|
Name |
Accession |
Description |
Interval |
E-value |
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
1-652 |
0e+00 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 1185.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 1 MSEILWQPSPERIANTRMDQFRRFINDRYSVQLSDYPALHQWSIDQRPDFWRAIVAFFDVQFRSPPSAVLiEDAEMPSAQ 80
Cdd:PRK03584 1 MGDPLWTPSAERIAASRMTAFIRWLAARRGLSFDDYAALWRWSVEDLEAFWQSVWDFFGVIGSTPYTVVL-AGRRMPGAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 81 WFPGATLNFAEHLLR-RRDDHPAVVAISEDGQREQLTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTLVGMLAT 159
Cdd:PRK03584 80 WFPGARLNYAENLLRhRRDDRPAIIFRGEDGPRRELSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLAT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 160 TSLGAIWSCSSPDFGTQGVIDRFGQIEPKVLITCAGYRYAGKDIDQTAKLNEILARLPSLEQLIIVPYARPQArveDYQT 239
Cdd:PRK03584 160 ASLGAIWSSCSPDFGVQGVLDRFGQIEPKVLIAVDGYRYGGKAFDRRAKVAELRAALPSLEHVVVVPYLGPAA---AAAA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 240 HARVTRWSDFY--PPGGEPEFVAVPFDHPLYILYSSGTTGVPKCIIHGTGGVLLTHLKEHGLHADLSRDDCLFYYTTCGW 317
Cdd:PRK03584 237 LPGALLWEDFLapAEAAELEFEPVPFDHPLWILYSSGTTGLPKCIVHGHGGILLEHLKELGLHCDLGPGDRFFWYTTCGW 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 318 MMWNWLVSVLAIGATAVLYDGSPFHPGPERLIDLIDAEKISVFGTSPKFLATLEKAGLQPRLSHDLGSLKGLISTGSPLS 397
Cdd:PRK03584 317 MMWNWLVSGLLVGATLVLYDGSPFYPDPNVLWDLAAEEGVTVFGTSAKYLDACEKAGLVPGETHDLSALRTIGSTGSPLP 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 398 PQSYDYVYREIKGELCLSSMSGGTDIVSCFVIGNPVLPVRRGEMQCKSLAMAIEVWDDQGQPLVGEKGELVCTRHFPAMP 477
Cdd:PRK03584 397 PEGFDWVYEHVKADVWLASISGGTDICSCFVGGNPLLPVYRGEIQCRGLGMAVEAWDEDGRPVVGEVGELVCTKPFPSMP 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 478 IGLWNDPDRQKLRASYFSQFPGVWAQGDYAEQRPNGSLLIHGRSDAVLNPGGVRIGTAEIYRQVEKVPQVQESLAIGQRW 557
Cdd:PRK03584 477 LGFWNDPDGSRYRDAYFDTFPGVWRHGDWIEITEHGGVVIYGRSDATLNRGGVRIGTAEIYRQVEALPEVLDSLVIGQEW 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 558 QD-DVRVVLFVRLNDGVELDEALEQQIRQVIRANTTPRHVPAKILAVTDIPRTISGKIVELAVRNVVHGEPVK---NTDA 633
Cdd:PRK03584 557 PDgDVRMPLFVVLAEGVTLDDALRARIRTTIRTNLSPRHVPDKIIAVPDIPRTLSGKKVELPVKKLLHGRPVKkavNRDA 636
|
650
....*....|....*....
gi 799207711 634 LANPQALEQFRDRPELTER 652
Cdd:PRK03584 637 LANPEALDWFADLAELRAA 655
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
18-643 |
0e+00 |
|
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); 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. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.
Pssm-ID: 341265 [Multi-domain] Cd Length: 629 Bit Score: 1018.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 18 MDQFRRFINDRYSVQLSDYPALHQWSIDQRPDFWRAIVAFFDVQFRSPPSAVLIEDAEMPSAQWFPGATLNFAEHLLRRR 97
Cdd:cd05943 1 MDAFRRWVNARHGLSLADYAALHRWSVDDPGAFWAAVWDFSGVRGSKPYDVVVVSGRIMPGARWFPGARLNYAENLLRHA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 98 D-DHPAVVAISEDGQREQLTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTLVGMLATTSLGAIWSCSSPDFGTQ 176
Cdd:cd05943 81 DaDDPAAIYAAEDGERTEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPDFGVP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 177 GVIDRFGQIEPKVLITCAGYRYAGKDIDQTAKLNEILARLPSLEQLIIVPYARPQARvEDYQTHARVTRWSDFY--PPGG 254
Cdd:cd05943 161 GVLDRFGQIEPKVLFAVDAYTYNGKRHDVREKVAELVKGLPSLLAVVVVPYTVAAGQ-PDLSKIAKALTLEDFLatGAAG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 255 EPEFVAVPFDHPLYILYSSGTTGVPKCIIHGTGGVLLTHLKEHGLHADLSRDDCLFYYTTCGWMMWNWLVSVLAIGATAV 334
Cdd:cd05943 240 ELEFEPLPFDHPLYILYSSGTTGLPKCIVHGAGGTLLQHLKEHILHCDLRPGDRLFYYTTCGWMMWNWLVSGLAVGATIV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 335 LYDGSPFHPGPERLIDLIDAEKISVFGTSPKFLATLEKAGLQPRLSHDLGSLKGLISTGSPLSPQSYDYVYREIKGELCL 414
Cdd:cd05943 320 LYDGSPFYPDTNALWDLADEEGITVFGTSAKYLDALEKAGLKPAETHDLSSLRTILSTGSPLKPESFDYVYDHIKPDVLL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 415 SSMSGGTDIVSCFVIGNPVLPVRRGEMQCKSLAMAIEVWDDQGQPLVGEKGELVCTRHFPAMPIGLWNDPDRQKLRASYF 494
Cdd:cd05943 400 ASISGGTDIISCFVGGNPLLPVYRGEIQCRGLGMAVEAFDEEGKPVWGEKGELVCTKPFPSMPVGFWNDPDGSRYRAAYF 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 495 SQFPGVWAQGDYAEQRPNGSLLIHGRSDAVLNPGGVRIGTAEIYRQVEKVPQVQESLAIGQRWQD-DVRVVLFVRLNDGV 573
Cdd:cd05943 480 AKYPGVWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDgDERVILFVKLREGV 559
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 574 ELDEALEQQIRQVIRANTTPRHVPAKILAVTDIPRTISGKIVELAVRNVVHGEPVKNTDALANPQALEQF 643
Cdd:cd05943 560 ELDDELRKRIRSTIRSALSPRHVPAKIIAVPDIPRTLSGKKVEVAVKKIIAGRPVKNAGALANPESLDLF 629
|
|
| ac_ac_CoA_syn |
TIGR01217 |
acetoacetyl-CoA synthase; This enzyme catalyzes the first step of the mevalonate pathway of ... |
3-649 |
0e+00 |
|
acetoacetyl-CoA synthase; This enzyme catalyzes the first step of the mevalonate pathway of IPP biosynthesis. Most bacteria do not use this pathway, but rather the deoxyxylulose pathway. [Central intermediary metabolism, Other]
Pssm-ID: 273507 [Multi-domain] Cd Length: 652 Bit Score: 812.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 3 EILWQPSPERIANTRMDQFRRFINDRYSVQLSDYPALHQWSIDQRPDFWRAIVAFFDVQFRSPPSAVLiEDAEMPSAQWF 82
Cdd:TIGR01217 4 QPLWQPDAQRIAQARMTRFQAWAGEHHGAAEGGYDALHRWSVDELDTFWKAVWEWFDVRFSTPCARVV-DDRTMPGAQWF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 83 PGATLNFAEHLLRRRDDHPAVVAISEDGQREQLTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTLVGMLATTSL 162
Cdd:TIGR01217 83 PGARLNYAENLLRAAGTEPALLYVDETHEPAPVTWAELRRQVASLAAALRALGVRPGDRVSGYLPNIPQAVVAMLATASV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 163 GAIWSCSSPDFGTQGVIDRFGQIEPKVLITCAGYRYAGKDIDQTAKLNEILARLPSLEQLIIVPYARPQARvEDYQTHAR 242
Cdd:TIGR01217 163 GAIWSSCSPDFGARGVLDRFQQIEPKLLFTVDGYRYNGKEHDRRDKVAEVRKELPTLRAVVHIPYLGPRET-EAPKIDGA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 243 VTrWSDFY--PPGGEPEFVAVPFDHPLYILYSSGTTGVPKCIIHGTGGVLLTHLKEHGLHADLSRDDCLFYYTTCGWMMW 320
Cdd:TIGR01217 242 LD-LEDFTaaAQAAELVFEQLPFDHPLWILFSSGTTGLPKCIVHSAGGTLVQHLKEHGLHCDLGPGDRLFYYTTTGWMMW 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 321 NWLVSVLAIGATAVLYDGSPFHPGPERLIDLIDAEKISVFGTSPKFLATLEKAGLQPRLSHDLGSLKGLISTGSPLSPQS 400
Cdd:TIGR01217 321 NWLVSGLATGATLVLYDGSPGFPATNVLWDIAERTGATLFGTSAKYVMACRKAGVHPARTHDLSALQCVASTGSPLPPDG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 401 YDYVYREIKGELCLSSMSGGTDIVSCFVIGNPVLPVRRGEMQCKSLAMAIEVWDDQGQPLVGEKGELVCTRHFPAMPIGL 480
Cdd:TIGR01217 401 FRWVYDEIKADVWLASISGGTDICSCFAGANPTLPVHIGEIQAPGLGTAVQSWDPEGKPVTGEVGELVCTNPMPSMPIRF 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 481 WNDPDRQKLRASYFSQFPGVWAQGDYAEQRPNGSLLIHGRSDAVLNPGGVRIGTAEIYRQVEKVPQVQESLAIGQRWQD- 559
Cdd:TIGR01217 481 WNDPDGSKYRDAYFDTYPGVWRHGDWITLTPRGGIVIHGRSDSTLNPQGVRMGSAEIYNAVERLDEVRESLCIGQEQPDg 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 560 DVRVVLFVRLNDGVELDEALEQQIRQVIRANTTPRHVPAKILAVTDIPRTISGKIVELAVRNVVHGEPVKNTDALANPQA 639
Cdd:TIGR01217 561 GYRVVLFVHLAPGATLDDALLDRIKRTIRAGLSPRHVPDEIIEVPGIPHTLTGKRVEVAVKRVLQGTPVDNPGAIDNPEL 640
|
650
....*....|
gi 799207711 640 LEQFRDRPEL 649
Cdd:TIGR01217 641 LDLYEELAEL 650
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
80-645 |
0e+00 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 686.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 80 QWFPGATLNFAEHLLRR----RDDHPAVVAISEDGQREQLTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTLVG 155
Cdd:COG0365 1 RWFVGGRLNIAYNCLDRhaegRGDKVALIWEGEDGEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 156 MLATTSLGAIWSCSSPDFGTQGVIDRFGQIEPKVLITCAGYRYAGKDIDQTAKLNEILARLPSLEQLIIVPYARPQARVE 235
Cdd:COG0365 81 MLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADGGLRGGKVIDLKEKVDEALEELPSLEHVIVVGRTGADVPME 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 236 DyqtharVTRWSDFYP-PGGEPEFVAVPFDHPLYILYSSGTTGVPKCIIHGTGGVLLTHLKEHGLHADLSRDDCLFYYTT 314
Cdd:COG0365 161 G------DLDWDELLAaASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYVLDLKPGDVFWCTAD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 315 CGWMM--WNWLVSVLAIGATAVLYDGSPFHPGPERLIDLIDAEKISVFGTSPKFLATLEKAGLQPRLSHDLGSLKGLIST 392
Cdd:COG0365 235 IGWATghSYIVYGPLLNGATVVLYEGRPDFPDPGRLWELIEKYGVTVFFTAPTAIRALMKAGDEPLKKYDLSSLRLLGSA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 393 GSPLSPQSYDYVYREIKgeLCLSSMSGGTDIVSCFVIGNPVLPVRRGEMQCKSLAMAIEVWDDQGQPL-VGEKGELVCTR 471
Cdd:COG0365 315 GEPLNPEVWEWWYEAVG--VPIVDGWGQTETGGIFISNLPGLPVKPGSMGKPVPGYDVAVVDEDGNPVpPGEEGELVIKG 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 472 HFPAMPIGLWNDPDRQklRASYFSQFPGVWAQGDYAEQRPNGSLLIHGRSDAVLNPGGVRIGTAEIYRQVEKVPQVQESL 551
Cdd:COG0365 393 PWPGMFRGYWNDPERY--RETYFGRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAA 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 552 AIGQRWQD-DVRVVLFVRLNDGVELDEALEQQIRQVIRANTTPRHVPAKILAVTDIPRTISGKIVELAVRNVVHGEPVKN 630
Cdd:COG0365 471 VVGVPDEIrGQVVKAFVVLKPGVEPSDELAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLRKIAEGRPLGD 550
|
570
....*....|....*
gi 799207711 631 TDALANPQALEQFRD 645
Cdd:COG0365 551 TSTLEDPEALDEIKE 565
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
30-637 |
9.19e-119 |
|
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: 366.82 E-value: 9.19e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 30 SVQLSDYPALHQWSIDQRPDFWRAIVAFFDVQFRSPPSAVLIEDAEMPSAQWFPGATLNFAEHLLRR----RDDHPAVVA 105
Cdd:cd05968 3 SLGIPDLEAFLERSAEDNAWFWGEFVKDVGIEWYEPPYQTLDLSGGKPWAAWFVGGRMNIVEQLLDKwladTRTRPALRW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 106 ISEDGQREQLTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTLVGMLATTSLGAIWSCSSPDFGTQGVIDRFGQI 185
Cdd:cd05968 83 EGEDGTSRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 186 EPKVLITCAGYRYAGKDIDQTAKLNEILARLPSLEQLIIVPYARpqarvEDYQTHARVTRWSDFYPPGGEPEFVAVPFDH 265
Cdd:cd05968 163 EAKALITADGFTRRGREVNLKEEADKACAQCPTVEKVVVVRHLG-----NDFTPAKGRDLSYDEEKETAGDGAERTESED 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 266 PLYILYSSGTTGVPKCIIHGTGGVLLTHLKEHGLHADLSRDDCLFYYTTCGWMMWNWLV-SVLAIGATAVLYDGSPFHPG 344
Cdd:cd05968 238 PLMIIYTSGTTGKPKGTVHVHAGFPLKAAQDMYFQFDLKPGDLLTWFTDLGWMMGPWLIfGGLILGATMVLYDGAPDHPK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 345 PERLIDLIDAEKISVFGTSPKFLATLEKAGLQPRLSHDLGSLKGLISTGSPLSPQSYDYVYREI-KGELCLSSMSGGTDI 423
Cdd:cd05968 318 ADRLWRMVEDHEITHLGLSPTLIRALKPRGDAPVNAHDLSSLRVLGSTGEPWNPEPWNWLFETVgKGRNPIINYSGGTEI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 424 VSCFVIGNPVLPVRRGEMQCKSLAMAIEVWDDQGQPLVGEKGELVCTRHFPAMPIGLWNDPDRqkLRASYFSQFPGVWAQ 503
Cdd:cd05968 398 SGGILGNVLIKPIKPSSFNGPVPGMKADVLDESGKPARPEVGELVLLAPWPGMTRGFWRDEDR--YLETYWSRFDNVWVH 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 504 GDYAEQRPNGSLLIHGRSDAVLNPGGVRIGTAEIYRQVEKVPQVQESLAIGQrwQDDVR---VVLFVRLNDGVELDEALE 580
Cdd:cd05968 476 GDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGV--PHPVKgeaIVCFVVLKPGVTPTEALA 553
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 799207711 581 QQIRQVIRANTTPRHVPAKILAVTDIPRTISGKIVELAVRNVVHGEPVKNTDALANP 637
Cdd:cd05968 554 EELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIRAAYLGKELGDLSSLENP 610
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
36-615 |
9.75e-98 |
|
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: 311.43 E-value: 9.75e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 36 YPALHQWSIDQRPDFWRAIVAFFDVQFRSPPSAVLIEDAEMPSAQWFPGATLNFA----EHLLRRRDDHPAVVAISEDG- 110
Cdd:cd17634 1 YETKYRQSINDPDTFWGEAGKILDWITPYQKVKNTSFAPGAPSIKWFEDATLNLAanalDRHLRENGDRTAIIYEGDDTs 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 111 QREQLTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTLVGMLATTSLGAIWSCSSPDFGTQGVIDRFGQIEPKVL 190
Cdd:cd17634 81 QSRTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 191 ITCAGYRYAGKDIDQTAKLNEIL-ARLPSLEQLIIVpyARPQArveDYQ-THARVTRWSDFY---PPGGEPEFVAvPFDh 265
Cdd:cd17634 161 ITADGGVRAGRSVPLKKNVDDALnPNVTSVEHVIVL--KRTGS---DIDwQEGRDLWWRDLIakaSPEHQPEAMN-AED- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 266 PLYILYSSGTTGVPKCIIHGTGGVLLTHLKEHGLHADLSRDDCLFYYTTCGWMMWN-WLV-SVLAIGATAVLYDGSPFHP 343
Cdd:cd17634 234 PLFILYTSGTTGKPKGVLHTTGGYLVYAATTMKYVFDYGPGDIYWCTADVGWVTGHsYLLyGPLACGATTLLYEGVPNWP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 344 GPERLIDLIDAEKISVFGTSPKFLATLEKAGLQPRLSHDLGSLKGLISTGSPLSPQSYDYVYREIKGELC-LSSMSGGTD 422
Cdd:cd17634 314 TPARMWQVVDKHGVNILYTAPTAIRALMAAGDDAIEGTDRSSLRILGSVGEPINPEAYEWYWKKIGKEKCpVVDTWWQTE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 423 ivscfvIGNPVLPVRRGEMQCKS-------LAMAIEVWDDQGQPL-VGEKGELVCTRHFPAMPIGLWNDPDRQKlrASYF 494
Cdd:cd17634 394 ------TGGFMITPLPGAIELKAgsatrpvFGVQPAVVDNEGHPQpGGTEGNLVITDPWPGQTRTLFGDHERFE--QTYF 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 495 SQFPGVWAQGDYAEQRPNGSLLIHGRSDAVLNPGGVRIGTAEIYRQVEKVPQVQESLAIGQRwqDDV---RVVLFVRLND 571
Cdd:cd17634 466 STFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIP--HAIkgqAPYAYVVLNH 543
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 799207711 572 GVELDEALEQQIRQVIRANTTPRHVPAKILAVTDIPRTISGKIV 615
Cdd:cd17634 544 GVEPSPELYAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKIM 587
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
35-636 |
1.06e-93 |
|
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: 301.40 E-value: 1.06e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 35 DYPALHQWSIDQRPDFWRAIVAFFDvqFRSPPSAVLIEDAEMPSAQWFPGATLNFAE-----HLLRRRDdHPAVVAISED 109
Cdd:cd05966 2 QYKELYKQSIEDPEEFWGEIAKELD--WFKPWDKVLDWSKGPPFIKWFEGGKLNISYncldrHLKERGD-KVAIIWEGDE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 110 G-QREQLTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTLVGMLATTSLGAIWSCSSPDFGTQGVIDRFGQIEPK 188
Cdd:cd05966 79 PdQSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFAGFSAESLADRINDAQCK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 189 VLITCAGYRYAGKDIDQTAKLNEILARLPSLEQLIIVPYA-RPQARVEDyqthaRVTRWSDF---YPPGGEPEFVAVpfD 264
Cdd:cd05966 159 LVITADGGYRGGKVIPLKEIVDEALEKCPSVEKVLVVKRTgGEVPMTEG-----RDLWWHDLmakQSPECEPEWMDS--E 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 265 HPLYILYSSGTTGVPKCIIHGTGGVLLTHLKEHGLHADLSRDDclFYYTT--CGWMM-WNWLV-SVLAIGATAVLYDGSP 340
Cdd:cd05966 232 DPLFILYTSGSTGKPKGVVHTTGGYLLYAATTFKYVFDYHPDD--IYWCTadIGWITgHSYIVyGPLANGATTVMFEGTP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 341 FHPGPERLIDLIDAEKISVFGTSPKFLATLEKAGLQPRLSHDLGSLKGLISTGSPLSPQSYDYVYREIKGELC------- 413
Cdd:cd05966 310 TYPDPGRYWDIVEKHKVTIFYTAPTAIRALMKFGDEWVKKHDLSSLRVLGSVGEPINPEAWMWYYEVIGKERCpivdtww 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 414 --------LSSMSGGTDIVScfviGNPVLPVrrgemqcksLAMAIEVWDDQGQPLVGE-KGELVCTRHFPAMPIGLWNDP 484
Cdd:cd05966 390 qtetggimITPLPGATPLKP----GSATRPF---------FGIEPAILDEEGNEVEGEvEGYLVIKRPWPGMARTIYGDH 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 485 DRqkLRASYFSQFPGVWAQGDYAEQRPNGSLLIHGRSDAVLNPGGVRIGTAEIYRQVEKVPQVQESLAIGQrwQDDVR-- 562
Cdd:cd05966 457 ER--YEDTYFSKFPGYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGR--PHDIKge 532
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 799207711 563 -VVLFVRLNDGVELDEALEQQIRQVIRANTTPRHVPAKILAVTDIPRTISGKIVELAVRNVVHG-EPVKNTDALAN 636
Cdd:cd05966 533 aIYAFVTLKDGEEPSDELRKELRKHVRKEIGPIATPDKIQFVPGLPKTRSGKIMRRILRKIAAGeEELGDTSTLAD 608
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
8-645 |
1.59e-79 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 264.70 E-value: 1.59e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 8 PSPERIANTRMDqfrrfindrysvqLSDYPALHQWSIDQRPDFWRAIVAFFDvqFRSPPSAVLieDAEMPSAQWFPGATL 87
Cdd:PRK00174 4 PPAEFAANALID-------------MEQYKALYQESVEDPEGFWAEQAKRLD--WFKPFDTVL--DWNAPFIKWFEDGEL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 88 NFA-----EHLLRRRDDhpavVAI---SED-GQREQLTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTLVGMLA 158
Cdd:PRK00174 67 NVSyncldRHLKTRGDK----VAIiweGDDpGDSRKITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 159 TTSLGAIWSCSSPDFGTQGVIDRFGQIEPKVLITC-AGYRyAGKDIDQTAKLNEILARLPSLEQLIIVPyaRPQARVE-- 235
Cdd:PRK00174 143 CARIGAVHSVVFGGFSAEALADRIIDAGAKLVITAdEGVR-GGKPIPLKANVDEALANCPSVEKVIVVR--RTGGDVDwv 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 236 ---DYQTHARVTRWSDFYPPggepefvaVPFD--HPLYILYSSGTTGVPKCIIHGTGGVLLTHLKEHGLHADLSRDDclF 310
Cdd:PRK00174 220 egrDLWWHELVAGASDECEP--------EPMDaeDPLFILYTSGSTGKPKGVLHTTGGYLVYAAMTMKYVFDYKDGD--V 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 311 YYTTC--GWmmwnwlvsV----------LAIGATAVLYDGSPFHPGPERLIDLIDAEKISVFGTSPKFLATLEKAGLQPR 378
Cdd:PRK00174 290 YWCTAdvGW--------VtghsyivygpLANGATTLMFEGVPNYPDPGRFWEVIDKHKVTIFYTAPTAIRALMKEGDEHP 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 379 LSHDLGSLKGLISTGSPLSPQSYDYVYREIKGELC---------------LSSMSGGTDIV--SCfviGNPVLPVrrgem 441
Cdd:PRK00174 362 KKYDLSSLRLLGSVGEPINPEAWEWYYKVVGGERCpivdtwwqtetggimITPLPGATPLKpgSA---TRPLPGI----- 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 442 qckslaMAiEVWDDQGQPL-VGEKGELVCTRHFPAMPIGLWNDPDRqkLRASYFSQFPGVWAQGDYAEQRPNGSLLIHGR 520
Cdd:PRK00174 434 ------QP-AVVDEEGNPLeGGEGGNLVIKDPWPGMMRTIYGDHER--FVKTYFSTFKGMYFTGDGARRDEDGYYWITGR 504
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 521 SDAVLNPGGVRIGTAEIYRQVEKVPQVQESLAIGQrwQDDVR---VVLFVRLNDGVELDEALEQQIRQVIRANTTPRHVP 597
Cdd:PRK00174 505 VDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGR--PDDIKgqgIYAFVTLKGGEEPSDELRKELRNWVRKEIGPIAKP 582
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 799207711 598 AKILAVTDIPRTISGKIVELAVRNVVHGEPVK-NTDALANPQALEQFRD 645
Cdd:PRK00174 583 DVIQFAPGLPKTRSGKIMRRILRKIAEGEEILgDTSTLADPSVVEKLIE 631
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
36-642 |
8.59e-72 |
|
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: 243.76 E-value: 8.59e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 36 YPALHQWSIDQRPDFWRAIVAFFDVQfrSPPSAVLiEDAEMPSAQWFPGATLNFA-----EHLLRRRDDHPAVVAIS-ED 109
Cdd:cd05967 1 YEEVYARSIAEPEAFWAEQARLIDWF--KPPEKIL-DNSNPPFTRWFVGGRLNTCynaldRHVEAGRGDQIALIYDSpVT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 110 GQREQLTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTLVGMLATTSLGAIWSCSSPDFGTQGVIDRFGQIEPKV 189
Cdd:cd05967 78 GTERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGFAAKELASRIDDAKPKL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 190 LITCAGYRYAGKDIDQTAKLNEIL--ARLPSLEQLIivpYARPQARVeDYQTHARVTRWSDFYPPGGEPEFVAVPFDHPL 267
Cdd:cd05967 158 IVTASCGIEPGKVVPYKPLLDKALelSGHKPHHVLV---LNRPQVPA-DLTKPGRDLDWSELLAKAEPVDCVPVAATDPL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 268 YILYSSGTTGVPKCIIHGTGG--VLLTHLKEH--GLHAdlsrDDCLFYYTTCGWMMWNWLV--SVLAIGATAVLYDGSP- 340
Cdd:cd05967 234 YILYTSGTTGKPKGVVRDNGGhaVALNWSMRNiyGIKP----GDVWWAASDVGWVVGHSYIvyGPLLHGATTVLYEGKPv 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 341 FHPGPERLIDLIDAEKISVFGTSPKFLATLEKAGLQPRL--SHDLGSLKGLISTGSPLSPQSYDYVyREIKGELCL---- 414
Cdd:cd05967 310 GTPDPGAFWRVIEKYQVNALFTAPTAIRAIRKEDPDGKYikKYDLSSLRTLFLAGERLDPPTLEWA-ENTLGVPVIdhww 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 415 SSMSGgtdivSCfVIGNPV----LPVRRGEMQCKSLAMAIEVWDDQGQPL-VGEKGELVCTRHFP--AMPiGLWNDPDRq 487
Cdd:cd05967 389 QTETG-----WP-ITANPVglepLPIKAGSPGKPVPGYQVQVLDEDGEPVgPNELGNIVIKLPLPpgCLL-TLWKNDER- 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 488 kLRASYFSQFPGVWAQGDYAEQRPNGSLLIHGRSDAVLNPGGVRIGTAEIYRQVEKVPQVQESLAIGQRwqDDVR--VVL 565
Cdd:cd05967 461 -FKKLYLSKFPGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVR--DELKgqVPL 537
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 799207711 566 -FVRLNDGVELD-EALEQQIRQVIRANTTPRHVPAKILAVTDIPRTISGKIVELAVRNVVHGEPVKNTDALANPQALEQ 642
Cdd:cd05967 538 gLVVLKEGVKITaEELEKELVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTLRKIADGEDYTIPSTIEDPSVLDE 616
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
36-643 |
3.40e-59 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 210.52 E-value: 3.40e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 36 YPALHQWSIDQRPDFWRAIVAFFDVQFRSPPSAVLIEDAEMP----SAQWFPGATLNFAEHLLRRR------DDHPAVVA 105
Cdd:PLN02654 32 YMEMYKRSVDDPAGFWSDIASQFYWKQKWEGDEVCSENLDVRkgpiSIEWFKGGKTNICYNCLDRNveagngDKIAIYWE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 106 ISEDGQREQLTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTLVGMLATTSLGAIWSCSSPDFGTQGVIDRFGQI 185
Cdd:PLN02654 112 GNEPGFDASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQRIVDC 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 186 EPKVLITCAGYRYAGKDIDQTAKLNEILARlpSLEQLIIV----PYARPQA--RVEDYQTHARVTRWSDF---YPPGGEP 256
Cdd:PLN02654 192 KPKVVITCNAVKRGPKTINLKDIVDAALDE--SAKNGVSVgiclTYENQLAmkREDTKWQEGRDVWWQDVvpnYPTKCEV 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 257 EFVAVpfDHPLYILYSSGTTGVPKCIIHGTGGVLLTHLKEHGLHADLSRDDCLFYYTTCGWMMWNWLVSV--LAIGATAV 334
Cdd:PLN02654 270 EWVDA--EDPLFLLYTSGSTGKPKGVLHTTGGYMVYTATTFKYAFDYKPTDVYWCTADCGWITGHSYVTYgpMLNGATVL 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 335 LYDGSPFHPGPERLIDLIDAEKISVFGTSPKFLATLEKAGLQPRLSHDLGSLKGLISTGSPLSPQSYDYVYREIKGELCL 414
Cdd:PLN02654 348 VFEGAPNYPDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGDEYVTRHSRKSLRVLGSVGEPINPSAWRWFFNVVGDSRCP 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 415 SSMSGGTDIVSCFVIgNPV---LPVRRGEMQCKSLAMAIEVWDDQGQPLVGE-KGELVCTRHFPAMPIGLWNDPDRQKlr 490
Cdd:PLN02654 428 ISDTWWQTETGGFMI-TPLpgaWPQKPGSATFPFFGVQPVIVDEKGKEIEGEcSGYLCVKKSWPGAFRTLYGDHERYE-- 504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 491 ASYFSQFPGVWAQGDYAEQRPNGSLLIHGRSDAVLNPGGVRIGTAEIYRQVEKVPQVQESLAIGQrwQDDVR---VVLFV 567
Cdd:PLN02654 505 TTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGI--EHEVKgqgIYAFV 582
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 799207711 568 RLNDGVELDEALEQQIRQVIRANTTPRHVPAKILAVTDIPRTISGKIVELAVRNVVHG--EPVKNTDALANPQALEQF 643
Cdd:PLN02654 583 TLVEGVPYSEELRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRKIASRqlDELGDTSTLADPGVVDQL 660
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
89-614 |
5.59e-54 |
|
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: 191.18 E-value: 5.59e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 89 FAEHLLRRRDDHPAVVAISEDGQReqLTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTLVGMLATTSLGAIWSC 168
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGRR--LTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 169 SSPDFGTQGVIDRFGQIEPKVLITCagyryagkdidqtaklneilarlpsleqliivpyarpqarvedyqtharvtrwsd 248
Cdd:COG0318 79 LNPRLTAEELAYILEDSGARALVTA------------------------------------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 249 fyppggepefvavpfdhplYILYSSGTTGVPKciihgtgGVLLTH------LKEHGLHADLSRDDCL-----FYYTTcGW 317
Cdd:COG0318 104 -------------------LILYTSGTTGRPK-------GVMLTHrnllanAAAIAAALGLTPGDVVlvalpLFHVF-GL 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 318 MMWnwLVSVLAIGATAVLYDGspFHPgpERLIDLIDAEKISVFGTSPKFLATLEKAGLQPRlsHDLGSLKGLISTGSPLS 397
Cdd:COG0318 157 TVG--LLAPLLAGATLVLLPR--FDP--ERVLELIERERVTVLFGVPTMLARLLRHPEFAR--YDLSSLRLVVSGGAPLP 228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 398 PQsydyVYREIKGELclssmsgGTDIV--------SCFVIGNPVLPVRRGEMQC-KSLA-MAIEVWDDQGQPL-VGEKGE 466
Cdd:COG0318 229 PE----LLERFEERF-------GVRIVegygltetSPVVTVNPEDPGERRPGSVgRPLPgVEVRIVDEDGRELpPGEVGE 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 467 LvCTRHfPAMPIGLWNDPDRqklRASYFSQfpGVWAQGDYAEQRPNGSLLIHGRSDAVLNPGGVRIGTAEIYRQVEKVPQ 546
Cdd:COG0318 298 I-VVRG-PNVMKGYWNDPEA---TAEAFRD--GWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPG 370
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 799207711 547 VQESLAIG---QRWQDdvRVVLFVRLNDGVELDEAleqQIRQVIRANTTPRHVPAKILAVTDIPRTISGKI 614
Cdd:COG0318 371 VAEAAVVGvpdEKWGE--RVVAFVVLRPGAELDAE---ELRAFLRERLARYKVPRRVEFVDELPRTASGKI 436
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
35-646 |
6.35e-53 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 192.47 E-value: 6.35e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 35 DYPALHQWSIDQRPDFWRAIVAFFDvqFRSPPSAVLiEDAEMPSAQWFPGATLNFA-----EHLLRRRDDhPAVVAIS-E 108
Cdd:PRK10524 3 SYSEFYQRSIDDPEAFWAEQARRID--WQTPFTQVL-DYSNPPFARWFVGGRTNLChnavdRHLAKRPEQ-LALIAVStE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 109 DGQREQLTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTLVGMLATTSLGAIWSCSSPDFGTQGVIDRFGQIEPK 188
Cdd:PRK10524 79 TDEERTYTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLACARIGAIHSVVFGGFASHSLAARIDDAKPV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 189 VLITC-AGYRyAGKDIDQTAKLNEI--LARLPSLEQLII----VPYARPQARVEDYQT------HARV-TRWsdfyppgg 254
Cdd:PRK10524 159 LIVSAdAGSR-GGKVVPYKPLLDEAiaLAQHKPRHVLLVdrglAPMARVAGRDVDYATlraqhlGARVpVEW-------- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 255 epefvaVPFDHPLYILYSSGTTGVPKCIIHGTGG--VLLTHLKEHglhadlsrddclFYYTTCGWMMW-----NWLV--- 324
Cdd:PRK10524 230 ------LESNEPSYILYTSGTTGKPKGVQRDTGGyaVALATSMDT------------IFGGKAGETFFcasdiGWVVghs 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 325 ----SVLAIGATAVLYDGSPFHPGPERLIDLIDAEKISVFGTSPKFLATLEKAGLQPRLSHDLGSLKGLISTGSPLSPQS 400
Cdd:PRK10524 292 yivyAPLLAGMATIMYEGLPTRPDAGIWWRIVEKYKVNRMFSAPTAIRVLKKQDPALLRKHDLSSLRALFLAGEPLDEPT 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 401 YDYVYREIK------------GELCLSSMSGGTDIVSCFviGNPVLPVrrgemqcksLAMAIEVWDDQ-GQPL-VGEKGE 466
Cdd:PRK10524 372 ASWISEALGvpvidnywqtetGWPILAIARGVEDRPTRL--GSPGVPM---------YGYNVKLLNEVtGEPCgPNEKGV 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 467 LVCTrhfPAMPIG----LWNDPDRqkLRASYFSQF-PGVWAQGDYAEQRPNGSLLIHGRSDAVLNPGGVRIGTAEIYRQV 541
Cdd:PRK10524 441 LVIE---GPLPPGcmqtVWGDDDR--FVKTYWSLFgRQVYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESI 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 542 EKVPQVQESLAIGQrwQDDVR---VVLFVRLNDGVELDE-----ALEQQIRQVIRANTTPRHVPAKILAVTDIPRTISGK 613
Cdd:PRK10524 516 SSHPAVAEVAVVGV--KDALKgqvAVAFVVPKDSDSLADrearlALEKEIMALVDSQLGAVARPARVWFVSALPKTRSGK 593
|
650 660 670
....*....|....*....|....*....|...
gi 799207711 614 IVELAVRNVVHGEPVKNTDALANPQALEQFRDR 646
Cdd:PRK10524 594 LLRRAIQAIAEGRDPGDLTTIEDPAALQQIRQA 626
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
265-614 |
1.51e-47 |
|
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: 170.54 E-value: 1.51e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 265 HPLYILYSSGTTGVPKCIIHGTGGvLLTHLKEHGLHADLSRDDCLFYYT-TCGWMMWNWLVSVLAIGATAVLYDGSPfhp 343
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRN-LLAAAAALAASGGLTEGDVFLSTLpLFHIGGLFGLLGALLAGGTVVLLPKFD--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 344 gPERLIDLIDAEKISVFGTSPKFLATLEKAGLQPRlsHDLGSLKGLISTGSPLSPQSYDYVYREIKGELclSSMSGGTDI 423
Cdd:cd04433 77 -PEAALELIEREKVTILLGVPTLLARLLKAPESAG--YDLSSLRALVSGGAPLPPELLERFEEAPGIKL--VNGYGLTET 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 424 VSCFVIGNPVLPVRR-GEMQCKSLAMAIEVWDDQGQPL-VGEKGELvCTRHfPAMPIGLWNDPDrqklrASYFSQFPGVW 501
Cdd:cd04433 152 GGTVATGPPDDDARKpGSVGRPVPGVEVRIVDPDGGELpPGEIGEL-VVRG-PSVMKGYWNNPE-----ATAAVDEDGWY 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 502 AQGDYAEQRPNGSLLIHGRSDAVLNPGGVRIGTAEIYRQVEKVPQVQESLAIG---QRWQDdvRVVLFVRLNDGVELDEA 578
Cdd:cd04433 225 RTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGvpdPEWGE--RVVAVVVLRPGADLDAE 302
|
330 340 350
....*....|....*....|....*....|....*.
gi 799207711 579 leqQIRQVIRANTTPRHVPAKILAVTDIPRTISGKI 614
Cdd:cd04433 303 ---ELRAHVRERLAPYKVPRRVVFVDALPRTASGKI 335
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
6-620 |
1.13e-46 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 176.04 E-value: 1.13e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 6 WQPSPERIANTRMDQF-----RRFINDRYSVQLSDYPALHQWSIDQRPDFWRAIVAFFDVQFRSPPSAVLIEDAEM-PSA 79
Cdd:PLN03052 87 WFPSPEIAKLTNLGRLleargKELLGSKYKDPISSFSEFQRFSVENPEVYWSIVLDELSLVFSVPPRCILDTSDESnPGG 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 80 QWFPGATLNFAEHLL----RRRDDHPAVVAISE---DGQREQLTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQT 152
Cdd:PLN03052 167 QWLPGAVLNVAECCLtpkpSKTDDSIAIIWRDEgsdDLPVNRMTLSELRSQVSRVANALDALGFEKGDAIAIDMPMNVHA 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 153 LVGMLATTSLGAIWSCSSPDFGTQGVIDRFGQIEPKVLITCAGYRYAGKDIDQTAKLNEILAR----LPSLEQLIIVPYA 228
Cdd:PLN03052 247 VIIYLAIILAGCVVVSIADSFAPSEIATRLKISKAKAIFTQDVIVRGGKSIPLYSRVVEAKAPkaivLPADGKSVRVKLR 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 229 RPQARVEDYQTHARVTRWSDFYPPggepefVAVPFDHPLYILYSSGTTGVPKCI--IHgtggvlLTHLK---EHGLHADL 303
Cdd:PLN03052 327 EGDMSWDDFLARANGLRRPDEYKA------VEQPVEAFTNILFSSGTTGEPKAIpwTQ------LTPLRaaaDAWAHLDI 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 304 SRDDCLFYYTTCGWMMWNWLV-SVLAIGATAVLYDGSPFHPGPERLIDliDAeKISVFGTSPKFLATLEKAGLQPRLshD 382
Cdd:PLN03052 395 RKGDIVCWPTNLGWMMGPWLVyASLLNGATLALYNGSPLGRGFAKFVQ--DA-KVTMLGTVPSIVKTWKNTNCMAGL--D 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 383 LGSLKGLISTGSPLSPQSYDYV-----YREIKgELClssmsGGTDIVSCFVIGNPVLPVRRGEMQCKSLAMAIEVWDDQG 457
Cdd:PLN03052 470 WSSIRCFGSTGEASSVDDYLWLmsragYKPII-EYC-----GGTELGGGFVTGSLLQPQAFAAFSTPAMGCKLFILDDSG 543
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 458 QPLVGEK---GELV-CTRHFPAMPIGLwnDPDRQKLrasYFSQFPgVWA------QGDYAEQRPNGSLLIHGRSDAVLNP 527
Cdd:PLN03052 544 NPYPDDApctGELAlFPLMFGASSTLL--NADHYKV---YFKGMP-VFNgkilrrHGDIFERTSGGYYRAHGRADDTMNL 617
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 528 GGVRIGTAEIYRQVEKVPQ-VQESLAIG----QRWQDDVRVVLFVRLNDGVELD-EALEQQIRQVIRANTTPRHVPAKIL 601
Cdd:PLN03052 618 GGIKVSSVEIERVCNAADEsVLETAAIGvpppGGGPEQLVIAAVLKDPPGSNPDlNELKKIFNSAIQKKLNPLFKVSAVV 697
|
650
....*....|....*....
