCGTNICLRQ-VTAKAIYSAIANYGVTHFCAAPVVLNTIVNAPKSETilPLPRVVHvMTAGAAPPPSVLFAMSE 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 374 R----FHIPQVAEFYGATECNCSLGNFDSQ--VGACGFNSRilsfvypiRLVR-VNEDTMELIRGPDGVCIPCQPGQPGQ 446
Cdd:PLN02479 333 KgfrvTHTYGLSETYGPSTVCAWKPEWDSLppEEQARLNAR--------QGVRyIGLEGLDVVDTKTMKPVPADGKTMGE 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 447 LV--GRIIQQdplrrfdGYLNqganNKKIASDVFKKGdqAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGT 524
Cdd:PLN02479 405 IVmrGNMVMK-------GYLK----NPKANEEAFANG--WFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENV 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 525 LSRLLQMADVAVygveVPGAEGRAGMAAVASPTSNCDLESFAQTL---------KKELPLYARPIFLRFLPeLHKTGTFK 595
Cdd:PLN02479 472 VYTHPAVLEASV----VARPDERWGESPCAFVTLKPGVDKSDEAAlaedimkfcRERLPAYWVPKSVVFGP-LPKTATGK 546
|
....*..
gi 291084711 596 FQKTELR 602
Cdd:PLN02479 547 IQKHVLR 553
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
70-604 |
5.21e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 62.47 E-value: 5.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 70 LQERKTVPLLFASVVRRHPDKTAliFEGTNTHWTFRQLDDYSSSVANFLQAR-GLVSGNVVALFMENRNEFVGLWLGMAK 148
Cdd:PRK05677 20 PDEYPNIQAVLKQSCQRFADKPA--FSNLGKTLTYGELYKLSGAFAAWLQQHtDLKPGDRIAVQLPNVLQYPVAVFGAMR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 149 LGVeaALINTNLRRDA--LRHCLDTSKARALIFGSEMAS--------------AVYEIQAILDPTLTLFCSGSWE----- 207
Cdd:PRK05677 98 AGL--IVVNTNPLYTAreMEHQFNDSGAKALVCLANMAHlaekvlpktgvkhvIVTEVADMLPPLKRLLINAVVKhvkkm 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 208 ------PSTVPANTE----HLDPLLEDAPKhlpsiPDkgftDKLFYIYTSGTTGLPKAAIVVHSRYYR--------MAAL 269
Cdd:PRK05677 176 vpayhlPQAVKFNDAlakgAGQPVTEANPQ-----AD----DVAVLQYTGGTTGVAKGAMLTHRNLVAnmlqcralMGSN 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 270 VYYGFrmrpdDIVYDCLPLYH--------------SAGNIVGIGQCVLHGMTVVIRK-KFSAsrFwddcIKYNCTIVQyi 334
Cdd:PRK05677 247 LNEGC-----EILIAPLPLYHiyaftfhcmammliGNHNILISNPRDLPAMVKELGKwKFSG--F----VGLNTLFVA-- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 335 geLCRyllNQPPREAE-SRHKVRMALGNGLRQSI---WTDFSSrfhiPQVAEFYGATECN--CSLGNFDS-QVGACGFns 407
Cdd:PRK05677 314 --LCN---NEAFRKLDfSALKLTLSGGMALQLATaerWKEVTG----CAICEGYGMTETSpvVSVNPSQAiQVGTIGI-- 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 408 rilsfvyPIrlvrvnEDTMELIRGPDGVCIPCqpGQPGQLVGRIIQQdplrrFDGYL-NQGANNKKIASDVFKKgdqayl 486
Cdd:PRK05677 383 -------PV------PSTLCKVIDDDGNELPL--GEVGELCVKGPQV-----MKGYWqRPEATDEILDSDGWLK------ 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 487 TGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLQMADVAVYGVevpgAEGRAGMA----AVASPTSNCDL 562
Cdd:PRK05677 437 TGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGV----PDEKSGEAikvfVVVKPGETLTK 512
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 291084711 563 ESFAQTLKKELPLYARPIFLRFLPELHKTGTFKFQKTELRKE 604
Cdd:PRK05677 513 EQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRRELRDE 554
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
104-545 |
2.52e-09 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 60.02 E-value: 2.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 104 FRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKLG-VEAAL-INTNL-RRDA----LRHCLDTSKARA 176
Cdd:PRK09192 52 YQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGlVPVPLpLPMGFgGRESyiaqLRGMLASAQPAA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 177 LIFGSEMASAVYEIQAILDPTLtlfcSGSWepstvpantEHLDpLLEDAPKHLPSI-PDkgftDKLFYIYTSGTTGLPKA 255
Cdd:PRK09192 132 IITPDELLPWVNEATHGNPLLH----VLSH---------AWFK-ALPEADVALPRPtPD----DIAYLQYSSGSTRFPRG 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 256 AIVVHSRYyrMA---ALVYYGFRMRPDDIVYDCLPLYHSAGnIVGigqCVLHGMTVVIRKKFSASR-F------WDDCIK 325
Cdd:PRK09192 194 VIITHRAL--MAnlrAISHDGLKVRPGDRCVSWLPFYHDMG-LVG---FLLTPVATQLSVDYLPTRdFarrplqWLDLIS 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 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 291084711 385 GATEcncslgnfdsqvgacgfNSRILSFVYP---IRLVRVNEDTMEL------------------------------IRG 431
Cdd:PRK09192 338 GLAE-----------------ATLAVSFSPLgsgIVVEEVDRDRLEYqgkavapgaetrrvrtfvncgkalpgheieIRN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 432 PDGVCIpcqpgqPGQLVGRIIQQDP-LRRfdGYLNQGANNKKIASDvfkkgdqAYL-TGDVLVMDElGYLYFRDRTGDTF 509
Cdd:PRK09192 401 EAGMPL------PERVVGHICVRGPsLMS--GYFRDEESQDVLAAD-------GWLdTGDLGYLLD-GYLYITGRAKDLI 464
|
490 500 510
....*....|....*....|....*....|....*...
gi 291084711 510 RWKGENVSTTEVEGTLSRL--LQMADVAVYGVEVPGAE 545
Cdd:PRK09192 465 IINGRNIWPQDIEWIAEQEpeLRSGDAAAFSIAQENGE 502
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
244-542 |
2.64e-09 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 60.71 E-value: 2.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 244 IYTSGTTGLPKAaiVVHSRYYRMA-----ALVyygFRMRPDDIVYDCLPLYHSAGNIV--------GIGqCVLH-----G 305
Cdd:PRK08633 788 IFSSGSEGEPKG--VMLSHHNILSnieqiSDV---FNLRNDDVILSSLPFFHSFGLTVtlwlplleGIK-VVYHpdptdA 861
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 306 MTVVirkKFSAsrfwddciKYNCTIVQYIGELCRYLLNQPPREAESRHKVRMALGNG--LRQSIWTDFSSRFHIPQVaEF 383
Cdd:PRK08633 862 LGIA---KLVA--------KHRATILLGTPTFLRLYLRNKKLHPLMFASLRLVVAGAekLKPEVADAFEEKFGIRIL-EG 929
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 384 YGATECN----CSLGN-----FDSQVGacgfnSRILSFVYPI--RLVR-VNEDTMElirgpdgvciPCQPGQPGQLVGRI 451
Cdd:PRK08633 930 YGATETSpvasVNLPDvlaadFKRQTG-----SKEGSVGMPLpgVAVRiVDPETFE----------ELPPGEDGLILIGG 994
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 452 IQqdplrRFDGYLNQGANNKKIASDVFKKGdqAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLQM 531
Cdd:PRK08633 995 PQ-----VMKGYLGDPEKTAEVIKDIDGIG--WYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAKALGG 1067
|
330
....*....|.
gi 291084711 532 ADVAVYGVEVP 542
Cdd:PRK08633 1068 EEVVFAVTAVP 1078
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
85-310 |
2.99e-09 |
|
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: 59.75 E-value: 2.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 85 RRHPDKTALIFEGTNTHW---TFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKLGVEAA------- 154
Cdd:cd05921 6 RQAPDRTWLAEREGNGGWrrvTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAApvspays 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 155 LINTNLRRdaLRHCLDTSKArALIFGSEMASAVYEIQAILDPTLTLFCSGSWEPSTvpaNTEHLDPLLE-----DAPKHL 229
Cdd:cd05921 86 LMSQDLAK--LKHLFELLKP-GLVFAQDAAPFARALAAIFPLGTPLVVSRNAVAGR---GAISFAELAAtpptaAVDAAF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 230 PSI-PDkgftDKLFYIYTSGTTGLPKAAIVVHsryyRMAALVY------YGFRMRPDDIVYDCLPLYHSAGNIVGIGQCV 302
Cdd:cd05921 160 AAVgPD----TVAKFLFTSGSTGLPKAVINTQ----RMLCANQamleqtYPFFGEEPPVLVDWLPWNHTFGGNHNFNLVL 231
|
....*...
gi 291084711 303 LHGMTVVI 310
Cdd:cd05921 232 YNGGTLYI 239
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
103-544 |
8.67e-09 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 58.50 E-value: 8.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 103 TFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRDalrhcldtskaralifgsE 182
Cdd:PRK06060 32 THGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRD------------------D 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 183 MASAVYEIQAILDPTLTLFCSgSWEPSTVPANTEhldpLLEDAPKHLPSIPDKGFTDKLFY-IYTSGTTGLPKAAIVVHS 261
Cdd:PRK06060 94 HALAARNTEPALVVTSDALRD-RFQPSRVAEAAE----LMSEAARVAPGGYEPMGGDALAYaTYTSGTTGPPKAAIHRHA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 262 RYYRMA-ALVYYGFRMRPDDIVYDCLPLY--HSAGNIVGI-----GQCVLHGMTVVIRKKFSASRFWDDCIKYNC-TIVQ 332
Cdd:PRK06060 169 DPLTFVdAMCRKALRLTPEDTGLCSARMYfaYGLGNSVWFplatgGSAVINSAPVTPEAAAILSARFGPSVLYGVpNFFA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 333 YIGELCryllnqpprEAESRHKVRMALGNGlrQSIWTDFSSRfhipqVAEFYGATECNCSLGNfdSQVGACgFNSRILSF 412
Cdd:PRK06060 249 RVIDSC---------SPDSFRSLRCVVSAG--EALELGLAER-----LMEFFGGIPILDGIGS--TEVGQT-FVSNRVDE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 413 VYPIRLVRVNEDTMELIRGPDGVCipCQPGQPGQLVGR---IIQQ-----DPLRRFDGYLNqgannkkiasdvfkkgdqa 484
Cdd:PRK06060 310 WRLGTLGRVLPPYEIRVVAPDGTT--AGPGVEGDLWVRgpaIAKGywnrpDSPVANEGWLD------------------- 368
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 291084711 485 ylTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLQMADVAVYGV-EVPGA 544
Cdd:PRK06060 369 --TRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVrESTGA 427
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
88-595 |
1.09e-08 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.