gi 799207711 602 AVTDIPRTISGKIVELAVR 620
Cdd:PLN03052 698 IVPSFPRTASNKVMRRVLR 716
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
115-620 |
3.14e-46 |
|
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: 169.44 E-value: 3.14e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 115 LTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTLVGMLATTSLGAIWSCSSPDFGTQGVIDRFGQIEPKVLITCA 194
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 195 gyryagkdidqtaklneilarlpsleqliivpyarpqarvedyqtharvtrwsdfyppggepefvavpfDHPLYILYSSG 274
Cdd:cd05972 81 ---------------------------------------------------------------------EDPALIYFTSG 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 275 TTGVPKCIIHgTGGVLLTHLKEHGLHADLSRDDCLFYYTTCGWMMWNW--LVSVLAIGATAVLYDGSPFHPgpERLIDLI 352
Cdd:cd05972 92 TTGLPKGVLH-THSYPLGHIPTAAYWLGLRPDDIHWNIADPGWAKGAWssFFGPWLLGATVFVYEGPRFDA--ERILELL 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 353 DAEKISVFGTSPKFLATLEKAGLqprLSHDLGSLKGLISTGSPLSPQSYDyVYREiKGELCLSSMSGGTDIVscFVIGN- 431
Cdd:cd05972 169 ERYGVTSFCGPPTAYRMLIKQDL---SSYKFSHLRLVVSAGEPLNPEVIE-WWRA-ATGLPIRDGYGQTETG--LTVGNf 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 432 PVLPVRRGEMQCKSLAMAIEVWDDQGQPLV-GEKGELVCTRHFPAMPIGLWNDPDRQKLRASyfsqfPGVWAQGDYAEQR 510
Cdd:cd05972 242 PDMPVKPGSMGRPTPGYDVAIIDDDGRELPpGEEGDIAIKLPPPGLFLGYVGDPEKTEASIR-----GDYYLTGDRAYRD 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 511 PNGSLLIHGRSDAVLNPGGVRIGTAEIYRQVEKVPQVQESLAIGQrwQDDVR---VVLFVRLNDGVELDEALEQQIRQVI 587
Cdd:cd05972 317 EDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGS--PDPVRgevVKAFVVLTSGYEPSEELAEELQGHV 394
|
490 500 510
....*....|....*....|....*....|...
gi 799207711 588 RANTTPRHVPAKILAVTDIPRTISGKIVELAVR 620
Cdd:cd05972 395 KKVLAPYKYPREIEFVEELPKTISGKIRRVELR 427
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
91-526 |
4.45e-45 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 165.95 E-value: 4.45e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 91 EHLLRRRDDHPAVvaisEDGQREQLTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTLVGMLATTSLGAIWSCSS 170
Cdd:pfam00501 2 ERQAARTPDKTAL----EVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 171 PDFGTQGVIDRFGQIEPKVLITcagyryagKDIDQTAKLNEILARLPSLEqLIIVPYARPQARVEDYQTHARVTRWSDFY 250
Cdd:pfam00501 78 PRLPAEELAYILEDSGAKVLIT--------DDALKLEELLEALGKLEVVK-LVLVLDRDPVLKEEPLPEEAKPADVPPPP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 251 PPGGEPefvavpfDHPLYILYSSGTTGVPKciihgtgGVLLTH---------LKEHGLHAD-LSRDDCLFYYTTCGWMM- 319
Cdd:pfam00501 149 PPPPDP-------DDLAYIIYTSGTTGKPK-------GVMLTHrnlvanvlsIKRVRPRGFgLGPDDRVLSTLPLFHDFg 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 320 WNWLV-SVLAIGATAVLYDGSPFHPgPERLIDLIDAEKISVFGTSPKFLATLEKAGLQPRLshDLGSLKGLISTGSPLSP 398
Cdd:pfam00501 215 LSLGLlGPLLAGATVVLPPGFPALD-PAALLELIERYKVTVLYGVPTLLNMLLEAGAPKRA--LLSSLRLVLSGGAPLPP 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 399 QSYDYVYREIKGEL------------CLSSMSGGTDIVSCFVIGNPVLPVRrgemqckslaMAIeVWDDQGQPL-VGEKG 465
Cdd:pfam00501 292 ELARRFRELFGGALvngygltettgvVTTPLPLDEDLRSLGSVGRPLPGTE----------VKI-VDDETGEPVpPGEPG 360
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 799207711 466 ELvCTRHfPAMPIGLWNDPDRQKlrASYFSqfPGVWAQGDYAEQRPNGSLLIHGRSDAVLN 526
Cdd:pfam00501 361 EL-CVRG-PGVMKGYLNDPELTA--EAFDE--DGWYRTGDLGRRDEDGYLEIVGRKKDQIK 415
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
115-620 |
3.57e-41 |
|
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: 155.74 E-value: 3.57e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 115 LTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTLVGMLATTSLGAIWSCSSPDFGTQGVIDRFGQIEPKVLITca 194
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLIT-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 195 gyryagkdidqtaklNEILARLPSLEQliivpyarpqarvedyqtharvtrwsdfyppggepefvavpfdhPLYILYSSG 274
Cdd:cd05969 79 ---------------TEELYERTDPED--------------------------------------------PTLLHYTSG 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 275 TTGVPKCIIHgTGGVLLTHLKEHGLHADLSRDDCLFYYTTCGWM--MWNWLVSVLAIGATAVLYDGSpFHPgpERLIDLI 352
Cdd:cd05969 100 TTGTPKGVLH-VHDAMIFYYFTGKYVLDLHPDDIYWCTADPGWVtgTVYGIWAPWLNGVTNVVYEGR-FDA--ESWYGII 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 353 DAEKISVFGTSPKFLATLEKAGLQPRLSHDLGSLKGLISTGSPLSPQSYDYVYREIKgeLCLSSMSGGTDIVSCFVIGNP 432
Cdd:cd05969 176 ERVKVTVWYTAPTAIRMLMKEGDELARKYDLSSLRFIHSVGEPLNPEAIRWGMEVFG--VPIHDTWWQTETGSIMIANYP 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 433 VLPVRRGEMQCKSLAMAIEVWDDQGQPL-VGEKGELVCTRHFPAMPIGLWNDPDRqklrasYFSQFPGVW-AQGDYAEQR 510
Cdd:cd05969 254 CMPIKPGSMGKPLPGVKAAVVDENGNELpPGTKGILALKPGWPSMFRGIWNDEER------YKNSFIDGWyLTGDLAYRD 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 511 PNGSLLIHGRSDAVLNPGGVRIGTAEIYRQVEKVPQVQESLAIGQrwQDDVR---VVLFVRLNDGVELDEALEQQIRQVI 587
Cdd:cd05969 328 EDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGK--PDPLRgeiIKAFISLKEGFEPSDELKEEIINFV 405
|
490 500 510
....*....|....*....|....*....|...
gi 799207711 588 RANTTPRHVPAKILAVTDIPRTISGKIVELAVR 620
Cdd:cd05969 406 RQKLGAHVAPREIEFVDNLPKTRSGKIMRRVLK 438
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
81-614 |
1.95e-39 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 153.13 E-value: 1.95e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 81 WFPGATLNFAEHLLRR-----RDDHPAVVAISEDgQREQLTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTLVG 155
Cdd:PRK04319 36 WLETGKVNIAYEAIDRhadggRKDKVALRYLDAS-RKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 156 MLATTSLGAIWSCSSPDFGTQGVIDRFGQIEPKVLITcagyryagkdidqTAKLNE--ILARLPSLEQLIIV-PYARPQA 232
Cdd:PRK04319 115 LLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVLIT-------------TPALLErkPADDLPSLKHVLLVgEDVEEGP 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 233 RVEDYqtHARVTRWSDfyppggEPEFVAVPFDHPLYILYSSGTTGVPKCIIHGTGGVLLTHLKehGLHA-DLSRDDclFY 311
Cdd:PRK04319 182 GTLDF--NALMEQASD------EFDIEWTDREDGAILHYTSGSTGKPKGVLHVHNAMLQHYQT--GKYVlDLHEDD--VY 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 312 YTTC--GWM--MWNWLVSVLAIGATAVLyDGSPFHPgpERLIDLIDAEKISVFGTSPKFLATLEKAGLQPRLSHDLGSLK 387
Cdd:PRK04319 250 WCTAdpGWVtgTSYGIFAPWLNGATNVI-DGGRFSP--ERWYRILEDYKVTVWYTAPTAIRMLMGAGDDLVKKYDLSSLR 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 388 GLISTGSPLSPQsydyVYREIKGELCL-------SSMSGGTdivscfVIGN-PVLPVRRGEMQcKSLAmAIE--VWDDQG 457
Cdd:PRK04319 327 HILSVGEPLNPE----VVRWGMKVFGLpihdnwwMTETGGI------MIANyPAMDIKPGSMG-KPLP-GIEaaIVDDQG 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 458 QPLV-GEKGELVCTRHFPAMPIGLWNDPDRQKlraSYFSqfPGVWAQGDYAEQRPNGSLLIHGRSDAVLNPGGVRIGTAE 536
Cdd:PRK04319 395 NELPpNRMGNLAIKKGWPSMMRGIWNNPEKYE---SYFA--GDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFE 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 537 iyrqVEKV----PQVQESLAIGQrwQDDVR---VVLFVRLNDGVELDEALEQQIRQVIRANTTPrHVPAKILAVTD-IPR 608
Cdd:PRK04319 470 ----VESKlmehPAVAEAGVIGK--PDPVRgeiIKAFVALRPGYEPSEELKEEIRGFVKKGLGA-HAAPREIEFKDkLPK 542
|
....*.
gi 799207711 609 TISGKI 614
Cdd:PRK04319 543 TRSGKI 548
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
99-614 |
2.44e-37 |
|
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: 144.59 E-value: 2.44e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 99 DHPAVVAisedgQREQLTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTLVGMLATTSLGAIWSCSSPDFGTQGV 178
Cdd:cd05930 2 DAVAVVD-----GDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 179 IDRFGQIEPKVLITCAgyryagkdidqtaklneilarlpsleqliivpyarpqarvedyqtharvtrwsdfyppggepef 258
Cdd:cd05930 77 AYILEDSGAKLVLTDP---------------------------------------------------------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 259 vavpfDHPLYILYSSGTTGVPKciihgtgGVLLTH------LKEHGLHADLSRDDCLFYYTT-----CGWMMWNWLVSvl 327
Cdd:cd05930 93 -----DDLAYVIYTSGSTGKPK-------GVMVEHrglvnlLLWMQEAYPLTPGDRVLQFTSfsfdvSVWEIFGALLA-- 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 328 aiGATAVLYDGSpFHPGPERLIDLIDAEKISVFGTSPKFLATLEKAGLQPRLShdlgSLKGLISTGSPLSPQSYDYvYRE 407
Cdd:cd05930 159 --GATLVVLPEE-VRKDPEALADLLAEEGITVLHLTPSLLRLLLQELELAALP----SLRLVLVGGEALPPDLVRR-WRE 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 408 IKGELCLSSMSG---GTDIVSCFVIGNPVLPVRR---GemqcKSLA-MAIEVWDDQGQPL-VGEKGELVCTRhfPAMPIG 479
Cdd:cd05930 231 LLPGARLVNLYGpteATVDATYYRVPPDDEEDGRvpiG----RPIPnTRVYVLDENLRPVpPGVPGELYIGG--AGLARG 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 480 LWNDPDrqkLRASYFSQFPGV-WAQ----GDYAEQRPNGSLLIHGRSDAVLNPGGVRIGTAEIYRQVEKVPQVQESLAIG 554
Cdd:cd05930 305 YLNRPE---LTAERFVPNPFGpGERmyrtGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVA 381
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 799207711 555 QRWQD-DVRVVLFVRLNDGVELDEAleqQIRQVIRAnTTPRH-VPAKILAVTDIPRTISGKI 614
Cdd:cd05930 382 REDGDgEKRLVAYVVPDEGGELDEE---ELRAHLAE-RLPDYmVPSAFVVLDALPLTPNGKV 439
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
87-614 |
5.07e-37 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 145.33 E-value: 5.07e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 87 LNFAEHLLRRRDDHPAVVAISEDGQReqLTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTLVGMLATTSLGAiw 166
Cdd:PRK06187 6 LTIGRILRHGARKHPDKEAVYFDGRR--TTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGA-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 167 scsspdfgtqgvidrfgqiepkVLITcAGYRYAGKDIDQTAK----------------LNEILARLPSLEQLIIV---PY 227
Cdd:PRK06187 82 ----------------------VLHP-INIRLKPEEIAYILNdaedrvvlvdsefvplLAAILPQLPTVRTVIVEgdgPA 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 228 ARPQARVEDYQTharvtrWSDfyppGGEPEFVAVPFD-HPLY-ILYSSGTTGVPKciihgtgGVLLTH--LKEHGLHA-- 301
Cdd:PRK06187 139 APLAPEVGEYEE------LLA----AASDTFDFPDIDeNDAAaMLYTSGTTGHPK-------GVVLSHrnLFLHSLAVca 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 302 --DLSRDDC------LFYYTTCGWMMWNWLVsvlaiGATAVL---YDgspfhpgPERLIDLIDAEKISVFGTSPKFLATL 370
Cdd:PRK06187 202 wlKLSRDDVylvivpMFHVHAWGLPYLALMA-----GAKQVIprrFD-------PENLLDLIETERVTFFFAVPTIWQML 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 371 EKAGLQPRlsHDLGSLKGLISTGSPLSPQSYDyVYREIKG-ELC----LSSMSGgtdIVSCFVIgNPVLPVRRGEMQCKS 445
Cdd:PRK06187 270 LKAPRAYF--VDFSSLRLVIYGGAALPPALLR-EFKEKFGiDLVqgygMTETSP---VVSVLPP-EDQLPGQWTKRRSAG 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 446 LAMA---IEVWDDQGQPL---VGEKGELVcTRHfPAMPIGLWNDPDRQKlrasyfSQFPGVWAQ-GDYAEQRPNGSLLIH 518
Cdd:PRK06187 343 RPLPgveARIVDDDGDELppdGGEVGEII-VRG-PWLMQGYWNRPEATA------ETIDGGWLHtGDVGYIDEDGYLYIT 414
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 519 GRSDAVLNPGGVRIGTAEIYRQVEKVPQVQESLAIG---QRWQDdvRVVLFVRLNDGVELDEAleqQIRQVIRANTTPRH 595
Cdd:PRK06187 415 DRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGvpdEKWGE--RPVAVVVLKPGATLDAK---ELRAFLRGRLAKFK 489
|
570
....*....|....*....
gi 799207711 596 VPAKILAVTDIPRTISGKI 614
Cdd:PRK06187 490 LPKRIAFVDELPRTSVGKI 508
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
93-614 |
7.60e-36 |
|
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: 140.05 E-value: 7.60e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 93 LLRRRDDHPAVVAISEDGQReqLTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTLVGMLATTSLGAIWscsspd 172
Cdd:cd17631 1 LRRRARRHPDRTALVFGGRS--LTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVF------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 173 fgtqgvidrfgqiepkvlitcagyryagkdidqtAKLNeilARLPSLEQLIIVPYARPqarvedyqtharvtrwsdfypp 252
Cdd:cd17631 73 ----------------------------------VPLN---FRLTPPEVAYILADSGA---------------------- 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 253 ggepefvAVPFDHPLYILYSSGTTGVPKciihgtgGVLLTH------LKEHGLHADLSRDDCLF-----YYTTCGWMmwn 321
Cdd:cd17631 94 -------KVLFDDLALLMYTSGTTGRPK-------GAMLTHrnllwnAVNALAALDLGPDDVLLvvaplFHIGGLGV--- 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 322 WLVSVLAIGATAVLydgsPFHPGPERLIDLIDAEKISVFGTSPkflaTLEKAGLQ-PRLS-HDLGSLKGLISTGSPlSPQ 399
Cdd:cd17631 157 FTLPTLLRGGTVVI----LRKFDPETVLDLIERHRVTSFFLVP----TMIQALLQhPRFAtTDLSSLRAVIYGGAP-MPE 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 400 SYDYVYREIKGELC----LSSMSGG----------TDIVSCfviGNPVLPVRrgemqckslamaIEVWDDQGQPL-VGEK 464
Cdd:cd17631 228 RLLRALQARGVKFVqgygMTETSPGvtflspedhrRKLGSA---GRPVFFVE------------VRIVDPDGREVpPGEV 292
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 465 GElVCTRHfPAMPIGLWNDPDRqklRASYFSqfpGVWAQ-GDYAEQRPNGSLLIHGRSDAVLNPGGVRIGTAEIYRQVEK 543
Cdd:cd17631 293 GE-IVVRG-PHVMAGYWNRPEA---TAAAFR---DGWFHtGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYE 364
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 799207711 544 VPQVQESLAIG---QRWQDdvRVVLFVRLNDGVELDealEQQIRQVIRANTTPRHVPAKILAVTDIPRTISGKI 614
Cdd:cd17631 365 HPAVAEVAVIGvpdEKWGE--AVVAVVVPRPGAELD---EDELIAHCRERLARYKIPKSVEFVDALPRNATGKI 433
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
86-620 |
9.11e-36 |
|
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: 141.86 E-value: 9.11e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 86 TLNFAEHLLRR----RDDHPAVVAISEDGQREQLTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTLVGMLATTS 161
Cdd:cd05970 15 NFNFAYDVVDAmakeYPDKLALVWCDDAGEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 162 LGAIWSCSSPDFGTQGVIDRFGQIEPKvLITCAgyryAGKDIDQtaKLNEILARLPSLEQLIIVPYARPQArVEDYqtHA 241
Cdd:cd05970 95 LGAIAIPATHQLTAKDIVYRIESADIK-MIVAI----AEDNIPE--EIEKAAPECPSKPKLVWVGDPVPEG-WIDF--RK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 242 RVTRWS-DFYPPGGEPEFVAvpfDHPLYILYSSGTTGVPKCIIHGTG---GVLLT-----HLKEHGLHadLSRDDClfyy 312
Cdd:cd05970 165 LIKNASpDFERPTANSYPCG---EDILLVYFSSGTTGMPKMVEHDFTyplGHIVTakywqNVREGGLH--LTVADT---- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 313 ttcGW--MMWNWLVSVLAIGATAVLYDGSPFHPgpERLIDLIDAEKISVFGTSPKFLATLEKAGLQprlSHDLGSLKGLI 390
Cdd:cd05970 236 ---GWgkAVWGKIYGQWIAGAAVFVYDYDKFDP--KALLEKLSKYGVTTFCAPPTIYRFLIREDLS---RYDLSSLRYCT 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 391 STGSPLSPQSYDyVYREIKGeLCLSSMSGGTDIVSCfvIGN-PVLPVRRGEMQCKSLAMAIEVWDDQGQPL-VGEKGElV 468
Cdd:cd05970 308 TAGEALNPEVFN-TFKEKTG-IKLMEGFGQTETTLT--IATfPWMEPKPGSMGKPAPGYEIDLIDREGRSCeAGEEGE-I 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 469 CTRHFPAMPIGLWN----DPDRQklrASYFsqFPGVWAQGDYAEQRPNGSLLIHGRSDAVLNPGGVRIGTAEIYRQVEKV 544
Cdd:cd05970 383 VIRTSKGKPVGLFGgyykDAEKT---AEVW--HDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQH 457
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 799207711 545 PQVQESLAIGqrWQDDVR---VVLFVRLNDGVELDEALEQQIRQVIRANTTPRHVPAKILAVTDIPRTISGKIVELAVR 620
Cdd:cd05970 458 PAVLECAVTG--VPDPIRgqvVKATIVLAKGYEPSEELKKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEIR 534
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
109-620 |
2.24e-34 |
|
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: 136.02 E-value: 2.24e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 109 DGQREQLTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTLVGMLATTSLGAIWSCSSPDFGTQGVIDRFGQIEPK 188
Cdd:cd05971 1 KGTPEKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 189 VLITcagyryagkdiDQTaklneilarlpsleqliivpyarpqarvedyqtharvtrwsdfyppggepefvavpfDHPLY 268
Cdd:cd05971 81 ALVT-----------DGS---------------------------------------------------------DDPAL 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 269 ILYSSGTTGVPKCIIHGTGgVLLTHLKEHGLHADLSRDDCLFYYTTCGWMmW-----NWLVSVLAIGATAVLYDGSPFHP 343
Cdd:cd05971 93 IIYTSGTTGPPKGALHAHR-VLLGHLPGVQFPFNLFPRDGDLYWTPADWA-WiggllDVLLPSLYFGVPVLAHRMTKFDP 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 344 GpeRLIDLIDAEKISVFGTSPKFLATLEKAGlqPRLSHDLGSLKGLISTGSPLSPQSYDYVYREIKGELclSSMSGGTDi 423
Cdd:cd05971 171 K--AALDLMSRYGVTTAFLPPTALKMMRQQG--EQLKHAQVKLRAIATGGESLGEELLGWAREQFGVEV--NEFYGQTE- 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 424 vSCFVIGN--PVLPVRRGEMQCKSLAMAIEVWDDQGQPL-VGEKGELVCTRHFPAMPIGLWNDPDRQKLRasyfsqFPGV 500
Cdd:cd05971 244 -CNLVIGNcsALFPIKPGSMGKPIPGHRVAIVDDNGTPLpPGEVGEIAVELPDPVAFLGYWNNPSATEKK------MAGD 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 501 WAQ-GDYAEQRPNGSLLIHGRSDAVLNPGGVRIGTAEIYRQVEKVPQVQESLAIGQrwQDDVR---VVLFVRLNDGVELD 576
Cdd:cd05971 317 WLLtGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGI--PDPIRgeiVKAFVVLNPGETPS 394
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 799207711 577 EALEQQIRQVIRANTTPRHVPAKILAVTDIPRTISGKIVELAVR 620
Cdd:cd05971 395 DALAREIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRRELR 438
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
81-621 |
4.19e-33 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 135.25 E-value: 4.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 81 WFPGATLNFAEHLLRRRDDHPA----VVAISED---GQREQLTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTL 153
Cdd:PTZ00237 52 WFKGGELNTCYNVLDIHVKNPLkrdqDALIYECpylKKTIKLTYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 154 VGMLATTSLGAIWSCSSPDFGTQGVIDRFGQIEPKVLITCagyryagkdiDQTAKLNEILARLPSLEQLIIVPYARPQ-- 231
Cdd:PTZ00237 132 IAMLSCARIGATHCVLFDGYSVKSLIDRIETITPKLIITT----------NYGILNDEIITFTPNLKEAIELSTFKPSnv 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 232 --------------ARVEDYQTHARVTRWSD------------FYppggepEFVAVPFDHPLYILYSSGTTGVPKCIIHG 285
Cdd:PTZ00237 202 itlfrnditsesdlKKIETIPTIPNTLSWYDeikkikennqspFY------EYVPVESSHPLYILYTSGTTGNSKAVVRS 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 286 TGGVLLThLKEHgLHADLSRDDC--LFYYTTCGWMMW-NWLVSVLAIGATAVLYDGSPFHPG--PERLIDLIDAEKISVF 360
Cdd:PTZ00237 276 NGPHLVG-LKYY-WRSIIEKDIPtvVFSHSSIGWVSFhGFLYGSLSLGNTFVMFEGGIIKNKhiEDDLWNTIEKHKVTHT 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 361 GTSPKFLATLEKA---GLQPRLSHDLGSLKGLISTGSPLSPQSYDYVYREIKgeLCLSSMSGGTDIVSCFVIGNPVLPVR 437
Cdd:PTZ00237 354 LTLPKTIRYLIKTdpeATIIRSKYDLSNLKEIWCGGEVIEESIPEYIENKLK--IKSSRGYGQTEIGITYLYCYGHINIP 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 438 RGEMQCKSLAMAIEVWDDQGQPL-VGEKGELVCTrhFPaMPIGLW-----NDPDRQKLrasyFSQFPGVWAQGDYAEQRP 511
Cdd:PTZ00237 432 YNATGVPSIFIKPSILSEDGKELnVNEIGEVAFK--LP-MPPSFAttfykNDEKFKQL----FSKFPGYYNSGDLGFKDE 504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 512 NGSLLIHGRSDAVLNPGGVRIGTAEIYRQVEKVPQVQESLAIGQRWQD--DVRVVLFVRLNDG----VELDEaLEQQIRQ 585
Cdd:PTZ00237 505 NGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDcyNVPIGLLVLKQDQsnqsIDLNK-LKNEINN 583
|
570 580 590
....*....|....*....|....*....|....*.
gi 799207711 586 VIRANTTPRHVPAKILAVTDIPRTISGKIVELAVRN 621
Cdd:PTZ00237 584 IITQDIESLAVLRKIIIVNQLPKTKTGKIPRQIISK 619
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
92-620 |
4.52e-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: 133.26 E-value: 4.52e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 92 HLLRRRDDHPAVVaiseDGQREqLTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQtlvgmLATTSLGAIWSCSSP 171
Cdd:cd05959 12 NLNEGRGDKTAFI----DDAGS-LTYAELEAEARRVAGALRALGVKREERVLLIMLDTVD-----FPTAFLGAIRAGIVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 172 dfgtqgvidrfgqIEPKVLITCAGYRYAGKDIDQTAKL--NEILARL--------PSLEQLIIVPYARPQARVEDYqtha 241
Cdd:cd05959 82 -------------VPVNTLLTPDDYAYYLEDSRARVVVvsGELAPVLaaaltkseHTLVVLIVSGGAGPEAGALLL---- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 242 rvtrwSDFyPPGGEPEFVAVPF--DHPLYILYSSGTTGVPKCIIHgtggvllthlkehgLHADL---------------S 304
Cdd:cd05959 145 -----AEL-VAAEAEQLKPAAThaDDPAFWLYSSGSTGRPKGVVH--------------LHADIywtaelyarnvlgirE 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 305 RDDC-----LFYYTTCGwmmwNWLVSVLAIGATAVLYdgsPFHPGPERLIDLIDAEKISVFGTSPKFLATLEKAglqPRL 379
Cdd:cd05959 205 DDVCfsaakLFFAYGLG----NSLTFPLSVGATTVLM---PERPTPAAVFKRIRRYRPTVFFGVPTLYAAMLAA---PNL 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 380 -SHDLGSLKGLISTGSPLSPQsydyVYREIKGELCLSSMSG--GTDIVSCFvIGNPVLPVRRGEMQCKSLAMAIEVWDDQ 456
Cdd:cd05959 275 pSRDLSSLRLCVSAGEALPAE----VGERWKARFGLDILDGigSTEMLHIF-LSNRPGRVRYGTTGKPVPGYEVELRDED 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 457 GQPL-VGEKGELVCtrHFPAMPIGLWNDPDRQKlrasyfSQFPGVWAQ-GDYAEQRPNGSLLIHGRSDAVLNPGGVRIGT 534
Cdd:cd05959 350 GGDVaDGEPGELYV--RGPSSATMYWNNRDKTR------DTFQGEWTRtGDKYVRDDDGFYTYAGRADDMLKVSGIWVSP 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 535 AEIYRQVEKVPQVQESLAIGqrWQDDVR---VVLFVRLNDGVELDEALEQQIRQVIRANTTPRHVPAKILAVTDIPRTIS 611
Cdd:cd05959 422 FEVESALVQHPAVLEAAVVG--VEDEDGltkPKAFVVLRPGYEDSEALEEELKEFVKDRLAPYKYPRWIVFVDELPKTAT 499
|
....*....
gi 799207711 612 GKIVELAVR 620
Cdd:cd05959 500 GKIQRFKLR 508
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
101-614 |
5.11e-33 |
|
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: 132.80 E-value: 5.11e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 101 PAVVAISEDGQreQLTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTLVGMLATTSLGAIWSCSSPDFGTqgviD 180
Cdd:cd12116 1 PDATAVRDDDR--SLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPA----D 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 181 RFGQI----EPKVLITcagyryagkDIDQTAKLNEILARLPSLEQLIIVPYARPQArvedyqtharvtrwsdfyppggep 256
Cdd:cd12116 75 RLRYIledaEPALVLT---------DDALPDRLPAGLPVLLLALAAAAAAPAAPRT------------------------ 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 257 efvAVPFDHPLYILYSSGTTGVPKciihgtgGVLLTHLK-EHGLHA-----DLSRDDCLFYYTTCGWMMwnwlvSVLAI- 329
Cdd:cd12116 122 ---PVSPDDLAYVIYTSGSTGRPK-------GVVVSHRNlVNFLHSmrerlGLGPGDRLLAVTTYAFDI-----SLLELl 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 330 -----GATAVLYDGSPFHpGPERLIDLIDAEKISVFGTSPKFLATLEKAGLQPRlshdlGSLKGLIStGSPLSPqsydyv 404
Cdd:cd12116 187 lpllaGARVVIAPRETQR-DPEALARLIEAHSITVMQATPATWRMLLDAGWQGR-----AGLTALCG-GEALPP------ 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 405 yrEIKGELCLSSMS-----GGTD--IVSC----------FVIGNPVLPVRrgemqckslamaIEVWDDQGQPL-VGEKGE 466
Cdd:cd12116 254 --DLAARLLSRVGSlwnlyGPTEttIWSTaarvtaaagpIPIGRPLANTQ------------VYVLDAALRPVpPGVPGE 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 467 L-VCTrhfPAMPIGLWNDPDrqkLRASYFSQFPGVWA------QGDYAEQRPNGSLLIHGRSDAVLNPGGVRIGTAEIYR 539
Cdd:cd12116 320 LyIGG---DGVAQGYLGRPA---LTAERFVPDPFAGPgsrlyrTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEA 393
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 799207711 540 QVEKVPQVQESLAIGQRWQDDVRVVLFVRLNDGVELDEAleqQIRQVIRAnTTPRH-VPAKILAVTDIPRTISGKI 614
Cdd:cd12116 394 ALAAHPGVAQAAVVVREDGGDRRLVAYVVLKAGAAPDAA---ALRAHLRA-TLPAYmVPSAFVRLDALPLTANGKL 465
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
68-628 |
1.04e-32 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 132.87 E-value: 1.04e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 68 AVLIED--AEMPSAQWFPGATLN--FAEHLlRRRDDHPAVVAISED-GQREQLTYAELAEHVAGLQKSLRAAGVTQGDRV 142
Cdd:PRK13295 5 AVLLPPrrAASIAAGHWHDRTINddLDACV-ASCPDKTAVTAVRLGtGAPRRFTYRELAALVDRVAVGLARLGVGRGDVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 143 AACMPNTWQTLVGMLATTSLGAIWSCSSPDFGTQGVIDRFGQIEPKVLITCAGYRyagkDIDQTAKLNEILARLPSLEQL 222
Cdd:PRK13295 84 SCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERELSFMLKHAESKVLVVPKTFR----GFDHAAMARRLRPELPALRHV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 223 IIVPYARPqarvEDYQTHARVTRWSDfyppggEPEFVAV-------PFDHPLYIlYSSGTTGVPKCIIHgTGGVLLTHLK 295
Cdd:PRK13295 160 VVVGGDGA----DSFEALLITPAWEQ------EPDAPAIlarlrpgPDDVTQLI-YTSGTTGEPKGVMH-TANTLMANIV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 296 EHGLHADLSRDDCLFYYTTCGWM---MWNWLVSVLaIGATAVLYDGSpfhpGPERLIDLIDAEKISVFGTSPKFLATLEK 372
Cdd:PRK13295 228 PYAERLGLGADDVILMASPMAHQtgfMYGLMMPVM-LGATAVLQDIW----DPARAAELIRTEGVTFTMASTPFLTDLTR 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 373 AglQPRLSHDLGSLKGLISTGSPLSPQSYDYVyREIKGELCLSSMsGGTD--IVSCFVIGNP--VLPVRRGemqCKSLAM 448
Cdd:PRK13295 303 A--VKESGRPVSSLRTFLCAGAPIPGALVERA-RAALGAKIVSAW-GMTEngAVTLTKLDDPdeRASTTDG---CPLPGV 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 449 AIEVWDDQGQPL-VGEKGELVCTRhfPAMPIGLWNDPDRqklrasYFSQFPGVWAQGDYAEQRPNGSLLIHGRSDAVLNP 527
Cdd:PRK13295 376 EVRVVDADGAPLpAGQIGRLQVRG--CSNFGGYLKRPQL------NGTDADGWFDTGDLARIDADGYIRISGRSKDVIIR 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 528 GGVRIGTAEIYRQVEKVPQVQESLAIG---QRWQDdvRVVLFVRLNDGVELDeaLEQQIRQVIRANTTPRHVPAKILAVT 604
Cdd:PRK13295 448 GGENIPVVEIEALLYRHPAIAQVAIVAypdERLGE--RACAFVVPRPGQSLD--FEEMVEFLKAQKVAKQYIPERLVVRD 523
|
570 580
....*....|....*....|....
gi 799207711 605 DIPRTISGKIVELAVRNVVHGEPV 628
Cdd:PRK13295 524 ALPRTPSGKIQKFRLREMLRGEDA 547
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
246-621 |
2.01e-32 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 131.48 E-value: 2.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 246 WSDF----YPPG----GEPEFVAVPFDHPLYILYSSGTTGVPKCIIhgtggvlLTHLK------EHGLHADLSRDDCLFY 311
Cdd:PLN03051 93 WCDFlgvaAAQGsvggNEYSPVYAPVESVTNILFSSGTTGEPKAIP-------WTHLSplrcasDGWAHMDIQPGDVVCW 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 312 YTTCGWMMWNWLV-SVLAIGATAVLYDGSPFHPGperLIDLIDAEKISVFGTSPKFLATLEKAGLQPRLSHDLGSLKGLI 390
Cdd:PLN03051 166 PTNLGWMMGPWLLySAFLNGATLALYGGAPLGRG---FGKFVQDAGVTVLGLVPSIVKAWRHTGAFAMEGLDWSKLRVFA 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 391 STGSPLSPQSYDYV------YREIKgELClssmsGGTDIVSCFVIGNPVLPVRRGEMQCKSLAMAIEVWDDQG------Q 458
Cdd:PLN03051 243 STGEASAVDDVLWLssvrgyYKPVI-EYC-----GGTELASGYISSTLLQPQAPGAFSTASLGTRFVLLNDNGvpypddQ 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 459 PLVGEKGElvctrhFPAMpIGLWNDPDRQKLRASYFSQFPGVWAQ-------GDYAEQRPNGSLLIHGRSDAVLNPGGVR 531
Cdd:PLN03051 317 PCVGEVAL------APPM-LGASDRLLNADHDKVYYKGMPMYGSKgmplrrhGDIMKRTPGGYFCVQGRADDTMNLGGIK 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 532 IGTAEIYRQVEKVPQ-VQESLAIGQRWQDDVRVVLFVRLNDGVELD-------EALEQQIRQVIRANTTPRHVPAKILAV 603
Cdd:PLN03051 390 TSSVEIERACDRAVAgIAETAAVGVAPPDGGPELLVIFLVLGEEKKgfdqarpEALQKKFQEAIQTNLNPLFKVSRVKIV 469
|
410
....*....|....*...
gi 799207711 604 TDIPRTISGKIVELAVRN 621
Cdd:PLN03051 470 PELPRNASNKLLRRVLRD 487
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
112-620 |
1.63e-29 |
|
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: 121.80 E-value: 1.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 112 REQLTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTLVGMLATTSLGAIWSCSSPdfgtqgvidrfgqiepkvLI 191
Cdd:cd05919 8 DRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINP------------------LL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 192 TCAGYRYAGKDidqtaklneilarlpsleqliivpyarpqarvedyqTHARVtrwsdfyppggepefVAVPFDHPLYILY 271
Cdd:cd05919 70 HPDDYAYIARD------------------------------------CEARL---------------VVTSADDIAYLLY 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 272 SSGTTGVPKCIIHGTGGVLLT---------HLKEHGLHADLSRddcLFYyttcGWMMWNWLVSVLAIGATAVLYDGSPfh 342
Cdd:cd05919 99 SSGTTGPPKGVMHAHRDPLLFadamarealGLTPGDRVFSSAK---MFF----GYGLGNSLWFPLAVGASAVLNPGWP-- 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 343 pGPERLIDLIDAEKISVFGTSPKFLATLEKAGLQPRlsHDLGSLKGLISTGSPLsPQSYDYVYREIKGELCLSSMsGGTD 422
Cdd:cd05919 170 -TAERVLATLARFRPTVLYGVPTFYANLLDSCAGSP--DALRSLRLCVSAGEAL-PRGLGERWMEHFGGPILDGI-GATE 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 423 IVSCFvIGNPVLPVRRGEMQCKSLAMAIEVWDDQGQPL-VGEKGELVCtrHFPAMPIGLWNDPDRQKLRasyfsqFPGVW 501
Cdd:cd05919 245 VGHIF-LSNRPGAWRLGSTGRPVPGYEIRLVDEEGHTIpPGEEGDLLV--RGPSAAVGYWNNPEKSRAT------FNGGW 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 502 -AQGDYAEQRPNGSLLIHGRSDAVLNPGGVRIGTAEIYRQVEKVPQVQESLAIGQRWQDD-VRVVLFVRLNDGVELDEAL 579
Cdd:cd05919 316 yRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGlSRLTAFVVLKSPAAPQESL 395
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 799207711 580 EQQIRQVIRANTTPRHVPAKILAVTDIPRTISGKIVELAVR 620
Cdd:cd05919 396 ARDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKLR 436
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
95-620 |
3.43e-29 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 121.94 E-value: 3.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 95 RRRDDHPAVVaisEDGQReqLTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTLVGMLATTSLGAIWSCSSPDFG 174
Cdd:PRK07656 16 RRFGDKEAYV---FGDQR--LTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 175 TQGVIDRFGQIEPKVLITCAGyrYAGKDIdqtaklnEILARLPSLEQLIIVPYARPQARVEDYQTharvtrWSDFYPPGG 254
Cdd:PRK07656 91 ADEAAYILARGDAKALFVLGL--FLGVDY-------SATTRLPALEHVVICETEEDDPHTEKMKT------FTDFLAAGD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 255 EPEF-VAVPFDHPLYILYSSGTTGVPKciihgtgGVLLTHL------KEHGLHADLSRDD---CL------FYYTTCgwm 318
Cdd:PRK07656 156 PAERaPEVDPDDVADILFTSGTTGRPK-------GAMLTHRqllsnaADWAEYLGLTEGDrylAAnpffhvFGYKAG--- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 319 mwnWLVSVLAiGATAVLydgspfHP--GPERLIDLIDAEKISVFGTSPkflaTLEKAGLQ-PRLS-HDLGSLKGLISTGS 394
Cdd:PRK07656 226 ---VNAPLMR-GATILP------LPvfDPDEVFRLIETERITVLPGPP----TMYNSLLQhPDRSaEDLSSLRLAVTGAA 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 395 PLSPQsydyVYREIKGEL---------CLSSMSGgtdiVSCFvigNPvlPVRRGEMQCKSLAMAIE-----VWDDQGQPL 460
Cdd:PRK07656 292 SMPVA----LLERFESELgvdivltgyGLSEASG----VTTF---NR--LDDDRKTVAGTIGTAIAgvenkIVNELGEEV 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 461 -VGEKGElVCTRHFPAMpIGLWNDPD--RQKLRASyfsqfpGVWAQGDYAEQRPNGSLLIHGR-SDAVLnpggvrIGTAE 536
Cdd:PRK07656 359 pVGEVGE-LLVRGPNVM-KGYYDDPEatAAAIDAD------GWLHTGDLGRLDEEGYLYIVDRkKDMFI------VGGFN 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 537 IY-RQVEKV----PQVQESLAIG---QRWQDDVRVvlFVRLNDGVELDealEQQIRQVIRANTTPRHVPAKILAVTDIPR 608
Cdd:PRK07656 425 VYpAEVEEVlyehPAVAEAAVIGvpdERLGEVGKA--YVVLKPGAELT---EEELIAYCREHLAKYKVPRSIEFLDELPK 499
|
570
....*....|..