Pssm-ID: 341281 [Multi-domain] Cd Length: 470 Bit Score: 58.07 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 88 PDKTALIFEGTNthWTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALRH 167
Cdd:cd12116 1 PDATAVRDDDRS--LSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 168 CLDTSKARALIFGSEMASavyeiqaildptlTLFCSGswepsTVPANTEHLDPLLEDAPKHLPSIPDKGFTdklfyIYTS 247
Cdd:cd12116 79 ILEDAEPALVLTDDALPD-------------RLPAGL-----PVLLLALAAAAAAPAAPRTPVSPDDLAYV-----IYTS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 248 GTTGLPKAAIVVH----------------SRYYRMAALVYYGFrmrpdDI----VYdcLPLyhsagnivgigqcvLHGMT 307
Cdd:cd12116 136 GSTGRPKGVVVSHrnlvnflhsmrerlglGPGDRLLAVTTYAF-----DIslleLL--LPL--------------LAGAR 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 308 VVIRKK---FSASRFWDDCIKYNCTIVQYIGELCRYLLNQPPREAESrhkVRMALGNglrQSIWTDFSSRF--HIPQVAE 382
Cdd:cd12116 195 VVIAPRetqRDPEALARLIEAHSITVMQATPATWRMLLDAGWQGRAG---LTALCGG---EALPPDLAARLlsRVGSLWN 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 383 FYGATEcncslgnfdSQVGACGfnSRILSFVYPIRLVRVNEDTMELIRGPDGVCIPcqPGQPGQLvgrIIQQDPLRRfdG 462
Cdd:cd12116 269 LYGPTE---------TTIWSTA--ARVTAAAGPIPIGRPLANTQVYVLDAALRPVP--PGVPGEL---YIGGDGVAQ--G 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 463 YLNQGAnnkkIASDVF------KKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLQMADVAV 536
Cdd:cd12116 331 YLGRPA----LTAERFvpdpfaGPGSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAV 406
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 291084711 537 YGVEVPGAEGRAGMAAVASPTSnCDLESFAQTLKKELPLYARPIFLRFLPELHKTGTFK 595
Cdd:cd12116 407 VVREDGGDRRLVAYVVLKAGAA-PDAAALRAHLRATLPAYMVPSAFVRLDALPLTANGK 464
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
79-280 |
1.25e-08 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 58.64 E-value: 1.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 79 LFASVVRRHPDKTALIFEGTntHWTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKLGVEAALINT 158
Cdd:PRK05691 2193 LFAAQAARTPQAPALTFAGQ--TLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDP 2270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 159 NLRRDALRHCLDTSKARALIFGSEMASAVYEIQAildpTLTLFCSGSWEPSTVPANTEHLDPLleDAPKHLPsipdkgft 238
Cdd:PRK05691 2271 EYPLERLHYMIEDSGIGLLLSDRALFEALGELPA----GVARWCLEDDAAALAAYSDAPLPFL--SLPQHQA-------- 2336
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 291084711 239 dklFYIYTSGTTGLPKAAIVVHSRYYRMAALVYYGFRMRPDD 280
Cdd:PRK05691 2337 ---YLIYTSGSTGKPKGVVVSHGEIAMHCQAVIERFGMRADD 2375
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
88-601 |
1.42e-08 |
|
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341305 [Multi-domain] Cd Length: 447 Bit Score: 57.48 E-value: 1.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 88 PDKTALIFEgtNTHWTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKLGveaalintnlrrdalrh 167
Cdd:cd17650 1 PDAIAVSDA--TRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAG----------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 168 cldtskaralifGSEMAsavyeiqaiLDPTLtlfcsgswepstvPAntEHLDPLLEDA-PKHLPSIPDkgftDKLFYIYT 246
Cdd:cd17650 62 ------------GAYVP---------IDPDY-------------PA--ERLQYMLEDSgAKLLLTQPE----DLAYVIYT 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 247 SGTTGLPKAAIVVHSRYYRMaalvYYGFRmrpDDIVYDCLPLYH----------SAGNIVgigQCVLHGMTVVI---RKK 313
Cdd:cd17650 102 SGTTGKPKGVMVEHRNVAHA----AHAWR---REYELDSFPVRLlqmasfsfdvFAGDFA---RSLLNGGTLVIcpdEVK 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 314 FSASRFWDDCIKYNCTIVQYIGELCRYLLNQPPREAESRHKVR-MALGNGLRQSIW-TDFSSRF-HIPQVAEFYGATECN 390
Cdd:cd17650 172 LDPAALYDLILKSRITLMESTPALIRPVMAYVYRNGLDLSAMRlLIVGSDGCKAQDfKTLAARFgQGMRIINSYGVTEAT 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 391 CSLGNFD-SQVGACGfnSRILSFVYPIRLVR--VNEDTMELIrgPDGVCIPCQPGQPGqlVGRiiqqdplrrfdGYLNQG 467
Cdd:cd17650 252 IDSTYYEeGRDPLGD--SANVPIGRPLPNTAmyVLDERLQPQ--PVGVAGELYIGGAG--VAR-----------GYLNRP 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 468 ANNK-KIASDVFKKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLQMADVAVYGVEvpGAEG 546
Cdd:cd17650 315 ELTAeRFVENPFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVRE--DKGG 392
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 291084711 547 RAGMAAVASPTSNCDLESFAQTLKKELPLYARPIFLRFLPELHKTGTFKFQKTEL 601
Cdd:cd17650 393 EARLCAYVVAAATLNTAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
84-261 |
1.83e-08 |
|
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: 57.17 E-value: 1.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 84 VRRHPDKTALifEGTNTHWTFRQLDDYSSSVANFLQARGLVSGNVVALFMENrnefvGLWLGMAKLGVeaalintnLRrd 163
Cdd:cd05918 9 ARSQPDAPAV--CAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEK-----SKWAVVAMLAV--------LK-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 164 alrhcldtskaralifgsemASAVYeiqAILDPTLtlfcsgswepstvPAntEHLDPLLED--APKHLPSIPDkgftDKL 241
Cdd:cd05918 72 --------------------AGGAF---VPLDPSH-------------PL--QRLQEILQDtgAKVVLTSSPS----DAA 109
|
170 180
....*....|....*....|
gi 291084711 242 FYIYTSGTTGLPKAAIVVHS 261
Cdd:cd05918 110 YVIFTSGSTGKPKGVVIEHR 129
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
86-261 |
7.09e-08 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 55.26 E-value: 7.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 86 RHPDKTALIFEGTNthWTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLrRDAL 165
Cdd:PRK09029 15 VRPQAIALRLNDEV--LTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQL-PQPL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 166 RHCLDTSkaralifgsemasavYEIQAILDPtltlfcsgswEPSTVPANTEHLDPLLEDAPKHLPSIPDKGFTdklfYIY 245
Cdd:PRK09029 92 LEELLPS---------------LTLDFALVL----------EGENTFSALTSLHLQLVEGAHAVAWQPQRLAT----MTL 142
|
170
....*....|....*.
gi 291084711 246 TSGTTGLPKAaiVVHS 261
Cdd:PRK09029 143 TSGSTGLPKA--AVHT 156
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
69-296 |
7.43e-08 |
|
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: 55.37 E-value: 7.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 69 YLQERKTVPLLFASVVRRHPDKTALIF------EGTNTHWTFRQLDDYSSSVANFLQARGLVSGNVVAL-FMENRNEFVG 141
Cdd:cd05906 1 PLHRPEGAPRTLLELLLRAAERGPTKGityidaDGSEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILqFDDNEDFIPA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 142 LW---LG---MAKLGVEAALINTNLRRDALRHCLDTSKARALIFGSEMASAVYEIQAILdptltlfcsgSWEPSTVPANT 215
Cdd:cd05906 81 FWacvLAgfvPAPLTVPPTYDEPNARLRKLRHIWQLLGSPVVLTDAELVAEFAGLETLS----------GLPGIRVLSIE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 216 EHLDPlleDAPKHLP-SIPDkgftDKLFYIYTSGTTGLPKAAIVVHSRYYRMAALVYYGFRMRPDDIVYDCLPLYHsAGN 294
Cdd:cd05906 151 ELLDT---AADHDLPqSRPD----DLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVPLDH-VGG 222
|
..