gi 799207711 609 TISGKIVELAVR 620
Cdd:PRK07656 500 NATGKVLKRALR 511
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
95-614 |
3.72e-29 |
|
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: 121.54 E-value: 3.72e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 95 RRRDDHPAVVaiseDGQREqLTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTLVGMLATTSLGAIWSCSSPDFG 174
Cdd:cd12117 8 ARTPDAVAVV----YGDRS-LTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 175 TQGVIDRFGQIEPKVLITCAGYRyagkdidqtaklneilARLPSLEQLIIVPYARPQArvedyqtharvtrwsdfypPGG 254
Cdd:cd12117 83 AERLAFMLADAGAKVLLTDRSLA----------------GRAGGLEVAVVIDEALDAG-------------------PAG 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 255 EPEFVAVPfDHPLYILYSSGTTGVPKciihgtgGVLLTH-----LKEHGLHADLSRDDCLFYYTTCGW-----MMWNWLV 324
Cdd:cd12117 128 NPAVPVSP-DDLAYVMYTSGSTGRPK-------GVAVTHrgvvrLVKNTNYVTLGPDDRVLQTSPLAFdastfEIWGALL 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 325 SvlaiGATAVLYDGSPFHPgPERLIDLIDAEKISV-FGTSPKF-LATLEKAGLqprlshdLGSLKGLISTGSPLSPQSYD 402
Cdd:cd12117 200 N----GARLVLAPKGTLLD-PDALGALIAEEGVTVlWLTAALFnQLADEDPEC-------FAGLRELLTGGEVVSPPHVR 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 403 YVYREIkGELCLSSMSG---GTDIVSCFVIGNPV-----LPVRR--GEMQCKSLamaievwDDQGQPL-VGEKGEL---- 467
Cdd:cd12117 268 RVLAAC-PGLRLVNGYGpteNTTFTTSHVVTELDevagsIPIGRpiANTRVYVL-------DEDGRPVpPGVPGELyvgg 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 468 --VCtrhfpampIGLWNDPDRQKLRASYFSQFPGV--WAQGDYAEQRPNGSLLIHGRSDAVLNPGGVRIGTAEIYRQVEK 543
Cdd:cd12117 340 dgLA--------LGYLNRPALTAERFVADPFGPGErlYRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRA 411
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 799207711 544 VPQVQES-LAIGQRWQDDVRVVLFVRLNDGVELDEaleqqIRQVIRANTTPRHVPAKILAVTDIPRTISGKI 614
Cdd:cd12117 412 HPGVREAvVVVREDAGGDKRLVAYVVAEGALDAAE-----LRAFLRERLPAYMVPAAFVVLDELPLTANGKV 478
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
115-621 |
9.40e-29 |
|
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: 119.55 E-value: 9.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 115 LTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTLVGMLATTSLGAIWSCSSPDFGTQGVIDRFGQIEPKVLITca 194
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVT-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 195 gyryagkDIDQTAKLNeilarlpsleqliivpyarpqarvedyqtharvtrwsdfyppggepefvavpfDHPLYILYSSG 274
Cdd:cd05973 79 -------DAANRHKLD-----------------------------------------------------SDPFVMMFTSG 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 275 TTGVPKCIIHGTGGVLLTH-LKEHGLhaDLSRDDCLFYYTTCGWM--MWNWLVSVLAIGATAVLYDGsPFhpGPERLIDL 351
Cdd:cd05973 99 TTGLPKGVPVPLRALAAFGaYLRDAV--DLRPEDSFWNAADPGWAygLYYAITGPLALGHPTILLEG-GF--SVESTWRV 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 352 IDAEKISVFGTSPKFLATLEKAGLqPRLSHDLGSLKGLISTGSPLSPQSYDYvYREIKGeLCLSSMSGGTDIvsCFVIGN 431
Cdd:cd05973 174 IERLGVTNLAGSPTAYRLLMAAGA-EVPARPKGRLRRVSSAGEPLTPEVIRW-FDAALG-VPIHDHYGQTEL--GMVLAN 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 432 ---PVLPVRRGEMQCKSLAMAIEVWDDQGQPLV-GEKGELVCTRH-FPAMPI-GLWNDPDrqklrasyfSQFPGVW-AQG 504
Cdd:cd05973 249 hhaLEHPVHAGSAGRAMPGWRVAVLDDDGDELGpGEPGRLAIDIAnSPLMWFrGYQLPDT---------PAIDGGYyLTG 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 505 DYAEQRPNGSLLIHGRSDAVLNPGGVRIGTAEIYRQVEKVPQVQESLAIGQrwQDDVR---VVLFVRLNDGVELDEALEQ 581
Cdd:cd05973 320 DTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGV--PDPERtevVKAFVVLRGGHEGTPALAD 397
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 799207711 582 QIRQVIRANTTPRHVPAKILAVTDIPRTISGKIVELAVRN 621
Cdd:cd05973 398 ELQLHVKKRLSAHAYPRTIHFVDELPKTPSGKIQRFLLRR 437
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
114-614 |
3.91e-28 |
|
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: 118.47 E-value: 3.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 114 QLTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTLVGMLATTSLGAIWSCSSPDFgTQGVIDR-FGQIEPKVLIT 192
Cdd:cd05911 10 ELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIY-TADELAHqLKISKPKVIFT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 193 cagyryagkDIDQTAKLNEILARLPSLEQlIIVPYARPqarvedyQTHARVTRWSDFYPPGGEPEFVAVPF---DHPLYI 269
Cdd:cd05911 89 ---------DPDGLEKVKEAAKELGPKDK-IIVLDDKP-------DGVLSIEDLLSPTLGEEDEDLPPPLKdgkDDTAAI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 270 LYSSGTTGVPKciihgtgGVLLTHlkeHGLHADLS-----------RDDCLFYYTTCGWMM-WNWLVSVLAIGATAVLYD 337
Cdd:cd05911 152 LYSSGTTGLPK-------GVCLSH---RNLIANLSqvqtflygndgSNDVILGFLPLYHIYgLFTTLASLLNGATVIIMP 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 338 gspfHPGPERLIDLIDAEKISVFGTSPKFLATLEKAglqPRL-SHDLGSLKGLISTGSPLSPQSYDYVyREIKGELCLSS 416
Cdd:cd05911 222 ----KFDSELFLDLIEKYKITFLYLVPPIAAALAKS---PLLdKYDLSSLRVILSGGAPLSKELQELL-AKRFPNATIKQ 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 417 MSGGTDiVSCFVIGNPVLPVRRGE-------MQCKslamaIEVWDDQGQPLVGEKGELVCtrHFPAMPIGLWNDPDrqkl 489
Cdd:cd05911 294 GYGMTE-TGGILTVNPDGDDKPGSvgrllpnVEAK-----IVDDDGKDSLGPNEPGEICV--RGPQVMKGYYNNPE---- 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 490 rASYFSQFPGVWAQ-GDYAEQRPNGSLLIHGRSDAVLNPGGVRIGTAEIyrqvEKV----PQVQESLAIGQrwQDDV--- 561
Cdd:cd05911 362 -ATKETFDEDGWLHtGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAEL----EAVllehPGVADAAVIGI--PDEVsge 434
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 799207711 562 RVVLFVRLNDGvelDEALEQQIRQVIRanttPRHVPAK-----ILAVTDIPRTISGKI 614
Cdd:cd05911 435 LPRAYVVRKPG---EKLTEKEVKDYVA----KKVASYKqlrggVVFVDEIPKSASGKI 485
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
116-552 |
1.21e-27 |
|
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: 115.83 E-value: 1.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 116 TYAELAEHVAGLQKSLRAA-GVTQGDRVAACMPNTWQTLVGMLATTSLGAIW---SCSSPDfgtqgviDRFGQI----EP 187
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYvplDPAYPA-------ERLAFIledaGA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 188 KVLITCAGYRYAGKDIDQTAKLNEILArLPSLEQLiivpyarpqarvedyqtharvtrwsdfyPPGGEPEFVAVPfDHPL 267
Cdd:TIGR01733 74 RLLLTDSALASRLAGLVLPVILLDPLE-LAALDDA----------------------------PAPPPPDAPSGP-DDLA 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 268 YILYSSGTTGVPKciihgtgGVLLTH------LKEHGLHADLSRDDCLFYYTT-----CGWMMWnwlvSVLAIGATAVLY 336
Cdd:TIGR01733 124 YVIYTSGSTGRPK-------GVVVTHrslvnlLAWLARRYGLDPDDRVLQFASlsfdaSVEEIF----GALLAGATLVVP 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 337 DGSPFHPGPERLIDLIDAEKISVFGTSPKFLATLEKAGLQprlshDLGSLKGLISTGSPLSPQSYDyVYREIKGELCLSS 416
Cdd:TIGR01733 193 PEDEERDDAALLAALIAEHPVTVLNLTPSLLALLAAALPP-----ALASLRLVILGGEALTPALVD-RWRARGPGARLIN 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 417 MSG---GTDIVSCFVIgnPVLPVRRGEMQ--CKSLA-MAIEVWDDQGQPL-VGEKGELVctrhfpampI-------GLWN 482
Cdd:TIGR01733 267 LYGpteTTVWSTATLV--DPDDAPRESPVpiGRPLAnTRLYVLDDDLRPVpVGVVGELY---------IggpgvarGYLN 335
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 799207711 483 DPDR--QKLRASYFSQFPG--VWAQGDYAEQRPNGSLLIHGRSDAVLNPGGVRIGTAEIYRQVEKVPQVQESLA 552
Cdd:TIGR01733 336 RPELtaERFVPDPFAGGDGarLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
73-642 |
1.32e-26 |
|
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: 116.11 E-value: 1.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 73 DAEMPSAQWFPGAtlnFAEHLlRRRDDHPAVVaiseDGQReQLTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQT 152
Cdd:COG1020 469 AAPYPADATLHEL---FEAQA-ARTPDAVAVV----FGDQ-SLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEM 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 153 LVGMLATTSLGAIW---SCSSPDfgtqgviDRFGQI----EPKVLITCAGYRyagkdidqtAKLNEILARLPSLEQLIIV 225
Cdd:COG1020 540 VVALLAVLKAGAAYvplDPAYPA-------ERLAYMledaGARLVLTQSALA---------ARLPELGVPVLALDALALA 603
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 226 PYarpqarvedyqtharvtrwsdfypPGGEPEFVAVPfDHPLYILYSSGTTGVPKciihgtgGVLLTH------LKEHGL 299
Cdd:COG1020 604 AE------------------------PATNPPVPVTP-DDLAYVIYTSGSTGRPK-------GVMVEHralvnlLAWMQR 651
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 300 HADLSRDDCLFYYTTCG-----WMMWNWLVSvlaiGATAVLYDGSPfHPGPERLIDLIDAEKISVFGTSPKFLATLEKAG 374
Cdd:COG1020 652 RYGLGPGDRVLQFASLSfdasvWEIFGALLS----GATLVLAPPEA-RRDPAALAELLARHRVTVLNLTPSLLRALLDAA 726
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 375 LQprlshDLGSLKGLISTGSPLSPQSYDYvYREIKGELCLSSMSG---GTDIVSCFVIGNPVLPVRR---GemqcKSLA- 447
Cdd:COG1020 727 PE-----ALPSLRLVLVGGEALPPELVRR-WRARLPGARLVNLYGpteTTVDSTYYEVTPPDADGGSvpiG----RPIAn 796
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 448 MAIEVWDDQGQPL-VGEKGELVC-----TRhfpampiGLWNDPDrqkLRASYFSQFPGVWAQ------GDYAEQRPNGSL 515
Cdd:COG1020 797 TRVYVLDAHLQPVpVGVPGELYIggaglAR-------GYLNRPE---LTAERFVADPFGFPGarlyrtGDLARWLPDGNL 866
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 516 LIHGRSDAVLNPGGVRIGTAEIYRQVEKVPQVQESLAIGQRWQD-DVRVVLFVRLNDGVELDEALEQQIRQVIRAnttPR 594
Cdd:COG1020 867 EFLGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDAPgDKRLVAYVVPEAGAAAAAALLRLALALLLP---PY 943
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 799207711 595 HVPAKILAVTDIPRTISGKIVELAVRNVVHGEPVKNTDALANPQALEQ 642
Cdd:COG1020 944 MVPAAVVLLLPLPLTGNGKLDRLALPAPAAAAAAAAAAPPAEEEEEEA 991
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
100-612 |
5.40e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 112.53 E-value: 5.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 100 HPAVVAISEDGQreQLTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTLVGMLATTSLGAIWSCSSPDFGTQGVI 179
Cdd:PRK06164 23 RPDAVALIDEDR--PLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 180 DRFGQIEPKVLITCAGYRyagkDIDQTAKLNEIL-ARLPSLEQLIIV-------PYARPQARVEDYQTHARVTrwsdfyP 251
Cdd:PRK06164 101 HILGRGRARWLVVWPGFK----GIDFAAILAAVPpDALPPLRAIAVVddaadatPAPAPGARVQLFALPDPAP------P 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 252 PGGEPEfvAVPFDHPLYILYSSGTTGVPKCIIHGTGGVLlthlkEHGlHAD-----LSRDDC-LFYYTTCGWMMWNWLVS 325
Cdd:PRK06164 171 AAAGER--AADPDAGALLFTTSGTTSGPKLVLHRQATLL-----RHA-RAIaraygYDPGAVlLAALPFCGVFGFSTLLG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 326 VLAIGATAVLydgSPFHPGPERLIDLIDAEKISVFGtSPKFLATLEKAGLQPRlshDLGSLKgLISTGSpLSPQSYDYVY 405
Cdd:PRK06164 243 ALAGGAPLVC---EPVFDAARTARALRRHRVTHTFG-NDEMLRRILDTAGERA---DFPSAR-LFGFAS-FAPALGELAA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 406 REIKGELCLSSMSGGTDIVSCFVIGNPVLPVR-RGEMQCKSLAMAIEV--WDDQGQPLV--GEKGELVCTRhfPAMPIGL 480
Cdd:PRK06164 314 LARARGVPLTGLYGSSEVQALVALQPATDPVSvRIEGGGRPASPEARVraRDPQDGALLpdGESGEIEIRA--PSLMRGY 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 481 WNDPD--RQKLRASyfsqfpGVWAQGDYAEQRPNGSLLIHGRSDAVLNPGGVRIGTAEIYRQVEKVPQVQESLAIGQRWQ 558
Cdd:PRK06164 392 LDNPDatARALTDD------GYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGATRD 465
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 799207711 559 DDVRVVLFVRLNDGVELDEAleqQIRQVIRANTTPRHVPAKILAVTDIPRTISG 612
Cdd:PRK06164 466 GKTVPVAFVIPTDGASPDEA---GLMAACREALAGFKVPARVQVVEAFPVTESA 516
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
99-614 |
6.22e-26 |
|
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: 111.59 E-value: 6.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 99 DHPAVVAISEdgqreQLTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTLVGMLATTSLGAIwscsspdfgtqgv 178
Cdd:cd12114 2 DATAVICGDG-----TLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAA------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 179 idrfgqiepkvlitcagyrYAGKDIDQ-TAKLNEILARlpSLEQLIIVPYARPQARVEdyqtHARVTRWSDfYPPGGEPE 257
Cdd:cd12114 64 -------------------YVPVDIDQpAARREAILAD--AGARLVLTDGPDAQLDVA----VFDVLILDL-DALAAPAP 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 258 FVAVPF--DHPLYILYSSGTTGVPKciihgtgGVLLTH---------------LKEH-------GLHADLSRDDcLFyyt 313
Cdd:cd12114 118 PPPVDVapDDLAYVIFTSGSTGTPK-------GVMISHraalntildinrrfaVGPDdrvlalsSLSFDLSVYD-IF--- 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 314 tcgwmmwnwlvSVLAIGATAVLYDGSPfHPGPERLIDLIDAEKISVFGTSPKFLATLEKAGLQPRLshDLGSLKGLISTG 393
Cdd:cd12114 187 -----------GALSAGATLVLPDEAR-RRDPAHWAELIERHGVTLWNSVPALLEMLLDVLEAAQA--LLPSLRLVLLSG 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 394 S--PLS-PQSYdyvyREIKGELCLSSMSGGTDIVscfvIGNPVLPVRRGEMQCKS------LA-MAIEVWDDQGQPL-VG 462
Cdd:cd12114 253 DwiPLDlPARL----RALAPDARLISLGGATEAS----IWSIYHPIDEVPPDWRSipygrpLAnQRYRVLDPRGRDCpDW 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 463 EKGELVCTRHFPAMpiGLWNDPdrQKLRASYFSQFPGV--WAQGDYAEQRPNGSLLIHGRSDAVLNPGGVRIGTAEIYRQ 540
Cdd:cd12114 325 VPGELWIGGRGVAL--GYLGDP--ELTAARFVTHPDGErlYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAA 400
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 799207711 541 VEKVPQVQESLAIGQRWQDDVRVVLFVRLNDGVelDEALEQQIRQVIRANTTPRHVPAKILAVTDIPRTISGKI 614
Cdd:cd12114 401 LQAHPGVARAVVVVLGDPGGKRLAAFVVPDNDG--TPIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKV 472
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
95-622 |
6.85e-26 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 112.17 E-value: 6.85e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 95 RRRDDHPAVVaISEDGQReqLTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTLVGMLATTSLGAIWSCSSPDFG 174
Cdd:PRK12583 29 ARFPDREALV-VRHQALR--YTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 175 TQGVIDRFGQIEPKVLITCAGYRYAgkdiDQTAKLNEIL-------------ARLPSLEQLIIVPYARPQArvedyqtha 241
Cdd:PRK12583 106 ASELEYALGQSGVRWVICADAFKTS----DYHAMLQELLpglaegqpgalacERLPELRGVVSLAPAPPPG--------- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 242 rVTRWSDFYppgGEPEFV----------AVPFDHPLYILYSSGTTGVPKciihgtgGVLLTH---LKEHGLHAD---LSR 305
Cdd:PRK12583 173 -FLAWHELQ---ARGETVsrealaerqaSLDRDDPINIQYTSGTTGFPK-------GATLSHhniLNNGYFVAEslgLTE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 306 DDCL-----FYYttCGWMMWNWLVSVlAIGATaVLYDGSPFHPgperLIDL--IDAEK-ISVFGTSPKFLATLEkaglQP 377
Cdd:PRK12583 242 HDRLcvpvpLYH--CFGMVLANLGCM-TVGAC-LVYPNEAFDP----LATLqaVEEERcTALYGVPTMFIAELD----HP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 378 -RLSHDLGSLKGLISTGSPLSPQsydyVYREIKGELCLSSMSGG-----TDIVSCFVIGNPVLPvRRGEMQCKSLA-MAI 450
Cdd:PRK12583 310 qRGNFDLSSLRTGIMAGAPCPIE----VMRRVMDEMHMAEVQIAygmteTSPVSLQTTAADDLE-RRVETVGRTQPhLEV 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 451 EVWDDQGQPL-VGEKGELvCTRHFPAMpIGLWNDPDRQKLRASYfsqfPGVWAQGDYAEQRPNGSLLIHGRSDAVLNPGG 529
Cdd:PRK12583 385 KVVDPDGATVpRGEIGEL-CTRGYSVM-KGYWNNPEATAESIDE----DGWMHTGDLATMDEQGYVRIVGRSKDMIIRGG 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 530 VRIGTAEIYRQVEKVPQVQESLAIG---QRWQDDvrVVLFVRLNDGVELDealEQQIRQVIRANTTPRHVPAKILAVTDI 606
Cdd:PRK12583 459 ENIYPREIEEFLFTHPAVADVQVFGvpdEKYGEE--IVAWVRLHPGHAAS---EEELREFCKARIAHFKVPRYFRFVDEF 533
|
570
....*....|....*.
gi 799207711 607 PRTISGKIVELAVRNV 622
Cdd:PRK12583 534 PMTVTGKVQKFRMREI 549
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
94-620 |
2.04e-25 |
|
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: 109.96 E-value: 2.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 94 LRRRDDHPAVVaisEDGQReqLTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTLVGMLATTSLGAIwscsspdf 173
Cdd:cd05936 9 ARRFPDKTALI---FMGRK--LTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAV-------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 174 gtqgVIdrfgQIEPkvLITCAGYRYAGKDIDqtAKLNEILARLPSLeqliIVPYARPQARVEDyqtharvtrwsdfyppg 253
Cdd:cd05936 76 ----VV----PLNP--LYTPRELEHILNDSG--AKALIVAVSFTDL----LAAGAPLGERVAL----------------- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 254 gEPEFVAVpfdhplyILYSSGTTGVPKciihgtgGVLLTH---------LKEHGLHADLSRDDCL--------FYYTTCg 316
Cdd:cd05936 123 -TPEDVAV-------LQYTSGTTGVPK-------GAMLTHrnlvanalqIKAWLEDLLEGDDVVLaalplfhvFGLTVA- 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 317 wmmwnwLVSVLAIGATAVLydgSPfHPGPERLIDLIDAEKISVFGTSPKFLATLekAGLQPRLSHDLGSLKGLISTGSPL 396
Cdd:cd05936 187 ------LLLPLALGATIVL---IP-RFRPIGVLKEIRKHRVTIFPGVPTMYIAL--LNAPEFKKRDFSSLRLCISGGAPL 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 397 SPQsydyVYREIK----GELC----LSSMSGgtdiVSCFvigNPVLPVRR-GEMQCKSLAMAIEVWDDQGQPL-VGEKGE 466
Cdd:cd05936 255 PVE----VAERFEeltgVPIVegygLTETSP----VVAV---NPLDGPRKpGSIGIPLPGTEVKIVDDDGEELpPGEVGE 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 467 LvCTRHFPAMPiGLWNDPD--RQKLRASYFsqfpgvwAQGDYAEQRPNGSLLIHGRSDAVLNPGGVrigtaEIY-RQVEK 543
Cdd:cd05936 324 L-WVRGPQVMK-GYWNRPEetAEAFVDGWL-------RTGDIGYMDEDGYFFIVDRKKDMIIVGGF-----NVYpREVEE 389
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 544 V----PQVQESLAIGQRwqDDVR---VVLFVRLNDGVELDealEQQIRQVIRANTTPRHVPAKILAVTDIPRTISGKIVE 616
Cdd:cd05936 390 VlyehPAVAEAAVVGVP--DPYSgeaVKAFVVLKEGASLT---EEEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILR 464
|
....
gi 799207711 617 LAVR 620
Cdd:cd05936 465 RELR 468
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
101-621 |
4.47e-25 |
|
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.
Pssm-ID: 341249 [Multi-domain] Cd Length: 493 Bit Score: 109.32 E-value: 4.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 101 PAVVAISEDGQREQLTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTLVGMLATTSLGAIWSCSSPDFGTQGVID 180
Cdd:cd05926 1 PDAPALVVPGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 181 RFGQIEPKVLITCAGYRYAgkdiDQTAKLNEILARLpSLEQLIIVPYARPQARVEDYqtharvtrwSDFYPPGGEPEFVA 260
Cdd:cd05926 81 YLADLGSKLVLTPKGELGP----ASRAASKLGLAIL-ELALDVGVLIRAPSAESLSN---------LLADKKNAKSEGVP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 261 VPFDHPLyILYSSGTTGVPKciihgtgGVLLTHL----------KEHglhaDLSRDDC------LFYY--TTCGwmmwnw 322
Cdd:cd05926 147 LPDDLAL-ILHTSGTTGRPK-------GVPLTHRnlaasatnitNTY----KLTPDDRtlvvmpLFHVhgLVAS------ 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 323 LVSVLAIGATAVL---YDGSPFHPgperlidLIDAEKISVFGTSPkflaTLEKAGLQ---PRLSHDLGSLKGLISTGSPL 396
Cdd:cd05926 209 LLSTLAAGGSVVLpprFSASTFWP-------DVRDYNATWYTAVP----TIHQILLNrpePNPESPPPKLRFIRSCSASL 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 397 SPQsydyVYREIKGE-----LCLSSMSGGTDIVSCfvigNPVLPVRRGEMQC-KSLAMAIEVWDDQGQPL-VGEKGElVC 469
Cdd:cd05926 278 PPA----VLEALEATfgapvLEAYGMTEAAHQMTS----NPLPPGPRKPGSVgKPVGVEVRILDEDGEILpPGVVGE-IC 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 470 TRHfPAMPIGLWNDPdrqKLRASYFsqFPGVWAQ-GDYAEQRPNGSLLIHGRSDAVLNPGGVRIGTAEIyrqvEKV---- 544
Cdd:cd05926 349 LRG-PNVTRGYLNNP---EANAEAA--FKDGWFRtGDLGYLDADGYLFLTGRIKELINRGGEKISPLEV----DGVllsh 418
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 545 PQVQESLAIGQrwQDDV---RVVLFVRLNDGVELDEAleqQIRQVIRANTTPRHVPAKILAVTDIPRTISGKIVELAVRN 621
Cdd:cd05926 419 PAVLEAVAFGV--PDEKygeEVAAAVVLREGASVTEE---ELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKVAE 493
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
89-614 |
4.19e-24 |
|
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: 106.21 E-value: 4.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 89 FAEHLlRRRDDHPAVVAisedgQREQLTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTLVGMLATTSLGAIWSC 168
Cdd:cd17646 4 VAEQA-ARTPDAPAVVD-----EGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 169 SSPDFGTqgviDRFGQI----EPKVLITcagyryagkdidqTAKLNEILARLPsleqliivpyarpqarvedyqTHARVT 244
Cdd:cd17646 78 LDPGYPA----DRLAYMladaGPAVVLT-------------TADLAARLPAGG---------------------DVALLG 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 245 RWSDFYPPGGEPEFVAVPfDHPLYILYSSGTTGVPKciihgtgGVLLTHlkeHGL---------HADLSRDDCLFYYTTC 315
Cdd:cd17646 120 DEALAAPPATPPLVPPRP-DNLAYVIYTSGSTGRPK-------GVMVTH---AGIvnrllwmqdEYPLGPGDRVLQKTPL 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 316 GW--MMWNWLVSVLAiGATAVLY--DGspfHPGPERLIDLIDAEKISVFGTSPKFLATLekagLQPRLSHDLGSLKGLIS 391
Cdd:cd17646 189 SFdvSVWELFWPLVA-GARLVVArpGG---HRDPAYLAALIREHGVTTCHFVPSMLRVF----LAEPAAGSCASLRRVFC 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 392 TGSPLSPQSYDYVYREIKGElcLSSMSGGT----DIVSCFV----------IGNPVLPVRrgemqckslamaIEVWDDQG 457
Cdd:cd17646 261 SGEALPPELAARFLALPGAE--LHNLYGPTeaaiDVTHWPVrgpaetpsvpIGRPVPNTR------------LYVLDDAL 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 458 QPL-VGEKGELVCTRhfPAMPIGLWNDPDrqkLRASYF--SQF-PG--VWAQGDYAEQRPNGSLLIHGRSDAVLNPGGVR 531
Cdd:cd17646 327 RPVpVGVPGELYLGG--VQLARGYLGRPA---LTAERFvpDPFgPGsrMYRTGDLARWRPDGALEFLGRSDDQVKIRGFR 401
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 532 IGTAEIYRQVEKVPQVQESLAIGQRWQD-DVRVVLFVRLNDGVEldEALEQQIRQVIRANTTPRHVPAKILAVTDIPRTI 610
Cdd:cd17646 402 VEPGEIEAALAAHPAVTHAVVVARAAPAgAARLVGYVVPAAGAA--GPDTAALRAHLAERLPEYMVPAAFVVLDALPLTA 479
|
....
gi 799207711 611 SGKI 614
Cdd:cd17646 480 NGKL 483
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
93-614 |
5.17e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 106.17 E-value: 5.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 93 LLRR-RDDHPAVVAISeDGQREqLTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTLVGMLATTSLGAIWscsSP 171
Cdd:PRK08316 16 ILRRsARRYPDKTALV-FGDRS-WTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVH---VP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 172 -DFGTQGVIDRF--GQIEPKVLITcagyryagkDIDQTAKLNEILARLPSlEQLIIVPYARPQARVedyqthARVTRWSD 248
Cdd:PRK08316 91 vNFMLTGEELAYilDHSGARAFLV---------DPALAPTAEAALALLPV-DTLILSLVLGGREAP------GGWLDFAD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 249 FYPPGGEPEF-VAVPFDHPLYILYSSGTTGVPKciihgtgGVLLTH---LKEHG---LHADLSRDD----CLFYYTTCGw 317
Cdd:PRK08316 155 WAEAGSVAEPdVELADDDLAQILYTSGTESLPK-------GAMLTHralIAEYVsciVAGDMSADDiplhALPLYHCAQ- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 318 mMWNWLVSVLAIGATAVLYDGspfhPGPERLIDLIDAEKISVFGTSPK-FLATLEKAGLQPRlshDLGSL-KGLIstGSP 395
Cdd:PRK08316 227 -LDVFLGPYLYVGATNVILDA----PDPELILRTIEAERITSFFAPPTvWISLLRHPDFDTR---DLSSLrKGYY--GAS 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 396 LSPqsydyvyREIKGEL--CLSSMS-----GGTDIVscfvignPVLPVRRGEMQCKSLAMA------IE--VWDDQGQPL 460
Cdd:PRK08316 297 IMP-------VEVLKELreRLPGLRfyncyGQTEIA-------PLATVLGPEEHLRRPGSAgrpvlnVEtrVVDDDGNDV 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 461 -VGEKGElVCTRHFPAMpIGLWNDPDRQKlrasyfSQFPGVW-AQGDYAEQRPNGSLLIHGRSDAVLNPGGVRIGTaeiy 538
Cdd:PRK08316 363 aPGEVGE-IVHRSPQLM-LGYWDDPEKTA------EAFRGGWfHSGDLGVMDEEGYITVVDRKKDMIKTGGENVAS---- 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 539 RQVEKV----PQVQESLAIG---QRWQDDVRVVlfVRLNDGVELDEAleqqirQVI---RANTTPRHVPAKILAVTDIPR 608
Cdd:PRK08316 431 REVEEAlythPAVAEVAVIGlpdPKWIEAVTAV--VVPKAGATVTED------ELIahcRARLAGFKVPKRVIFVDELPR 502
|
....*.
gi 799207711 609 TISGKI 614
Cdd:PRK08316 503 NPSGKI 508
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
83-614 |
1.28e-23 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 106.67 E-value: 1.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 83 PGATLnfAEHLLRRRDDHPAVVAISEDGQreQLTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTLVGMLATTSL 162
Cdd:PRK10252 456 PETTL--SALVAQQAAKTPDAPALADARY--QFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEA 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 163 GAIWSCSSPDFGTQGVIDRFGQIEPKVLITCAgyryagkdidqtaklnEILARLPSLEQLIIVPYARPQArvedyqthar 242
Cdd:PRK10252 532 GAAWLPLDTGYPDDRLKMMLEDARPSLLITTA----------------DQLPRFADVPDLTSLCYNAPLA---------- 585
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 243 vtrwsdfyPPGGEPEFVAVPfDHPLYILYSSGTTGVPKciihgtgGVLLTH------LKEHGLHADLSRDDCLFYYTTCG 316
Cdd:PRK10252 586 --------PQGAAPLQLSQP-HHTAYIIFTSGSTGRPK-------GVMVGQtaivnrLLWMQNHYPLTADDVVLQKTPCS 649
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 317 WMmwnwlVSV------LAIGATAVLyDGSPFHPGPERLIDLIDAEKISVFGTSPKFLATLEKAGLQPRLSHDLGSLKGLI 390
Cdd:PRK10252 650 FD-----VSVweffwpFIAGAKLVM-AEPEAHRDPLAMQQFFAEYGVTTTHFVPSMLAAFVASLTPEGARQSCASLRQVF 723
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 391 STGSPLSPQSYDYVYREIKGElcLSSMSGGTDI---VSCFVIGNPVLPVRRGemqcKSLAMAIEVW-------DDQGQPL 460
Cdd:PRK10252 724 CSGEALPADLCREWQQLTGAP--LHNLYGPTEAavdVSWYPAFGEELAAVRG----SSVPIGYPVWntglrilDARMRPV 797
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 461 -VGEKGELVCTRHFPAMpiGLWNDPDrqkLRASYFSQFPGV-----WAQGDYAEQRPNGSLLIHGRSDAVLNPGGVRIGT 534
Cdd:PRK10252 798 pPGVAGDLYLTGIQLAQ--GYLGRPD---LTASRFIADPFApgermYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIEL 872
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 535 AEIYRQVEKVPQVQESLAIGQRWQDDV-------RVVLFVRLNDGVELD-EALEQQIRQviranTTPRH-VPAKILAVTD 605
Cdd:PRK10252 873 GEIDRAMQALPDVEQAVTHACVINQAAatggdarQLVGYLVSQSGLPLDtSALQAQLRE-----RLPPHmVPVVLLQLDQ 947
|
....*....
gi 799207711 606 IPRTISGKI 614
Cdd:PRK10252 948 LPLSANGKL 956
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
89-614 |
1.86e-23 |
|
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: 103.94 E-value: 1.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 89 FAEHLLRRRDDHPAVVAisedgQREQLTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTLVGMLAttslgaiwsc 168
Cdd:cd12115 4 LVEAQAARTPDAIALVC-----GDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLA---------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 169 sspdfgtqgvidrfgqiepkVLITCAGYryagkdidqtaklneilarlpsleqliiVPY--ARPQARVEDYQTHARvtrw 246
Cdd:cd12115 69 --------------------VLKAGAAY----------------------------VPLdpAYPPERLRFILEDAQ---- 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 247 sdfyppggePEFVAVPFDHPLYILYSSGTTGVPKciihgtgGVLLTHlkeHGLHADLsrddclfyyttcGWMMWNW---- 322
Cdd:cd12115 97 ---------ARLVLTDPDDLAYVIYTSGSTGRPK-------GVAIEH---RNAAAFL------------QWAAAAFsaee 145
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 323 LVSVLAigATAVLYDGSPF-------HPGPERLID----LID---AEKISVFGTSPKFLATLEKAGLQPRlshdlgSLKG 388
Cdd:cd12115 146 LAGVLA--STSICFDLSVFelfgplaTGGKVVLADnvlaLPDlpaAAEVTLINTVPSAAAELLRHDALPA------SVRV 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 389 LISTGSPLSPQSYDYVYREIKGElCLSSMSGGTDIVSCfvigNPVLPVRRGEMQCKSLAMAI-----EVWDDQGQPL-VG 462
Cdd:cd12115 218 VNLAGEPLPRDLVQRLYARLQVE-RVVNLYGPSEDTTY----STVAPVPPGASGEVSIGRPLantqaYVLDRALQPVpLG 292
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 463 EKGELVCtrHFPAMPIGLWNDPdrqKLRASYF---SQFPG--VWAQGDYAEQRPNGSLLIHGRSDAVLNPGGVRIGTAEI 537
Cdd:cd12115 293 VPGELYI--GGAGVARGYLGRP---GLTAERFlpdPFGPGarLYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEI 367
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 538 YRQVEKVPQVQESLAIGqrWQD---DVRVVLFVRLNDGVELD-EALEQQIRQVIranttPRH-VPAKILAVTDIPRTISG 612
Cdd:cd12115 368 EAALRSIPGVREAVVVA--IGDaagERRLVAYIVAEPGAAGLvEDLRRHLGTRL-----PAYmVPSRFVRLDALPLTPNG 440
|
..
gi 799207711 613 KI 614
Cdd:cd12115 441 KI 442
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
91-626 |
2.13e-23 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 104.71 E-value: 2.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 91 EHLLRRRDDHPAVVAISEDGQREQLTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTLVGMLATTSLGAIwSCSS 170
Cdd:PRK05857 18 DRVFEQARQQPEAIALRRCDGTSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAI-AVMA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 171 PDFGTQGVIDRFGQI-EPKVLITCAGYRYAgkdidqTAKLNEILARLPSLeqliivpyarpqaRVEDYQTHARVTRWSDF 249
Cdd:PRK05857 97 DGNLPIAAIERFCQItDPAAALVAPGSKMA------SSAVPEALHSIPVI-------------AVDIAAVTRESEHSLDA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 250 YPPGGEPEFVAvpfDHPLYILYSSGTTGVPKciihgtgGVLLTHLKEHGLhADLSRDDCLFYYTtcgWM----------- 318
Cdd:PRK05857 158 ASLAGNADQGS---EDPLAMIFTSGTTGEPK-------AVLLANRTFFAV-PDILQKEGLNWVT---WVvgettysplpa 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 319 -----MWnWLVSVLAIGATAVlydgspfhPGPER---LIDLIDAEKISVFGTSP----KFLATLEKAGLqprlshDLGSL 386
Cdd:PRK05857 224 thiggLW-WILTCLMHGGLCV--------TGGENttsLLEILTTNAVATTCLVPtllsKLVSELKSANA------TVPSL 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 387 KGLISTGSplSPQSYDYVYREIKG---------------ELCLSSMSGGTDIVSCFVIGNPvLPvrrgemqckslamAIE 451
Cdd:PRK05857 289 RLVGYGGS--RAIAADVRFIEATGvrtaqvyglsetgctALCLPTDDGSIVKIEAGAVGRP-YP-------------GVD 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 452 VW---DDQGQPLVGEKGELVCTRHF----PAMPIGLWNDPDR-QKLRASyfsqfpGVWAQGDYAEQRPNGSLLIHGRSDA 523
Cdd:PRK05857 353 VYlaaTDGIGPTAPGAGPSASFGTLwiksPANMLGYWNNPERtAEVLID------GWVNTGDLLERREDGFFYIKGRSSE 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 524 VLNPGGVRIGTAEIYRQVEKVPQVQESlAIGQRWQDDVRVVLFVRLNDGVELDEALEQQIRQVI----RANTTPRHVPAK 599
Cdd:PRK05857 427 MIICGGVNIAPDEVDRIAEGVSGVREA-ACYEIPDEEFGALVGLAVVASAELDESAARALKHTIaarfRRESEPMARPST 505
|
570 580
....*....|....*....|....*..
gi 799207711 600 ILAVTDIPRTISGKIVELAVRNVVHGE 626
Cdd:PRK05857 506 IVIVTDIPRTQSGKVMRASLAAAATAD 532
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
100-614 |
3.00e-23 |
|
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: 103.10 E-value: 3.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 100 HPAVVAISEDGQReqLTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTLVGMLATTSLGAIwscsspdfgtqgvi 179
Cdd:cd05945 4 NPDRPAVVEGGRT--LTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHA-------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 180 drfgqiepkvlitcagyrYAGKDIDQTAK-LNEILARlpsleqliivpyARPQArvedyqtharvtrwsdfyppggepeF 258
Cdd:cd05945 68 ------------------YVPLDASSPAErIREILDA------------AKPAL-------------------------L 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 259 VAVPfDHPLYILYSSGTTGVPKCIIHGTGGVLLTH--------LKEH---GLHADLSRDDCLFYYTTCgwmmwnwlvsvL 327
Cdd:cd05945 93 IADG-DDNAYIIFTSGSTGRPKGVQISHDNLVSFTnwmlsdfpLGPGdvfLNQAPFSFDLSVMDLYPA-----------L 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 328 AIGAT------AVLYDgspfhpgPERLIDLIDAEKISVFGTSPKFLATLekAGLQPRLSHDLGSLKGLISTGSPLSPQsy 401
Cdd:cd05945 161 ASGATlvpvprDATAD-------PKQLFRFLAEHGITVWVSTPSFAAMC--LLSPTFTPESLPSLRHFLFCGEVLPHK-- 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 402 dyVYREIKGELCLSSMS---GGTDI-VSCFVI--------GNPVLPVRRgemqCKSlAMAIEVWDDQGQPL-VGEKGELV 468
Cdd:cd05945 230 --TARALQQRFPDARIYntyGPTEAtVAVTYIevtpevldGYDRLPIGY----AKP-GAKLVILDEDGRPVpPGEKGELV 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 469 CTRhfPAMPIGLWNDPDrqkLRASYFSQFPGVWA--QGDYAEQRPNGSLLIHGRSDAVLNPGGVRIGTAEIYRQVEKVPQ 546
Cdd:cd05945 303 ISG--PSVSKGYLNNPE---KTAAAFFPDEGQRAyrTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPG 377
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 799207711 547 VQESLAIGQRWQDDV-RVVLFVRLNDGVEldEALEQQIRQVIRANTTPRHVPAKILAVTDIPRTISGKI 614
Cdd:cd05945 378 VKEAVVVPKYKGEKVtELIAFVVPKPGAE--AGLTKAIKAELAERLPPYMIPRRFVYLDELPLNANGKI 444
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
79-615 |
4.10e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 103.85 E-value: 4.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 79 AQWFPGATLnfAEHLLRRRDDHPAVvaISEDGQreqLTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTLVGMLA 158
Cdd:PRK07788 46 RRYGPFAGL--VAHAARRAPDRAAL--IDERGT---LTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 159 TTSLGAIWSCSSPDFGT---QGVIDRFGQiepKVLItcagyryagkdIDQ--TAKLNEILARLPSLEQLIIVPYARPQAR 233
Cdd:PRK07788 119 AGKVGARIILLNTGFSGpqlAEVAAREGV---KALV-----------YDDefTDLLSALPPDLGRLRAWGGNPDDDEPSG 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 234 VEDyQTHARVTRwsdfyppGGEPEFVAVPFDHPLYILYSSGTTGVPKCIIHG------TGGVLLTHLKehglhadLSRDD 307
Cdd:PRK07788 185 STD-ETLDDLIA-------GSSTAPLPKPPKPGGIVILTSGTTGTPKGAPRPepsplaPLAGLLSRVP-------FRAGE 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 308 C------LFYYTtcGWMMWNwlVSvLAIGATAVL---YDgspfhpgPERLIDLIDAEKISVFGTSPKFLATLEKAGLQPR 378
Cdd:PRK07788 250 TtllpapMFHAT--GWAHLT--LA-MALGSTVVLrrrFD-------PEATLEDIAKHKATALVVVPVMLSRILDLGPEVL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 379 LSHDLGSLKGLISTGSPLSPQSYDYVYREIkGELcLSSMSGGTDIVSCFV------------IGNPVLPVRrgemqcksl 446
Cdd:PRK07788 318 AKYDTSSLKIIFVSGSALSPELATRALEAF-GPV-LYNLYGSTEVAFATIatpedlaeapgtVGRPPKGVT--------- 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 447 amaIEVWDDQGQPL-VGEKGELVCTRHFPAmpIGLWNDPDRQKLRasyfsqfpGVWAQGDYAEQRPNGSLLIHGRSDAVL 525
Cdd:PRK07788 387 ---VKILDENGNEVpRGVVGRIFVGNGFPF--EGYTDGRDKQIID--------GLLSSGDVGYFDEDGLLFVDGRDDDMI 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 526 NPGGVRIGTAEIYRQVEKVPQVQESLAIGqrwQDDV----RVVLFVRLNDGVELDealEQQIRQVIRANTTPRHVPAKIL 601
Cdd:PRK07788 454 VSGGENVFPAEVEDLLAGHPDVVEAAVIG---VDDEefgqRLRAFVVKAPGAALD---EDAIKDYVRDNLARYKVPRDVV 527
|
570
....*....|....