gi 291084711 295 IV 296
Cdd:cd05906 223 LV 224
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
70-602 |
9.49e-08 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 55.21 E-value: 9.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 70 LQERKTVPLLFASVVRRHPDKTAliFEGTNTHWTFRQLDDYSSSVANFLQAR-GLVSGNVVALFMENRNEFVGLWLGMAK 148
Cdd:PRK12492 20 LAAYKSVVEVFERSCKKFADRPA--FSNLGVTLSYAELERHSAAFAAYLQQHtDLVPGDRIAVQMPNVLQYPIAVFGALR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 149 LGVeaALINTNLRRDA--LRHCLDTSKARALIFGSEMASAVYE------IQAILDPTLTLFCSGS--WEPSTVPANTEHL 218
Cdd:PRK12492 98 AGL--IVVNTNPLYTAreMRHQFKDSGARALVYLNMFGKLVQEvlpdtgIEYLIEAKMGDLLPAAkgWLVNTVVDKVKKM 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 219 DP------------LLEDAPKHLPSIPDKGFTDKLFYIYTSGTTGLPKAAIVVHSRYYRMAALVYYGFRMRPDD------ 280
Cdd:PRK12492 176 VPayhlpqavpfkqALRQGRGLSLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVRACLSQLGPDgqplmk 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 281 ----IVYDCLPLYHSAGNIVGIGQCVLHG-MTVVIRKKFSASRFWDDCIKYNCTIVQYIGELCRYLLNQPP-REAE-SRH 353
Cdd:PRK12492 256 egqeVMIAPLPLYHIYAFTANCMCMMVSGnHNVLITNPRDIPGFIKELGKWRFSALLGLNTLFVALMDHPGfKDLDfSAL 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 354 KVRMALGNGLRQSI---WTDFSSrfhiPQVAEFYGATECncslgnfdSQVGAC---GFNSRILSFVYPirlvrVNEDTME 427
Cdd:PRK12492 336 KLTNSGGTALVKATaerWEQLTG----CTIVEGYGLTET--------SPVASTnpyGELARLGTVGIP-----VPGTALK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 428 LIrGPDGVCIPCqpGQPGQLVGRIIQQdplrrFDGYLNQGANNKKI--ASDVFKkgdqaylTGDVLVMDELGYLYFRDRT 505
Cdd:PRK12492 399 VI-DDDGNELPL--GERGELCIKGPQV-----MKGYWQQPEATAEAldAEGWFK-------TGDIAVIDPDGFVRIVDRK 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 506 GDTFRWKGENVSTTEVEGTLSRLLQMADVAVYGVevpgAEGRAGMAA---VASPTSNCDLESFAQTLKKELPLYARPIFL 582
Cdd:PRK12492 464 KDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGV----PDERSGEAVklfVVARDPGLSVEELKAYCKENFTGYKVPKHI 539
|
570 580
....*....|....*....|
gi 291084711 583 RFLPELHKTGTFKFQKTELR 602
Cdd:PRK12492 540 VLRDSLPMTPVGKILRRELR 559
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
86-261 |
1.59e-07 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 54.42 E-value: 1.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 86 RHPDKTALIFEGTNTH---WTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKLG-----------V 151
Cdd:PRK03584 96 RRDDRPAIIFRGEDGPrreLSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLATASLGaiwsscspdfgV 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 152 EAALintnlrrDALRHcldtSKARALI------FGS---EMASAVYEIQAILdPTLTLFCS----GSWEPSTVPANTEHL 218
Cdd:PRK03584 176 QGVL-------DRFGQ----IEPKVLIavdgyrYGGkafDRRAKVAELRAAL-PSLEHVVVvpylGPAAAAAALPGALLW 243
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 291084711 219 DPLLEDAPKHLPSIPDKGFTDKLFYIYTSGTTGLPKAaiVVHS 261
Cdd:PRK03584 244 EDFLAPAEAAELEFEPVPFDHPLWILYSSGTTGLPKC--IVHG 284
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
100-292 |
2.56e-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: 53.52 E-value: 2.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 100 THWTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFvgLWLGMAKLGVEAAlintnlrrDALRHCLDTSKARALIF 179
Cdd:cd17640 4 KRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRW--LIADQGIMALGAV--------DVVRGSDSSVEELLYIL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 180 GSEMASAVyeiqaildptltlfcsgswepstvpantehldpLLEDAPKHLPSIpdkgftdklfyIYTSGTTGLPKAAIVV 259
Cdd:cd17640 74 NHSESVAL---------------------------------VVENDSDDLATI-----------IYTSGTTGNPKGVMLT 109
|
170 180 190
....*....|....*....|....*....|....