gi 799207711 602 AVTDIPRTISGKIV 615
Cdd:PRK07788 528 FLDELPRNPTGKVL 541
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
101-614 |
2.16e-22 |
|
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: 100.52 E-value: 2.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 101 PAVVAISEDGQReqLTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTLVGMLATTSLGAIWSCSSPDFgtqgvid 180
Cdd:cd17649 1 PDAVALVFGDQS--LSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEY------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 181 rfgqiepkvlitcagyryagkdidqtaklneilarlpsleqliivPYARPQARVEDyqtharvtrwsdfyppGGEPEFVA 260
Cdd:cd17649 72 ---------------------------------------------PAERLRYMLED----------------SGAGLLLT 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 261 VPFDHPLYILYSSGTTGVPKCII--HGTggvLLTHLKEHGLHADLSRDDCLFYYTTCGW--MMWNWLVSvLAIGATAVLY 336
Cdd:cd17649 91 HHPRQLAYVIYTSGSTGTPKGVAvsHGP---LAAHCQATAERYGLTPGDRELQFASFNFdgAHEQLLPP-LICGACVVLR 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 337 DGSPFHPgPERLIDLIDAEKISVFGTSPKFLATLEKAgLQPRLSHDLGSLKGLISTGSPLSPqsyDYVYREIKGELCLSS 416
Cdd:cd17649 167 PDELWAS-ADELAEMVRELGVTVLDLPPAYLQQLAEE-ADRTGDGRPPSLRLYIFGGEALSP---ELLRRWLKAPVRLFN 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 417 MSGGTDIVscfvIGNPVLPVRRGEmQCKSLAMAI---------EVWDDQGQPL-VGEKGELVCTRhfPAMPIGLWNDPDr 486
Cdd:cd17649 242 AYGPTEAT----VTPLVWKCEAGA-ARAGASMPIgrplggrsaYILDADLNPVpVGVTGELYIGG--EGLARGYLGRPE- 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 487 qkLRASYF----SQFPG--VWAQGDYAEQRPNGSLLIHGRSDAVLNPGGVRIGTAEIYRQVEKVPQVQESLAIGQRWQDD 560
Cdd:cd17649 314 --LTAERFvpdpFGAPGsrLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAGG 391
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 799207711 561 VRVVLFVRLNDGVELdEALEQQIRQVIRANTTPRHVPAKILAVTDIPRTISGKI 614
Cdd:cd17649 392 KQLVAYVVLRAAAAQ-PELRAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKL 444
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
87-614 |
7.51e-22 |
|
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: 99.45 E-value: 7.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 87 LNFAEHLLRRRDDHPAVVAISeDGQReQLTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTLVGMLATTSLGAIw 166
Cdd:COG1021 25 ETLGDLLRRRAERHPDRIAVV-DGER-RLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAI- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 167 scssPDFGT----QGVIDRF-GQIEPKVLITCAgyRYAGKDIDQTAklNEILARLPSLEQLIIVPYARPqarvedyqtha 241
Cdd:COG1021 102 ----PVFALpahrRAEISHFaEQSEAVAYIIPD--RHRGFDYRALA--RELQAEVPSLRHVLVVGDAGE----------- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 242 rVTRWSDFYPPGGEPEFVAVPFDHPLYILYSSGTTGVPKCIIHgtggvllTHlkehglhadlsrDDclFYYTT------C 315
Cdd:COG1021 163 -FTSLDALLAAPADLSEPRPDPDDVAFFQLSGGTTGLPKLIPR-------TH------------DD--YLYSVrasaeiC 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 316 GW-----------MMWNWLVS------VLAIGATAVLYDGspfhPGPERLIDLIDAEKISVFGTSPKfLAT--LEKAglq 376
Cdd:COG1021 221 GLdadtvylaalpAAHNFPLSspgvlgVLYAGGTVVLAPD----PSPDTAFPLIERERVTVTALVPP-LALlwLDAA--- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 377 PRLSHDLGSLKGLISTGSPLSPQsydyVYREIKGEL-C-LSS---MSGG---------TDIVSCFVIGNPVLP---VRrg 439
Cdd:COG1021 293 ERSRYDLSSLRVLQVGGAKLSPE----LARRVRPALgCtLQQvfgMAEGlvnytrlddPEEVILTTQGRPISPddeVR-- 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 440 emqckslamaieVWDDQGQPL-VGEKGELvCTRHfPAMPIGLWNDPDrqkLRASYFSQfPGVWAQGDYAEQRPNGSLLIH 518
Cdd:COG1021 367 ------------IVDEDGNPVpPGEVGEL-LTRG-PYTIRGYYRAPE---HNARAFTP-DGFYRTGDLVRRTPDGYLVVE 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 519 GRSDAVLNPGGVRIGTAEIYRQVEKVPQVQESLAIGQrwQDDV---RVVLFVRLnDGVELDEAleqQIRQVIRANTTPRH 595
Cdd:COG1021 429 GRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAM--PDEYlgeRSCAFVVP-RGEPLTLA---ELRRFLRERGLAAF 502
|
570 580
....*....|....*....|
gi 799207711 596 -VPAKILAVTDIPRTISGKI 614
Cdd:COG1021 503 kLPDRLEFVDALPLTAVGKI 522
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
99-613 |
1.35e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 98.80 E-value: 1.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 99 DHPAVVAisedGQReQLTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTLVGMLATTSLGAIwscsspdfgTQGV 178
Cdd:PRK07798 18 DRVALVC----GDR-RLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAV---------PVNV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 179 IDR---------FGQIEPKVLITCAGYRyagkdidqtAKLNEILARLPSLEQLIIV------PYARPQARVEDYQTHARV 243
Cdd:PRK07798 84 NYRyvedelrylLDDSDAVALVYEREFA---------PRVAEVLPRLPKLRTLVVVedgsgnDLLPGAVDYEDALAAGSP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 244 TRwsDFYPPGGEpefvavpfDhpLYILYSSGTTGVPKCII---------------HGTGGVLLThlkEHGLHADLSRDDC 308
Cdd:PRK07798 155 ER--DFGERSPD--------D--LYLLYTGGTTGMPKGVMwrqedifrvllggrdFATGEPIED---EEELAKRAAAGPG 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 309 LFYYTTCGWM----MWNWLVSVLAiGATAVLYDGSPFHPgpERLIDLIDAEKI-SVFGTSPKFLATLEKAgLQPRLSHDL 383
Cdd:PRK07798 220 MRRFPAPPLMhgagQWAAFAALFS-GQTVVLLPDVRFDA--DEVWRTIEREKVnVITIVGDAMARPLLDA-LEARGPYDL 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 384 GSLKGLISTGSPLSPqsydyvyrEIKGELCL------------SSMSG--GTDIVSCFVI--GNPVLPVRRGemqcksla 447
Cdd:PRK07798 296 SSLFAIASGGALFSP--------SVKEALLEllpnvvltdsigSSETGfgGSGTVAKGAVhtGGPRFTIGPR-------- 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 448 maIEVWDDQGQPLV---GEKGELVCTRHfpaMPIGLWNDPDRQklrASYFSQFPGV-WA-QGDYAEQRPNGSLLIHGRSD 522
Cdd:PRK07798 360 --TVVLDEDGNPVEpgsGEIGWIARRGH---IPLGYYKDPEKT---AETFPTIDGVrYAiPGDRARVEADGTITLLGRGS 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 523 AVLNPGGVRIGTAEIYRQVEKVPQVQESLAIG---QRW-QddvRVVLFVRLNDGVELDEAleqQIRQVIRANTTPRHVPA 598
Cdd:PRK07798 432 VCINTGGEKVFPEEVEEALKAHPDVADALVVGvpdERWgQ---EVVAVVQLREGARPDLA---ELRAHCRSSLAGYKVPR 505
|
570
....*....|....*
gi 799207711 599 KILAVTDIPRTISGK 613
Cdd:PRK07798 506 AIWFVDEVQRSPAGK 520
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
101-614 |
2.32e-21 |
|
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: 97.38 E-value: 2.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 101 PAVVAISEDGQReqLTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTLVGMLAttslgaiwscsspdfgtqgvid 180
Cdd:cd17643 1 PEAVAVVDEDRR--LTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLA---------------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 181 rfgqiepkvlITCAGYRYAGKDIDQtaklneilarlpsleqliivPYARPQARVEDYQtharvtrwsdfyppggePEFVA 260
Cdd:cd17643 57 ----------ILKAGGAYVPIDPAY--------------------PVERIAFILADSG-----------------PSLLL 89
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 261 VPFDHPLYILYSSGTTGVPKciihgtgGVLLTH-----LKEHGLHA-DLSRDDCLFYYTTCG-----WMMWnwlvSVLAI 329
Cdd:cd17643 90 TDPDDLAYVIYTSGSTGRPK-------GVVVSHanvlaLFAATQRWfGFNEDDVWTLFHSYAfdfsvWEIW----GALLH 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 330 GATAVL--YDGSpfhPGPERLIDLIDAEKISVFGTSPK-FLATLEKAGLQPRlshDLGSLKGLISTGSPLSPQSY-DYVY 405
Cdd:cd17643 159 GGRLVVvpYEVA---RSPEDFARLLRDEGVTVLNQTPSaFYQLVEAADRDGR---DPLALRYVIFGGEALEAAMLrPWAG 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 406 REIKGELCLSSMSGGTDiVSCFVIGNPVLP--VRRGEMQ---CKSLAMAIEVWDDQGQPL-VGEKGELV----------- 468
Cdd:cd17643 233 RFGLDRPQLVNMYGITE-TTVHVTFRPLDAadLPAAAASpigRPLPGLRVYVLDADGRPVpPGVVGELYvsgagvargyl 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 469 -----CTRHFPAMPIGlwNDPDRQklrasYFSqfpgvwaqGDYAEQRPNGSLLIHGRSDAVLNPGGVRIGTAEIYRQVEK 543
Cdd:cd17643 312 grpelTAERFVANPFG--GPGSRM-----YRT--------GDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALAT 376
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 799207711 544 VPQVQESLAIGQRWQD-DVRVVLFVRLNDGVELDEAleqQIRQVIRANTTPRHVPAKILAVTDIPRTISGKI 614
Cdd:cd17643 377 HPSVRDAAVIVREDEPgDTRLVAYVVADDGAAADIA---ELRALLKELLPDYMVPARYVPLDALPLTVNGKL 445
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
88-620 |
3.09e-21 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 97.93 E-value: 3.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 88 NFAEHLLRRRDDHPAVVAISEDGQreQLTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTLVGMLATTSLGAIws 167
Cdd:PRK07786 18 NWVNQLARHALMQPDAPALRFLGN--TTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAI-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 168 csspdfgtqGVIDRFGQIEPKVlitcagyRYAGKDIDQTAKLNE-ILARL--------PSLEqLIIVPYARPQARVEDYQ 238
Cdd:PRK07786 94 ---------AVPVNFRLTPPEI-------AFLVSDCGAHVVVTEaALAPVatavrdivPLLS-TVVVAGGSSDDSVLGYE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 239 THARVTrwsdfyppGGEPEFVAVPFDHPLYILYSSGTTGVPKciihgtgGVLLTHLKEHG--------LHADLSRD---- 306
Cdd:PRK07786 157 DLLAEA--------GPAHAPVDIPNDSPALIMYTSGTTGRPK-------GAVLTHANLTGqamtclrtNGADINSDvgfv 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 307 -DCLFYYTTCGWMmwnwlVSVLAIGATAVLYDGSPFHPGpeRLIDLIDAEKI-SVFGTSPKFLATLEKAGLQPRlshDLg 384
Cdd:PRK07786 222 gVPLFHIAGIGSM-----LPGLLLGAPTVIYPLGAFDPG--QLLDVLEAEKVtGIFLVPAQWQAVCAEQQARPR---DL- 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 385 SLKGLISTGSPLSPQSYDYVYREIKGELCLSSMsGGTDI--VSCFVIGNPVLPvRRGEMQCKSLAMAIEVWDDQGQPL-V 461
Cdd:PRK07786 291 ALRVLSWGAAPASDTLLRQMAATFPEAQILAAF-GQTEMspVTCMLLGEDAIR-KLGSVGKVIPTVAARVVDENMNDVpV 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 462 GEKGELVctRHFPAMPIGLWNDPdrqklrASYFSQFPGVW-AQGDYAEQRPNGSLLIHGRSDAVLNPGGVRIGTAEIYRQ 540
Cdd:PRK07786 369 GEVGEIV--YRAPTLMSGYWNNP------EATAEAFAGGWfHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENV 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 541 VEKVPQVQESLAIG---QRWQD-DVRVVLFVRLNDGVELDEALEQQIRQVIRAnttpRHvPAKILAVTDIPRTISGKIVE 616
Cdd:PRK07786 441 LASHPDIVEVAVIGradEKWGEvPVAVAAVRNDDAALTLEDLAEFLTDRLARY----KH-PKALEIVDALPRNPAGKVLK 515
|
....
gi 799207711 617 LAVR 620
Cdd:PRK07786 516 TELR 519
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
99-614 |
4.50e-21 |
|
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: 96.55 E-value: 4.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 99 DHPAVVAISEdgqreQLTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTLVGMLATTSLGAIWSCSSPDFgtqgv 178
Cdd:cd17652 2 DAPAVVFGDE-----TLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAY----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 179 idrfgqiepkvlitcagyryagkdidqtaklneilarlpsleqliivPYARPQARVEDYQTHARVTrwsdfyppggepef 258
Cdd:cd17652 72 -----------------------------------------------PAERIAYMLADARPALLLT-------------- 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 259 vaVPfDHPLYILYSSGTTGVPKciihgtgGVLLTHLKEHGLHADLSR------DDCLFYYTTCGW--MMWNWLVSVLAiG 330
Cdd:cd17652 91 --TP-DNLAYVIYTSGSTGRPK-------GVVVTHRGLANLAAAQIAafdvgpGSRVLQFASPSFdaSVWELLMALLA-G 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 331 ATAVLYDGSPFHPGPErLIDLIDAEKISVFGTSPKFLATLEKAGLQPrlshdlgsLKGLISTGSPLSPQSYD-------- 402
Cdd:cd17652 160 ATLVLAPAEELLPGEP-LADLLREHRITHVTLPPAALAALPPDDLPD--------LRTLVVAGEACPAELVDrwapgrrm 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 403 ---YVYREIKGELCLSSMSGGTDIVScfvIGNPVLPVRrgemqckslamaIEVWDDQGQPL-VGEKGELVCTRhfPAMPI 478
Cdd:cd17652 231 inaYGPTETTVCATMAGPLPGGGVPP---IGRPVPGTR------------VYVLDARLRPVpPGVPGELYIAG--AGLAR 293
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 479 GLWNDPD--RQKLRASYFSQfPG--VWAQGDYAEQRPNGSLLIHGRSDAVLNPGGVRIGTAEIYRQVEKVPQVQESLAIG 554
Cdd:cd17652 294 GYLNRPGltAERFVADPFGA-PGsrMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVV 372
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 799207711 555 QRWQ-DDVRVVLFVRLNDGVELDEAleqQIRQVIRaNTTPRH-VPAKILAVTDIPRTISGKI 614
Cdd:cd17652 373 RDDRpGDKRLVAYVVPAPGAAPTAA---ELRAHLA-ERLPGYmVPAAFVVLDALPLTPNGKL 430
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
101-614 |
7.55e-21 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 98.11 E-value: 7.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 101 PAVVAISEDGQReqLTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTLVGMLATTSLGAIWSCSSPDFGTQGVID 180
Cdd:PRK12316 4565 PDAVAVVFDEEK--LTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAY 4642
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 181 RFGQIEPKVLITcagyryagkdidQTaklnEILARLPSLEQLiivpyarpQARVEDyqthaRVTRWSDFypPGGEPEFVA 260
Cdd:PRK12316 4643 MMEDSGAALLLT------------QS----HLLQRLPIPDGL--------ASLALD-----RDEDWEGF--PAHDPAVRL 4691
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 261 VPfDHPLYILYSSGTTGVPK--CIIHGTggvLLTHLKEHGLHADLSRDDCLFYYTTCGW--MMWNWLvSVLAIGATAVLY 336
Cdd:PRK12316 4692 HP-DNLAYVIYTSGSTGRPKgvAVSHGS---LVNHLHATGERYELTPDDRVLQFMSFSFdgSHEGLY-HPLINGASVVIR 4766
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 337 DGSPFHPgpERLIDLIDAEKISVFGTSPKFLATLEKaglQPRLSHDLGSLKGLISTGSPLSPQSYDYVYREIKgELCLSS 416
Cdd:PRK12316 4767 DDSLWDP--ERLYAEIHEHRVTVLVFPPVYLQQLAE---HAERDGEPPSLRVYCFGGEAVAQASYDLAWRALK-PVYLFN 4840
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 417 MSGGTDIVScfvigNPVLPVRRGEMQCKSLAM---------AIEVWDDQGQPL-VGEKGELVCTRHFPAMpiGLWNDPDr 486
Cdd:PRK12316 4841 GYGPTETTV-----TVLLWKARDGDACGAAYMpigtplgnrSGYVLDGQLNPLpVGVAGELYLGGEGVAR--GYLERPA- 4912
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 487 qkLRASYF--SQF--PG--VWAQGDYAEQRPNGSLLIHGRSDAVLNPGGVRIGTAEIYRQVEKVPQVQESLAIGQRWQDD 560
Cdd:PRK12316 4913 --LTAERFvpDPFgaPGgrLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAVG 4990
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 799207711 561 VRVVLFV-----RLNDGVELDEALEQQIRQVIRANTTPRHVPAKILAVTDIPRTISGKI 614
Cdd:PRK12316 4991 KQLVGYVvpqdpALADADEAQAELRDELKAALRERLPEYMVPAHLVFLARMPLTPNGKL 5049
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
89-614 |
7.85e-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: 96.26 E-value: 7.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 89 FAEHLlRRRDDHPAVVAiseDGQReqLTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTLVGMLATTSLGAIWSC 168
Cdd:cd17651 1 FERQA-ARTPDAPALVA---EGRR--LTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 169 SSPDFGTQGVIDRFGQIEPKVLITCAGYryagkdidqtaklneiLARLPsleqliivPYARPQARVEDYQTHArvtrwsd 248
Cdd:cd17651 75 LDPAYPAERLAFMLADAGPVLVLTHPAL----------------AGELA--------VELVAVTLLDQPGAAA------- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 249 fyPPGGEPeFVAVPFDHPLYILYSSGTTGVPKciihgtgGVLLTH------LKEHGLHADLSRDDclfyyTTCGWMMWNW 322
Cdd:cd17651 124 --GADAEP-DPALDADDLAYVIYTSGSTGRPK-------GVVMPHrslanlVAWQARASSLGPGA-----RTLQFAGLGF 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 323 LVSV------LAIGATAVLydgSPFH--PGPERLIDLIDAEKIS-VFGTSPKFLATLEKAGLQPRLshdLGSLKGLISTG 393
Cdd:cd17651 189 DVSVqeifstLCAGATLVL---PPEEvrTDPPALAAWLDEQRISrVFLPTVALRALAEHGRPLGVR---LAALRYLLTGG 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 394 SPLSPQSYDYVYREIKGELCLSSMSGGTD--IVSCFV-------------IGNPVLPVRrgemqckslamaIEVWDDQGQ 458
Cdd:cd17651 263 EQLVLTEDLREFCAGLPGLRLHNHYGPTEthVVTALSlpgdpaawpapppIGRPIDNTR------------VYVLDAALR 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 459 PL-VGEKGEL----VCTRHfpampiGLWNDPD--RQKLRASYFSQFPGVWAQGDYAEQRPNGSLLIHGRSDAVLNPGGVR 531
Cdd:cd17651 331 PVpPGVPGELyiggAGLAR------GYLNRPEltAERFVPDPFVPGARMYRTGDLARWLPDGELEFLGRADDQVKIRGFR 404
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 532 IGTAEIYRQVEKVPQVQESLAIGQRWQD-DVRVVLFVRLNDGVELD-EALEQQIRQVIranttPRH-VPAKILAVTDIPR 608
Cdd:cd17651 405 IELGEIEAALARHPGVREAVVLAREDRPgEKRLVAYVVGDPEAPVDaAELRAALATHL-----PEYmVPSAFVLLDALPL 479
|
....*.
gi 799207711 609 TISGKI 614
Cdd:cd17651 480 TPNGKL 485
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
114-620 |
2.40e-20 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 95.07 E-value: 2.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 114 QLTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTLVGMLATTSLGAIWSCSSPDFGTQGVIDRFGQIEPKVLI-- 191
Cdd:PRK05605 57 TTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVEHNPLYTAHELEHPFEDHGARVAIvw 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 192 -----TCAGYRyagkdidQTAKLNEILA-----RLPSLEQLII-VPYarPQARVEDYQTHARVT---RWSDFY--PPGGE 255
Cdd:PRK05605 137 dkvapTVERLR-------RTTPLETIVSvnmiaAMPLLQRLALrLPI--PALRKARAALTGPAPgtvPWETLVdaAIGGD 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 256 PEFVAVP---FDHPLYILYSSGTTGVPKciihgtgGVLLTHLkehGLHA----------DLSRDDCLFY--------Y-- 312
Cdd:PRK05605 208 GSDVSHPrptPDDVALILYTSGTTGKPK-------GAQLTHR---NLFAnaaqgkawvpGLGDGPERVLaalpmfhaYgl 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 313 TTCgwmmwnwLVSVLAIGATAVLYdgspfhPGPErlIDLI-DAEKIS----VFGTSP---KFLATLEKAGLqprlshDLG 384
Cdd:PRK05605 278 TLC-------LTLAVSIGGELVLL------PAPD--IDLIlDAMKKHpptwLPGVPPlyeKIAEAAEERGV------DLS 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 385 SLKGLISTGSPLsPQSYDYVYREIKGELcLSSMSGGTDiVSCFVIGNPVLPVRR-GEMQCKSLAMAIEVWD----DQGQP 459
Cdd:PRK05605 337 GVRNAFSGAMAL-PVSTVELWEKLTGGL-LVEGYGLTE-TSPIIVGNPMSDDRRpGYVGVPFPDTEVRIVDpedpDETMP 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 460 lVGEKGELVCTRhfPAMPIGLWNDPDrqklrASYFSQFPGVWAQGDYAEQRPNGSLLIHGRSDAVLNPGGVRIGTAEIYR 539
Cdd:PRK05605 414 -DGEEGELLVRG--PQVFKGYWNRPE-----ETAKSFLDGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEE 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 540 QVEKVPQVQESLAIG-QRWQDDVRVVLFVRLNDGVELDEAleqQIRQVIRANTTPRHVPAKILAVTDIPRTISGKIVELA 618
Cdd:PRK05605 486 VLREHPGVEDAAVVGlPREDGSEEVVAAVVLEPGAALDPE---GLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRRE 562
|
..
gi 799207711 619 VR 620
Cdd:PRK05605 563 VR 564
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
93-621 |
2.40e-20 |
|
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: 95.00 E-value: 2.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 93 LLRR-RDDHPA--VVAISEDGQREQLTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTLVGMLATTSLGAIwsCS 169
Cdd:cd12119 1 LLEHaARLHGDreIVSRTHEGEVHRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAV--LH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 170 ------SPDfgtqgvidrfgQI-------EPKVLITcagyryagkDIDQTAKLNEILARLPSLEQLIIVPYARPQA---- 232
Cdd:cd12119 79 tinprlFPE-----------QIayiinhaEDRVVFV---------DRDFLPLLEAIAPRLPTVEHVVVMTDDAAMPepag 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 233 -RVEDYQtharvtRWSDfyppGGEPEFVAVPFDH--PLYILYSSGTTGVPKciihgtgGVLLTH--LKEHGL---HAD-- 302
Cdd:cd12119 139 vGVLAYE------ELLA----AESPEYDWPDFDEntAAAICYTSGTTGNPK-------GVVYSHrsLVLHAMaalLTDgl 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 303 -LSRDDClfyyttcgwMM----------WNWLVSVLAIGATAVLYDGspfHPGPERLIDLIDAEKISVFGTSPKF----L 367
Cdd:cd12119 202 gLSESDV---------VLpvvpmfhvnaWGLPYAAAMVGAKLVLPGP---YLDPASLAELIEREGVTFAAGVPTVwqglL 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 368 ATLEKAGlqprlsHDLGSLKGLISTGSPLsPQSydyVYREIKgELCLSSMS--GGTDI--VSCFVIGNPVLPVRRGEMQC 443
Cdd:cd12119 270 DHLEANG------RDLSSLRRVVIGGSAV-PRS---LIEAFE-ERGVRVIHawGMTETspLGTVARPPSEHSNLSEDEQL 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 444 KSLAMA--------IEVWDDQGQPL------VGE---KGELVCTRHF--PAMPIGLWNDpdrqklrasyfsqfpGVWAQG 504
Cdd:cd12119 339 ALRAKQgrpvpgveLRIVDDDGRELpwdgkaVGElqvRGPWVTKSYYknDEESEALTED---------------GWLRTG 403
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 505 DYAEQRPNGSLLIHGRSDAVLNPGGVRIGTAEIYRQVEKVPQVQESLAIG---QRWQDdvRVVLFVRLNDGVELDealEQ 581
Cdd:cd12119 404 DVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGvphPKWGE--RPLAVVVLKEGATVT---AE 478
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 799207711 582 QIRQVIRANTTPRHVPAKILAVTDIPRTISGKIVELAVRN 621
Cdd:cd12119 479 ELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKALRE 518
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
115-620 |
2.41e-20 |
|
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: 93.98 E-value: 2.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 115 LTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTLVGMLATTSLGAIwscsspdfgTQGVIDRFGQIEpkvlitca 194
Cdd:cd05903 2 LTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAV---------TNPILPFFREHE-------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 195 gyryagkdidqtakLNEILARlpSLEQLIIVPyarpqarvedyqtharvTRWSDFyppggepEFVAVPfDHPLYILYSSG 274
Cdd:cd05903 65 --------------LAFILRR--AKAKVFVVP-----------------ERFRQF-------DPAAMP-DAVALLLFTSG 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 275 TTGVPKciihgtgGVLLTHlkeHGLHADLSRddcLFYYTTCGWMMWNWLVSVLA--------------IGATAVLYDGSp 340
Cdd:cd05903 104 TTGEPK-------GVMHSH---NTLSASIRQ---YAERLGLGPGDVFLVASPMAhqtgfvygftlpllLGAPVVLQDIW- 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 341 fhpGPERLIDLIDAEKISVFGTSPKFLATL----EKAGlqPRLSHdlgsLKGLISTGSPLSPQsydyVYREIK--GELCL 414
Cdd:cd05903 170 ---DPDKALALMREHGVTFMMGATPFLTDLlnavEEAG--EPLSR----LRTFVCGGATVPRS----LARRAAelLGAKV 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 415 SSMSGGTDIVSCFVIGNPVLPVRRGEMQCKSLAMA-IEVWDDQGQPLV-GEKGELVCTRhfPAMPIGLWNDPDrqklraS 492
Cdd:cd05903 237 CSAYGSTECPGAVTSITPAPEDRRLYTDGRPLPGVeIKVVDDTGATLApGVEGELLSRG--PSVFLGYLDRPD------L 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 493 YFSQFPGVWAQ-GDYAEQRPNGSLLIHGRSDAVLNPGGVRIGTAEIYRQVEKVPQVQESLAIG---QRWQDdvRVVLFVR 568
Cdd:cd05903 309 TADAAPEGWFRtGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVAlpdERLGE--RACAVVV 386
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 799207711 569 LNDGVELDeaLEQQIRQVIRANTTPRHVPAKILAVTDIPRTISGKIVELAVR 620
Cdd:cd05903 387 TKSGALLT--FDELVAYLDRQGVAKQYWPERLVHVDDLPRTPSGKVQKFRLR 436
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
76-293 |
2.54e-20 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 95.17 E-value: 2.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 76 MPSAQWFPGATlNFAEHLLRRRDDHPAVVAISE--DGQREQLTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTL 153
Cdd:COG1022 1 MSEFSDVPPAD-TLPDLLRRRAARFPDRVALREkeDGIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 154 VGMLATTSLGA----IWSCSSPDfgtqgvidrfgQI-------EPKVLITcagyryagKDIDQTAKLNEILARLPSLEQL 222
Cdd:COG1022 80 IADLAILAAGAvtvpIYPTSSAE-----------EVayilndsGAKVLFV--------EDQEQLDKLLEVRDELPSLRHI 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 799207711 223 IIVpyarpQARVEDyqTHARVTRWSDFYPPG---GEPEFV-----AVPFDHPLYILYSSGTTGVPKciihgtgGVLLTH 293
Cdd:COG1022 141 VVL-----DPRGLR--DDPRLLSLDELLALGrevADPAELearraAVKPDDLATIIYTSGTTGRPK-------GVMLTH 205
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
271-620 |
4.09e-20 |
|
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.
Pssm-ID: 341268 [Multi-domain] Cd Length: 439 Bit Score: 93.31 E-value: 4.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 271 YSSGTTGVPKCIIHGTGGVLLThLKEHGLHA-DLSRDD-------CLFYYTTCGWMMWNWLVsvlaiGATAVLYDGSPfh 342
Cdd:cd05958 104 FTSGTTGAPKATMHFHRDPLAS-ADRYAVNVlRLREDDrfvgsppLAFTFGLGGVLLFPFGV-----GASGVLLEEAT-- 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 343 pgPERLIDLIDAEKISVFGTSPKFLATLekAGLQPRLSHDLGSLKGLISTGSPLsPQSYDYVYREIKGELCLSSMsGGTD 422
Cdd:cd05958 176 --PDLLLSAIARYKPTVLFTAPTAYRAM--LAHPDAAGPDLSSLRKCVSAGEAL-PAALHRAWKEATGIPIIDGI-GSTE 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 423 IVSCFvIGNPVLPVRRGEMQCKSLAMAIEVWDDQGQPL-VGEKGELVCTRhfpamPIGLWNDPDrqKLRASYFSqfpGVW 501
Cdd:cd05958 250 MFHIF-ISARPGDARPGATGKPVPGYEAKVVDDEGNPVpDGTIGRLAVRG-----PTGCRYLAD--KRQRTYVQ---GGW 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 502 -AQGDYAEQRPNGSLLIHGRSDAVLNPGGVRIGTAEIYRQVEKVPQVQESLAIGQrwQDDVRVVL---FVRLNDGVELDE 577
Cdd:cd05958 319 nITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGH--PDESRGVVvkaFVVLRPGVIPGP 396
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 799207711 578 ALEQQIRQVIRANTTPRHVPAKILAVTDIPRTISGKIVELAVR 620
Cdd:cd05958 397 VLARELQDHAKAHIAPYKYPRAIEFVTELPRTATGKLQRFALR 439
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
62-614 |
4.48e-20 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 95.61 E-value: 4.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 62 FRSPPSAVLIEDAEMPSAQWFPGATLNFAEHLLRRrddHPAVVAISEDGQReqLTYAELAEHVAGLQKSLRAAGVTQGDR 141
Cdd:PRK12467 490 LDAEERARELVRWNAPATEYAPDCVHQLIEAQARQ---HPERPALVFGEQV--LSYAELNRQANRLAHVLIAAGVGPDVL 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 142 VAACMPNTWQTLVGMLATTSLGAIWSCSSPDFGTqgviDRFGqiepkvlitcagYRYAGKDIDQTAKLNEILARLPSLEQ 221
Cdd:PRK12467 565 VGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQ----DRLA------------YMLDDSGVRLLLTQSHLLAQLPVPAG 628
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 222 LIIVPYARPQARVEDYQTHarvtrwsdFYPPGGEPEFVAvpfdhplYILYSSGTTGVPKciihgtgGVLLTHLKEHGLHA 301
Cdd:PRK12467 629 LRSLCLDEPADLLCGYSGH--------NPEVALDPDNLA-------YVIYTSGSTGQPK-------GVAISHGALANYVC 686
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 302 DLSR------DDCLFYYTTCGWMMWNW-LVSVLAIGATAVLYDGSPfHPGPERLIDLIDAEKISVFGTSPKFLatleKAG 374
Cdd:PRK12467 687 VIAErlqlaaDDSMLMVSTFAFDLGVTeLFGALASGATLHLLPPDC-ARDAEAFAALMADQGVTVLKIVPSHL----QAL 761
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 375 LQPRLSHDLGSLKGLISTGSPLSPQSYDYVyREIKGELCLSSMSGGTDI---VSCFVIGNPVLPVRRGEMQCKSLAMAIE 451
Cdd:PRK12467 762 LQASRVALPRPQRALVCGGEALQVDLLARV-RALGPGARLINHYGPTETtvgVSTYELSDEERDFGNVPIGQPLANLGLY 840
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 452 VWDDQGQPL-VGEKGELVCTRHfpampiGLWNDPDRQ-KLRASYFSQFPG------VWAQGDYAEQRPNGSLLIHGRSDA 523
Cdd:PRK12467 841 ILDHYLNPVpVGVVGELYIGGA------GLARGYHRRpALTAERFVPDPFgadggrLYRTGDLARYRADGVIEYLGRMDH 914
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 524 VLNPGGVRIGTAEIYRQVEKVPQVQESLAIGQRWQDDVRVVLFVRLNDGVE------LDEALEQQIRQVIranttPRH-V 596
Cdd:PRK12467 915 QVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAGLQLVAYLVPAAVADgaehqaTRDELKAQLRQVL-----PDYmV 989
|
570
....*....|....*...
gi 799207711 597 PAKILAVTDIPRTISGKI 614
Cdd:PRK12467 990 PAHLLLLDSLPLTPNGKL 1007
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
264-614 |
7.79e-20 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 91.57 E-value: 7.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 264 DHPLYILYSSGTTGVPKciihgtgGVLLTHlkeH---------GLHADLSRDD--CL---FYYttC-GWMMWNwlVSVLA 328
Cdd:cd05917 2 DDVINIQFTSGTTGSPK-------GATLTH---HnivnngyfiGERLGLTEQDrlCIpvpLFH--CfGSVLGV--LACLT 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 329 IGATAVlYDGSPFHPGPerLIDLIDAEKISV-FGTSPKFLATLEkaglQPR-LSHDLGSLKGLISTGSPLSPQsydyVYR 406
Cdd:cd05917 68 HGATMV-FPSPSFDPLA--VLEAIEKEKCTAlHGVPTMFIAELE----HPDfDKFDLSSLRTGIMAGAPCPPE----LMK 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 407 EIKGELCLSSMS---GGTD---IVSCFVIGNPVlPVRRGEMQCKSLAMAIEVWDDQG--QPLVGEKGELvCTRHFPAMpI 478
Cdd:cd05917 137 RVIEVMNMKDVTiayGMTEtspVSTQTRTDDSI-EKRVNTVGRIMPHTEAKIVDPEGgiVPPVGVPGEL-CIRGYSVM-K 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 479 GLWNDPDRQKLRASyfsqfPGVWAQ-GDYAEQRPNGSLLIHGRSDAVLNPGGVRIGTAEIYRQVEKVPQVQESLAIG--- 554
Cdd:cd05917 214 GYWNDPEKTAEAID-----GDGWLHtGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGvpd 288
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 555 QRWQDDVrvVLFVRLNDGVELDEAleqQIRQVIRANTTPRHVPAKILAVTDIPRTISGKI 614
Cdd:cd05917 289 ERYGEEV--CAWIRLKEGAELTEE---DIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKI 343
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
98-398 |
1.12e-19 |
|
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: 92.68 E-value: 1.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 98 DDHPAVVAI--SEDGQReqLTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTLVGMLATTSLGAIWSCSSPdFGT 175
Cdd:cd05904 16 SAHPSRPALidAATGRA--LTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANP-LST 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 176 QGVIDRfgQIE---PKVLITcagyryagkdidqtakLNEILARLPSLEQLIIVpyarpqarVEDYQTHARVTRWSDFYPP 252
Cdd:cd05904 93 PAEIAK--QVKdsgAKLAFT----------------TAELAEKLASLALPVVL--------LDSAEFDSLSFSDLLFEAD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 253 GGEPEFVAVPFDHPLYILYSSGTTGVPKciihgtgGVLLTH--------LKEHGLHADLSRDDC------LFYYTTCGWM 318
Cdd:cd05904 147 EAEPPVVVIKQDDVAALLYSSGTTGRSK-------GVMLTHrnliamvaQFVAGEGSNSDSEDVflcvlpMFHIYGLSSF 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 319 MwnwlVSVLAIGATAVL---YDgspfhpgPERLIDLIDAEKISVFGTSPKFLATLEKAGLQPrlSHDLGSLKGLISTGSP 395
Cdd:cd05904 220 A----LGLLRLGATVVVmprFD-------LEELLAAIERYKVTHLPVVPPIVLALVKSPIVD--KYDLSSLRQIMSGAAP 286
|
...
gi 799207711 396 LSP 398
Cdd:cd05904 287 LGK 289
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
92-614 |
1.51e-19 |
|
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: 92.19 E-value: 1.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 92 HLLRRRDDH--PAVVAISEDGQREQLTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTLVGMLATTSLGAIwscs 169
Cdd:cd05923 4 FEMLRRAASraPDACAIADPARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAV---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 170 spdfgtqgvidrfgqiepkvlITCAGYRYAGKDIDQTAKLNEILArlpsleqlIIVPYARPQARvEDYQTHARVTRWSDF 249
Cdd:cd05923 80 ---------------------PALINPRLKAAELAELIERGEMTA--------AVIAVDAQVMD-AIFQSGVRVLALSDL 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 250 yPPGGEPEFVAVPF-------DHPLYILYSSGTTGVPKCII----HGTGGVLLTHLKEHGLHADLSRddclfyytTCGWM 318
Cdd:cd05923 130 -VGLGEPESAGPLIedpprepEQPAFVFYTSGTTGLPKGAVipqrAAESRVLFMSTQAGLRHGRHNV--------VLGLM 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 319 MWNWLVSVLAIGATAVLYDGS---PFHPGPERLIDLIDAEKISVFGTSPKFLATLEKAGLQPrlSHDLGSLKGLISTGSP 395
Cdd:cd05923 201 PLYHVIGFFAVLVAALALDGTyvvVEEFDPADALKLIEQERVTSLFATPTHLDALAAAAEFA--GLKLSSLRHVTFAGAT 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 396 LSPQSYDYVYREIKGElcLSSMSGGTDIVSCFVIGNP-------------VLPVRRGEMQCKSLAmaievwddqgqplVG 462
Cdd:cd05923 279 MPDAVLERVNQHLPGE--KVNIYGTTEAMNSLYMRDArtgtemrpgffseVRIVRIGGSPDEALA-------------NG 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 463 EKGELVCTRHFPAMPIGLWNDP--DRQKLRAsyfsqfpGVWAQGDYAEQRPNGSLLIHGRSDAVLNPGGVRIGTAEIYRQ 540
Cdd:cd05923 344 EEGELIVAAAADAAFTGYLNQPeaTAKKLQD-------GWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERV 416
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 799207711 541 VEKVPQVQESLAIG---QRWQDdvRVVLFVRLNDGVELDEALEQQIRQVIRANTTPrhvPAKILAVTDIPRTISGKI 614
Cdd:cd05923 417 LSRHPGVTEVVVIGvadERWGQ--SVTACVVPREGTLSADELDQFCRASELADFKR---PRRYFFLDELPKNAMNKV 488
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
91-614 |
1.58e-19 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 92.57 E-value: 1.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 91 EHLLRRRDDHPAVVAiSEDGQReqLTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTLVGMLATTSLGAIWSCSS 170
Cdd:PRK08315 23 DRTAARYPDREALVY-RDQGLR--WTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVTIN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 171 PDFGTQGVIDRFGQIEPKVLITCAGYryagKDIDQTAKLNEIL-------------ARLPSLEQLIIVpyarpqarveDY 237
Cdd:PRK08315 100 PAYRLSELEYALNQSGCKALIAADGF----KDSDYVAMLYELApelatcepgqlqsARLPELRRVIFL----------GD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 238 QTHARVTRWSDFYPPGGEPEFVAVP-------FDHPLYILYSSGTTGVPKciihgtgGVLLTHlkeH---------GLHA 301
Cdd:PRK08315 166 EKHPGMLNFDELLALGRAVDDAELAarqatldPDDPINIQYTSGTTGFPK-------GATLTH---RnilnngyfiGEAM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 302 DLSRDD--CL---FYYttC-GWMMwnwlvSVLAI---GATAVlYDGSPFHPgperLIDL--IDAEK-ISVFGTSPKFLAT 369
Cdd:PRK08315 236 KLTEEDrlCIpvpLYH--CfGMVL-----GNLACvthGATMV-YPGEGFDP----LATLaaVEEERcTALYGVPTMFIAE 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 370 LEkaglQPRL-SHDLGSLKGLISTGSPlSPQSydyVYREIKGELCLSsmsggtDIVSCFviG----NPVL-------PVR 437
Cdd:PRK08315 304 LD----HPDFaRFDLSSLRTGIMAGSP-CPIE---VMKRVIDKMHMS------EVTIAY--GmtetSPVStqtrtddPLE 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 438 RgemQCKSLAMA---IEV--WD-DQGQPL-VGEKGELvCTRHFPAMpIGLWNDPdrQKLRASYfsqFPGVWAQ-GDYAEQ 509
Cdd:PRK08315 368 K---RVTTVGRAlphLEVkiVDpETGETVpRGEQGEL-CTRGYSVM-KGYWNDP--EKTAEAI---DADGWMHtGDLAVM 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 510 RPNGSLLIHGRS-DAVLNpGGvrigtaE-IY-RQVE----KVPQVQeslaigqrwqdDVRVV------------LFVRLN 570
Cdd:PRK08315 438 DEEGYVNIVGRIkDMIIR-GG------EnIYpREIEeflyTHPKIQ-----------DVQVVgvpdekygeevcAWIILR 499
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 799207711 571 DGVELDealEQQIRQVIRA----NTTPRHvpakILAVTDIPRTISGKI 614
Cdd:PRK08315 500 PGATLT---EEDVRDFCRGkiahYKIPRY----IRFVDEFPMTVTGKI 540
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
89-614 |
1.86e-19 |
|
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.
Pssm-ID: 341244 [Multi-domain] Cd Length: 482 Bit Score: 92.01 E-value: 1.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 89 FAEHLLRRRDDHPAVVAISEDGQReqLTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTLVGMLATTSLGAIwsc 168
Cdd:cd05920 17 LGDLLARSAARHPDRIAVVDGDRR--LTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAV--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 169 sspdfgtqgvidrfgqiepkVLITCAGYRYAgkDIDQTAKLNEILArlpsleqlIIVPyarPQARVEDYQTHARVTRWSd 248
Cdd:cd05920 92 --------------------PVLALPSHRRS--ELSAFCAHAEAVA--------YIVP---DRHAGFDHRALARELAES- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 249 fyppggEPEfvavpfdhPLYILYSSGTTGVPKCIIHgtggvllTHlKEHGLHADLSRDDCLF----YYTTCGWMMWNWLV 324
Cdd:cd05920 138 ------IPE--------VALFLLSGGTTGTPKLIPR-------TH-NDYAYNVRASAEVCGLdqdtVYLAVLPAAHNFPL 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 325 S------VLAIGATAVLYDgspfHPGPERLIDLIDAEKISVFGTSPKFLATLEKAGLQPRLshDLGSLKGLISTGSPLSP 398
Cdd:cd05920 196 AcpgvlgTLLAGGRVVLAP----DPSPDAAFPLIEREGVTVTALVPALVSLWLDAAASRRA--DLSSLRLLQVGGARLSP 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 399 Q-----------SYDYVYREIKGELCLSSMSGGTDIVsCFVIGNPVLPVRRgemqckslamaIEVWDDQGQPL-VGEKGE 466
Cdd:cd05920 270 AlarrvppvlgcTLQQVFGMAEGLLNYTRLDDPDEVI-IHTQGRPMSPDDE-----------IRVVDEEGNPVpPGEEGE 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 467 LVcTRHfPAMPIGLWNDPDRQklrASYFSQfPGVWAQGDYAEQRPNGSLLIHGRSDAVLNPGGVRIGTAEIYRQVEKVPQ 546
Cdd:cd05920 338 LL-TRG-PYTIRGYYRAPEHN---ARAFTP-DGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPA 411
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 799207711 547 VQESLAIG---QRWQDdvRVVLFVRLNdgvelDEALE-QQIRQVIRANTTPRH-VPAKILAVTDIPRTISGKI 614
Cdd:cd05920 412 VHDAAVVAmpdELLGE--RSCAFVVLR-----DPPPSaAQLRRFLRERGLAAYkLPDRIEFVDSLPLTAVGKI 477
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
92-614 |
2.29e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 92.03 E-value: 2.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 92 HLLRRRDDHPAVVAIsedGQreQLTYAEL---AEHVAGLqksLRAAGVTQGDRVAACMPNTWQTLVGMLATTSLGAIWSC 168
Cdd:PRK06178 41 AWARERPQRPAIIFY---GH--VITYAELdelSDRFAAL---LRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 169 SSPDFGTQGVIDRFGQIEPKVLITcagyryagkdIDQTAKLNEILARLPSLEQLIIVPY-----ARPQARVEDYQTHAR- 242
Cdd:PRK06178 113 VSPLFREHELSYELNDAGAEVLLA----------LDQLAPVVEQVRAETSLRHVIVTSLadvlpAEPTLPLPDSLRAPRl 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 243 -VTRWSDFYP----PGGEPEFVAVPFDHPLYILYSSGTTGVPKCIIHGTGGVLLTHLKEHGLHADLSRDDCLFYYTTCGW 317
Cdd:PRK06178 183 aAAGAIDLLPalraCTAPVPLPPPALDALAALNYTGGTTGMPKGCEHTQRDMVYTAAAAYAVAVVGGEDSVFLSFLPEFW 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 318 MMWN--WLVSVLAIGATAVL---YDgspfhpgPERLIDLIDAEKISV-FGTSPKFLATLEkaglQPRLS-HDLGSLK--G 388
Cdd:PRK06178 263 IAGEnfGLLFPLFSGATLVLlarWD-------AVAFMAAVERYRVTRtVMLVDNAVELMD----HPRFAeYDLSSLRqvR 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 389 LISTGSPLSPQsYDYVYREIKGELCLSSMSGGTDIVSC--FVIG----------NPV---LPVRRGEmqckslamaIEVW 453
Cdd:PRK06178 332 VVSFVKKLNPD-YRQRWRALTGSVLAEAAWGMTETHTCdtFTAGfqdddfdllsQPVfvgLPVPGTE---------FKIC 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 454 D-DQGQPL-VGEKGELvCTRHfPAMPIGLWNDPD--RQKLRASYFSqfpgvwaQGDYAEQRPNGSLLIHGRSDAVLNPGG 529
Cdd:PRK06178 402 DfETGELLpLGAEGEI-VVRT-PSLLKGYWNKPEatAEALRDGWLH-------TGDIGKIDEQGFLHYLGRRKEMLKVNG 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 530 VRIGTAEIYRQVEKVPQVQESLAIGQRWQDDVRV-VLFVRLNDGVELDEAleqQIRQVIRANTTPRHVPaKILAVTDIPR 608
Cdd:PRK06178 473 MSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVpVAFVQLKPGADLTAA---ALQAWCRENMAVYKVP-EIRIVDALPM 548
|
....*.
gi 799207711 609 TISGKI 614
Cdd:PRK06178 549 TATGKV 554
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
88-621 |
2.51e-19 |
|
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: 91.76 E-value: 2.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 88 NFAEHLLR---------RRDDHPAVVAISEDGQREQLTYAELAEHVAGLQKSLR-AAGVTQGDRVAACMPNT---WQTLV 154
Cdd:cd05928 6 NFASDVLDqwadkekagKRPPNPALWWVNGKGDEVKWSFRELGSLSRKAANVLSgACGLQRGDRVAVILPRVpewWLVNV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 155 GMLATtslGAIWSCSSPDFGTQGVIDRFGQIEPKVLITcagyryagkdIDQTA-KLNEILARLPSLE-QLIIVPYARPQa 232
Cdd:cd05928 86 ACIRT---GLVFIPGTIQLTAKDILYRLQASKAKCIVT----------SDELApEVDSVASECPSLKtKLLVSEKSRDG- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 233 rvedyqtharvtrWSDFYPPGGE--PEFVAVPFDH--PLYILYSSGTTGVPKCIIHGTGGVLLTHLKEHGLHADLSRDDC 308
Cdd:cd05928 152 -------------WLNFKELLNEasTEHHCVETGSqePMAIYFTSGTTGSPKMAEHSHSSLGLGLKVNGRYWLDLTASDI 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 309 LFYYTTCGWMM--WNWLVSVLAIGATAVLYDGSPFHPgpERLIDLIDAEKISVFGTSPkflaTLEKAGLQPRL-SHDLGS 385
Cdd:cd05928 219 MWNTSDTGWIKsaWSSLFEPWIQGACVFVHHLPRFDP--LVILKTLSSYPITTFCGAP----TVYRMLVQQDLsSYKFPS 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 386 LKGLISTGSPLSPQSYDYvYREIKGeLCLSSMSGGTDIVscFVIGNPV-LPVRRGEMQCKSLAMAIEVWDDQGQPL-VGE 463
Cdd:cd05928 293 LQHCVTGGEPLNPEVLEK-WKAQTG-LDIYEGYGQTETG--LICANFKgMKIKPGSMGKASPPYDVQIIDDNGNVLpPGT 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 464 KGElVCTRHFPAMPIGLWN----DPDrqKLRASYFSQFpgvWAQGDYAEQRPNGSLLIHGRSDAVLNPGGVRIGTAEIYR 539
Cdd:cd05928 369 EGD-IGIRVKPIRPFGLFSgyvdNPE--KTAATIRGDF---YLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVES 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 540 QVEKVPQVQESLAIGQrwQDDVR---VVLFVRLN-DGVELD-EALEQQIRQVIRANTTPRHVPAKILAVTDIPRTISGKI 614
Cdd:cd05928 443 ALIEHPAVVESAVVSS--PDPIRgevVKAFVVLApQFLSHDpEQLTKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKI 520
|
....*..
gi 799207711 615 VELAVRN 621
Cdd:cd05928 521 QRNELRD 527
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
96-614 |
3.01e-19 |
|
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: 91.24 E-value: 3.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 96 RRDDHPAVVaiSEDgqrEQLTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTLVGMLATTSLGAIWSCSSPDFgt 175
Cdd:cd17655 9 KTPDHTAVV--FED---QTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDY-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 176 qgvidrfgqiePKVLItcagyRYAGKDidqtAKLNEILArlpsleqliivpyARPQARVEDYQTHARVTRWSDFYPPGGE 255
Cdd:cd17655 82 -----------PEERI-----QYILED----SGADILLT-------------QSHLQPPIAFIGLIDLLDEDTIYHEESE 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 256 PEFVAVPFDHPLYILYSSGTTGVPKciihgtgGVLLTHLKEHGLHADLSR-------DDCL----FYYTTCGWMMWnwlv 324
Cdd:cd17655 129 NLEPVSKSDDLAYVIYTSGSTGKPK-------GVMIEHRGVVNLVEWANKviyqgehLRVAlfasISFDASVTEIF---- 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 325 SVLAIGATAVLYDGSPFHPGPErLIDLIDAEKISVFGTSPKFLATLEKAGLQPRLShdlgsLKGLISTGSPLSPqsyDYV 404
Cdd:cd17655 198 ASLLSGNTLYIVRKETVLDGQA-LTQYIRQNRITIIDLTPAHLKLLDAADDSEGLS-----LKHLIVGGEALST---ELA 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 405 YREIKG--------------ELCLSSMSG----GTDIVSCFVIGNPVLPVRrgemqckslamaIEVWDDQGQPL-VGEKG 465
Cdd:cd17655 269 KKIIELfgtnptitnaygptETTVDASIYqyepETDQQVSVPIGKPLGNTR------------IYILDQYGRPQpVGVAG 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 466 ELVCTRHFPAMpiGLWNDPDrqkLRASYFSQFPGV-----WAQGDYAEQRPNGSLLIHGRSDAVLNPGGVRIGTAEIYRQ 540
Cdd:cd17655 337 ELYIGGEGVAR--GYLNRPE---LTAEKFVDDPFVpgermYRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEAR 411
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 799207711 541 VEKVPQVQESLAIGQRWQDDvRVVLFVRLNDGVELDEAleqQIRQVIrANTTPRH-VPAKILAVTDIPRTISGKI 614
Cdd:cd17655 412 LLQHPDIKEAVVIARKDEQG-QNYLCAYIVSEKELPVA---QLREFL-ARELPDYmIPSYFIKLDEIPLTPNGKV 481
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
260-620 |
3.94e-19 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 90.58 E-value: 3.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 260 AVPFDHP--LYILYSSGTTGVPKciihgtgGVLLTH---------LKEH-GLHADLSRDDCLFYYTTCGWmmwNWLVSVL 327
Cdd:cd05922 111 AHEVSHEdlALLLYTSGSTGSPK-------LVRLSHqnllanarsIAEYlGITADDRALTVLPLSYDYGL---SVLNTHL 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 328 AIGATAVLYDGSPFhpgPERLIDLIDAEKISVFGTSPKFLATLEKAGLQPRlshDLGSLKGLISTGSPLSPQSYDyVYRE 407
Cdd:cd05922 181 LRGATLVLTNDGVL---DDAFWEDLREHGATGLAGVPSTYAMLTRLGFDPA---KLPSLRYLTQAGGRLPQETIA-RLRE 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 408 iKGELC-LSSMSGGTDIVSCFVIGNPVLPVRRGEMQCKSLA-MAIEVWDDQGQPL-VGEKGELVCTRHFPAMpiGLWNDP 484
Cdd:cd05922 254 -LLPGAqVYVMYGQTEATRRMTYLPPERILEKPGSIGLAIPgGEFEILDDDGTPTpPGEPGEIVHRGPNVMK--GYWNDP 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 485 drQKLRASyfSQFPGVWAQGDYAEQRPNGSLLIHGRSDAVLNPGGVRIGTAEIYRQVEKVPQVQESLAIGQRWQDDVRVV 564
Cdd:cd05922 331 --PYRRKE--GRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDPLGEKLA 406
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 799207711 565 LFVRLNDGVELDEALeqqirQVIRANTTPRHVPAKILAVTDIPRTISGKIVELAVR 620
Cdd:cd05922 407 LFVTAPDKIDPKDVL-----RSLAERLPPYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
112-614 |
6.25e-19 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 89.66 E-value: 6.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 112 REQLTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTLVGMLATTSLGAIwscsspdfgtqgvidrfgqiepKVLI 191
Cdd:cd05934 1 GRRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAV----------------------LVPI 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 192 tcagyryagkdidQTAKLNEILARlpsleqliIVPYARPQARVEDyqtharvtrwsdfyppggepefvavpfdhPLYILY 271
Cdd:cd05934 59 -------------NTALRGDELAY--------IIDHSGAQLVVVD-----------------------------PASILY 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 272 SSGTTGVPKciihgtgGVLLTHLKEHGL------HADLSRDDCLF-----YYTTCgwMMWNWLVSVLAiGATAVLydGSP 340
Cdd:cd05934 89 TSGTTGPPK-------GVVITHANLTFAgyysarRFGLGEDDVYLtvlplFHINA--QAVSVLAALSV-GATLVL--LPR 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 341 FHPGpeRLIDLIDAEKISVFGTSPKFLATLEKAglqprlshdlgslkglistgsPLSPQSYDYVYREIKGELCLSSMS-- 418
Cdd:cd05934 157 FSAS--RFWSDVRRYGATVTNYLGAMLSYLLAQ---------------------PPSPDDRAHRLRAAYGAPNPPELHee 213
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 419 -------------GGTDiVSCFVIGNPVLPVRRGEMQCKSLAMAIEVWDDQGQPL-VGEKGELVCTRHFP-AMPIGLWND 483
Cdd:cd05934 214 feerfgvrllegyGMTE-TIVGVIGPRDEPRRPGSIGRPAPGYEVRIVDDDGQELpAGEPGELVIRGLRGwGFFKGYYNM 292
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 484 PDrqKLRASyfsqFPGVWAQ-GDYAEQRPNGSLLIHGRSDAVLNPGGVRIGTAEIYRQVEKVPQVQESLAIGQRwqDDVR 562
Cdd:cd05934 293 PE--ATAEA----MRNGWFHtGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVP--DEVG 364
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 799207711 563 ---VVLFVRLNDGVELDEAleqQIRQVIRANTTPRHVPAKILAVTDIPRTISGKI 614
Cdd:cd05934 365 edeVKAVVVLRPGETLDPE---ELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKV 416
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
52-614 |
1.88e-18 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 90.61 E-value: 1.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 52 RAIVAFFDVQFRSPPSavliedaEMPSAQWFpgatlnfAEHLLRRRDdhpAVVAISEDgqrEQLTYAELAEHVAGLQKSL 131
Cdd:PRK12467 3078 RQVLHAWNATAAAYPS-------ERLVHQLI-------EAQVARTPE---APALVFGD---QQLSYAELNRRANRLAHRL 3137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 132 RAAGVTQGDRVAACMPNTWQTLVGMLATTSLGAIWSCSSPDFGTQGVIDRFGQIEPKVLITcagyryagkdidqTAKLNE 211
Cdd:PRK12467 3138 IAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLLT-------------QAHLLE 3204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 212 ILARLPSLEQLIIvpyarpqarvedyqtharvtrwsDFYPPGGEPEFVAVPFDHP---LYILYSSGTTGVPKciihGTG- 287
Cdd:PRK12467 3205 QLPAPAGDTALTL-----------------------DRLDLNGYSENNPSTRVMGenlAYVIYTSGSTGKPK----GVGv 3257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 288 --GVLLTHLKEHGLHADLSRDDCLFYYTTCGW--MMWNWLvSVLAIGATAVLYDGSpfHPGPERLIDLIDAEKISVFGTS 363
Cdd:PRK12467 3258 rhGALANHLCWIAEAYELDANDRVLLFMSFSFdgAQERFL-WTLICGGCLVVRDND--LWDPEELWQAIHAHRISIACFP 3334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 364 PKFL-ATLEKAGLQprlshDLGSLKGLISTGSPLSPQSYDYVYREIKgELCLSSMSGGT---------DIVSCFVIGNPV 433
Cdd:PRK12467 3335 PAYLqQFAEDAGGA-----DCASLDIYVFGGEAVPPAAFEQVKRKLK-PRGLTNGYGPTeavvtvtlwKCGGDAVCEAPY 3408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 434 LPVRRGemqcksLA-MAIEVWDDQGQPL-VGEKGELVCTRHFPAMpiGLWNDPDrqkLRASYF--SQFPG----VWAQGD 505
Cdd:PRK12467 3409 APIGRP------VAgRSIYVLDGQLNPVpVGVAGELYIGGVGLAR--GYHQRPS---LTAERFvaDPFSGsggrLYRTGD 3477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 506 YAEQRPNGSLLIHGRSDAVLNPGGVRIGTAEIYRQVEKVPQVQESLAIGQRWQDDVRVVLFVRLNDgveLDEALEQQIRQ 585
Cdd:PRK12467 3478 LARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLARDGAGGKQLVAYVVPAD---PQGDWRETLRD 3554
|
570 580
....*....|....*....|....*....
gi 799207711 586 VIRANTTPRHVPAKILAVTDIPRTISGKI 614
Cdd:PRK12467 3555 HLAASLPDYMVPAQLLVLAAMPLGPNGKV 3583
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
95-625 |
3.14e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 88.02 E-value: 3.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 95 RRRDDHPAVVAisedgQREQLTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTLVGMLATTSLGAIWscsspdfg 174
Cdd:PRK06145 13 RRTPDRAALVY-----RDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVF-------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 175 tQGVIDRFGQIEPKVLITCAGYRYAGKDidqtaklnEILARLPSLEQLIIVPYARPQARVEDY-QTHARVTrwsdfyppg 253
Cdd:PRK06145 80 -LPINYRLAADEVAYILGDAGAKLLLVD--------EEFDAIVALETPKIVIDAAAQADSRRLaQGGLEIP--------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 254 gePEFVAVPFDhpLY-ILYSSGTTGVPKCIIHGTGGVlltHLK--EHGLHADLSRDDCLFYYTTCgwmmwnWLVSVLAIG 330
Cdd:PRK06145 142 --PQAAVAPTD--LVrLMYTSGTTDRPKGVMHSYGNL---HWKsiDHVIALGLTASERLLVVGPL------YHVGAFDLP 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 331 ATAVLYDGSPFHP----GPERLIDLIDAEKISVFGTSPKFLATLekAGLQPRLSHDLGSLKGLISTGSPlSPQSYDYVYR 406
Cdd:PRK06145 209 GIAVLWVGGTLRIhrefDPEAVLAAIERHRLTCAWMAPVMLSRV--LTVPDRDRFDLDSLAWCIGGGEK-TPESRIRDFT 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 407 EIKGELCLSSMSGGTDIVScfviGNPVLPVRRGEMQCKSLAMA-----IEVWDDQGQPLV-GEKGElVCTRHfPAMPIGL 480
Cdd:PRK06145 286 RVFTRARYIDAYGLTETCS----GDTLMEAGREIEKIGSTGRAlahveIRIADGAGRWLPpNMKGE-ICMRG-PKVTKGY 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 481 WNDPdrQKLRASYFsqfpGVWAQ-GDYAEQRPNGSLLIHGRSDAVLNPGGVRIGTAEIYRQVEKVPQVQESLAIG---QR 556
Cdd:PRK06145 360 WKDP--EKTAEAFY----GDWFRsGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGvhdDR 433
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 557 WQDdvRVVLFVRLNDGVELD-EALEQQIRQVIRANTTPRhvpaKILAVTDIPRTISGKIVELAVRNVVHG 625
Cdd:PRK06145 434 WGE--RITAVVVLNPGATLTlEALDRHCRQRLASFKVPR----QLKVRDELPRNPSGKVLKRVLRDELNG 497
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
100-614 |
1.13e-17 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 86.73 E-value: 1.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 100 HPAVVAISEDgQREQLTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPnTWQ--TLVgMLATTSLGAIWSCSSPDFGTQG 177
Cdd:PRK06087 36 MPDKIAVVDN-HGASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLP-GWCefTII-YLACLKVGAVSVPLLPSWREAE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 178 VIDRFGQIEPKVLITCAGYRyagkdidQTAKLNEILA---RLPSLEQLIIVPYARPQARVEDY-QTHARvtrwsdfYPPG 253
Cdd:PRK06087 113 LVWVLNKCQAKMFFAPTLFK-------QTRPVDLILPlqnQLPQLQQIVGVDKLAPATSSLSLsQIIAD-------YEPL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 254 GEPefVAVPFDHPLYILYSSGTTGVPKciihgtgGVLLTH----LKEHGLHADLSR--DDCLFYYTTCGWM--MWNWLVS 325
Cdd:PRK06087 179 TTA--ITTHGDELAAVLFTSGTEGLPK-------GVMLTHnnilASERAYCARLNLtwQDVFMMPAPLGHAtgFLHGVTA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 326 VLAIGATAVLYDgspfHPGPERLIDLIDAEKIS-VFGTSP---KFLATLEKAGlqprlsHDLGSLKGLISTGSPLsPQSy 401
Cdd:PRK06087 250 PFLIGARSVLLD----IFTPDACLALLEQQRCTcMLGATPfiyDLLNLLEKQP------ADLSALRFFLCGGTTI-PKK- 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 402 dyVYREIKGE-LCLSSMSGGTDivSC---FVigNPVLPVRRgEMQCKSLAMA---IEVWDDQGQPL-VGEKGElVCTRHf 473
Cdd:PRK06087 318 --VARECQQRgIKLLSVYGSTE--SSphaVV--NLDDPLSR-FMHTDGYAAAgveIKVVDEARKTLpPGCEGE-EASRG- 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 474 PAMPIGLWNDPDRQKlRAS-----YFSqfpgvwaqGDYAEQRPNGSLLIHGRSDAVLNPGGVRIGTAEIYRQVEKVPQVQ 548
Cdd:PRK06087 389 PNVFMGYLDEPELTA-RALdeegwYYS--------GDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIH 459
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 799207711 549 ESLAIG---QRWQDdvRVVLFVRLNDGvELDEALEQQIRQVIRANTTPRHVPAKILAVTDIPRTISGKI 614
Cdd:PRK06087 460 DACVVAmpdERLGE--RSCAYVVLKAP-HHSLTLEEVVAFFSRKRVAKYKYPEHIVVIDKLPRTASGKI 525
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
87-620 |
1.36e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 86.25 E-value: 1.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 87 LNFAeHLL----RRRDDHPAVVaiseDGQReQLTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTLVGMLATTSL 162
Cdd:PRK07470 7 MNLA-HFLrqaaRRFPDRIALV----WGDR-SWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 163 GAIWscsspdfgtqgVIDRFGQIEPKV--LITCAGYRYAGKDIDQTAKLNEILARLPSLEQLIIVPYARPQarvEDYQth 240
Cdd:PRK07470 81 GAVW-----------VPTNFRQTPDEVayLAEASGARAMICHADFPEHAAAVRAASPDLTHVVAIGGARAG---LDYE-- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 241 ARVTRwsdfyPPGGEPEFVAVPFDHPLYILYSSGTTGVPKCII--HGTGGVLLT-HLKEhgLHADLSRDDClfyyttcgw 317
Cdd:PRK07470 145 ALVAR-----HLGARVANAAVDHDDPCWFFFTSGTTGRPKAAVltHGQMAFVITnHLAD--LMPGTTEQDA--------- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 318 mmwNWLVSVL------------AIGATAVLYDGSPFHpgPERLIDLIDAEKISVFGTSPKFLATLEKaglQPRL-SHDLG 384
Cdd:PRK07470 209 ---SLVVAPLshgagihqlcqvARGAATVLLPSERFD--PAEVWALVERHRVTNLFTVPTILKMLVE---HPAVdRYDHS 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 385 SLKGLISTGSPLspqsydyvYREIKgELCLSSMsgGTDIVSCF----VIGN-PVLP-----------VRRGEMQCKSLAM 448
Cdd:PRK07470 281 SLRYVIYAGAPM--------YRADQ-KRALAKL--GKVLVQYFglgeVTGNiTVLPpalhdaedgpdARIGTCGFERTGM 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 449 AIEVWDDQGQPL-VGEKGElVCTRHfPAMPIGLWNDP--DRQKLRASYFSqfpgvwaQGDYAEQRPNGSLLIHGRSDAVL 525
Cdd:PRK07470 350 EVQIQDDEGRELpPGETGE-ICVIG-PAVFAGYYNNPeaNAKAFRDGWFR-------TGDLGHLDARGFLYITGRASDMY 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 526 NPGGVRIGTAEIYRQVEKVPQVQESLAIG---QRWqDDVRVVLFVrLNDGVELDEAleqQIRQVIRANTTPRHVPAKILA 602
Cdd:PRK07470 421 ISGGSNVYPREIEEKLLTHPAVSEVAVLGvpdPVW-GEVGVAVCV-ARDGAPVDEA---ELLAWLDGKVARYKLPKRFFF 495
|
570
....*....|....*...
gi 799207711 603 VTDIPRTISGKIVELAVR 620
Cdd:PRK07470 496 WDALPKSGYGKITKKMVR 513
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
91-614 |
2.97e-17 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 86.55 E-value: 2.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 91 EHLLRRRDDHPAVVAiseDGQReqLTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTLVGMLATTSLGAIWSCSS 170
Cdd:PRK12316 2010 AEQAARAPEAIAVVF---GDQH--LSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLD 2084
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 171 PDFGTQGVIDRFGQIEPKVLITCAGyryagkdidqtaklneILARLPSLEQLIIVPYARPQArvedyqtharvtrWSDFy 250
Cdd:PRK12316 2085 PNYPAERLAYMLEDSGAALLLTQRH----------------LLERLPLPAGVARLPLDRDAE-------------WADY- 2134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 251 pPGGEPEfVAVPFDHPLYILYSSGTTGVPK--CIIHGTggvLLTHLKEHGLHADLSRDDCLFYYTTCGW--MMWNWLVSV 326
Cdd:PRK12316 2135 -PDTAPA-VQLAGENLAYVIYTSGSTGLPKgvAVSHGA---LVAHCQAAGERYELSPADCELQFMSFSFdgAHEQWFHPL 2209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 327 LAiGATAVLYDGSpfHPGPERLIDLIDAEKISVFGTSPKFLATL----EKAGLQPrlshdlgSLKGLISTGSPLSPQSYD 402
Cdd:PRK12316 2210 LN-GARVLIRDDE--LWDPEQLYDEMERHGVTILDFPPVYLQQLaehaERDGRPP-------AVRVYCFGGEAVPAASLR 2279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 403 YVYREIKGELcLSSMSGGTDIVScfvigNPVLPVRRGEMQCKSLAMAI---------EVWDDQGQPL----VGE---KGE 466
Cdd:PRK12316 2280 LAWEALRPVY-LFNGYGPTEAVV-----TPLLWKCRPQDPCGAAYVPIgralgnrraYILDADLNLLapgmAGElylGGE 2353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 467 LVCTRHFpampiglwndpDRQKLRASYFSQFP------GVWAQGDYAEQRPNGSLLIHGRSDAVLNPGGVRIGTAEIYRQ 540
Cdd:PRK12316 2354 GLARGYL-----------NRPGLTAERFVPDPfsasgeRLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEAR 2422
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 799207711 541 VEKVPQVQESLAIGQRWQDDVRVVLFVRLNDGVELDealEQQIRQVIRANTTPRHVPAKILAVTDIPRTISGKI 614
Cdd:PRK12316 2423 LQAHPAVREAVVVAQDGASGKQLVAYVVPDDAAEDL---LAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKL 2493
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
91-614 |
1.02e-16 |
|
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: 83.13 E-value: 1.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 91 EHLLRRRDDHPAVVAISEDGQReqLTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTLVGMLATTSLGAIwscss 170
Cdd:cd17653 1 DAFERIAAAHPDAVAVESLGGS--LTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAA----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 171 pdfgtqgvidrfgqiepkvlitcagyrYAGKDIDqtaklneilarlpsleqliiVPYARPQARVEdyQTHARVTrwsdFY 250
Cdd:cd17653 74 ---------------------------YVPLDAK--------------------LPSARIQAILR--TSGATLL----LT 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 251 PPGGepefvavpfDHPLYILYSSGTTGVPKciihgtgGVLLTH--------LKEHGLHADLSRDDCLFY---YTTCGWMM 319
Cdd:cd17653 101 TDSP---------DDLAYIIFTSGSTGIPK-------GVMVPHrgvlnyvsQPPARLDVGPGSRVAQVLsiaFDACIGEI 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 320 WnwlvSVLAIGATAVLYDgspfHPGPerLIDLIDaeKISVFGTSPKFLATLEKAGLQprlshdlgSLKGLISTGSPLSPQ 399
Cdd:cd17653 165 F----STLCNGGTLVLAD----PSDP--FAHVAR--TVDALMSTPSILSTLSPQDFP--------NLKTIFLGGEAVPPS 224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 400 sydyVYREIKGELCLSSMSGGTDI-VSCFV----IGNPVL---PVRRGemqckslamAIEVWDDQGQP-LVGEKGELvCT 470
Cdd:cd17653 225 ----LLDRWSPGRRLYNAYGPTECtISSTMtellPGQPVTigkPIPNS---------TCYILDADLQPvPEGVVGEI-CI 290
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 471 RHFPAMPiGLWNDPDrQKLRASYFSQF-PGV--WAQGDYAEQRPNGSLLIHGRSDAVLNPGGVRIGTAEIYRQVEKV-PQ 546
Cdd:cd17653 291 SGVQVAR-GYLGNPA-LTASKFVPDPFwPGSrmYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEVVLQSqPE 368
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 799207711 547 VQESLAIgqrwQDDVRVVLFVrLNDGVELDealeqQIRQVIRANTTPRHVPAKILAVTDIPRTISGKI 614
Cdd:cd17653 369 VTQAAAI----VVNGRLVAFV-TPETVDVD-----GLRSELAKHLPSYAVPDRIIALDSFPLTANGKV 426
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
99-620 |
1.92e-16 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 82.75 E-value: 1.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 99 DHPAVVaISEDGqrEQLTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTLVgmlattslgAIWSCSSPDFGTQGV 178
Cdd:PRK13390 12 DRPAVI-VAETG--EQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALV---------VLWAALRSGLYITAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 179 IDRFGQIEPKVLITCAGYRYagkdIDQTAKLNEILARLPSLEQLIIvpyarpqarvedyQTHARVTRWSDFY-------P 251
Cdd:PRK13390 80 NHHLTAPEADYIVGDSGARV----LVASAALDGLAAKVGADLPLRL-------------SFGGEIDGFGSFEaalagagP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 252 PGGEPEFVAVpfdhplyILYSSGTTGVPKCI--------IHGTGGVLLTHLKehGLHaDLSRDDclFYYTTCGWMM---W 320
Cdd:PRK13390 143 RLTEQPCGAV-------MLYSSGTTGFPKGIqpdlpgrdVDAPGDPIVAIAR--AFY-DISESD--IYYSSAPIYHaapL 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 321 NWLVSVLAIGATAVL---YDGSPfhpgperLIDLIDAEKISVFGTSPKFLATLEKAGLQPRLSHDLGSLKGLISTGSPlS 397
Cdd:PRK13390 211 RWCSMVHALGGTVVLakrFDAQA-------TLGHVERYRITVTQMVPTMFVRLLKLDADVRTRYDVSSLRAVIHAAAP-C 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 398 PQSYDYVYREIKGELCLSSMSGgTDIVSCFVIGNPVLPVRRGEMQcKSLAMAIEVWDDQGQPL-VGEKGELVCTRHfpAM 476
Cdd:PRK13390 283 PVDVKHAMIDWLGPIVYEYYSS-TEAHGMTFIDSPDWLAHPGSVG-RSVLGDLHICDDDGNELpAGRIGTVYFERD--RL 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 477 PIGLWNDPdrQKLRASYFSQFPGVWAQGDYAEQRPNGSLLIHGRSDAVLNPGGVRIGTAEIYRQVEKVPQVQESLAIG-- 554
Cdd:PRK13390 359 PFRYLNDP--EKTAAAQHPAHPFWTTVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGvp 436
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 799207711 555 -QRWQDDVRVVlfVRLNDGVELDEALEQQIRQVIRANTTPRHVPAKILAVTDIPRTISGKIVELAVR 620
Cdd:PRK13390 437 dPEMGEQVKAV--IQLVEGIRGSDELARELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
101-614 |
3.39e-16 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 83.08 E-value: 3.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 101 PAVVAISEDGQReqLTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTLVGMLATTSLGAIWSCSSPDFGTQGVID 180
Cdd:PRK12316 3071 PDAVALAFGEQR--LSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAY 3148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 181 RFGQIEPKVLITCAGYRYAGKDIDQTAKLneilarlpsleqliivpyarpQARVEDYQTHarvtrwsdfyppggEPEFVA 260
Cdd:PRK12316 3149 MLEDSGAQLLLSQSHLRLPLAQGVQVLDL---------------------DRGDENYAEA--------------NPAIRT 3193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 261 VPfDHPLYILYSSGTTGVPKCIIHGTGGvLLTHLKEHGLHADLSRDDCLFYYTTCGWMMWNWLVSVLAIGATAVLYDGSP 340
Cdd:PRK12316 3194 MP-ENLAYVIYTSGSTGKPKGVGIRHSA-LSNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPE 3271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 341 FHPGPERLIDLIDAEKISVFGTSPKFLATLekagLQPRLSHDLGSLKGLISTGSPLSPQSYDYVYreikGELCLSSMSGG 420
Cdd:PRK12316 3272 DWRDPALLVELINSEGVDVLHAYPSMLQAF----LEEEDAHRCTSLKRIVCGGEALPADLQQQVF----AGLPLYNLYGP 3343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 421 TDIV------SCFVIGNPVLPVRRGEMQckslaMAIEVWDDQGQPL-VGEKGELVCTRHFPAMpiGLWNDPDRQKLR--A 491
Cdd:PRK12316 3344 TEATitvthwQCVEEGKDAVPIGRPIAN-----RACYILDGSLEPVpVGALGELYLGGEGLAR--GYHNRPGLTAERfvP 3416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 492 SYFSQFPGVWAQGDYAEQRPNGSLLIHGRSDAVLNPGGVRIGTAEIYRQVEKVPQVQESLAIGQRWQDDVRVVlfVRLND 571
Cdd:PRK12316 3417 DPFVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLAVDGRQLVAYV--VPEDE 3494
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 799207711 572 GVELDEALEQQIRQviranTTPRH-VPAKILAVTDIPRTISGKI 614
Cdd:PRK12316 3495 AGDLREALKAHLKA-----SLPEYmVPAHLLFLERMPLTPNGKL 3533
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
268-614 |
4.16e-15 |
|
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.
Pssm-ID: 341303 [Multi-domain] Cd Length: 453 Bit Score: 78.21 E-value: 4.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 268 YILYSSGTTGVPKCIIHGTGGV--LLTHLKE------HGLHADLSRDDCLFYYTtcgwmMWNWLVSVLAiGATAVLYDGS 339
Cdd:cd17648 98 YAIYTSGTTGKPKGVLVEHGSVvnLRTSLSEryfgrdNGDEAVLFFSNYVFDFF-----VEQMTLALLN-GQKLVVPPDE 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 340 pFHPGPERLIDLIDAEKISVFGTSPKFLATLEKAglqpRLSHdlgsLKGLISTGSPLSPQSYDYVYREIKGELclssMSG 419
Cdd:cd17648 172 -MRFDPDRFYAYINREKVTYLSGTPSVLQQYDLA----RLPH----LKRVDAAGEEFTAPVFEKLRSRFAGLI----INA 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 420 -GTDIVSCFVIGNPVLPVRRGEMQ-CKSLA-MAIEVWDDQGQPL-VGEKGEL----VC-TRhfpampiGLWNDPD--RQK 488
Cdd:cd17648 239 yGPTETTVTNHKRFFPGDQRFDKSlGRPVRnTKCYVLNDAMKRVpVGAVGELylggDGvAR-------GYLNRPEltAER 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 489 LRASYF--------SQFPGVWAQGDYAEQRPNGSLLIHGRSDAVLNPGGVRIGTAEIYRQVEKVPQVQESLAIGQRWQDD 560
Cdd:cd17648 312 FLPNPFqteqerarGRNARLYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAKEDASQ 391
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 561 V------RVVLFVRLNDGVeLDEaleQQIRQVIRANTTPRHVPAKILAVTDIPRTISGKI 614
Cdd:cd17648 392 AqsriqkYLVGYYLPEPGH-VPE---SDLLSFLRAKLPRYMVPARLVRLEGIPVTINGKL 447
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
267-613 |
4.25e-15 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 77.42 E-value: 4.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 267 LYILYSSGTTGVPKCII---HGTGGVLLT--------HLKEHGLHADLSRDDCLFYYTTCGWM----MWNWLVSVLaiGA 331
Cdd:cd05924 6 LYILYTGGTTGMPKGVMwrqEDIFRMLMGgadfgtgeFTPSEDAHKAAAAAAGTVMFPAPPLMhgtgSWTAFGGLL--GG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 332 TAVLYDGSPFHPgpERLIDLIDAEKI-SVFGTSPKFLATLEKAgLQPRLSHDLGSLKGLISTGSPLSPqsydyvyrEIKG 410
Cdd:cd05924 84 QTVVLPDDRFDP--EEVWRTIEKHKVtSMTIVGDAMARPLIDA-LRDAGPYDLSSLFAISSGGALLSP--------EVKQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 411 ELCL------------SSMSGGTDIVSCFVIGNPVLP-VRRGEMQCkslamaieVWDDQGQPLVGEKGEL--VCTRHFpa 475
Cdd:cd05924 153 GLLElvpnitlvdafgSSETGFTGSGHSAGSGPETGPfTRANPDTV--------VLDDDGRVVPPGSGGVgwIARRGH-- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 476 MPIGLWNDPdrqKLRASYFSQFPGV-WA-QGDYAEQRPNGSLLIHGRSDAVLNPGGVRIGTAEIYRQVEKVPQVQESLAI 553
Cdd:cd05924 223 IPLGYYGDE---AKTAETFPEVDGVrYAvPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVV 299
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 799207711 554 GQ---RWQDdvRVVLFVRLNDGVELDEA-LEQQIRQVIRANTTPRHVpakiLAVTDIPRTISGK 613
Cdd:cd05924 300 GRpdeRWGQ--EVVAVVQLREGAGVDLEeLREHCRTRIARYKLPKQV----VFVDEIERSPAGK 357
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
266-614 |
8.10e-15 |
|
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: 76.15 E-value: 8.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 266 PLYILYSSGTTGVPKCII--HGTGGVLLTHLKEHGLhaDLSRDDCLFY--YTTCGWMMWNWLVSVLAIGATAVLYDGSPF 341
Cdd:cd17635 3 PLAVIFTSGTTGEPKAVLlaNKTFFAVPDILQKEGL--NWVVGDVTYLplPATHIGGLWWILTCLIHGGLCVTGGENTTY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 342 hpgpERLIDLIDAEKISVFGTSPKFLATLekAGLQPRLSHDLGSLKGLISTGS-------------PLSPQSYDYVYREI 408
Cdd:cd17635 81 ----KSLFKILTTNAVTTTCLVPTLLSKL--VSELKSANATVPSLRLIGYGGSraiaadvrfieatGLTNTAQVYGLSET 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 409 KGELCLSSMSGGTDIVScfvIGNPVlpvrRGemqckslaMAIEVWDDQGQPLV-GEKGELVCTRhfPAMPIGLWNDPDRQ 487
Cdd:cd17635 155 GTALCLPTDDDSIEINA---VGRPY----PG--------VDVYLAATDGIAGPsASFGTIWIKS--PANMLGYWNNPERT 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 488 KlrasyfSQFPGVWAQ-GDYAEQRPNGSLLIHGRSDAVLNPGGVRIGTAEIYRQVEKVPQVQES--LAIGQRWQDDVrVV 564
Cdd:cd17635 218 A------EVLIDGWVNtGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECacYEISDEEFGEL-VG 290
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 799207711 565 LFVRLNDgvELDEALEQQIRQVIRANTTPRHVPAKILAVTDIPRTISGKI 614
Cdd:cd17635 291 LAVVASA--ELDENAIRALKHTIRRELEPYARPSTIVIVTDIPRTQSGKV 338
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
99-614 |
1.59e-14 |
|
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341311 [Multi-domain] Cd Length: 479 Bit Score: 76.36 E-value: 1.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 99 DHPAVVAisedgQREQLTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTLVGMLATTSLGAIWSCSSPDFGTQGV 178
Cdd:cd17656 3 DAVAVVF-----ENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 179 IDRFGQIEPKVLITCAGyryagkdidqtaklneiLARLPSLEQLIIVPyarpqarvedyqtharvtRWSDFYPPGGEPEF 258
Cdd:cd17656 78 IYIMLDSGVRVVLTQRH-----------------LKSKLSFNKSTILL------------------EDPSISQEDTSNID 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 259 VAVPFDHPLYILYSSGTTGVPKciihgtgGVLLTH------LKEHGLHADLSRDDCLFYYTTCGW-MMWNWLVSVLAIGA 331
Cdd:cd17656 123 YINNSDDLLYIIYTSGTTGKPK-------GVQLEHknmvnlLHFEREKTNINFSDKVLQFATCSFdVCYQEIFSTLLSGG 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 332 TAVLYDGSPFHPGPErLIDLIDAEKISVFGTSPKFLATL-EKAGLQPRLSHdlgSLKGLISTGSPLS-PQSYDYVYREIK 409
Cdd:cd17656 196 TLYIIREETKRDVEQ-LFDLVKRHNIEVVFLPVAFLKFIfSEREFINRFPT---CVKHIITAGEQLViTNEFKEMLHEHN 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 410 GELCLSSMSGGTDIVSCFVIGN----PVLPVRRGEMQCkslaMAIEVWDDQGQPL-VGEKGELVCTRhfPAMPIGLWNdp 484
Cdd:cd17656 272 VHLHNHYGPSETHVVTTYTINPeaeiPELPPIGKPISN----TWIYILDQEQQLQpQGIVGELYISG--ASVARGYLN-- 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 485 dRQKLRASYFSQFP-----GVWAQGDYAEQRPNGSLLIHGRSDAVLNPGGVRIGTAEIYRQVEKVPQVQESLAIGqrWQD 559
Cdd:cd17656 344 -RQELTAEKFFPDPfdpneRMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLD--KAD 420
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 799207711 560 DVR-------VVLFVRLNDgVELDEALEQQIRQVIranttprhVPAKILAVTDIPRTISGKI 614
Cdd:cd17656 421 DKGekylcayFVMEQELNI-SQLREYLAKQLPEYM--------IPSFFVPLDQLPLTPNGKV 473
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
91-620 |
2.29e-14 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 76.53 E-value: 2.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 91 EHLLRRRDDHPAVVAIS------EDGQREQLTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTLVGMLATTSLG- 163
Cdd:PRK07529 29 ELLSRAAARHPDAPALSflldadPLDRPETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGEAAGi 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 164 --AIWSCSSPDfgtqgvidrfgQI-------EPKVLITCAGYryAGKDIDQtaKLNEILARLPSLEQLI----------- 223
Cdd:PRK07529 109 anPINPLLEPE-----------QIaellraaGAKVLVTLGPF--PGTDIWQ--KVAEVLAALPELRTVVevdlarylpgp 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 224 ---IVPYARPQARVEDYQTHARVTRWSD---FYPPGGEPEFVAVPFdhplyilYSSGTTGVPKCIIHGTGGVLLTHLkeh 297
Cdd:PRK07529 174 krlAVPLIRRKAHARILDFDAELARQPGdrlFSGRPIGPDDVAAYF-------HTGGTTGMPKLAQHTHGNEVANAW--- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 298 GLHADLSRDD-----C---LFY----YTTCgwmmwnwlVSVLAIGATAVLydgspfhPGP-----ERLID----LIDAEK 356
Cdd:PRK07529 244 LGALLLGLGPgdtvfCglpLFHvnalLVTG--------LAPLARGAHVVL-------ATPqgyrgPGVIAnfwkIVERYR 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 357 ISVFGTSPKFLATLekagLQ-PRLSHDLGSLKGLISTGSPLSPQsydyVYREIKGELCLSSMSG-----GTDIVSCfvig 430
Cdd:PRK07529 309 INFLSGVPTVYAAL----LQvPVDGHDISSLRYALCGAAPLPVE----VFRRFEAATGVRIVEGyglteATCVSSV---- 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 431 NPvlpvRRGEMQCKSL-------AMAIEVWDDQGQPL----VGEKGELvCTRHfPAMPIGLWNDPDRQKLRASyfsqfpG 499
Cdd:PRK07529 377 NP----PDGERRIGSVglrlpyqRVRVVILDDAGRYLrdcaVDEVGVL-CIAG-PNVFSGYLEAAHNKGLWLE------D 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 500 VWAQ-GDYAEQRPNGSLLIHGRSDAVLNPGGVRIGTAEIYRQVEKVPQVQESLAIGqrwQDDVRV----VLFVRLNDGVE 574
Cdd:PRK07529 445 GWLNtGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAAVG---RPDAHAgelpVAYVQLKPGAS 521
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 799207711 575 LDEA-LEQQIRQVI--RANttprhVPAKILAVTDIPRTISGKIVELAVR 620
Cdd:PRK07529 522 ATEAeLLAFARDHIaeRAA-----VPKHVRILDALPKTAVGKIFKPALR 565
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
115-620 |
3.72e-14 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 74.91 E-value: 3.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 115 LTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTLVGMLATTSLGAIWSCSSPDFGTQGVIDRFgqiepkvlitca 194
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRDRV------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 195 gyryagkDIDQTAKlneilarlpsleqliivpyarpqARVEDyQTHArvtrwsdfyppggepefvavpfDHPLYILYSSG 274
Cdd:cd05974 69 -------DRGGAVY-----------------------AAVDE-NTHA----------------------DDPMLLYFTSG 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 275 TTGVPKCIIHGTGGVLLTHLKEHgLHADLSRDDCLFYYTTCGWM--MWNWLVSVLAIGATAVLYDGSPFHpgPERLIDLI 352
Cdd:cd05974 96 TTSKPKLVEHTHRSYPVGHLSTM-YWIGLKPGDVHWNISSPGWAkhAWSCFFAPWNAGATVFLFNYARFD--AKRVLAAL 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 353 DAEKISVFGTSPkflaTLEKAGLQPRLSHDLGSLKGLISTGSPLSPQSYDYVYREIKgeLCLSSMSGGTDiVSCFVIGNP 432
Cdd:cd05974 173 VRYGVTTLCAPP----TVWRMLIQQDLASFDVKLREVVGAGEPLNPEVIEQVRRAWG--LTIRDGYGQTE-TTALVGNSP 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 433 VLPVRRGEMQCKSLAMAIEVWDDQGQPlvGEKGElVCTRHFPAMPIGLW----NDPDRQK--LRASYFSqfpgvwaQGDY 506
Cdd:cd05974 246 GQPVKAGSMGRPLPGYRVALLDPDGAP--ATEGE-VALDLGDTRPVGLMkgyaGDPDKTAhaMRGGYYR-------TGDI 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 507 AEQRPNGSLLIHGRSDAVLNPGGVRIGTAEIYRQVEKVPQVQESLAIGQrwQDDVRVVL---FVRLNDGVELDEALEQQI 583
Cdd:cd05974 316 AMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPS--PDPVRLSVpkaFIVLRAGYEPSPETALEI 393
|
490 500 510
....*....|....*....|....*....|....*..