gi 291084711 260 H-SRYYRMAALvYYGFRMRPDDIVYDCLPLYHSA 292
Cdd:cd17640 110 HaNLLHQIRSL-SDIVPPQPGDRFLSILPIWHSY 142
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
86-330 |
3.85e-07 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 53.22 E-value: 3.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 86 RH----PDKTALIFEGTN----THWTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKLGVEAALIN 157
Cdd:PRK00174 75 RHlktrGDKVAIIWEGDDpgdsRKITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVVF 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 158 TNLRRDALRHCLDTSKARALIFGSE--MASAVYEIQAILDPTLTLfCSG--------------SWEPS--------TVPA 213
Cdd:PRK00174 155 GGFSAEALADRIIDAGAKLVITADEgvRGGKPIPLKANVDEALAN-CPSvekvivvrrtggdvDWVEGrdlwwhelVAGA 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 214 NTEHldplledAPKHLPSipdkgfTDKLFYIYTSGTTGLPKAaiVVHSR--YyrmaaLVY------YGFRMRPDDiVYDC 285
Cdd:PRK00174 234 SDEC-------EPEPMDA------EDPLFILYTSGSTGKPKG--VLHTTggY-----LVYaamtmkYVFDYKDGD-VYWC 292
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 291084711 286 lplyhSA--GNIVGigqcvlH----------GMTVVIrkkF-------SASRFWDDCIKYNCTI 330
Cdd:PRK00174 293 -----TAdvGWVTG------HsyivygplanGATTLM---FegvpnypDPGRFWEVIDKHKVTI 342
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
102-308 |
3.99e-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: 53.20 E-value: 3.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 102 WTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKLGVeaalINTNLRRDALR----HCLDTSKARAL 177
Cdd:cd17641 12 FTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGA----LSLGIYQDSMAeevaYLLNYTGARVV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 178 IFG-SEMASAVYEIQAILDPTLTLFcsgSWEPSTVpanTEHLDPLLEDAPK-------HLPSIPDKG--------FTDKL 241
Cdd:cd17641 88 IAEdEEQVDKLLEIADRIPSVRYVI---YCDPRGM---RKYDDPRLISFEDvvalgraLDRRDPGLYerevaagkGEDVA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 291084711 242 FYIYTSGTTGLPKAAIVVHSRYYRM-AALVYYGFRmRPDDIVYDCLPLYHSAGNIVGIGQCVLHGMTV 308
Cdd:cd17641 162 VLCTTSGTTGKPKLAMLSHGNFLGHcAAYLAADPL-GPGDEYVSVLPLPWIGEQMYSVGQALVCGFIV 228
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
520-595 |
4.15e-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: 47.92 E-value: 4.15e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 291084711 520 EVEGTLSRLLQMADVAVYGVEVPgAEGRAGMA-AVASPTSNCDLESFAQTLKKELPLYARPIFLRFLPELHKTGTFK 595
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDE-LKGEAPVAfVVLKPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
88-282 |
4.95e-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: 52.64 E-value: 4.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 88 PDKTALIFEGTntHWTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALRH 167
Cdd:cd17652 1 PDAPAVVFGDE--TLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 168 CLDTSKARALIfgsemasavyeiqaildptltlfcsgswepsTVPANtehldplledapkhlpsipdkgftdkLFY-IYT 246
Cdd:cd17652 79 MLADARPALLL-------------------------------TTPDN--------------------------LAYvIYT 101
|
170 180 190
....*....|....*....|....*....|....*.
gi 291084711 247 SGTTGLPKAAIVVHSRYYRMAALVYYGFRMRPDDIV 282
Cdd:cd17652 102 SGSTGRPKGVVVTHRGLANLAAAQIAAFDVGPGSRV 137
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
79-261 |
5.08e-07 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 53.42 E-value: 5.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 79 LFASVVRRHPDKTALIFeGTNThWTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKLGVEAALINT 158
Cdd:PRK12316 516 LFEEQVERTPEAPALAF-GEET-LDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDP 593
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 159 NLRRDALRHCLDTSKARALIFGSEMASAV---YEIQAILDPTLTLFCSGSWE--PSTvpanteHLDPlledapkhlpsip 233
Cdd:PRK12316 594 EYPAERLAYMLEDSGVQLLLSQSHLGRKLplaAGVQVLDLDRPAAWLEGYSEenPGT------ELNP------------- 654
|
170 180
....*....|....*....|....*....
gi 291084711 234 dkgftDKLFY-IYTSGTTGLPKAAIVVHS 261
Cdd:PRK12316 655 -----ENLAYvIYTSGSTGKPKGAGNRHR 678
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
85-310 |
1.84e-06 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 51.03 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 85 RRHPDKTALIFEGTNTHW---TFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNE-----FVGLWLGMAKLGVEAA-- 154
Cdd:PRK08180 50 QEAPDRVFLAERGADGGWrrlTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEhallaLAAMYAGVPYAPVSPAys 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 155 LINTNLRRdaLRHCLDTSKArALIFGSEmaSAVYE--IQAILDPTLTLFCSGSWEPstvPANTEHLDPLLEDAP------ 226
Cdd:PRK08180 130 LVSQDFGK--LRHVLELLTP-GLVFADD--GAAFAraLAAVVPADVEVVAVRGAVP---GRAATPFAALLATPPtaavda 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 227 KHLPSIPD---KgftdklfYIYTSGTTGLPKAAIVVHsryyRM-----AAL--VYYGFRMRPDDIVyDCLPLYHSAGNIV 296
Cdd:PRK08180 202 AHAAVGPDtiaK-------FLFTSGSTGLPKAVINTH----RMlcanqQMLaqTFPFLAEEPPVLV-DWLPWNHTFGGNH 269
|
250
....*....|....
gi 291084711 297 GIGQCVLHGMTVVI 310
Cdd:PRK08180 270 NLGIVLYNGGTLYI 283
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
75-290 |
1.98e-06 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 50.89 E-value: 1.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 75 TVPLLFASVVRRHPDKT-----ALI---FEGTNTHWTFRQ--LDDYS--------SSVANFlqARGLVS-----GNVVAL 131
Cdd:PLN02387 59 TLAALFEQSCKKYSDKRllgtrKLIsreFETSSDGRKFEKlhLGEYEwitygqvfERVCNF--ASGLVAlghnkEERVAI 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 132 FMENRNEfvglWL----GMAKLGVEAALINTNLRRDALRHCLDTSKARALIFGS-------EMAS-------AVYEIQAI 193
Cdd:PLN02387 137 FADTRAE----WLialqGCFRQNITVVTIYASLGEEALCHSLNETEVTTVICDSkqlkkliDISSqletvkrVIYMDDEG 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 194 LDPTLTLFCSGSWEPSTVPanteHLDPLLEDAPKHlPSIPDKgfTDKLFYIYTSGTTGLPKAAIVVHSRYYRMAALVYYG 273
Cdd:PLN02387 213 VDSDSSLSGSSNWTVSSFS----EVEKLGKENPVD-PDLPSP--NDIAVIMYTSGSTGLPKGVMMTHGNIVATVAGVMTV 285
|
250
....*....|....*...