gi 799207711 584 RQVIRANTTPrHVPAKILAVTDIPRTISGKIVELAVR 620
Cdd:cd05974 394 FRFSRERLAP-YKRIRRLEFAELPKTISGKIRRVELR 429
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
91-614 |
4.03e-14 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 76.53 E-value: 4.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 91 EHLLRRRDDHPAVVAisedGQrEQLTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTLVGMLATTSLGAIWSCSS 170
Cdd:PRK12316 518 EEQVERTPEAPALAF----GE-ETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLD 592
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 171 PDFGTQGVIDRFGQIEPKVLITcagyryagkdidQTAklneILARLPSLEQLIIVPYARPQARVEDYQTHArvtrwsdfy 250
Cdd:PRK12316 593 PEYPAERLAYMLEDSGVQLLLS------------QSH----LGRKLPLAAGVQVLDLDRPAAWLEGYSEEN--------- 647
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 251 ppggePEFVAVPfDHPLYILYSSGTTGVPKciihgtgGVLLTH----------LKEHGLHA-DLSRDDCLFYYTTCGWMM 319
Cdd:PRK12316 648 -----PGTELNP-ENLAYVIYTSGSTGKPK-------GAGNRHralsnrlcwmQQAYGLGVgDTVLQKTPFSFDVSVWEF 714
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 320 WNWLVSvlaiGATAVLYdGSPFHPGPERLIDLIDAEKISVFGTSPKFL-ATLEKAGLQprlshDLGSLKGLISTGSPLSP 398
Cdd:PRK12316 715 FWPLMS----GARLVVA-APGDHRDPAKLVELINREGVDTLHFVPSMLqAFLQDEDVA-----SCTSLRRIVCSGEALPA 784
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 399 QSYDYVYREI-KGEL--------------CLSSMSGGTDIVScfvIGNPVLPVRrgemqckslamaIEVWDDQGQPL-VG 462
Cdd:PRK12316 785 DAQEQVFAKLpQAGLynlygpteaaidvtHWTCVEEGGDSVP---IGRPIANLA------------CYILDANLEPVpVG 849
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 463 EKGELVC-----TRHFPAMPiGLwndpDRQKLRASYFSQFPGVWAQGDYAEQRPNGSLLIHGRSDAVLNPGGVRIGTAEI 537
Cdd:PRK12316 850 VLGELYLagrglARGYHGRP-GL----TAERFVPSPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEI 924
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 799207711 538 YRQVEKVPQVQESLAIGQRWQDDVRVVlfVRLNDGVELDEALEQQIRQVIranttPRH-VPAKILAVTDIPRTISGKI 614
Cdd:PRK12316 925 EARLLEHPWVREAAVLAVDGKQLVGYV--VLESEGGDWREALKAHLAASL-----PEYmVPAQWLALERLPLTPNGKL 995
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
88-400 |
5.86e-14 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 74.94 E-value: 5.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 88 NFAEHLL---RRRDDHPAVVA---ISEDGQR--EQLTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTLVGMLAT 159
Cdd:PRK09274 7 NIARHLPraaQERPDQLAVAVpggRGADGKLayDELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 160 TSLGAIWSCSSPDFGTQGVIDRFGQIEPKVLItcaGYRYAgkdidqtaklneILARL------PSLEQLIIV--PYARPQ 231
Cdd:PRK09274 87 FKAGAVPVLVDPGMGIKNLKQCLAEAQPDAFI---GIPKA------------HLARRlfgwgkPSVRRLVTVggRLLWGG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 232 ARVEDYQTHarvtrwsdfyPPGGEPEFVAVPFDHPLYILYSSGTTGVPKciihgtgGVLLTH---------LKEHGLHAD 302
Cdd:PRK09274 152 TTLATLLRD----------GAAAPFPMADLAPDDMAAILFTSGSTGTPK-------GVVYTHgmfeaqieaLREDYGIEP 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 303 LSRDDCLFYyttcgwmmwnwLVSV--LAIGATAVLYDGSPFHPG---PERLIDLIDAEKISVFGTSPKFLATLEKAGLQP 377
Cdd:PRK09274 215 GEIDLPTFP-----------LFALfgPALGMTSVIPDMDPTRPAtvdPAKLFAAIERYGVTNLFGSPALLERLGRYGEAN 283
|
330 340
....*....|....*....|...
gi 799207711 378 RLShdLGSLKGLISTGSPLSPQS 400
Cdd:PRK09274 284 GIK--LPSLRRVISAGAPVPIAV 304
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
94-620 |
6.71e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 74.64 E-value: 6.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 94 LRRRDDHPAVVaiseDGQREqLTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTLVGMLATTSLGAIWSCSSPDF 173
Cdd:PRK06188 22 LKRYPDRPALV----LGDTR-LTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHPLG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 174 GTQGVIDRFGQIEPKVLItcagyryagkdIDQTAKLN---EILARLPSLEQLII---VPYARpqarveDYQTHArvtrws 247
Cdd:PRK06188 97 SLDDHAYVLEDAGISTLI-----------VDPAPFVEralALLARVPSLKHVLTlgpVPDGV------DLLAAA------ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 248 DFYPPGgEPEFVAVPFDhPLYILYSSGTTGVPKciihgtgGVLLTHlkehglhadlsrddclfyytTCGWMM-------W 320
Cdd:PRK06188 154 AKFGPA-PLVAAALPPD-IAGLAYTGGTTGKPK-------GVMGTH--------------------RSIATMaqiqlaeW 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 321 NW-------------------LVSVLAIGATAVLYDGspFHPgpERLIDLIDAEKISVFGTSPKFLATLEKAglqPRLS- 380
Cdd:PRK06188 205 EWpadprflmctplshaggafFLPTLLRGGTVIVLAK--FDP--AEVLRAIEEQRITATFLVPTMIYALLDH---PDLRt 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 381 HDLGSLKGLISTGSPLSP-----------QSYDYVYREIKGELCLSSMS----GGTD---IVSCfviGNPVLPVRrgemq 442
Cdd:PRK06188 278 RDLSSLETVYYGASPMSPvrlaeaierfgPIFAQYYGQTEAPMVITYLRkrdhDPDDpkrLTSC---GRPTPGLR----- 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 443 ckslamaIEVWDDQGQPL-VGEKGELvCTRHfPAMPIGLWNDPDrQKLRAsyfsqFPGVWAQ-GDYAEQRPNGSLLIHGR 520
Cdd:PRK06188 350 -------VALLDEDGREVaQGEVGEI-CVRG-PLVMDGYWNRPE-ETAEA-----FRDGWLHtGDVAREDEDGFYYIVDR 414
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 521 SDAVLNPGGVrigtaEIY-RQVEKV----PQVQESLAIG---QRWQDDVRVVlfVRLNDGVELDEAleqQIRQVIRANTT 592
Cdd:PRK06188 415 KKDMIVTGGF-----NVFpREVEDVlaehPAVAQVAVIGvpdEKWGEAVTAV--VVLRPGAAVDAA---ELQAHVKERKG 484
|
570 580
....*....|....*....|....*...
gi 799207711 593 PRHVPAKILAVTDIPRTISGKIVELAVR 620
Cdd:PRK06188 485 SVHAPKQVDFVDSLPLTALGKPDKKALR 512
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
265-614 |
2.09e-13 |
|
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: 71.67 E-value: 2.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 265 HPLYILYSSGTTGVPKCIIHGTGGVLLTH-LKEHGLHadLSRDDCLFYYTTcgwmmwnwLVSVLAI-GATAVLYDGSPFH 342
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRSERSWIESFvCNEDLFN--ISGEDAILAPGP--------LSHSLFLyGAISALYLGGTFI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 343 ----PGPERLIDLIDAEKISVFGTSPKFLATLEKAGlqprlSHDLgSLKGLISTGSPLSPQSYDYVYREI-KGELCLSSm 417
Cdd:cd17633 71 gqrkFNPKSWIRKINQYNATVIYLVPTMLQALARTL-----EPES-KIKSIFSSGQKLFESTKKKLKNIFpKANLIEFY- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 418 sgGTDIVScFVIGN------PVLPVRRgemQCKSLAMAIEVWDDQGQPLVGEKGELVctrhFPAMPIGLWNDPDrqklra 491
Cdd:cd17633 144 --GTSELS-FITYNfnqesrPPNSVGR---PFPNVEIEIRNADGGEIGKIFVKSEMV----FSGYVRGGFSNPD------ 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 492 SYFSQfpgvwaqGDYAEQRPNGSLLIHGRSDAVLNPGGVRIGTAEIYRQVEKVPQVQESLAIG---QRWQDdvrVVLFVr 568
Cdd:cd17633 208 GWMSV-------GDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGipdARFGE---IAVAL- 276
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 799207711 569 lndgVELDEALEQQIRQVIRANTTPRHVPAKILAVTDIPRTISGKI 614
Cdd:cd17633 277 ----YSGDKLTYKQLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKI 318
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
102-615 |
3.16e-13 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 72.24 E-value: 3.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 102 AVVAISEDGQReqLTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTLVGMLATTSLGAIWSCSSPDFgtqgVIDR 181
Cdd:PRK08276 1 PAVIMAPSGEV--VTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHL----TAAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 182 FGQI----EPKVLITCAGYRYAGKdidqtaklnEILARLPS-LEQLIIVPYARPqaRVEDYqtharvTRWSDFYPPGGEP 256
Cdd:PRK08276 75 IAYIvddsGAKVLIVSAALADTAA---------ELAAELPAgVPLLLVVAGPVP--GFRSY------EEALAAQPDTPIA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 257 efvavpfDHPL--YILYSSGTTGVPKciihgtgGVL--LTHLKEHGLHADLSRDDCLFYYTT--CGWMM---------WN 321
Cdd:PRK08276 138 -------DETAgaDMLYSSGTTGRPK-------GIKrpLPGLDPDEAPGMMLALLGFGMYGGpdSVYLSpaplyhtapLR 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 322 WLVSVLAIGATAVLYDgspfHPGPERLIDLIDAEKISVFGTSPKFLATLEKAGLQPRLSHDLGSLKGLISTGSPLSPqsy 401
Cdd:PRK08276 204 FGMSALALGGTVVVME----KFDAEEALALIERYRVTHSQLVPTMFVRMLKLPEEVRARYDVSSLRVAIHAAAPCPV--- 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 402 dyvyrEIK-------G----ELCLSSMSGGTDIVSCF-------VIGNPVLPVrrgemqckslamaIEVWDDQGQPL-VG 462
Cdd:PRK08276 277 -----EVKramidwwGpiihEYYASSEGGGVTVITSEdwlahpgSVGKAVLGE-------------VRILDEDGNELpPG 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 463 EKGELvctrHF--PAMPIGLWNDPDrqKLRASYFsqfPGVWAQ-GDYAEQRPNGSLLIHGR-SDAVLNpGGVRIGTAEIY 538
Cdd:PRK08276 339 EIGTV----YFemDGYPFEYHNDPE--KTAAARN---PHGWVTvGDVGYLDEDGYLYLTDRkSDMIIS-GGVNIYPQEIE 408
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 539 RQVEKVPQVQESLAIG---QRWQDDVRVVlfVRLNDGVELDEALEQQIRQVIRANTTPRHVPAKILAVTDIPRTISGKIV 615
Cdd:PRK08276 409 NLLVTHPKVADVAVFGvpdEEMGERVKAV--VQPADGADAGDALAAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLY 486
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
95-620 |
4.56e-13 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 72.03 E-value: 4.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 95 RRRDDHPAVVAISEDgqrEQLTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTLVGMLATTSLGAIWSCSSpdfg 174
Cdd:PRK13391 8 QTTPDKPAVIMASTG---EVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVN---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 175 TQGVIDRFGQI----EPKVLITCAgyryAGKDIdqtakLNEILARLPSLEQLIIVPYARPQARVEDYQTH-ARVTRWsdf 249
Cdd:PRK13391 81 SHLTPAEAAYIvddsGARALITSA----AKLDV-----ARALLKQCPGVRHRLVLDGDGELEGFVGYAEAvAGLPAT--- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 250 yPPGGEPEFVAvpfdhplyILYSSGTTGVPKCIihgtggvlLTHLKEHGLHADLSrddclfyYTTCGWMMWN-------- 321
Cdd:PRK13391 149 -PIADESLGTD--------MLYSSGTTGRPKGI--------KRPLPEQPPDTPLP-------LTAFLQRLWGfrsdmvyl 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 322 ------------WLVSVLAIGATAVLYDgspfHPGPERLIDLIDAEKISVFGTSPKFLATLEKAGLQPRLSHDLGSLKGL 389
Cdd:PRK13391 205 spaplyhsapqrAVMLVIRLGGTVIVME----HFDAEQYLALIEEYGVTHTQLVPTMFSRMLKLPEEVRDKYDLSSLEVA 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 390 ISTGSPLSPQsydyvyreIKGEL------CLSSMSGGTDIVSCFVIGNPVLPVRRGEMQcKSLAMAIEVWDDQGQPL-VG 462
Cdd:PRK13391 281 IHAAAPCPPQ--------VKEQMidwwgpIIHEYYAATEGLGFTACDSEEWLAHPGTVG-RAMFGDLHILDDDGAELpPG 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 463 EKGELVCTRhfpAMPIGLWNDPDrqKLRASYFSQfpGVWAQ-GDYAEQRPNGSLLIHGRSDAVLNPGGVRIGTAEIYRQV 541
Cdd:PRK13391 352 EPGTIWFEG---GRPFEYLNDPA--KTAEARHPD--GTWSTvGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLL 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 542 EKVPQVQESLAIGQRWQD---DVRVVlfVRLNDGVELDEALEQQIRQVIRANTTPRHVPAKILAVTDIPRTISGKIVELA 618
Cdd:PRK13391 425 ITHPKVADAAVFGVPNEDlgeEVKAV--VQPVDGVDPGPALAAELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRL 502
|
..
gi 799207711 619 VR 620
Cdd:PRK13391 503 LR 504
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
106-614 |
8.32e-13 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 71.16 E-value: 8.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 106 ISEDGQREQLTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTLVGMLATTsLGAIWSCSSPDFGTQGVID-RFGQ 184
Cdd:cd05906 31 IDADGSEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACV-LAGFVPAPLTVPPTYDEPNaRLRK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 185 IE--------PKVLITCAGyryagkdidqTAKLNEILARLPSLEQLIIVpyarpqarVEDYQTHARVTRWsdfypPGGEP 256
Cdd:cd05906 110 LRhiwqllgsPVVLTDAEL----------VAEFAGLETLSGLPGIRVLS--------IEELLDTAADHDL-----PQSRP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 257 EFVAVpfdhplyILYSSGTTGVPKCIIHgTGGVLLTHLKEHGLHADLSRDDclfyyTTCGWMMWNWLVSVLAIGATAVLY 336
Cdd:cd05906 167 DDLAL-------LMLTSGSTGFPKAVPL-THRNILARSAGKIQHNGLTPQD-----VFLNWVPLDHVGGLVELHLRAVYL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 337 DGSPFHPGPE-------RLIDLIDAEKISVfgT-SPKFLATL--EKAGLQPRLSHDLGSLKGLISTGSPLSPQSYDYVYR 406
Cdd:cd05906 234 GCQQVHVPTEeiladplRWLDLIDRYRVTI--TwAPNFAFALlnDLLEEIEDGTWDLSSLRYLVNAGEAVVAKTIRRLLR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 407 EIK---------------GELClssmSGGTDIVSC----------FV-IGNPVlPvrrgemqckslAMAIEVWDDQGQPL 460
Cdd:cd05906 312 LLEpyglppdairpafgmTETC----SGVIYSRSFptydhsqaleFVsLGRPI-P-----------GVSMRIVDDEGQLL 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 461 -VGEKGEL-VCTrhfPAMPIGLWNDPDrqkLRASYFSqfPGVWAQ-GDYAEQRpNGSLLIHGRSDAVLNPGGVRIGTAEI 537
Cdd:cd05906 376 pEGEVGRLqVRG---PVVTKGYYNNPE---ANAEAFT--EDGWFRtGDLGFLD-NGNLTITGRTKDTIIVNGVNYYSHEI 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 538 YRQVEKVPQVQES--LAIGQRWQDDVR---VVLFV----RLNDGVELDEALEQQIRQVIraNTTPRHV-PakiLAVTDIP 607
Cdd:cd05906 447 EAAVEEVPGVEPSftAAFAVRDPGAETeelAIFFVpeydLQDALSETLRAIRSVVSREV--GVSPAYLiP---LPKEEIP 521
|
....*..
gi 799207711 608 RTISGKI 614
Cdd:cd05906 522 KTSLGKI 528
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
104-614 |
1.02e-12 |
|
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: 70.40 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 104 VAISEDGQReqLTYAELAEHVAGLQKSLRAAG-VTQGDRVAACMPNTWQTLVGMLATTSLGAIwscsspdfgtqgvidrf 182
Cdd:cd05941 3 IAIVDDGDS--ITYADLVARAARLANRLLALGkDLRGDRVAFLAPPSAEYVVAQLAIWRAGGV----------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 183 gqiepkvlitcagyryagkdidqtaklneilarlpsleqliIVPYAR--PQARVEDYQTHARVTRWSDfyppggepefva 260
Cdd:cd05941 64 -----------------------------------------AVPLNPsyPLAELEYVITDSEPSLVLD------------ 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 261 vpfdhPLYILYSSGTTGVPKciihgtgGVLLTHlkeHGLHADLsrdDCLFYYttcgwmmWNW-----LVSVLAI------ 329
Cdd:cd05941 91 -----PALILYTSGTTGRPK-------GVVLTH---ANLAANV---RALVDA-------WRWteddvLLHVLPLhhvhgl 145
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 330 --GATAVLYDGS------PFHPGPERLIDLIDAekISVFGTSP----KFLATLEKAGLQPRLSHDLG--SLKGLISTGSP 395
Cdd:cd05941 146 vnALLCPLFAGAsveflpKFDPKEVAISRLMPS--ITVFMGVPtiytRLLQYYEAHFTDPQFARAAAaeRLRLMVSGSAA 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 396 LSPQSYDYvYREIKGELCLSSMsGGTDIVscFVIGNPVLPVRRGemqcKSLAMAIE------VWDDQGQPL-VGEKGELv 468
Cdd:cd05941 224 LPVPTLEE-WEAITGHTLLERY-GMTEIG--MALSNPLDGERRP----GTVGMPLPgvqariVDEETGEPLpRGEVGEI- 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 469 CTRHfPAMPIGLWNDPDRQKlrasyfSQFP--GVWAQGDYAEQRPNGSLLIHGR-SDAVLNPGGVRIGTAEIYRQVEKVP 545
Cdd:cd05941 295 QVRG-PSVFKEYWNKPEATK------EEFTddGWFKTGDLGVVDEDGYYWILGRsSVDIIKSGGYKVSALEIERVLLAHP 367
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 799207711 546 QVQESLAIGQrwQDDV---RVVLFVRLNDGVE-LD-EALEQQIRQVIrantTPRHVPAKILAVTDIPRTISGKI 614
Cdd:cd05941 368 GVSECAVIGV--PDPDwgeRVVAVVVLRAGAAaLSlEELKEWAKQRL----APYKRPRRLILVDELPRNAMGKV 435
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
100-622 |
1.25e-12 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 70.66 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 100 HPAVVAISedGQREQLTYAELAEHVAGLQKSLR-AAGVTQGDRVAACMPNTWQTLVGMLATTSLGAIWSCSSPDFGTQGV 178
Cdd:PRK06839 15 HPDRIAII--TEEEEMTYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENEL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 179 IDRFGQIEPKVLitCAGYRYAGKDIDQTAKLNeiLARLPSLEQLiivpyarpqARVEDYQTharvtrwSDFYPPGGepef 258
Cdd:PRK06839 93 IFQLKDSGTTVL--FVEKTFQNMALSMQKVSY--VQRVISITSL---------KEIEDRKI-------DNFVEKNE---- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 259 vavpfDHPLYILYSSGTTGVPKciihgtgGVLLTHLKE-----HGLHA-DLSRDDC------LFYYTTCGWMMwnwLVSV 326
Cdd:PRK06839 149 -----SASFIICYTSGTTGKPK-------GAVLTQENMfwnalNNTFAiDLTMHDRsivllpLFHIGGIGLFA---FPTL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 327 LAIGATAVlydgsPFHPGPERLIDLIDAEKISVFGTSPKFLATLEKAGLqpRLSHDLGSLKGLISTGSPlSPQSYDYVYR 406
Cdd:PRK06839 214 FAGGVIIV-----PRKFEPTKALSMIEKHKVTVVMGVPTIHQALINCSK--FETTNLQSVRWFYNGGAP-CPEELMREFI 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 407 EiKGeLCLSSMSGGTDIV-SCFVIGNPVLPVRRGEMQCKSLAMAIEVWDDQGQPL-VGEKGELvcTRHFPAMPIGLWNDP 484
Cdd:PRK06839 286 D-RG-FLFGQGFGMTETSpTVFMLSEEDARRKVGSIGKPVLFCDYELIDENKNKVeVGEVGEL--LIRGPNVMKEYWNRP 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 485 DR--QKLRASYFSQfpgvwaqGDYAEQRPNGSLLIHGRSDAVLNPGGVRIGTAEIYRQVEKVPQVQESLAIG---QRWQD 559
Cdd:PRK06839 362 DAteETIQDGWLCT-------GDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGrqhVKWGE 434
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 799207711 560 DVRVvlFVRLNDGVELdeaLEQQIRQVIRANTTPRHVPAKILAVTDIPRTISGKIVELAVRNV 622
Cdd:PRK06839 435 IPIA--FIVKKSSSVL---IEKDVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQLVNQ 492
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
83-335 |
1.37e-12 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 70.67 E-value: 1.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 83 PGATLNFAEHLLRRRDDHPAVVAISEDGQReqLTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTLVGMLATTSL 162
Cdd:PRK08279 33 PDSKRSLGDVFEEAAARHPDRPALLFEDQS--ISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 163 GAIwsCSSPDFGTQG--VIDRFGQIEPKVLITCAgyryagkdidqtaklnEILARLPSLEQLIIVPyarPQARVEDYQTH 240
Cdd:PRK08279 111 GAV--VALLNTQQRGavLAHSLNLVDAKHLIVGE----------------ELVEAFEEARADLARP---PRLWVAGGDTL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 241 ARVTRWSDF------YPPGGEPEFVAVPFDHPLYILYSSGTTGVPKciihgtgGVLLTH------LKEHGLHADLSRDDC 308
Cdd:PRK08279 170 DDPEGYEDLaaaaagAPTTNPASRSGVTAKDTAFYIYTSGTTGLPK-------AAVMSHmrwlkaMGGFGGLLRLTPDDV 242
|
250 260 270
....*....|....*....|....*....|..
gi 799207711 309 L-----FYYTTCGWMMWNwlvSVLAIGATAVL 335
Cdd:PRK08279 243 LycclpLYHNTGGTVAWS---SVLAAGATLAL 271
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
99-614 |
6.92e-12 |
|
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: 67.88 E-value: 6.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 99 DHPAVVaiseDGQReQLTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTLVGMLATTSLGAIWSCSSPDFgtqgv 178
Cdd:cd17650 2 DAIAVS----DATR-QLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDY----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 179 idrfgqiepkvlitcagyryagkdidqtaklneilarlpsleqliivPYARPQARVEDYQTHARVTrwsdfyppggEPEF 258
Cdd:cd17650 72 -----------------------------------------------PAERLQYMLEDSGAKLLLT----------QPED 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 259 VAvpfdhplYILYSSGTTGVPKciihgtgGVLLTHLKEHGLHADLSRDDCLFYYTTCGWMMWNWLVSVLAIGATAVLYDG 338
Cdd:cd17650 95 LA-------YVIYTSGTTGKPK-------GVMVEHRNVAHAAHAWRREYELDSFPVRLLQMASFSFDVFAGDFARSLLNG 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 339 SPFHPGPE-------RLIDLIDAEKISVFGTSPKF----LATLEKAGLqprlshDLGSLKGLISTGSPLSPQSYDYVYRE 407
Cdd:cd17650 161 GTLVICPDevkldpaALYDLILKSRITLMESTPALirpvMAYVYRNGL------DLSAMRLLIVGSDGCKAQDFKTLAAR 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 408 IKG-----------ELCLSS----MSGGTDIVSCFV-IGNPvLPvrrgemqckslAMAIEVWDDQGQPL-VGEKGEL--- 467
Cdd:cd17650 235 FGQgmriinsygvtEATIDStyyeEGRDPLGDSANVpIGRP-LP-----------NTAMYVLDERLQPQpVGVAGELyig 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 468 ---VCTrhfpampiGLWNDPDRQKLRASYFSQFPG--VWAQGDYAEQRPNGSLLIHGRSDAVLNPGGVRIGTAEIYRQVE 542
Cdd:cd17650 303 gagVAR--------GYLNRPELTAERFVENPFAPGerMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLA 374
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 799207711 543 KVPQVQESLAIGQrwQDD---VRVVLFVRLNDGV---ELDEALEQQIRQVIranttprhVPAKILAVTDIPRTISGKI 614
Cdd:cd17650 375 RHPAIDEAVVAVR--EDKggeARLCAYVVAAATLntaELRAFLAKELPSYM--------IPSYYVQLDALPLTPNGKV 442
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
95-614 |
1.20e-11 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 67.68 E-value: 1.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 95 RRRDDHPAVVAISEdgqreQLTYAEL---AEHVAG-LQkslRAAGVTQGDRVAACMPNTWQTLVGMLATTSLGAIWSCSS 170
Cdd:PRK08314 21 RRYPDKTAIVFYGR-----AISYRELleeAERLAGyLQ---QECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 171 PDFGTQgvidrfgqiEPKVLITCAGYRYA--GKDI-DQTAKLNEILArlpsLEQLIIVPYA---------------RPQA 232
Cdd:PRK08314 93 PMNREE---------ELAHYVTDSGARVAivGSELaPKVAPAVGNLR----LRHVIVAQYSdylpaepeiavpawlRAEP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 233 RVEDYQtHARVTRWSDFYPPGGEPEFVAVPFDHPLYILYSSGTTGVPKCIIHGTGGVLLTHLKEhGLHADLSRDDC---- 308
Cdd:PRK08314 160 PLQALA-PGGVVAWKEALAAGLAPPPHTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGS-VLWSNSTPESVvlav 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 309 --LFYYTTcgwmMWNWLVSVLAIGATAVL---YDgspfhpgPERLIDLIDAEKISVFGTSP----KFLAtlekaglQPRL 379
Cdd:PRK08314 238 lpLFHVTG----MVHSMNAPIYAGATVVLmprWD-------REAAARLIERYRVTHWTNIPtmvvDFLA-------SPGL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 380 -SHDLGSLKGLISTGSPLsPQSydyVYREIKGELCLSSMSG-G-TDIVScFVIGNpvlPVRRGEMQCkslaMAIEVWD-- 454
Cdd:PRK08314 300 aERDLSSLRYIGGGGAAM-PEA---VAERLKELTGLDYVEGyGlTETMA-QTHSN---PPDRPKLQC----LGIPTFGvd 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 455 ------DQGQPL-VGEKGELVCtrHFPAMPIGLWNDPDRQklrASYFSQFPG--VWAQGDYAEQRPNGSLLIHGRSDAVL 525
Cdd:PRK08314 368 arvidpETLEELpPGEVGEIVV--HGPQVFKGYWNRPEAT---AEAFIEIDGkrFFRTGDLGRMDEEGYFFITDRLKRMI 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 526 NPGGVRIGTAEIYRQVEKVPQVQESLAIGQRwqDDVR---VVLFVRLNDGVElDEALEQQIRQVIRANTTPRHVPAKILA 602
Cdd:PRK08314 443 NASGFKVWPAEVENLLYKHPAIQEACVIATP--DPRRgetVKAVVVLRPEAR-GKTTEEEIIAWAREHMAAYKYPRIVEF 519
|
570
....*....|..
gi 799207711 603 VTDIPRTISGKI 614
Cdd:PRK08314 520 VDSLPKSGSGKI 531
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
91-614 |
2.92e-11 |
|
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341299 [Multi-domain] Cd Length: 465 Bit Score: 65.92 E-value: 2.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 91 EHLLRRRDDHPAVVAisedgQREQLTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTLVGMLATTSLGAIWSCSS 170
Cdd:cd17644 7 EEQVERTPDAVAVVF-----EDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 171 PDFGTQgvidrfgqiepkvlitcagyryagkdidqtaKLNEILarlpsleqliivpyarpqarvEDYQTHARVTrwsdfy 250
Cdd:cd17644 82 PNYPQE-------------------------------RLTYIL---------------------EDAQISVLLT------ 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 251 ppggEPEFVAvpfdhplYILYSSGTTGVPKciihgtgGVLLTHLK----EHGLHADL---SRDDCLFYYTTCGWMMWNWL 323
Cdd:cd17644 104 ----QPENLA-------YVIYTSGSTGKPK-------GVMIEHQSlvnlSHGLIKEYgitSSDRVLQFASIAFDVAAEEI 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 324 VSVLAIGATAVLYDGSPFhPGPERLIDLIDAEKISVFGTSPKFLATLEKAGLQPRLSHDlGSLKGLISTGSPLSPQSYDy 403
Cdd:cd17644 166 YVTLLSGATLVLRPEEMR-SSLEDFVQYIQQWQLTVLSLPPAYWHLLVLELLLSTIDLP-SSLRLVIVGGEAVQPELVR- 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 404 VYREIKGEL--CLSSM--SGGTDIVSCFVIGNPVLPVRRGEMQCKSLA-MAIEVWDDQGQPL-VGEKGELvctrHFPAMP 477
Cdd:cd17644 243 QWQKNVGNFiqLINVYgpTEATIAATVCRLTQLTERNITSVPIGRPIAnTQVYILDENLQPVpVGVPGEL----HIGGVG 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 478 I--GLWNDPD--RQKLRASYFSQFPG--VWAQGDYAEQRPNGSLLIHGRSDAVLNPGGVRIGTAEIYRQVEKVPQVQESL 551
Cdd:cd17644 319 LarGYLNRPEltAEKFISHPFNSSESerLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAV 398
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 552 AIGQRWQ-DDVRVVLFV-----RLNDGVELDEALEQQIrqviranttPRH-VPAKILAVTDIPRTISGKI 614
Cdd:cd17644 399 VIVREDQpGNKRLVAYIvphyeESPSTVELRQFLKAKL---------PDYmIPSAFVVLEELPLTPNGKI 459
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
115-614 |
4.92e-11 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 65.49 E-value: 4.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 115 LTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTLVGMLATTSLGAIWSCSSPDFGTQGVIDRFGQIEPKVLITCA 194
Cdd:PRK12406 12 RSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAHA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 195 gyryagkDIdqtakLNEILARLPSLEQLIIVPyaRPQARVEDYqthaRVTRWSDFYPPG---------GEPEFVAVPFDH 265
Cdd:PRK12406 92 -------DL-----LHGLASALPAGVTVLSVP--TPPEIAAAY----RISPALLTPPAGaidwegwlaQQEPYDGPPVPQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 266 PLYILYSSGTTGVPKciihgtgGVLLTH-LKEHGLHADLSRDdclfyyttcgwmmwnwLVSVLAIGATAV----LYDGSP 340
Cdd:PRK12406 154 PQSMIYTSGTTGHPK-------GVRRAApTPEQAAAAEQMRA----------------LIYGLKPGIRALltgpLYHSAP 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 341 FHPG-----------------PERLIDLIDAEKISVFGTSPKFLATLEKAGLQPRLSHDLGSLKGLISTGSPLSpqsydy 403
Cdd:PRK12406 211 NAYGlragrlggvlvlqprfdPEELLQLIERHRITHMHMVPTMFIRLLKLPEEVRAKYDVSSLRHVIHAAAPCP------ 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 404 vyREIKGEL------CLSSMSGGTDI-VSCFVIGNPVLPvRRGEMQCKSLAMAIEVWDDQGQPL-VGEKGELVCtrHFPA 475
Cdd:PRK12406 285 --ADVKRAMiewwgpVIYEYYGSTESgAVTFATSEDALS-HPGTVGKAAPGAELRFVDEDGRPLpQGEIGEIYS--RIAG 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 476 MPIGLW-NDPD-RQKLRASyfsqfpGVWAQGDYAEQRPNGSLLIHGR-SDAVLNpGGVRIGTAEIYRQVEKVPQVQESLA 552
Cdd:PRK12406 360 NPDFTYhNKPEkRAEIDRG------GFITSGDVGYLDADGYLFLCDRkRDMVIS-GGVNIYPAEIEAVLHAVPGVHDCAV 432
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 799207711 553 IGQRWQD-DVRVVLFVRLNDGVELDEAleqQIRQVIRANTTPRHVPAKILAVTDIPRTISGKI 614
Cdd:PRK12406 433 FGIPDAEfGEALMAVVEPQPGATLDEA---DIRAQLKARLAGYKVPKHIEIMAELPREDSGKI 492
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
99-647 |
6.71e-11 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 65.44 E-value: 6.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 99 DHPAVVAisedgqREQLTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTLVGMLATTSLGAIWSCSSPDFGTQGv 178
Cdd:PRK06060 21 DRPAFYA------ADVVTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDD- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 179 idrfgqiepkvlitcagyrYAGKDIDQTAKLneILARLPSLEQLiivpyaRPQARVEDYQTHARVTRW--SDFYPPGGep 256
Cdd:PRK06060 94 -------------------HALAARNTEPAL--VVTSDALRDRF------QPSRVAEAAELMSEAARVapGGYEPMGG-- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 257 efvavpfDHPLYILYSSGTTGVPKCIIHGTGGVL--LTHLKEHGLH---ADLSRDDCLFYYttcGWMMWNWLVSVLAIGA 331
Cdd:PRK06060 145 -------DALAYATYTSGTTGPPKAAIHRHADPLtfVDAMCRKALRltpEDTGLCSARMYF---AYGLGNSVWFPLATGG 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 332 TAVLydgSPFHPGPERLIDLIDAEKISVFGTSPKFLATLEKAglqprLSHD-LGSLKGLISTGSPLSPQSYDYVYrEIKG 410
Cdd:PRK06060 215 SAVI---NSAPVTPEAAAILSARFGPSVLYGVPNFFARVIDS-----CSPDsFRSLRCVVSAGEALELGLAERLM-EFFG 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 411 ELCLSSMSGGTDIVSCFViGNPVLPVRRGEMQCKSLAMAIEVWDDQGQPlVGEKGELVCTRHFPAMPIGLWNDPDRQKLR 490
Cdd:PRK06060 286 GIPILDGIGSTEVGQTFV-SNRVDEWRLGTLGRVLPPYEIRVVAPDGTT-AGPGVEGDLWVRGPAIAKGYWNRPDSPVAN 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 491 ASYFSQFPGVWAQGDyaeqrpnGSLLIHGRSDAVLNPGGVRIGTAEIYRQVEKVPQVQESLAIGQRWQDDVRVV-LFVRL 569
Cdd:PRK06060 364 EGWLDTRDRVCIDSD-------GWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLqAFLVA 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 570 NDGVELDEALEQQIRQVIRANTTPRHVPAKILAVTDIPRTISGKIvelaVRNVVHGE-PVKNTDALANPQ----ALEQFR 644
Cdd:PRK06060 437 TSGATIDGSVMRDLHRGLLNRLSAFKVPHRFAVVDRLPRTPNGKL----VRGALRKQsPTKPIWELSLTEpgsgVRAQRD 512
|
...
gi 799207711 645 DRP 647
Cdd:PRK06060 513 DLS 515
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
94-622 |
1.27e-10 |
|
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341297 [Multi-domain] Cd Length: 532 Bit Score: 64.09 E-value: 1.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 94 LRRRDDHPAVVAISEDGQREQLTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTLVGMLATTSLGAIWSCSSPDF 173
Cdd:cd17642 24 MKRYASVPGTIAFTDAHTGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 174 GTQGVIDRFGQIEPKVLITcagyryAGKDIDQTAKlneILARLPSLEQLIIVpyarpqARVEDYQTHARVTRW-SDFYPP 252
Cdd:cd17642 104 NERELDHSLNISKPTIVFC------SKKGLQKVLN---VQKKLKIIKTIIIL------DSKEDYKGYQCLYTFiTQNLPP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 253 G-GEPEFVAVPFDHP---LYILYSSGTTGVPKCI--IHGTGGVLLTHLKEHGLHADLSRDDCL-----FYYttcGWMMWN 321
Cdd:cd17642 169 GfNEYDFKPPSFDRDeqvALIMNSSGSTGLPKGVqlTHKNIVARFSHARDPIFGNQIIPDTAIltvipFHH---GFGMFT 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 322 wLVSVLAIGATAVLydgspFHPGPERL-IDLIDAEKISVFGTSPKFLATLEKAGLQPRlsHDLGSLKGLISTGSPLSPQS 400
Cdd:cd17642 246 -TLGYLICGFRVVL-----MYKFEEELfLRSLQDYKVQSALLVPTLFAFFAKSTLVDK--YDLSNLHEIASGGAPLSKEV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 401 YDYVYREIKgelcLSSMSGG---TDIVSCFVIgNPVLPVRRGEMQCKSLAMAIEVWD-DQGQPL-VGEKGELvCTRHfPA 475
Cdd:cd17642 318 GEAVAKRFK----LPGIRQGyglTETTSAILI-TPEGDDKPGAVGKVVPFFYAKVVDlDTGKTLgPNERGEL-CVKG-PM 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 476 MPIGLWNDPDRQKLRASYfsqfPGVWAQGDYAEQRPNGSLLIHGRSDAVLNPGGVRIGTAEIYRQVEKVPQVQESLAIGQ 555
Cdd:cd17642 391 IMKGYVNNPEATKALIDK----DGWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGI 466
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 799207711 556 rwQDDVRVVL---FVRLNDGVELDealEQQIRQVIRANTTP-RHVPAKILAVTDIPRTISGKIVELAVRNV 622
Cdd:cd17642 467 --PDEDAGELpaaVVVLEAGKTMT---EKEVMDYVASQVSTaKRLRGGVKFVDEVPKGLTGKIDRRKIREI 532
|
|
| ACAS_N |
pfam16177 |
Acetyl-coenzyme A synthetase N-terminus; This domain is found at the N-terminus of many ... |
36-92 |
2.35e-10 |
|
Acetyl-coenzyme A synthetase N-terminus; This domain is found at the N-terminus of many acetyl-coenzyme A synthetase enzymes.
Pssm-ID: 465043 [Multi-domain] Cd Length: 55 Bit Score: 56.33 E-value: 2.35e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 799207711 36 YPALHQWSIDQRPDFWRAIVAFFDvqFRSPPSAVLiEDAEMPSAQWFPGATLNFAEH 92
Cdd:pfam16177 1 YEALYRRSIEDPEGFWGEVAKELD--WFKPFDKVL-DGSNGPFAKWFVGGKLNVCYN 54
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
114-614 |
4.24e-10 |
|
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: 62.11 E-value: 4.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 114 QLTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTLVGMLATTSLGAIWSCSSPdfgtqgvidrfgqiepkvlitc 193
Cdd:cd05935 1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINP---------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 194 agyryagkdIDQTAKLNEILArlpsleqliivpyarpqarveDYQTHARVTrwsdfyppGGEPEFVAVpfdhplyILYSS 273
Cdd:cd05935 59 ---------MLKERELEYILN---------------------DSGAKVAVV--------GSELDDLAL-------IPYTS 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 274 GTTGVPKCIIHGTGGVLLTHLKE----HGLHADLSRdDCLFYYTTCGwmMWNWLVSVLAIGATAVL---YDgspfhpgPE 346
Cdd:cd05935 94 GTTGLPKGCMHTHFSAAANALQSavwtGLTPSDVIL-ACLPLFHVTG--FVGSLNTAVYVGGTYVLmarWD-------RE 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 347 RLIDLIDAEKISVFGTSPKFLATL-EKAGLQPRlshDLGSLKGLISTGSPLSPQsydyVYREIKGELCLSSMS--GGTDI 423
Cdd:cd05935 164 TALELIEKYKVTFWTNIPTMLVDLlATPEFKTR---DLSSLKVLTGGGAPMPPA----VAEKLLKLTGLRFVEgyGLTET 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 424 VSCfVIGNPVLpvrRGEMQCKSLAM----AIEVWDDQGQPL-VGEKGELVCtrHFPAMPIGLWNdpdRQKLRASYFSQFP 498
Cdd:cd05935 237 MSQ-THTNPPL---RPKLQCLGIP*fgvdARVIDIETGRELpPNEVGEIVV--RGPQIFKGYWN---RPEETEESFIEIK 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 499 G--VWAQGDYAEQRPNGSLLIHGRSDAVLNPGGVRIGTAEIYRQVEKVPQVQESLAIG---QRWQDDVRVVLFVRLNDGV 573
Cdd:cd05935 308 GrrFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISvpdERVGEEVKAFIVLRPEYRG 387
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 799207711 574 ELDEA-LEQQIRQVIRANTTPRHVpakiLAVTDIPRTISGKI 614
Cdd:cd05935 388 KVTEEdIIEWAREQMAAYKYPREV----EFVDELPRSASGKI 425
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
95-614 |
5.02e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 62.13 E-value: 5.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 95 RRRDDHPAVVAISeDGQReqLTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTLVGMLATTSLGAI-----WSCS 169
Cdd:PRK09088 6 RLQPQRLAAVDLA-LGRR--WTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIyvplnWRLS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 170 SPDFgtQGVIDRfgqIEPKVLITCAGYRYAGkdidqtaklneilarlpsleqLIIVPYARPQARVEdyqtharvtrwsdf 249
Cdd:PRK09088 83 ASEL--DALLQD---AEPRLLLGDDAVAAGR---------------------TDVEDLAAFIASAD-------------- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 250 yppGGEPEFVA-VPFDHPLYILYSSGTTGVPKciihgtgGVLLTH------------LKEHGLHADLSRDDCLFYytTCG 316
Cdd:PRK09088 123 ---ALEPADTPsIPPERVSLILFTSGTSGQPK-------GVMLSErnlqqtahnfgvLGRVDAHSSFLCDAPMFH--IIG 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 317 wmMWNWLVSVLAIGATAVLYDGspFHPGPE--RLIDLidAEKISVFGTSPKFLATLEKaglQPRL-SHDLGSLKGLISTG 393
Cdd:PRK09088 191 --LITSVRPVLAVGGSILVSNG--FEPKRTlgRLGDP--ALGITHYFCVPQMAQAFRA---QPGFdAAALRHLTALFTGG 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 394 SPlspqsydYVYREIKGEL-------CLSSMS-GGTdivscfVIGNPVLPVR-RGEMQCKSLAMA---IEVWDDQGQPL- 460
Cdd:PRK09088 262 AP-------HAAEDILGWLddgipmvDGFGMSeAGT------VFGMSVDCDViRAKAGAAGIPTPtvqTRVVDDQGNDCp 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 461 VGEKGELVCTRhfPAMPIGLWNDPDRQklrASYFSQfPGVWAQGDYAEQRPNGSLLIHGRSDAVLNPGGVRIGTAEIYRQ 540
Cdd:PRK09088 329 AGVPGELLLRG--PNLSPGYWRRPQAT---ARAFTG-DGWFRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAV 402
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 799207711 541 VEKVPQVQESLAIG---QRWQDDVRVVLFVRLNDGVELDEALEQQIRQVIRANttprhVPAKILAVTDIPRTISGKI 614
Cdd:PRK09088 403 LADHPGIRECAVVGmadAQWGEVGYLAIVPADGAPLDLERIRSHLSTRLAKYK-----VPKHLRLVDALPRTASGKL 474
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
95-624 |
5.69e-10 |
|
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341242 [Multi-domain] Cd Length: 481 Bit Score: 62.17 E-value: 5.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 95 RRRDDHPAVVAisEDGQreqLTYAELAEHVAGLQKSLRAAGVTQGDRVAACM-PNTWqTLVGMLATTSLGAIWscsspdf 173
Cdd:cd05918 10 RSQPDAPAVCA--WDGS---LTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFeKSKW-AVVAMLAVLKAGGAF------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 174 gtqgvidrfgqiepkVLItcagyryagkDIDQtaklneilarlpsleqliivPYARPQARVEDyqTHARVtrwsdfyppg 253
Cdd:cd05918 77 ---------------VPL----------DPSH--------------------PLQRLQEILQD--TGAKV---------- 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 254 gepeFVAVPFDHPLYILYSSGTTGVPKciihgtgGVLLTH------LKEHGLHADLSRDD-CL-FY-YTtcgwmmwnWLV 324
Cdd:cd05918 100 ----VLTSSPSDAAYVIFTSGSTGKPK-------GVVIEHralstsALAHGRALGLTSESrVLqFAsYT--------FDV 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 325 SV------LAIGATAVLydgspfhpgP---ERLIDL---IDAEKISVFGTSPKFLATLEKAglqprlshDLGSLKGLIST 392
Cdd:cd05918 161 SIleifttLAAGGCLCI---------PseeDRLNDLagfINRLRVTWAFLTPSVARLLDPE--------DVPSLRTLVLG 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 393 GSPLSPQsydyVYREIKGELCLSSMSGGTDiVSCFVIGNPVLPvrrgEMQCKSL--AMAIEVW----DDQGQPL-VGEKG 465
Cdd:cd05918 224 GEALTQS----DVDTWADRVRLINAYGPAE-CTIAATVSPVVP----STDPRNIgrPLGATCWvvdpDNHDRLVpIGAVG 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 466 ELVCTRHFPAMpiGLWNDPDRQKLRasyFSQFPGVWAQ------------GDYAEQRPNGSLLIHGRSDAVLNPGGVRIG 533
Cdd:cd05918 295 ELLIEGPILAR--GYLNDPEKTAAA---FIEDPAWLKQegsgrgrrlyrtGDLVRYNPDGSLEYVGRKDTQVKIRGQRVE 369
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 534 TAEI----YRQVEKVPQVQESLAIGQRWQDDVRVVLFVRLNDG-----------VELDEALEQQIRQVIRA--NTTPRH- 595
Cdd:cd05918 370 LGEIehhlRQSLPGAKEVVVEVVKPKDGSSSPQLVAFVVLDGSssgsgdgdslfLEPSDEFRALVAELRSKlrQRLPSYm 449
|
570 580
....*....|....*....|....*....
gi 799207711 596 VPAKILAVTDIPRTISGKIVELAVRNVVH 624
Cdd:cd05918 450 VPSVFLPLSHLPLTASGKIDRRALRELAE 478
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
108-293 |
6.54e-10 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 62.11 E-value: 6.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 108 EDGQREQLTYAELAEHVAGLQKSLRAA-GVTQGDRVAACMPNTWQTLVGMLATTSLGAIWSCSSPDFGTQGVIDRFGQIE 186
Cdd:PRK05620 32 GGAEQEQTTFAAIGARAAALAHALHDElGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 187 PKVLItcAGYRYAGkdidqtaKLNEILARLPSLEQLIIV---------PYARPQARVEDYQT----HARVTRWSDfyppg 253
Cdd:PRK05620 112 DEVIV--ADPRLAE-------QLGEILKECPCVRAVVFIgpsdadsaaAHMPEGIKVYSYEAlldgRSTVYDWPE----- 177
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 799207711 254 gepefvaVPFDHPLYILYSSGTTGVPKciihgtgGVLLTH 293
Cdd:PRK05620 178 -------LDETTAAAICYSTGTTGAPK-------GVVYSH 203
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
266-612 |
8.11e-10 |
|
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341291 [Multi-domain] Cd Length: 331 Bit Score: 60.78 E-value: 8.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 266 PLYILYSSGTTGVPKciihgtgGVLLTH--LKEHGLHADLSRD-DCLFYYTTCGWM----MWNWLVSVLAIGATAVlydg 338
Cdd:cd17636 2 PVLAIYTAAFSGRPN-------GALLSHqaLLAQALVLAVLQAiDEGTVFLNSGPLfhigTLMFTLATFHAGGTNV---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 339 spFHP--GPERLIDLIDAEKIS---VFGTSPKFLATLEKAGLqprlsHDLGSL---------KGLIS-TGSPLSPQSYDY 403
Cdd:cd17636 71 --FVRrvDAEEVLELIEAERCThafLLPPTIDQIVELNADGL-----YDLSSLrsspaapewNDMATvDTSPWGRKPGGY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 404 VYREIKGELCLSSMSGGTdivscfvIGN-----PVLPVRrgemqckslamaieVWDDQGQPL-VGEKGElVCTRHFPAMP 477
Cdd:cd17636 144 GQTEVMGLATFAALGGGA-------IGGagrpsPLVQVR--------------ILDEDGREVpDGEVGE-IVARGPTVMA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 478 iGLWNDPD--RQKLRAsyfsqfpGVWAQGDYAEQRPNGSLLIHGRSDAVLNPGGVRIGTAEIYRQVEKVPQVQESLAIG- 554
Cdd:cd17636 202 -GYWNRPEvnARRTRG-------GWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGv 273
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 799207711 555 --QRWQDDVRVVlfVRLNDGVELDEA-LEQQIRQVIRANTTPRHVpakiLAVTDIPRTISG 612
Cdd:cd17636 274 pdPRWAQSVKAI--VVLKPGASVTEAeLIEHCRARIASYKKPKSV----EFADALPRTAGG 328
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
77-619 |
1.26e-09 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 61.06 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 77 PSAQWFPGATLNFAEHLLRRRDDHPAVVAISedgQREQLTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTLVGM 156
Cdd:PRK05852 9 PMASDFGPRIADLVEVAATRLPEAPALVVTA---DRIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 157 LATTSLGAIWSCSSPdfgtqgvidrfgqiepkvlitcagyryAGKDIDQTAKLNEILARLPSLEQLIIVPYARPQARVed 236
Cdd:PRK05852 86 LAASRADLVVVPLDP---------------------------ALPIAEQRVRSQAAGARVVLIDADGPHDRAEPTTRW-- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 237 YQTHARVTRwsDFYPPGGEPEF-----------VAVPF---DHPLYILYSSGTTGVPKcIIHGTGGVLLTHLkeHGLHA- 301
Cdd:PRK05852 137 WPLTVNVGG--DSGPSGGTLSVhldaateptpaTSTPEglrPDDAMIMFTGGTTGLPK-MVPWTHANIASSV--RAIITg 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 302 -DLSRDDCL-----FYYttcGWMMWNWLVSVLAIGATAVLydgspfhPGPERL--------IDLIDAEKISVFGTSPKFL 367
Cdd:PRK05852 212 yRLSPRDATvavmpLYH---GHGLIAALLATLASGGAVLL-------PARGRFsahtfwddIKAVGATWYTAVPTIHQIL 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 368 ATLEKAGLQPRLSHdlgSLKGLISTGSPLSPQSYDYVYREIKGE-LCLSSMSGGTDIVSCFVI---GNPVLPVRRGEMQC 443
Cdd:PRK05852 282 LERAATEPSGRKPA---ALRFIRSCSAPLTAETAQALQTEFAAPvVCAFGMTEATHQVTTTQIegiGQTENPVVSTGLVG 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 444 KSLAMAIEVWDDQGQPL-VGEKGELVCtrHFPAMPIGLWNDPdrqKLRASYFSQfpGVWAQGDYAEQRPNGSLLIHGRSD 522
Cdd:PRK05852 359 RSTGAQIRIVGSDGLPLpAGAVGEVWL--RGTTVVRGYLGDP---TITAANFTD--GWLRTGDLGSLSAAGDLSIRGRIK 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 523 AVLNPGGVRIGTAEIYRQVEKVPQVQESLAIG---QRWQDDVRVVLFVRLNDGVELDEALEQqirqvIRANTTPRHVPAK 599
Cdd:PRK05852 432 ELINRGGEKISPERVEGVLASHPNVMEAAVFGvpdQLYGEAVAAVIVPRESAPPTAEELVQF-----CRERLAAFEIPAS 506
|
570 580
....*....|....*....|
gi 799207711 600 ILAVTDIPRTISGKIVELAV 619
Cdd:PRK05852 507 FQEASGLPHTAKGSLDRRAV 526
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
103-620 |
1.95e-09 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 60.54 E-value: 1.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 103 VVAISEDGQREQLTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTLVGMLATTSLGAIWSCSSPDFGTQGVIDRF 182
Cdd:PRK06018 28 VVTRSVEGPIVRTTYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWII 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 183 GQIEPKVLITcagyryagkDIDQTAKLNEILARLPSLEQLIIVPYAR--PQARV------EDYQTHARVT-RWSDFyppg 253
Cdd:PRK06018 108 NHAEDRVVIT---------DLTFVPILEKIADKLPSVERYVVLTDAAhmPQTTLknavayEEWIAEADGDfAWKTF---- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 254 gePEFVAVPfdhplyILYSSGTTGVPKciihgtgGVLLTHlKEHGLHADL----------SRDDCL-----FYYTTcgwm 318
Cdd:PRK06018 175 --DENTAAG------MCYTSGTTGDPK-------GVLYSH-RSNVLHALManngdalgtsAADTMLpvvplFHANS---- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 319 mWNWLVSVLAIGATAVLydgspfhPGPE----RLIDLIDAEKISVFGTSPK----FLATLEKAGLQprlshdLGSLKGLI 390
Cdd:PRK06018 235 -WGIAFSAPSMGTKLVM-------PGAKldgaSVYELLDTEKVTFTAGVPTvwlmLLQYMEKEGLK------LPHLKMVV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 391 STGSPLsPQSYDYVYREIKGELC----LSSMSG-GTdivscfvignpvLPVRRGEMQCKSLAMAIEVWDDQGQP------ 459
Cdd:PRK06018 301 CGGSAM-PRSMIKAFEDMGVEVRhawgMTEMSPlGT------------LAALKPPFSKLPGDARLDVLQKQGYPpfgvem 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 460 -LVGEKGElvctrhfpAMPiglW--NDPDRQKLR-----ASYFS------QFPGVWAQGDYAEQRPNGSLLIHGRSDAVL 525
Cdd:PRK06018 368 kITDDAGK--------ELP---WdgKTFGRLKVRgpavaAAYYRvdgeilDDDGFFDTGDVATIDAYGYMRITDRSKDVI 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 526 NPGGVRIGTAEIYRQVEKVPQVQESLAIGQ---RWqdDVRVVLFVRLNDGVeldEALEQQIRQVIRANTTPRHVPAKILA 602
Cdd:PRK06018 437 KSGGEWISSIDLENLAVGHPKVAEAAVIGVyhpKW--DERPLLIVQLKPGE---TATREEILKYMDGKIAKWWMPDDVAF 511
|
570
....*....|....*...
gi 799207711 603 VTDIPRTISGKIVELAVR 620
Cdd:PRK06018 512 VDAIPHTATGKILKTALR 529
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
66-620 |
5.45e-09 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 59.00 E-value: 5.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 66 PSAVLIEDAEMPSAQWFPGatlnfaehLLRRRDDH-PAVVAISEDGQReqLTYAELAEHVAGLQKSLRAAGVTQGDRVAA 144
Cdd:PRK06155 7 GLAARAVDPLPPSERTLPA--------MLARQAERyPDRPLLVFGGTR--WTYAEAARAAAAAAHALAAAGVKRGDRVAL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 145 CMPNTWQTLVGMLATTSLGAIWSCSSPDFGTQGVIDRFGQIEPKVLITCAGYryagkdidqTAKLNEILARLPSLEQLII 224
Cdd:PRK06155 77 MCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLVVEAAL---------LAALEAADPGDLPLPAVWL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 225 VPyARPQARVEdyqtharvTRWSDF-YPPGGEP-EFVAVPFDHPLYILYSSGTTGVPKciihgtgGVLLTHLKEH--GLH 300
Cdd:PRK06155 148 LD-APASVSVP--------AGWSTApLPPLDAPaPAAAVQPGDTAAILYTSGTTGPSK-------GVCCPHAQFYwwGRN 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 301 A----DLSRDDCLF-----YYTTCgwmmWNWLVSVLAIGATAVLydGSPFhpGPERLIDLIDAEKISVFGTSPKFLATLE 371
Cdd:PRK06155 212 SaedlEIGADDVLYttlplFHTNA----LNAFFQALLAGATYVL--EPRF--SASGFWPAVRRHGATVTYLLGAMVSILL 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 372 KaglQPRLSHDLGS-LKGLISTGSPlsPQSYDyVYREIKGeLCLSSMSGGTDivSCFVIGNPVLPVRRGEMQCKSLAMAI 450
Cdd:PRK06155 284 S---QPARESDRAHrVRVALGPGVP--AALHA-AFRERFG-VDLLDGYGSTE--TNFVIAVTHGSQRPGSMGRLAPGFEA 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 451 EVWDDQGQPL-VGEKGELVCTRHFP-AMPIGLWNDPDR--QKLRASYFSqfpgvwaQGDYAEQRPNGSLLIHGRSDAVLN 526
Cdd:PRK06155 355 RVVDEHDQELpDGEPGELLLRADEPfAFATGYFGMPEKtvEAWRNLWFH-------TGDRVVRDADGWFRFVDRIKDAIR 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 527 PGGVRIGTAEIYRQVEKVPQVQESLAIGQRWQ---DDVRVVLFVRlnDGVELDEAleqqirQVIRaNTTPR----HVPAK 599
Cdd:PRK06155 428 RRGENISSFEVEQVLLSHPAVAAAAVFPVPSElgeDEVMAAVVLR--DGTALEPV------ALVR-HCEPRlayfAVPRY 498
|
570 580
....*....|....*....|.
gi 799207711 600 ILAVTDIPRTISGKIVELAVR 620
Cdd:PRK06155 499 VEFVAALPKTENGKVQKFVLR 519
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
99-621 |
6.87e-09 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.
Pssm-ID: 341283 [Multi-domain] Cd Length: 486 Bit Score: 58.46 E-value: 6.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 99 DHPAVVaiseDGQReQLTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTwqtlvgmlattslgaiwscsspdfgtqgv 178
Cdd:cd12118 19 DRTSIV----YGDR-RYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNT----------------------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 179 idrfgqiePKVLITCAGYRYAGkdidqtAKLNEILARLPSLEQLIIVPYARPQARVEDYQ--THARVTRwsdfyppgGEP 256
Cdd:cd12118 65 --------PAMYELHFGVPMAG------AVLNALNTRLDAEEIAFILRHSEAKVLFVDREfeYEDLLAE--------GDP 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 257 EFVAVPFD---HPLYILYSSGTTGVPKCIIHGTGGVLLTHLkEHGLHADLsRDDCLFYYT-----TCGW-MMWnwlvSVL 327
Cdd:cd12118 123 DFEWIPPAdewDPIALNYTSGTTGRPKGVVYHHRGAYLNAL-ANILEWEM-KQHPVYLWTlpmfhCNGWcFPW----TVA 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 328 AIGATAVLYDgspfHPGPERLIDLIDAEKISVFGTSPKFLATLEKAGlqprlSHDLGSLKGLIST---GSPLSPQSYDYV 404
Cdd:cd12118 197 AVGGTNVCLR----KVDAKAIYDLIEKHKVTHFCGAPTVLNMLANAP-----PSDARPLPHRVHVmtaGAPPPAAVLAKM 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 405 yREIKGELC----LSSMSGgtDIVSCfvIGNP---VLPV-RRGEMQCKS-----LAMAIEVWDDQGQPLV---GEK-GEL 467
Cdd:cd12118 268 -EELGFDVThvygLTETYG--PATVC--AWKPewdELPTeERARLKARQgvryvGLEEVDVLDPETMKPVprdGKTiGEI 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 468 VCTRHfpAMPIGLWNDPD--RQKLRASYFSQfpgvwaqGDYAEQRPNGSLLIHGRSDAVLNPGGVRIGTAEIYRQVEKVP 545
Cdd:cd12118 343 VFRGN--IVMKGYLKNPEatAEAFRGGWFHS-------GDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHP 413
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 799207711 546 QVQESLAIGQ---RWQDdvRVVLFVRLNDGVeldEALEQQIRQVIRANTTPRHVPaKILAVTDIPRTISGKIVELAVRN 621
Cdd:cd12118 414 AVLEAAVVARpdeKWGE--VPCAFVELKEGA---KVTEEEIIAFCREHLAGFMVP-KTVVFGELPKTSTGKIQKFVLRD 486
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
255-614 |
6.89e-09 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341309 [Multi-domain] Cd Length: 449 Bit Score: 58.64 E-value: 6.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 255 EPEFVAVPFDHPL-YILYSSGTTGVPKCIIHGTGGVL--LTHLKehgLHADLSRDDCLFYYTtcgwmMWNWLVSVLAI-- 329
Cdd:cd17654 108 EHRHFNIRTDECLaYVIHTSGTTGTPKIVAVPHKCILpnIQHFR---SLFNITSEDILFLTS-----PLTFDPSVVEIfl 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 330 ----GATaVLYDGSPFHPGPERLIDLIDAE-KISVFGTSPKFLATLEKAGLQPRLSHDLGSLKGLISTGSPLSPQSYDYV 404
Cdd:cd17654 180 slssGAT-LLIVPTSVKVLPSKLADILFKRhRITVLQATPTLFRRFGSQSIKSTVLSATSSLRVLALGGEPFPSLVILSS 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 405 YREIKGELCLSSMSGGTDiVSCFVIGNPV----LPVRRGEmqcKSLAMAIEVWDDQGQPLVGE-KGELVCTRhfpampiG 479
Cdd:cd17654 259 WRGKGNRTRIFNIYGITE-VSCWALAYKVpeedSPVQLGS---PLLGTVIEVRDQNGSEGTGQvFLGGLNRV-------C 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 480 LWNDPDRQKLRASYfsqfpgvwAQGDYAeQRPNGSLLIHGRSDAVLNPGGVRIGTAEIYRQVEKVPQVQeslAIGQRWQD 559
Cdd:cd17654 328 ILDDEVTVPKGTMR--------ATGDFV-TVKDGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGVE---SCAVTLSD 395
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 799207711 560 DVRVVLFVRLndgvELDEALEQQIRQVIRANTTprHVPAKILAVTDIPRTISGKI 614
Cdd:cd17654 396 QQRLIAFIVG----ESSSSRIHKELQLTLLSSH--AIPDTFVQIDKLPLTSHGKV 444
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
109-614 |
7.52e-09 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341240 [Multi-domain] Cd Length: 463 Bit Score: 58.61 E-value: 7.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 109 DGQREQLTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTLVGMLATTSLGAIWSCSSPDFGTQGVIDRFGQIEPK 188
Cdd:cd05914 2 YYGGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 189 VLITcagyryagkdidqtaklneilarlpsleqliivpyarpqarvedyqtharvtrwsdfyppgGEPEFVAVpfdhply 268
Cdd:cd05914 82 AIFV-------------------------------------------------------------SDEDDVAL------- 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 269 ILYSSGTTGVPKciihgtgGVLLTH---------LKEHGLHADLSRDDCLFYYTTCGWMMWNWLVSVLAiGATAVLYDGS 339
Cdd:cd05914 94 INYTSGTTGNSK-------GVMLTYrnivsnvdgVKEVVLLGKGDKILSILPLHHIYPLTFTLLLPLLN-GAHVVFLDKI 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 340 pfhpgPERLIDLIDAEKISVFGTSPKFLATLEKA--GLQPRLS-------------------------HDL--GSLKGLI 390
Cdd:cd05914 166 -----PSAKIIALAFAQVTPTLGVPVPLVIEKIFkmDIIPKLTlkkfkfklakkinnrkirklafkkvHEAfgGNIKEFV 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 391 STGSPLSPQSYDYvYREIKGELCLS-SMSGGTDIVScfviGNPvlpvrRGEMQCKSLAMAI---EVWDDQGQPLVGEkGE 466
Cdd:cd05914 241 IGGAKINPDVEEF-LRTIGFPYTIGyGMTETAPIIS----YSP-----PNRIRLGSAGKVIdgvEVRIDSPDPATGE-GE 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 467 LVCTRhfPAMPIGLWNDPDrqkLRASYFSQfPGVWAQGDYAEQRPNGSLLIHGRS-DAVLNPGGVRIGTAEIYRQVEKVP 545
Cdd:cd05914 310 IIVRG--PNVMKGYYKNPE---ATAEAFDK-DGWFHTGDLGKIDAEGYLYIRGRKkEMIVLSSGKNIYPEEIEAKINNMP 383
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 546 QVQESLAIGQRWQDDVRVVLFvrlndgVELDEALEQQIRQVIRA------NTTPRHVP--AKILAV----TDIPRTISGK 613
Cdd:cd05914 384 FVLESLVVVQEKKLVALAYID------PDFLDVKALKQRNIIDAikwevrDKVNQKVPnyKKISKVkivkEEFEKTPKGK 457
|
.
gi 799207711 614 I 614
Cdd:cd05914 458 I 458
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
504-621 |
1.12e-08 |
|
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: 57.34 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 504 GDYAEQRPNGSLLIHGRSDAVLNPGGVRIGTAEIYRQVEKVPQVQESLAIGQ---RWQDdvRVVLFVRLNDGVELDEaLE 580
Cdd:cd17630 210 KDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVpdeELGQ--RPVAVIVGRGPADPAE-LR 286
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 799207711 581 QQIRQVIRANTTPRHvpakILAVTDIPRTISGKIVELAVRN 621
Cdd:cd17630 287 AWLKDKLARFKLPKR----IYPVPELPRTGGGKVDRRALRA 323
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
95-621 |
1.19e-08 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 57.85 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 95 RRRDDHPAVVAISEdgqreQLTYAELAE----HVAGLQKSlraAGVTQGDRVAACMPNTWQTLVGMLATTSLGAIWSCSS 170
Cdd:PRK05677 35 QRFADKPAFSNLGK-----TLTYGELYKlsgaFAAWLQQH---TDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVNTN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 171 PDFGTQGVIDRFGQIEPKVLITCAGYRY-AGKDIDQTAK----LNEILARLPSLEQLII----------VP-YARPQA-R 233
Cdd:PRK05677 107 PLYTAREMEHQFNDSGAKALVCLANMAHlAEKVLPKTGVkhviVTEVADMLPPLKRLLInavvkhvkkmVPaYHLPQAvK 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 234 VEDYQTHARVTRWSDFYPPGGEpefVAVpfdhplyILYSSGTTGVPKciihgtgGVLLTH-------LKEHGLHADLSRD 306
Cdd:PRK05677 187 FNDALAKGAGQPVTEANPQADD---VAV-------LQYTGGTTGVAK-------GAMLTHrnlvanmLQCRALMGSNLNE 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 307 DC-----------LFYYT-TCGWMMwnwlvsvlAIGATAVLYDGSPFHPGperLIDLIDAEKISVF-GTSPKFLATLEKA 373
Cdd:PRK05677 250 GCeiliaplplyhIYAFTfHCMAMM--------LIGNHNILISNPRDLPA---MVKELGKWKFSGFvGLNTLFVALCNNE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 374 GLQprlSHDLGSLKGLISTGSPLSpQSYDYVYREIKGelCLSSMSGGTDIVSCFVIGNPVLPVRRGEMQCKSLAMAIEVW 453
Cdd:PRK05677 319 AFR---KLDFSALKLTLSGGMALQ-LATAERWKEVTG--CAICEGYGMTETSPVVSVNPSQAIQVGTIGIPVPSTLCKVI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 454 DDQGQPL-VGEKGELvCTRHfPAMPIGLWNDPD-RQKLRASyfsqfPGVWAQGDYAEQRPNGSLLIHGRSDAVLNPGGVR 531
Cdd:PRK05677 393 DDDGNELpLGEVGEL-CVKG-PQVMKGYWQRPEaTDEILDS-----DGWLKTGDIALIQEDGYMRIVDRKKDMILVSGFN 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 532 IGTAEIYRQVEKVPQVQESLAIG---QRWQDDVRVVLFVRLNDGVEldealEQQIRQVIRANTTPRHVPAKILAVTDIPR 608
Cdd:PRK05677 466 VYPNELEDVLAALPGVLQCAAIGvpdEKSGEAIKVFVVVKPGETLT-----KEQVMEHMRANLTGYKVPKAVEFRDELPT 540
|
570
....*....|...
gi 799207711 609 TISGKIVELAVRN 621
Cdd:PRK05677 541 TNVGKILRRELRD 553
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
114-620 |
1.84e-08 |
|
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: 57.44 E-value: 1.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 114 QLTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTLVGMLATTSLGAIWSCSSPDFGTQGVIDRFGQIEPKVLITc 193
Cdd:cd05915 24 RTTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVLLF- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 194 agyryagkDIDQTAKLNEILARLPSleqliIVPYARPQARVEDYQtharvtrwsDFYPPGgEPEFVAV-PFDH--PLYIL 270
Cdd:cd05915 103 --------DPNLLPLVEAIRGELKT-----VQHFVVMDEKAPEGY---------LAYEEA-LGEEADPvRVPEraACGMA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 271 YSSGTTGVPKCIIHGTGGVLLtHLKEHGLHADLSRDDCLFYYTTCGWMM---WNWLVSVLAIGATAVLYDGSpfhPGPER 347
Cdd:cd05915 160 YTTGTTGLPKGVVYSHRALVL-HSLAASLVDGTALSEKDVVLPVVPMFHvnaWCLPYAATLVGAKQVLPGPR---LDPAS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 348 LIDLIDAEKISVFGTSPKFLATLEKAglQPRLSHDLGSLKGLISTGSplSPQSYDYVYREIkGELCLSSMSGGTDI---- 423
Cdd:cd05915 236 LVELFDGEGVTFTAGVPTVWLALADY--LESTGHRLKTLRRLVVGGS--AAPRSLIARFER-MGVEVRQGYGLTETspvv 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 424 VSCFVIGN-PVLPvRRGEMQCKS------LAMAIEVWD--DQGQPLVGEKGELVCTRHFPAMPiGLWNDPDRQKLRAsyf 494
Cdd:cd05915 311 VQNFVKSHlESLS-EEEKLTLKAktglpiPLVRLRVADeeGRPVPKDGKALGEVQLKGPWITG-GYYGNEEATRSAL--- 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 495 sqFPGVWAQG-DYAEQRPNGSLLIHGRSDAVLNPGGVRIGTAEIYRQVEKVPQVQESLAIGQrwQDDV---RVVLFVRLN 570
Cdd:cd05915 386 --TPDGFFRTgDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAI--PHPKwqeRPLAVVVPR 461
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 799207711 571 DGveldEALEQQIRQVI-RANTTPRHVPAKILAVTDIPRTISGKIVELAVR 620
Cdd:cd05915 462 GE----KPTPEELNEHLlKAGFAKWQLPDAYVFAEEIPRTSAGKFLKRALR 508
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
245-620 |
2.09e-08 |
|
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: 57.00 E-value: 2.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 245 RWSDFYP-PGGEPEFVAVPFDHPLYILYSSGTTGVPKCIIHGTGGVLLT--HLKEHGLHADLSRDDC------LFYYTTC 315
Cdd:cd05929 105 GLEDYEAaEGGSPETPIEDEAAGWKMLYSGGTTGRPKGIKRGLPGGPPDndTLMAAALGFGPGADSVylspapLYHAAPF 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 316 GWMMwnwlvSVLAIGATAVLYDgspfHPGPERLIDLIDAEKISVFGTSPKFLATLEKAGLQPRLSHDLGSLKGLISTGSP 395
Cdd:cd05929 185 RWSM-----TALFMGGTLVLME----KFDPEEFLRLIERYRVTFAQFVPTMFVRLLKLPEAVRNAYDLSSLKRVIHAAAP 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 396 LSPQSYDyvyREIK--GELCLSSMSGGTDIVSCFV-----------IGNPVLpvrrGEMQckslamaieVWDDQGQPL-V 461
Cdd:cd05929 256 CPPWVKE---QWIDwgGPIIWEYYGGTEGQGLTIIngeewlthpgsVGRAVL----GKVH---------ILDEDGNEVpP 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 462 GEKGELVCTrhfPAMPIGLWNDPDRQKLRASyfsqfPGVWAQ-GDYAEQRPNGSLLIHGRSDAVLNPGGVRIGTAEIYRQ 540
Cdd:cd05929 320 GEIGEVYFA---NGPGFEYTNDPEKTAAARN-----EGGWSTlGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENA 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 541 VEKVPQVQESLAIGQRWQD-DVRVVLFVRLNDGVELDEALEQQIRQVIRANTTPRHVPAKILAVTDIPRTISGKIVELAV 619
Cdd:cd05929 392 LIAHPKVLDAAVVGVPDEElGQRVHAVVQPAPGADAGTALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLL 471
|
.
gi 799207711 620 R 620
Cdd:cd05929 472 R 472
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
99-614 |
2.90e-08 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 56.51 E-value: 2.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 99 DHPAVVAisedgQREQLTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTLVGMLATTSLGAI-----WSCSSPDF 173
Cdd:PRK03640 17 DRTAIEF-----EEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVavllnTRLSREEL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 174 GTQgvidrFGQIEPKVLITCAGyrYAGKD-IDQTAKLNEilarlpsleqLIIVPYaRPQARVEDYqtharvtrwsdfypp 252
Cdd:PRK03640 92 LWQ-----LDDAEVKCLITDDD--FEAKLiPGISVKFAE----------LMNGPK-EEAEIQEEF--------------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 253 ggepefvavPFDHPLYILYSSGTTGVPKciihgtgGVLLTHlKEH-----------GLHAdlsrDDClfyyttcgwmmwn 321
Cdd:PRK03640 139 ---------DLDEVATIMYTSGTTGKPK-------GVIQTY-GNHwwsavgsalnlGLTE----DDC------------- 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 322 WL-------VSVLAI-------GATAVLYDgspfHPGPERLIDLIDAEKISVFGTSPKFLATLeKAGLQPRLSHDlgSLK 387
Cdd:PRK03640 185 WLaavpifhISGLSIlmrsviyGMRVVLVE----KFDAEKINKLLQTGGVTIISVVSTMLQRL-LERLGEGTYPS--SFR 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 388 GLISTGSPLSP--------------QSYDYVyrEIKGELC-LSSMSGGTDIVScfvIGNPVLPVRrgemqckslamaIEV 452
Cdd:PRK03640 258 CMLLGGGPAPKplleqckekgipvyQSYGMT--ETASQIVtLSPEDALTKLGS---AGKPLFPCE------------LKI 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 453 WDDQGQPLVGEKGELVCTRhfPAMPIGLWNDPDrqKLRASyfsqFPGVWAQ-GDYAEQRPNGSLLIHGRSDAVLNPGGVR 531
Cdd:PRK03640 321 EKDGVVVPPFEEGEIVVKG--PNVTKGYLNRED--ATRET----FQDGWFKtGDIGYLDEEGFLYVLDRRSDLIISGGEN 392
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 532 IGTAEIYRQVEKVPQVQESLAIG---QRWqDDVRVVLFVRlndGVELDEAleqQIRQVIRANTTPRHVPAKILAVTDIPR 608
Cdd:PRK03640 393 IYPAEIEEVLLSHPGVAEAGVVGvpdDKW-GQVPVAFVVK---SGEVTEE---ELRHFCEEKLAKYKVPKRFYFVEELPR 465
|
....*.
gi 799207711 609 TISGKI 614
Cdd:PRK03640 466 NASGKL 471
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
116-319 |
5.59e-08 |
|
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: 55.89 E-value: 5.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 116 TYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTLVGMLATTSLGAIwscSSPDFgtQGVIDRfgqiEPKVLITCAG 195
Cdd:cd17641 13 TWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGAL---SLGIY--QDSMAE----EVAYLLNYTG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 196 YRYA-GKDIDQTAKLNEILARLPSLEQLIIVP------YARPQ-ARVEDYQTHARVTRWSDfyPPGGEPEFVAVPFDHPL 267
Cdd:cd17641 84 ARVViAEDEEQVDKLLEIADRIPSVRYVIYCDprgmrkYDDPRlISFEDVVALGRALDRRD--PGLYEREVAAGKGEDVA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 799207711 268 YILYSSGTTGVPKciihgtgGVLLTH--LKEHG---LHAD-LSRDDCLFYYTTCGWMM 319
Cdd:cd17641 162 VLCTTSGTTGKPK-------LAMLSHgnFLGHCaayLAADpLGPGDEYVSVLPLPWIG 212
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
108-367 |
7.58e-08 |
|
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: 55.42 E-value: 7.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 108 EDGQREQLTYAELAEHVAGLQKSLRAaGVTQGDRVAACMPNTWQTLVGMLATTSLGAI-----WSCSSpdfgtQGVIDRF 182
Cdd:cd05909 1 EDTLGTSLTYRKLLTGAIALARKLAK-MTKEGENVGVMLPPSAGGALANFALALSGKVpvmlnYTAGL-----RELRACI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 183 GQIEPKVLITCAGYRYAGK-----DIDQTAK---LNEILARLPSLEQLIIVPYARPQARVEDYQtharvtrwsdFYPPGG 254
Cdd:cd05909 75 KLAGIKTVLTSKQFIEKLKlhhlfDVEYDARivyLEDLRAKISKADKCKAFLAGKFPPKWLLRI----------FGVAPV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 255 EPEFVAVpfdhplyILYSSGTTGVPKciihgtgGVLLTHlkeHGL---------HADLSRDDCL---------FYYTTCG 316
Cdd:cd05909 145 QPDDPAV-------ILFTSGSEGLPK-------GVVLSH---KNLlanveqitaIFDPNPEDVVfgalpffhsFGLTGCL 207
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 799207711 317 WMMwnwlvsvLAIGATAVLYDgSPFHpgPERLIDLIDAEKISVFGTSPKFL 367
Cdd:cd05909 208 WLP-------LLSGIKVVFHP-NPLD--YKKIPELIYDKKATILLGTPTFL 248
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
97-402 |
9.05e-08 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 55.23 E-value: 9.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 97 RDDHPAVVAISEDGQREQLTYAELAEHVAGLQKSL-RAAGVTQGDRVAACMPNTWQTLVGMLATTSLGAIWSCSSPdfgt 175
Cdd:PLN02574 49 HHNHNGDTALIDSSTGFSISYSELQPLVKSMAAGLyHVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNP---- 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 176 qgvIDRFGQIEPKVLITCAGYRYAGKdidqtaklnEILARLPSLE-QLIIVPyarpqarvEDYQTHARVTRWSDFYPP-G 253
Cdd:PLN02574 125 ---SSSLGEIKKRVVDCSVGLAFTSP---------ENVEKLSPLGvPVIGVP--------ENYDFDSKRIEFPKFYELiK 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 254 GEPEFVAVPF---DHPLYILYSSGTTGVPKciihgtgGVLLTHLK-----------EHGLHADLSRDD----CLFYYTTC 315
Cdd:PLN02574 185 EDFDFVPKPVikqDDVAAIMYSSGTTGASK-------GVVLTHRNliamvelfvrfEASQYEYPGSDNvylaALPMFHIY 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 316 GWMMwnWLVSVLAIGATAVL---YDGSpfhpgpeRLIDLIDAEKISVFGTSPKFLATLEKAGlQPRLSHDLGSLKGLIST 392
Cdd:PLN02574 258 GLSL--FVVGLLSLGSTIVVmrrFDAS-------DMVKVIDRFKVTHFPVVPPILMALTKKA-KGVCGEVLKSLKQVSCG 327
|
330
....*....|
gi 799207711 393 GSPLSPQSYD 402
Cdd:PLN02574 328 AAPLSGKFIQ 337
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
451-614 |
1.21e-07 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 54.69 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 451 EVWDDQGQPL-VGEKGELvCTRHFPAMPI--GLWNDPDRQklrASYFSqfPGVWAQ-GDYAEQRPNGSLLIHGRSDAVLN 526
Cdd:PRK08008 352 EIRDDHNRPLpAGEIGEI-CIKGVPGKTIfkEYYLDPKAT---AKVLE--ADGWLHtGDTGYVDEEGFFYFVDRRCNMIK 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 527 PGGVRIGTAEIYRQVEKVPQVQESLAIGQRwqDDVR---VVLFVRLNDGVELDEaleQQIRQVIRANTTPRHVPAKILAV 603
Cdd:PRK08008 426 RGGENVSCVELENIIATHPKIQDIVVVGIK--DSIRdeaIKAFVVLNEGETLSE---EEFFAFCEQNMAKFKVPSYLEIR 500
|
170
....*....|.