gi 291084711 274 F-RMRPDDIVYDCLPLYH 290
Cdd:PLN02387 286 VpKLGKNDVYLAYLPLAH 303
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
74-295 |
2.97e-06 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 50.43 E-value: 2.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 74 KTVPLLFASVVRRHPDKTALI-FEGTNTHW---TFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKL 149
Cdd:PRK12582 49 RSIPHLLAKWAAEAPDRPWLAqREPGHGQWrkvTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 150 GVEAA-------LINTNLRRdaLRHCLDTSKARaLIF---GSEMASAVYEIQAiLDPTLtLFCSGSWE-PSTVPANTEHL 218
Cdd:PRK12582 129 GVPAApvspaysLMSHDHAK--LKHLFDLVKPR-VVFaqsGAPFARALAALDL-LDVTV-VHVTGPGEgIASIAFADLAA 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 219 DPLLEDAPKHLPSI-PDKgfTDKlfYIYTSGTTGLPKAAIVVHSryyRMAALVYYGFRMRPDD------IVYDCLPLYH- 290
Cdd:PRK12582 204 TPPTAAVAAAIAAItPDT--VAK--YLFTSGSTGMPKAVINTQR---MMCANIAMQEQLRPREpdppppVSLDWMPWNHt 276
|
....*
gi 291084711 291 SAGNI 295
Cdd:PRK12582 277 MGGNA 281
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
96-604 |
3.64e-06 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 50.14 E-value: 3.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 96 EGTNTHWTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALRHCLDTSKAR 175
Cdd:PRK06018 34 EGPIVRTTYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 176 ALIFGsemASAVYEIQAILD--PTLTLFC---SGSWEPSTVPANTEHLDPLLEDApkhlpsipDKGFTDKLF-------Y 243
Cdd:PRK06018 114 VVITD---LTFVPILEKIADklPSVERYVvltDAAHMPQTTLKNAVAYEEWIAEA--------DGDFAWKTFdentaagM 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 244 IYTSGTTGLPKAAI------VVHSryyrMAALVYYGFRMRPDDIVYDCLPLYHSagNIVGIGQ-CVLHGMTVVIR-KKFS 315
Cdd:PRK06018 183 CYTSGTTGDPKGVLyshrsnVLHA----LMANNGDALGTSAADTMLPVVPLFHA--NSWGIAFsAPSMGTKLVMPgAKLD 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 316 ASRFWDDCIKYNCTIVQYIGELCRYLLNQPPREAESRHKVRMAL--GNGLRQSIWTDFSSrfHIPQVAEFYGATECN--C 391
Cdd:PRK06018 257 GASVYELLDTEKVTFTAGVPTVWLMLLQYMEKEGLKLPHLKMVVcgGSAMPRSMIKAFED--MGVEVRHAWGMTEMSplG 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 392 SLGNFDSQVGACGFNSRI---LSFVYPIRLVRVNedtmelIRGPDGVCIPcqpgQPGQLVGRIIQQDPlrrfdgylnqga 468
Cdd:PRK06018 335 TLAALKPPFSKLPGDARLdvlQKQGYPPFGVEMK------ITDDAGKELP----WDGKTFGRLKVRGP------------ 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 469 nnkKIASDVFKKGDQA------YLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLQMADVAVYGVEVP 542
Cdd:PRK06018 393 ---AVAAAYYRVDGEIldddgfFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHP 469
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 291084711 543 GAEGRAGMAAVASPTSNCDLESFAQTLKKELPLYARPIFLRFLPELHKTGTFKFQKTELRKE 604
Cdd:PRK06018 470 KWDERPLLIVQLKPGETATREEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALREQ 531
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
413-614 |
4.54e-06 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 49.95 E-value: 4.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 413 VYPIRLVRVNEDTMElirgpdgvciPCQPGQPGQLVgriiqqdplrrFDGYLNQGA------NNKKIASDVFKK-GDQAY 485
Cdd:PRK10524 417 MYGYNVKLLNEVTGE----------PCGPNEKGVLV-----------IEGPLPPGCmqtvwgDDDRFVKTYWSLfGRQVY 475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 486 LTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLQMADVAVYGVEVPgAEGRAGMA--------AVASPT 557
Cdd:PRK10524 476 STFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDA-LKGQVAVAfvvpkdsdSLADRE 554
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 291084711 558 SNCDLE-SFAQTLKKELPLYARPIFLRFLPELHKTGTFKFqkteLRK------EGFDP---SVVKDP 614
Cdd:PRK10524 555 ARLALEkEIMALVDSQLGAVARPARVWFVSALPKTRSGKL----LRRaiqaiaEGRDPgdlTTIEDP 617
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
101-290 |
6.22e-06 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.
Pssm-ID: 341294 [Multi-domain] Cd Length: 507 Bit Score: 49.14 E-value: 6.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 101 HW-TFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALRHCLDTSKARALif 179
Cdd:cd17639 4 KYmSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECSAI-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 180 gsemasavyeiqaildptltlFCSGSwepstvpantehldplledapkhlpsiPDkgftDKLFYIYTSGTTGLPKAaiVV 259
Cdd:cd17639 82 ---------------------FTDGK---------------------------PD----DLACIMYTSGSTGNPKG--VM 107
|
170 180 190
....*....|....*....|....*....|....*
gi 291084711 260 HSRYYRMAALVYYGFR----MRPDDIVYDCLPLYH 290
Cdd:cd17639 108 LTHGNLVAGIAGLGDRvpelLGPDDRYLAYLPLAH 142
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
228-605 |
1.08e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 48.45 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 228 HLPSIPDKGFTdkLFYIYTSGTTGLPKAaiVVHSRYYRMAAL--VYYGFRMRPDDIVYDCLPLYHSAGNIVGIGQCVLHG 305
Cdd:PRK07787 120 HRYPEPDPDAP--ALIVYTSGTTGPPKG--VVLSRRAIAADLdaLAEAWQWTADDVLVHGLPLFHVHGLVLGVLGPLRIG 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 306 MTVVIRKKFSASRFWDDCiKYNCTIvqYIGELCRYL-LNQPPREAESRHKVRMaLGNGlrqsiwtdfSSRFHIP------ 378