gi 799207711 604 TDIPRTISGKI 614
Cdd:PRK08008 501 KDLPRNCSGKI 511
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
266-614 |
2.18e-07 |
|
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: 53.43 E-value: 2.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 266 PLYILYSSGTTGVPKciihgtgGVLLTH-----LKEHGLHA-DLSRDDC------LFYYTTCGWMMwnwlvSVLAIGATA 333
Cdd:cd17637 2 PFVIIHTAAVAGRPR-------GAVLSHgnliaANLQLIHAmGLTEADVylnmlpLFHIAGLNLAL-----ATFHAGGAN 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 334 VL---YDgspfhpgPERLIDLIDAEKISVFGTSPKFLAT-LEKAGLQPRlshDLGSLKGLISTGSPLSPQSYdyvyrEIK 409
Cdd:cd17637 70 VVmekFD-------PAEALELIEEEKVTLMGSFPPILSNlLDAAEKSGV---DLSSLRHVLGLDAPETIQRF-----EET 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 410 GELCLSSMSGGTDiVSCFVIGNPVLPvRRGEMQCKSLAMAIEVWDDQGQPL-VGEKGELVCTRhfPAMPIGLWNDPDrqk 488
Cdd:cd17637 135 TGATFWSLYGQTE-TSGLVTLSPYRE-RPGSAGRPGPLVRVRIVDDNDRPVpAGETGEIVVRG--PLVFQGYWNLPE--- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 489 lrASYFSqFPGVWAQ-GDYAEQRPNGSLLIHGRSDA--VLNPGGVRIGTAEiyrqVEKV----PQVQESLAIG---QRWQ 558
Cdd:cd17637 208 --LTAYT-FRNGWHHtGDLGRFDEDGYLWYAGRKPEkeLIKPGGENVYPAE----VEKVilehPAIAEVCVIGvpdPKWG 280
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 799207711 559 DDVRVVlfVRLNDGVEL-DEALEQQIRQVIRANTTPRHVpakiLAVTDIPRTISGKI 614
Cdd:cd17637 281 EGIKAV--CVLKPGATLtADELIEFVGSRIARYKKPRYV----VFVEALPKTADGSI 331
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
89-366 |
3.43e-07 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 54.02 E-value: 3.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 89 FAEHLLRRrddhPAVVAISEDGQreQLTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTLVGMLATTSLGAIWSC 168
Cdd:PRK05691 2194 FAAQAART----PQAPALTFAGQ--TLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVP 2267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 169 SSPDFGtqgvIDRFG-QIEPKVLITCAGYRyagkdidqtaKLNEILARLPsleqliivpyarpqarvedyqthARVTRWS 247
Cdd:PRK05691 2268 LDPEYP----LERLHyMIEDSGIGLLLSDR----------ALFEALGELP-----------------------AGVARWC 2310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 248 --------DFYPPGgEPEFVAVPfDHPLYILYSSGTTGVPKciihgtgGVLLTHlKEHGLHA-------DLSRDDC-LFY 311
Cdd:PRK05691 2311 leddaaalAAYSDA-PLPFLSLP-QHQAYLIYTSGSTGKPK-------GVVVSH-GEIAMHCqavierfGMRADDCeLHF 2380
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 799207711 312 YTTCGWMMWNWLVSVLAIGATAVLYDGSPFhpGPERLIDLIDAEKISVFGTSPKF 366
Cdd:PRK05691 2381 YSINFDAASERLLVPLLCGARVVLRAQGQW--GAEEICQLIREQQVSILGFTPSY 2433
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
110-598 |
3.47e-07 |
|
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: 52.98 E-value: 3.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 110 GQREQLTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTLVGMLATTSLGAIwscSSPDFGTQGVidrfgqiepkv 189
Cdd:cd05907 1 GVWQPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAV---PVPIYPTSSA----------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 190 litcagyryagkdiDQTAK-LNEILARlpsleqLIIVpyarpqarvedyqtharvtrwsdfyppgGEPEFVAVpfdhply 268
Cdd:cd05907 67 --------------EQIAYiLNDSEAK------ALFV----------------------------EDPDDLAT------- 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 269 ILYSSGTTGVPKciihgtgGVLLTHlkEHGLHADLSRDDCLfyYTTCGwmmwNWLVSVL----AIGATAVLYdgSPFHPG 344
Cdd:cd05907 92 IIYTSGTTGRPK-------GVMLSH--RNILSNALALAERL--PATEG----DRHLSFLplahVFERRAGLY--VPLLAG 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 345 -----PERLIDLIDAekISVFgtSPKFLA----TLEK--AGLQPRLSHDL----------GSLKGLISTGSPLSP----- 398
Cdd:cd05907 155 ariyfASSAETLLDD--LSEV--RPTVFLavprVWEKvyAAIKVKAVPGLkrklfdlavgGRLRFAASGGAPLPAellhf 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 399 -QSYDYVYREIKGelclssMSGGTDIVSCfvigNPVLPVRRGEMqckslamaievwddqGQPL------VGEKGELVCtr 471
Cdd:cd05907 231 fRALGIPVYEGYG------LTETSAVVTL----NPPGDNRIGTV---------------GKPLpgvevrIADDGEILV-- 283
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 472 HFPAMPIGLWNDPDrqklrASYFSQFPGVW-AQGDYAEQRPNGSLLIHGRS-DAVLNPGGVRIGTAEIYRQVEKVPQVQE 549
Cdd:cd05907 284 RGPNVMLGYYKNPE-----ATAEALDADGWlHTGDLGEIDEDGFLHITGRKkDLIITSGGKNISPEPIENALKASPLISQ 358
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 799207711 550 SLAIGqrwQDDVRVVLFVRLNdgvelDEALEQQIRQVIRANTTPRHVPA 598
Cdd:cd05907 359 AVVIG---DGRPFLVALIVPD-----PEALEAWAEEHGIAYTDVAELAA 399
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
93-293 |
4.49e-07 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 52.96 E-value: 4.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 93 LLRRRDDHPAVVAI-SEDGQReqLTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTLVGMLATTSLGAIWSCSSP 171
Cdd:PRK07514 8 ALRAAFADRDAPFIeTPDGLR--YTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 172 DFgTQGVIDRF-GQIEPKVLItCAGYRYAGkdidqtakLNEILARL--PSLEQLiivpyarpqarveDYQTHARVTRWSD 248
Cdd:PRK07514 86 AY-TLAELDYFiGDAEPALVV-CDPANFAW--------LSKIAAAAgaPHVETL-------------DADGTGSLLEAAA 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 799207711 249 FYPpggePEFVAVPF--DHPLYILYSSGTTGVPKciihgtgGVLLTH 293
Cdd:PRK07514 143 AAP----DDFETVPRgaDDLAAILYTSGTTGRSK-------GAMLSH 178
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
251-628 |
6.95e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 52.38 E-value: 6.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 251 PPGGEPEFVAVPFDHPLYILYSSGTTGVPKCII--HG---TGGVLLTHlkehglHADLSRDDCLfyYTTCGW-----MMW 320
Cdd:PRK07867 139 HRDAEPPFRVADPDDLFMLIFTSGTSGDPKAVRctHRkvaSAGVMLAQ------RFGLGPDDVC--YVSMPLfhsnaVMA 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 321 NWLVSV-----LAI----------------GATAVLYDGSPFH---PGPERLIDLIDAEKIsVFGT--SPKFLATLEkAG 374
Cdd:PRK07867 211 GWAVALaagasIALrrkfsasgflpdvrryGATYANYVGKPLSyvlATPERPDDADNPLRI-VYGNegAPGDIARFA-RR 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 375 LQPRLSHDLGSLKGLIS-TGSPLSPQSydyvyreikgelCLSSMSGGTDIVSCfVIGNPVLPVRRGEMQCKSLAMAIevw 453
Cdd:PRK07867 289 FGCVVVDGFGSTEGGVAiTRTPDTPPG------------ALGPLPPGVAIVDP-DTGTECPPAEDADGRLLNADEAI--- 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 454 ddqgqplvgekGELVCTRHfPAMPIGLWNDP--DRQKLRAsyfsqfpGVWAQGDYAEQRPNGSLLIHGRSDAVLNPGGVR 531
Cdd:PRK07867 353 -----------GELVNTAG-PGGFEGYYNDPeaDAERMRG-------GVYWSGDLAYRDADGYAYFAGRLGDWMRVDGEN 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 532 IGTAEIYRQVEKVPQVQESLAIGQrwQDDV---RVVLFVRLNDGVELD-EALEQQIRQviRANTTPRHVPAKILAVTDIP 607
Cdd:PRK07867 414 LGTAPIERILLRYPDATEVAVYAV--PDPVvgdQVMAALVLAPGAKFDpDAFAEFLAA--QPDLGPKQWPSYVRVCAELP 489
|
410 420
....*....|....*....|...
gi 799207711 608 RTISGKIV--ELAVRNVVHGEPV 628
Cdd:PRK07867 490 RTATFKVLkrQLSAEGVDCADPV 512
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
77-614 |
7.17e-07 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 52.86 E-value: 7.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 77 PSAQWFPgatlnfaEHLLRRRDDHPAVVAISEDGqrEQLTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTLVGM 156
Cdd:PRK05691 1128 PAQAWLP-------ELLNEQARQTPERIALVWDG--GSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGL 1198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 157 LATTSLGAIWSCSSPDFGTQGVIDRFGQIEPKVLITcagyryagkdidQTAklneILARLPSLEQLIIVPYArpQARVED 236
Cdd:PRK05691 1199 LAILKAGGAYVPLDPDYPAERLAYMLADSGVELLLT------------QSH----LLERLPQAEGVSAIALD--SLHLDS 1260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 237 YQTHarvtrwsdfyPPGgepefVAVPFDHPLYILYSSGTTGVPKciihgtgGVLLTH--LKE--HGLHAD--LSRDDCLF 310
Cdd:PRK05691 1261 WPSQ----------APG-----LHLHGDNLAYVIYTSGSTGQPK-------GVGNTHaaLAErlQWMQATyaLDDSDVLM 1318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 311 YYTTCGWMMWNWLVSVLAIGATAVLYDGSPFHPGPERLIDLIDAEKISVFGTSPKFLATLekagLQPRLSHDLGSLKGLI 390
Cdd:PRK05691 1319 QKAPISFDVSVWECFWPLITGCRLVLAGPGEHRDPQRIAELVQQYGVTTLHFVPPLLQLF----IDEPLAAACTSLRRLF 1394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 391 STGSPLSPQSYDYVYREIKGeLCLSSMSGGTDIV------SCFVIGNPVLPVRR--GEMQCKslamaieVWDDQGQPL-V 461
Cdd:PRK05691 1395 SGGEALPAELRNRVLQRLPQ-VQLHNRYGPTETAinvthwQCQAEDGERSPIGRplGNVLCR-------VLDAELNLLpP 1466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 462 GEKGELVCTrhfpamPIGLWND-PDRQKLRASYFSQFPG------VWAQGDYAEQRPNGSLLIHGRSDAVLNPGGVRIGT 534
Cdd:PRK05691 1467 GVAGELCIG------GAGLARGyLGRPALTAERFVPDPLgedgarLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEP 1540
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 535 AEIYRQVEKVPQVQESLAIGQRWQDDVRVVLFVRLNDGvelDEALEQQIRQVIRANTTPRHVPAKILAVTDIPRTISGKI 614
Cdd:PRK05691 1541 EEIQARLLAQPGVAQAAVLVREGAAGAQLVGYYTGEAG---QEAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKL 1617
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
255-592 |
3.08e-06 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 50.15 E-value: 3.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 255 EPE-FVAVPF-DHPLYILYSSGTTGVPKciihgtgGVLLTHlkeHGLHADLSRDDCLFYYTTCGWMMWNWLVSVL---AI 329
Cdd:cd05910 74 EPDaFIGIPKaDEPAAILFTSGSTGTPK-------GVVYRH---GTFAAQIDALRQLYGIRPGEVDLATFPLFALfgpAL 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 330 GATAVLYDGSPFHPG---PERLIDLI-DAEKISVFGtSPKFLATLEKAGLQprLSHDLGSLKGLISTGSPLSPQSYDYVY 405
Cdd:cd05910 144 GLTSVIPDMDPTRPAradPQKLVGAIrQYGVSIVFG-SPALLERVARYCAQ--HGITLPSLRRVLSAGAPVPIALAARLR 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 406 REIKGELCLSSMSGGTDIVSCFVIGNPVL------PVRRGEMQCKSLAMA-------------IEVWDDQGQPLVGEKGE 466
Cdd:cd05910 221 KMLSDEAEILTPYGATEALPVSSIGSRELlatttaATSGGAGTCVGRPIPgvrvriieiddepIAEWDDTLELPRGEIGE 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 467 LVCTRhfPAMPIGLWNDPDrqklrASYFSQFP----GVWAQ-GDYAEQRPNGSLLIHGR-SDAVLNPGGvRIGTAEIYRQ 540
Cdd:cd05910 301 ITVTG--PTVTPTYVNRPV-----ATALAKIDdnseGFWHRmGDLGYLDDEGRLWFCGRkAHRVITTGG-TLYTEPVERV 372
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 799207711 541 VEKVPQVQESLAIGQRWQDDVRVVLFVRLNDGVELDEA-LEQQIRQVIRANTT 592
Cdd:cd05910 373 FNTHPGVRRSALVGVGKPGCQLPVLCVEPLPGTITPRArLEQELRALAKDYPH 425
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
80-615 |
3.20e-06 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 50.14 E-value: 3.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 80 QWFPGATLNFAEHLlRRRDDHPAVVaisedGQREQLTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTLVGMLAT 159
Cdd:PRK13382 40 REGMGPTSGFAIAA-QRCPDRPGLI-----DELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 160 TSLGA---IWSCSSPDFGTQGVIDRFG--------QIEPKVLITCAGYRYAGKDIDQTAKLNEILarlpsLEQLIIVPY- 227
Cdd:PRK13382 114 NRIGAdilLLNTSFAGPALAEVVTREGvdtviydeEFSATVDRALADCPQATRIVAWTDEDHDLT-----VEVLIAAHAg 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 228 ARPQARVEdyqtHARVtrwsdfyppggepefvavpfdhplyILYSSGTTGVPKCIIH-GTGGVLLthlkehgLHADLSRD 306
Cdd:PRK13382 189 QRPEPTGR----KGRV-------------------------ILLTSGTTGTPKGARRsGPGGIGT-------LKAILDRT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 307 DclfyyttcgW-----------MMWNW----LVSVLAIGATAVL---YDgspfhpgPERLIDLIDAEKISVFGTSPKFLA 368
Cdd:PRK13382 233 P---------WraeeptvivapMFHAWgfsqLVLAASLACTIVTrrrFD-------PEATLDLIDRHRATGLAVVPVMFD 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 369 TLEKAGLQPRLSHDLGSLKGLISTGSPLSPQsydyVYREIKGEL--CLSSMSGGTDiVSCFVIGNPVlPVRRGEMQCKSL 446
Cdd:PRK13382 297 RIMDLPAEVRNRYSGRSLRFAAASGSRMRPD----VVIAFMDQFgdVIYNNYNATE-AGMIATATPA-DLRAAPDTAGRP 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 447 AMA--IEVWDDQGQPL-VGEKGElvctrhfpampIGLWNDpdrqklrasyfSQF------------PGVWAQGDYAEQRP 511
Cdd:PRK13382 371 AEGteIRILDQDFREVpTGEVGT-----------IFVRND-----------TQFdgytsgstkdfhDGFMASGDVGYLDE 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 512 NGSLLIHGRSDAVLNPGGVRIGTAEIYRQVEKVPQVQESLAIGQrwqDD----VRVVLFVRLNDGVEldeALEQQIRQVI 587
Cdd:PRK13382 429 NGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGV---DDeqygQRLAAFVVLKPGAS---ATPETLKQHV 502
|
570 580
....*....|....*....|....*...
gi 799207711 588 RANTTPRHVPAKILAVTDIPRTISGKIV 615
Cdd:PRK13382 503 RDNLANYKVPRDIVVLDELPRGATGKIL 530
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
543-613 |
4.63e-06 |
|
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: 44.84 E-value: 4.63e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 799207711 543 KVPQVQESLAIGQRwqDDVR---VVLFVRLNDGVEldeALEQQIRQVIRANTTPRHVPAKILAVTDIPRTISGK 613
Cdd:pfam13193 8 SHPAVAEAAVVGVP--DELKgeaPVAFVVLKPGVE---LLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
100-614 |
7.28e-06 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 49.40 E-value: 7.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 100 HPAVVAISedGQREQLTYAELAEHVAGLQKSLRAAGVtQGDRVAACMPNTWQTLVGM-LATTSLGAIWSCSSPDFGTQGV 178
Cdd:PRK05691 3733 HPQRIAAS--CLDQQWSYAELNRAANRLGHALRAAGV-GVDQPVALLAERGLDLLGMiVGSFKAGAGYLPLDPGLPAQRL 3809
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 179 IDRFGQIEPKVLITCAGYRYAGKdidqtaklnEILARLPSleqliivpYARPQARVEDYQTHARVtrwsdfypPGGEPEF 258
Cdd:PRK05691 3810 QRIIELSRTPVLVCSAACREQAR---------ALLDELGC--------ANRPRLLVWEEVQAGEV--------ASHNPGI 3864
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 259 VAVPfDHPLYILYSSGTTGVPKCIIHGTGGVLLTHL-KEHGLHadLSRDDCLFYYTTCGW--MMWNWLVSVLaIGATAVL 335
Cdd:PRK05691 3865 YSGP-DNLAYVIYTSGSTGLPKGVMVEQRGMLNNQLsKVPYLA--LSEADVIAQTASQSFdiSVWQFLAAPL-FGARVEI 3940
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 336 YDGSPFHpGPERLIDLIDAEKISVFGTSPKFLatlekaglQPRLSHD---LGSLKGLISTGSPLSP-------QSYD--- 402
Cdd:PRK05691 3941 VPNAIAH-DPQGLLAHVQAQGITVLESVPSLI--------QGMLAEDrqaLDGLRWMLPTGEAMPPelarqwlQRYPqig 4011
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 403 ----YVYREIKGELCLSSMSGGTDIVSCFVIGNPVLPVRRGEMqckslamaievwdDQGQPLV--GEKGELVCTRhfPAM 476
Cdd:PRK05691 4012 lvnaYGPAECSDDVAFFRVDLASTRGSYLPIGSPTDNNRLYLL-------------DEALELVplGAVGELCVAG--TGV 4076
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 477 PIGLWNDPDRQKLrASYFSQF--PG--VWAQGDYAEQRPNGSLLIHGRSDAVLNPGGVRIGTAEIYRQVEKVPQVQESLA 552
Cdd:PRK05691 4077 GRGYVGDPLRTAL-AFVPHPFgaPGerLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAV 4155
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 799207711 553 IGQRWQDDVRVVLFVRLNDGVELDEALEQQIRQVIRANTTPRHVPAKILAVTDIPRTISGKI 614
Cdd:PRK05691 4156 AVQEGVNGKHLVGYLVPHQTVLAQGALLERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKL 4217
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
109-284 |
1.07e-05 |
|
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: 48.62 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 109 DGQREQLTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTLVGMLATTSLGAIwscSSPDFGTQGViDRFGQI--- 185
Cdd:cd05932 1 GGQVVEFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHI---SVPLYPTLNP-DTIRYVleh 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 186 -EPKVLItcagyryagkdidqTAKLNEILARLPSL-EQLIIVPYARPQARVEDYQtharvtrWSDF---YPP-GGEPefv 259
Cdd:cd05932 77 sESKALF--------------VGKLDDWKAMAPGVpEGLISISLPPPSAANCQYQ-------WDDLiaqHPPlEERP--- 132
|
170 180
....*....|....*....|....*.
gi 799207711 260 aVPFDHPLY-ILYSSGTTGVPKCIIH 284
Cdd:cd05932 133 -TRFPEQLAtLIYTSGTTGQPKGVML 157
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
91-614 |
1.49e-05 |
|
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: 47.93 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 91 EHLLRRRDDHPAVVaisEDGQReqLTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTLVGMLATTSLGAIWSCSS 170
Cdd:cd17645 5 EEQVERTPDHVAVV---DRGQS--LTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPID 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 171 PDFGTQGVIDRFGQIEPKVLITcagyryagkdidqtaklneilarlpsleqliivpyarpqarvedyqtharvtrwsdfy 250
Cdd:cd17645 80 PDYPGERIAYMLADSSAKILLT---------------------------------------------------------- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 251 ppggEPEFVAvpfdhplYILYSSGTTGVPKciihgtgGVLLTHlkeHGL------HAD---LSRDDCLFYYTTCGWMMWN 321
Cdd:cd17645 102 ----NPDDLA-------YVIYTSGSTGLPK-------GVMIEH---HNLvnlcewHRPyfgVTPADKSLVYASFSFDASA 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 322 W-LVSVLAIGATAVLYDgSPFHPGPERLIDLIDAEKISVfgtspKFLATlekAGLQPRLSHDLGSLKGLISTGsplspqs 400
Cdd:cd17645 161 WeIFPHLTAGAALHVVP-SERRLDLDALNDYFNQEGITI-----SFLPT---GAAEQFMQLDNQSLRVLLTGG------- 224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 401 yDYVYREIKGELCLSSMSGGTD---IVSCFVIGNPV--LPVRRGEMQCKSLAMAievWDDQGQPLvGEKGELVCTRHfpA 475
Cdd:cd17645 225 -DKLKKIERKGYKLVNNYGPTEntvVATSFEIDKPYanIPIGKPIDNTRVYILD---EALQLQPI-GVAGELCIAGE--G 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 476 MPIGLWNDPDRQKLRASYFSQFPG--VWAQGDYAEQRPNGSLLIHGRSDAVLNPGGVRIGTAEIYRQVEKVPQVQESLAI 553
Cdd:cd17645 298 LARGYLNRPELTAEKFIVHPFVPGerMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVL 377
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 799207711 554 GQRWQD-DVRVVLFVRLNDGVELDEaleqqIRQVIRaNTTPRH-VPAKILAVTDIPRTISGKI 614
Cdd:cd17645 378 AKEDADgRKYLVAYVTAPEEIPHEE-----LREWLK-NDLPDYmIPTYFVHLKALPLTANGKV 434
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
269-615 |
1.81e-05 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 47.68 E-value: 1.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 269 ILYSSGTTGVPKCI-----IHGTGGVLLTHLKEHGLHADLSRDDCLFYYTTCGWMMwnwLVSVLAIGATAVLYDgspfHP 343
Cdd:PRK13383 179 VLLTSGTTGKPKGVprapqLRSAVGVWVTILDRTRLRTGSRISVAMPMFHGLGLGM---LMLTIALGGTVLTHR----HF 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 344 GPERLIDLIDAEKISVFGTSPKFLATLEKAGLQPRLSHDLGSLKGLISTGSPLSPqSYDYVYREIKGELcLSSMSGGTDi 423
Cdd:PRK13383 252 DAEAALAQASLHRADAFTAVPVVLARILELPPRVRARNPLPQLRVVMSSGDRLDP-TLGQRFMDTYGDI-LYNGYGSTE- 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 424 VSCFVIGNPVLPVRRGEMQCKSLA-MAIEVWDDQGQPlVGEK--------GELVCTRhfpampiglWNDPDRQKLrasyf 494
Cdd:PRK13383 329 VGIGALATPADLRDAPETVGKPVAgCPVRILDRNNRP-VGPRvtgrifvgGELAGTR---------YTDGGGKAV----- 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 495 sqFPGVWAQGDYAEQRPNGSLLIHGRSDAVLNPGGVRIGTAEIYRQVEKVPQVQESLAIG---QRWQDdvRVVLFVRLND 571
Cdd:PRK13383 394 --VDGMTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGvpdERFGH--RLAAFVVLHP 469
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 799207711 572 GVELDEAleqQIRQVIRANTTPRHVPAKILAVTDIPRTISGKIV 615
Cdd:PRK13383 470 GSGVDAA---QLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVL 510
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
271-620 |
2.18e-05 |
|
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: 47.09 E-value: 2.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 271 YSSGTTGVPKCIIHGTGGVllTHLKEHGLHADLSR-DDCLFyyttCGWMMWN------WLVSVLAIGATAVLydgspfhP 343
Cdd:cd05944 9 HTGGTTGTPKLAQHTHSNE--VYNAWMLALNSLFDpDDVLL----CGLPLFHvngsvvTLLTPLASGAHVVL-------A 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 344 GP-----ERLID----LIDAEKISVFGTSPKFLATLekagLQPRLSHDLGSLKGLISTGSPLSPQsydyVYREIKGELCL 414
Cdd:cd05944 76 GPagyrnPGLFDnfwkLVERYRITSLSTVPTVYAAL----LQVPVNADISSLRFAMSGAAPLPVE----LRARFEDATGL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 415 SSMSG-GTDIVSCFVIGNPvlpvRRGEMQCKSLAMA-------IEVWDDQGQPL----VGEKGElVCTRHFPAMPIGLWN 482
Cdd:cd05944 148 PVVEGyGLTEATCLVAVNP----PDGPKRPGSVGLRlpyarvrIKVLDGVGRLLrdcaPDEVGE-ICVAGPGVFGGYLYT 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 483 DPDRQKLRAsyfsqfpGVWAQ-GDYAEQRPNGSLLIHGRSDAVLNPGGVRIGTAEIYRQVEKVPQVQESLAIGqrwQDDV 561
Cdd:cd05944 223 EGNKNAFVA-------DGWLNtGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVG---QPDA 292
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 799207711 562 RV----VLFVRLNDGVELDEA-LEQQIRQVI--RANttprhVPAKILAVTDIPRTISGKIVELAVR 620
Cdd:cd05944 293 HAgelpVAYVQLKPGAVVEEEeLLAWARDHVpeRAA-----VPKHIEVLEELPVTAVGKVFKPALR 353
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
95-294 |
2.53e-05 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 47.49 E-value: 2.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 95 RRRDdhpAVVAISedGQReQLTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTLVGMLATTSLGAI-------WS 167
Cdd:PLN02860 19 LRGN---AVVTIS--GNR-RRTGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIvaplnyrWS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 168 CSSPDFGTQgvidrfgQIEPKVLITCAGYRYAGKDIDQTaklneilaRLPSLEQLIIV--PYARPQARVEDYQTHARVTR 245
Cdd:PLN02860 93 FEEAKSAML-------LVRPVMLVTDETCSSWYEELQND--------RLPSLMWQVFLesPSSSVFIFLNSFLTTEMLKQ 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 799207711 246 WSdFYPPggEPEFVAVPFDHPLyILYSSGTTGVPKciihgtgGVLLTHL 294
Cdd:PLN02860 158 RA-LGTT--ELDYAWAPDDAVL-ICFTSGTTGRPK-------GVTISHS 195
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
113-168 |
5.45e-05 |
|
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: 46.19 E-value: 5.45e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 799207711 113 EQLTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTLVGMLATTSLGAIWSC 168
Cdd:cd05940 2 EALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAAL 57
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
513-621 |
6.71e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 45.93 E-value: 6.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 513 GSLLIHGRSDAVLNPGGVRIGTAEIYRQVEKVPQVQESLAIG---QRWQDdvRVVLFVRLNdgveldeALEQQIRQVIRA 589
Cdd:PRK07638 375 GFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGvpdSYWGE--KPVAIIKGS-------ATKQQLKSFCLQ 445
|
90 100 110
....*....|....*....|....*....|..
gi 799207711 590 NTTPRHVPAKILAVTDIPRTISGKIVELAVRN 621
Cdd:PRK07638 446 RLSSFKIPKEWHFVDEIPYTNSGKIARMEAKS 477
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
248-478 |
8.27e-05 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 45.53 E-value: 8.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 248 DFYPPGgepeFVAVPFDHPLYILYSSGTTGVPKCIIHGTGGVLLTHLK-EHGLH-ADLSRDD----CLFY-YTTCGWMMW 320
Cdd:COG1541 71 DNYPFG----LFAVPLEEIVRIHASSGTTGKPTVVGYTRKDLDRWAELfARSLRaAGVRPGDrvqnAFGYgLFTGGLGLH 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 321 NwlvSVLAIGATAVlydgsPFHPG-PERLIDLIDAEKISVFGTSPKFLATL----EKAGLQPRLShdlgSLKGLISTGSP 395
Cdd:COG1541 147 Y---GAERLGATVI-----PAGGGnTERQLRLMQDFGPTVLVGTPSYLLYLaevaEEEGIDPRDL----SLKKGIFGGEP 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 396 LSPQsydyVYREIKGELclssmsgGTDIVSCFvignpvlpvrrG--EMQCkslAMAIE--------VWDDQ--------- 456
Cdd:COG1541 215 WSEE----MRKEIEERW-------GIKAYDIY-----------GltEVGP---GVAYEceaqdglhIWEDHflveiidpe 269
|
250 260
....*....|....*....|....*..
gi 799207711 457 -GQPL-VGEKGELVCT---RHfpAMPI 478
Cdd:COG1541 270 tGEPVpEGEEGELVVTtltKE--AMPL 294
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
101-164 |
1.31e-04 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 44.86 E-value: 1.31e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 799207711 101 PAVVAISEDGqrEQLTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTLVGMLATTSLGA 164
Cdd:PRK09029 17 PQAIALRLND--EVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGA 78
|
|
| PaaK |
cd05913 |
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic ... |
243-478 |
1.75e-04 |
|
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic degradation pathway, by converting phenylacetic acid (PA) into phenylacetyl-CoA (PA-CoA). Phenylacetate-CoA ligase has been found in proteobacteria as well as gram positive prokaryotes. The enzyme is specifically induced after aerobic growth in a chemically defined medium containing PA or phenylalanine (Phe) as the sole carbon source. PaaKs are members of the adenylate-forming enzyme (AFE) family. However, sequence comparison reveals divergent features of PaaK with respect to the superfamily, including a novel N-terminal sequence.
Pssm-ID: 341239 [Multi-domain] Cd Length: 425 Bit Score: 44.54 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 243 VTRWSDF---YPPGGepefVAVPFDHPLYILYSSGTTGVPKciihgtggvllthlkehglhadlsrddcLFYYTTCGWMM 319
Cdd:cd05913 58 FTTKEDLrdnYPFGL----FAVPREKVVRIHASSGTTGKPT----------------------------VVGYTKNDLDV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 320 WNWLV--SVLAIGAT-------AVLY----DGSPFHPGPERL---------------IDLIDAEKISVFGTSPKFLATL- 370
Cdd:cd05913 106 WAELVarCLDAAGVTpgdrvqnAYGYglftGGLGFHYGAERLgalvipagggnterqLQLIKDFGPTVLCCTPSYALYLa 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 371 ---EKAGLQPRLShdlgSLKGLISTGSPLSPQsydyVYREIKGELCLSSmsggTDIVSCFVIGNPVLP---VRRGEMQCK 444
Cdd:cd05913 186 eeaEEEGIDPREL----SLKVGIFGAEPWTEE----MRKRIERRLGIKA----YDIYGLTEIIGPGVAfecEEKDGLHIW 253
|
250 260 270
....*....|....*....|....*....|....*...
gi 799207711 445 SLAMAIEVWDDQ-GQPL-VGEKGELVCT--RHFpAMPI 478
Cdd:cd05913 254 EDHFIPEIIDPEtGEPVpPGEVGELVFTtlTKE-AMPL 290
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
512-614 |
5.97e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 42.72 E-value: 5.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 512 NGSLLIHGRSDAVLNPGGVRIGTAEIYRQVEKVPQVQEslAIGQRWQDDV---RVVLFVRLNDGVELDealeqQIRQVIR 588
Cdd:PRK08308 304 RGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQE--AVVYRGKDPVageRVKAKVISHEEIDPV-----QLREWCI 376
|
90 100
....*....|....*....|....*.
gi 799207711 589 ANTTPRHVPAKILAVTDIPRTISGKI 614
Cdd:PRK08308 377 QHLAPYQVPHEIESVTEIPKNANGKV 402
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
59-293 |
8.36e-04 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 42.56 E-value: 8.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 59 DVQFRSPpsAVLIEDAE-----MPSAQ---WFPGATLNFAEHLLRRRDDHPAVVAISEDGQREQLTYAELAEHVAGLQKS 130
Cdd:PRK08180 8 PVAFAPP--AVEVERRAdgtiyLRSAEplgDYPRRLTDRLVHWAQEAPDRVFLAERGADGGWRRLTYAEALERVRAIAQA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 131 LRAAGVTQGDRVAACMPNTWQTLVGMLATTSLGAIWSCSSP-------DFGT-QGVIDRfgqIEPKVLITCAGYRYAgkd 202
Cdd:PRK08180 86 LLDRGLSAERPLMILSGNSIEHALLALAAMYAGVPYAPVSPayslvsqDFGKlRHVLEL---LTPGLVFADDGAAFA--- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 203 idqtaklneilarlPSLEqlIIVPYARPQARVEDYQTHARVTRWSDFY----PPGGEPEFVAVPFDHPLYILYSSGTTGV 278
Cdd:PRK08180 160 --------------RALA--AVVPADVEVVAVRGAVPGRAATPFAALLatppTAAVDAAHAAVGPDTIAKFLFTSGSTGL 223
|
250
....*....|....*
gi 799207711 279 PKciihgtgGVLLTH 293
Cdd:PRK08180 224 PK-------AVINTH 231
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
497-614 |
9.21e-04 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 42.14 E-value: 9.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 497 FPGVWAQ-GDYAEQRPNGSLLIHGRSDAVLNPGGVRIGTAEIYRQVEKVPQVQESLAIG---QRWQDDvrVVLFVRLNDG 572
Cdd:PLN02479 427 FANGWFHsGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVArpdERWGES--PCAFVTLKPG 504
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 799207711 573 VE-LDEA-LEQQIRQVIRANTTPRHVPaKILAVTDIPRTISGKI 614
Cdd:PLN02479 505 VDkSDEAaLAEDIMKFCRERLPAYWVP-KSVVFGPLPKTATGKI 547
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
113-335 |
1.01e-03 |
|
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: 42.28 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 113 EQLTYAELAEHVAGLQKSLRA-AGVTQGDRVAACMPNTWQTLVGMLATTSLGAIWSCSSPDFGTQGVIDRFGQIEPKVLI 191
Cdd:cd05938 4 ETYTYRDVDRRSNQAARALLAhAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAKVLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 192 TcagyryagkDIDQTAKLNEILarlPSLEQLII-VPYARPQARVEDYQT-HARVTRWSDFYPPGGEPEFVAvPFDHPLYI 269
Cdd:cd05938 84 V---------APELQEAVEEVL---PALRADGVsVWYLSHTSNTEGVISlLDKVDAASDEPVPASLRAHVT-IKSPALYI 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 799207711 270 lYSSGTTGVPKCIIhgtggvlLTHLK---------EHGLHADLSRDDCLFYYTTCGWMMwnWLVSVLAIGATAVL 335
Cdd:cd05938 151 -YTSGTTGLPKAAR-------ISHLRvlqcsgflsLCGVTADDVIYITLPLYHSSGFLL--GIGGCIELGATCVL 215
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
504-633 |
1.49e-03 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 41.54 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 504 GDYAEQRPNGSLLIHGRSDAVLNPGGVRIGTAEIYRQVEKVPQVQESLAIGQ---RWQDDvrVVLFVRLNDGVELDEALE 580
Cdd:PLN03102 425 GDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMphpTWGET--PCAFVVLEKGETTKEDRV 502
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 581 QQI----RQVI---RANTTPRHVPAKILAVTDIPRTISGKIVELAVRNVVHGEPVKNTDA 633
Cdd:PLN03102 503 DKLvtreRDLIeycRENLPHFMCPRKVVFLQELPKNGNGKILKPKLRDIAKGLVVEDEDN 562
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
99-293 |
1.77e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 41.47 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 99 DHPAVVaiseDGQREQlTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQTLVGMLATTSLGAIWSC--SSPDFGTQ 176
Cdd:PRK08162 33 DRPAVI----HGDRRR-TWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTlnTRLDAASI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 177 GVIDRFGqiEPKVLITcagyryagkDIDQTAKLNEILARLPSLeQLIIVPYARPQarvedYQTHARV--TRWSDFYpPGG 254
Cdd:PRK08162 108 AFMLRHG--EAKVLIV---------DTEFAEVAREALALLPGP-KPLVIDVDDPE-----YPGGRFIgaLDYEAFL-ASG 169
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 799207711 255 EPEFVAV-PFDH--PLYILYSSGTTGVPKciihgtgGVLLTH 293
Cdd:PRK08162 170 DPDFAWTlPADEwdAIALNYTSGTTGNPK-------GVVYHH 204
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
74-158 |
1.85e-03 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 41.16 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 74 AEMPSAQWfpgATL-NFAEHLLRRRDDHPAVVAISEdgqreQLTYAELAEHVAGLQKSLRAAGVTQGDRVAACMPNTWQT 152
Cdd:PRK07059 15 AEIDASQY---PSLaDLLEESFRQYADRPAFICMGK-----AITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQY 86
|
....*.
gi 799207711 153 LVGMLA 158
Cdd:PRK07059 87 PVAIAA 92
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
450-621 |
3.45e-03 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 40.42 E-value: 3.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 450 IEVWDDQGQPL-VGEKGELvCTRHfPAMPIGLWNDPDRQklrASYFSQfpGVWAQGDYAEQRPNGSLLIHGRSDAVLNPG 528
Cdd:PRK08974 389 IKLVDDDGNEVpPGEPGEL-WVKG-PQVMLGYWQRPEAT---DEVIKD--GWLATGDIAVMDEEGFLRIVDRKKDMILVS 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 529 GVRIGTAEIYRQVEKVPQVQESLAIGQrwQDDVR---VVLFVrlndgVELDEAL-EQQIRQVIRANTTPRHVPAKILAVT 604
Cdd:PRK08974 462 GFNVYPNEIEDVVMLHPKVLEVAAVGV--PSEVSgeaVKIFV-----VKKDPSLtEEELITHCRRHLTGYKVPKLVEFRD 534
|
170
....*....|....*..
gi 799207711 605 DIPRTISGKIVELAVRN 621
Cdd:PRK08974 535 ELPKSNVGKILRRELRD 551
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
454-621 |
4.63e-03 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 39.86 E-value: 4.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 454 DDQGQPL-VGEKGELvCTRHfPAMPIGLWNDPDRqklrASYFSQFPGVWAQGDYAEQRPNGSLLIHGRSDAVLNPGGVRI 532
Cdd:PRK08751 397 DDAGTVLaIGEIGEL-CIKG-PQVMKGYWKRPEE----TAKVMDADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNV 470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 533 GTAEIYRQVEKVPQVQESLAIG---QRWQDDVRVVLfvrlndgVELDEALE-QQIRQVIRANTTPRHVPAKILAVTDIPR 608
Cdd:PRK08751 471 YPNEIEDVIAMMPGVLEVAAVGvpdEKSGEIVKVVI-------VKKDPALTaEDVKAHARANLTGYKQPRIIEFRKELPK 543
|
170
....*....|...
gi 799207711 609 TISGKIVELAVRN 621
Cdd:PRK08751 544 TNVGKILRRELRD 556
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
111-333 |
6.16e-03 |
|
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.
Pssm-ID: 341287 [Multi-domain] Cd Length: 588 Bit Score: 39.75 E-value: 6.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 111 QREQLTYAELAEHVAGLQKSLRAAG-VTQGDRVAACMPNTWQTLVGMLATTSLGAI---WSCSSPDFGTQGVIDrfgQIE 186
Cdd:cd17632 64 RFETITYAELWERVGAVAAAHDPEQpVRPGDFVAVLGFTSPDYATVDLALTRLGAVsvpLQAGASAAQLAPILA---ETE 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 187 PKVLITcagyryagkDIDQTAKLNEILARLPSLEQLIIVPYARP-----------QARVED----YQTHARVTRWSDFYP 251
Cdd:cd17632 141 PRLLAV---------SAEHLDLAVEAVLEGGTPPRLVVFDHRPEvdahraalesaRERLAAvgipVTTLTLIAVRGRDLP 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207711 252 PGgePEFVAVPFDHPLYIL-YSSGTTGVPKCIIHGTGGVLLTHLKEHGLHADLSRDDCLFYYTTCGWMMW-NWLVSVLAI 329
Cdd:cd17632 212 PA--PLFRPEPDDDPLALLiYTSGSTGTPKGAMYTERLVATFWLKVSSIQDIRPPASITLNFMPMSHIAGrISLYGTLAR 289
|
....
gi 799207711 330 GATA 333
Cdd:cd17632 290 GGTA 293
|
|
| |