Cdd:PRK07787 196 NRFVHTGRPTPEAYAQAL-SEGGTL--YFGVPTVWSrIAADPEAARALRGARL-LVSG---------SAALPVPvfdrla 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 379 -----QVAEFYGATEC--NCS-LGNFDSQVGACGFnsrilsfvyPIRLVRVNedtmelIRGPDGVCIPCQpgqpGQLVGR 450
Cdd:PRK07787 263 altghRPVERYGMTETliTLStRADGERRPGWVGL---------PLAGVETR------LVDEDGGPVPHD----GETVGE 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 451 IIQQDPLrRFDGYLnqgaNNKKIASDVFkKGDQAYLTGDVLVMDELGYLYF--RDRTgDTFRWKGENVSTTEVEGTLSRL 528
Cdd:PRK07787 324 LQVRGPT-LFDGYL----NRPDATAAAF-TADGWFRTGDVAVVDPDGMHRIvgREST-DLIKSGGYRIGAGEIETALLGH 396
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 291084711 529 LQMADVAVYGVEVPGAEGRagMAAVASPTSNCDLESFAQTLKKELPLYARPIFLRFLPELHKTGTFKFQKTELRKEG 605
Cdd:PRK07787 397 PGVREAAVVGVPDDDLGQR--IVAYVVGADDVAADELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLLSEG 471
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
95-261 |
1.20e-05 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 48.43 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 95 FEGTnTHWTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALRHCLDTSKA 174
Cdd:PTZ00216 116 FNET-RYITYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETEC 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 175 RALIF-GSEMASAVYEIQAILDPTLTLFCSGSWEPS------TVPANTEHLDPLLEDAPKHLPSIPDKgfTDKLFYI-YT 246
Cdd:PTZ00216 195 KAIVCnGKNVPNLLRLMKSGGMPNTTIIYLDSLPASvdtegcRLVAWTDVVAKGHSAGSHHPLNIPEN--NDDLALImYT 272
|
170
....*....|....*
gi 291084711 247 SGTTGLPKAaiVVHS 261
Cdd:PTZ00216 273 SGTTGDPKG--VMHT 285
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
73-579 |
3.24e-05 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 47.47 E-value: 3.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 73 RKTVPLLFASVVRRHPDKTALIFEGTNThwTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEF-VGLwLGMAKLGV 151
Cdd:PRK05691 1130 QAWLPELLNEQARQTPERIALVWDGGSL--DYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLlVGL-LAILKAGG 1206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 152 EAALINTNLRRDALRHCLDTSKARALIFGSEMASAVYEIQAIldptltlfcsgswepSTVPANTEHLDplleDAPKHLPS 231
Cdd:PRK05691 1207 AYVPLDPDYPAERLAYMLADSGVELLLTQSHLLERLPQAEGV---------------SAIALDSLHLD----SWPSQAPG 1267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 232 IPDKGftDKLFY-IYTSGTTGLPKAAIVVHS----RYYRMAALvyygFRMRPDDIVYDCLPLYHSagniVGIGQC---VL 303
Cdd:PRK05691 1268 LHLHG--DNLAYvIYTSGSTGQPKGVGNTHAalaeRLQWMQAT----YALDDSDVLMQKAPISFD----VSVWECfwpLI 1337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 304 HGMTVVIR---KKFSASRFWDDCIKYNCTIVQYIGELCRYLLNQPprEAESRHKVRM------ALGNGLRQSIwtdfssR 374
Cdd:PRK05691 1338 TGCRLVLAgpgEHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDEP--LAAACTSLRRlfsggeALPAELRNRV------L 1409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 375 FHIPQVA--EFYGATE---------CNCSLGNFdSQVGacgfnsRILSFVypirLVRVNEDTMELIrgpdgvcipcQPGQ 443
Cdd:PRK05691 1410 QRLPQVQlhNRYGPTEtainvthwqCQAEDGER-SPIG------RPLGNV----LCRVLDAELNLL----------PPGV 1468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 444 PGQLVgriIQQDPLRRfdGYLNQ-GANNKKIASDVF-KKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEV 521
Cdd:PRK05691 1469 AGELC---IGGAGLAR--GYLGRpALTAERFVPDPLgEDGARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEI 1543
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 291084711 522 EgtlSRLLQMADVAVYGVEVpgAEGRAGMAAVASPTS----NCDLESFAQTLKKELPLYARP 579
Cdd:PRK05691 1544 Q---ARLLAQPGVAQAAVLV--REGAAGAQLVGYYTGeagqEAEAERLKAALAAELPEYMVP 1600
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
487-614 |
9.71e-05 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 45.54 E-value: 9.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 487 TGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLQMADVAVYGVEVPGAEGRAGMAAVASPTSNCDLESfA 566
Cdd:PRK05620 434 TGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLAVTVLAPGIEPTRET-A 512
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 291084711 567 QTLKKEL----PLYARPIFLRFLPELHKTGTFKFQKTELRK---EG-FDPSVVKDP 614
Cdd:PRK05620 513 ERLRDQLrdrlPNWMLPEYWTFVDEIDKTSVGKFDKKDLRQhlaDGdFEIIKLKGP 568
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
67-258 |
1.23e-04 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 45.54 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 67 RRYLQERKTVPLlFASVVRRHPDKTALifEGTNTHWTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGM 146
Cdd:PRK05691 3714 RDYPLEQSYVRL-FEAQVAAHPQRIAA--SCLDQQWSYAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLLGMIVGS 3790
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 147 AKLGVEAALINTNLRRDALRHCLDTSKARALIFGsemASAVYEIQAILDptlTLFCSGS-----WEpsTVPANtehldpl 221
Cdd:PRK05691 3791 FKAGAGYLPLDPGLPAQRLQRIIELSRTPVLVCS---AACREQARALLD---ELGCANRprllvWE--EVQAG------- 3855
|
170 180 190
....*....|....*....|....*....|....*...
gi 291084711 222 leDAPKHLPSIpdKGFTDKLFY-IYTSGTTGLPKAAIV 258
Cdd:PRK05691 3856 --EVASHNPGI--YSGPDNLAYvIYTSGSTGLPKGVMV 3889
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
73-272 |
1.27e-04 |
|
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.
Pssm-ID: 274582 [Multi-domain] Cd Length: 1389 Bit Score: 45.44 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 73 RKTVPLLFASVVRRHPDKTALI----FEGTNTH---WTFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLG 145
Cdd:TIGR03443 235 RGAIHDIFADNAEKHPDRTCVVetpsFLDPSSKtrsFTYKQINEASNILAHYLLKTGIKRGDVVMIYAYRGVDLVVAVMG 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 146 MAKLGVEAALINTNLRRDALRHCLDTSKARALIfgsemasaVYEIQAILDPTLTLFCSGSWE-PSTVPA----------- 213
Cdd:TIGR03443 315 VLKAGATFSVIDPAYPPARQTIYLSVAKPRALI--------VIEKAGTLDQLVRDYIDKELElRTEIPAlalqddgslvg 386
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 291084711 214 ---NTEHLDPL-----LEDAPKHLPSIPDKGFTdklfYIYTSGTTGLPKAaivVHSRYYrmaALVYY 272
Cdd:TIGR03443 387 gslEGGETDVLapyqaLKDTPTGVVVGPDSNPT----LSFTSGSEGIPKG---VLGRHF---SLAYY 443
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
244-308 |
2.30e-04 |
|
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341256 [Multi-domain] Cd Length: 596 Bit Score: 44.27 E-value: 2.30e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 291084711 244 IYTSGTTGLPKAAIVVHSRYYRMAALVYYGFRMRPDD----IVYDCLPLYHSAGNIVGIGQCVLHGMTV 308
Cdd:cd05933 156 IYTSGTTGMPKGVMLSHDNITWTAKAASQHMDLRPATvgqeSVVSYLPLSHIAAQILDIWLPIKVGGQV 224
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
238-308 |
2.35e-04 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 44.57 E-value: 2.35e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 291084711 238 TDKLFYIYTSGTTGLPKAAIVVH----SRYYRMAALVYYGfrmrPDDIVYDCLPLYHSAGNIVGIGQCVLHGMTV 308
Cdd:PRK06814 793 DDPAVILFTSGSEGTPKGVVLSHrnllANRAQVAARIDFS----PEDKVFNALPVFHSFGLTGGLVLPLLSGVKV 863
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
241-522 |
4.20e-04 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 43.58 E-value: 4.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 241 LFYIYTSGTTGLPKAaiVVHSRYYRMAALVYYGFRMRPDDIVYdclpLYHSAGNIVGIG------QCVLHGMTVV----- 309
Cdd:PTZ00237 257 LYILYTSGTTGNSKA--VVRSNGPHLVGLKYYWRSIIEKDIPT----VVFSHSSIGWVSfhgflyGSLSLGNTFVmfegg 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 310 -IRKKFSASRFWDDCIKYNCTIVQYIGELCRYLLNQPPrEAE--------SRHKVRMALGNGLRQSIWTDFSSRFHIpQV 380
Cdd:PTZ00237 331 iIKNKHIEDDLWNTIEKHKVTHTLTLPKTIRYLIKTDP-EATiirskydlSNLKEIWCGGEVIEESIPEYIENKLKI-KS 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 381 AEFYGATECNCSL----GNFDSQVGACGFNSrilSFVYPIRLvrvNEDTMELirgpdgvcipcqpgqPGQLVGRIIQQDP 456
Cdd:PTZ00237 409 SRGYGQTEIGITYlycyGHINIPYNATGVPS---IFIKPSIL---SEDGKEL---------------NVNEIGEVAFKLP 467
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 291084711 457 LRrfDGYLNQGANNKKIASDVFKKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVE 522
Cdd:PTZ00237 468 MP--PSFATTFYKNDEKFKQLFSKFPGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIE 531
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
482-604 |
4.65e-04 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 43.16 E-value: 4.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 482 DQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLQMADVAVYGVEVPGAEGRAGMAAVASPTSNCD 561
Cdd:PRK07008 408 DGWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLVVVKRPGAEVT 487
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 291084711 562 LESFAQTLKKELPLYARPIFLRFLPELHKTGTFKFQKTELRKE 604
Cdd:PRK07008 488 REELLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKLREQ 530
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
477-605 |
7.22e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 42.33 E-value: 7.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 477 VFKKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLQMADVAVYGVEVPGAEGRAGMAAVASp 556
Cdd:PRK08308 285 VVKMGDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVISH- 363
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 291084711 557 tSNCDLESFAQTLKKELPLYARPIFLRFLPELHKTGTFKFQKTELRKEG 605
Cdd:PRK08308 364 -EEIDPVQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLLELGE 411
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
103-205 |
1.05e-03 |
|
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: 42.06 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 103 TFRQLDDYSSSVANFLQARGLVSGNVVALFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALRHCLDTSKARALIfGSE 182
Cdd:cd05910 4 SFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEAEPDAFI-GIP 82
|
90 100
....*....|....*....|...
gi 291084711 183 MAsavyeiqaiLDPTLTLFCSGS 205
Cdd:cd05910 83 KA---------DEPAAILFTSGS 96
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
451-579 |
3.26e-03 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 40.36 E-value: 3.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 451 IIQQDPLrrFDGYLNQGANNKKIasdvFKKGDQAYLtgdvlvmDELGYLYFRDRTGDTFRWKGENVSTTEVEGTL--SRL 528
Cdd:PRK07445 305 TIQAQSL--ALGYYPQILDSQGI----FETDDLGYL-------DAQGYLHILGRNSQKIITGGENVYPAEVEAAIlaTGL 371
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 291084711 529 LQmaDVAVYGVevpgAEGRAG--MAAVASP-TSNCDLESFAQTLKKELPLYARP 579
Cdd:PRK07445 372 VQ--DVCVLGL----PDPHWGevVTAIYVPkDPSISLEELKTAIKDQLSPFKQP 419
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
438-527 |
7.50e-03 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 39.20 E-value: 7.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084711 438 PCQPGQPGQLVGRiiqqDPLRrFDGYLNQGANNKKiasdVFKKgDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVS 517
Cdd:PRK10946 374 PLPQGEVGRLMTR----GPYT-FRGYYKSPQHNAS----AFDA-NGFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIA 443
|
90
....*....|
gi 291084711 518 TTEVEGTLSR 527
Cdd:PRK10946 444 AEEIENLLLR 453
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
227-290 |
8.48e-03 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.
Pssm-ID: 341250 [Multi-domain] Cd Length: 545 Bit Score: 39.12 E-value: 8.48e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 291084711 227 KHLPSIPDKgftDKLFYI-YTSGTTGLPKAAIVVHSryyRMAALV-------YYGFRMRPDDIVYDCLPLYH 290
Cdd:cd05927 105 KVPPPPPKP---EDLATIcYTSGTTGNPKGVMLTHG---NIVSNVagvfkilEILNKINPTDVYISYLPLAH 170
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